Yuki Yamagata yuki.yamagata[at]riken.jp Homeostasis imbalance process ontology (HOIP) systematizes a wide variety of processes triggered by homeostatic imbalance. The version of HoiP focuses on COVID-19 infectious processes and cellular senescence. The HoIP contains an is-a hierarchy that is organized into three layers: the top layer contains general terms, mostly derived from the Basic Formal Ontology. The top layer also defines functioning-related processes. The intermediate layer contains biomedical terms in OBO foundry from VO, UBERON, Cell Ontology, NCBI Taxon, ChEBI, Gene Ontology, PATO, OGG, INOH, HINO, DOID, HP, Protein Ontology, Symptom Ontology, CIDO, BSPO, WBbt, WBIs, HuPSON, NCIT, and Relational ontology (RO). The lower layer contains homeostasis imbalance-dependent terms. Related article: Ontology for Cellular Senescence Mechanisms Yuki Yamagata, Tsubasa Fukuyama, Shuichi Onami, Hiroshi Masuya bioRxiv 2023.03.09.531883; doi: https://doi.org/10.1101/2023.03.09.531883 Homeostasis imbalance process ontology (HOIP) severe COVID-19 course: http://purl.bioontology.org/ontology/HOIP/HOIP_0039222 COVID-19 course associated with acute respiratory distress syndrome http://purl.bioontology.org/ontology/HOIP/HOIP_0036006 COVID-19 specific process. http://purl.bioontology.org/ontology/HOIP/HOIP_0037002 Cellular senescence course: http://purl.bioontology.org/ontology/HOIP/HOIP_0060024 Chronic cellular senescence course http://purl.bioontology.org/ontology/HOIP/HOIP_0060195 2024/04/03 CorrespondingAuthor MeSH term(s) related to the NCBI PubMed article. has associated MeSH term A name given to the figure. Figure title The concise, meaningful, and human-friendly name for a class or property preferred by the ontology developers. editor preferred term A phrase describing how a term should be used and/or a citation to a work which uses it. May also include other kinds of examples that facilitate immediate understanding, such as widely know prototypes or instances of a class, or cases where a relation is said to hold. example of usage has curation status The official OBI definition, explaining the meaning of a class or property. Shall be Aristotelian, formalized and normalized. Can be augmented with colloquial definitions. definition An administrative note intended for its editor. It may not be included in the publication version of the ontology, so it should contain nothing necessary for end users to understand the ontology. GROUP:OBI:<http://purl.obfoundry.org/obo/obi> editor note Name of editor entering the term in the file. The term editor is a point of contact for information regarding the term. The term editor may be, but is not always, the author of the definition, which may have been worked upon by several people GROUP:OBI:<http://purl.obolibrary.org/obo/obi> term editor An alternative name for a class or property which means the same thing as the preferred name (semantically equivalent) PERSON:Daniel Schober GROUP:OBI:<http://purl.obolibrary.org/obo/obi> alternative term formal citation, e.g. identifier in external database to indicate / attribute source(s) for the definition. Free text indicate / attribute source(s) for the definition. EXAMPLE: Author Name, URI, MeSH Term C04, PUBMED ID, Wiki uri on 31.01.2007 PERSON:Daniel Schober Discussion on obo-discuss mailing-list, see http://bit.ly/hgm99w GROUP:OBI:<http://purl.obolibrary.org/obo/obi> definition source An administrative note of use for a curator but of no use for a user PERSON:Alan Ruttenberg curator note An IRI or similar locator for a request or discussion of an ontology term. term tracker item imported from For external terms/classes, the ontology from which the term was imported GROUP:OBI:<http://purl.obolibrary.org/obo/obi> imported from elucidation An axiom associated with a term expressed using natural language has associated axiom(nl) An axiom expressed in first order logic using CLIF syntax has associated axiom(fol) has associated axiom(fol) A URI that is intended to be unique label for an axiom used for tracking change to the ontology. For an axiom expressed in different languages, each expression is given the same URI has axiom label the symbol assigned by the nomenclature authority symbol from nomenclature authority the full name assigned by the nomenclature authority Oliver He, Yue Liu full name from nomenclature authority A GeneID in the NCBI Gene database NCBI GeneID the NCBI LocusTag name of a gene NCBI LocusTag the map location of a gene Oliver He, Yue Liu gene map location a date of content modification modification date The NCBITaxon ontology ID of an organism. Oliver He, Yue Liu organism NCBITaxon ID A chromosome ID where a gene is located. Oliver He chromosome ID of gene an annotation property that specifies the type of a gene Oliver He type of gene an annotation property that specifies a nomenclature status Oliver He nomenclature status an annotation property that shows the GO information associated with a specific gene. Yongqun He has GO association An annotation property that represents a gene's association with PubMed publication(s). Yongqun He has PubMed association X is the opposite of y if there exists some distance metric M, and there exists no z such as M(x,z) <= M(x,y) or M(y,z) <= M(y,x). is opposite_of An alternate textual definition for a class taken unmodified from an external source. This definition may have been used to derive a generalized definition for the new class. external definition Notes on the homology status of this class. This annotation property may be replaced with an annotation property from an external ontology such as IAO homology notes Notes on the how instances of this class vary across species. taxon notes Notes on the evolved function of instances of this class. function_notes Notes on the structure, composition or histology of instances of this class. structure_notes Notes on the ontogenic development of instances of this class. development_notes A mapping between the singular form and the FMA set term fma_set_term charge formula InChI InChIKey Monoisotopic Mass smiles has_rank An entity responsible for making contributions to the resource. Contributor An entity primarily responsible for making the resource. Examples of a Creator include a person, an organization, or a service. Typically, the name of a Creator should be used to indicate the entity. Creator A point or period of time associated with an event in the lifecycle of the resource. Date An account of the resource. Description may include but is not limited to: an abstract, a table of contents, a graphical representation, or a free-text account of the resource. Description The file format, physical medium, or dimensions of the resource. Recommended practice is to use a controlled vocabulary where available. For example, for file formats one could use the list of Internet Media Types [MIME]. Format An unambiguous reference to the resource within a given context. Recommended practice is to identify the resource by means of a string conforming to an identification system. Identifier Recommended best practice is to use RFC 3066 [RFC3066], which, in conjunction with ISO 639 [ISO639], defines two- and three-letter primary language tags with optional subtags. Examples include "en" or "eng" for English, "akk" for Akkadian, and "en-GB" for English used in the United Kingdom. A language of the intellectual content of the resource. Language A related resource from which the described resource is derived. The described resource may be derived from the related resource in whole or in part. Recommended best practice is to identify the related resource by means of a string conforming to a formal identification system. Source The topic of the resource. Typically, the subject will be represented using keywords, key phrases, or classification codes. Recommended best practice is to use a controlled vocabulary. Subject A name given to the resource. Title An alternative identifier for this class; should follow ID syntax. These can result from class merges has_alternative_id An alias in which the alias is broader than the primary class name. Example: cell division is a broad synonym of cytokinesis has_broad_synonym The textual definition of the current term. There must be zero or one instances of this tag per term description database cross reference An alias in which the alias exhibits true synonymy. Example: ornithine cycle is an exact synonym of urea cycle. has_exact_synonym An alias in which the alias is narrower than the primary class name. Example: pyrimidine-dimer repair by photolyase is a narrow synonym of photoreactive repair has_narrow_synonym An alias in which the alias is related the primary class name, but not necessarily broader or narrower. Example: cytochrome bc1 complex is a related synonym of ubiquinol-cytochrome-c reductase activity; virulence is a related synonym of pathogenesis has_related_synonym saved_by A description of the subject resource. comment The defininition of the subject resource. isDefinedBy A human-readable name for the subject. label notation preferred label The depiction property is a relationship between a thing and an Image that depicts it. As such it is an inverse of the depicts relationship. A common use of depiction (and depicts) is to indicate the contents of a digital image, for example the people or objects represented in an online photo gallery. depiction A homepage for some thing. homepage 'Metafunctioning type of' is a relation between the type of metafunctioning and functioning process. Metafunctioning is a functional process to other process, for example, preventing, controlling and so on. is_metafuntioning_type_of metafuntioning type of 'has molecular reaction' is a relation that holds between a whole occurrent (process) and its molecular process. has molecular reaction 'finding of' is a relation between a finding and an entity, where the finding is a representational artifact that a result of a laboratory test or an observation. is finding of finding of 'component of' is a relation between molecular components and a molecular complex. component of inverse of 'has cause': p 'has cause' q if p exerts some causal influence on q directly, where p is a cause and q is its effect. causally downstream of results in has result HOIP_0000069 p 'has cause' q if p exerts some causal influence on q directly, where p is a cause and q is its effect. has cause HOIP_0000076 'Relation between a role and a process' is a relationship that holds between a role of material entity and a process in which causality is involved, with either the material entity or some part of the material entity plays a role and some influence over the process. relation between a role and a process 'manifested phenotype of' is a relation between a phenotype and an entity, where there is a bearer of the realizable entity that participates in the process, and the phenotype comes to be realized in the course of the process. manifested phenotype of This shattering realizes the fragility in the course of breaking the cup (process). 'mainfests phenotype' is a relation between an entity and quality, where there is a bearer of the realizable entity that participates in the process, and the phenotype comes to be realized in the course of the process. manifests phenotype Inherit means to receive a property (or an attribute and its value) from another entity (other than the ancestor) . inherit 'has family member' is a relation between (molecule ) family and a molecule. A protein family is a group of evolutionarily-related proteins. In many cases a protein family has a corresponding gene family. A protein family is a group of evolutionarily-related proteins. In many cases a protein family has a corresponding gene family. has family member A protein family is a group of evolutionarily-related proteins. In many cases a protein family has a corresponding gene family. Wikipedia:Protein family 'dysfunctioning of' is a relation between an impaired or abnormal functioning and a normal functioning process. is dysfuctioning of dysfunctioning of 'molecular reaction of' is a relation that holds between a molecular process and its whole process. is molecular reaction of molecular_reaction_of molecular reaction of 'relates assay' is a relation between an entity and the assay in which the entity was related (e.g., can be expressed, observed, and so on). related assay 'has context' is a relation between an entity and its context dependent on. Role is intrinsically context-dependent. has context 'has related human gene' is a relation between a molecule and the related gene. has related human gene The cross-sectional area of the coronary artery has attribute value 'small.' 'has attribute value' is a relation between an attribute and its value. has attribute value 'dysfunctioning of' is a relation between an increasing function process and a normal one. hyperfunction of 'malfunctioning of' is a relation between an abnormal functioning and a normal functioning process. malfunctioning of has related rat gene 'has state' is a relation between an entity and the state. has state 'has attribute' is a relation between an entity and its attribute, in which the attribute specifically depends on the bearer for its existence. 'has way' is a relation between an entity and its way, in which the way specifically depends on the bearer for its context. has attribute 'has agent' is a relation between a participant and a process, in which the participant is active in the relevant process. Example: A protease is an agent in proteolysis process. has agent Metafunctioning type is a relation between functional process and the type of metafunction. Metafunctioning is a functional process to other process, for example, preventing, controlling and so on. metafunctioning type 'property of' is a relation between a property and the entity, , in which the property specifically depends on the bearer for its existence. http://semanticscience.org/resource/SIO_000224 is property of property of 'is attribute of' is a relation that associates an attribute with an entity. is attribute of is_attribute_of attribute of 'has finding' is a relation between an entity and its finding, where the finding is a representational artifact that a result of a laboratory test or an observation. has finding Proteolysis is a context of the protease role of the molecule. 'context of' is a relation between a context and an entity. Role is intrinsically context-dependent. context of 'related assay of' is a relationship between an assay and the entity, in which the entity can be related (e.g., can be expressed, observed, and so on) in the assay like in vivo, in vitro or clinical test. related assay of 'agent of' is a relation between a participant and a process, in which the participant is active in the relevant process. is agent of agent of 'famly of' is a relationship between a molecule and its family. A protein family is a group of evolutionarily-related proteins. In many cases a protein family has a corresponding gene family. A protein family is a group of evolutionarily-related proteins. In many cases a protein family has a corresponding gene family. family_of family of A protein family is a group of evolutionarily-related proteins. In many cases a protein family has a corresponding gene family. Wikipedia:Protein family "has ocurrent part" is a relation that holds between a whole occurrent (process) and its part. has occurrent part "has pathway" is a relation that holds between a whole occurrent (process) for signaling and its pathway. has pathway 'pathway of' is a relation that holds between a pathway and its whole (signaling) process. is pathway of is_pathway_of pathway_of pathway of 'has dysfunctioning' is a relation between a normal functioning process and an impaired or abnormal functioning. has_dysfunctioning has dysfunctioning 'Attribute value of' is a relation between a value and its attribute is attribute value of attribute value of observed in A relation between a process/process sequence and a disease. realizes disease phenpotype of A relation that holds between a disease or an organism and a phenotype has symptom 'mainfests symptom' is a relation between an entity and quality, where there is a bearer of the realizable entity that participates in the process, and the symptom comes to be realized in the course of the process. manifests symptom has way p results in the developmental progression of s iff p is a developmental process and s is an anatomical structure and p causes s to undergo a change in state at some point along its natural developmental cycle (this cycle starts with its formation, through the mature structure, and ends with its loss) results in developmental progression of c stands in this relationship to p if and only if there exists some p' such that c is capable_of p', and p' is part_of p. capable of part of Inverse of 'has part equation' equation is part of is performed on 'stopping function of' is a relation between an arrested functioning and a normal functioning process. stopping function of 'losing function of' is a relation between a process of loss of function and a normal functioning process. losing function of has negatively result has whole-part result is about GO biological process relates of a Gene Ontology (GO) biological process to datum. is about GO biological process is about GO molecular function related gene 'relates imaging assay' is a relation between an entity and the assay in which the entity can be observed in imaging. related imaging assay has core process The entity A, upstream of the entity B, has an activity that negatively regulates an activity performed by B. negatively regulates activity of The entity A, iupstream of the entity B, has an activity that positively regulates an activity performed by B. positively regulates activity of The relation that links two events, processes, states, or objects such that one event, process, state, or object (a cause) contributes to the negative effect of another event, process, state, or object (a negative effect). causally related to, negative is part of my brain is part of my body (continuant parthood, two material entities) my stomach cavity is part of my stomach (continuant parthood, immaterial entity is part of material entity) this day is part of this year (occurrent parthood) a core relation that holds between a part and its whole Everything is part of itself. Any part of any part of a thing is itself part of that thing. Two distinct things cannot be part of each other. Occurrents are not subject to change and so parthood between occurrents holds for all the times that the part exists. Many continuants are subject to change, so parthood between continuants will only hold at certain times, but this is difficult to specify in OWL. See https://code.google.com/p/obo-relations/wiki/ROAndTime Parthood requires the part and the whole to have compatible classes: only an occurrent can be part of an occurrent; only a process can be part of a process; only a continuant can be part of a continuant; only an independent continuant can be part of an independent continuant; only an immaterial entity can be part of an immaterial entity; only a specifically dependent continuant can be part of a specifically dependent continuant; only a generically dependent continuant can be part of a generically dependent continuant. (This list is not exhaustive.) A continuant cannot be part of an occurrent: use 'participates in'. An occurrent cannot be part of a continuant: use 'has participant'. A material entity cannot be part of an immaterial entity: use 'has location'. A specifically dependent continuant cannot be part of an independent continuant: use 'inheres in'. An independent continuant cannot be part of a specifically dependent continuant: use 'bearer of'. http://www.obofoundry.org/ro/#OBO_REL:part_of part_of part of realized in this disease is realized in this disease course this fragility is realized in this shattering this investigator role is realized in this investigation is realized by realized_in [copied from inverse property 'realizes'] to say that b realizes c at t is to assert that there is some material entity d & b is a process which has participant d at t & c is a disposition or role of which d is bearer_of at t& the type instantiated by b is correlated with the type instantiated by c. (axiom label in BFO2 Reference: [059-003]) Paraphrase of elucidation: a relation between a realizable entity and a process, where there is some material entity that is bearer of the realizable entity and participates in the process, and the realizable entity comes to be realized in the course of the process realized in X precedes y if and only if the time point at which x ends is before or equivalent to the time point at which y starts. Formally: x precedes y iff ω(x) <= α(y), where α is a function that maps a process to a start point, and ω is a function that maps a process to an end point. precedes x ventral to y iff x is further along the dorso-ventral axis than y, towards the front. A dorso-ventral axis is an axis that extends through an organism from back (e.g. spinal column) to front (e.g. belly). x ventral to y iff x is further along the dorso-ventral axis than y, towards the front. A dorso-ventral axis is an axis that extends through an organism from back (e.g. spinal column) to front (e.g. belly). BSPO:0000102 spatial ventral_to ventral_to ventral to x ventral to y iff x is further along the dorso-ventral axis than y, towards the front. A dorso-ventral axis is an axis that extends through an organism from back (e.g. spinal column) to front (e.g. belly). BSPO:cjm BSPO:0000103 spatial vicinity_of vicinity_of vicinity of On the opposite side from. For example, the left arm is contralateral to the right arm (and the right leg). On the opposite side from. For example, the left arm is contralateral to the right arm (and the right leg). BSPO:0000106 spatial contralateral_to contralateral_to contralateral to On the opposite side from. For example, the left arm is contralateral to the right arm (and the right leg). BSPO:cjm Near the outer surface of the organism. Thus, skin is superficial to the muscle layer. Near the outer surface of the organism. Thus, skin is superficial to the muscle layer. BSPO:0000108 spatial superficial_to superficial_to superficial to Near the outer surface of the organism. Thus, skin is superficial to the muscle layer. BSPO:cjm Closer to the right side of the organism. Example: The dorsal fin is right of the left pectoral fin, but is left of the right eye. On the type level: X left of Y <=> every instance x of X is right of some instance y of Y, and there exists some organism o such that x part of o and y part of o. Closer to the right side of the organism. Example: The dorsal fin is right of the left pectoral fin, but is left of the right eye. On the type level: X left of Y <=> every instance x of X is right of some instance y of Y, and there exists some organism o such that x part of o and y part of o. BSPO:0000111 spatial right_of right_of right of Closer to the right side of the organism. Example: The dorsal fin is right of the left pectoral fin, but is left of the right eye. On the type level: X left of Y <=> every instance x of X is right of some instance y of Y, and there exists some organism o such that x part of o and y part of o. BSPO:cjm X lateral to y if x is further from the midsagittal plane than y. Jennifer Girón 2021-04-21 lateral to X medial to y if x is closer to the midsagittal plane than y. Jennifer Girón 2021-04-21 medial to x in proximal side of y <=> if y is subdivided into two proximal and distal portions, y is part of the proximal portion. x in proximal side of y <=> if y is subdivided into two proximal and distal portions, y is part of the proximal portion. BSPO:0000124 spatial in_proximal_side_of in_proximal_side_of in proximal side of x in proximal side of y <=> if y is subdivided into two proximal and distal portions, y is part of the proximal portion. BSPO:PATO_mtg_2009 x in distal side of y <=> if y is subdivided into two proximal and distal portions, y is part of the distal portion. x in distal side of y <=> if y is subdivided into two proximal and distal portions, y is part of the distal portion. BSPO:0000125 spatial in_distal_side_of in_distal_side_of in distal side of x in distal side of y <=> if y is subdivided into two proximal and distal portions, y is part of the distal portion. BSPO:PATO_mtg_2009 X in lateral side of Y <=> if X is in left side of Y or X is in right side of Y. X is often, but not always a paired structure X in lateral side of Y <=> if X is in left side of Y or X is in right side of Y. X is often, but not always a paired structure BSPO:0000126 spatial in_lateral_side_of in_lateral_side_of in lateral side of https://github.com/obophenotype/uberon/wiki/Modeling-paired-structures-Design-Pattern X in lateral side of Y <=> if X is in left side of Y or X is in right side of Y. X is often, but not always a paired structure UBERON:cjm X superficial part of Y <=> if Y is subdivided into two superficial and deep portions, X is part of the superficial portion. X superficial part of Y <=> if Y is subdivided into two superficial and deep portions, X is part of the superficial portion. BSPO:0001100 spatial in_superficial_part_of in_superficial_part_of in superficial part of X superficial part of Y <=> if Y is subdivided into two superficial and deep portions, X is part of the superficial portion. BSPO:cjm X superficial part of Y <=> if Y is subdivided into two superficial and deep portions, X is part of the deep portion. X superficial part of Y <=> if Y is subdivided into two superficial and deep portions, X is part of the deep portion. BSPO:0001101 spatial in_deep_part_of in_deep_part_of in deep part of X superficial part of Y <=> if Y is subdivided into two superficial and deep portions, X is part of the deep portion. BSPO:cjm X proximalmost part of Y <=> X is in proximal side of Y and X is adjacent to the proximal boundary of Y X proximalmost part of Y <=> X is in proximal side of Y and X is adjacent to the proximal boundary of Y BSPO:0001106 spatial proximalmost_part_of proximalmost_part_of proximalmost part of X proximalmost part of Y <=> X is in proximal side of Y and X is adjacent to the proximal boundary of Y https://orcid.org/0000-0002-6601-2165 X distalmost part of Y <=> X is in distal side of Y and X is adjacent to the distal boundary of Y X distalmost part of Y <=> X is in distal side of Y and X is adjacent to the distal boundary of Y BSPO:0001108 spatial distalmost_part_of distalmost_part_of distalmost part of X distalmost part of Y <=> X is in distal side of Y and X is adjacent to the distal boundary of Y https://orcid.org/0000-0002-6601-2165 BSPO:0001113 spatial preaxialmost_part_of preaxialmost_part_of preaxialmost part of x preaxial to y iff x is further along the preaxial-postaxial axis than y, towards the postaxial side. x preaxial to y iff x is further along the preaxial-postaxial axis than y, towards the postaxial side. BSPO:0001114 spatial posterior to (developmentally) posterior to (developmentally) postaxial_to postaxial_to postaxial to x preaxial to y iff x is further along the preaxial-postaxial axis than y, towards the postaxial side. http://medical-dictionary.thefreedictionary.com/postaxial posterior to (developmentally) MA:th BSPO:0001115 spatial postaxialmost_part_of postaxialmost_part_of postaxialmost part of X intersects median plane of iff X crosses the midine plane of Y. BSPO:0005001 spatial intersects_midsagittal_plane_of intersects_midsagittal_plane_of intersects midsagittal plane of x immediately anterior to y iff x anterior to y and x is contiguous with y. x immediately anterior to y iff x anterior to y and x is contiguous with y. BSPO:0015009 spatial immediately_anterior_to immediately_anterior_to immediately anterior to x immediately anterior to y iff x anterior to y and x is contiguous with y. BSPO:curators x immediately distal to y iff x distal to y and x is contiguous with y. x immediately distal to y iff x distal to y and x is contiguous with y. BSPO:0015010 spatial immediately_distal_to immediately_distal_to immediately distal to x immediately distal to y iff x distal to y and x is contiguous with y. BSPO:curators x immediately dorsal to y iff x dorsal to y and x is contiguous with y. x immediately dorsal to y iff x dorsal to y and x is contiguous with y. BSPO:0015011 spatial immediately_dorsal_to immediately_dorsal_to immediately dorsal to x immediately dorsal to y iff x dorsal to y and x is contiguous with y. BSPO:curators x immediately posterior to y iff x posterior_to y and x is contiguous with y. x immediately posterior to y iff x posterior_to y and x is contiguous with y. BSPO:0015012 spatial immediately_posterior_to immediately_posterior_to immediately posterior to x immediately posterior to y iff x posterior_to y and x is contiguous with y. BSPO:curators x immediately proximal to y iff x proximal to y and x is contiguous with y. x immediately proximal to y iff x proximal to y and x is contiguous with y. BSPO:0015013 spatial immediately_proximal_to immediately_proximal_to immediately proximal to x immediately proximal to y iff x proximal to y and x is contiguous with y. BSPO:curators x immediately superficial to y iff x superficial to y and x is contiguous with y. x immediately superficial to y iff x superficial to y and x is contiguous with y. BSPO:0015014 spatial immediately_superficial_to immediately_superficial_to immediately superficial to x immediately superficial to y iff x superficial to y and x is contiguous with y. BSPO:curators x immediately ventral to y iff x ventral to y and x is contiguous with y. x immediately ventral to y iff x ventral to y and x is contiguous with y. BSPO:0015015 spatial immediately_ventral_to immediately_ventral_to immediately ventral to x immediately ventral to y iff x ventral to y and x is contiguous with y. BSPO:curators x immediately left of y iff x left_of y and x is contiguous with y. x immediately left of y iff x left_of y and x is contiguous with y. BSPO:0015016 spatial immediately_left_of immediately_left_of immediately left of x immediately left of y iff x left_of y and x is contiguous with y. BSPO:curators x immediately right of y iff x right of y and x is contiguous with y. x immediately right of y iff x right of y and x is contiguous with y. BSPO:0015017 spatial immediately_right_of immediately_right_of immediately right of x immediately right of y iff x right of y and x is contiguous with y. BSPO:curators X dorsal side of Y <=> if Y is subdivided into two dorsal and ventral portions, X is part of the dorsal portion. X dorsal side of Y <=> if Y is subdivided into two dorsal and ventral portions, X is part of the dorsal portion. BSPO:0015101 spatial in_dorsal_side_of in_dorsal_side_of in dorsal side of X dorsal side of Y <=> if Y is subdivided into two dorsal and ventral portions, X is part of the dorsal portion. BSPO:cjm X ventral side of Y <=> if Y is subdivided into two dorsal and ventral portions, X is part of the ventral portion. X ventral side of Y <=> if Y is subdivided into two dorsal and ventral portions, X is part of the ventral portion. BSPO:0015102 spatial in_ventral_side_of in_ventral_side_of in ventral side of X ventral side of Y <=> if Y is subdivided into two dorsal and ventral portions, X is part of the ventral portion. BSPO:cjm nearer to the aboral opening of the organism, on the oral-aboral axis. nearer to the aboral opening of the organism, on the oral-aboral axis. BSPO:0015202 spatial aboral_to aboral_to aboral to nearer to the aboral opening of the organism, on the oral-aboral axis. BSPO:cjm x preaxial to y iff x is further along the preaxial-postaxial axis than y, towards the front. x preaxial to y iff x is further along the preaxial-postaxial axis than y, towards the front. BSPO:1000000 spatial anterior to (developmentally) anterior to (developmentally) lateral (radial) to medial (tibial) to preaxial_to preaxial_to preaxial to x preaxial to y iff x is further along the preaxial-postaxial axis than y, towards the front. http://medical-dictionary.thefreedictionary.com/preaxial anterior to (developmentally) MA:th has measurement unit label An information artifact IA mentions an entity E exactly when it has a component/part that denotes E 7/6/2009 Alan Ruttenberg. P4 RC1 munges our GCI so remove it for now: mentions some entity equivalentTo has_part some ('generically denotes' some entity) 7/6/2009 Alan Ruttenberg: Add this relation following conversation with Jonathan Rees that N&S GCI for is_about was too strong. Really it was simply sufficient. To effect this change we introduce this relation, which is subproperty of is_about, and have previous GCI use this relation "mentions" in it's (logical) definition PERSON: Jonathan Rees Person: Alan Ruttenberg mentions relating a cartesian spatial coordinate datum to a unit label that together with the values represent a point has coordinate unit label relates a process to a time-measurement-datum that represents the duration of the process Person:Alan Ruttenberg is duration of inverse of the relation of is quality measurement of 2009/10/19 Alan Ruttenberg. Named 'junk' relation useful in restrictions, but not a real instance relationship Person:Alan Ruttenberg is quality measured as A relation between a data item and a quality of a material entity where the material entity is the specified output of a material transformation which achieves an objective specification that indicates the intended value of the specified quality. Person:Alan Ruttenberg Person:Bjoern Peters is quality specification of inverse of the relation of is quality specification of 2009/10/19 Alan Ruttenberg. Named 'junk' relation useful in restrictions, but not a real instance relationship Person:Alan Ruttenberg Person:Bjoern Peters quality is specified as relates a time stamped measurement datum to the time measurement datum that denotes the time when the measurement was taken Alan Ruttenberg has time stamp relates a time stamped measurement datum to the measurement datum that was measured Alan Ruttenberg has measurement datum is_specified_input_of bearer of this apple is bearer of this red color this vase is bearer of this fragility Inverse of characteristic_of a relation between an independent continuant (the bearer) and a specifically dependent continuant (the dependent), in which the dependent specifically depends on the bearer for its existence A bearer can have many dependents, and its dependents can exist for different periods of time, but none of its dependents can exist when the bearer does not exist. bearer_of is bearer of bearer_of is bearer of bearer of has characteristic A journal article is an information artifact that inheres in some number of printed journals. For each copy of the printed journal there is some quality that carries the journal article, such as a pattern of ink. The journal article (a generically dependent continuant) is concretized as the quality (a specifically dependent continuant), and both depend on that copy of the printed journal (an independent continuant). An investigator reads a protocol and forms a plan to carry out an assay. The plan is a realizable entity (a specifically dependent continuant) that concretizes the protocol (a generically dependent continuant), and both depend on the investigator (an independent continuant). The plan is then realized by the assay (a process). A relationship between a generically dependent continuant and a specifically dependent continuant, in which the generically dependent continuant depends on some independent continuant in virtue of the fact that the specifically dependent continuant also depends on that same independent continuant. A generically dependent continuant may be concretized as multiple specifically dependent continuants. is concretized as A relationship between a specifically dependent continuant and a generically dependent continuant, in which the generically dependent continuant depends on some independent continuant in virtue of the fact that the specifically dependent continuant also depends on that same independent continuant. Multiple specifically dependent continuants can concretize the same generically dependent continuant. concretizes this red color is a quality of this apple a relation between a quality and an independent continuant (the bearer), in which the quality specifically depends on the bearer for its existence A quality inheres in its bearer at all times for which the quality exists. is quality of quality_of quality of this investigator role is a role of this person a relation between a role and an independent continuant (the bearer), in which the role specifically depends on the bearer for its existence A role inheres in its bearer at all times for which the role exists, however the role need not be realized at all the times that the role exists. is role of role_of role of a relation between two distinct material entities, the old entity and the new entity, in which the new entity begins to exist when the old entity ceases to exist, and the new entity inherits the significant portion of the matter of the old entity derives into is location of my head is the location of my brain this cage is the location of this rat a relation between two independent continuants, the location and the target, in which the target is entirely within the location Most location relations will only hold at certain times, but this is difficult to specify in OWL. See http://purl.obolibrary.org/obo/ro/docs/temporal-semantics/ location_of location of Containment obtains in each case between material and immaterial continuants, for instance: lung contained_in thoracic cavity; bladder contained_in pelvic cavity. Hence containment is not a transitive relation. If c part_of c1 at t then we have also, by our definition and by the axioms of mereology applied to spatial regions, c located_in c1 at t. Thus, many examples of instance-level location relations for continuants are in fact cases of instance-level parthood. For material continuants location and parthood coincide. Containment is location not involving parthood, and arises only where some immaterial continuant is involved. To understand this relation, we first define overlap for continuants as follows: c1 overlap c2 at t =def for some c, c part_of c1 at t and c part_of c2 at t. The containment relation on the instance level can then be defined (see definition): contained in contains This is redundant with the more specific 'independent and not spatial region' constraint. We leave in the redundant axiom for use with reasoners that do not use negation. This is redundant with the more specific 'independent and not spatial region' constraint. We leave in the redundant axiom for use with reasoners that do not use negation. A part of relation that applies only between occurents. is occurent part of occurent part of during which ends starts during ends during A is spatially_disjoint_from B if and only if they have no parts in common There are two ways to encode this as a shortcut relation. The other possibility to use an annotation assertion between two classes, and expand this to a disjointness axiom. Chris Mungall Note that it would be possible to use the relation to label the relationship between a near infinite number of structures - between the rings of saturn and my left earlobe. The intent is that this is used for parsiomoniously for disambiguation purposes - for example, between siblings in a jointly exhaustive pairwise disjointness hierarchy BFO_0000051 exactly 0 (BFO_0000050 some ?Y) spatially disjoint from https://github.com/obophenotype/uberon/wiki/Part-disjointness-Design-Pattern A relationship that holds between a biological entity and a phenotype. Here a phenotype is construed broadly as any kind of quality of an organism part, a collection of these qualities, or a change in quality or qualities (e.g. abnormally increased temperature). The subject of this relationship can be an organism (where the organism has the phenotype, i.e. the qualities inhere in parts of this organism), a genomic entity such as a gene or genotype (if modifications of the gene or the genotype causes the phenotype), or a condition such as a disease (such that if the condition inheres in an organism, then the organism has the phenotype). has phenptype X develops from y if and only if either (a) x directly develops from y or (b) there exists some z such that x directly develops from z and z develops from y develops from A relation that holds between two occurrents. This is a grouping relation that collects together all the Allen relations. temporally related to ends A faulty traffic light (material entity) whose malfunctioning (a process) is causally upstream of a traffic collision (a process): the traffic light acts upstream of the collision. c acts upstream of p if and only if c enables some f that is involved in p' and p' occurs chronologically before p, is not part of p, and affects the execution of p. c is a material entity and f, p, p' are processes. acts upstream of A gene product that has some activity, where that activity may be a part of a pathway or upstream of the pathway. c acts upstream of or within p if c is enables f, and f is causally upstream of or within p. c is a material entity and p is an process. affects acts upstream of or within https://wiki.geneontology.org/Acts_upstream_of_or_within Inverse of 'expressed in' expresses p 'results in development of' c if and only if p is a developmental process and p results in the state of c changing from its initial state as a primordium or anlage through its mature state and to its final state. results in development of results in maturation of A relationship that holds between entities participating in some developmental process (GO:0032502) developmentally related to c involved_in p if and only if c enables some process p', and p' is part of p actively involved in enables part of involved in https://wiki.geneontology.org/Involved_in inverse of regulates: process(P1) regulates process(P2) iff: P1 results in the initiation or termination of P2 OR affects the frequency of its initiation or termination OR affects the magnitude or rate of output of P2. regulated by inverse of negatively regulates: Process(P1) negatively regulates process(P2) iff: P1 terminates P2, or P1 descreases the the frequency of initiation of P2 or the magnitude or rate of output of P2. negatively regulated by inverse of positively regulates: Process(P1) postively regulates process(P2) iff: P1 initiates P2, or P1 increases the the frequency of initiation of P2 or the magnitude or rate of output of P2. positively regulated by results in growth of p 'results in determination of' c if and only if p is a developmental process and c is a cell and p results in the state of c changing to be determined. Once a cell becomes determined, it becomes committed to differentiate down a particular pathway regardless of its environment. results in determination of An organism that is a member of a population of organisms An organism that is a member of a population of organisms is member of is a mereological relation between a item and a collection. is member of is a mereological relation between a item and a collection. is member of is member of member part of member part of SIO member of 'input of' is a relation between a participant and a process, where the participant is present at the start of the process. is input of input of 'output of' is a relation between a participant and a process, where the participant is present at the end of the process. is output of output_of output of relation that links two events, processes, states, or objects such that one event, process, state, or object (a cause) contributes to the production of another event, process, state, or object (an effect) where the cause is partly or wholly responsible for the effect, and the effect is partly or wholly dependent on the cause. This branch of the ontology deals with causal relations between entities. It is divided into two branches: causal relations between occurrents/processes, and causal relations between material entities. We take an 'activity flow-centric approach', with the former as primary, and define causal relations between material entities in terms of causal relations between occurrents. To define causal relations in an activity-flow type network, we make use of 3 primitives: * Temporal: how do the intervals of the two occurrents relate? * Is the causal relation regulatory? * Is the influence positive or negative? The first of these can be formalized in terms of the Allen Interval Algebra. Informally, the 3 bins we care about are 'direct', 'indirect' or overlapping. Note that all causal relations should be classified under a RO temporal relation (see the branch under 'temporally related to'). Note that all causal relations are temporal, but not all temporal relations are causal. Two occurrents can be related in time without being causally connected. We take causal influence to be primitive, elucidated as being such that has the upstream changed, some qualities of the donwstream would necessarily be modified. For the second, we consider a relationship to be regulatory if the system in which the activities occur is capable of altering the relationship to achieve some objective. This could include changing the rate of production of a molecule. For the third, we consider the effect of the upstream process on the output(s) of the downstream process. If the level of output is increased, or the rate of production of the output is increased, then the direction is increased. Direction can be positive, negative or neutral or capable of either direction. Two positives in succession yield a positive, two negatives in succession yield a positive, otherwise the default assumption is that the net effect is canceled and the influence is neutral. Each of these 3 primitives can be composed to yield a cross-product of different relation types. Do not use this relation directly. It is intended as a grouping for a diverse set of relations, all involving cause and effect. causally related to relation that links two events, processes, states, or objects such that one event, process, state, or object (a cause) contributes to the production of another event, process, state, or object (an effect) where the cause is partly or wholly responsible for the effect, and the effect is partly or wholly dependent on the cause. https://en.wikipedia.org/wiki/Causality c involved in regulation of p if c is involved in some p' and p' regulates some p involved in regulation of c involved in regulation of p if c is involved in some p' and p' positively regulates some p involved in positive regulation of c involved in regulation of p if c is involved in some p' and p' negatively regulates some p involved in negative regulation of c involved in or regulates p if and only if either (i) c is involved in p or (ii) c is involved in regulation of p OWL does not allow defining object properties via a Union involved in or reguates involved in or involved in regulation of A relationship that holds between two entities in which the processes executed by the two entities are causally connected. Considering relabeling as 'pairwise interacts with' This relation and all sub-relations can be applied to either (1) pairs of entities that are interacting at any moment of time (2) populations or species of entity whose members have the disposition to interact (3) classes whose members have the disposition to interact. Note that this relationship type, and sub-relationship types may be redundant with process terms from other ontologies. For example, the symbiotic relationship hierarchy parallels GO. The relations are provided as a convenient shortcut. Consider using the more expressive processual form to capture your data. In the future, these relations will be linked to their cognate processes through rules. in pairwise interaction with interacts with http://purl.obolibrary.org/obo/ro/docs/interaction-relations/ http://purl.obolibrary.org/obo/MI_0914 An interaction that holds between two genetic entities (genes, alleles) through some genetic interaction (e.g. epistasis) genetically interacts with http://purl.obolibrary.org/obo/MI_0208 An interaction relationship in which the two partners are molecular entities that directly physically interact with each other for example via a stable binding interaction or a brief interaction during which one modifies the other. binds molecularly binds with molecularly interacts with http://purl.obolibrary.org/obo/MI_0915 Axiomatization to GO to be added later An interaction relation between x and y in which x catalyzes a reaction in which a phosphate group is added to y. phosphorylates The entity A, immediately upstream of the entity B, has an activity that regulates an activity performed by B. For example, A and B may be gene products and binding of B by A regulates the kinase activity of B. A and B can be physically interacting but not necessarily. Immediately upstream means there are no intermediate entity between A and B. molecularly controls directly regulates activity of The entity A, immediately upstream of the entity B, has an activity that negatively regulates an activity performed by B. For example, A and B may be gene products and binding of B by A negatively regulates the kinase activity of B. directly inhibits molecularly decreases activity of directly negatively regulates activity of The entity A, immediately upstream of the entity B, has an activity that positively regulates an activity performed by B. For example, A and B may be gene products and binding of B by A positively regulates the kinase activity of B. directly activates molecularly increases activity of directly positively regulates activity of An interaction relation between x and y in which x catalyzes a reaction in which one or more ubiquitin groups are added to y Axiomatization to GO to be added later ubiquitinates relation between physical entity and a process or stage X existence starts during y if and only if the time point at which x starts is after or equivalent to the time point at which y starts and before or equivalent to the time point at which y ends. Formally: x existence starts during y iff α(x) >= α(y) & α(x) <= ω(y). existence starts during X existence overlaps y if and only if either (a) the start of x is part of y or (b) the end of x is part of y. Formally: x existence starts and ends during y iff (α(x) >= α(y) & α(x) <= ω(y)) OR (ω(x) <= ω(y) & ω(x) >= α(y)) existence overlaps X existence ends during y if and only if the time point at which x ends is before or equivalent to the time point at which y ends and after or equivalent to the point at which y starts. Formally: x existence ends during y iff ω(x) <= ω(y) and ω(x) >= α(y). existence ends during A relationship between a material entity and a process where the material entity has some causal role that influences the process causal agent in process p is causally related to q if and only if p or any part of p and q or any part of q are linked by a chain of events where each event pair is one of direct activation or direct inhibition. p may be upstream, downstream, part of or a container of q. p is causally related to q if and only if p or any part of p and q or any part of q are linked by a chain of events where each event pair is one where the execution of p influences the execution of q. p may be upstream, downstream, part of, or a container of q. http://purl.obolibrary.org/obo/ro/docs/causal-relations Do not use this relation directly. It is intended as a grouping for a diverse set of relations, all involving cause and effect. causal relation between processes causal relation between processes The intent is that the process branch of the causal property hierarchy is primary (causal relations hold between occurrents/processes), and that the material branch is defined in terms of the process branch Do not use this relation directly. It is intended as a grouping for a diverse set of relations, all involving cause and effect. causal relation between entities A coral reef environment is determined by a particular coral reef s determined by f if and only if s is a type of system, and f is a material entity that is part of s, such that f exerts a strong causal influence on the functioning of s, and the removal of f would cause the collapse of s. The label for this relation is probably too general for its restricted use, where the domain is a system. It may be relabeled in future determined by (system to material entity) determined by inverse of determined by determines (material entity to system) determines The entity or characteristic A is causally upstream of the entity or characteristic B, A having an effect on B. An entity corresponds to any biological type of entity as long as a mass is measurable. A characteristic corresponds to a particular specificity of an entity (e.g., phenotype, shape, size). causally influences (entity-centric) causally influences This relation is intended to be used in combination with PATO, to be able to refine PATO quality classes using modifiers such as 'abnormal' and 'normal'. It has yet to be formally aligned into an ontological framework; it's not clear what the ontological status of the "modifiers" are. has modifier A relationship that holds between a material entity and a process in which causality is involved, with either the material entity or some part of the material entity exerting some influence over the process, or the process influencing some aspect of the material entity. Do not use this relation directly. It is intended as a grouping for a diverse set of relations, all involving cause and effect. causal relation between material entity and a process Holds between entity A (a transcription factor) and a nucleic acid B if and only if A down-regulates the expression of B. The nucleic acid can be a gene or an mRNA. represses expression of Holds between entity A (a transcription factor) and nucleic acid B if and only if A up-regulates the expression of B. The nucleic acid can be a gene or mRNA. increases expression of 2018-01-26T23:49:30Z acts upstream of or within, positive effect https://wiki.geneontology.org/Acts_upstream_of_or_within,_positive_effect 2018-01-26T23:49:51Z acts upstream of or within, negative effect https://wiki.geneontology.org/Acts_upstream_of_or_within,_negative_effect c 'acts upstream of, positive effect' p if c is enables f, and f is causally upstream of p, and the direction of f is positive 2018-01-26T23:53:14Z acts upstream of, positive effect https://wiki.geneontology.org/Acts_upstream_of,_positive_effect c 'acts upstream of, negative effect' p if c is enables f, and f is causally upstream of p, and the direction of f is negative 2018-01-26T23:53:22Z acts upstream of, negative effect https://wiki.geneontology.org/Acts_upstream_of,_negative_effect The entity A has an activity that regulates an activity of the entity B. For example, A and B are gene products where the catalytic activity of A regulates the kinase activity of B. regulates activity of The entity A has an activity that regulates the quantity or abundance or concentration of the entity B. regulates quantity of The entity A is not immediately upstream of the entity B but A has an activity that regulates an activity performed by B. indirectly regulates activity of The entity A has an activity that down-regulates by repression the quantity of B. The down-regulation is due to A having an effect on an intermediate entity (typically a DNA or mRNA element) which can produce B. For example, protein A (transcription factor) indirectly decreases by repression the quantity of protein B (gene product) if and only if A negatively regulates the process of transcription or translation of a nucleic acid element that produces B. decreases by repression quantity of The entity A has an activity that up-regulates by expression the quantity of B. The up-regulation is due to A having an effect on an intermediate entity (typically a DNA or mRNA element) which can produce B. For example, protein A (transcription factor) indirectly increases by expression the quantity of protein B (gene product) if and only if A positively regulates the process of transcription or translation of a nucleic acid element that produces B. increases by expression quantity of The entity A has an activity that directly positively regulates the quantity of B. directly positively regulates quantity of The entity A has an activity that directly negatively regulates the quantity of B. directly negatively regulates quantity of The entity A is not immediately upstream of the entity B and has an activity that up-regulates an activity performed by B. indirectly activates indirectly positively regulates activity of AKT1 destabilizes quantity of FOXO (interaction from Signor database: SIGNOR-252844) An entity A directly interacts with B and A has an activity that decreases the amount of an entity B by degradating it. destabilizes quantity of AKT1 stabilizes quantity of XIAP (interaction from Signor database: SIGNOR-119488) An entity A physically interacts with B and A has an activity that increases the amount of an entity B by stabilizing it. stabilizes quantity of The entity A is not immediately upstream of the entity B and has an activity that down-regulates an activity performed by B. indirectly inhibits indirectly negatively regulates activity of The entity A, immediately upstream of B, has an activity that directly regulates the quantity of B. directly regulates quantity of The entity A is not immediately upstream of the entity B, but A has an activity that regulates the quantity or abundance or concentration of B. indirectly regulates quantity of The entity A does not physically interact with the entity B, and A has an activity that down-regulates the quantity or abundance or concentration of B. indirectly negatively regulates quantity of The entity A does not physically interact with the entity B, and A has an activity that up-regulates the quantity or abundance or concentration of B. indirectly positively regulates quantity of A molecularly-interacts-with relationship between two entities, where the subject catalyzes a myristoylation activity that takes the object as input myristoylates mibolerone (CHEBI:34849) is agonist of androgen receptor (PR:P10275) a relation between a ligand (material entity) and a receptor (material entity) that implies the binding of the ligand to the receptor activates some activity of the receptor is agonist of pimavanserin (CHEBI:133017) is inverse agonist of HTR2A (PR:P28223) a relation between a ligand (material entity) and a receptor (material entity) that implies the binding of the ligand to the receptor inhibits some activity of the receptor to below basal level is inverse agonist of tretinoin (CHEBI:15367) is antagonist of Nuclear receptor ROR-beta (PR:Q92753) a relation between a ligand (material entity) and a receptor (material entity) that implies the binding of the ligand to the receptor reduces some activity of the receptor to basal level is antagonist of A relation between an axis and a part of an organism, in which the part defines the initial point of the axis. A relation between an axis and a part of an organism, in which the part defines the initial point of the axis. :has_start_point spatial has_start_point has_start_point Axes can be defined in a given species by subtyping the relevant axis type and stating a start and end point. has start point A relation between an axis and a part of an organism, in which the part defines the initial point of the axis. BSPO:cjm a relation that holds between a whole model/equation and an equation as a part has part equation is performed by has measurement value XYZTImageCollection A family of transmembrane proteins that play a role in the transport of organic anions including bile acids and bilirubin. OATP SLCO Solute Carrier Organic Anion OATP family A laboratory test or analysis of the biological activity of a substance performed by studying its effect in an experimental situation outside the organism, e.g. in the test tube rather than in living systems. A laboratory test or analysis of the biological activity of a substance performed by studying its effect in an experimental situation outside the organism, e.g. in the test tube rather than in living systems. in vitro assay A laboratory test or analysis of the biological activity of a substance performed by studying its effect in an experimental situation outside the organism, e.g. in the test tube rather than in living systems. https://ncim.nci.nih.gov/ncimbrowser/ConceptReport.jsp?dictionary=NCI Metathesaurus&code=C1511123 Organic Cation Transporter proteins carry positively charged chemical substances containing covalently bound carbon atoms through solubility barriers, such as lipid membranes or across epithelial layers. After binding substrate, transmembrane transporters often undergo an energy-dependent conformational change that moves the substrate across the membrane with (symport) or against (antiport) concentration gradients. OCT family Organic Cation Transport Protein Organic Cation Transporter Catalysis of the reaction: ATP + GTP = 2 diphosphate + cyclic GMP-AMP. cyclic GMP-AMP synthase activity cGAS activation HOIP:HOIP_0000001 P53 signaling is a process that a signal is transmitted by the PERK. PERK generally plays a endoplasmic reticulum membrane stress sensor role. p53 signaling HOIP_0000001 HOIP:HOIP_0000002 Phospholipase transport to lysosome is a subtype of molecule transport: A process of the directed movement of phospholipase to the lysosome. phospholipase transport to lysosome HOIP_0000002 HOIP:HOIP_0000003 Moving solid is a subtype of moving. A process that change the location of the solid. . moving solid HOIP_0000003 HOIP:HOIP_0000006 Abcb11 HOIP_0000006 HOIP:HOIP_0000007 Generating periodic motion is a subtype of generating motion: A process that generates the directed movement in which the object decreases in volume. generating periodic motion HOIP_0000007 HOIP:HOIP_0000008 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of cell death. cell death [cell death (course)] HOIP_0000008 HOIP:HOIP_0000009 Biological functions constantly adapt to functional demand to maintain a homeostatic steady state. Homeostatic imbalance course is a subtype of process sequence: A series of changing processes in an organism from a homeostatic balance to an imbalance between functional supply and functional demand. homeostasis imbalance course HOIP_0000009 HOIP:HOIP_0000010 Changing membrane fluidity is a subtype of changing fluidity: A process that changes the fluidity of the membrane. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID:1697167 PMID:2080227 PMID:22960355 changing membrane fluidity [phospholipidosis (severe)] HOIP_0000010 PMID:2080227 Cationic amphiphilic drugs and phospholipid storage disorder. HOIP:HOIP_0000011 Generating signal is a subtype of generating: A process that produces a signal as an output. generating signal HOIP_0000011 HOIP:HOIP_0000013 PPARalpha activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating PPAR alpha ( (Peroxisome Proliferator Activated Receptor Alpha)) with a nuclear receptor role to be higher. PPAR alpha activation activating peroxisome proliferator-activated receptor alpha PPARalpha activation HOIP_0000013 HOIP:HOIP_0000014 NCBI-Human-GeneID:8879 NCBI-Mouse-GeneID:20397 NCBI-Rat-GeneID:286896 Sgpl1 (mol) HOIP_0000014 NCBI-Human-GeneID:8879 https://www.ncbi.nlm.nih.gov/gene/8879 NCBI-Mouse-GeneID:20397 https://www.ncbi.nlm.nih.gov/gene/20397 NCBI-Rat-GeneID:286896 http://www.ncbi.nlm.nih.gov/gene/286896 HOIP:HOIP_0000015 Changing sensitivity is a subtype of changing quality: A process that changes the sensitivity of the object. changing sensitivity HOIP_0000015 HOIP:HOIP_0000016 Hypofunction of detoxification is a subtype of hypofunctioning: A process that performs a decreased or insufficient detoxification. This entity is a specific course-dependent process. This process can constitute the course of Hepatic encephalopathy. hypofunction of detoxification [hepatic encephalopathy] HOIP_0000016 HOIP:HOIP_0000017 Increasing ammonia concentration in blood is a subtype of increasing concentration: A process that changes the ammonia concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of Hepatic encephalopathy. increasing ammonia concentration in blood [Hepatic encephalopathy] HOIP_0000017 HOIP:HOIP_0000018 Arole played by the entity that isoenergetic transfer of ubiquitin from one protein to another via the reaction X-ubiquitin + Y -> Y-ubiquitin + X, where both the X-ubiquitin and Y-ubiquitin linkages are thioester bonds between the C-terminal glycine of ubiquitin and a sulfhydryl side group of a cysteine residue. GO:0061631 IMR:0000328 (obsolete) E2 ubiquitin-conjugating enzyme (E2) ubiquitin-conjugating enzyme HOIP_0000018 HOIP:HOIP_0000019 Generating substance is a subtype of generating: A process that produces a substance as an output. generating substance HOIP_0000019 HOIP:HOIP_0000020 Changing activity is a subtype of changing quality: A process that changes the activity of the object. changing activity HOIP_0000020 HOIP:HOIP_0000021 Inactivation is a subtype of changing activity: A process that changes the activity of the object to be lower. inactivation HOIP_0000021 HOIP:HOIP_0000022 Changing direction is a subtype of changing quality: A process that changes the direction of the object. changing direction HOIP_0000022 HOIP:HOIP_0000023 Molecular activation is a subtype of activating: A process that changes the activity of the moleule to be higher. molecular activation HOIP_0000023 HOIP:HOIP_0000024 Changing bond is a subtype of changing between operands: A process that changes a bond between objects. changing bond HOIP_0000024 HOIP:HOIP_0000025 Changing disulfide bond is a subtype of changing bond: A process that changes a disulfide bond which is a covalent bond mediated by 2 sulfur atoms. changing disulfide bond HOIP_0000025 HOIP:HOIP_0000027 Integrated signaling pathway is a subtype of pathway: Sequence of linked reactions, which has signaling pathway and gene regulated pathway. 1. signal detection (acceptance), 2. signal transduction, 3. gene regulation (genetic information conversion process), 4. celllular process execution This entity covers from 1, 2, and 3. integrated signaling pathway HOIP_0000027 HOIP:HOIP_0000029 Hepatic fibrosis dependent gene is a subtype of course dependent chemical entity. This gene can participate in the course of hepatic fibrosis as a gene product. Gene profile:Human/in vitro/Hepatocyte/ hepatic fibrosis dependent molecule (human in vitro) HOIP_0000029 HOIP:HOIP_0000030 Dysfunction of calcium transport is a subtype of dysfunctioning: A process that performs an abnormal and incomplete calcium transport. This entity is a specific course-dependent process. This process can constitute the course of necrosis. dysfunction of calcium transport [necrosis (course)] HOIP_0000030 HOIP:HOIP_0000031 CREBPH activation is a subtype of molecular activation: A process that changes the activity of the CRBPH to be higher. CREB3L3 activation HOIP_0000031 HOIP:HOIP_0000033 Acyl-CoA oxidase family EC 1.3.3.6 ACOX family HOIP_0000033 HOIP:HOIP_0000035 Hypofunction of extracellular matrix disassembly is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient extracellular matrix disassembly. hypofunction of extracellular matrix disassembly HOIP_0000035 HOIP:HOIP_0000036 A role played by the entity which regulates tranport process. tranport regulator role HOIP_0000036 HOIP:HOIP_0000037 Changing disulfide bond is a subtype of changing bond: A process that changes a disulfide bond which is a covalent bond mediated by 2 sulfur atoms. This entity is a specific course-dependent process. This process can constitute the course of ER stress. changing disulfide bond [ER stress] HOIP_0000037 HOIP:HOIP_0000038 A role played by the entity that has a toxic effect. toxic agent HOIP_0000038 HOIP:HOIP_0000040 Increasing weight is a subtype of changing weight: A process that changes the weight of the object to be higher. increasing weight HOIP_0000040 HOIP:HOIP_0000042 Mitochondrial dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete mitochondrial function. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. mitochondrial dysfunction [oxidative stress (course)] HOIP_0000042 HOIP:HOIP_0000044 ATF6 (golgi apparatus) (canonical)[ER stress] HOIP_0000044 HOIP:HOIP_0000045 Hypofunction of bile acid and bile salt transport is a subtype of hypofunction of transport: A process that performs a decreased or insufficient bile acid and bile salt transport. hypofunction of bile acid and bile salt transport HOIP_0000045 HOIP:HOIP_0000046 Cleavage of ATF6-alpha by S2P is a subtype of proteolysis: A process n which ATF6-alpha is cleaved by endopeptidase S2P( MBTPS2). Site-2 cleavage comes after site-1 cleavage. cleavage of ATF6-alpha by S2P HOIP_0000046 HOIP:HOIP_0000047 NCBI-Human-GeneID:4780 NCBI-Mouse-GeneID:18024 NCBI-Rat-GeneID:83619 PMID:25203443 NRF2 (canonical)[ER stress] HOIP_0000047 NCBI-Human-GeneID:4780 http://www.ncbi.nlm.nih.gov/gene/4780 NCBI-Mouse-GeneID:18024 http://www.ncbi.nlm.nih.gov/gene/18024 NCBI-Rat-GeneID:83619 http://www.ncbi.nlm.nih.gov/gene/83619 PMID:25203443 De-differentiation confers multidrug resistance via noncanonical PERK-Nrf2 signaling. HOIP:HOIP_0000048 Cleavage of ATF6-alpha by S1P is a subtype of proteolysis: A process in which ATF6-alpha is cleaved by endopeptidase S1P( MBTPS1). cleavage of ATF6-alpha by S1P HOIP_0000048 HOIP:HOIP_0000049 Cleavage of ATF6-alpha by S1P is a subtype of proteolysis: A process in which ATF6-alpha is cleaved by endopeptidase S1P( MBTPS1). This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:10564271 PMID:11163209 PMID:15299016 Reactome:R-HSA-381135 http://purl.obolibrary.org/obo/HINO_0008875 cleavage of ATF6-alpha by S1P [ER stress] HOIP_0000049 HOIP:HOIP_0000050 Inflammatory cytokine gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). inflammatory cytokine gene expression [non-alcoholic steatohepatitis (course)] HOIP_0000050 HOIP:HOIP_0000051 ChREBP activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating ChREBP to be higher. ChREBP activation HOIP_0000051 HOIP:HOIP_0000052 A monoatomic or polyatomic species having one or more elementary charges of the proton. cation HOIP_0000052 HOIP:HOIP_0000053 Translocation of ATF6 from the cytosol to the nucleus is a subtype of nuclear transport: A process that of the directed movement of ATF6 from the cytoplasm to the nucleus. Translocation of ATF6 from the cytosol to the nucleus HOIP_0000053 HOIP:HOIP_0000054 Increasing liver weight is a subtype of increasing weight: A process that changes the weight of the liver to be higher. increasing liver weight HOIP_0000054 HOIP:HOIP_0000055 Translocation of ATF6 from the cytosol to the nucleus is a subtype of nuclear transport: A process that of the directed movement of ATF6 from the cytoplasm to the nucleus. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:10564271 PMID:10856300 R-HSA-381026 Translocation of ATF6 from the cytosol to the nucleus [ER stress] HOIP_0000055 HOIP:HOIP_0000056 A role played by the entity which regulatess bile acid transport process. bile acid transport regulator role HOIP_0000056 HOIP:HOIP_0000057 Combining role with an extracellular or intracellular signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity or state as part of signal transduction. transmembrane signaling receptor role HOIP_0000057 HOIP:HOIP_0000058 Combining role with an extracellular messenger (called a death ligand), and transmitting the signal from one side of the plasma membrane to the other to initiate apoptotic or necrotic cell death. Combining role with an extracellular messenger (called a death ligand), and transmitting the signal from one side of the plasma membrane to the other to initiate apoptotic or necrotic cell death. related molecular function GO:0005035 death receptor role HOIP_0000058 Combining role with an extracellular messenger (called a death ligand), and transmitting the signal from one side of the plasma membrane to the other to initiate apoptotic or necrotic cell death. PMID:10209153 HOIP:HOIP_0000059 lysosome damage is a subtype of organelle damage. A process that injures the structure of the lysosome. lysosome damage HOIP_0000059 HOIP:HOIP_0000060 Ground glass appearance [Liver PathologicalFindings] is a type of finding observed in hepatocyte cytoplasm. Based on the pathological morphology, lesions are observed as a frosted-like change in whole or most of the hepatocytes. Monochromatic eosinophilic change across the whole or most of the hepatocyte. It is often observed as a changing response to the hepatic metabolism enzyme inducer such as phenobarbital. In electron microscopy, it is regarded as prominent proliferation of smooth endoplasmic reticulum, dispersion of rough endoplasmic reticulum, with decrease of stored glycogen. Monochromatic eosinophilic change across the whole or most of the hepatocyte. It is often observed as a changing response to the hepatic metabolism enzyme inducer such as phenobarbital. In electron microscopy, it is regarded as prominent proliferation of smooth endoplasmic reticulum, dispersion of rough endoplasmic reticulum, with decrease of stored glycogen. Open TG-GatesID:FI-L0830 ground glass appearance [Liver Pathological Findings] HOIP_0000060 Monochromatic eosinophilic change across the whole or most of the hepatocyte. It is often observed as a changing response to the hepatic metabolism enzyme inducer such as phenobarbital. In electron microscopy, it is regarded as prominent proliferation of smooth endoplasmic reticulum, dispersion of rough endoplasmic reticulum, with decrease of stored glycogen. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0000061 A process in which a signal to eIF2a is transduced by PERK. This process is dependent on the translation attenuation and can constitute the course of ER stress. PERK signaling to eIF2a [ER stress - translation attenuation] HOIP_0000061 HOIP:HOIP_0000062 A process in which a signal to eIF2a is transduced by PERK. This entity is a specific course-dependent process. This process can constitute the course of PERK - eIF2A pathway. PERK signaling to eIF2a [PERK - eIF2A pathway] HOIP_0000062 HOIP:HOIP_0000063 PERK dimerization is a subtype of protein dimerization: The formation of a PERK dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This entity is a specific course-dependent process. This process can constitute the course of ER stress and involves inflammation. Reactome:R-HSA-381087 http://www.ncbi.nlm.nih.gov/pubmed/11907036 PERK dimerization [ER stress - translation attenuation] HOIP_0000063 HOIP:HOIP_0000064 A role played by the protein that has a structure of misfolding unfolded protein role HOIP_0000064 HOIP:HOIP_0000065 Cellular tissue is a subtype of object aggregate that consists of cells or tissues. cellular tissue HOIP_0000065 HOIP:HOIP_0000067 PERK signaling (integrated pathway) is a subtype of integrated signaling pathway: Sequence of linked reactions, which has ATF6 signaling and gene regulation pathway. PERK signaling (integrated pathway) HOIP_0000067 HOIP:HOIP_0000068 Negative regulation of formation of cytoplasmic translation initiation complex is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of formation of cytoplasmic translation initiation complex. negative regulation of formation of translation initiation complex negative regulation of formation of cytoplasmic translation initiation complex HOIP_0000068 HOIP:HOIP_0000070 organelle damage is a subtype of damaging. organelle damage HOIP_0000070 HOIP:HOIP_0000071 The chemical reactions and pathways resulting in the breakdown of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid). sphingolipid breakdown sphingolipid catabolism sphingolipid degradation sphingolipid catabolic process HOIP_0000071 HOIP:HOIP_0000072 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required. insulin deficiency HOIP_0000072 HOIP:HOIP_0000073 natural killer cell activation is a subtype of macrophage activation: A change in morphology and behavior of a natural killer (NK) cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). natural killer cell activation [phospholipidosis (severe (excessive defense))] HOIP_0000073 HOIP:HOIP_0000074 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required. This entity is a specific course-dependent process. This process can constitute the course of ER stress. insulin deficiency [ER stress] HOIP_0000074 HOIP:HOIP_0000075 Increasing GDF15 level is a subtype of increasing quantity: A process that changes the amount of GDF15 level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 increasing GDF15 level [mitochondrial disorder (course)] HOIP_0000075 PMID:29222479 Treatment with alcohol also increased the levels of secreted GDF15 in supernatants of cultured hepatocytes. We next investigated the effect of mitochondrial dysfunction on GDF15 expression in hepatocytes. Inhibition of the mitochondrial OXPHOS complex using oligomycin or rotenone significantly increased Gdf15 expression and GDF15 secretion by cultured hepatocytes. Hepatic Gdf15 expression and serum levels of GDF15 were remarkably increased in alcohol-fed mice. It may drive the protective effect against alcohol- or CCl4-induced liver injury. This evidence suggests that mitochondrial dysfunction may be a double-edged sword, as it may affect disease progression as well as protection. HOIP:HOIP_0000080 A role played by the entity that shows an expression change according to the degree of tumor progression. tumor progression marker role HOIP_0000080 HOIP:HOIP_0000082 A role played by the entity which inhibits bile acid transport process. bile acid transport inhibitor role HOIP_0000082 HOIP:HOIP_0000083 Bile pigment deposition is a subtype of accumulation of pigments: The aggregation of bile pigmentin a particular location in an organism, tissue or cell. bile pigment deposition HOIP_0000083 HOIP:HOIP_0000085 Hypofunction of transmembrane transport is a subtype of hypofunction of transport: A process that performs a decreased or insufficient transmembrane transport. hypofunction of transmembrane transport HOIP_0000085 HOIP:HOIP_0000087 NCBI-Rat-GeneID:24908 https://omim.org/entry/602634 ERDJ4 Dnajb9 apoptosis inhibitor (rat)[ER stress] HOIP_0000087 NCBI-Rat-GeneID:24908 http://www.ncbi.nlm.nih.gov/gene/24908 HOIP:HOIP_0000088 Increasing acetyl CoA is a subtype of increasing quantity: A process that changes the amount of acetyl CoA to be larger. increasing acetyl CoA HOIP_0000088 HOIP:HOIP_0000090 PMID:26481188 meloxicam - apotosis inducing factor [ER stress] HOIP_0000090 HOIP:HOIP_0000091 Endoplasmic reticulum proliferation in hepatocyte is a subtype of increasing number of hepatocyte organelle: A process that becomes larger in the number of endoplasmic reticulum in hepatocyte(s). increasing number of hepatocellular endoplasmic reticulum endoplasmic reticulum proliferation in hepatocyte HOIP_0000091 HOIP:HOIP_0000093 Increasing number of objects is a subtype of changing: A process that becomes larger in the number of physical objects. increasing number of objects HOIP_0000093 HOIP:HOIP_0000094 Maintaining permeability is a subtype of changing permeability: A process that changes the permeability of the membrane to be lower. maintaining permeability HOIP_0000094 HOIP:HOIP_0000095 Hyperfunction of fatty acid beta-oxidation is a subtype of hyperfunction of fatty acid oxidation: A process that performs an excessive fatty acid beta-oxidation. hyperfunction of fatty acid beta-oxidation HOIP_0000095 HOIP:HOIP_0000097 A fatty acid oxidation process in which the methyl group at the end of the fatty acid molecule (the omega carbon) is first oxidized to a hydroxyl group, then to an oxo group, and finally to a carboxyl group. The long chain dicarboxylates derived from omega-oxidation then enter the beta-oxidation pathway for further degradation. fatty acid omega-oxidation HOIP_0000097 HOIP:HOIP_0000098 Hyperfunction of lipid oxidation is a subtype of hyperfunction of lipid catabolic process: A process that performs an excessive lipid degradation. hyperfunction of lipid oxidation HOIP_0000098 HOIP:HOIP_0000099 Hyperfunction of fatty acid oxidation is a subtype of hyperfunction of lipid oxidation: A process that performs an excessive fatty acid oxidation. http://purl.obolibrary.org/obo/MP_0014171 hyperfunction of fatty acid oxidation HOIP_0000099 HOIP:HOIP_0000100 Hyperfunction of lipid degradation is a subtype of hyperfunction of decompoing: A process that performs an excessive lipid degradation. http://purl.obolibrary.org/obo/MP_0008034 hyperfunction of lipid degradation HOIP_0000100 HOIP:HOIP_0000102 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. increasing demand for response to oxidative stress HOIP_0000102 HOIP:HOIP_0000104 Peroxisomal proliferation in hepatocyte is a subtype of hepatocyte organelle proliferation: A process that becomes larger in the number of peroxisome in hepatocyte(s). increasing peroxisome number in hepatocytes peroxisomal proliferation in hepatocyte HOIP_0000104 HOIP:HOIP_0000107 Peroxisomal Acox biosynthetic process is a subtype of protein production: A process that makes existent of a Peroxisomal acyl -coenzyme A oxidase (ACOX) due to biosynthesis or secretion resulting in an increase in its levels. peroxisomal Acox biosynthetic process HOIP_0000107 HOIP:HOIP_0000108 Organelle proliferation is a subtype of increasing number of objects: A process that becomes larger in the number of organelles. organelle proliferation HOIP_0000108 HOIP:HOIP_0000111 Molecule transport is a subtype of transport: A process of the directed movement of molecules into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter or pore.. molecule transport HOIP_0000111 HOIP:HOIP_0000112 A metabolic process by which 3-methyl branched fatty acids are degraded. These compounds are not degraded by the normal peroxisomal beta-oxidation pathway, because the 3-methyl blocks the dehydrogenation of the hydroxyl group by hydroxyacyl-CoA dehydrogenase. The 3-methyl branched fatty acid is converted in several steps to pristenic acid, which can then feed into the beta-oxidative pathway. GO:0001561 fatty acid alpha-oxidation HOIP_0000112 HOIP:HOIP_0000113 Controlling is a subtype of meta-function of "ToControl". When a function fa regularizes the behavior of ft, its meta-function is said to be 'to control ft'. controlling HOIP_0000113 HOIP:HOIP_0000114 Phosphoethanolamine catabolic process is a subtype of catabolic process: A process of the chemical reactions resulting in the breakdown of phosphoethanolamine. phosphoethanolamine catabolic process HOIP_0000114 HOIP:HOIP_0000115 Negative regulation of decomposing is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of decomposing. negative regulation of decomposing HOIP_0000115 HOIP:HOIP_0000117 Drug metabolism phase I by Cytochrome P450 is a subtype of drug metabolism phase I: A process that is biotransformed by cytochrome P450 (CYP) superfamily . This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. xenobiotic metabolism phase I by CyP [glutathione depletion (course)] xenobiotic metabolism phase I by P450 [glutathione depletion (course)] drug metabolism phase I by Cytochrome P450 [glutathione depletion (course)] HOIP_0000117 HOIP:HOIP_0000119 Regulation of beta oxidation related gene expression is a subtype of regulation of gene expression: A process that modulates the frequency, rate or extent of fatty acid beta oxidation related gene expression. regulation of beta oxidation related gene expression HOIP_0000119 HOIP:HOIP_0000120 phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate. NCBI-Human-GeneID:25833 NCBI-Mouse-GeneID:18988 NCBI-Rat-GeneID:116544 phospholipase A1 PLA1 (mol) HOIP_0000120 NCBI-Human-GeneID:25833 http://www.ncbi.nlm.nih.gov/gene/25833 NCBI-Mouse-GeneID:18988 http://www.ncbi.nlm.nih.gov/gene/18988 NCBI-Rat-GeneID:116544 http://www.ncbi.nlm.nih.gov/gene/116544 HOIP:HOIP_0000123 Receiving abnormal protein signal by PERK is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by PERK. This process is dependent on the translation attenuation and can constitute the course of ER stress. receiving abnormal protein signal by PERK [ER stress - translation attenuation] HOIP_0000123 HOIP:HOIP_0000124 Transcription factor activation is a subtype of molecular activation: A process that changes the activity of the molecule with a transcription factor role to be higher. transcription factor activation HOIP_0000124 HOIP:HOIP_0000126 Negative regulation of mRNA catabolic process is a subtype of negative regulation of decomposing: Any process that stops, prevents or reduces the frequency, rate or extent of mRNA catabolic process. down regulation of mRNA breakdown down regulation of mRNA catabolic process down regulation of mRNA catabolism down regulation of mRNA degradation negative regulation of mRNA catabolic process HOIP_0000126 HOIP:HOIP_0000129 Regulation of mitochondrial beta oxidation related gene is a subtype of regulation of beta oxidation related gene expression: A process that modulates the frequency, rate or extent of mitochondrial fatty acid beta oxidation related gene expression. regulation of mitochondrial beta oxidation related gene HOIP_0000129 HOIP:HOIP_0000131 Lipid transport to mitochondria is a subtype of lipid transport: A process that of the directed movement of lipids into a mitochondrion. lipid transport to mitochondria HOIP_0000131 HOIP:HOIP_0000132 Unfolded protein is a subtype of substance with role. This entity can participate in a unfolded protein response in the course of ER stress. unfolded protein [ER stress] HOIP_0000132 HOIP:HOIP_0000133 Maintaining membrane permeability is a subtype of maintaining permeability: A process that keeps the permeability of the membrane. maintaining membrane permeability HOIP_0000133 HOIP:HOIP_0000134 Biological structure formation is a subtype of having extra parts: A process that changes to form a structure component. biological structure formation HOIP_0000134 HOIP:HOIP_0000135 NCBI-Human-GeneID:2539 NCBI-Rat-GeneID:24377 PMID:24287781 http://omim.org/entry/305900 G6PD (canonical)[glutathione depletion (course)] HOIP_0000135 NCBI-Human-GeneID:2539 http://www.ncbi.nlm.nih.gov/gene/2539 NCBI-Rat-GeneID:24377 http://www.ncbi.nlm.nih.gov/gene/24377 HOIP:HOIP_0000137 NCBI-Human-GeneID:1647 NCBI-Mouse-GeneID:13197 NCBI-Rat-GeneID:25112 GADD45A (canonical)[glutathione depletion (course)] HOIP_0000137 NCBI-Human-GeneID:1647 http://www.ncbi.nlm.nih.gov/gene/1647 NCBI-Mouse-GeneID:13197 http://www.ncbi.nlm.nih.gov/gene/13197 NCBI-Rat-GeneID:25112 http://www.ncbi.nlm.nih.gov/gene/25112 HOIP:HOIP_0000138 Increasing size is a subtype of changing size: A process that changes the size of the object to be larger. A size change process in which the size is increasing. increasing size HOIP_0000138 HOIP:HOIP_0000139 Increasing volume is a subtype of increasing size: A process that changes the volume of the object to be higher. increasing volume HOIP_0000139 HOIP:HOIP_0000140 Increasing area is a subtype of changing area: A process that changes the area of the object to be larger. increasing area HOIP_0000140 HOIP:HOIP_0000141 Increasing length is a subtype of changing length: A process that changes the length of the object to be higher. increasing length HOIP_0000141 HOIP:HOIP_0000142 Increasing cell volume is a changing process to change the volume of the cell to increase. cell swelling increasing cell volume HOIP_0000142 HOIP:HOIP_0000143 Increasing volume of mitochondria is a changing process to change the volume of the mitochondria to increase. increasing volume of mitochondria HOIP_0000143 HOIP:HOIP_0000144 Increasing energy is a subtype of increasing quantity: A process that changes the amount of energy to be larger. increasing energy HOIP_0000144 HOIP:HOIP_0000145 Function-related process is a process that related to the execution of a function, a metafunction, and the malfunction. FBRL: A Function and Behavior Representation Language. Sasajima, M., Kitamura, Y., Ikeda, M. & Mizoguchi, R., In Proc. of IJCAI-95 (pp. 1830-1836), 1995 doi:10.1115/DETC2006-9913 https://doi.org/10.1016/S1474-0346(02)00006-X This tree is based on a functional concept ontology (Kitamura 2002). function-related process HOIP_0000145 doi:10.1115/DETC2006-9913 An ontology-based annotation framework for representing the functionality of engineering devices. Kitamura, Y., Washio, N., Koji, Y., Sasajima, M., Takafuji, S., & Mizoguchi, R., In Proc. of ASME 2006 International Design Engineering Technical Conferences & Computers and Information in Engineering Conference (ASME IDETC/CIE 2006), DETC2006-99131, 2006. https://doi.org/10.1016/S1474-0346(02)00006-X A functional concept ontology and its application to automatic identification of functional structures, Kitamura, Y., Sano, T., Namba, K., & Mizoguchi, R., Advanced Engineering Informatics, 16(2),145-163, 2002 HOIP:HOIP_0000147 Refolding-unfolding imbalance is a subtype of imbalance: A process that lacks a balance between protein refolding and unfolding. This entity is a specific course-dependent process. This process can constitute the course of ER stress. refolding-unfolding imbalance [ER stress] HOIP_0000147 HOIP:HOIP_0000148 Massive hepatic necrosis is a subtype of classification of cell death by distribution: A hepatocyte necrosis localized around multiple lobules. massive hepatic necrosis HOIP_0000148 HOIP:HOIP_0000150 NCBI-Human-GeneID:23645 NCBI-Mouse-GeneID:17872 NCBI-Rat-GeneID:171071 GADD34 (mol) HOIP_0000150 NCBI-Human-GeneID:23645 http://www.ncbi.nlm.nih.gov/gene/23645 NCBI-Mouse-GeneID:17872 http://www.ncbi.nlm.nih.gov/gene/17872 NCBI-Rat-GeneID:171071 http://www.ncbi.nlm.nih.gov/gene/171071 HOIP:HOIP_0000152 TIMP1 production is a subtype of protein production: A process that makes existent of a TIMP1 protein due to biosynthesis or secretion resulting in an increase in its levels. TIMP1 production HOIP_0000152 HOIP:HOIP_0000154 A role played by the entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. electron carrier electron transporter related molecular function GO:0009055 electron transfer moecule HOIP_0000154 HOIP:HOIP_0000155 A role played by the entity that causes blood cells to grow and mature (Haematopoiesis). hematopoietic factor HOIP_0000155 HOIP:HOIP_0000156 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). inflammatory cell infiltration [phospholipidosis (severe (excessive defense))] HOIP_0000156 HOIP:HOIP_0000157 Decreasing sensitivity is a subtype of changing sensitivity: A process that changes the sensitivity to be lower. decreasing sensitivity HOIP_0000157 HOIP:HOIP_0000158 Nuclear receptor activation is a subtype of activation of transcription factor: A process that changes the activity of the molecule with a nuclear receptor role to be higher. nuclear receptor activation nuclear receptor activation HOIP_0000158 HOIP:HOIP_0000159 PMID:25450203 PPAR alpha Peroxisome Proliferator-Activated Receptor Alpha PPARA (mol) HOIP_0000159 HOIP:HOIP_0000160 Androgen Receptor AR HOIP_0000160 HOIP:HOIP_0000161 Progesterone Receptor PGR (mol) HOIP_0000161 HOIP:HOIP_0000162 PPAR gamma Peroxisome Proliferator-Activated Receptor Gamma PPARG HOIP_0000162 HOIP:HOIP_0000163 Release of phospholipid from lysosome is a subtype of moving A to the outside of B: A process that that moves phospholipids to the outside of the lysosome. release of phospholipid from lysosome HOIP_0000163 HOIP:HOIP_0000164 Increasing hepatocellular volume is a subtype of increasing cell volume to change the volume of the hepatocyte to increase. hepatocellular hypertrophy hepatocellular swelling increasing hepatocellular volume HOIP_0000164 HOIP:HOIP_0000166 Addition of foreign substance is a subtype of assembling: A process that foreign substance to make an addition. addition of foreign substance HOIP_0000166 HOIP:HOIP_0000167 Dysfunction of calcium transport is a subtype of dysfunctioning: A process that performs an abnormal and incomplete calcium transport. dysfunction of calcium transport HOIP_0000167 HOIP:HOIP_0000168 Having extra parts is a subtype of changing structure: A process that changes to have additional parts of the structure. having extra parts HOIP_0000168 HOIP:HOIP_0000169 Accumulation of xenobiotics is a subtype of accumulation of substances in a biological object: A process that keeps xenobiotics in an organism, tissue, organelle, or cell. accumulation of xenobiotics HOIP_0000169 HOIP:HOIP_0000170 Accumulation of compound in ER is a subtype of accumulation of xenobiotics: A process that keeps compound in the ER (endoplasmic reticulum). This entity is a specific course-dependent process. This process can constitute the course of ER stress. accumulation of compound in ER [ER stress] HOIP_0000170 HOIP:HOIP_0000171 A role played by the role which catalyse the joining of two molecules with concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate. EC:6.-.-.- related molecular function GO:0016874 ligase HOIP_0000171 HOIP:HOIP_0000172 A role played by a chemical substance that reacts with the endogenous target molecule or critically alters the biological environment, initiating structural/functional alternations that result in toxicity. A role played by a chemical substance that reacts with the endogenous target molecule or critically alters the biological environment, initiating structural/functional alternations that result in toxicity. ultimate toxicant HOIP_0000172 A role played by a chemical substance that reacts with the endogenous target molecule or critically alters the biological environment, initiating structural/functional alternations that result in toxicity. ISBN:0071769234 HOIP:HOIP_0000173 Drug metabolism phase I is a subtype of drug metabolic process: A process that of biotransformation reactions involving hydrolysis, reduction, and oxidation or introduces a functional group (such as -OH, -NH2, -SH or -COOH) to increase in the water solubility of a xenobiotic. Functionalization of exogenous substances to prepare them for conjugation in PHASE II DETOXIFICATION. Phase I enzymes include CYTOCHROME P450 enzymes and some OXIDOREDUCTASES. Excess induction of phase I over phase II detoxification leads to higher levels of FREE RADICALS that can induce CANCER and other cell damage. Induction or antagonism of phase I detoxication is the basis of a number of DRUG INTERACTIONS. MeSH:D050216 Reactome: R-HSA-211945 http://purl.bioontology.org/ontology/MESH/D050216 Phase 1 of metabolism is concerned with functionalization, that is the introduction or exposure of functional groups on the chemical structure of a compound. This provides a 'handle' for phase 2 conjugating species with which to react with. Many xenobiotics are lipophilic and almost chemically inert (e.g. PAHs) so would not necessarily undergo a phase 2 reaction. Making them more chemically reactive would facilitate their excretion but also increases their chance of reacting with cellular macromolecules (e.g. proteins, DNA). There is a fine balance between producing a more reactive metabolite and conjugation reactions. There are two groups of enzymes in phase 1 - oxidoreductases and hydrolases. Oxidoreductases introduce an oxygen atom into or remove electrons from their substrates. The major oxidoreductase enzyme system is called the P450 monooxygenases. Other systems include flavin-containing monooxygenases (FMO), cyclooxygenases (COX) and monoamine oxidases (MAO). Hydrolases hydrolyse esters, amides, epoxides and glucuronides. Phase 1 of metabolism is concerned with functionalization, that is the introduction or exposure of functional groups on the chemical structure of a compound. This provides a 'handle' for phase 2 conjugating species with which to react with. Many xenobiotics are lipophilic and almost chemically inert (e.g. PAHs) so would not necessarily undergo a phase 2 reaction. Making them more chemically reactive would facilitate their excretion but also increases their chance of reacting with cellular macromolecules (e.g. proteins, DNA). There is a fine balance between producing a more reactive metabolite and conjugation reactions. There are two groups of enzymes in phase 1 - oxidoreductases and hydrolases. Oxidoreductases introduce an oxygen atom into or remove electrons from their substrates. The major oxidoreductase enzyme system is called the P450 monooxygenases. Other systems include flavin-containing monooxygenases (FMO), cyclooxygenases (COX) and monoamine oxidases (MAO). Hydrolases hydrolyse esters, amides, epoxides and glucuronides. drug metabolism phase I HOIP_0000173 Reactome: R-HSA-211945 Phase 1 - Functionalization of compounds (Homo sapiens) Phase 1 of metabolism is concerned with functionalization, that is the introduction or exposure of functional groups on the chemical structure of a compound. This provides a 'handle' for phase 2 conjugating species with which to react with. Many xenobiotics are lipophilic and almost chemically inert (e.g. PAHs) so would not necessarily undergo a phase 2 reaction. Making them more chemically reactive would facilitate their excretion but also increases their chance of reacting with cellular macromolecules (e.g. proteins, DNA). There is a fine balance between producing a more reactive metabolite and conjugation reactions. There are two groups of enzymes in phase 1 - oxidoreductases and hydrolases. Oxidoreductases introduce an oxygen atom into or remove electrons from their substrates. The major oxidoreductase enzyme system is called the P450 monooxygenases. Other systems include flavin-containing monooxygenases (FMO), cyclooxygenases (COX) and monoamine oxidases (MAO). Hydrolases hydrolyse esters, amides, epoxides and glucuronides. Reactome: R-HSA-211945 HOIP:HOIP_0000175 Peroxisome fatty acid beta oxidation gene expression is a subtype of gene expression: A process that The process in which a gene sequence is converted into a mature peroxisome fatty acid beta oxidation gene product or products (proteins or RNA) . peroxisome fatty acid beta oxidation gene expression HOIP_0000175 HOIP:HOIP_0000177 Hyperfunction of peroxisomal fatty acid beta-oxidation is a subtype of hyperfunction of fatty acid beta-oxidation: A process that performs an excessive peroxisomal fatty acid beta-oxidation. hyperfunction of peroxisomal fatty acid beta-oxidation HOIP_0000177 HOIP:HOIP_0000180 Increasing demand for peroxisomal fatty acid beta oxidation is a subtype of increasing functional demand: A process that changes the functional demand for peroxisomal fatty acid beta oxidation to be higher. increasing demand for peroxisomal fatty acid beta oxidation HOIP_0000180 HOIP:HOIP_0000183 Regulation of cell cycle related gene expression is a subtype of regulation of gene expression: A process that modulates the frequency, rate or extent of cel cycle related gene expression. regulation of cell cycle related gene expression HOIP_0000183 HOIP:HOIP_0000185 Biochemical degradation is a subtype of decompoing: A process that biochemically decomposes a single chemical entity into multiple element biochemical degradation HOIP_0000185 HOIP:HOIP_0000186 A role played by the protein related to the microtubules of the cytoskeleton. IMR:0000196 (obsolete) related cell structure GO:0015630 microtubule cytoskeletal protein HOIP_0000186 HOIP:HOIP_0000189 A role played by the entity that ihibits the obesity. inhibitor of obesity HOIP_0000189 HOIP:HOIP_0000193 PMID:23856494 ATP dependent GCLC (canonical)[glutathione depletion (course)] HOIP_0000193 PMID:23856494 GSH is synthesized by two successive enzymatic reactions (Fig. 1). The first reaction, catalyzed by glutamate cysteine ligase (GCL), couples L-glutamate to L-cysteine to form γ-glutamylcysteine (γ-GC) . HOIP:HOIP_0000194 Accumulation of abnormal proteins in ER is a subtype of accumulation of abnormal proteins: A process that keeps abnormal protein(s) in the ER (endoplasmic reticulum). This entity is a specific course-dependent process. This process can constitute the course of ER stress. accumulation of abnormal proteins in ER [ER stress] HOIP_0000194 HOIP:HOIP_0000195 Any process that modulates the frequency, rate or extent of gene expression by miRNA. regulation of gene expression by miRNA HOIP_0000195 HOIP:HOIP_0000197 Oncogene mRNA stabilization is a subtype of keeping structure: A process that maintaing the mRNA structure of ongogenes. oncogene mRNA stabilization HOIP_0000197 HOIP:HOIP_0000200 Phospholipid transport from lysosome is a subtype of phospholipid transfer : A process of the transfer of a phospholipid from the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). phospholipid transport from lysosome into cytosol [phospholipidosis (normal course)] HOIP_0000200 HOIP:HOIP_0000201 An inorganic radical in which a free electron resides on one or more oxygen atoms of an oxygen species. oxygen radical HOIP_0000201 HOIP:HOIP_0000203 Liver dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete liver function. liver dysfunction HOIP_0000203 HOIP:HOIP_0000204 The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. autophagy [ER stress] HOIP_0000204 HOIP:HOIP_0000205 Redox-active reactant formation is a subtype of biosynthetic process: A process that that generates a redox-active reactant. A number of xenobiotics exert a toxic effect theough their metabolites. The increased reactivity may be due to conversion into electrophiles, free radicals, nucleophiles, or redox-active reactants. Casarett and Doull's toxicology 8th ed. Chapter 3 step1 Delibery:From the site to exposure to the target redox-active reactant formation HOIP_0000205 HOIP:HOIP_0000206 Liver dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete liver function. This entity is a specific course-dependent process. This process can constitute the course of ER stress. liver dysfunction [ER stress] HOIP_0000206 HOIP:HOIP_0000207 Dysfunction of sodium transport is a subtype of dysfunctioning: A process that performs an abnormal and incomplete sodium transport dysfunction of sodium transport HOIP_0000207 HOIP:HOIP_0000208 Dysfunction of generating protein is a subtype of dysfunctioning: A process that performs an abnormal and incomplete generating protein. dysfunction of generating protein HOIP_0000208 HOIP:HOIP_0000209 Free radicals formation is a subtype of biosynthetic process: A process that that generates a free radical, a highly reactive molecule with an unsatisfied electron valence pair. A number of xenobiotics exert a toxic effect theough their metabolites. The increased reactivity may be due to conversion into electrophiles, free radicals, nucleophiles, or redox-active reactants. Casarett and Doull's toxicology 8th ed. Chapter 3 step1 Delibery:From the site to exposure to the target free radicals formation HOIP_0000209 HOIP:HOIP_0000210 Nucleophiles formation is a subtype of biosynthetic process: The chemical reaction resulting in the formation of nucleophiles by donating electrons. A number of xenobiotics exert a toxic effect theough their metabolites. The increased reactivity may be due to conversion into electrophiles, free radicals, nucleophiles, or redox-active reactants. Casarett and Doull's toxicology 8th ed. Chapter 3 step1 Delibery:From the site to exposure to the target Nucleophiles generally are detoxificated by conjugation of a functinal group to the nucleophilic atom. Sulfonation, glucuronidation, methylation, and acetylation are common reactions. nucleophiles formation HOIP_0000210 HOIP:HOIP_0000211 IL-2 gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature IL-2 gene product or products (proteins or RNA). IL-2 gene expression HOIP_0000211 HOIP:HOIP_0000212 Electrophiles formation is a subtype of biosynthetic process: A process that that generates electrophiles. Electrophile is a reagent that forms a bond to its reaction partner (the nucleophile) by accepting both bonding electrons from that reaction partner.. A number of xenobiotics exert a toxic effect theough their metabolites. Electrophiles are molecules that contain an electron-deficient atom with a partial or full positive charge that can react by sharing electron pairs with electron rich atoms in nucleophiles. Electrophilic toxicants generally are detoxificated by conjugation of with the nucleophile, glutathione. This reaction can be facilitated by glutathione S-trasferases. electrophiles formation HOIP_0000212 HOIP:HOIP_0000213 Protein quality control for misfolded or incompletely synthesized proteins is a subtype of keeping quality: A process that maintains the protein quality. protein quality control for misfolded or incompletely synthesized proteins GO:0006515 (protein quality control for misfolded or incompletely synthesized proteins) focuses on ERAD process. Our entity includes the process such as protein folding, ERAD and translation attenuation for unfolded protein response. protein quality control for unfolded proteins HOIP_0000213 HOIP:HOIP_0000214 Protein quality control for misfolded or incompletely synthesized proteins is a subtype of keeping quality: A process that maintains the protein quality mediated by the gene expression regulation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. protein quality control for unfolded via gene expression regulation [ER stress] HOIP_0000214 HOIP:HOIP_0000215 Dysfunction of protein quality control is a subtype of dysfunctioning: A process that performs an abnormal and incomplete protein quality control function. dysfunction of protein quality control HOIP_0000215 HOIP:HOIP_0000216 Increasing number of stress responses is a subtype of increasing number of actions: A process that becomes larger in the number of stress responses. increasing number of stress responses HOIP_0000216 HOIP:HOIP_0000218 Icreasing volume of endoplasmic reticulum is a subtype of increasing organelle volume: A process that changes the volume of the endoplasmic reticulum to be higher. icreasing volume of endoplasmic reticulum HOIP_0000218 HOIP:HOIP_0000220 Deacreasing size is a subtype of changing size: A process that changes the size of the object to be smaller. deacreasing size HOIP_0000220 HOIP:HOIP_0000221 Hepatocellular atrophy is a subtype of decreasing volume: A process that changes the volume of the hepatocyte to be relatively low. hepatocellular atrophy HOIP_0000221 HOIP:HOIP_0000222 Damaging is a subtype of changing structure: A process that injuries the structure as the direct or indirect result of an external force. http://purl.bioontology.org/ontology/MESH/D014947 injury http://purl.obolibrary.org/obo/OGMS_0000102 damaging HOIP_0000222 HOIP:HOIP_0000223 Drug-, radiation-induced, or spontaneous injuries to DNA that introduce deviations from its normal double-helical conformation. These changes include structural distortions that interfere with replication and transcription, as well as point mutations that disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. If the damage is minor, it can often be repaired (DNA repair); extensive damage can induce apoptosis. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. DNA damage [apoptosis (course)] HOIP_0000223 HOIP:HOIP_0000224 TIMP1 production is a subtype of protein production: A process that makes existent of a TIMP1 protein due to biosynthesis or secretion resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. TIMP1 production [hepatic fibrosis course] HOIP_0000224 HOIP:HOIP_0000225 Cellular damage is a subtype of damaging: A process that injures the structure of the cell as the direct or indirect result of an external force. Cell damage (also known as cell injury) is a variety or changes of stress that a cell suffers due to external as well internal environmental changes. Among other causes, this can be due to physical, chemical, infectious, biological, nutritional or immunological factors. Cell damage can be reversible or irreversible. Depending on the extent of injury, the cellular response may be adaptive and where possible, homeostasis is restored. Cell death occurs when the severity of the injury exceeds the cell’s ability to repair itself. Cell death is relative to both the length of exposure to a harmful stimulus and the severity of the damage caused. Cell death may occur by necrosis or apoptosis. cell and tissue damage cell and tissue damage PMID:8703628 http://purl.jp/bio/4/id/200906069918862451 https://en.wikipedia.org/wiki/Cell_damage cellular damage HOIP_0000225 cell and tissue damage http://purl.obolibrary.org/obo/MPATH_1 HOIP:HOIP_0000226 Cellular damage is a subtype of damaging: A process that injuries the structure of the cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of necrosis. cellular damage [necrosis (course)] HOIP_0000226 HOIP:HOIP_0000227 Cytoskeleton damage is a subtype of cellular damage: A process that injures the structure of the cytoskeleton as the direct or indirect result of an external force. cytoskeleton damage HOIP_0000227 HOIP:HOIP_0000228 Six proteins were regulated at both basal and inducible levels exhibiting the largest dynamic range of Nrf2 regulation: cytochrome P4502A5 (CYP2A5; 17.2-fold), glutathione-S-transferase-Mu 3 (GSTM3; 6.4-fold), glutathione-S-transferase Mu 1 (GSTM1; 5.9-fold), ectonucleoside-triphosphate diphosphohydrolase (ENTPD5; 4.6-fold), UDP-glucose-6-dehydrogenase (UDPGDH; 4.1-fold) and epoxide hydrolase (EPHX1; 3.0-fold). These proteins, or their products, thus provide a potential source of biomarkers for Nrf2 activity. NCBI-Human-GeneID:2947 NCBI-Mouse-GeneID:14864 NCBI-Rat-GeneID:108348148 PMID:22496397 PMID:25202346 GSTM3 (canonical)[glutathione depletion (course)] HOIP_0000228 NCBI-Human-GeneID:2947 http://www.ncbi.nlm.nih.gov/gene/2947 NCBI-Mouse-GeneID:14864 http://www.ncbi.nlm.nih.gov/gene/14864 NCBI-Rat-GeneID:108348148 http://www.ncbi.nlm.nih.gov/gene/108348148 PMID:22496397 Coordinated regulation of hepatic phase I and II drug-metabolizing genes and transporters using AhR-, CAR-, PXR-, PPARα-, and Nrf2-null mice. PMID:25202346 GSTM3 overexpression sensitized the PLC/PRF/5R cells to radiation mainly though induction of apoptosis. GSTM3 increased the expression of cell cycle- and apoptosis-related genes (Bcl-2, Bax, p21, p27 and p53) in PRF/PLC/5R cells with irradiation HOIP:HOIP_0000229 NCBI-Human-GeneID:2940 NCBI-Mouse-GeneID:14859 NCBI-Rat-GeneID:494500 GSTA3 (canonical)[glutathione depletion (course)] HOIP_0000229 NCBI-Human-GeneID:2940 http://www.ncbi.nlm.nih.gov/gene/2940 NCBI-Mouse-GeneID:14859 http://www.ncbi.nlm.nih.gov/gene/14859 NCBI-Rat-GeneID:494500 http://www.ncbi.nlm.nih.gov/gene/494500 HOIP:HOIP_0000230 Gene expression by AP-1 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by AP-1. gene expression by AP-1 HOIP_0000230 HOIP:HOIP_0000231 The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. membrane blebbing [apoptosis (course)] HOIP_0000231 HOIP:HOIP_0000232 Increasing membrane permeabilization is a subtype of changing permeability: A process that changes the permeability of the membrane to be higher. increasing membrane permeabilization HOIP_0000232 HOIP:HOIP_0000233 Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). positive regulation of mitochondrial membrane permeability [phospholipidosis (severe)] HOIP_0000233 HOIP:HOIP_0000234 Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. GO:1902110 positive regulation of mitochondrial membrane permeability [apoptosis (course)] HOIP_0000234 GO:1902110 positive regulation of mitochondrial membrane permeability involved in apoptotic process HOIP:HOIP_0000235 Dysregulation of apoptosis is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of apoptotic process appropriately or cannot realize it at all. dysregulation of apoptosis HOIP_0000235 HOIP:HOIP_0000236 A pathologic process that involves the transformation of normal cells to a neoplastic state and resulting in polyclonal or monoclonal neoplastic cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of cell death. tumorigenesis [cell death (course)] HOIP_0000236 HOIP:HOIP_0000237 Gene expression by p53 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by XBP1. gene expression by p53 HOIP_0000237 HOIP:HOIP_0000238 Changing cytoskeleton is a subtype of changing structure: A process that changes the structure of cytoskeleton. changing cytoskeleton HOIP_0000238 HOIP:HOIP_0000239 Changing cytoskeleton is a subtype of changing structure: A process that changes the structure of cytoskeleton. This entity is a specific course-dependent process. This process can constitute the course of anoikis. changing cytoskeleton [anoikis (course)] HOIP_0000239 HOIP:HOIP_0000240 Hypofunction of keeping structure is a subtype of hypofunctioning: A process that performs a decreased or insufficient keeping structure. hypofunction of keeping structure HOIP_0000240 HOIP:HOIP_0000241 Hypofunction of keeping structure is a subtype of hypofunctioning: A process that performs a decreased or insufficient keeping structure. This entity is a specific course-dependent process. This process can constitute the course of anoikis. hypofunction of keeping structure [anoikis (course)] HOIP_0000241 HOIP:HOIP_0000242 Decreasing area is a subtype of changing area: A process that changes the area of the object to be smaller. decreasing area HOIP_0000242 HOIP:HOIP_0000243 Decreasing volume is a subtype of changing volume: A process that changes the volume of the object to be relatively low decreasing volume HOIP_0000243 HOIP:HOIP_0000244 Decreasing length is a subtype of changing length: A process that changes the length of the object to be lower. decreasing length HOIP_0000244 HOIP:HOIP_0000245 Decreasing contact area with ECM is a subtype of decreasing area: A process that changes the contact area with extracellular matrix (ECM) to be smaller. decreasing contact area with ECM HOIP_0000245 HOIP:HOIP_0000246 Decreasing contact area with ECM is a subtype of decreasing area: A process that changes the contact area with extracellular matrix (ECM) to be smaller. This entity is a specific course-dependent process. This process can constitute the course of anoikis. decreasing contact area with ECM [anoikis (course)] HOIP_0000246 HOIP:HOIP_0000247 Accumulation of substances in a biological object is a subtype of storing: A process that keeps substances in an organism, tissue, organelle, or cell. related quality http://purl.obolibrary.org/obo/PATO_0002269 accumulation of substances in a biological object HOIP_0000247 HOIP:HOIP_0000248 Protein accumulation is a subtype of accumulation of substances in a biological object: A process that keeps protein(s) in a biological object. protein accumulation HOIP_0000248 HOIP:HOIP_0000249 Increasing sensitivity is a subtype of changing sensitivity: A process that changes the sensitivity to be lhigher. increasing sensitivity HOIP_0000249 HOIP:HOIP_0000250 Accumulation of abnormal proteins in ER is a subtype of accumulation of abnormal proteins: A process that keeps abnormal protein(s) in the ER (endoplasmic reticulum). And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of ER stress (severe) . accumulation of abnormal proteins in ER [ER stress (severe) ] HOIP_0000250 HOIP:HOIP_0000251 Accumulation of abnormal proteins is a subtype of protein accumulation: A process that keeps abnormal protein(s) in a biological object. accumulation of abnormal proteins HOIP_0000251 HOIP:HOIP_0000252 Mitochondrial dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete mitochondrial function. This entity is a specific course-dependent process. This process can constitute the course of necrosis. mitochondrial dysfunction [necrosis (course)] HOIP_0000252 HOIP:HOIP_0000253 Increasing size of liver is a subtype of increasing size: A process that changes the size of the liver to be larger. hepatomegaly increasing size of liver HOIP_0000253 HOIP:HOIP_0000254 Vitamine accumulation is a subtype of accumulation of substances in a biological object: A process that keeps vitamin in a biological object. vitamine accumulation HOIP_0000254 HOIP:HOIP_0000255 Accumulation of protein aggregates is a subtype of protein accumulation: A process that keeps protein aggregates in a biological object. Protein aggretates are often insoluble and tend to sequester Fe 2+ ions. Fe 2+ helps to produce ROS. accumulation of protein aggregates HOIP_0000255 HOIP:HOIP_0000256 Fatty acid strorage is a subtype of accumulation of substances in a biological object: A process that keeps fatty acid in a biological object. fatty acid strorage HOIP_0000256 HOIP:HOIP_0000257 Substance with stress sensor role is a subtype of substance with role. This entity is participating in a stress response and playing a stress sensor role. This entity is inferred from Description Logic. substance with stress sensor role HOIP_0000257 HOIP:HOIP_0000258 Melanin deposition is a subtype of accumulation of pigments: The aggregation of melanin in a particular location in an organism, tissue or cell. http://purl.obolibrary.org/obo/MPATH_44 melanin deposition HOIP_0000258 HOIP:HOIP_0000259 Lipofuscin deposition is a subtype of accumulation of pigments: The aggregation of lipofuscin in a particular location in an organism, tissue or cell. lipofuscin deposition HOIP_0000259 HOIP:HOIP_0000260 Substance with apoptosis inducer role is a subtype of substance with role. This entity is participating in a positive regulation of apoptosis process and playing an apoptosis inducer role. This entity is inferred from Description Logic. substance with apoptosis inducer role HOIP_0000260 HOIP:HOIP_0000261 Changing relationship between operands is a subtype of changing: A process that changing the relationship between multiple objects. changing relationship between operands HOIP_0000261 HOIP:HOIP_0000262 The totality of all processes through which ATP depltion is realized. ATP depletion [course] HOIP_0000262 HOIP:HOIP_0000263 Bile acid strorage is a subtype of accumulation of substances in a biological object: A process that keeps bile acid within the liver (intrahepatic), or outside the liver (extrahepatic) in the bile duct system. bile acid accumulation in hepatocyte HOIP_0000263 HOIP:HOIP_0000266 A role played by the entity that catalyses the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues. GO:0004842 ubiquitin ligase HOIP_0000266 HOIP:HOIP_0000267 Increasing amount of carbohydrate is a subtype of increasing quantity: A process that changes the amount of carbohydrates to be higher. increasing amount of carbohydrate HOIP_0000267 HOIP:HOIP_0000269 Bile acid transport to hepatocyte is a subtype of bile acid and bile salt transport: A process that transports bile acid within a hepatocyte by means of some agent such as a transporter or pore. PMID:9806540 bile acid transport to hepatocyte HOIP_0000269 HOIP:HOIP_0000270 YAMATO:ontology Location-independent. State corresponds not to generic quality but to property. It is possessed by continuants and processes. state HOIP_0000270 HOIP:HOIP_0000271 Primitive process is a unit of process. Process series at a certain granular level can appear as one primitive process at the higher level. Whether the process is a primitive process or not depends on the setting of the granularity. When one does not consider the details more than a certain level, or a level as the minimum grain size, the process at that level becomes the primitive process. primitive process HOIP_0000271 HOIP:HOIP_0000274 PERK signaling is a process that a signal is transmitted by the PERK. PERK generally plays a endoplasmic reticulum membrane stress sensor role. http://purl.obolibrary.org/obo/GO_0014065 PERK signaling HOIP_0000274 HOIP:HOIP_0000275 Value of quality. Although this is essentially a role played by quantity, YAMATO doesn't deal with it so for simplicity. YAMATO Ontology quality value HOIP_0000275 HOIP:HOIP_0000277 This is essentially a value and non-quantitative, therefore, there is no ordering among values, unlike non-categorial values. Categorical quality has typicality which no quantity has. It is generically dependent on entity because it is always referred to with something as a species. YAMATO Ontology categorical HOIP_0000277 HOIP:HOIP_0000278 It is just a quantity independent of what quantity it is of. That is, 10cm and 11cm exist just as it is in the quantity space and are just different. On the other hand, when a thing's length is 10cm long at time t1 and 11cm long at t2, we say the length of the thing CHANGED. The 10cm long of a thing has its identity which persists having possibly different values. Note that quantity is not specifically dependent on anything, but generically dependent on physical entity. YAMATO Ontology quantity HOIP_0000278 HOIP:HOIP_0000279 Dysfunction of fatty acid degradation is a subtype of hypofunctioning: A process that performs a decreased or insufficient lipid degradation. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. dysfunction of fatty acid degradation [alcoholic fatty liver] HOIP_0000279 HOIP:HOIP_0000280 Tumor cell survial is a subtype of cell survival: A process that keeps the viability of a tumor cell. tumor cell survial HOIP_0000280 HOIP:HOIP_0000281 Phospholipid accumulation in lysosome is a subtype of phospholipid accumulation: A process that keeps phospholipid in the lysosome. phospholipid accumulation in lysosome HOIP_0000281 HOIP:HOIP_0000282 lipoprotein lipase Ensembl:ENSG00000175445 HGNC:6677 MIM:609708 NCBI-Human-GeneID:4023 NCBI-Mouse-GeneID:16956 NCBI-Rat-GeneID:24539 LPL (mol) HOIP_0000282 NCBI-Human-GeneID:4023 http://www.ncbi.nlm.nih.gov/gene/4023 NCBI-Mouse-GeneID:16956 http://www.ncbi.nlm.nih.gov/gene/16956 NCBI-Rat-GeneID:24539 http://www.ncbi.nlm.nih.gov/gene/24539 HOIP:HOIP_0000283 Converting to acetyl CoA is a subtype of metabolic process that transforms into acetyl CoA. converting to acetyl CoA HOIP_0000283 HOIP:HOIP_0000284 Increasing fatty acid synthesis substrate is a subtype of increasing quantity: A process that changes the production amount of the substrate of the fatty acid synthesis. Increaseing fatty acid synthesis substrate HOIP_0000284 HOIP:HOIP_0000285 A series of molecular signals mediated by PERK (PKR-like ER kinase). PERK signal transduction pathway HOIP_0000285 HOIP:HOIP_0000286 A value which is greater than the normal or average. large (value) HOIP_0000286 HOIP:HOIP_0000287 A qualitative value which is lower than the threshold, normal or average. small (value) HOIP_0000287 HOIP:HOIP_0000288 Although these are qualitative values, they are essentially quantitative because they are derived from the quantitative values by introducing threshold value, and hence the values are ordinal. YAMATO Ontology qualitative quantity HOIP_0000288 HOIP:HOIP_0000289 YAMATO Ontology meta attribute value HOIP_0000289 HOIP:HOIP_0000290 YAMATO Ontology numbers quality value HOIP_0000290 HOIP:HOIP_0000291 many HOIP_0000291 HOIP:HOIP_0000292 few HOIP_0000292 HOIP:HOIP_0000293 Times quality value is a subtype of meta attribute value. YAMATO Ontology times quality value HOIP_0000293 HOIP:HOIP_0000294 many times HOIP_0000294 HOIP:HOIP_0000295 few times HOIP_0000295 HOIP:HOIP_0000296 Acute phase proteins coding gene expression via cytokine is a subtype of gene expression: A process that The process in which a gene sequence is converted into a mature acute phase proteins coding gene product or products (proteins or RNA) by cytokine. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition Acute phase proteins coding gene expression via cytokine is a subtype of gene expression: A process that The process in which a gene sequence is converted into a mature acute phase proteins coding gene product or products (proteins or RNA) by cytokine. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition IL-1, TNF, IL-6 or other cytokines released from macrophages and endtherial cells act on cell surface receptors to change transcriptions of genes involving tissue injury and repair. acute phase proteins coding gene expression via cytokine HOIP_0000296 Acute phase proteins coding gene expression via cytokine is a subtype of gene expression: A process that The process in which a gene sequence is converted into a mature acute phase proteins coding gene product or products (proteins or RNA) by cytokine. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition ISBN:0071769234 HOIP:HOIP_0000297 Oxidative stress dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the course of ER stress. under construction oxidative dependent chemical entity HOIP_0000297 HOIP:HOIP_0000298 NCBI-Human-GeneID:9695 NCBI-Mouse-GeneID:192193 NCBI-Rat-GeneID:297504 EDEM (mol) HOIP_0000298 NCBI-Human-GeneID:9695 http://www.ncbi.nlm.nih.gov/gene/9695 NCBI-Mouse-GeneID:192193 http://www.ncbi.nlm.nih.gov/gene/192193 NCBI-Rat-GeneID:297504 http://www.ncbi.nlm.nih.gov/gene/297504 HOIP:HOIP_0000300 This is an abstraction of the kinds at the class level. In the use case, it is sometimes referred to with # operator as a class constraint like "#generic quality". In a common term, it would be called "attribute". Its instance is not equal to its value. The value itself belongs to "quality value". Its instance is still an attribute which refers to a specific quantity. Its instnace plays a quality role like length plays one's height as a quality role. Quality such as one's height, one's weight, etc. are roles, and hence must be defined in the context of respective contexts(entities). Therefore, they are not defined as basic type like length, weight, etc. See "physical" in which a most generic quality is defined. Quality in DOLCE corresponds to quality role type in YAMATO. This is why "quality" is invisible in YAMATO in spite of it knows "quality". YAMATO Ontology generic quality attribute HOIP_0000300 HOIP:HOIP_0000301 NCBI-Human-GeneID:9451 NCBI-Mouse-GeneID:13666 NCBI-Rat-GeneID:29702 PERK - stress sensor (canonical)[ER stress] HOIP_0000301 NCBI-Human-GeneID:9451 http://www.ncbi.nlm.nih.gov/gene/9451 NCBI-Mouse-GeneID:13666 http://www.ncbi.nlm.nih.gov/gene/13666 NCBI-Rat-GeneID:29702 http://www.ncbi.nlm.nih.gov/gene/29702 HOIP:HOIP_0000302 An attribute that counting numbers of objects and how many times an event happens are essential not to individuals in them but to collectives of objects or events. counting generic quality HOIP_0000302 HOIP:HOIP_0000303 not clock time but times (how many times). Contrary to the intuition, "times" should not be taken as a generic quality. What should be taken as a generic quality is the pai rof "event" and times. That is, "what event happens many times" corresponds to "color is red". For example, "A month which has many accidents" corresponds to "A rose whose color is red". number of times HOIP_0000303 HOIP:HOIP_0000304 not numerals but "number" of somethings(=how many things) number of objects HOIP_0000304 HOIP:HOIP_0000305 YAMATO ontology non-meta generic quality HOIP_0000305 HOIP:HOIP_0000307 A physical attribute entity inhering in a bearer that has mass near a gravitational body. http://purl.obolibrary.org/obo/PATO_0000128 weight attribute HOIP_0000307 HOIP:HOIP_0000308 A role played by the entity which catalyses the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. EC:4.-.-.- related molecular function GO:0016829 lyase HOIP_0000308 HOIP:HOIP_0000309 meta generic quality HOIP_0000309 HOIP:HOIP_0000310 A 2-D extent attribute inhering in a bearer by virtue of the bearer's two dimensional extent. area (attribute) HOIP_0000310 HOIP:HOIP_0000311 Color as a kind is a generic quality. Red is a subclass of color and/or a value of color as discussed below, and being red is a property of things. The differentiation between red as a value of color and being red as a property is critical. In summary, there are three kinds of red. It is unary rather than binary just like ordinary classes such as animal, car, etc color (attribute) HOIP_0000311 HOIP:HOIP_0000312 Moving drug to the inside of liver is a subtype of moving A to the inside of B: A process that of the movement of drug into a liver. moving drug to the inside of liver HOIP_0000312 HOIP:HOIP_0000315 A composite chromatic quality composed of hue, saturation and intensity parts. colorness (quality) HOIP_0000315 HOIP:HOIP_0000316 A color brightness which is relatively high. high brightness HOIP_0000316 HOIP:HOIP_0000320 A role played by the entity which receives acute phase response signal and transmits operand(s). acute phase response role HOIP_0000320 HOIP:HOIP_0000321 FADs2 (mol) HOIP_0000321 HOIP:HOIP_0000322 Lamellar body formation in lysosome is a subtype of biological structure formation: A process that costructs lamellar body in lysosome. lamellar body formation in lysosome myelin figureformation in lysosome HOIP_0000322 HOIP:HOIP_0000323 The totality of all processes through which cell death is realized. PMID:18846107 PMID:21760595 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ cell death (course) HOIP_0000323 PMID:18846107 Classification of cell death recommendations of the Nomenclature Committee on Cell Death 2009 PMID:21760595 Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012 HOIP:HOIP_0000324 Apoptosis (course) is a subtype of cell death (course). The totality of all processes through which apoptosis is realized. apoptosis (course) HOIP_0000324 HOIP:HOIP_0000326 Pyroptosis (course) is a subtype of cell death (course). The totality of all processes through which pyroptosis is realized. Pyroptosis is related to a caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as Il-1beta and Il-18. PMID:18846107 PMID:21760595 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ under construction pyroptosis (course) HOIP_0000326 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ The term pyroptosis has been introduced in 2000 by Brennan and Cookson to functionally describe the peculiar death of macrophages infected by Salmonella typhimurium. Several other bacterial triggers of this atypical cell death modality have been identified, including Shigella flexneri, Listeria monocytogenes, Pseudomonas aeruginosa, Francisella tularensis and the Bacillus anthracis. However, it has become clear that pyroptosis neither constitutes a macrophage-specific process nor a cell death subroutine that only results from bacterial infection. Of note, pyroptotic cells can exhibit apoptotic and/or necrotic morphological features. HOIP:HOIP_0000327 Apoptosis modulator is a role played by any substance that regulates the process of apoptosis (programmed cell death) in multi-celled organisms. apoptosis regulator role HOIP_0000327 HOIP:HOIP_0000328 A role played by the entity which enables the facilitated diffusion of an ion (by an energy-independent process) by passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism. May be either selective (it enables passage of a specific ion only) or non-selective (it enables passage of two or more ions of same charge but different size). related molecular function GO:0005216 ion channel HOIP_0000328 HOIP:HOIP_0000329 A role played by the entity that ihibits the activity of tumor cells. inhibitor of tumor cell activity role HOIP_0000329 HOIP:HOIP_0000330 A role that controls the rate, timing and/or magnitude of transcription of genetic information. The function of transcriptional regulators is to modulate gene expression at the transcription step so that they are expressed in the right cell at the right time and in the right amount throughout the life of the cell and the organism. IMR:0000369 (obsolete) related molecular function GO:0140110 transcription regulator HOIP_0000330 HOIP:HOIP_0000331 A role played by the entity which enables the transfer of a drug from one side of a membrane to the other. A drug is any naturally occurring or synthetic substance, other than a nutrient, that, when administered or applied to an organism, affects the structure or functioning of the organism; in particular, any such substance used in the diagnosis, prevention, or treatment of disease. related molecular function GO:0015238 drug transmembrane transporter HOIP_0000331 HOIP:HOIP_0000332 The totality of genetic information belonging to a cell or an organism; in particular, the DNA that carries this information. http://purl.obolibrary.org/obo/OGG_0000000001 genome HOIP_0000332 HOIP:HOIP_0000333 Separating is a subtype of changing between operands: A process that divides the whole object into multiple components. separating into multiple components separating HOIP_0000333 HOIP:HOIP_0000334 Hyperfunction of Kupffer cell differentiation is a subtype of hyperfunction of cell differentiation: A process that performs an excesssive kupffer cell differentiation. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). hyperfunction of Kupffer cell differentiation [phospholipidosis (severe (excessive defense))] HOIP_0000334 HOIP:HOIP_0000335 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. ATF6 signaling HOIP_0000335 HOIP:HOIP_0000336 Amino acid conjugatied bile acid transport into bile canaliculus is a subtype of canalicular bile acid transport: A process that enables the transfer of amino acid conjugated bile acid from one side of a hepatocyte plasma membrane into a bile canaliculus. amino acid conjugatied bile acid transport into bile canaliculus HOIP_0000336 HOIP:HOIP_0000337 Changing fluidity is a subtype of changing quality: A process that changes the fluidity of the object. changing fluidity HOIP_0000337 HOIP:HOIP_0000338 The multiplication or reproduction of cells, resulting in the rapid expansion of a cell population. This entity is a specific course-dependent process. This process can constitute the course of cell death. cell proliferation [cell death (course)] HOIP_0000338 HOIP:HOIP_0000339 Tumor cell proliferation is a subtype of cell proliferation: A process of the multiplication or reproduction of tumor cells, resulting in the rapid expansion of a tumor cell population. tumor cell proliferation HOIP_0000339 HOIP:HOIP_0000340 Tumor cell proliferation is a subtype of cell proliferation: A process of the multiplication or reproduction of tumor cells, resulting in the rapid expansion of a tumor cell population. This entity is a specific course-dependent process. This process can constitute the course of cell death. tumor cell proliferation [cell death (course)] HOIP_0000340 HOIP:HOIP_0000341 Increasing number of dead cells in liver is a subtype of increasing number of objects: A process that becomes larger in the number of dead cells in the liver. increasing number of dead cells in liver HOIP_0000341 HOIP:HOIP_0000342 Increasing number of dead cells in liver is a subtype of cell proliferation: A process that becomes larger in the number of dead cells in the liver. This entity is a specific course-dependent process. This process can constitute the course of ER stress. increasing number of dead cells in liver [ER stress] HOIP_0000342 HOIP:HOIP_0000343 Decomposing is a subtype of separating: A process that divides a whole object into constituents. decomposing HOIP_0000343 HOIP:HOIP_0000344 Increasing number of action is a subtype of changing: A process that becomes larger in the number of actions or activities. increasing number of action HOIP_0000344 HOIP:HOIP_0000345 Increasing autodigestion of abnormal lysosome is a subtype of increasing autophagy: A process that becomes larger in the number of autodigestion of abnormal lysosome. increasing autodigestion of abnormal lysosome HOIP_0000345 HOIP:HOIP_0000346 Hypofunction of ATP biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient ATP biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of necrosis. hypofunction of ATP biosynthesis [necrosis (course)] HOIP_0000346 HOIP:HOIP_0000347 Increasing number of bile duct in liver is a subtype of increasing number of objects: A process that becomes larger in the number of bile duct in the liver. increasing number of bile duct in liver HOIP_0000347 HOIP:HOIP_0000348 Decreasing number of objects is a subtype of changing: A process that becomes smaller in number of physical objects. decreasing number of objects HOIP_0000348 HOIP:HOIP_0000349 Cleavage of ATF6-alpha by S2P is a subtype of proteolysis: A process n which ATF6-alpha is cleaved by endopeptidase S2P( MBTPS2). Site-2 cleavage comes after site-1 cleavage. This entity is a specific course-dependent process. This process can constitute the course of ER stress. cleavage of ATF6-alpha by S2P [ER stress] HOIP_0000349 HOIP:HOIP_0000351 Decreasing number of cells is a subtype of decreasing number of objects: A process that becomes smaller in number of cells. decreasing number of cells HOIP_0000351 HOIP:HOIP_0000352 Increasing concentration is a subtype of changing concentration: A process that changes the concentration of the object to be higher. increasing concentration HOIP_0000352 HOIP:HOIP_0000353 Increasing calcium ion concentration is a subtype of increasing concentration: A process that changes the calcium ion concentration in the blood to be higher. increasing calcium ion concentration HOIP_0000353 HOIP:HOIP_0000354 Increase in intracellular calcium level is a subtype of increase in calcium level: A process that changes the calcium ion concentration within a cell to be higher. increase in intracellular calcium level HOIP_0000354 HOIP:HOIP_0000355 Increase in intracellular calcium level is a subtype of increase in calcium level: A process that changes the calcium ion concentration within a cell to be higher. This entity is a specific course-dependent process. This process can constitute the course of necrosis. increase in intracellular calcium level [necrosis (course)] HOIP_0000355 HOIP:HOIP_0000356 Amino acid conjugatied bile acid transport into bile canaliculus is a subtype of canalicular bile acid transport: A process that enables the transfer of amino acid conjugated bile acid from one side of a hepatocyte plasma membrane into a bile canaliculus. This entity is a specific course-dependent process. This process can constitute the course of Cholestasis. amino acid conjugatied bile acid transport into bile canaliculus [Cholestasis] HOIP_0000356 HOIP:HOIP_0000357 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. PERK activation HOIP_0000357 HOIP:HOIP_0000358 AMPK activation is a subtype of molecular activation: A process that changes the activity of the AMPK (AMP-activated protein kinase) to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:26481188 AMPK activation [ER stress] HOIP_0000358 PMID:26481188 Blocking autophagy by 3-methyladenine (3-MA) or Atg5 siRNA knock-down enhanced meloxicam lethality for HCC by activation of ER stress-related apoptosis. In addition, GRP78 seemed to lead to autophagic activation via the AMPK-mTOR signalling pathway. Blocking AMPK with a chemical inhibitor inhibited autophagy suggesting that meloxicam-regulated autophagy requires activation of AMPK. CONCLUSIONS: Our results revealed that both ER stress and autophagy were involved in cell death evoked by meloxicam in HCC cells. This inhibition of autophagy to enhance meloxicam lethality, suggests a novel therapeutic strategy against HCC. HOIP:HOIP_0000359 Decreasing blood flow is a subtype of decreasing flow: A process that changes the blood flow to be smaller. decreasing blood flow HOIP_0000359 HOIP:HOIP_0000360 Oxidative stress dependent chemical compound is a subtype of course dependent chemical entity. This entity (drug) can participate in the course of oxidative stress. Oxidative dependent chemical compound HOIP_0000360 HOIP:HOIP_0000361 Increasing demand for response to stress is a subtype of increasing functional demand: A process that changes the functional demand for the response to the stress to be higher. increasing demand for response to stress HOIP_0000361 HOIP:HOIP_0000362 Increasing demand for response to ER stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the endoplasmic reticulum (ER) stress to be higher. increasing demand for response to ER stress HOIP_0000362 HOIP:HOIP_0000363 Increasing demand for response to ER stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the edoplasmic reticulum (ER) stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress (severe) . increasing demand for response to ER stress [ER stress (severe) ] HOIP_0000363 HOIP:HOIP_0000364 Increaseing production quantity of ROS is a subtype of increasing quantity: A process that changes the production amount of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen, to be higher. increasing production quantity of ROS HOIP_0000364 HOIP:HOIP_0000365 Increasing production quantity of RNS is a subtype of increasing quantity: A process that changes the production amount of reactive nitrogen species (RNS) to be higher increasing production quantity of RNS HOIP_0000365 HOIP:HOIP_0000366 Increasing calcium ion is a subtype of increasing quantity: A process that changes the calcium ion becomes larger. increasing calcium ion inflow into cell HOIP_0000366 HOIP:HOIP_0000367 Increasing sodium ion inflow into cell is a subtype of increasing quantity: A process that changes the sodium ion inflow into the cell to be larger. increasing sodium ion inflow into cell HOIP_0000367 HOIP:HOIP_0000368 increasing extracellular potassium outflow is a subtype of increasing quantity: A process that changes the phospholipid inflow into the hepatocyte to be larger. increasing extracellular potassium outflow HOIP_0000368 HOIP:HOIP_0000369 Negative regulation process is a subtype of controlling: A process that that stops, prevents, or reduces the frequency, rate or extent of function. Controlling to the negative (-) direction. negative regulation process HOIP_0000369 HOIP:HOIP_0000371 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of ER stress (mild). negative regulation of apoptotic process [ER stress (mild)] HOIP_0000371 HOIP:HOIP_0000372 EVOL6 HOIP_0000372 HOIP:HOIP_0000374 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. regulation of cell cycle [apoptosis (course)] HOIP_0000374 HOIP:HOIP_0000375 The process in which a gene's sequence is converted into a mature gene product or products (proteins or RNA) by transcription factor Gene expression by transcriptional regulator HOIP_0000375 HOIP:HOIP_0000376 Cell survial is a subtype of keeong quantity: A process that keeps the viability of a cell. This entity is a specific course-dependent process. This process can constitute the course of ER stress. cell survival [ER stress] cell survival [ER stress] HOIP_0000376 HOIP:HOIP_0000377 Cell survial is a subtype of keeong quantity: A process that keeps the viability of a cell. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. normal cell survival [apoptosis (course)] HOIP_0000377 HOIP:HOIP_0000378 Functioning process is a subtype of function-related process: A process that executes and manifests function. functioning process HOIP_0000378 HOIP:HOIP_0000379 Receiving is a subtype of functioning process: A process that that gets an object as input. receiving HOIP_0000379 HOIP:HOIP_0000380 Making existence is a subtype of functioning process: A process that makes a target object to be present in another object. making existence HOIP_0000380 HOIP:HOIP_0000381 Generating is a subtype of funcioning: A process that produces output from nothing. 対象物が存在しない状態から生成する generating HOIP_0000381 HOIP:HOIP_0000382 Protein production is a subtype of generating: A process that synthesizes protein (s) resulting in having output (s). protein production HOIP_0000382 HOIP:HOIP_0000384 Chaperon production is a subtype of protein production: A process that makes existent of a protein with a chaperon role due to biosynthesis or secretion resulting in an increase in its levels. chaperon production HOIP_0000384 HOIP:HOIP_0000385 Abnormal protein-degrading enzyme production is a subtype of protein production: A process that makes existent of an abnormal protein-degrading enzyme protein due to biosynthesis or secretion resulting in an increase in its levels. abnormal protein-degrading enzyme production HOIP_0000385 HOIP:HOIP_0000386 Any process that activates or increases the frequency, rate or extent of ERAD pathway. This entity is a specific course-dependent process. This process can constitute the course of ER stress. positive regulation of ERAD [ER stress] HOIP_0000386 HOIP:HOIP_0000387 Changing is a subtype of making existence: A process that makes a target object different. changing HOIP_0000387 HOIP:HOIP_0000388 PERK autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by PERK of one or more of its own amino acid residues (cis-autophosphorylation), or residues on PERK (trans-autophosphorylation). This process is dependent on the translation attenuation and can constitute the course of ER stress. PERK autophosphorylation [ER stress - translation attenuation] HOIP_0000388 HOIP:HOIP_0000389 Converting signal to information is a subtype of converting to information: A process that changes a signal to information. converting signal to information HOIP_0000389 HOIP:HOIP_0000391 Converting signal to information is a subtype of converting to information: A process that changes a signal to information. This entity is a specific course-dependent process. This process can constitute the course of cell death. converting signal to information [cell death (course)] HOIP_0000391 HOIP:HOIP_0000392 Changing an operand is a subtype of changing: A process that makes one object different. changing an operand HOIP_0000392 HOIP:HOIP_0000393 Membrane phospholipid catabolic process is a subtype of lipid catabolic process: The chemical reactions resulting in the breakdown of membrane phopholipids membrane phospholipid catabolic process HOIP_0000393 HOIP:HOIP_0000394 Changing quantity is a subtype of changing attribute: A process that changes the amount of the object as an output. changing quantity HOIP_0000394 HOIP:HOIP_0000395 Increasing quantity is a subtype of changing quantity: A process that changes the magnitude of the object to be larger. increasing quantity HOIP_0000395 HOIP:HOIP_0000396 Decreasing quantity is a subtype of changing quantity: A process that changes the magnitude of the object to be smaller. decreasing quantity HOIP_0000396 HOIP:HOIP_0000397 Decreasing production quantity of protein is a subtype of decreasing quantity: A process that changes the production quantity of the protein to be lower. This entity is a specific course-dependent process. This process can constitute the course of ER stress. decreasing production quantity of protein [ER stress] HOIP_0000397 HOIP:HOIP_0000398 Hyperfunction of hypoxia resonsive gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive hypoxia resonsive gene expression. hyperfunction of hypoxia resonsive gene expression HOIP_0000398 HOIP:HOIP_0000399 The process in which a gene's sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. This entity is a specific course-dependent process. This process can constitute the course of cell death. gene expression [cell death (course)] HOIP_0000399 HOIP:HOIP_0000401 Activating is a subtype of changing activity: A process that changes the activity of the object to be higher. inceasing activity activating HOIP_0000401 HOIP:HOIP_0000402 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PERK activation [ER stress] HOIP_0000402 HOIP:HOIP_0000403 NRF2 activation by PERK is a subtype of NRF2 activation: A process that changes the activity of NRF2 (Nuclear Factor, Erythroid 2 Like 2) to be higher by PERK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Mild ER stress activates Nrf2 and the antiapoptotic factor BI-1. Activation of Nrf2 through its phosphorylation by PERK,and BI-1 protect the endoplasmic reticulum from further damage by inhibiting the production of ROS by CYP2E1(Lee et al., 2007; Kim et al., 2009). Mild ER stress activates Nrf2 and the antiapoptotic factor BI-1. Activation of Nrf2 through its phosphorylation by PERK,and BI-1 protect the endoplasmic reticulum from further damage by inhibiting the production of ROS by CYP2E1(Lee et al., 2007; Kim et al., 2009). NRF2 activation by PERK [ER stress (mild)] HOIP_0000403 Mild ER stress activates Nrf2 and the antiapoptotic factor BI-1. Activation of Nrf2 through its phosphorylation by PERK,and BI-1 protect the endoplasmic reticulum from further damage by inhibiting the production of ROS by CYP2E1(Lee et al., 2007; Kim et al., 2009). casarett and dolls HOIP:HOIP_0000404 Cyp7a1 (mol) HOIP_0000404 HOIP:HOIP_0000405 AMPK activation is a subtype of molecular activation: A process that changes the activity of the AMPK (AMP-activated protein kinase) to be higher. AMPK activation HOIP_0000405 HOIP:HOIP_0000406 Positive regulation of autophagy by AMPK is a subtype of positive regulation of autophagy: A process that that activates or increases the frequency, rate or extent of autophagy by AMPK. PMID:18439900 positive regulation of autophagy by AMPK HOIP_0000406 HOIP:HOIP_0000407 GRP78 activation by MLX is a subtype of molecular activation: A process that changes the activity of the GRP78/ HSPA5 (Heat Shock Protein Family A (Hsp70) Member 5) to be higher by MLX. GRP78 activation by MLX HOIP_0000407 HOIP:HOIP_0000408 PLA2 activation is a subtype of molecular activation: A process that changes the activity of the member of the phospholipase A2 family (PLA2) to be higher. PLA2 activation HOIP_0000408 HOIP:HOIP_0000409 Protease activation is a subtype of molecular activation: A process that changes the activity of the molecule with a protease role to be higher. protease activation HOIP_0000409 HOIP:HOIP_0000410 Changing shape is a subtype of changing structure: A process that changes the form of the operand. changing shape HOIP_0000410 HOIP:HOIP_0000411 Liver X receptor activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating LXR ( liver X receptor) with a nuclear receptor role to be higher. LxR alpha activation activating LXR alpha liver X receptor activation HOIP_0000411 HOIP:HOIP_0000412 Changing membrane fluidity is a subtype of changing fluidity: A process that changes the fluidity of the membrane. changing membrane fluidity HOIP_0000412 HOIP:HOIP_0000413 Any process that activates or increases the frequency, rate or extent of protein refolding. This entity is a specific course-dependent process. This process can constitute the course of ER stress. positive regulation of protein refolding [ER stress] HOIP_0000413 HOIP:HOIP_0000414 Keeping quantity is a subtype of changing amount: A process that maintains the magnitude of the object at a constant level . keeping quantity HOIP_0000414 HOIP:HOIP_0000415 Changing quality is a subtype of changing an operand: A process that changes the quality of the object. changing quality HOIP_0000415 HOIP:HOIP_0000416 Negative regulation of formation of cytoplasmic translation initiation complex by eIF2a is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of formation of cytoplasmic translation initiation complex by eIF2a. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:23334697 PMID:9930704 negative regulation of formation of cytoplasmic translation initiation complex by eIF2a [ER stress] HOIP_0000416 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. HOIP:HOIP_0000417 Changing volume is a subtype of changing quality: A process that changes the volume of the object. changing volume HOIP_0000417 HOIP:HOIP_0000418 Homeostatic imbalance of number of smooth endoplasmic reticulum is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of the proliferation and elimination of smooth endoplasmic reticulum. homeostatic imbalance of number of smooth endoplasmic reticulum HOIP_0000418 HOIP:HOIP_0000420 For ontology reasoning. process based on specific viewpoint HOIP_0000420 HOIP:HOIP_0000421 Keeps volume is a subtype of changing volume: A process that keeps the volume of the object. keeps volume HOIP_0000421 HOIP:HOIP_0000422 Changing density is a subtype of changing quality: A process that changes the density of the object. changing density HOIP_0000422 HOIP:HOIP_0000423 biological defense role HOIP_0000423 HOIP:HOIP_0000424 Changing hardness is a subtype of changing quality: A process that changes the hardness of the object. changing hardness HOIP_0000424 HOIP:HOIP_0000425 Changing phase is a subtype of changing an operand: A process that changes the phase of the operand. changing phase HOIP_0000425 HOIP:HOIP_0000426 Solidifying is a subtype of changing phase: A process that changes the phase of the operand to a solid phase. solidifying HOIP_0000426 HOIP:HOIP_0000427 Vaporizing is a subtype of changing phase: A process that changes the phase of the operand to a vapor phase. vaporizing HOIP_0000427 HOIP:HOIP_0000428 Liquefying is a subtype of changing phase: A process that changes the phase of the operand to a liquid phase. liquefying HOIP_0000428 HOIP:HOIP_0000429 Moving is a subtype of changing an operand: A process that change the location of the operand. act on one position moving HOIP_0000429 HOIP:HOIP_0000430 Elevating is a subtype of moving: A process that changes the location of the operand from a lower to a higher place or position. elevating HOIP_0000430 HOIP:HOIP_0000431 Lowering is a subtype of moving: A process that changes the location of the operand from a higher to a lower place or position. lowering HOIP_0000431 HOIP:HOIP_0000432 Moving fluid is a subtype of moving: A process that changes the location of the liquid. moving fluid HOIP_0000432 HOIP:HOIP_0000433 Keeping position is a subtype of moving: A process that maintains in the fixed position. keeping position HOIP_0000433 HOIP:HOIP_0000434 Malfunctioning process is a subtype of function-related process: A process that cannot perform a function appropriately or cannot realize it at all. malfunctioning process HOIP_0000434 HOIP:HOIP_0000435 Hyperfunctioning is a subtype of malfunctioning process: A process that performs an excessive function. hyperfunctioning HOIP_0000435 HOIP:HOIP_0000436 Hypofunctioning is a subtype of malfunctioning process: A process that performs a decreased or insufficient functioning. decreasing function hypofunctioning HOIP_0000436 HOIP:HOIP_0000437 Arresting function is a subtype of malfunctioning process: A process that arrests the progress of function execution. arresting function HOIP_0000437 HOIP:HOIP_0000438 Dysfunctioning is a subtype of malfunctioning process: A process that performs an abnormal and incomplete functioning. dysfunctioning HOIP_0000438 HOIP:HOIP_0000439 Loss of function (process) is a subtype of malfunctioning process: A process that results in no longer having a function or the process that gradually loses it. loss of function (process) HOIP_0000439 HOIP:HOIP_0000441 Sifting is a subtype of changing between operands: A process to move an operand from one medium to another medium. Changing medium from medium A to medium B. sifting HOIP_0000441 HOIP:HOIP_0000442 Transmitting is a subtype of sifting: A process to send out an operand from a medium A to a medium B. transmitting HOIP_0000442 HOIP:HOIP_0000444 Caspase signaling is a process that a signal is transmitted by the caspase. caspase signaling HOIP_0000444 HOIP:HOIP_0000445 Caspase signaling is a process that a signal is transmitted by the caspase. This entity is a specific course-dependent process. This process can constitute the course of ER stress. caspase signaling [ER stress] HOIP_0000445 HOIP:HOIP_0000446 Caspase signaling is a process that a signal is transmitted by the caspase. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. caspase signaling [apoptosis (course)] HOIP_0000446 HOIP:HOIP_0000447 Death Domain signaling is a subtype of biological signaling: A process in which a signal is transmitted from the cell membrane receptor starting with a ligand. The death domain at the cytoplsmic tail of the receptor binds the other death domain of the docking protein to form a death-inducing signaling complex (DISC). This signal triggers the assembly of intracellular proteins to form a death including signaling complex (DISC), which includes a specific intiator procaspase (procaspase-8, 10). These initiator procasapases cleave and converts effector procaspases (i.e., caspase-3, 6, 7) to activate. Then, these effector caspases cleave target proteins, which leads to execute apoptosis. ISBN:0123878179 extrinsic (Death Domain) signaling HOIP_0000447 ISBN:0123878179 In hepatocytes, extrinsic pathway apoptosis induction requires caspase-9 mediated cleavage of Bid, a BCL-2 family protein and subsequent mitochondrial outer menbrane permeablization for executioner apoptosis activation. DRUG INDUCED LIVER DISEASE CHAPTER 5, 3rd Ed. Editors: Neil Kaplowitz Laurie DeLev HOIP:HOIP_0000448 Death Domain signaling is a subtype of biological signaling: A process in which a signal is transmitted from the cell membrane receptor starting with a ligand. The death domain at the cytoplsmic tail of the receptor binds the other death domain of the docking protein to form a death-inducing signaling complex (DISC). This entity is a specific course-dependent process. This process can constitute the course of apoptosis. extrinsic (Death domain) signaling [apoptosis (course)] HOIP_0000448 HOIP:HOIP_0000449 NRF2 signaling is a subtype of signaling that a signal is transmitted by the NRF2. NRF2 signaling HOIP_0000449 HOIP:HOIP_0000450 NRF2 signaling is a subtype of signaling that a signal is transmitted by the NRF2. This entity is a specific course-dependent process. This process can constitute the course of ER stress. NRF2 signaling [ER stress] HOIP_0000450 HOIP:HOIP_0000451 PMID:26481188 GRP78 - autophagy inducing factor (canonical)[ER stress - autophagy indution] HOIP_0000451 HOIP:HOIP_0000452 P53 signaling isis a process that a signal is transmitted by the p53. This entity is a specific course-dependent process. This process can constitute the course of ER stress. p53 signaling [ER stress] HOIP_0000452 HOIP:HOIP_0000453 P53 signaling is a process that a signal is transmitted by p53. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. p53 signaling [apoptosis (course)] HOIP_0000453 HOIP:HOIP_0000454 PERK signaling is a process that a signal is transmitted by the PERK. PERK generally plays a endoplasmic reticulum membrane stress sensor role. This entity is a specific course-dependent process. This process can constitute the course of PERK pathway. PERK signaling [PERK pathway] HOIP_0000454 HOIP:HOIP_0000455 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to oxidative stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. increasing demand for response to oxidative stress [oxidative stress (course)] HOIP_0000455 HOIP:HOIP_0000456 The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon. This entity is a specific course-dependent process. This process can constitute the course of ER stress. retrograde protein transport from ER to cytosol [ER stress] HOIP_0000456 HOIP:HOIP_0000457 The process that results in the movement of arachidonic acid from the cell membrane. The process that results in the movement of arachidonic acid from the cell membrane. release of arachidonic acid from cell membrane HOIP_0000457 The process that results in the movement of arachidonic acid from the cell membrane. PMID:21910409 HOIP:HOIP_0000458 Removing (from A) is a subtype of taking: A process that takes an unnecessary operand from a medium. removing (from A) HOIP_0000458 HOIP:HOIP_0000459 Giving is a subtype of sifting: A process that provides an object to a medium. giving HOIP_0000459 HOIP:HOIP_0000460 ER to Golgi transport is a subtype of transport: A process of the directed movement of substances from the endoplasmic reticulum (ER) to the Golgi. ER to Golgi transport HOIP_0000460 HOIP:HOIP_0000461 Oxidation-antioxidtion inbalance is a subtype of imbalance: A process that lacks a balance between oxidation and anti-oxidation that inhibits oxidation. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. oxidation-antioxidtion inbalance [oxidative stress (course)] HOIP_0000461 HOIP:HOIP_0000462 Detaching is a subtype of separating: A process that disaggregates the whole object into constituent components. タイプが異種のものを異なる部分に分離する 個々に認識できる異なる部分構成要素が結合された全体物を複数の部分構成要素に分ける detaching HOIP_0000462 HOIP:HOIP_0000463 Dissociation of PERK:BIP heterodimer is a subtype of detaching: A process that disaggregates PERK-BIP heterodimers into BIP and PERK. This process is dependent on the translation attenuation and can constitute the course of ER stress. PMID:10854322 PMID:11907036 PERK (EIF2AK3) is a single-pass transmembrane protein located in the Endoplasmic Reticulum (ER) membrane. PERK has an N-terminal luminal domain and a C-terminal cytosolic domain. It is maintained in an inactive state by association of its luminal domain with BiP, a chaperone in the ER. Because BiP also binds unfolded proteins, BiP dissociates from PERK when unfolded proteins exceed chaperone activity in the ER. Dissociation of PERK:BIP Heterodimer [ER stress translation attenuation] HOIP_0000463 HOIP:HOIP_0000464 Changing position is a subtype of changing between operands: A process that that changes the relative position between objects. changing position HOIP_0000464 HOIP:HOIP_0000465 Changing distance is a subtype of changing position: A process that changes the relative position between objects. changing distance HOIP_0000465 HOIP:HOIP_0000466 Increasing distance is a subtype of changing distance: A process that keeps object A away from object B. increasing distance HOIP_0000466 HOIP:HOIP_0000467 Increasing free radical is a subtype of increasing quantity: A process that changes the amount of free radicals to be larger. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. increasing free radical [oxidative stress (course)] HOIP_0000467 HOIP:HOIP_0000468 Assembling is a subtype of changing composition: A process that combines multiple components as one configuration. assembling HOIP_0000468 HOIP:HOIP_0000469 Joining is a subtype of combining: A process that makes bonds between the components. 構成要素間に結合力関係を生じさせる． 出力混合物は結合関係となる joining HOIP_0000469 HOIP:HOIP_0000470 Lysosome homeostasis is a subtype of homeostatic process: A process that that preserves a lysosome in a stable functional or structural state. All of the lysosomal enzymes are acid hydrolases, which are active at the acidic pH (about 5) that is maintained within lysosomes but not at the neutral pH (about 7.2) characteristic of the rest of the cytoplasm (Figure 9.35). The requirement of these lysosomal hydrolases for acidic pH provides double protection against uncontrolled digestion of the contents of the cytosol; even if the lysosomal membrane were to break down, the released acid hydrolases would be inactive at the neutral pH of the cytosol. All of the lysosomal enzymes are acid hydrolases, which are active at the acidic pH (about 5) that is maintained within lysosomes but not at the neutral pH (about 7.2) characteristic of the rest of the cytoplasm (Figure 9.35). The requirement of these lysosomal hydrolases for acidic pH provides double protection against uncontrolled digestion of the contents of the cytosol; even if the lysosomal membrane were to break down, the released acid hydrolases would be inactive at the neutral pH of the cytosol. lysosome homeostasis HOIP_0000470 All of the lysosomal enzymes are acid hydrolases, which are active at the acidic pH (about 5) that is maintained within lysosomes but not at the neutral pH (about 7.2) characteristic of the rest of the cytoplasm (Figure 9.35). The requirement of these lysosomal hydrolases for acidic pH provides double protection against uncontrolled digestion of the contents of the cytosol; even if the lysosomal membrane were to break down, the released acid hydrolases would be inactive at the neutral pH of the cytosol. ISBN:0815340729 HOIP:HOIP_0000471 Signaling is a subtype of transmitting: A process that transmits signals from medium A to medium B. signaling HOIP_0000471 HOIP:HOIP_0000473 Hyperfunction of increasing number is a subtype of hyperfunction of increasing: A process that performs an excessive nu,ber of the object. hyperfunction of increasing number HOIP_0000473 HOIP:HOIP_0000474 Keeping quality is a subtype of changing quality: A process that keeps the quality of the object constant. keeping quality HOIP_0000474 HOIP:HOIP_0000475 Changing pressure is a subtype of changing quality: A process that changes the pressure of the object . changing pressure HOIP_0000475 HOIP:HOIP_0000476 Changing temperature is a subtype of changing quality: A process that changes the temperature of the object. changing temperature HOIP_0000476 HOIP:HOIP_0000477 Insulin signaling is a subtype of signaling, in which a signal mediated by the insulin receptor. insulin receptor signaling HOIP_0000477 HOIP:HOIP_0000478 Hyperfunction of lipid transport to peroxisome is a subtype of hyperfunction of transport: A process that performs an excesssive lipid transport to peroxisome. hyperfunction of long-chain fatty acid import into peroxisome HOIP_0000478 HOIP:HOIP_0000480 Hyperfunction of lipid transport to mitochondria is a subtype of hyperfunction of transport: A process that performs an excesssive lipid transport to mitochondria. hyperfunction of lipid transport to mitochondria HOIP_0000480 HOIP:HOIP_0000481 A mebrane potential which is relatively low. decreased membrane potential HOIP_0000481 HOIP:HOIP_0000482 Insufficient functioning is a subtype of malfunctioning process: A process that lacks performing the function required. insufficient functioning HOIP_0000482 HOIP:HOIP_0000483 Glutathione depletion is a subtype of depleting: A process that lessens markedly in the amount of glutathione. glutathione depletion HOIP_0000483 HOIP:HOIP_0000484 Increasing autophagy is a subtype of increasing number of actions: A process that becomes larger in the number of autophagy. increasing autophagy HOIP_0000484 HOIP:HOIP_0000485 ATP depletion is a subtype of depleting: A process that lessens markedly in the amount of adenosine triphosphate (ATP) . ATP depletion HOIP_0000485 HOIP:HOIP_0000486 ATP depletion is a subtype of depleting: A process that lessens markedly in the amount of adenosine triphosphate (ATP) . This entity is a specific course-dependent process. This process can constitute the course of necrosis. ATP depletion [necrosis (course)] HOIP_0000486 HOIP:HOIP_0000487 Autophagy inducer is a role played by any compound that promotes the process of autophagy (the self-digestion of one or more components of a cell through the action of enzymes originating within the same cell). autophagy inducer HOIP_0000487 HOIP:HOIP_0000488 Accumulation of fluids is a subtype of accumulation of substances in a biological object: A process that keeps fluid in an organism, tissue, organelle, or cell. accumulation of fluids HOIP_0000488 HOIP:HOIP_0000489 A laboratory test or analysis of the biological properties or activities of a substance performed by testing its effect on an organism. http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C18641 in vivo assay HOIP_0000489 HOIP:HOIP_0000490 Ligand molecule is a subtype of signaling dependent molecule. This entity is dependent on a signal transduction system and can participate in signaling process. リガンドロールを担った分子。ロールホルダー。 ligand molecule [signal transduction system] HOIP_0000490 HOIP:HOIP_0000491 A tube that is part of a excretory system. excretory tube HOIP_0000491 HOIP:HOIP_0000492 Glycogen accumulation is a subtype of accumulation of substances in a biological object: A process that keeps glycogen in a biological object. glycogen accumulation HOIP_0000492 HOIP:HOIP_0000493 In the imbalance model, the basic units are as follows: In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that inculdes step 1 to 4. The defense performance level is lower (L) than the medium (M) in the normal condition . Threfore even if the functional demand level is Medium level (M) in the daily life, which leads to the imbalance and leads to abnormal manifestation. imbalance L<M HOIP_0000493 HOIP:HOIP_0000494 Hypofunction of ion transport is a subtype of hypofunction of transport: A process that performs a decreased or insufficient ion transport. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID: 9061852 hypofunction of ion transport [phospholipidosis (severe)] HOIP_0000494 PMID: 9061852 ICAD may influence a wide variety of cell functions, including: phosphorylation pathways, ion transport, and other metabolic pathways. In rat lung, amiodarone inhibits Mg2+-ATPase and Na+,K+-ATPase in areas where phospholipid is located . In this location and probably in others, CADs may affect ion transport and oxidative phosphorylation. These effects may be due to the increasing intracytoplasmic Ca2+. HOIP:HOIP_0000495 Hypofunction of ion transport is a subtype of hypofunction of transport: A process that performs a decreased or insufficient ion transport. hypofunction of ion transport HOIP_0000495 HOIP:HOIP_0000497 Hypofunction of phospholipid deradation by phospholipase A2 is a subtype of hypofunction of phospholipid degradation: A process that performs a decreased or insufficient phospholipid deradation by phospholipase A2. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe).. hypofunction of phospholipid degradation by phospholipase A2 [Phospholipidosis　(severe)] HOIP_0000497 HOIP:HOIP_0000501 The totality of all processes through which glutathione depletion is realized. PMID:16500922 PMID:22995213 PMID:23856494 PMID:24287781 glutathione depletion (course) HOIP_0000501 PMID:16500922 Mechanisms of liver injury. III. Role of glutathione redox status in liver injury. PMID:22995213 Modulation of oxidative stress as an anticancer strategy. PMID:23856494 Glutathione defense mechanism in liver injury: insights from animal models. HOIP:HOIP_0000502 CASPASE (canonical)[ER stress] HOIP_0000502 HOIP:HOIP_0000503 Hyperfunction of alcohol metabolism is a subtype of hyperfunctioning: A process that performs an excessive alcohol metabolism. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis by alcoholic liver injury. hyperfunction of alcohol metabolism [hepatic fibrosis by alcoholic liver injury] HOIP_0000503 HOIP:HOIP_0000504 Malfunctioning of regulation of gene expression is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of gene expression appropriately or cannot realize it at all. malfunctioning of regulation of gene expression HOIP_0000504 HOIP:HOIP_0000505 Dissociation of Bip complex is a subtype of detaching: A process that disaggregates a Bip complex into Bip and other molecule(s). This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:10854322 PMID:23334697 dissociation of BIP complex [ER stress] HOIP_0000505 PMID:10854322 Perturbation of protein folding promotes reversible dissociation of BiP from the lumenal domains of PERK and IRE1. PMID:23334697 The ER luminal domains of the UPR sensors (PERK, IRE1, and ATF6) and unfolded proteins compete for binding sites on GRP78. When the UPR sensors are bound to GRP78, they are kept in an inactive state. Accumulation of unfolded proteins overwhelms the protein folding chaperones and sequesters them away from the UPR sensors unmasking oligomerization sequences in IRE1 and PERK or Golgi localization sequences in ATF6. HOIP:HOIP_0000506 A role played by the entity which transfers directed movement of bile acid and bile salts out of a hepatocyte and into the bile canaliculus. Bile canaliculi are the thin tubes formed by hepatocyte membranes. Bile acids are any of a group of steroid carboxylic acids occurring in bile, where they are present as the sodium salts of their amides with glycine or taurine. related molecular function GO:0015126 canalicular bile acid transmembrane transporter HOIP_0000506 HOIP:HOIP_0000507 Activation of thioredoxin pathway is a subtype of activating: A process that changes the activity of the thioredoxin pathway to be higher. activation of thioredoxin pathway HOIP_0000507 HOIP:HOIP_0000508 Decreasing amount of abnormal protein is a subtype of decreasing quantity: A process that changes the quantity of the abnormal protein to be lower. decreasing amount of abnormal protein HOIP_0000508 HOIP:HOIP_0000509 Any member of a group of steroid carboxylic acids occuring in bile, where they are present as the sodium salts of their amides with glycine or taurine. Bile salt Gallensaeure bile acids ISBN:0123878179 http://purl.obolibrary.org/obo/CHEBI_3098 bile acid HOIP_0000509 ISBN:0123878179 In the small intestine, bile salts are essential for lipid digestion and the absorption of fat and fat soluble vitamin ISBN:0123878179 bile salts have detergent properties and can easily become cytotoxic. HOIP:HOIP_0000512 Apoptosis triggered by inadequate or inappropriate adherence to substrate e.g. after disruption of the interactions between normal epithelial cells and the extracellular matrix. This entity is a specific course-dependent process. This process can constitute the course of anoikis. anoikis [anoikis (course)] HOIP_0000512 HOIP:HOIP_0000513 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This entity is a specific course-dependent process. This process can constitute the course of ER stress. ISBN:0123878179 apoptotic process [ER stress] HOIP_0000513 ISBN:0123878179 After an initiall adaptation phase (UPR), continued ER sress may lead to an irresible phase involving commitenent to apoptosis. Perk leads to upregulation of the transcription factor CHOP and mitochondria-mediated cell death. HOIP:HOIP_0000514 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. apoptotic process [apoptosis (course)] HOIP_0000514 HOIP:HOIP_0000515 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. apoptotic process [oxidative stress (course)] HOIP_0000515 HOIP:HOIP_0000516 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. This entity is a specific course-dependent process. This process can constitute the course of ER stress. protein catabolic process [ER stress] HOIP_0000516 HOIP:HOIP_0000517 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. increasing demand for response to oxidative stress [ER stress] HOIP_0000517 HOIP:HOIP_0000518 This gene encodes a secreted ligand of the TGF-beta (transforming growth factor-beta) superfamily of proteins. Ligands of this family bind various TGF-beta receptors leading to recruitment and activation of SMAD family transcription factors that regulate gene expression. The encoded preproprotein is proteolytically processed to generate each subunit of the disulfide-linked homodimer. The protein is expressed in a broad range of cell types, acts as a pleiotropic cytokine and is involved in the stress response program of cells after cellular injury. Increased protein levels are associated with disease states such as tissue hypoxia, inflammation, acute injury and oxidative stress. [provided by RefSeq, Aug 2016] NCBI-Human-GeneID:9518 PMID:21242297 PMID:23799024 PMID:25698447 GDF15 (human) [cell death (course)] HOIP_0000518 NCBI-Human-GeneID:9518 http://www.ncbi.nlm.nih.gov/gene/9518 PMID:21242297 Growth differentiation factor 15 deficiency protects against atherosclerosis by attenuating CCR2-mediated macrophage chemotaxis. J. Exp. Med. 208: 217-225, 2011. PMID:23799024 Adaptive induction of growth differentiation factor 15 attenuates endothelial cell apoptosis in response to high glucose stimulus. PMID:25698447 Growth differentiation factor-15 encodes a novel microRNA 3189 that functions as a potent regulator of cell death. HOIP:HOIP_0000519 Catalysis role of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. EC:1. related molecular function GO:0016491 oxidoreductase HOIP_0000519 HOIP:HOIP_0000520 The difference in distribution of cell death depends on the location of the toxic expression. Zone 3 hepatocytes are rich in P450, which produce drug metabolites to cause cell death. classification of cell death by distribution HOIP_0000520 HOIP:HOIP_0000521 Centrilobular necrosis is a subtype of classification of cell death by distribution: A hepatocyte necrosis localized around centrilobular zone. centrilobular necrosis HOIP_0000521 HOIP:HOIP_0000522 Periportal necrosis is a subtype of classification of cell death by distribution: A hepatocyte necrosis localized around the portal vein. periportal necrosis HOIP_0000522 HOIP:HOIP_0000523 Zonal necrosis is a subtype of classification of cell death by distribution: A hepatocyte necrosis localized around hepatic the lobule such as centrilobular (acinar zone 3) necrosis, midzonal (midlobular) necrosis, and periportal (perilobular) necrosis. zonal necrosis HOIP_0000523 HOIP:HOIP_0000524 A process that changes the magnitude of the inflammation to be larger. expanding inflammation HOIP_0000524 HOIP:HOIP_0000525 Expanding inflammation is a subtype of increasing quantity: A process that changes the magnitude of the inflammation the object to be larger. This entity is a specific course-dependent process. This process can constitute the course of cell death. expanding inflammation [cell death (course)] HOIP_0000525 HOIP:HOIP_0000526 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. leaking content from cell HOIP_0000526 HOIP:HOIP_0000527 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. This entity is a specific course-dependent process. This process can constitute the course of cell death. leaking content from cell [Nerosis] HOIP_0000527 HOIP:HOIP_0000528 NAPQI production is a subtype of generating a substance : A process that synthesizes NAPQI (N-acetyl-p-benzoquinone imine) as output. NAPQI production HOIP_0000528 HOIP:HOIP_0000532 Malfunctioning of controlling is a subtype of malfunctioning process: A process that cannot perform a controlling function appropriately or cannot realize it at all. malfunctioning of controlling HOIP_0000532 HOIP:HOIP_0000533 Cell repair is a subtype of repairing: A process that restores the cell after damage. cell repair HOIP_0000533 HOIP:HOIP_0000534 Cell repair is a subtype of repairing: A process that restores the cell after damage. This entity is a specific course-dependent process. This process can constitute the course of cell death. cell repair [cell death (course)] HOIP_0000534 HOIP:HOIP_0000535 Repairing is a subtype of changing an operand: A process that restores the object after damage. repairing HOIP_0000535 HOIP:HOIP_0000536 JNK signaling is a process that a signal is transmitted by the JNK (a stress-activated protein kinase (SAPK) ). This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. JNK signaling [oxidative stress (course)] HOIP_0000536 HOIP:HOIP_0000537 Extracellular matrix excess deposition is a subtype of accumulation of substances in a biological object: A process that puts extracellular matrix down in an organism, tissue, organelle, or cell. extracellular matrix excess deposition HOIP_0000537 HOIP:HOIP_0000538 process on structural viewpoint HOIP_0000538 HOIP:HOIP_0000539 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of Phosphoipidosis(severe). PMID:18955971 necrosis [phospholipidosis (severe)] HOIP_0000539 PMID:18955971 Massive Lysosomal membrane permeabilization (LMP) often results in cell death without caspase activation; this cell death may adopt a subapoptotic or necrotic appearance. The regulation of LMP is perturbed in cancer cells, suggesting that specific strategies for LMP induction might lead to novel therapeutic avenues. HOIP:HOIP_0000540 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. inflammatory cell infiltration HOIP_0000540 HOIP:HOIP_0000541 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course-dependent process. This process can constitute the course of necrosis. inflammatory cell infiltration [necrosis (course)] HOIP_0000541 HOIP:HOIP_0000542 Abnormality of membrane is a subtype of changing abnormal cellular structure: A process that changes the membrane stucture abnormally. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. abnormality of membrane [oxidative stress (course)] HOIP_0000542 HOIP:HOIP_0000543 Lipoperoxidation is a subtype of lipid oxidation: The degradation of lipids caused by an oxidative attack from free radicals. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. lipoperoxidation [oxidative stress (course)] HOIP_0000543 HOIP:HOIP_0000544 Changing area is a subtype of changing quality: A process that changes the area of the object. changing area HOIP_0000544 HOIP:HOIP_0000546 Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. positive regulation of mitochondrial membrane permeability [oxidative stress (course)] HOIP_0000546 HOIP:HOIP_0000549 Phosphorylation of eIF2-alpha by PERK is a subtype of eIF2a phosphorylation: A process that The process of introducing a phosphate group into eIF2a by PERK. Phosphorylation of eIF2-alpha by PERK HOIP_0000549 HOIP:HOIP_0000550 cause HOIP_0000550 HOIP:HOIP_0000551 result HOIP_0000551 HOIP:HOIP_0000552 Changing length is a subtype of changing quality: A process that changes the length of the object. changing length HOIP_0000552 HOIP:HOIP_0000553 upstream HOIP_0000553 HOIP:HOIP_0000554 downstream HOIP_0000554 HOIP:HOIP_0000555 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. leaking content from cell [phospholipidosis (severe)] HOIP_0000555 HOIP:HOIP_0000556 Negative regulation of phospholipase C mediated phospholipid degradation is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase C mediated phospholipid degradation. negative regulation of phospholipase C mediated phospholipid degradation HOIP_0000556 HOIP:HOIP_0000557 Sorting transport signal of NPC1 / NPC2 is a subtype of extractng: A process that obtains a necessary NPC1/NPC2 transport signal. transport signal sorting of NPC1 / NPC2 HOIP_0000557 HOIP:HOIP_0000558 Any process that increases the rate, frequency or extent of macrophage derived foam cell differentiation. Macrophage derived foam cell differentiation is the process in which a macrophage acquires the specialized features of a foam cell. The degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). positive regulation of macrophage derived foam cell differentiation [phospholipidosis (severe (excessive defense))] HOIP_0000558 HOIP:HOIP_0000559 A role played by the entity that inhibits the catalysis of the hydrolysis of a phospholipid. phospholipase inhibitor role HOIP_0000559 HOIP:HOIP_0000561 HYOU1 - chaperone -vitro (human)[ER stress] HOIP_0000561 HOIP:HOIP_0000562 A role played by the entity that inhibits the catalysis of the reaction: a phospholipid + H2O = 1,2-diacylglycerol + a phosphatidate. EC.3.1.4.3 (phospholipase C) inhibitor phospholipase C inhibitor role HOIP_0000562 HOIP:HOIP_0000563 NCBI-Human-GeneID:2538 NCBI-Mouse-GeneID:14377 NCBI-Rat-GeneID:25634 OMIM:232200 RGD:2644 G6Pase Glucose-6-Phosphatase Alpha Glucose-6-Phosphatase Catalytic Subunit G6PC (mol) HOIP_0000563 NCBI-Human-GeneID:2538 http://www.ncbi.nlm.nih.gov/gene/2538 NCBI-Mouse-GeneID:14377 http://www.ncbi.nlm.nih.gov/gene/14377 NCBI-Rat-GeneID:25634 http://www.ncbi.nlm.nih.gov/gene/25634 HOIP:HOIP_0000564 A molecular messenger in which the molecule is specifically involved in transmitting information between cells. Such molecules are released from the cell sending the signal, cross over the gap between cells by diffusion, and interact with specific receptors in another cell, triggering a response in that cell by activating a series of enzyme controlled reactions which lead to changes inside the cell. signal molecule signaling molecule signalling molecule role HOIP_0000564 HOIP:HOIP_0000565 Catalysis role of the reaction: donor + hydrogen peroxide = oxidized donor + 2 H2O. EC:1.11.1.7 oxyperoxidase related molecular function GO:0004601 peroxidase HOIP_0000565 HOIP:HOIP_0000566 Calcium ion homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a calcium ion homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. calcium ion homeostasis imbalance [oxidative stress (course)] HOIP_0000566 HOIP:HOIP_0000567 Imbalance process is a subtype of changing balance: A process that becomes lacking a correct balance between operands. imbalance process HOIP_0000567 HOIP:HOIP_0000568 Homeostasis imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance. Imbalance of homeostasis in the body is a lacking balance between performing amounts of defense (supply) and required amounts of protection (demand) in the maintenance of an internal state. homeostasis imbalance HOIP_0000568 HOIP:HOIP_0000569 Endoplasmic reticulum stress response imbalance is a subtype of stress response imbalance: A process that lacks a balance between the stimulation (stress) acting on the endoplasmic reticulum and the biological defence response. This entity is a specific course-dependent process. This process can constitute the course of ER stress. endoplasmic reticulum stress response imbalance [ER stress] HOIP_0000569 HOIP:HOIP_0000570 Stress response imbalance is a subtype of imbalance: A process that lacks a balance between the stimulation (stress) and the response. stress response imbalance HOIP_0000570 HOIP:HOIP_0000571 Endoplasmic reticulum stress response imbalance is a subtype of stress response imbalance: A process that lacks a balance between the stimulation (stress) acting on the endoplasmic reticulum and the biological defence response. endoplasmic reticulum stress response imbalance HOIP_0000571 HOIP:HOIP_0000572 Protein quality control imbalance is a subtype of imbalance: A process that lacks a balance between abnormal protein (misfolded or attenuated proteins) production and breakdown. protein quality control imbalance HOIP_0000572 HOIP:HOIP_0000573 Increasing demand for response to ER stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the endoplasmic reticulum (ER) stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. increasing demand for response to ER stress [apoptosis (course)] HOIP_0000573 HOIP:HOIP_0000574 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of cell death. increasing demand for response to oxidative stress [cell death] HOIP_0000574 HOIP:HOIP_0000575 bile acid and bile salt transporter HOIP_0000575 HOIP:HOIP_0000576 Metabolic intermediate accumulation is a subtype of accumulation of substances in a biological object: A process that keeps intermediate(s) of metabolism in an organism, tissue, organelle, or cell. metabolic intermediate accumulation HOIP_0000576 HOIP:HOIP_0000577 Decreasing pH is a subtype of changing pH: A process that changes the pH to be lower. decreasing pH HOIP_0000577 HOIP:HOIP_0000578 Decreasing cellular pH is a subtype of decreasing pH: A process that changes the cellular pH to be lower. decreasing cellular pH HOIP_0000578 HOIP:HOIP_0000579 Decreasing cellular pH is a subtype of decreasing pH: A process that changes the cellular pH to be lower. This entity is a specific course-dependent process. This process can constitute the course of cell death. decreasing cellular pH [cell death (course)] HOIP_0000579 HOIP:HOIP_0000580 Ischemia is a changing process to lack enough to blood supply. ischemia HOIP_0000580 HOIP:HOIP_0000582 Ischemia is a changing process to lack enough to blood supply. This entity is a specific course-dependent process. This process can constitute the course of necrosis. ischemia [necrosis (course)] HOIP_0000582 HOIP:HOIP_0000583 ATF6 (ATF6-alpha) activates chaperone genes is a subtype of molecular activation: A process that changes the activity of the molecule with chaperone role to be higher by ATF6. ATF6 (ATF6-alpha) activates chaperone genes HOIP_0000583 HOIP:HOIP_0000584 Regulation of Cxcl2 expression by TNF-alpha is a subtype of regulation of gene expression by TNF-alpha: A process that Any process that modulates the frequency, rate or extent of Cxcl2 expression by TNFalpha. TNFalpha->JNK->AP-1->CXCL1 mRNA expression TNFalpha->p38MAPK->PI3K->AKT->CXCL1 release from the cell membrane PMID:24487964 CXCL1 is one of the members of chemokines, which are small heparin-binding proteins that generally direct the movement of circulating leukocytes to sites of inflammation or injury. TNF-α stimulates CXCL1 release from human ECs through JNK-mediated CXCL1 mRNA expression and p38 MAPK- and PI-3K-mediated CXCL1 secretory processes. regulation of Cxcl2 expression by TNF-alpha HOIP_0000584 HOIP:HOIP_0000585 Regulation of gene expression by TNF-alpha is a subtype of molecular activation: Any process that modulates the frequency, rate or extent of gene expression by TNFalpha. regulation of gene expression by TNF-alpha HOIP_0000585 HOIP:HOIP_0000586 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. This entity is a specific course-dependent process. This process can constitute the course of PERK pathway. PERK activation [PERK pathway] HOIP_0000586 HOIP:HOIP_0000587 NCBI-Human-GeneID:6319 SCD (mol) HOIP_0000587 NCBI-Human-GeneID:6319 http://www.ncbi.nlm.nih.gov/gene/6319 HOIP:HOIP_0000588 Change in H+ ion concentrations is a subtype of changing concentration: A process that changes the hydrogen ion (H+) concentration in the blood. change in H+ ion concentrations HOIP_0000588 HOIP:HOIP_0000589 Changing weight is a subtype of changing quality: A process that changes the weight of the object. changing weight HOIP_0000589 HOIP:HOIP_0000590 Bile reflux is a subtype of back-flow: A process that changes the bile flow to the opposite direction. MeSH:D001655 bile reflux HOIP_0000590 HOIP:HOIP_0000592 Oxidative stress dependent molecule is a subtype of course dependent chemical entity. This molecule can participate in the course of oxidative stress as a gene product. Gene profile:Human/in vitro/Hepatocyte/ oxidative stress dependent molecule (human in vivo) HOIP_0000592 HOIP:HOIP_0000593 ISBN:0071769234 CCL4_ [Lipidosis] HOIP_0000593 ISBN:0071769234 Types of hepatobiliary injury: Fatty liver: Amiodarone, CCl4, ethanol, fialuridine, tamoxifen, valproic acid in Table 13-2. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0000594 Oxidative stress dependent molecule is a subtype of course dependent chemical entity. This molecule can participate in the course of oxidative stress as a gene product. Gene profile:caonical that described in textbooks or articles. oxidative stress dependent molecule (caonical) HOIP_0000594 HOIP:HOIP_0000595 ISBN:0071769234 CCL4 -necrosis inducer [Lipidosis] HOIP_0000595 ISBN:0071769234 Types of hepatobiliary injury: Fatty liver: Amiodarone, CCl4, ethanol, fialuridine, tamoxifen, valproic acid in Table 13-2. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0000596 Oxidative stress dependent molecule is a subtype of course dependent chemical entity. This molecule can participate in the course of oxidative stress as a gene product. Gene profile:Rat/Liver oxidative stress dependent molecule (rat) HOIP_0000596 HOIP:HOIP_0000598 A role played by the entity to perform peroxiidation of the target object. lipoperoxidator role HOIP_0000598 HOIP:HOIP_0000600 Meta-functioning process is a type of function-related process that executes a function for another function. https://doi.org/10.1016/S1474-0346(02)00006-XK For example, the 'to vaporize' function of the boiler is to perform a meta-function to enable for the 'to rotate' function of the turbine. The meta-functions are result of teleological interpretation of causal relations among base-functions of different components (i.e., inter-components relations). meta-functioning process HOIP_0000600 https://doi.org/10.1016/S1474-0346(02)00006-XK Kitamura Y. Advanced Engineering Informatics (former Artificial Intelligence in Engineering), Vol. 16, No. 2, pp. 145-163, 2002. HOIP:HOIP_0000601 Storing is a subtype of receiving: A process that keeps target object(s). storing HOIP_0000601 HOIP:HOIP_0000602 Depleting is a subtype of decreasing quantity: A process that that lessens markedly in quantity of the object to nearly zero. depleting HOIP_0000602 HOIP:HOIP_0000603 Pathway system is a subtype of object aggregates. This entity has sub-parts and has a goal of transmitting as a systemic context. pathway system HOIP_0000603 HOIP:HOIP_0000604 CREB3L3 signaling is a subtype of signaling that a signal is transmitted by CREB3L3. CREB3L3 signaling HOIP_0000604 HOIP:HOIP_0000605 Hypofunction of ATP biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient ATP biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. hypofunction of ATP biosynthesis [oxidative stress (course)] HOIP_0000605 HOIP:HOIP_0000606 Catalysis role of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. EC:2. related molecular function GO:0016740 transferase HOIP_0000606 HOIP:HOIP_0000607 Maintaining mitochondrial membrane permeability is a subtype of maintaining membrane permeability is a changing process to keep the permeability of the membrane: A process that keeps the permeability of the mitochondrial membrane. maintaining mitochondrial membrane permeability HOIP_0000607 HOIP:HOIP_0000608 Process sequence is a subtype of occurrents that is a series of process. process sequence HOIP_0000608 HOIP:HOIP_0000609 Signaling pathway is a subtype of pathway: Sequence of linked reactions in which a signal is transmitted to other(s). signaling cascade 1. signal detection (acceptance), 2. signal transduction, 3. gene regulation (genetic information conversion process), 4. celllular process execution This entity covers from 1 to 2. signaling pathway HOIP_0000609 HOIP:HOIP_0000610 Metabolic pathway is a subtype of pathway: Sequence of enzyme reactions to change metabolism, including anabolism and catabolism. metabolic pathway HOIP_0000610 HOIP:HOIP_0000611 A series of molecular signals mediated by death-domain superfamily. PMID:12189384 death domain signanaling pathway HOIP_0000611 HOIP:HOIP_0000612 The process in which the anatomical structures of the nodule are generated and organized. GO:0009877 nodule morphogenesis is part of some nodulation. However, nodulation is defined as the formation of nitrogen-fixing root nodules on plant roots. Therefore, TXPO does not reuse GO terms and defines originally. nodule formation HOIP_0000612 HOIP:HOIP_0000613 NCBI-Human-GeneID:2719 NCBI-Mouse-GeneID:14734 NCBI-Rat-GeneID:25236 GPC3 (mol) HOIP_0000613 NCBI-Human-GeneID:2719 https://www.ncbi.nlm.nih.gov/gene/2719 NCBI-Mouse-GeneID:14734 https://www.ncbi.nlm.nih.gov/gene/14734 NCBI-Rat-GeneID:25236 https://www.ncbi.nlm.nih.gov/gene/25236 HOIP:HOIP_0000616 Increasing volume of liver is a subtype of increasing volume: A process that changes the volume of the liver to be higher. increasing volume of liver HOIP_0000616 HOIP:HOIP_0000617 A peptide containing ten or more amino acid residues. polypeptide HOIP_0000617 HOIP:HOIP_0000618 Increasing ROS/RNS is a process of changing amount to increase the magnitude of the ROS or RNS. increase of ROS and RNS production HOIP_0000618 HOIP:HOIP_0000619 Removing damaged object is a subtype of removing: A process that takes a damaged object from an organism, tissue, organelle, or cell. removing damaged object HOIP_0000619 HOIP:HOIP_0000620 Removing damaged organelle is a subtype of removing damaged object: A process that takes a damaged organelle from a cell. removing damaged organelle HOIP_0000620 HOIP:HOIP_0000621 Negative regulation of phospholipase C mediated phosphatidylcholine degradation is a subtype of negative regulation of phosphatidylcholine catabolic process: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase C mediated phosphatidylcholine degradation. negative regulation of phospholipase C mediated phosphatidylcholine degradation HOIP_0000621 HOIP:HOIP_0000622 A signaling role played by the entity such as protein, polypeptide, or glycoprotein that acts on neighboring cells to alter their behavior. A signaling role played by the entity such as protein, polypeptide, or glycoprotein that acts on neighboring cells to alter their behavior. Extracellular signal protein or peptide that acts as a local mediator in cell-cell communication. Extracellular signal protein or peptide that acts as a local mediator in cell-cell communication. IMR:0000006 (obsolete) related molecular function GO:0005125 cytokine HOIP_0000622 A signaling role played by the entity such as protein, polypeptide, or glycoprotein that acts on neighboring cells to alter their behavior. ISBN:0815344546 Extracellular signal protein or peptide that acts as a local mediator in cell-cell communication. ISBN:0815340729 HOIP:HOIP_0000623 A role of regulating receiving process of receptors such that the proportion of receptors in the active form is changed. related molecular function GO:0030545 regulator role of receiving HOIP_0000623 HOIP:HOIP_0000624 A role played by the entity that Interacts selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. Binding to a specific receptor protein and activating intracellular signaling cascades that alter the behavior of the cell. Binding to a specific receptor protein and activating intracellular signaling cascades that alter the behavior of the cell. IMR:0000002 (obsolete) Wikipedia:Ligand_(biochemistry) http://purl.obolibrary.org/obo/CHEBI_52214 related molecular function GO:0005102 ligand HOIP_0000624 Binding to a specific receptor protein and activating intracellular signaling cascades that alter the behavior of the cell. ISBN:0815340729 HOIP:HOIP_0000625 A role played by the entity to increase number of operand(s) role related to increasing number HOIP_0000625 HOIP:HOIP_0000626 A role played by the entity to replicate DNA. DNA replication factor role HOIP_0000626 HOIP:HOIP_0000627 Removing damaged cell is a subtype of removing damaged object: A process that takes a damaged cell from an organism or tissue. removing damaged cell HOIP_0000627 HOIP:HOIP_0000628 Negative regulation of phopholipase C mediated phosphatidyliserine degradation is a subtype of negative regulation of phosphatidylserine degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phopholipase C mediated phosphatidyliserine degradation. negative regulation of phopholipase C mediated phosphatidyliserine degradation HOIP_0000628 HOIP:HOIP_0000631 Removing xenobiotics is a subtype of taking process: A process that removes xenobiotics from an organ, tissue, cell, organelle, or makes a clearance of it from the body. xenobiotics excretion HOIP_0000631 HOIP:HOIP_0000632 Increasinging length of time is a subtype of changing length of time: A process that changes the length of time to be longer. increasinging length of time HOIP_0000632 HOIP:HOIP_0000633 Increasing functional demand is a subtype of increasing quantity: A process changes the functional demand to be higher. Rubin　Pathology increasing functional demand HOIP_0000633 HOIP:HOIP_0000634 Signal transduction system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals as a systemic context. signal transduction system HOIP_0000634 HOIP:HOIP_0000635 Phospholipase family HOIP_0000635 HOIP:HOIP_0000638 role related to decreasing amount HOIP_0000638 HOIP:HOIP_0000640 NCBI-Rat-GeneID:54318 PMID:24623724 Eif2s1 (rat) [cell death (course)] HOIP_0000640 NCBI-Rat-GeneID:54318 http://www.ncbi.nlm.nih.gov/gene/54318 HOIP:HOIP_0000641 NCBI-Rat-GeneID:171493 Osgin1 (rat)[cell death (course)] HOIP_0000641 NCBI-Rat-GeneID:171493 http://www.ncbi.nlm.nih.gov/gene/171493 HOIP:HOIP_0000642 Txrnd1 (rat) [cell death (course)] HOIP_0000642 HOIP:HOIP_0000643 Increasing AST concentration in blood is a subtype of increasing concentration: A process that changes the aspartate amino transferase (AST) concentration to be higher. http://purl.bioontology.org/ontology/MEDDRA/10003544 inreasing blood GOT concentration inreasing blood AST concentration HOIP_0000643 HOIP:HOIP_0000644 Decreasing lipid is a subtype of decreasing quantity: A process that changes the quantity of the lipid to be lower. decreasing lipid HOIP_0000644 HOIP:HOIP_0000645 NCBI-Rat-GeneID:24451 Hmox1 (rat) [cell death (course)] HOIP_0000645 NCBI-Rat-GeneID:24451 http://www.ncbi.nlm.nih.gov/gene/24451 HOIP:HOIP_0000650 Nifib (rat)[cell death (course)] HOIP_0000650 HOIP:HOIP_0000652 The pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins. PW:0001277 glutathione biosynthetic pathway HOIP_0000652 HOIP:HOIP_0000653 NCBI-Rat-GeneID:24516 JUN (canonical) [cell death (course)] HOIP_0000653 NCBI-Rat-GeneID:24516 http://www.ncbi.nlm.nih.gov/gene/24516 HOIP:HOIP_0000655 Hyperfunction of antioxidant gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive antioxidant gene expression. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of antioxidant gene expression [glutathione depletion (course)] HOIP_0000655 HOIP:HOIP_0000656 antixidant gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) involved in antioxidant process. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. antioxidant gene expression [Gutathione depletion] HOIP_0000656 HOIP:HOIP_0000657 A physical quality that inheres in a bearer by calculation under some condition. predicted (quality) HOIP_0000657 HOIP:HOIP_0000658 Hyperfunction of antioxidant gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive antioxidant gene expression. This entity is a specific course-dependent process. This process can constitute the course of glutathione depletion. hyperfunction of antioxidant gene expression HOIP_0000658 HOIP:HOIP_0000660 Changing protein structure is a subtype of changing structure: A process that changes the stucture of the protein. changing protein structure HOIP_0000660 HOIP:HOIP_0000662 Cytoplasmic alternation [Liver PathologicalFindings] is a type of finding observed in the liver. Lesions are observed as changes in cytoplasm based on pathological morphology. Changes in cytoplasm in the hepatocytes. Liver is responsible for drug metabolism; therefore these findings are most frequently observed results in drug safety studies. It shows various morphological images depending on the kind of chemical substance. Changes in cytoplasm in the hepatocytes. Liver is responsible for drug metabolism; therefore these findings are most frequently observed results in drug safety studies. It shows various morphological images depending on the kind of chemical substance. cytoplasmic change [Liver PathologicalFindings] cytoplasmic alternation [Liver Pathological Findings] HOIP_0000662 Changes in cytoplasm in the hepatocytes. Liver is responsible for drug metabolism; therefore these findings are most frequently observed results in drug safety studies. It shows various morphological images depending on the kind of chemical substance. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0000664 Caspase signaling is a process that a signal is transmitted by the caspase. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). PMID:15720040 caspase signaling [phospholipidosis (severe (excessive defense))] HOIP_0000664 PMID:15720040 Induction of apoptosis by cationic amphiphilic drugs amiodarone and imipramine. HOIP:HOIP_0000665 NCBI-Human-GeneID:1842 NCBI-Mouse-GeneID:407800 NCBI-Rat-GeneID:100361383 ECM2 (mol) HOIP_0000665 NCBI-Human-GeneID:1842 http://www.ncbi.nlm.nih.gov/gene/1842 NCBI-Mouse-GeneID:407800 http://www.ncbi.nlm.nih.gov/gene/407800 NCBI-Rat-GeneID:100361383 http://www.ncbi.nlm.nih.gov/gene/100361383 HOIP:HOIP_0000666 NCBI-Human-GeneID:229 NCBI-Mouse-GeneID: 230163 NCBI-Rat-GeneID: 24190 PMID:26376879 ALDOB (mol) HOIP_0000666 NCBI-Human-GeneID:229 http://www.ncbi.nlm.nih.gov/gene/229 NCBI-Mouse-GeneID: 230163 http://www.ncbi.nlm.nih.gov/gene/230163 NCBI-Rat-GeneID: 24190 http://www.ncbi.nlm.nih.gov/gene/229 PMID:26376879 Aldolase B inhibits metastasis through Ten-Eleven Translocation 1 and serves as a prognostic biomarker in hepatocellular carcinoma. HOIP:HOIP_0000667 Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. This entity is a specific course-dependent process. This process can constitute the course of cell death. regulation of gene expression [cell death (course)] HOIP_0000667 HOIP:HOIP_0000668 A role played by the entity which responses to any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. related process GO:0006979 response to oxidative stress oxidative stress responsive factor role HOIP_0000668 HOIP:HOIP_0000670 ISBN:0071769234 ethanol [Lipidosis] HOIP_0000670 ISBN:0071769234 Exposure to ethanol induces steatosis, which may enhance the subsequent inflammatory insults. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0000671 Decreasing concentration is a subtype of changing concentration: A process that changes the concentration of the object to be lower. decreasing concentration HOIP_0000671 HOIP:HOIP_0000672 gene expression by estrogen receptor HOIP_0000672 HOIP:HOIP_0000673 Starvation is a subtype of depleting: A process that lessens markedly in quantity of the nourishment. http://purl.bioontology.org/ontology/MESH/D013217 starvation HOIP_0000673 HOIP:HOIP_0000674 PERK autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by PERK of one or more of its own amino acid residues (cis-autophosphorylation), or residues on PERK (trans-autophosphorylation). This entity is a specific course-dependent process. This process can constitute the course of ER stress. PERK autophosphorylation [ER stress] HOIP_0000674 HOIP:HOIP_0000675 Any process that stops, prevents, or reduces the frequency, rate or extent of glycolysis. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. negative regulation of glycolytic process [glutathione depletion (course)] HOIP_0000675 HOIP:HOIP_0000676 Catalysis of the reaction: D-fructose-1-phosphate = dihydroxyacetone phosphate + D-glyceraldehyde. fructose-1-phosphate aldolase HOIP_0000676 HOIP:HOIP_0000677 The totality of all processes through which oxidative stress is realized. Generation of free radicals or depletion of free radical scavengers and other antioxidant defences such as glutathione -> generation of reactive oxyen metabolites ->damaging effects on cell oxidative stress (course) HOIP_0000677 HOIP:HOIP_0000678 Necrosis (course) is a subtype of cell death (course). The totality of all processes through which necrosis is realized. Necrosis is a type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. PMID:18846107 PMID:20823910 necrosis (course) HOIP_0000678 HOIP:HOIP_0000679 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that includes step 1 to 4, and the defense performance level is very higher (VH) than usual which leads to imbalance and abnormal manifestations. imbalance VH (excess defense function) HOIP_0000679 HOIP:HOIP_0000680 In the imbalance model, the basic units are as follows: In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that inculdes step 1 to 4. The defense performance level is Moderate (M) in the normal coindition; however, the functional demand level is High (H), which leads to the imbalance. imbalance M<H HOIP_0000680 HOIP:HOIP_0000681 Scarring is a subtype of changing material: A process of keeping area replaced into fibrous tissue by injury. scarring HOIP_0000681 HOIP:HOIP_0000682 Maintaining balance is a subtype of changing balance: A process that keeps the steady state between operands. maintaining balance HOIP_0000682 HOIP:HOIP_0000684 Maintaining stress response balance is a subtype of maintaining balance: A process that keeps a balance between the stimulation (stress) and the response. maintaining stress response balance HOIP_0000684 HOIP:HOIP_0000685 Maintaining endoplasmic reticulum stress response balance is a subtype of maintaining stress response balance: A process that keeps a balance between the stimulation (stress) acting on the endoplasmic reticulum and the biological defence response. maintaining endoplasmic reticulum stress response balance HOIP_0000685 HOIP:HOIP_0000687 Increasing demand for response to ER stress (moderate) is a subtype of increasing the demand for response to ER stress: A process that changes the functional demand for the response to the edoplasmic reticulum (ER) stress to be moderately higher. increasing demand for response to ER stress (moderate) HOIP_0000687 HOIP:HOIP_0000688 Increasing demand for response to ER stress (mild) is a subtype of increasing the demand for response to ER stress: A process that changes the functional demand for the response to the edoplasmic reticulum (ER) stress to be mildly higher. increasing demand for response to ER stress (mild) HOIP_0000688 HOIP:HOIP_0000689 Increasing demand for response to ER stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the edoplasmic reticulum (ER) stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress (mild). increasing demand for response to ER stress [ER stress (mild) ] HOIP_0000689 HOIP:HOIP_0000690 Increasing demand for response to ER stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the edoplasmic reticulum (ER) stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress (moderate). increasing the demand for response to ER stress [ER stress] [ER stress (moderate) ] HOIP_0000690 HOIP:HOIP_0000691 reduced oxygenation of body tissues resulting in the decreased pressure of this component of body gases; commonly due to hypoxemia This entity is a specific course-dependent process. This process can constitute the course of ER stress. hypoxia [ER stress] HOIP_0000691 HOIP:HOIP_0000692 Lysosomal proliferation in hepatocyte is a subtype of increasing number of organelle: A process that becomes larger in the number of lysosome in hepatocyte(s). lysosomal proliferation in hepatocyte HOIP_0000692 HOIP:HOIP_0000693 The chemical reactions and pathways resulting in the formation of glycolipid, a class of 1,2-di-O-acylglycerols joined at oxygen 3 by a glycosidic linkage to a carbohydrate part (usually a mono-, di- or tri-saccharide). This entity is a specific course-dependent process. This process can constitute the course of ER stress. glycolipid biosynthetic process [ER stress] HOIP_0000693 HOIP:HOIP_0000694 Lysosomal cholesterol storage is a subtype of cholesterol storage: A process that keeps cholesterol in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. lysosomal cholesterol storage [phospholipidosis (imbalance course)] HOIP_0000694 HOIP:HOIP_0000696 A process that changes the activity of the eIF2a by PERK. changing activity of eIF2a by PERK HOIP_0000696 HOIP:HOIP_0000697 EIF2a phosphorylation is a subtype of phosphorylation: The process of introducing a phosphate group into eIF2a. This entity is a specific course-dependent process. This process can constitute the course of ER stress. eIFF2a phophorylation [ER stress] HOIP_0000697 HOIP:HOIP_0000698 Gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by ATF4. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:23334697 R-HSA-380994 ATF4 is a transcription factor and activates expression of IL-8, MCP1, IGFBP-1, CHOP, HERP1 and ATF3. gene expression by ATF4 [ER stress] HOIP_0000698 PMID:23334697 ATF4 is a bZIP transcription factor that controls the regulation of expression of pro-survival UPR-target genes (e.g., the chaperones glucose regulated protein [GRP]78 and GRP94) as well as genes involved in other functions such as redox homeostasis, amino acid metabolism, apoptosis, and autophagy. HOIP:HOIP_0000699 Changing velocity is a subtype of changing quality: A process that chnges the velocity of the object. changing speed HOIP_0000699 HOIP:HOIP_0000700 Phosphorylation of eIF2-alpha by PERK is a subtype of eIF2a phosphorylation: A process that The process of introducing a phosphate group into eIF2a by PERK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:23334697 PMID:9930704 Reactome:R-HSA-381111 The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Phosphorylation of eIF2-alpha by PERK [ER stress] HOIP_0000700 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Nature. 1999 Jan 21;397(6716):271-4. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Erratum in Nature 1999 Mar 4;398(6722):90. Protein synthesis and the folding of the newly synthesized proteins into the correct three-dimensional structure are coupled in cellular compartments of the exocytosis pathway by a process that modulates the phosphorylation level of eukaryotic initiation factor-2alpha (eIF2alpha) in response to a stress signal from the endoplasmic reticulum (ER). Activation of this process leads to reduced rates of initiation of protein translation during ER stress. ER stress increases PERK's protein-kinase activity and PERK phosphorylates eIF2alpha on serine residue 51, inhibiting translation of messenger RNA into protein. These properties implicate PERK in a signalling pathway that attenuates protein translation in response to ER stress. Comment in Translational control perks up. [Nature. 1999] The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Id:R-HSA-381111 HOIP:HOIP_0000701 PERK-eIF2a signaling (integrated pathway) is a subtype of PERK signaling (integrated pathway): Sequence of linked reactions, which has PERK-eIF2a signaling and gene regulation pathway. PERK-eIF2a signaling (integrated pathway) HOIP_0000701 HOIP:HOIP_0000703 Expression of CHOP (DDIT3, GADD153) is a subtype of gene expression: The process in which a gene sequence is converted into a mature CHOP (DDIT3, GADD153) gene product or products (proteins or RNA). http://www.reactome.org/PathwayBrowser/#/R-HSA-380994&SEL=R-HSA-1791107&PATH=R-HSA-392499,R-HSA-381119,R-HSA-381042 Expression of CHOP (DDIT3, GADD153) HOIP_0000703 HOIP:HOIP_0000704 Expression of CCL2 is a subtype of inflammatory cytokine gene expression: A process that convert a CCL2 (C-C Motif Chemokine Ligand 2) gene's sequenes into a mature gene prduct(s), i.e., (m)RNA, or protein. http://www.reactome.org/PathwayBrowser/#/R-HSA-380994&SEL=R-HSA-1791056&PATH=R-HSA-392499,R-HSA-381119,R-HSA-381042 The CCL2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein. expression of CCL2 HOIP_0000704 HOIP:HOIP_0000705 IGFBP1 activation is a subtype of molecular activation: A process that changes the activity of the IGFBP1 (Insulin Like Growth Factor Binding Protein 1) to be higher. IGFBP1 activation HOIP_0000705 HOIP:HOIP_0000706 ATF4 gene expression by eIF2a is a subtype of gene expression: The process in which a gene sequence is converted into a mature ATF4 gene product or products (proteins or RNA) by eIF2a. http://www.reactome.org/PathwayBrowser/#/R-HSA-381119&SEL=R-HSA-381128&PATH=R-HSA-392499 Phosphorylation of eIF2-alpha causes increased translation of ATF4 mRNA. In mouse the mRNA of ATF4 contains 2 upstream ORFs (uORFs) (Vattem and Wek 2004). The second uORF overlaps the ORF encoding ATF4 and thus prevents translation of ATF4. When eIF2-alpha is phosphorylated, translation of the uORFs is suppressed and translation of the ORF encoding ATF4 is increased. ATF4 gene expression by eIF2a HOIP_0000706 HOIP:HOIP_0000707 ATF4 gene expression by eIF2a is a subtype of gene expression: The process in which a gene sequence is converted into a mature ATF4 gene product or products (proteins or RNA) by eIF2a. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:23334697 Reactome:R-HSA-381128 http://www.ncbi.nlm.nih.gov/pubmed/18426796 ATF4 gene expression by eIF2a [ER stress] HOIP_0000707 PMID:23334697 Under conditions of eIF2α phosphorylation, a subset of mRNAs with small upstream open reading frames (such as activating transcription factor 4 [ATF4]) or internal ribosome entry sites are preferentially translated. ATF4 is a bZIP transcription factor that controls the regulation of expression of pro-survival UPR-target genes (e.g., the chaperones glucose regulated protein [GRP]78 and GRP94) as well as genes involved in other functions such as redox homeostasis, amino acid metabolism, apoptosis, and autophagy. HOIP:HOIP_0000708 IGFBP1 activation is a subtype of molecular activation: A process that changes the activity of the IGFBP1 (Insulin Like Growth Factor Binding Protein 1) to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:16687408 IGFBP1 activation [ER stress] HOIP_0000708 PMID:16687408 Endoplasmic reticulum stress induction of insulin-like growth factor-binding protein-1 involves ATF4. Mutation of the ATF4 led to the loss of IGFBP-1 regulation. Increased secretion of IGFBP-1 during hepatic ER stress may thus constitute a signal to modulate cell growth and metabolism and induce a systemic adaptive response. Indeed, various transgenic mice overexpressing the IGFBP-1 gene consistently display impaired glucose tolerance and abnormalities in insulin action in addition to alterations of reproduction, intrauterine, and postnatal growth restrictions. HOIP:HOIP_0000709 Expression of CCL2 is a subtype of inflammatory cytokine gene expression: A process that convert a CCL2 (C-C Motif Chemokine Ligand 2) gene's sequenes into a mature gene prduct(s), i.e., (m)RNA, or protein. This entity is a specific course-dependent process. This process can constitute the course of ER stress. expression of CCL2 [ER stress] HOIP_0000709 HOIP:HOIP_0000710 ATF6 activation is a subtype of molecular activation: A process that changes the activity of the ATF6 (Activating Transcription Factor 6) to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. ATF6 activation [ER stress] HOIP_0000710 HOIP:HOIP_0000711 Deacreasing velocity is a subtype of changing velocity: A process that changes the velocity of the object to be slower. Deacreasing velocity HOIP_0000711 HOIP:HOIP_0000712 PERK dimerization is a subtype of protein dimerization: The formation of a PERK dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. PERK dimerization HOIP_0000712 HOIP:HOIP_0000713 PERK dimerization is a subtype of protein dimerization: The formation of a PERK dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Reactome:R-HSA-381087 http://www.ncbi.nlm.nih.gov/pubmed/11907036 PERK dimerization [ER stress] HOIP_0000713 HOIP:HOIP_0000714 Hypofunction of cholesterol transport is a subtype of hypofunction of transport: A process that performs a decreased or insufficient cholesterol transport. hypofunction of cholesterol transport HOIP_0000714 HOIP:HOIP_0000717 Hypofunction of cholesterol transport from lysosome is a subtype of hypofunction of transport: A process that performs a decreased or insufficient cholestsrol transport from lysosomes. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). hypofunction of cholesterol transport from lysosome [phospholipidosis (severe)] HOIP_0000717 HOIP:HOIP_0000718 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. This entity is a specific course-dependent process. This process can constitute the course of ATF6 pathway. ATF6 signaling [ATF6 pathway] HOIP_0000718 HOIP:HOIP_0000719 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. This entity is a specific course-dependent process. This process can constitute the course of ER stress. ATF6 signaling [ER stress] HOIP_0000719 HOIP:HOIP_0000720 IRE1 signaling is a process that a signal is transmitted by the IRE1 (Inositol-requiring transmembrane kinase/endonuclease). IRE1 generally plays a endoplasmic reticulum membrane stress sensor role. IRE1 signaling HOIP_0000720 HOIP:HOIP_0000721 IRE1 signaling is a process that a signal is transmitted by the IRE1 (Inositol-requiring transmembrane kinase/endonuclease). IRE1 generally plays a endoplasmic reticulum membrane stress sensor role. This process is dependent on the refolding and can constitute the course of ER stress. IRE1 signaling [ER stress - refolding] HOIP_0000721 HOIP:HOIP_0000722 Translational attenuation is a regulatory mechanism analogous to ribosome-mediated transcriptional attenuation. the system requires the presence of a short orf, called a leader peptide, encoded in the mrna upstream of the ribosome-binding site and start codon of the gene whose translation is to be regulated. certain conditions, such as presence of the antibiotic tetracycline in bacteria or amino acid starvation, may cause slowing or stalling of the ribosome translating the leader peptide. the stalled ribosome masks a region of the mrna and affects which of two alternative mrna folded structures will form, therefore controlling whether or not a ribosome will bind and initiate translation of the downstream gene. translational attenuation is analogous to ribosome-mediated transcriptional attenuation, in which mrna remodeling caused by ribosome stalling regulates transcriptional termination rather than translational initiation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:23334697 PMID:9930704 attenuation of translation [ER stress] HOIP_0000722 PMID:23334697 General protein translation is inhibited via the PERK pathway to reduce increased protein burden in the ER. PMID:9930704 ER stress increases PERK's protein-kinase activity and PERK phosphorylates eIF2alpha on serine residue 51, inhibiting translation of messenger RNA into protein. These properties implicate PERK in a signalling pathway that attenuates protein translation in response to ER stress. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature: 1999, 397(6716);271-4 HOIP:HOIP_0000723 XBP1 activation is a subtype of activation of transcription factor: A process that changes the activity of XBP1 (X-Box Binding Protein 1) to be higher. XBP1 activation HOIP_0000723 HOIP:HOIP_0000725 XBP1 splicing is a subtype of removing: The process of removing sections of the XBP1 RNA transcript to remove sequences. XBP1 splicing HOIP_0000725 HOIP:HOIP_0000726 XBP1 splicing is a subtype of removing: The process of removing sections of the XBP1 RNA transcript to remove sequences. This entity is a specific course-dependent process. This process can constitute the course of ER stress. XBP1 splicing [ER stress] HOIP_0000726 HOIP:HOIP_0000727 ERAD related gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature ER-associated degradation (ERAD) gene product or products (proteins or RNA). ERAD related gene expression HOIP_0000727 HOIP:HOIP_0000728 ERAD related gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature ER-associated degradation (ERAD) gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of ER stress. ERAD related gene expression [ER stress] HOIP_0000728 HOIP:HOIP_0000729 IRE1 activation is a subtype of molecular activation: A process that changes the activity of the IRE1 to be higher. IRE1 activation HOIP_0000729 HOIP:HOIP_0000730 IRE1 activation is a subtype of molecular activation: A process that changes the activity of the IRE1 to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. IRE1 activation [ER stress] HOIP_0000730 HOIP:HOIP_0000731 Hypofunction of endosome to lysosome transport of low-density lipoprotein particle is a subtype of hypofunction of cholesterol transport: A process that performs a decreased or insufficient endosome to lysosome transport of low-density lipoprotein particle. decreasing endosome to lysosome transport of LDL hypofunction of endosome to lysosome transport of low-density lipoprotein particle HOIP_0000731 HOIP:HOIP_0000733 Starvation is a subtype of depleting: A process that lessens markedly in quantity of the nourishment. This entity is a specific course-dependent process. This process can constitute the course of ER stress. starvation [ER stress] HOIP_0000733 HOIP:HOIP_0000734 Increasing demand for response to ER stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the edoplasmic reticulum (ER) stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. increasing demand for response to ER stress [ER stress] HOIP_0000734 HOIP:HOIP_0000736 NCBI-Human-GeneID:30814 PLA2G2E (mol) HOIP_0000736 NCBI-Human-GeneID:30814 http://www.ncbi.nlm.nih.gov/gene/30814 HOIP:HOIP_0000737 NCBI-Human-GeneID:123688 NCBI-Mouse-GeneID:235386 NCBI-Rat-GeneID:300723 Hykk (mol) HOIP_0000737 NCBI-Human-GeneID:123688 http://www.ncbi.nlm.nih.gov/gene/123688 NCBI-Mouse-GeneID:235386 https://www.ncbi.nlm.nih.gov/gene/235386 NCBI-Rat-GeneID:300723 http://www.ncbi.nlm.nih.gov/gene/300723 HOIP:HOIP_0000738 Lgpat2 HOIP_0000738 HOIP:HOIP_0000740 Lgpat HOIP_0000740 HOIP:HOIP_0000741 Supplying from stored substance(s) is a subtype of making existence: A process that supplies (the stored) objects to the output. A process of supplying the operand from the stored substances supplying (from stored substance(s)) HOIP_0000741 HOIP:HOIP_0000742 PERK autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by PERK of one or more of its own amino acid residues (cis-autophosphorylation), or residues on PERK (trans-autophosphorylation). PERK autophosphorylation HOIP_0000742 HOIP:HOIP_0000744 Removing phospholipid by Kupffer cell or macrophage is a subtype of removing: A process that takes dead cells from a cell by Kupffer cells or macrophages . Removing dead cell by Kupffer cell or macrophage HOIP_0000744 HOIP:HOIP_0000745 Increasing number of stress responses is a subtype of increasing number of actions: A process that becomes larger in the number of stress responses. This entity is a specific course-dependent process. This process can constitute the course of ER stress. increasing number of stress responses [ER stress] HOIP_0000745 HOIP:HOIP_0000747 Increasing demand for protein quality control is a subtype of increasing functional demand: A process that changes the functional demand for the protein quality control to be higher. increasing demand for protein quality control HOIP_0000747 HOIP:HOIP_0000751 Endoplasmic reticulum dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete endoplasmic reticulum function. endoplasmic reticulum dysfunction HOIP_0000751 HOIP:HOIP_0000752 Endoplasmic reticulum dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete endoplasmic reticulum function. This entity is a specific course-dependent process. This process can constitute the course of ER stress. endoplasmic reticulum dysfunction [ER stress] HOIP_0000752 HOIP:HOIP_0000753 ER stress dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of ER stress as a gene product. Gene profile:Rat/Liver/ ER stress dependent molecule (rat) HOIP_0000753 HOIP:HOIP_0000754 CHOP->NfKB->CXCL10->inflammation in beta cells PMID:22653339 NCBI-Human-GeneID:3627 PMID:22653339 http://www.ncbi.nlm.nih.gov/gene/3627 cxcl10 [ER stress] HOIP_0000754 NCBI-Human-GeneID:3627 http://www.ncbi.nlm.nih.gov/gene/3627 PMID:22653339 CHOP Knock down resulted in reduced cytokine-induced NF-κB activity and expression of key NF-κB target genes involved in apoptosis and inflammation, including iNOS, FAS, IRF-7, IL-15, CCL5 and CXCL10. HOIP:HOIP_0000755 Any process that modulates the frequency, rate or extent of lysophagy. regulation of lysophagy HOIP_0000755 HOIP:HOIP_0000757 Any process that activates, maintains or increases the rate of lysophagy. positive regulation of lysophagy HOIP_0000757 HOIP:HOIP_0000758 A pathologic process that involves the transformation of normal cells to a neoplastic state and resulting in polyclonal or monoclonal neoplastic cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:22883813 PMID:27334111 tumorigenesis [ER stress] HOIP_0000758 PMID:22883813 ER stress-induced inflammation: does it aid or impede disease progression? PMID:27334111 Critical role of XBP1 in cancer signalling is regulated by PIN1. HOIP:HOIP_0000759 A role played by the entity that activates the activity of tumor cells. activator of tumor cell activity role HOIP_0000759 HOIP:HOIP_0000760 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:20303879 PMID:21038418 PMID:22883813 PMID:25232821 PMID:26609140 PMID:27346803 PMID:27814504 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2887297/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2887297/figure/F1/ inflammatory response [ER stress] HOIP_0000760 PMID:20303879 IRE1->JNK->AP-1->inflammatory response IRE1->XBP1s->IL6, IL8, MCP1 IRE1->IKK->NfkB ATF6->NfkB Perk->reducedIkB->NfkB PMID:21038418 Endoplasmic reticulum stress and related signaling networks, (adipo)cytokines, and innate immunity are emerging as central pathways that regulate key features of NASH. PMID:21038418 Inflammation Preceding Steatosis. Simple hepatic steatosis, which is benign and nonprogressive in the majority of patients, and NASH may reflect different disease entities. Inflammation results in a stress response of hepatocytes, may lead to lipid accumulation, and therefore could precede steatosis in NASH. PMID:22883813 ER stress-induced inflammation: does it aid or impede disease progression? PMID:27814504 Hepatic inflammation improves glucose homeostasis through IKKβ-XBP1s Interaction. HOIP:HOIP_0000761 NfkB signaling is a subtype of biological signaling: A process that in which a signal is transduced with the regulation of transcription of target genes by NF-kappaB. PW:0000499 http://purl.obolibrary.org/obo/GO_0007249 NfkB signaling HOIP_0000761 HOIP:HOIP_0000763 Bone-marrow-derived inhibitory cell migration is a moving process of bone-marrow-derived inhibitory cell to inflammatory site. bone-marrow-derived inhibitory cell migration HOIP_0000763 HOIP:HOIP_0000764 The orderly movement of a macrophage from one site to another. This entity is a specific course-dependent process. This process can constitute the course of ER stress. macrophage migration [ER stress] HOIP_0000764 HOIP:HOIP_0000765 Generating motion is a subtype of generating: A process that generates the directed movement. 出力に任意の生成した運動を出す generating motion HOIP_0000765 HOIP:HOIP_0000766 Tumor growth is a subtype of cell growth: The process in which a tumor cell increases in size. http://jglobal.jst.go.jp/en/detail?JGLOBAL_ID=200906011379989142 http://purl.obolibrary.org/obo/MP_0003721 tumor growth HOIP_0000766 HOIP:HOIP_0000767 Tumor growth is a subtype of cell growth: The process in which a tumor cell increases in size. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:29198525 tumor growth [ER stress] HOIP_0000767 PMID:29198525 A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response. HOIP:HOIP_0000768 oxidative stress ->oxidized lipids production ->ER stress induction (PERK(->eIF2a), JNK)->activation of autophagy->HO-1activation->cell survival Oxidized lipids activate autophagy in a JNK-dependent manner by stimulating the endoplasmic reticulum stress response. HNE modification of ER proteins results in the activation of the adaptive arm of the unfolded protein response. This HNE-mediated response is characterized by the phosphorylation of PERK, eIF2α, and JNK, activation of autophagy, and the induction of HO-1. HNE-stimulated conversion of LC3 (an essential step in autophagosome formation and marker of autophagy) and HO-1 induction is shown to be mediated by ER stress via JNK activation. PMID:24024137 NCBI-Rat-GeneID:24451 PMID:12649161 http://omim.org/entry/141250 Heme Oxygenase 1 [ER stress] Hmox1 (rat)[ER stress] HOIP_0000768 NCBI-Rat-GeneID:24451 http://www.ncbi.nlm.nih.gov/gene/24451 PMID:12649161 The basal level of heme oxygenase expression in the skin may serve as a first protective environment against acute oxidative and inflammatory insults. HOIP:HOIP_0000769 JNK signaling is a process that a signal is transmitted by the JNK (a stress-activated protein kinase (SAPK) ). JNK signaling HOIP_0000769 HOIP:HOIP_0000770 JNK signaling is a process that a signal is transmitted by the JNK (a stress-activated protein kinase (SAPK) ). This entity is a specific course-dependent process. This process can constitute the course of ER stress. JNK signaling [ER stress] HOIP_0000770 HOIP:HOIP_0000772 lysosomal phospholopase A2 group XV phospholipaseA2 HOIP_0000772 HOIP:HOIP_0000773 Drug-, radiation-induced, or spontaneous injuries to DNA that introduce deviations from its normal double-helical conformation. These changes include structural distortions that interfere with replication and transcription, as well as point mutations that disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. If the damage is minor, it can often be repaired (DNA repair); extensive damage can induce apoptosis. The degree is severe. This entity is a specific course-dependent process. This process can constitute the course of necrosis. DNA damage (severe) [necrosis (course)] HOIP_0000773 HOIP:HOIP_0000776 This gene is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. [provided by RefSeq, Jul 2008] NCBI-Human-GeneID:3484 PMID:16687408 http://purl.bioontology.org/ontology/MESH/D018970 IGFBP1 (human)[ER stress] HOIP_0000776 NCBI-Human-GeneID:3484 http://www.ncbi.nlm.nih.gov/gene/3484 PMID:16687408 Endoplasmic reticulum stress induction of insulin-like growth factor-binding protein-1 involves ATF4. HOIP:HOIP_0000778 NCBI-Rat-GeneID:24770 PERK->ATF4->CCl2 reactome CCL2 (human)[ER stress] HOIP_0000778 NCBI-Rat-GeneID:24770 http://www.ncbi.nlm.nih.gov/gene/24770 HOIP:HOIP_0000779 NCBI-Rat-GeneID:246273 PMID:12791994 PMID:15775988 PMID:17369260 http://omim.org/entry/607898 Trib3 (rat)[ER stress] HOIP_0000779 NCBI-Rat-GeneID:246273 http://www.ncbi.nlm.nih.gov/gene/246273 PMID:12791994 TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin by liver. Science 300: 1574-1577, 2003. PMID:15775988 TRB3 is a novel target of CHOP/ATF4 and downregulates its own induction by repression of CHOP/ATF4 functions, and that it is involved in CHOP-dependent cell death during ER stress. PMID:17369260 TRB3 inhibits the transcriptional activation of stress-regulated genes by a negative feedback on the ATF4 pathway. HOIP:HOIP_0000780 arrestin beta 2 NCBI-Human-GeneID:409 NCBI-Mouse-GeneID:216869 NCBI-Rat-GeneID:25388 PMID:30283336 ARRB2 (mol) HOIP_0000780 NCBI-Human-GeneID:409 http://www.ncbi.nlm.nih.gov/gene/409 NCBI-Mouse-GeneID:216869 http://www.ncbi.nlm.nih.gov/gene/216869 NCBI-Rat-GeneID:25388 http://www.ncbi.nlm.nih.gov/gene/25388 HOIP:HOIP_0000782 Malfunction of mitochondria is a subtype of malfunctioning process: A process that cannot perform a mitochondrial function appropriately or cannot realize it at all. malfunction of mitochondrial function HOIP_0000782 HOIP:HOIP_0000783 https://omim.org/entry/602634 ERDJ4 Dnajb9 (rat)[ER stress] HOIP_0000783 HOIP:HOIP_0000785 G protein-coupled receptor class C group 5 member B NCBI-Human-GeneID:51704 NCBI-Mouse-GeneID:64297 NCBI-Rat-GeneID:293546 GPRC5B (mol) HOIP_0000785 NCBI-Human-GeneID:51704 http://www.ncbi.nlm.nih.gov/gene/51704 NCBI-Mouse-GeneID:64297 http://www.ncbi.nlm.nih.gov/gene/64297 NCBI-Rat-GeneID:293546 http://www.ncbi.nlm.nih.gov/gene/293546 HOIP:HOIP_0000787 ISBN:0071769234 tamoxifen [Lipidosis] HOIP_0000787 ISBN:0071769234 Drug-induced steatosis is mainly caused by compounds such as 4,4′- diethylaminoethoxyhexestrol, amiodarone, tamoxifen, perhexiline, etc., which accumulate in mitochondria and inhibit β-oxidation and mitochondrial respiration. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0000788 ISBN:0071769234 valproic acid [Lipidosis] HOIP_0000788 ISBN:0071769234 Types of hepatobiliary injury: Fatty liver: Amiodarone, CCl4, ethanol, fialuridine, tamoxifen, valproic acid. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0000789 Increasing demand for drug metabolism is a subtype of increasing functional demand: A process changes the functional demand for the for drug metabolism to be higher. increasing demand for drug metabolism HOIP_0000789 HOIP:HOIP_0000791 NCBI-Mouse-GeneID:13198 PMID:15601821 PMID:15775988 PMID:22761832 PMID:25904325 http://www.omim.org/entry/126337 Chop [ER stress] Ddit3 (mouse)[ER stress] HOIP_0000791 NCBI-Mouse-GeneID:13198 http://www.ncbi.nlm.nih.gov/gene/13198 PMID:15775988 TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. HOIP:HOIP_0000793 ER stress dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of ER stress as a gene product. Gene profile:Human/in vitro/Hepatocyte/ ER stress dependent molecule (human in vitro) HOIP_0000793 HOIP:HOIP_0000794 ER stress dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the course of ER stress. ER stress dependent chemical entity HOIP_0000794 HOIP:HOIP_0000795 A laboratory test or analysis of the biological activity of a substance performed by studying its effect in an experimental situation outside the human, e.g. in the test tube rather than in living systems. in vitro assay (human) HOIP_0000795 HOIP:HOIP_0000796 ER stress and PPARα activation contribute to carcinogenesis in a fatty liver. PMID:22009939 Hepatosteatosis in peroxisome deficient liver despite increased beta-oxidation capacity and impaired lipogenesis. Biochimie (2011) 93:1828–38. FGF21-FGFR1 coordinates phospholipid homeostasis, lipid droplet function and ER stress in obesity.Endocrinology. 2016 PMID:27690692 Fibroblast growth factor 21 (FGF21) is an endocrine growth factor, a regulator of fatty acids and glucose metabolism. Recently, it has been reported that FGF21 expression is regulated by activating transcription factor 4 (ATF4), a transcription factor activated by various stimuli such as endoplasmic reticulum (ER) stress. PMID:27010621 Endoplasmic reticulum stress induces up-regulation of hepatic beta-Klotho expression through ATF4 signaling pathway. PMID:25727012 NCBI-Human-GeneID:26291 PMID:17550777 PMID:22009939 PMID:25727012 PMID:27010621 PMID:27690692 FGF21 (human)[ER stress] HOIP_0000796 PMID:24217556 NCBI-Human-GeneID:26291 http://www.ncbi.nlm.nih.gov/gene/26291 PMID:17550777 Endocrine regulation of the fasting response by PPARα-mediated induction of fibroblast growth factor 21: FGF21 is induced directly by PPARalpha in liver in response to fasting and PPARalpha agonists. FGF21 in turn stimulates lipolysis in white adipose tissue and ketogenesis in liver. PPARalpha-FGF21 endocrine signaling pathway in regulating diverse metabolic and behavioral aspects of the adaptive response to starvation. PMID:22009939 ER stress and PPARα activation contribute to carcinogenesis in a fatty liver. PMID:27010621 FGF21 expression is regulated by activating transcription factor 4 (ATF4), a transcription factor activated by various stimuli such as endoplasmic reticulum (ER) stress. PMID:27690692 FGF21 is regulated by PPARa: Hepatic fibroblast growth factor 21 is regulated by PPARα and is a key mediator of hepatic lipid metabolism in ketotic states. HOIP:HOIP_0000797 Any process that activates, maintains or increases the rate of lysophagy. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). positive regulation of lysophagy [phospholipidosis (severe)] HOIP_0000797 HOIP:HOIP_0000798 MANF is upregulated in ER stress in vitro and protect cells from ER stress-induced cell death in vivo. NCBI-Human-GeneID:7873 PMID:18561914 PMID:21047780 PMID:23956175 PMID:24726366 Armet [ER stress] mesencephalic astrocyte-derived neurotrophic factor [ER stress] MANF (human)[ER stress] HOIP_0000798 NCBI-Human-GeneID:7873 http://www.ncbi.nlm.nih.gov/gene/7873 PMID:18561914 Armet, a UPR-upregulated protein, inhibits cell proliferation and ER stress-induced cell death. Armet/MANF protein was upregulated by various forms of ER stress in several cell lines as well as by cerebral ischemia of rat. Armet/MANF was localized in the ER and Golgi and was also a secreted protein. Silencing Armet/MANF by siRNA oligos in HeLa cells rendered cells more susceptible to ER stress-induced death, but surprisingly increased cell proliferation and reduced cell size. PMID:21047780 Mesencephalic astrocyte-derived neurotrophic factor (MANF) has a unique mechanism to rescue apoptotic neurons. PMID:23956175 Armet/Manf and Creld2 are components of a specialized ER stress response provoked by inappropriate formation of disulphide bonds: implications for genetic skeletal diseases. PMID:24726366 MANF deficiency results in pancreatic beta cell depletion and diabetes in mice. MANF is highly expressed in mouse and human islet beta cells and exocrine acinar cells. MANF deficiency leads to ER stress and chronic unfolded protein response in beta cells. MANF protein enhances proliferation of beta cells in vitro and in vivo in diabetic mice. HOIP:HOIP_0000799 Permeabilization of mitochondrial membrane is a subtype of moving. A process that change the location of the operand thorough mitochondrial membrane. permeabilization mitochondrial membrane HOIP_0000799 HOIP:HOIP_0000800 NCBI-Human-GeneID:10525 R-HSA-1791066.1 https://omim.org/entry/601746 HYOU1 (human)[ER stress] HOIP_0000800 NCBI-Human-GeneID:10525 http://www.ncbi.nlm.nih.gov/gene/10525 HOIP:HOIP_0000801 NCBI-Human-GeneID:4189 https://omim.org/entry/602634 ERDJ4 DNAJB9 - chaperone -vitro (human)[ER stress] HOIP_0000801 NCBI-Human-GeneID:4189 http://www.ncbi.nlm.nih.gov/gene/4189 HOIP:HOIP_0000802 NCBI-Human-GeneID:7184 PMID:23334697 GRP94 [ER stress] HSP90B1 (human)[ER stress] HOIP_0000802 NCBI-Human-GeneID:7184 http://www.ncbi.nlm.nih.gov/gene/7184 PMID:23334697 Toxicol Pathol. 2013 Feb;41(2):235-62. doi: 10.1177/0192623312470764. Epub 2013 Jan 18. Xenobiotic perturbation of ER stress and the unfolded protein response. HOIP:HOIP_0000804 A role played by molecules that catalysis of the cleavage of a C-C bond in a molecule containing a hydroxyl group and a carbonyl group to form two smaller molecules, each being an aldehyde or a ketone. aldolase aldehyde-lyase HOIP_0000804 HOIP:HOIP_0000805 PMID:10818100 PMID:21091435 PMID:23334697 PMID:24469402 http://www.uniprot.org/uniprot/Q86YB8#function https://omim.org/entry/615437 ERO1LB (human)[ER stress] HOIP_0000805 PMID:21091435 The endoplasmic reticulum sulfhydryl oxidase Ero1-beta drives efficient oxidative protein folding with loose regulation. PMID:23334697 Xenobiotic perturbation of ER stress and the unfolded protein response. PMID:24469402 Deregulation of Pancreas-Specific Oxidoreductin ERO1β in the Pathogenesis of Diabetes Mellitus HOIP:HOIP_0000806 NCBI-Human-GeneID:2673 PMID:27255611 IRE1->Xbp1->GFPT1 reactome GFPT1 (human)[ER stress] HOIP_0000806 NCBI-Human-GeneID:2673 http://www.ncbi.nlm.nih.gov/gene/2673 HOIP:HOIP_0000807 This gene encodes a member of the gamma-glutamylcyclotransferase family of proteins. The encoded protein has been shown to promote neuronal differentiation by deglycination of the Notch receptor, which prevents receptor maturation and inhibits Notch signaling. This protein may also play a role in the unfolded protein response, and in regulation of glutathione levels and oxidative balance in the cell. Elevated expression of this gene may indicate increased risk of cancer recurrence among breast and ovarian cancer patients. [provided by RefSeq, Sep 2016] NCBI-Human-GeneID:79094 PMID:19109178 PMID:23070364 PMID:25931127 http://purl.obolibrary.org/obo/NCBIGene_79094 CHAC1 (human)[ER stress] HOIP_0000807 NCBI-Human-GeneID:79094 http://www.ncbi.nlm.nih.gov/gene/79094 PMID:19109178 CHAC1/MGC4504 is a novel proapoptotic component of the unfolded protein response, downstream of the ATF4-ATF3-CHOP cascade. Acts as a pro-apoptotic component of the unfolded protein response pathway by mediating the pro-apoptotic effects of the ATF4-ATF3-DDIT3/CHOP cascade. PMID:23070364 Mammalian proapoptotic factor ChaC1 and its homologues function as γ-glutamyl cyclotransferases acting specifically on glutathione. Glutathione depletion is an important factor for apoptosis initiation and execution ( PMID:25931127 Human CHAC1 Protein Degrades Glutathione, and mRNA Induction Is Regulated by the Transcription Factors ATF4 and ATF3 and a Bipartite ATF/CRE Regulatory Element. HOIP:HOIP_0000809 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). PMID:26006114 insulin resistance [non-alcoholic steatohepatitis (course)] HOIP_0000809 PMID:26006114 PMID:26006114 Insulin resistance alters hepatic ethanol metabolism: studies in mice and children with non-alcoholic fatty liver disease. HOIP:HOIP_0000810 NCBI-Human-GeneID:9709 PMID:16289116 HERPUD1 (human)[ER stress] HOIP_0000810 NCBI-Human-GeneID:9709 http://www.ncbi.nlm.nih.gov/gene/9709 HOIP:HOIP_0000812 ER stress dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of ER stress as a gene product. Gene profile:Mouse//Liver/ ER stress dependent moleule (mouse) HOIP_0000812 HOIP:HOIP_0000813 Tumor cell survial is a subtype of keeong quantity: A process that keeps the viability of a tumor cell. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. tumor cell survial [glutathione depletion (course)] HOIP_0000813 HOIP:HOIP_0000814 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. cell death [oxidative stress (course)] HOIP_0000814 HOIP:HOIP_0000815 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. Inflammatory response [oxidative stress (course)] HOIP_0000815 HOIP:HOIP_0000816 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. hepatic fibrosis HOIP_0000816 HOIP:HOIP_0000817 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of ER stress. hepatic fibrosis [ER stress] HOIP_0000817 HOIP:HOIP_0000820 Membrane protein production is a subtype of protein production: A process that makes existent of a membrane protein due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. membrane protein production HOIP_0000820 HOIP:HOIP_0000822 Decreasing amount of xenobiotics is a subtype of decreasing quantity: A process that changes the quantity of xenobiotics to be lower. decreasing amount of xenobiotics HOIP_0000822 HOIP:HOIP_0000823 A role of combining with a signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate. EC:2.7.10.1 transmembrane receptor tyrosine kinase related molecular function GO:0004714 transmembrane receptor protein tyrosine kinase HOIP_0000823 HOIP:HOIP_0000824 IRE - stress sensor (canonical)[ER stress -Refolding] HOIP_0000824 HOIP:HOIP_0000825 A physical attribute inhering in a bearer by virtue of the bearer's function. functional attribute HOIP_0000825 HOIP:HOIP_0000827 Negative regulation of phospholipase A2 mediated phospholipid degradation is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase A2 mediated phospholipid degradation. negative regulation of phospholipase A2 mediated phospholipid degradation HOIP_0000827 HOIP:HOIP_0000828 HSP90B1 - chaperone -vitro (human)[ER stress] HOIP_0000828 HOIP:HOIP_0000829 http://www.ncbi.nlm.nih.gov/gene/83939 phosphorylated eIF2A [ER stress] P-EIF2A (canonical)[ER stress] HOIP_0000829 HOIP:HOIP_0000830 IL-2 signaling is a process that a signal is transmitted by the cytokine IL-2. Reactomre:R-HSA-451927.2 IL-2 signaling HOIP_0000830 HOIP:HOIP_0000831 The multiplication or reproduction of cells, resulting in the rapid expansion of a cell population. This entity is a specific course-dependent process. This process can constitute the course of ER stress. cell proliferation [ER stress] HOIP_0000831 HOIP:HOIP_0000832 A role played by the entity which inhibits the process of cell death. cell death inhibitor HOIP_0000832 HOIP:HOIP_0000833 IL-2 signaling is a process that a signal is transmitted by the cytokine IL-2. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). PMID:28732506 Reactome:R-HSA-451927.2 IL-2 signaling [phospholipidosis (severe (excessive defense))] HOIP_0000833 PMID:9108028 PMID:28732506 Blimp-1 is also crucial for inducing cytokine production by inflammatory T helper cells and effector Treg cells. The gene encoding IL-2 is one of the most important genes targeted by Blimp-1 in T cells, because IL-2 production is indispensable for T cell proliferation and differentiation HOIP:HOIP_0000834 fatty acid http://purl.obolibrary.org/obo/CHEBI_35366 fatty acid HOIP_0000834 HOIP:HOIP_0000836 Tumor cell survial is a subtype of cell survival: A process that keeps the viability of a tumor cell. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). tumor cell survial [phospholipidosis (severe (excessive defense))] HOIP_0000836 HOIP:HOIP_0000838 Cell death dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the course of cell death. cell death dependent chemical entity HOIP_0000838 HOIP:HOIP_0000839 Cell death dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of cell death as a gene product. Gene profile:Rat/Liver/ cell death dependent molecule (rat) HOIP_0000839 HOIP:HOIP_0000840 Cell death dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of cell death as a gene product. Gene profile:Human/in vitro/Hepatocyte/ cell death dependent molecule (human in vitro) HOIP_0000840 HOIP:HOIP_0000841 Increasing liver weight is a subtype of increasing weight: A process that changes the weight of the liver to be higher. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). PMID:9742123 increasing liver weight [phospholipidosis (severe (excessive defense))] HOIP_0000841 PMID:9742123 Mol Cell Biol. 1998 Oct;18(10):6063-74. FGF-18, a novel member of the fibroblast growth factor family, stimulates hepatic and intestinal proliferation. FGF-18 is highly conserved between humans and mice and is most homologous to FGF-8 among the FGF family members. The two tissues which appeared to be the primary targets of FGF-18 were the liver and small intestine, both of which exhibited histologic evidence of proliferation and showed significant gains in organ weight following 7 (sometimes 3) days of FGF-18 treatment. Transgenic mice that overexpressed FGF-18 in the liver also exhibited an increase in liver weight and hepatocellular proliferation. These results suggest that FGF-18 is a pleiotropic growth factor that stimulates proliferation in a number of tissues, most notably the liver and small intestine. HOIP:HOIP_0000842 Inflammatory cytokine gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. inflammatory cytokine gene expression [oxidative stress (course)] HOIP_0000842 HOIP:HOIP_0000843 NCBI-Rat-GeneID:24842 TP53 (canonical) [cell death (course)] HOIP_0000843 NCBI-Rat-GeneID:24842 http://www.ncbi.nlm.nih.gov/gene/24842 HOIP:HOIP_0000844 Inflammasome activation is a subtype of activating: A process that changes the activity of the inflammasome, to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:29558368 inflammasome activation [glutathione depletion (course)] HOIP_0000844 PMID:29558368 HMGB1 promotes ductular reaction and tumorigenesis in autophagy-deficient livers:HMGB1 was released from autophagy-deficient hepatocytes independently of cellular injury but depended on NRF2 and the inflammasome, which was activated by NRF2. HOIP:HOIP_0000845 NCBI-Rat-GeneID:314856 MDM2 (canonical) [cell death (course)] HOIP_0000845 NCBI-Rat-GeneID:314856 http://www.ncbi.nlm.nih.gov/gene/314856 HOIP:HOIP_0000847 NCBI-Mouse-GeneID:15289 Hmgb1 (mouse)[glutathione depletion (course)] HOIP_0000847 NCBI-Mouse-GeneID:15289 http://www.ncbi.nlm.nih.gov/gene/15289 HOIP:HOIP_0000848 Increasing demand for glutathione conjugation is a subtype of increasing functional demand: A process changes the functional demand for the for glutathione conjugation to be higher. increasing demand for glutathione conjugation HOIP_0000848 HOIP:HOIP_0000850 NCBI-Human-GeneID:4780 NCBI-Mouse-GeneID:18024 NCBI-Rat-GeneID:83619 NRF2 -inflammasone activator (canonical)[glutathione depletion (course)] HOIP_0000850 NCBI-Human-GeneID:4780 http://www.ncbi.nlm.nih.gov/gene/4870 NCBI-Mouse-GeneID:18024 http://www.ncbi.nlm.nih.gov/gene/18024 NCBI-Rat-GeneID:83619 http://www.ncbi.nlm.nih.gov/gene/363735 HOIP:HOIP_0000851 A role played by the entity which positive regulates the inflammasone activity. inflammasome activator HOIP_0000851 HOIP:HOIP_0000852 Increasing ALT concentration in blood is a subtype of increasing concentration: A process that changes the alanine aminotransferase (ALT) concentration to be higher. http://purl.bioontology.org/ontology/MEDDRA/10001845 increasing blood GPT concentration increasing blood ALT concentration HOIP_0000852 HOIP:HOIP_0000853 NCBI-Rat-GeneID:24518 Jund (rat)[cell death (course)] HOIP_0000853 NCBI-Rat-GeneID:24518 http://www.ncbi.nlm.nih.gov/gene/24518 HOIP:HOIP_0000854 This entity is a role in which a process plays an essential role in the course of abnormal manifestation. core process (value) HOIP_0000854 HOIP:HOIP_0000855 NCBI-Human-GeneID:4780 NCBI-Rat-GeneID:83619 NRF2 -antioxidant (canonical)[glutathione depletion (course)] HOIP_0000855 NCBI-Human-GeneID:4780 http://www.ncbi.nlm.nih.gov/gene/4780 NCBI-Rat-GeneID:83619 http://www.ncbi.nlm.nih.gov/gene/83619 HOIP:HOIP_0000856 NCBI-Human-GeneID:2678 NCBI-Mouse-GeneID:14598 NCBI-Rat-GeneID:116568 gamma-glutamyltransferase 1 GGT1 (mol) HOIP_0000856 NCBI-Human-GeneID:2678 http://www.ncbi.nlm.nih.gov/gene/2678 NCBI-Mouse-GeneID:14598 http://www.ncbi.nlm.nih.gov/gene/14598 NCBI-Rat-GeneID:116568 http://www.ncbi.nlm.nih.gov/gene/116568 HOIP:HOIP_0000857 NCBI-Human-GeneID:2678 NCBI-Mouse-GeneID:14598 NCBI-Rat-GeneID:116568 gamma-glutamyltransferase 1 GGT1 (canonical)[lipidosis] HOIP_0000857 NCBI-Human-GeneID:2678 http://www.ncbi.nlm.nih.gov/gene/2678 NCBI-Mouse-GeneID:14598 http://www.ncbi.nlm.nih.gov/gene/14598 NCBI-Rat-GeneID:116568 http://www.ncbi.nlm.nih.gov/gene/116568 HOIP:HOIP_0000858 Catalysis of the reaction: (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl-amino acid. EC 2.3.2.2 gamma-GTP The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions gamma-glutamyltransferase. HOIP_0000858 HOIP:HOIP_0000859 Increasing γ-glutamyltransferase concentration in blood is a subtype of increasing concentration: A process that changes the γ-glutamyltransferase (GGT) concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). increasing γ-glutamyltransferase concentration in blood [non-alcoholic steatohepatitis (course)] HOIP_0000859 HOIP:HOIP_0000860 Increasing ALT concentration in blood is a subtype of increasing concentration: A process that changes the alanine aminotransferase (ALT) concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). http://purl.bioontology.org/ontology/MEDDRA/10001845 increasing blood GPT concentration [lipidosis] increasing blood ALT concentration [non-alcoholic steatohepatitis (course)] HOIP_0000860 HOIP:HOIP_0000861 Increasing AST concentration in blood is a subtype of increasing concentration: A process that changes the aspartate amino transferase (AST) concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). http://purl.bioontology.org/ontology/MEDDRA/10003544 inreasing blood GOT concentration [non-alcoholic steatohepatitis (course)] increasing blood AST concentration [non-alcoholic steatohepatitis (course)] HOIP_0000861 HOIP:HOIP_0000862 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). leaking content from cell [non-alcoholic steatohepatitis (course)] HOIP_0000862 HOIP:HOIP_0000863 A tumor necrosis factor that is encoded in the genome of human. NCBI-Human-GeneID:7124 TNF (human) [cell death (course)] HOIP_0000863 NCBI-Human-GeneID:7124 http://www.ncbi.nlm.nih.gov/gene/7124 HOIP:HOIP_0000864 NCBI-Human-GeneID:596 BCL2 (human) [cell death (course)] HOIP_0000864 NCBI-Human-GeneID:596 http://www.ncbi.nlm.nih.gov/gene/596 HOIP:HOIP_0000865 A concentration attribute inhering in a bearer by virtue of the bearer's exhibiting concentration. concentration (attribute) HOIP_0000865 HOIP:HOIP_0000866 NCBI-Human-GeneID:572 BAD (human) [cell death (course)] HOIP_0000866 NCBI-Human-GeneID:572 http://www.ncbi.nlm.nih.gov/gene/572 HOIP:HOIP_0000867 NCBI-Human-GeneID:356 FASLG (human) [cell death (course)] HOIP_0000867 NCBI-Human-GeneID:356 http://www.ncbi.nlm.nih.gov/gene/356 HOIP:HOIP_0000868 NCBI-Mouse-GeneID:217698 NCBI-Rat-GeneID:503049 Acot5 (mol) HOIP_0000868 NCBI-Mouse-GeneID:217698 http://www.ncbi.nlm.nih.gov/gene/217698 NCBI-Rat-GeneID:503049 http://www.ncbi.nlm.nih.gov/gene/503049 HOIP:HOIP_0000869 Malfunctioning of mitochondrial ATP synthesis coupled electron transferr is a subtype of malfunctioning process: A process that cannot perform a respiratory electron transport chain appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:21145849 PMID:23299992 PMID:25339807 PMID:31623280 PMID:31649547 mitochondrial respiratory chain abnormality [mitochondrial disorder (course)] HOIP_0000869 PMID:21145849 Table 1. PMID:23299992 Experimental investigations also pointed to a progressive reduction of MRC activity during NAFLD, which could impair energy output and aggravate ROS overproduction by the damaged MRC. It is likely that this event triggers a vicious cycle since mitochondrial ROS are able to oxidatively damage nearby MRC enzymes and mtDNA. Other mechanisms leading to impaired MRC activity could include higher levels of different lipid intermediates including free FAs, increased generation of lipid peroxidation products such as 4‐HNE, and reduced adiponectin action. Several MRC complexes including COX are sensitive to ROS and RNS. In addition, COX can be inhibited by low levels of NO and inactivated by 4‐hydroxynonenal (4‐HNE), a reactive aldehyde generated during lipid peroxidation. Some lipid derivatives such as FAs can directly inhibit several enzymes involved in MRC and OXPHOS. PMID:25339807 iNOS induction is linked to alterations in the NO-dependent control of mitochondrial respiration (at the level of cytochrome c oxidase), which potentially contributes to the development of alcoholic steatohepatitis. Thus, the CL-dependent alterations of the ETC organization in supercomplexes could be another factor contributing to ROS generation and to mitochondrial bioenergetic decay in NAFLD. Another consequence of cytochrome c release from mitochondria is that it interferes with electron transport through ETC, resulting in ROS formation and triggering a new vicious cycle, which will worsen the disturbance. PMID:31623280 Bellanti et al. showed through targeted lipidomic analysis that rats fed diets rich in cholesterol exhibited increased toxic hepatic triol, which induces apoptosis and impaired mitochondrial respiration in vitro. PMID:31649547 Recent study has found that hepatic fatty acid accumulation can cause damaged mitochondria accumulation, which can impair mitochondrial respiratory chain function and fatty acid oxidative degradation. HOIP:HOIP_0000871 ER stress dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of ER stress as a gene product. Gene profile:caonical that described in textbooks or articles. ER stress dependent molecule (canonical) HOIP_0000871 HOIP:HOIP_0000872 Dissociation of Bip complex is a subtype of detaching: A process that disaggregates a Bip complex into Bip and other molecule(s). dissociation of BIP complex HOIP_0000872 HOIP:HOIP_0000873 NCBI-Human-GeneID:5562 NCBI-Mouse-GeneID:105787 NCBI-Rat-GeneID:65248 AMPK (canonical)[ER stress] HOIP_0000873 NCBI-Human-GeneID:5562 http://www.ncbi.nlm.nih.gov/gene/5562 NCBI-Mouse-GeneID:105787 http://www.ncbi.nlm.nih.gov/gene/105787 NCBI-Rat-GeneID:65248 http://www.ncbi.nlm.nih.gov/gene/65248 HOIP:HOIP_0000874 Negative regulation of endoplasmic reticulum-associated degradation is a subtype of negative regulation of protein catabolic process: A process that stops, prevents, or reduces the frequency, rate or extent of endoplasmic reticulum-associated degradation. negative regulation of endoplasmic reticulum-associated degradation HOIP_0000874 HOIP:HOIP_0000875 IRE - stress sensor (canonical)[ER stress -ERAD] HOIP_0000875 HOIP:HOIP_0000876 A role played by the entity which interferes with the activity of PERK. PERK inhibitor HOIP_0000876 HOIP:HOIP_0000877 NCBI-Human-GeneID:9817 NCBI-Mouse-GeneID:50868 NCBI-Rat-GeneID:117519 Kelch Like ECH Associated Protein 1 KEAP1 (mol) HOIP_0000877 NCBI-Human-GeneID:9817 http://www.ncbi.nlm.nih.gov/gene/9817 NCBI-Mouse-GeneID:50868 http://www.ncbi.nlm.nih.gov/gene/50868 NCBI-Rat-GeneID:117519 http://www.ncbi.nlm.nih.gov/gene/117519 HOIP:HOIP_0000878 NCBI-Human-GeneID:9451 NCBI-Mouse-GeneID:13666 NCBI-Rat-GeneID:29702 http://omim.org/entry/604032 EIF2AK3 PERK (canonical)[ER stress] HOIP_0000878 NCBI-Human-GeneID:9451 http://www.ncbi.nlm.nih.gov/gene/9451 NCBI-Mouse-GeneID:13666 http://www.ncbi.nlm.nih.gov/gene/13666 NCBI-Rat-GeneID:29702 http://www.ncbi.nlm.nih.gov/gene/29702 HOIP:HOIP_0000879 NCBI-Human-GeneID:22926 NCBI-Mouse-GeneID:226641 NCBI-Rat-GeneID:304962 ATF6 (canonical)[ER stress] HOIP_0000879 NCBI-Human-GeneID:22926 http://www.ncbi.nlm.nih.gov/gene/22926 NCBI-Mouse-GeneID:226641 http://www.ncbi.nlm.nih.gov/gene/226641 NCBI-Rat-GeneID:304962 http://www.ncbi.nlm.nih.gov/gene/304962 HOIP:HOIP_0000880 ISBN:0071769234 amiodarone [Lipidosis] HOIP_0000880 ISBN:0071769234 Drug-induced steatosis is mainly caused by compounds such as amiodarone, tamoxifen, which accumulate in mitochondria and inhibit β-oxidation and mitochondrial respiration. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0000881 A role played by the entity which receives some stress and transmits operand(s). stress sensor HOIP_0000881 HOIP:HOIP_0000882 A role played by the entity which receives a stimulus and transmits operand(s). sensor HOIP_0000882 HOIP:HOIP_0000884 Hyperfunction of dead cell phagocytosis by Kupffer cells is a subtype of hyperfunctioning: A process that performs phagocytosis of dead cells by Kupffer cells or macrophages execessively. hyperfunction of dead cell phagocytosis by Kupffer cells (macrophages) HOIP_0000884 HOIP:HOIP_0000885 A role of the entity which carries substances between the nucleus and the cytoplasm of a cell by moving along with the target protein. IMR:0000653 (obsolete) relatd molecular function GO:0140142 nucleocytoplasmic carrier HOIP_0000885 HOIP:HOIP_0000886 ER process HOIP_0000886 HOIP:HOIP_0000887 Gene expression regulation system is a subtype of pathway system. This entity has sub-parts and has a goal of regulating gene expressions as a systemic context. gene expression regulation system HOIP_0000887 HOIP:HOIP_0000888 Lipidosis (course) is a subtype of process sequences: The courses of processes through which lipidosis is realized via lipid homeostasis imbalance. ISBN:0071769234 PMID:10962028 PMID:15254578 PMID:21145849 PMID:23262638 PMID:24954301 fatty liver (imbalance course) lipidosis (imbalance course) HOIP_0000888 ISBN:0071769234 Fatty liver (steatosis) is defined biochemically as an appreciable increase in the hepatic lipid (mainly triglyceride) content, which is <5 wt% in the normal human liver. HOIP:HOIP_0000889 Glutathione depletion dependent process is a subtype of course dependent process: A process that can constitute the course of glutathione depletion . glutathione depletion dependent process HOIP_0000889 HOIP:HOIP_0000890 Hyperfunction of fatty acid biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive fatty acid biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). hyperfunction of fatty acid biosynthesis [lipidosis (imbalance course)] HOIP_0000890 HOIP:HOIP_0000891 Hypofunction of lipid degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient lipid degradation. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). hypofunction of lipid degradation [lipidosis (imbalance course)] HOIP_0000891 HOIP:HOIP_0000892 Increaing in fatty acid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the fatty acid inflow into the hepatocyte to be larger. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). increaing in fatty acid inflow into hepatocyte [lipidosis (imbalance course)] HOIP_0000892 HOIP:HOIP_0000893 Lipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of lipid metabolism. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course)]. lipid metabolism imbalance [lipidosis (imbalance course)]] HOIP_0000893 HOIP:HOIP_0000895 A sheet or layer to separate or connect between biological structures. Wikipedia:Biological_membrane biological membrane HOIP_0000895 HOIP:HOIP_0000896 Deacreasing flow velocity is a subtype of changing flow: A process that changes the velocity of the object to be slower. Deacreasing flow rate HOIP_0000896 HOIP:HOIP_0000897 Lipid storage in liver is a subtype of lipid storage: The accumulation and maintenance in cells or tissues of lipids in the liver. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). ISBN:0071769234 lipid storage in liver [non-alcoholic steatohepatitis (course)] HOIP_0000897 ISBN:0071769234 Fatty liver (steatosis) is defined biochemically as an appreciable increase in the hepatic lipid (mainly triglyceride) content, which is <5 wt% in the normal human liver. HOIP:HOIP_0000898 Hyperfunction of lipid biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive lipid biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). hyperfunction of lipid biosynthesis [lipidosis (imbalance course)] HOIP_0000898 HOIP:HOIP_0000899 Hyperfunction of lipid synthetic gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive lipid biosynthetic gene expression. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). hyperfunction of lipid synthetic gene expression [lipidosis (imbalance course)] HOIP_0000899 HOIP:HOIP_0000901 Hypofunction of mitochondrial fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient fatty acid beta-oxidation. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). hypofunction of mitochondrial fatty acid beta-oxidation [lipidosis (imbalance course)] HOIP_0000901 HOIP:HOIP_0000903 Increasing phospholipid inflow (severe) is a subtype of increase in phospholipid inflow: A process that changes the phospholipid inflow into the hepatocyte to be larger. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). increasing phospholipid inflow (severe) [phospholipidosis (severe)] HOIP_0000903 HOIP:HOIP_0000904 NRF2 signaling is a subtype of signaling that a signal is transmitted by the NRF2. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. NRF2 signaling [glutathione depletion (course)] HOIP_0000904 HOIP:HOIP_0000905 Negative regulation of phospholipid degradation is a subtype of negative regulation of decomposing: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid degradation. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). negative regulation of phospholipid degradation [phospholipidosis (imbalance course)] HOIP_0000905 HOIP:HOIP_0000906 IRE - stress sensor (canonical)[ER stress - apotosis] HOIP_0000906 HOIP:HOIP_0000907 Phospholipid homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. phospholipid homeostasis imbalance [phospholipidosis (imbalance course)] HOIP_0000907 HOIP:HOIP_0000908 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of phospholipids. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). hyperfunction of phospholipid biosynthesis [phospholipidosis (imbalance course)] HOIP_0000908 HOIP:HOIP_0000909 Increasing demand for phospholipid degradation is a subtype of increasing functional demand: A process that changes the functional demand for the phospholipid degradation to be higher. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. increasing demand for phospholipid degradation [phospholipidosis (imbalance course)] HOIP_0000909 HOIP:HOIP_0000910 Phospholipid accumulation in lysosome is a subtype of phospholipid accumulation: A process that keeps phospholipid in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). phospholipid accumulation in lysosome [phospholipidosis (imbalance course)] HOIP_0000910 HOIP:HOIP_0000911 Hypofunction of phospholipase transport to lysosome is a subtype of hypofunction of phospholipase transport to lysosome : A process that performs a decreased or insufficient phospholipase transport to lysosome severely. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). hypofunction of phospholipase transport to lysosome [phospholipidosis (severe)] HOIP_0000911 HOIP:HOIP_0000912 Increasing lysosomal pH is a subtype of changing pH: A process that changes the pH in lysosome to be higher. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis(severe). PMID:1697167 increasing lysosomal pH [Phospholipidosis(severe)] HOIP_0000912 Lysosomal Re-acidification Prevents Lysosphingolipid-Induced Lysosomal Impairment and Cellular Toxicity. PMID:27977664 HOIP:HOIP_0000913 Forming a complex of drugs and biological substance is a subtype of protein complex assembly: The aggregation, arrangement and bonding together between drugs and biological molecules to form a complex. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). forming a complex of CAD and phospholipid [phospholipidosis (mild)] HOIP_0000913 HOIP:HOIP_0000914 Hypofunction of phospholipid deradation by phospholipase is a subtype of hypofunction of phospholipid degradation: A process that performs a decreased or insufficient phospholipid deradation by phospholipase. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. hypofunction of phospholipid deradation by phospholipase [phospholipidosis (imbalance course)] HOIP_0000914 HOIP:HOIP_0000915 Hyperfunction of phospholipid synthesis gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive phospholipid synthetic gene expression. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. hyperfunction of phospholipid synthesis gene expression [phospholipidosis (imbalance course)] HOIP_0000915 HOIP:HOIP_0000916 Hyperfunction of accumulation is a subtype of hyperfunctioning: A process that performs accumulating excessively. hyperfunction of accumulation HOIP_0000916 HOIP:HOIP_0000919 Lipid homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a lipid homeostastasis balance. The degree is mild. This entity is a specific course-dependent process. This process can constitute the course of simple steatosis. lipid homeostasis imbalance (mild) [simple steatosis] HOIP_0000919 HOIP:HOIP_0000920 Phospholipid accumulation in lysosome is a subtype of phospholipid accumulation: A process that keeps phospholipid in the lysosome. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). phospholipid accumulation in lysosome [phospholipidosis (severe)] HOIP_0000920 HOIP:HOIP_0000921 Increasing hepatocellular volume is a changing process to change the volume of the hepatocyte to increase. This entity is a specific course-dependent process. This process can constitute the course of [phospholipidosis (severe (excessive defense)). increasing hepatocellular volume [phospholipidosis (severe (excessive defense))] HOIP_0000921 HOIP:HOIP_0000922 Mild accumulation of abnormal proteins in ER is a subtype of accumulation of abnormal proteins in ER: A process that keeps abnormal protein(s) in the ER (endoplasmic reticulum) mildly. mild accumulation of abnormal proteins in ER HOIP_0000922 HOIP:HOIP_0000923 Increasing phospholipid is a subtype of increasing quantity: A process that changes the amount of phospholipid to be larger. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). increasing phospholipid [phospholipidosis (imbalance course)] HOIP_0000923 HOIP:HOIP_0000925 Hypofunction of phospholipid degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient phospholipid degradation. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). hypofunction of phospholipid degradation [phospholipidosis (imbalance course)] HOIP_0000925 HOIP:HOIP_0000926 A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). phagocytosis [phospholipidosis (normal course)] HOIP_0000926 HOIP:HOIP_0000927 Any biological process that results in permanent cessation of all vital functions of a cell. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). cell death [phospholipidosis (severe)] HOIP_0000927 HOIP:HOIP_0000928 Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)) . PMID:17090686 positive regulation of apoptotic process [phospholipidosis (severe (excessive defense))] HOIP_0000928 PMID:15720040 PMID:17090686 PMID:17090686 Sphingosine-1-phosphate lyase potentiates apoptosis via p53- and p38-dependent pathways and is down-regulated in colon cancer. HOIP:HOIP_0000929 A process that becomes lacking a homeostastasis balance of the sphingomyelin metabolism in the nervous system. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. sphingomyelin metabolism imbalance in nervous system [course of Niemann–Pick disease type A] HOIP_0000929 HOIP:HOIP_0000930 Compound accumulation in lysosome is a subtype of accumulation of xenobiotics: A process that keeps compound in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. compound accumulation in lysosome [phospholipidosis (imbalance course)] HOIP_0000930 HOIP:HOIP_0000932 The directed movement of carbohydrate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Carbohydrates are any of a group of organic compounds based of the general formula Cx(H2O)y. This entity is a specific course-dependent process. This process can constitute the course of Ground glass appearance. carbohydrate transport [Ground glass appearance] HOIP_0000932 HOIP:HOIP_0000933 Mitochondrial dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete mitochondrial function. This entity is a specific course-dependent process. This process can constitute the Mitochondrial disorder. PMID:23299992 PMID:25339807 PMID:29222479 PMID:30250064 PMID:31623280 mitochondrial dysfunction [mitochondrial disorder (course)] HOIP_0000933 PMID:23299992 Furthermore, high glucose levels promote ROS overproduction within hepatocytes, thus favoring oxidative stress and mitochondrial dysfunction. NAFLD has been associated with higher hepatic expression of the inducible nitric oxide (NO) synthase (iNOS), mainly as a consequence of tumor necrosis factor‐α (TNF‐α) overproduction by the Kupffer cells. NO can readily react with the superoxide anion, thus generating the RNS peroxynitrite, which has deleterious effects on mitochondrial function and genome. PMID:25339807 In liver cells, mitochondrial dysfunction plays a critical role by amplifying the apoptotic signal and integrating both pathways into a final common pathway. Mitochondrial dysfunction results in the release of several proapoptotic proteins into the cytosol, including cytochrome c. PMID:29222479 Hepatocytes display an eosinophilic cytoplasm upon hematoxylin-eosin staining, reflecting abundant mitochondria. Thus, it is not surprising that mitochondrial dysfunction promotes cellular damage and is linked to liver diseases. PMID:30250064 not reported in the liver. Strikingly, NEAT1-depleted single cell clones showed a consistent reduction in mitochondrial DNA (mtDNA) (Fig. 7a), reduced mitochondrial respiration (by detection of the oxygen consumption rate (OCR); Fig. 7b) and adenosine triphosphate (ATP) production (Fig. 7c), reduced OCR and extracellular acidification rate (ECAR) rate (Fig. 7d), suggesting that the aberrant NEAT1 expression could cause mitochondrial dysfunction. PMID:31623280 Emerging evidence suggests that mitochondrial dysfunction or maladaptation contributes to detrimental effects on hepatocyte bioenergetics, reactive oxygen species (ROS) homeostasis, endoplasmic reticulum (ER) stress, inflammation, and cell death leading to NASH and HCC. Just like in NASH, oxidative stress, mitochondrial dysfunction, and oxidized mtDNA also contribute to the progression of HCC through influences on inflammation, cell death, and ER stress. Moreover, in vitro treatment of liver cells with saturated fatty acids (palmitic and stearic acids) reproduces mitochondrial dysfunction found in NASH, including decreasing cellular ATP content and mtDNA-encoded oxidative phosphorylation (OXPHOS) subunit expression, coupled with increased oxidative stress. Among these, mitochondrial dysfunction is linked to cancer progression through increased ROS production, impaired mitochondrial respiration, ER stress, and alteration of nutrient metabolism. HOIP:HOIP_0000939 Hyperfunction of iron supply is a subtype of hyperfunctioning: A process that performs an excesssive iorn supply. This entity is a specific course-dependent process. This process can constitute the course of Ground glass appearance. hyperfunction of iron supply [Ground glass appearance] HOIP_0000939 HOIP:HOIP_0000940 Hypofunction of decomposing is a subtype of hypofunctioning: A process that performs a decreased or insufficient decomposing. hypofunction of decomposing HOIP_0000940 HOIP:HOIP_0000946 Changing balance of phospholipid metabolism is a subtype of changing balance: A process that changes the balance between phospholipid anabolism and catabolism. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. changing balance of phospholipid metabolism [phospholipidosis (course)] HOIP_0000946 HOIP:HOIP_0000949 This process is totality of all processes through which the phospholipidosis is realized caused by obesity. The severity is moderate. phospholipidosis via obese HOIP_0000949 HOIP:HOIP_0000950 Overeating is a subtype of increasing quantity: A process that changes the ingestion amount of food to be larger. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. overeating [phospholipidosis via obese] HOIP_0000950 HOIP:HOIP_0000951 Changing phospholipid homeostasis is a subtype of changing balance: A process that changes the steady state of phospholipid within an organism or cell. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. changing phospholipid homeostasis [phospholipidosis (course)] HOIP_0000951 HOIP:HOIP_0000957 Changing phospholipid homeostasis is a subtype of changing balance: A process that changes the steady state of phospholipid within an organism or cell. changing phospholipid homeostasis HOIP_0000957 HOIP:HOIP_0000960 Carbohydrate storage is a subtype of accumulation of substances in a biological object: The accumulation and maintenance in cells or tissues of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. carbohydrate storage HOIP_0000960 HOIP:HOIP_0000968 Making existence of foreign substance is a subtype of making existence: A process that puts froreign substances with an object. making existence of foreign substance HOIP_0000968 HOIP:HOIP_0000974 A ketoimine that has formula C8H7NO2. PMID:10741631 PMID:21177773 http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-76397 N-(4-oxocyclohexa-2,5-dien-1-ylidene)acetamide [glutathione depletion (course)] N-acetyl-1,4-benzoquinone imine [glutathione depletion (course)] CHEBI:29132 NAPQI [glutathione depletion (course)] HOIP_0000974 HOIP:HOIP_0000987 Dioxins and dioxin-like compounds accumulation in liver is a subtype of compound accumulation in liver: A process that keeps dioxins and dioxin-like compoundsin the liver. This entity is a specific course-dependent process. This process can constitute the course of Ground glass appearance. dioxins and dioxin-like compounds accumulation in liver [Ground glass appearance] HOIP_0000987 HOIP:HOIP_0000993 insulin receptor signaling pathway is a subtype of integrated signaling pathway: The series of molecular signals generated as a consequence of the insulin receptor binding to insulin. This entity is a specific course-dependent process. This process can constitute the course of ER stress. insulin receptor signaling pathway [ER stress] HOIP_0000993 HOIP:HOIP_0001002 NCBI-Human-GeneID:3309 NCBI-Mouse-GeneID:14828 NCBI-Rat-GeneID:25617 GRP78 HSPA5 BIP (mol) HOIP_0001002 NCBI-Human-GeneID:3309 http://www.ncbi.nlm.nih.gov/gene/3309 NCBI-Mouse-GeneID:14828 http://www.ncbi.nlm.nih.gov/gene/14828 NCBI-Rat-GeneID:25617 http://www.ncbi.nlm.nih.gov/gene/25617 HOIP:HOIP_0001007 Damage Specific DNA Binding Protein 2 NCBI-Human-GeneID:1643 NCBI-Mouse-GeneID:107986 NCBI-Rat-GeneID:100362121 OMIM: 600811 DDB2 (mol) HOIP_0001007 NCBI-Human-GeneID:1643 http://www.ncbi.nlm.nih.gov/gene/1643 NCBI-Mouse-GeneID:107986 http://www.ncbi.nlm.nih.gov/gene/107986 NCBI-Rat-GeneID:100362121 http://www.ncbi.nlm.nih.gov/gene/100362121 HOIP:HOIP_0001017 A protein that is a translation product of the human GOT1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:2805 NCBI-Mouse-GeneID:14718 NCBI-Rat-GeneID:24401 AST1 [lipidosis] glutamic-oxaloacetic transaminase 1 GOT1 (canonical)[lipidosis] HOIP_0001017 NCBI-Human-GeneID:2805 http://www.ncbi.nlm.nih.gov/gene/2805 NCBI-Mouse-GeneID:14718 http://www.ncbi.nlm.nih.gov/gene/14718 NCBI-Rat-GeneID:24401 http://www.ncbi.nlm.nih.gov/gene/24401 HOIP:HOIP_0001020 AT-Rich Interaction Domain 5A NCBI-Human-GeneID:10865 NCBI-Mouse-GeneID:214855 NCBI-Rat-GeneID:316327 OMIM: 611583 PMID:15941852 PMID:29358370 MRF1 ARID5A [Ground glass appearance] HOIP_0001020 NCBI-Human-GeneID:10865 http://www.ncbi.nlm.nih.gov/gene/10865 NCBI-Mouse-GeneID:214855 http://www.ncbi.nlm.nih.gov/gene/214855 NCBI-Rat-GeneID:316327 http://www.ncbi.nlm.nih.gov/gene/316327 PMID:15941852 Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha. PMID:29358370 Regulation of inflammatory responses by dynamic subcellular localization of RNA-binding protein Arid5a. HOIP:HOIP_0001021 An enzyme that catalyzes L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate Wikipedia:Aspartate_transaminase EC 2.6.1.1 aspartate transaminase HOIP_0001021 HOIP:HOIP_0001024 A protein that is a translation product of the GPT gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:2875 NCBI-Mouse-GeneID:76282 NCBI-Rat-GeneID:81670 ALT1 GPT1 glutamic--pyruvic transaminase GPT (canonical)[lipidosis] HOIP_0001024 NCBI-Human-GeneID:2875 http://www.ncbi.nlm.nih.gov/gene/2875 NCBI-Mouse-GeneID:76282 http://www.ncbi.nlm.nih.gov/gene/76282 NCBI-Rat-GeneID:81670 http://www.ncbi.nlm.nih.gov/gene/81670 HOIP:HOIP_0001027 An enzyme that catalyzes L-alanine + 2-oxoglutarate = pyruvate + L-glutamate EC 2.6.1.2 Glutamic Pyruvic Transaminase Alanine transaminase HOIP_0001027 HOIP:HOIP_0001029 Increasing demand for response to mitochondrial oxidative stress is a subtype of increasing the demand for response to oxidative stress: A process that changes the functional demand for the response to the mitochondrial oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:23299992 PMID:29335519 increasing demand for response to mitochondrial oxidative stress [mitochondrial disorder (course)] HOIP_0001029 PMID:23299992 Furthermore, enhanced mtFAO without concomitant up‐regulation of the mitochondrial respiratory chain (MRC) activity induces reactive oxygen species (ROS) overproduction within different MRC components upstream of cytochrome c oxidase. This event seems to play a significant role in the initiation of oxidative stress and subsequent development of nonalcoholic steatohepatitis (NASH) in some individuals. Furthermore, high glucose levels promote ROS overproduction within hepatocytes, thus favoring oxidative stress and mitochondrial dysfunction. PMID:29335519 Metabolic reprogramming by PCK1 promotes TCA cataplerosis, oxidative stress and apoptosis in liver cancer cells and suppresses hepatocellular carcinoma. HOIP:HOIP_0001036 Hypofunction of fatty acid degradation is a subtype of hypofunctioning: A process that performs a decreased or insufficient lipid degradation. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). hypofunction of fatty acid degradation [lipidosis (imbalance course) ] HOIP_0001036 HOIP:HOIP_0001038 Lipid homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a lipid homeostastasis balance. This entity is a specific course-dependent process. The degree is severe. This process can constitute the course of non-alcoholic steatohepatitis (course). lipid homeostasis imbalance (severe) [non-alcoholic steatohepatitis (course)] HOIP_0001038 HOIP:HOIP_0001039 Lipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of lipid metabolism. The degree is mild. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis. lipid metabolism imbalance (mild) [simple steatosis] HOIP_0001039 HOIP:HOIP_0001041 The totality of all processes through which alcoholic fatty liver is realized. PMID:17854140 under construction alcoholic fatty liver HOIP_0001041 HOIP:HOIP_0001044 Lipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of lipid metabolism. The degree is severe. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis. lipid metabolism imbalance (severe) [non-alcoholic steatohepatitis (course)] HOIP_0001044 HOIP:HOIP_0001049 Moving free fatty acid to the hepatocyte is a subtype of moving A to the inside of B: A process of the movement of free fatty acid into a hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). moving fatty acid to the hepatocyte [lipidosis (normal course)] HOIP_0001049 HOIP:HOIP_0001054 Catalysis role of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein. related molecular function GO:0004715 non-membrane spanning protein tyrosine kinase HOIP_0001054 HOIP:HOIP_0001056 Decreasing lipid is a subtype of decreasing quantity: A process that changes the quantity of the lipid to be lower. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course) decreasing lipid [llipidosis (normal course)] HOIP_0001056 HOIP:HOIP_0001059 Increasing lipid is a subtype of increasing quantity: A process that changes the amount of lipid to be larger. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). increasing lipid [lipidosis (normal course)] HOIP_0001059 HOIP:HOIP_0001062 Increasing lipid is a subtype of increasing quantity: A process that changes the amount of lipid to be larger. increasing lipid HOIP_0001062 HOIP:HOIP_0001063 IL-1beta processing is a subtype of protein processing: A process that IL-1beta maturation process achieved by the cleavage of pro IL-1beta. IL-1beta processing HOIP_0001063 HOIP:HOIP_0001065 IL-1beta processing is a subtype of protein processing: A process that IL-1beta maturation process achieved by the cleavage of pro IL-1beta. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). IL-1beta processing [non-alcoholic steatohepatitis (course)] HOIP_0001065 HOIP:HOIP_0001075 Increasing lipid material is a subtype of increasing quantity: A process that changes the amount of lipid material to be larger. increasing lipid material HOIP_0001075 HOIP:HOIP_0001078 Increasing lipid material is a subtype of increasing quantity: A process that changes the amount of lipid material to be larger. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis (normal condition). increasing lipid material [lipidosis] HOIP_0001078 HOIP:HOIP_0001079 NCBI-Human-GeneID:834 PMID:20303873 CASP1 -IL1beta activator (canonical)[lipidosis] HOIP_0001079 NCBI-Human-GeneID:834 http://www.ncbi.nlm.nih.gov/gene/834 HOIP:HOIP_0001080 A role played by the entity that activates the activity of the cytokine IL-1b. IL-1b activator role HOIP_0001080 HOIP:HOIP_0001082 A role played by the entity which regulates the cellular senescence. cellular senescence regulator HOIP_0001082 HOIP:HOIP_0001083 Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). positive regulation of mitochondrial membrane permeability [non-alcoholic steatohepatitis (course)] HOIP_0001083 HOIP:HOIP_0001085 Decreasing mitochondrial membrane potential is a subtype of decreasing membrane potential: A process that changes the electrical potential of a mitochondrial membrane to be lower. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). decreasing mitochondrial membrane potential [non-alcoholic steatohepatitis (course)] HOIP_0001085 HOIP:HOIP_0001086 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). reactive oxygen species biosynthetic process [non-alcoholic steatohepatitis (course)] HOIP_0001086 HOIP:HOIP_0001088 Lipidosis dependent molecule is a subtype of course dependent chemical entity. This molecule can participate in the course of lipidosis as a gene product. Gene profile:Rat/Liver/ lipidosis dependent molecule (rat) HOIP_0001088 HOIP:HOIP_0001089 Lipidosis dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the course of lipidosis. lipidosis dependent chemical entity HOIP_0001089 HOIP:HOIP_0001090 Lipidosis dependent molecule is a subtype of course dependent chemical entity. This molecule can participate in the course of lipidosis as a gene product. Gene profile:Human/in vitro/Hepatocyte/ lipidosis dependent molecule (human in vitro) HOIP_0001090 HOIP:HOIP_0001091 This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. NCBI-Human-GeneID:125 PMID:26006114 PMID:29063269 PMID:29718361 ADH1B (human)[lipidosis] HOIP_0001091 This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. http://www.ncbi.nlm.nih.gov/gene/211 NCBI-Human-GeneID:125 http://www.ncbi.nlm.nih.gov/gene/125 PMID:29718361 The protein levels of ADH1A, ADH1B, and ADH4 were each decreased in the NASH groups, which was consistent with a decreased overall ADH activity. The protein level of ALDH2 was significantly increased in both NASH groups, while ALDH1A1 and ALDH1B1 were only decreased in NASH (fatty) samples. ALDH activity represented by oxidation of acetaldehyde was decreased in the NASH (fatty) group. HOIP:HOIP_0001092 NCBI-Human-GeneID:125 ADH1B (mol) HOIP_0001092 NCBI-Human-GeneID:125 https://www.ncbi.nlm.nih.gov/gene/125 HOIP:HOIP_0001093 NCBI-Human-GeneID:637 NCBI-Mouse-GeneID:12122 NCBI-Rat-GeneID:64625 BID (human)[Lipidosis] HOIP_0001093 NCBI-Human-GeneID:637 http://www.ncbi.nlm.nih.gov/gene/637 NCBI-Mouse-GeneID:12122 http://www.ncbi.nlm.nih.gov/gene/12122 NCBI-Rat-GeneID:64625 http://www.ncbi.nlm.nih.gov/gene/64625 HOIP:HOIP_0001094 EC 1.1.1.1 Alcohol dehydrogenase family alcohol dehydrogenase (NAD) ADH family HOIP_0001094 HOIP:HOIP_0001095 Hypofunction of alcohol metabolism is a subtype of hyperfunctioning: A process that performs a decreased or insufficient alcohol metabolism. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis. PMID:29718361 hyporfunction of alcohol metabolism [non-alcoholic steatohepatitis (course)] HOIP_0001095 PMID:29718361 The protein levels of ADH1A, ADH1B, and ADH4 were each decreased in the NASH groups, which was consistent with a decreased overall ADH activity. HOIP:HOIP_0001096 Hypofunction of alcohol metabolism is a subtype of hyperfunctioning: A process that performs a decreased or insufficient alcohol metabolism. hypofunction of alcohol metabolism HOIP_0001096 HOIP:HOIP_0001097 NCBI-Human-GeneID:572 NCBI-Mouse-GeneID:12015 NCBI-Rat-GeneID:64639 BAD (human)[Lipidosis] HOIP_0001097 NCBI-Human-GeneID:572 http://www.ncbi.nlm.nih.gov/gene/572 NCBI-Mouse-GeneID:12015 http://www.ncbi.nlm.nih.gov/gene/12015 NCBI-Rat-GeneID:64639 http://www.ncbi.nlm.nih.gov/gene/64639 HOIP:HOIP_0001098 NCBI-Human-GeneID:5021 NCBI-Mouse-GeneID:18430 NCBI-Rat-GeneID:25342 OXTR (mol) HOIP_0001098 NCBI-Human-GeneID:5021 https://www.ncbi.nlm.nih.gov/gene/5021 NCBI-Mouse-GeneID:18430 https://www.ncbi.nlm.nih.gov/gene/18430 NCBI-Rat-GeneID:25342 https://www.ncbi.nlm.nih.gov/gene/25342 HOIP:HOIP_0001101 Increasing free fatty acid is a subtype of increasing quantity: A process that changes the amount of free fatty acid to be larger. increasing free fatty acid HOIP_0001101 HOIP:HOIP_0001103 NCBI-Human-GeneID:7392 NCBI-Mouse-GeneID:22282 NCBI-Rat-GeneID:81817 USF2 (human)[Lipidosis] HOIP_0001103 NCBI-Human-GeneID:7392 http://www.ncbi.nlm.nih.gov/gene/7392 NCBI-Mouse-GeneID:22282 http://www.ncbi.nlm.nih.gov/gene/22282 NCBI-Rat-GeneID:81817 http://www.ncbi.nlm.nih.gov/gene/81817 HOIP:HOIP_0001104 NCBI-Human-GeneID:834 PMID:20303873 CASP1 (canonical)[lipidosis] HOIP_0001104 NCBI-Human-GeneID:834 http://www.ncbi.nlm.nih.gov/gene/834 HOIP:HOIP_0001105 Lipidosis dependent molecule is a subtype of course dependent chemical entity. This molecule can participate in the course of lipidosis as a gene product. Gene profile:Mouse/Liver/ Lipidosis dependent molecule (mouse) HOIP_0001105 HOIP:HOIP_0001106 NCBI-Human-GeneID:129607 NCBI-Mouse-GeneID:22169 NCBI-Rat-GeneID:314004 CMPK2 (mol) HOIP_0001106 NCBI-Human-GeneID:129607 https://www.ncbi.nlm.nih.gov/gene/129607 NCBI-Mouse-GeneID:22169 https://www.ncbi.nlm.nih.gov/gene/22169 NCBI-Rat-GeneID:314004 https://www.ncbi.nlm.nih.gov/gene/314004 HOIP:HOIP_0001107 Inflammasome activation is a subtype of activating: A process that changes the activity of the inflammasome to be higher. inflammasome activation HOIP_0001107 HOIP:HOIP_0001108 A protein that is a translation product of the human USF1 gene or a 1:1 ortholog thereof. PMID:19303849 PMID:20817607 PMID:7499393 PMID:9334210 PMID:9890958 USF1 (canonical)[lipidosis] HOIP_0001108 PMID:7499393 Upstream stimulatory factors bind to insulin response sequence of the fatty acid synthase promoter. USF1 is regulated. PMID:9334210 Upstream stimulatory factor binding to the E-box at -65 is required for insulin regulation of the fatty acid synthase promoter. PMID:9890958 Essential role in vivo of upstream stimulatory factors for a normal dietary response of the fatty acid synthase gene in the liver. HOIP:HOIP_0001109 PMID:20817607 insulin(canonical)[lipidosis] HOIP_0001109 HOIP:HOIP_0001111 A protein family that is a translation product of the human USF gene or a 1:1 ortholog thereof. upstream transcription factor USF (mol) HOIP_0001111 HOIP:HOIP_0001112 USF1 activation is a subtype of molecular activation: A process that changes the activity of the USF1 to be higher. USF1 activation HOIP_0001112 HOIP:HOIP_0001113 USF1 activation is a subtype of molecular activation: A process that changes the activity of the USF1 to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:7499393 USF1 activation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001113 HOIP:HOIP_0001114 SREBP activation is a subtype of molecular activation: A process that changes the activity of the SREBP to be higher. SREBP activation HOIP_0001114 HOIP:HOIP_0001115 SREBP activation is a subtype of molecular activation: A process that changes the activity of the SREBP to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:21286345 SREBP activation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001115 PMID:21286345 The decreased expression of hepatic FXR is associated with an increased expression of LXR, SREBP-1C, and hepatic triglyceride synthesis; furthermore, increased SREBP-1C is associated with the degree of hepatic steatosis in the NAFLD patients. HOIP:HOIP_0001116 Malfunctioning of insulin signaling is a subtype of malfunctioning process: A process that cannot perform insulin signaling appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:26490400 PMID:30642126 malfunctioning of insulin signaling [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001116 HOIP:HOIP_0001117 Liver X receptor activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating LXR ( liver X receptor) with a nuclear receptor role to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:21286345 PMID:26490400 PMID:29904174 PMID:30642126 LXRa activation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001117 PMID:30642126 Upregulation of SREBP-1c and ChREBP has been speculated to be the principal regulators of NAFLD formation, which is induced by insulin resistance and transcriptionally controlled by LXRa HOIP:HOIP_0001118 Increasing NAD/NAD+ ratio is a subtype of increasing ratio: A process that changes the ratio of NAD to NAD+ to be higher. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. increasing NAD/NAD+ ratio [alcoholic fatty liver] HOIP_0001118 HOIP:HOIP_0001119 NCBI-Human-GeneID:10062 NCBI-Mouse-GeneID:22259 NCBI-Rat-GeneID:58852 PMID:21286345 Liver X Receptor Alpha [lipidosis] NR1H3 [lipidosis] LXRA (canonical)[lipidosis] HOIP_0001119 NCBI-Human-GeneID:10062 http://www.ncbi.nlm.nih.gov/gene/10062 NCBI-Mouse-GeneID:22259 http://www.ncbi.nlm.nih.gov/gene/22259 NCBI-Rat-GeneID:58852 http://www.ncbi.nlm.nih.gov/gene/58852 HOIP:HOIP_0001120 NCBI-Human-GeneID:10062 NCBI-Mouse-GeneID:22259 NCBI-Rat-GeneID:58852 Liver X Receptor Alpha NR1H3 LXRa (mol) HOIP_0001120 NCBI-Human-GeneID:10062 http://www.ncbi.nlm.nih.gov/gene/10062 NCBI-Mouse-GeneID:22259 http://www.ncbi.nlm.nih.gov/gene/22259 NCBI-Rat-GeneID:58852 http://www.ncbi.nlm.nih.gov/gene/58852 HOIP:HOIP_0001121 ChREBP activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating ChREBP to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:30642126 ChREBP activation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001121 PMID:30642126 Upregulation of SREBP-1c and ChREBP has been speculated to be the principal regulators of NAFLD formation, which is induced by insulin resistance and transcriptionally controlled by LXRa HOIP:HOIP_0001122 organophosphate HOIP_0001122 HOIP:HOIP_0001123 NCBI-Human-GeneID:51085 NCBI-Mouse-GeneID:58805 NCBI-Rat-GeneID:171078 Carbohydrate-Responsive Element-Binding Protein [lipidosis] MLXIPL CHREBP (canonical)[lipidosis] HOIP_0001123 NCBI-Human-GeneID:51085 http://www.ncbi.nlm.nih.gov/gene/51085 NCBI-Mouse-GeneID:58805 http://www.ncbi.nlm.nih.gov/gene/58805 NCBI-Rat-GeneID:171078 http://www.ncbi.nlm.nih.gov/gene/171078 HOIP:HOIP_0001124 NCBI-Human-GeneID:51085 NCBI-Mouse-GeneID:58805 NCBI-Rat-GeneID:171078 Carbohydrate-Responsive Element-Binding Protein [lipidosis] MLXIPL CHREBP (mol) HOIP_0001124 NCBI-Human-GeneID:51085 http://www.ncbi.nlm.nih.gov/gene/51085 NCBI-Mouse-GeneID:58805 http://www.ncbi.nlm.nih.gov/gene/58805 NCBI-Rat-GeneID:171078 http://www.ncbi.nlm.nih.gov/gene/171078 HOIP:HOIP_0001125 Malfunctioning of insulin signaling is a subtype of malfunctioning process: A process that cannot perform insulin signaling appropriately or cannot realize it at all. malfunctioning of insulin signaling HOIP_0001125 HOIP:HOIP_0001126 Dysfunction of peroxisomal fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient fatty acid degradation severely. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). dysfunction of peroxisomal fatty acid beta-oxidation [non-alcoholic steatohepatitis (course)] HOIP_0001126 HOIP:HOIP_0001127 The totality of all processes through which non-alcoholic steatohepatitis (NASH) is realized. NASH (course) non-alcoholic steatohepatitis (course) HOIP_0001127 HOIP:HOIP_0001128 The totality of all processes through which simple steatosis is realized. simple steatosis HOIP_0001128 HOIP:HOIP_0001129 Lipid accumulation in hepatocyte is a subtype of lipid strorage in hepatocyte: A process that keeps lipids in hepatocytes mildly. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course)]. lipid accumulation in hepatocyte [lipidosis (imbalance course)] lipid strorage in hepatocyte [lipidosis (imbalance course)]] HOIP_0001129 HOIP:HOIP_0001130 Malfunctioning of TCA cycle is a subtype of malfunctioning of metabolism: A process that cannot perform a tricarboxylic acid cycle appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. malfunctioning of TCA cycle [alcoholic fatty liver] HOIP_0001130 HOIP:HOIP_0001131 Increasing acetyl CoA is a subtype of increasing quantity: A process that changes the amount of acetyl CoA to be larger. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. acetyl CoA increase [alcoholic fatty liver] HOIP_0001131 HOIP:HOIP_0001132 Increasing production amount of acetaldehyde is a subtype of increasing quantity: A process that changes the production amount of acetaldehyde to be higher. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. PMID:17854140 Increasing production amount of acetaldehyde [alcoholic fatty liver] HOIP_0001132 PMID:17854140 Ethanol administration to rodents or ethanol exposure to ethanol-metabolizing cultured cells causes a general down-regulation of PPAR-α. Further, RXR-PPAR-α extracted from hepatoma cells previously exposed to ethanol or acetaldehyde binds poorly to an oligonucleotide containing peroxisome proliferator response elements, indicating that acetaldehyde is responsible for the action of ethanol. It is possible that acetaldehyde, because of its ability to covalently bind proteins]can form adducts with the PPAR-α transcription complex, thereby preventing its ability to bind the promoter element(s). HOIP:HOIP_0001139 A role played by the entity which negative regulates the cellular senescence. cellular senescence inhibitor HOIP_0001139 HOIP:HOIP_0001141 The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis. PMID:18556558 lipid biosynthetic process [lipidosis (normal course)] HOIP_0001141 PMID:18556558 X-box binding protein 1 (XBP1), known as a key regulator of the unfolded protein response (UPR) secondary to ER stress, is a only recently characterized regulator of hepatic lipogenesis. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 2008; 320: 1492-1496. XBP1 protein expression in mice was elevated after feeding carbohydrates and corresponded with the induction of critical genes involved in fatty acid synthesis. Inducible, selective deletion of XBP1 in the liver resulted in marked hypocholesterolemia and hypotriglyceridemia, secondary to a decreased production of lipids from the liver. This phenotype was not accompanied by hepatic steatosis or compromise in protein secretory function. The identification of XBP1 as a regulator of lipogenesis has important implications for human dyslipidemias. HOIP:HOIP_0001144 carboxylic acid HOIP_0001144 HOIP:HOIP_0001145 caspase-3 HOIP_0001145 HOIP:HOIP_0001146 Acyl-CoA thioesterase ACOT family HOIP_0001146 HOIP:HOIP_0001148 alkaline ceramidase ACER HOIP_0001148 HOIP:HOIP_0001149 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. negative regulation of apoptotic process [glutathione depletion (course)] HOIP_0001149 HOIP:HOIP_0001150 Hyperfunction of alcohol metabolism is a subtype of hyperfunctioning: A process that performs an excessive alcohol metabolism. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. hyperfunction of alcohol metabolism [alcoholic fatty liver] HOIP_0001150 HOIP:HOIP_0001152 unsaturated fatty acid HOIP_0001152 HOIP:HOIP_0001153 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of lipids. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis. positive regulation of lipid biosynthetic process [lipidosis] HOIP_0001153 HOIP:HOIP_0001154 Lipidosis (normal course) is a subtype of process sequences: The courses of processes through which lipid homeostasis balance is keeping. lipidosis (normal course) HOIP_0001154 HOIP:HOIP_0001155 Lipidosis is a subtype of process sequences: The courses of processes through which lipidosis is realized. lipidosis (course) HOIP_0001155 HOIP:HOIP_0001156 keeping lipid metabolism balance is a subtype of maintaining balance: A process that keeps a balance of lipid metabolism. keeping lipid metaolism balance HOIP_0001156 HOIP:HOIP_0001157 Maintaining lipid metabolism balance is a subtype of maintaining balance: A process that keeps a balance of lipid metabolism. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). maintaining lipid metabolism balance [lipidosis (normal course)] HOIP_0001157 HOIP:HOIP_0001160 Changing balance of lipid metabolism is a subtype of changing balance: A process that changes the balance between lipid anabolism and catabolism. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (course). changing balance of lipid metabolism [lipidosis (course)] HOIP_0001160 HOIP:HOIP_0001161 Changing balance of lipid metabolism is a subtype of changing balance: A process that changes the balance between lipid anabolism and catabolism. changing balance of lipid metabolism HOIP_0001161 HOIP:HOIP_0001162 Changing lipid homeostasis is a subtype of changing balance: A process that changes the steady state of lipid within an organism or cell. changing lipid homeostasis HOIP_0001162 HOIP:HOIP_0001163 Changing lipid homeostasis is a subtype of changing balance: A process that changes the steady state of lipid within an organism or cell. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (course). changing lipid homeostasis [lipidosis (course)] HOIP_0001163 HOIP:HOIP_0001164 Any process involved in the maintenance of an internal steady state of lipid within an organism or cell. maintaining lipid homeostasis HOIP_0001164 HOIP:HOIP_0001165 ATP degradation is a subtype of catabolic process: A process of the chemical reactions resulting in the breakdown of ATP: ATP + H2O = ADP + phosphate + 2 H+. ATP degradation HOIP_0001165 HOIP:HOIP_0001166 arachidonic acid HOIP_0001166 HOIP:HOIP_0001167 Cholesteroltransport gene mutation is a subtype of gene mutation: A process thatchanges the sequence of a cholesterol transport gene. cholesterol transport gene mutation HOIP_0001167 HOIP:HOIP_0001168 Any process involved in the maintenance of an internal steady state of lipid within an organism or cell. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course) . maintaining lipid homeostasis [lipidosis (normal course)] HOIP_0001168 HOIP:HOIP_0001169 Keeping amount of lipid in liver is a subtype of keeping amount: A process that maintaining the amount of lipid in the liver. keeping amount of lipid in liver HOIP_0001169 HOIP:HOIP_0001170 Keeping amount of lipid in liver is a subtype of keeping amount: A process that maintaining the amount of lipid in the liver. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). keeping amount of lipid in liver [lipidosis (normal course)] HOIP_0001170 HOIP:HOIP_0001172 NCBI-Human-GeneID:9817 NCBI-Mouse-GeneID:50868 NCBI-Rat-GeneID:117519 Kelch Like ECH Associated Protein 1 KEAP1 [glutathione depletion (course)] HOIP_0001172 NCBI-Human-GeneID:9817 http://www.ncbi.nlm.nih.gov/gene/9817 NCBI-Mouse-GeneID:50868 http://www.ncbi.nlm.nih.gov/gene/50868 NCBI-Rat-GeneID:117519 http://www.ncbi.nlm.nih.gov/gene/117519 HOIP:HOIP_0001174 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of lipids. This process can constitute the course of lipidosis (normal course). positive regulation of lipid catabolic process [lipidosis (normal course)] HOIP_0001174 HOIP:HOIP_0001177 Cholesterol homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a cholesterol homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick C. Cholesterol homeostasis imbalance [Niemann–Pick disease type C] HOIP_0001177 HOIP:HOIP_0001178 Increasing drug metabolite is a subtype of increasing quantity: A process that changes the amount of drug metabolites to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. increasing drug metabolite [glutathione depletion (course)] HOIP_0001178 HOIP:HOIP_0001179 Compound accumulation in liver is a subtype of accumulation of xenobiotics: A process that keeps compound in the liver. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. compound accumulation in liver [glutathione depletion (course)] HOIP_0001179 HOIP:HOIP_0001180 Hyperfunction of drug metabolizing enzyme gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive drug metabolizing enzyme gene expression. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of drug metabolizing enzyme gene expression [glutathione depletion (course)] HOIP_0001180 HOIP:HOIP_0001181 Hyperfunction of cutochrome P450 gene expression is a subtype of hyperfunction of drug metabolizing enzyme gene expression: A process that performs an excesssive gene expression of cytochrome p450. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of Cytochrome P450 gene expression [glutathione depletion (course)] hyperfunction of P450 gene expression [glutathione depletion (course)] hyperfunction of cytochrome P450 gene expression [glutathione depletion (course)] HOIP_0001181 HOIP:HOIP_0001182 Hyperfunction of drug metabolism phase I is a subtype of hyperfunctioning of drug metabolism: A process that performs an excessive drug metabolism phase I. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of drug metabolism by P450 [glutathione depletion (course)] hyperfunction of drug metabolism phase I by Cytochrome P450 [glutathione depletion (course)] HOIP_0001182 HOIP:HOIP_0001183 Cytochrome P450 activation is a subtype of molecular activation: A process that changes the activity of the cytochrome P450 to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. Cytochrome P450 activation [glutathione depletion (course)] P450 activation [glutathione depletion (course)] cytochrome P450 activation [glutathione depletion (course)] HOIP_0001183 HOIP:HOIP_0001184 NAPQI production is a subtype of generating a substance : A process that synthesizes NAPQI (N-acetyl-p-benzoquinone imine) as output. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:21177773 NAPQI production [glutathione depletion (course)] HOIP_0001184 PMID:21177773 cytochrome P450 (CYP) enzymes, including CYP2E1, CYP1A2, and CYP3A4, convert 5–9% of acetaminophen to a highly reactive metabolite, N-acetyl-p-benzoquinonimine (NAPQI) (Corcoran et al., 1980; Dahlin et al., 1984) HOIP:HOIP_0001185 Increasing demand for glutathione conjugation is a subtype of increasing functional demand: A process changes the functional demand for the for glutathione conjugation to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. increasing demand for glutathione conjugation [glutathione depletion (course)] HOIP_0001185 HOIP:HOIP_0001186 Increasing demand for response to mitochondrial oxidative stress is a subtype of increasing the demand for response to oxidative stress: A process that changes the functional demand for the response to the mitochondrial oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. increasing demand for response to mitochondrial oxidative stres [oxidative stress (course)] HOIP_0001186 HOIP:HOIP_0001187 JNK translocation from cytoplasm to mitochondria is a subtype of transmitting: A process that of the directed movement of JNK from the cytoplasm to the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. chronic ethanol-induced activation of KCs is attributed to gut-sourced LPS, which is a major component of outer membrane of Gram-negative bacteria and passes through the intestinal epithelial barrier. Chronic ethanol exposure can increase translocation of LPS from gut to liver by enhancing the intestinal permeability and altering the gut microflora. JNK translocation from cytoplasm to mitochondria [glutathione depletion (course)] HOIP_0001187 chronic ethanol-induced activation of KCs is attributed to gut-sourced LPS, which is a major component of outer membrane of Gram-negative bacteria and passes through the intestinal epithelial barrier. Chronic ethanol exposure can increase translocation of LPS from gut to liver by enhancing the intestinal permeability and altering the gut microflora. PMID:27965666 HOIP:HOIP_0001188 Any process that stops, prevents, or reduces the frequency, rate or extent of glutathione conjugation process. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. ISBN:0071769234 negative regulation glutathione conjugation [glutathione depletion (course)] HOIP_0001188 ISBN:0071769234 Michael acceptors such as diethyl maleate (DEA) and phorone are commonly used in vivo to deplete GSH levels in experimental animals. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0001189 Hypofunction of drug metabolism phase II is a subtype of hypofunction of drug metabolism: A process that performs a decreased or insufficient drug metabolism phase II. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hypofunction of drug metabolism phase II [glutathione depletion (course)] HOIP_0001189 HOIP:HOIP_0001190 Decreasing excretion quantity of bile acid is a subtype of decreasing quantity: A process that changes the excretion quantity of of bile acids to be lower. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. decreasing excretion quantity of the conjugates [glutathione depletion (course)] HOIP_0001190 HOIP:HOIP_0001191 Glutathione conjugation (supply) - function demand imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance between glutathione conjugation supply and demand. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. Glutathione conjugation (supply) - function demand imbalance [glutathione depletion (course)] HOIP_0001191 HOIP:HOIP_0001192 NAPQI accumulation is a subtype of accumulation of substances in a biological object: A process that keeps NAPQI (N-acetyl-p-benzoquinone imine) within a biological object(s). NAPQI is an intermediate metabolite of the paracetamol and plays a role as a toxic substance in the body. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. NAPQI accumulation [glutathione depletion (course)] HOIP_0001192 HOIP:HOIP_0001193 Glutathione depletion is a subtype of depleting: A process that lessens markedly in the amount of glutathione. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. glutathione depletion [glutathione depletion (course)] HOIP_0001193 HOIP:HOIP_0001194 The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. The formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other protein. https://reactome.org/PathwayBrowser/#/R-HSA-174403 glutathione biosynthetic process [glutathione depletion (course)] HOIP_0001194 HOIP:HOIP_0001195 JNK translocation from cytoplasm to mitochondria is a subtype of molecule transport: A process that of the directed movement of JNK from the cytoplasm to the mitochondria. JNK translocation from cytoplasm to mitochondria HOIP_0001195 HOIP:HOIP_0001196 Protein binding by NAPQI is a subtype of protein binding: Interacting between a protein and NAPQI. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. protein binding by NAPQI [glutathione depletion (course)] HOIP_0001196 HOIP:HOIP_0001197 Malfunctioning of mitochondrial ATP synthesis coupled electron transpor is a subtype of malfunctioning process: A process that cannot perform a respiratory electron transport chain appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. malfunctioning of mitochondrial ATP synthesis coupled electron transport [glutathione depletion (course)] HOIP_0001197 HOIP:HOIP_0001198 Drug-, radiation-induced, or spontaneous injuries to DNA that introduce deviations from its normal double-helical conformation. These changes include structural distortions that interfere with replication and transcription, as well as point mutations that disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. If the damage is minor, it can often be repaired (DNA repair); extensive damage can induce apoptosis. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. DNA damage [glutathione depletion (course)] HOIP_0001198 HOIP:HOIP_0001199 Increasing free radical is a subtype of increasing quantity: A process that changes the amount of free radicals to be larger. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. increasing free radical [glutathione depletion (course)] HOIP_0001199 HOIP:HOIP_0001200 Lipoperoxidation is a subtype of lipid oxidation: The degradation of lipids caused by an oxidative attack from free radicals. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. lipoperoxidation [glutathione depletion (course)] HOIP_0001200 HOIP:HOIP_0001201 Increasing demand for response to mitochondrial oxidative stress is a subtype of increasing the demand for response to oxidative stress: A process that changes the functional demand for the response to the mitochondrial oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. increasing demand for response to mitochondrial oxidative stress [glutathione depletion (course)] HOIP_0001201 HOIP:HOIP_0001202 Mitochondrial dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete mitochondrial function. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. mitochondrial dysfunction [glutathione depletion (course)] HOIP_0001202 HOIP:HOIP_0001203 Hypofunction of ATP biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient ATP biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hypofunction of ATP biosynthesis [glutathione depletion (course)] HOIP_0001203 HOIP:HOIP_0001204 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. cell death [glutathione depletion (course)] HOIP_0001204 HOIP:HOIP_0001205 Abnormality of membrane is a subtype of changing abnormal cellular structure: A process that changes the membrane stucture abnormally. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. abnormality of membrane [glutathione depletion (course)] HOIP_0001205 HOIP:HOIP_0001206 Calcium ion homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a calcium ion homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. calcium ion homeostasis imbalance [glutathione depletion (course)] HOIP_0001206 HOIP:HOIP_0001207 Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. positive regulation of mitochondrial membrane permeability [glutathione depletion (course)] HOIP_0001207 HOIP:HOIP_0001208 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that inculdes step 1 to 4. The defense performance level is Moderate (M) in daily life; however, the functional demand level is Very high (VH), which leads to the imbalance and leads to abnormal manifestation. imbalance M<VH HOIP_0001208 HOIP:HOIP_0001209 Aryl hydrocarbon receptor activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating AhR (aryl hydrocarbon receptor) with a nuclear receptor role to be higher. AhR activity is combining with an aryl hydrocarbon and transmitting the signal to initiate a change in cell activity. The aryl hydrocarbon receptor is a ligand-activated transcription factor which translocates to the nucleus to activate transcription upon ligand-binding.Combining with an aryl hydrocarbon and transmitting the signal to initiate a change in cell activity. The aryl hydrocarbon receptor is a ligand-activated transcription factor which translocates to the nucleus to activate transcription upon ligand-binding. PMID:1325649 AhR activating AhR activation aryl hydrocarbon receptor activity aryl hydrocarbon receptor activity aryl hydrocarbon receptor activation HOIP_0001209 aryl hydrocarbon receptor activity GO:0004874 HOIP:HOIP_0001210 Constitutive androstane receptor activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating CAR ( constitutive androstane receptor) with a nuclear receptor role to be higher. CAR activating CAR activation activating CAR constitutive androstane receptor activation HOIP_0001210 HOIP:HOIP_0001211 ATF4 gene expression regulation system is a subtype of pathway system. This entity has sub-parts and has a goal of regulating gene expressions by ATF4 as a systemic context. ATF4 gene expression regulation system HOIP_0001211 HOIP:HOIP_0001212 Forming a complex with Cyp is a subtype of protein complex assembly: The aggregation, arrangement and bonding together with Cyp (cytochrome P450) to form a complex. forming a complex with Cyp HOIP_0001212 HOIP:HOIP_0001213 P53 activation is a subtype of activation of transcription factor: A process that changes the activity of one of the p53 family of proteins to be higher. p53 activation HOIP_0001213 HOIP:HOIP_0001214 Retinoid X receptor activation is a subtype of activating nuclear receptor: A process that changes the activity of the RXR (retinoid X receptor) with a nuclear receptor role to be higher. activating RXR RXR activation retinoid X receptor activation HOIP_0001214 HOIP:HOIP_0001215 Hyperfunction of lipase gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive lipase gene expression. hyperfunction of lipase gene expression HOIP_0001215 HOIP:HOIP_0001216 A process of liquid water accumulation in a particular location in an organism, tissue or cell. water accumulation HOIP_0001216 HOIP:HOIP_0001217 Increasing number of apoptotic cells in liver is a subtype of increasing number of dead cells in liver: A process that becomes larger in the number of apoptotic cells in the liver. increasing number of apoptotic cells in liver HOIP_0001217 HOIP:HOIP_0001218 Hyperfunction of lipase gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive lipase gene expression. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). hyperfunction of lipase gene expression [lipidosis (normal course)] HOIP_0001218 HOIP:HOIP_0001219 Apoptosis inducer activation is a subtype of molecular activation: A process that changes the activity of the molecule with an apoptosis inducer role to be higher. activating apoptosis inducer apoptosis inducer activation HOIP_0001219 HOIP:HOIP_0001220 The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). lipid catabolic process [lipidosis (normal course)] HOIP_0001220 HOIP:HOIP_0001221 Lipid transport from liver is a subtype of lipid transport. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). lipid transport from hepatocyte to extrahepatic [lipidosis (normal course)] HOIP_0001221 HOIP:HOIP_0001222 hydoroxy acid HOIP_0001222 HOIP:HOIP_0001223 Positive regulation process is a subtype of controlling: A process that activates or increases the frequency, rate or extent of function. Any process that activates, maintains or increases the rate or extent of a process. positive regulation process HOIP_0001223 HOIP:HOIP_0001224 A moving process of alcohol from the outside to the inside of a body. alcohol intake HOIP_0001224 HOIP:HOIP_0001225 A role played by the entity that shows an expression change according to some context. marker role HOIP_0001225 HOIP:HOIP_0001227 Hyperfunction of glucuronic acid conjugation is a subtype of hyperfunction of drug metabolism phase II: A process that performs an excessive glucuronic acid conjugation. hyperfunction of glucuronic acid conjugation HOIP_0001227 HOIP:HOIP_0001228 Hyperfunction of glutathione conjugation is a subtype of hyperfunction of drug metabolism phase II: A process that performs an excessive glutathione conjugation. hyperfunction of glutathione conjugation HOIP_0001228 HOIP:HOIP_0001229 Increasing hepatic vascular lumen area is a subtype of increasing area: A process that changes the area of the hepatic vascular lumen area to be larger. increasing hepatic vascular lumen area HOIP_0001229 HOIP:HOIP_0001230 Smooth endoplasmic reticulum proliferation in hepatocyte is a subtype of endoplasmic reticulum proliferation in hepatocyte: A process that becomes larger in the number of smooth endoplasmic reticulum in hepatocyte(s). increasing number of sER smooth endoplasmic reticulum proliferation in hepatocyte HOIP_0001230 HOIP:HOIP_0001231 A moving process of a tumor cell from the outside to the inside of other organ. tumor cell invasion HOIP_0001231 HOIP:HOIP_0001232 sequestering of triglyceride (severe) is a subtype of lipid strorage in hepatocyte: A process that keeps triglycerides in hepatocytes. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. sequestering of triglyceride (severe) [alcoholic fatty liver] HOIP_0001232 HOIP:HOIP_0001233 Glucose homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a glucose homeostastasis balance. glucose homeostasis imbalance HOIP_0001233 HOIP:HOIP_0001234 Phenobarbital accumulation in liver is a subtype of compound accumulation in liver: A process that keeps phenobarbital in the liver. phenobarbital accumulation in liver HOIP_0001234 HOIP:HOIP_0001235 Carbohydrate storage in liver is a subtype of carbohydrate storage: The accumulation in hepatocytes of carbohydrates. carbohydrate storage in liver HOIP_0001235 HOIP:HOIP_0001236 Hyperfunction of drug metabolism phase II is a subtype of hyperfunction of drug metabolism: A process that performs an excessive drug metabolism phase II. hyperfunction of drug metabolism phase II HOIP_0001236 HOIP:HOIP_0001237 Hyperfunction of iron supply is a subtype of hyperfunctioning: A process that performs an excesssive iorn supply. hyperfunction of iron supply HOIP_0001237 HOIP:HOIP_0001238 citric acid HOIP_0001238 HOIP:HOIP_0001239 lactic acid HOIP_0001239 HOIP:HOIP_0001240 CAD accumulation in lysosome is a subtype of compound accumulation in lysosome: A process that keeps CAD (Cationic Amphiphilic Drug) in the lysosome. CAD accumulation in lysosome HOIP_0001240 HOIP:HOIP_0001241 CAD accumulation in lysosome is a subtype of compound accumulation in lysosome: A process that keeps CAD (Cationic Amphiphilic Drugs) in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). CAD accumulation in lysosome [phospholipidosis (mild)] HOIP_0001241 HOIP:HOIP_0001242 Compound accumulation in lysosome is a subtype of accumulation of xenobiotics: A process that keeps compound in the lysosome. compound accumulation in lysosome HOIP_0001242 HOIP:HOIP_0001243 Phospholipid homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. phospholipid homeostasis imbalance phospholipid homeostasis imbalance HOIP_0001243 HOIP:HOIP_0001244 Phospholipid accumulation is a subtype of accumulation of substances in a biological object: A process that keeps phospholipid in an organism, tissue, organelle, or cell. phospholipid accumulation HOIP_0001244 HOIP:HOIP_0001245 Increasing blood glucose lebvel is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:22883813 increasing blood glucose level [ER stress] HOIP_0001245 PMID:22883813 ER stress-induced inflammation: does it aid or impede disease progression?: ER stress in various cells plays an important role in the pathogenesis of several diseases, including obesity, type 2 diabetes, cancer, and intestinal bowel and airway diseases. Moreover, it has been suggested that ER stress-induced inflammation contributes substantially to disease progression. HOIP:HOIP_0001246 Hyperfunction of reduction of NAD(+) to NADH is a subtype of hyperfunction of reduction: A process that performs an excesssive reduction of NAD(+) to NADH. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. hyperfunction of reduction of NAD(+) to NADH [alcoholic fatty liver] HOIP_0001246 HOIP:HOIP_0001247 Increasing lysosomal pH is a subtype of changing pH: A process that changes the pH in lysosome to be higher. increasing lysosomal pH HOIP_0001247 HOIP:HOIP_0001248 Increasing demand for phospholipid degradation is a subtype of increasing functional demand: A process that changes the functional demand for the phospholipid degradation to be higher. increasing demand for phospholipid degradation HOIP_0001248 HOIP:HOIP_0001249 Undigested membrane material accumulation is a subtype of accumulation of substances in a biological object: A process that keeps undigested membrane material. undigested membrane material accumulation HOIP_0001249 HOIP:HOIP_0001250 Increasing phospholipid is a subtype of increasing quantity: A process that changes the amount of phospholipid to be larger. increasing phospholipid HOIP_0001250 HOIP:HOIP_0001251 Increasing phospholipid inflow is a subtype of increasing quantity: A process that changes the phospholipid inflow into the hepatocyte to be larger. increasing phospholipid inflow HOIP_0001251 HOIP:HOIP_0001252 NCBI-Rat-GeneID:171402 PMID:17906635 PMID:27467521 The birth rate of Elovl6 knockout mice was lower, and the surviving mice were smaller in size and had reduced body weight. Crucial role of a long-chain fatty acid elongase, Elovl6, in obesity-induced insulin resistance. Secondary regulation of PPARa activity could be a part of SREBP-1c/Elovl6 regulation of lipogenesis. Elovl6 (mouse)[lipidosis] HOIP_0001252 NCBI-Rat-GeneID:171402 http://www.ncbi.nlm.nih.gov/gene/171402 PMID:17906635 Mice deficient for Elovl6, the gene encoding the elongase that catalyzes the conversion of palmitate to stearate, were generated and shown to become obese and develop hepatosteatosis when fed a high-fat diet or mated to leptin-deficient ob/ob mice. However, they showed marked protection from hyperinsulinemia, hyperglycemia and hyperleptinemia. Amelioration of insulin resistance was associated with restoration of hepatic insulin receptor substrate-2 and suppression of hepatic protein kinase C epsilon activity resulting in restoration of Akt phosphorylation. HOIP:HOIP_0001253 Hypofunction of phospholipid degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient phospholipid degradation. hypofunction of phospholipid degradation HOIP_0001253 HOIP:HOIP_0001254 Forming a complex of drugs and biological substance is a subtype of protein complex assembly: The aggregation, arrangement and bonding together between drugs and biological molecules to form a complex. forming a complex of drugs and biological substance HOIP_0001254 HOIP:HOIP_0001255 Increase in alcohol inflow into hepatocyte is a subtype of increasing quantity: A process that changes the alcohol inflow into the hepatocyte to be larger. increase in alcohol inflow into hepatocyte HOIP_0001255 HOIP:HOIP_0001256 Negative regulation of phospholipid degradation is a subtype of negative regulation of decomposing: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid degradation. negative regulation of phospholipid degradation HOIP_0001256 HOIP:HOIP_0001257 Hyperfunction of dead cell phagocytosis by Kupffer cells (macrophages) is a subtype of hyperfunctioning: A process that performs phagocytosis of dead cells by Kupffer cells or macrophages execessively. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). hyperfunction of dead cell phagocytosis by Kupffer cells (macrophages) [phospholipidosis (severe (excessive defense))] HOIP_0001257 HOIP:HOIP_0001258 Any process that stops, prevents, or reduces the frequency, rate or extent of lysophagy. negative regulation of lysophagy HOIP_0001258 HOIP:HOIP_0001259 Increase in alcohol inflow into hepatocyte is a subtype of increasing quantity: A process that changes the alcohol inflow into the hepatocyte to be larger. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. increase in alcohol inflow into hepatocyte [alcoholic fatty liver] HOIP_0001259 HOIP:HOIP_0001260 Forming a complex of CAD and phospholipid is a subtype of forming a complex of drugs and biological substance: A process that forms a complex consisiting phospholipids and CAD (Cationic Amphiphilic Drugs cationic amphiphile drug) in the lysosomal membrane, which causes structural change of the membrane. The degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). forming a complex of CAD and phospholipid [phospholipidosis (moderate) ] HOIP_0001260 HOIP:HOIP_0001261 Hypofunction of phospholipid export from lysosome is a subtype of hypofunction of export: A process that performs a decreased or insufficient phospholipid export from lysosome. hypofunction of phospholipid export from lysosome HOIP_0001261 HOIP:HOIP_0001262 Hypofunction of phospholipid export from lysosome is a subtype of hypofunction of export: A process that performs a decreased or insufficient phospholipid export from lysosome. And the degree is severe. This process can constitute the course of phospholipidosis (severe). hypofunction of phospholipid export from lysosome [phospholipidosis (severe)] HOIP_0001262 HOIP:HOIP_0001263 Changing balance of phospholipid metabolism is a subtype of changing balance: A process that changes the balance between phospholipid anabolism and catabolism. changing balance of phospholipid metabolism HOIP_0001263 HOIP:HOIP_0001264 Hyperfunction of glycerophospholipid synthesis gene expression is a subtype of hyperfunction of phospholipid synthesis gene expression: A process that performs an excesssive glycerophospholipid synthestic gene expression. hyperfunction of glycerophospholipid synthesis gene expression HOIP_0001264 HOIP:HOIP_0001265 Lipid storage in liver is a subtype of lipid storage: The accumulation and maintenance in cells or tissues of lipids in the liver. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. lipid storage in liver [hepatic fibrosis course] HOIP_0001265 HOIP:HOIP_0001267 Moving lipid to the hepatocyte is a subtype of moving A to the inside of B: A process of the movement of lipid into a hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). moving lipid to the hepatocyte [lipidosis (normal course)] HOIP_0001267 HOIP:HOIP_0001268 Malfunctioning of TCA cycle is a subtype of malfunctioning of metabolism: A process that cannot perform a tricarboxylic acid cycle appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis by alcoholic liver injury. malfunctioning of TCA cycle [hepatic fibrosis by alcoholic liver injury] HOIP_0001268 HOIP:HOIP_0001269 Malfunctioning of TCA cycle is a subtype of malfunctioning of metabolism: A process that cannot perform a tricarboxylic acid cycle appropriately or cannot realize it at all. malfunctioning of TCA cycle HOIP_0001269 HOIP:HOIP_0001270 Moving lipid to the hepatocye is a subtype of moving A to the inside of B: A process of the movement of lipid into a hepatocyte. moving lipid to the hepatocye HOIP_0001270 HOIP:HOIP_0001271 The directed movement of lipid, out of a hepatocyte. lipid efflux from hepatocyte HOIP_0001271 HOIP:HOIP_0001272 Hyperfunction of alcohol metabolism is a subtype of hyperfunctioning: A process that performs an excessive alcohol metabolism. hyperfunction of alcohol metabolism HOIP_0001272 HOIP:HOIP_0001274 Catalysis role of the reaction: ATP + ethanolamine = ADP + 2 H(+) + phosphoethanolamine. EC:2.7.1.82 related molecular function GO:0004305 ethanolamine kinase activity ethanolamine kinase HOIP_0001274 HOIP:HOIP_0001275 NCBI-Human-GeneID:83939 NCBI-Mouse-GeneID:229317 NCBI-Rat-GeneID:502531 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=Retrieve&dopt=full_report&list_uids=83939 EIF2A (canonical)[ER stress] HOIP_0001275 NCBI-Human-GeneID:83939 http://www.ncbi.nlm.nih.gov/gene/83939 NCBI-Mouse-GeneID:229317 http://www.ncbi.nlm.nih.gov/gene/229317 NCBI-Rat-GeneID:502531 http://www.ncbi.nlm.nih.gov/gene/502531 HOIP:HOIP_0001276 Lipid storage in liver is a subtype of lipid storage: The accumulation and maintenance in cells or tissues of lipids in the liver. lipid storage in liver HOIP_0001276 HOIP:HOIP_0001281 The non-covalent aggregation and arrangement of proteins and lipids in the liver to form a very-low-density lipoprotein particle. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). VLDL formation [lipidosis (normal course)] HOIP_0001281 HOIP:HOIP_0001282 CASPASE-2 (canonical)[ER stress] HOIP_0001282 HOIP:HOIP_0001283 NRF2 activation is a subtype of activation of transcription factor: A process that changes the activity of NRF2 (Nuclear Factor, Erythroid 2 Like 2) to be higher. NRF2 activation HOIP_0001283 HOIP:HOIP_0001284 CD36 activation is a subtype of molecular activation: A process that changes the activity of the CD36 to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:17728375 PMID:18242221 CD36 activation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001284 PMID:17728375 Increased hepatic CD36 expression contributes to dyslipidemia associated with diet-induced obesity. During diet-induced obesity, CD36 protein levels in the liver are significantly elevated, and these elevated levels correlate with increased hepatic triglyceride storage and secretion. These alterations in liver lipid storage and secretion were also observed upon forced expression of hepatic CD36 in the absence of DIO and were accompanied with a marked rise in hepatic fatty acid uptake in vivo, demonstrating that increased CD36 expression is sufficient to recapitulate the aberrant liver lipid handling observed in DIO. PMID:18242221 Scavenger receptors class A-I/II and CD36 are the principal receptors responsible for the uptake of modified low density lipoprotein leading to lipid loading in macrophages. HOIP:HOIP_0001285 Liver dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete liver function. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). liver dysfunction [phospholipidosis (severe)] HOIP_0001285 HOIP:HOIP_0001286 Obesity is a subtype of increasing weight: A process that changes the body weight to be higher. obesity HOIP_0001286 HOIP:HOIP_0001287 Hypofunction of phosphosphingolipid degradation is a subtype of hypofunction of phospholipid degradation: A process that performs a decreased or insufficient phosphosphingolipid degradation. hypofunction of phosphosphingolipid degradation HOIP_0001287 HOIP:HOIP_0001288 Hyperfunction of reduction of NAD(+) to NADH is a subtype of hyperfunction of reduction: A process that performs an excesssive reduction of NAD(+) to NADH. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis by alcoholic liver injury. hyperfunction of reduction of NAD(+) to NADH [hepatic fibrosis by alcoholic liver injury] HOIP_0001288 HOIP:HOIP_0001289 Increasing NAD/NAD+ ratio is a subtype of increasing ratio: A process that changes the ratio of NAD to NAD+ to be higher. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis by alcoholic liver injury. increasing NAD/NAD+ ratio [hepatic fibrosis by alcoholic liver injury] HOIP_0001289 HOIP:HOIP_0001290 Hyperfunction of sphingophospholipid synthesis gene expression is a subtype of hyperfunction of phospholipid synthesis gene expression: A process that performs an excesssive sphingophospholipid synthetic gene expression. hyperfunction of sphingophospholipid synthesis gene expression HOIP_0001290 HOIP:HOIP_0001291 The chemical reactions and pathways resulting in the formation of phosphosphingolipids. phosphosphingolipid anabolism phosphosphingolipid formation phosphosphingolipid synthesis sphingophospholipid anabolism sphingophospholipid biosynthesis sphingophospholipid formation phosphosphingolipid biosynthesis HOIP_0001291 HOIP:HOIP_0001292 Increasing NAD/NAD+ ratio is a subtype of increasing ratio: A process that changes the ratio of NAD to NAD+ to be higher. increasing NAD/NAD+ ratio HOIP_0001292 HOIP:HOIP_0001293 Sphingophopholipid metabolism imbalance is a subtype of phospholipid metabolism imbalance: A process that becomes lacking a homeostastasis balance of sphingophopholipid metabolism. sphingophopholipid metabolism imbalance HOIP_0001293 HOIP:HOIP_0001294 Any process that stops, prevents, or reduces the frequency, rate or extent of lysophagy. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). negative regulation of lysophagy [phospholipidosis (severe)] HOIP_0001294 HOIP:HOIP_0001295 Glycerophospholipid metabolism imbalance is a subtype of phospholipid metabolism imbalance: A process that becomes lacking a homeostastasis balance of glycerophospholipid metabolism. glycerophospholipid metabolism imbalance HOIP_0001295 HOIP:HOIP_0001296 increasing number of damaged lysosomes is a subtype of increasing number : A process that becomes larger in the number of damaged lysosomes. increasing number of damaged lysosomes HOIP_0001296 HOIP:HOIP_0001297 Hypofunction of maintaining lysosome homeostasis is a subtype of hypofunctioning: A process that performs a decreased or insufficient maintaining lysosome homeostasis. hypofunction of maintaining lysosome homeostasis HOIP_0001297 HOIP:HOIP_0001298 The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). autophagy [phospholipidosis (normal course)] HOIP_0001298 HOIP:HOIP_0001299 An attribute that inheres in a bearer by virtue of network network attribute HOIP_0001299 HOIP:HOIP_0001300 Refolding promoting gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature refolding inducing gene product or products (proteins or RNA) . refolding promoting gene expression HOIP_0001300 HOIP:HOIP_0001301 NCBI-Human-GeneID:6319 PMID:19850634 PMID:21045174 PMID:26519296 PMID:4382040 Stearoyl-CoA Desaturase [lipidosis] SCD (canonical)[lipidosis] HOIP_0001301 NCBI-Human-GeneID:6319 http://www.ncbi.nlm.nih.gov/gene/6319 PMID:19850634 Hepatic lipid composition and stearoyl-coenzyme A desaturase 1 mRNA expression can be estimated from plasma VLDL fatty acid ratios. PMID:26519296 Remarkably, liver stearoyl-CoA desaturase (Scd) mRNA expression was by far the most highly-induced transcript in WD-fed rats (approximately 30-fold, FDR = 0.01) which supports previous literature underscoring this gene as a crucial target during NAFLD development. HOIP:HOIP_0001302 Hyperfunction of reduction of NAD(+) to NADH is a subtype of hyperfunction of reduction: A process that performs an excesssive reduction of NAD(+) to NADH. hyperfunction of reduction of NAD(+) to NADH HOIP_0001302 HOIP:HOIP_0001303 PLB HOIP_0001303 HOIP:HOIP_0001304 Negative regulation of glycerophospholipid degradation is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of glycerophospholipid degradation. negative regulation of glycerophospholipid degradation HOIP_0001304 HOIP:HOIP_0001305 Increasing acetyl CoA is a subtype of increasing quantity: A process that changes the amount of acetyl CoA to be larger. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis by alcoholic liver injury. acetyl CoA increase [hepatic fibrosis by alcoholic liver injury] HOIP_0001305 HOIP:HOIP_0001306 ATF6 (ATF6-alpha) activates chaperone genes is a subtype of molecular activation: A process that changes the activity of the molecule with chaperone role to be higher by ATF6. This process is dependent on the refolding and can constitute the course of ER stress. ATF6 (ATF6-alpha) activates chaperone genes [ER stress - refolding] HOIP_0001306 HOIP:HOIP_0001307 A role played by the entity which enables the transfer of choline from one side of a membrane to the other. Choline (2-hydroxyethyltrimethylammonium) is an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine. related molecular function GO:0015220 choline transmembrane transporter HOIP_0001307 HOIP:HOIP_0001308 Lgpat1 HOIP_0001308 HOIP:HOIP_0001309 CD36 activation is a subtype of molecular activation: A process that changes the activity of the CD36 to be higher. PMID:17728375 PMID:27974793 CD 36 activation HOIP_0001309 PMID:27974793 Targeting metastasis-initiating cells through the fatty acid receptor CD36. HOIP:HOIP_0001310 Hypofunction of fatty acid beta-oxidation is a subtype of hypofunction of fatty acid oxidation: A process that performs a decreased or insufficient fatty acid beta-oxidation. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. hypofunction of fatty acid beta-oxidation [Fibrosis] HOIP_0001310 HOIP:HOIP_0001311 Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of insulin. This entity is a specific course-dependent process. This process can constitute the course of ER stress. negative regulation of insulin secretion [ER stress] HOIP_0001311 HOIP:HOIP_0001312 NCBI-Human-GeneID:948 NCBI-Mouse-GeneID:12491 NCBI-Rat-GeneID:29184 CD36 (mol) HOIP_0001312 NCBI-Human-GeneID:948 http://www.ncbi.nlm.nih.gov/gene/948 NCBI-Mouse-GeneID:12491 http://www.ncbi.nlm.nih.gov/gene/12491 NCBI-Rat-GeneID:29184 http://www.ncbi.nlm.nih.gov/gene/29184 HOIP:HOIP_0001313 AP-1 activation is a subtype of molecular activation: A process that changes the activity of the AP-1 to be higher. AP-1 activation HOIP_0001313 HOIP:HOIP_0001314 Increasing phospholipid material is a subtype of increasing quantity: A process that changes the amount of phospholipid material to be larger. increasing phospholipid material HOIP_0001314 HOIP:HOIP_0001315 Increasing phospholipid material is a subtype of increasing quantity: A process that changes the amount of phospholipid material to be larger. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). increasing phospholipid material [Phospholipidosis (severe)] HOIP_0001315 HOIP:HOIP_0001316 A role played by the entity to change the molecule (activity). role related to molecular change HOIP_0001316 HOIP:HOIP_0001317 Increasing glycerophospholipid material is a subtype of increasing materials for lipid formation: A process that changes the amount of glycerophospholipid material to be larger. increasing glycerophospholipid material HOIP_0001317 HOIP:HOIP_0001318 Increasing glycerophospholipid material is a subtype of increasing materials for lipid formation: A process that changes the amount of glycerophospholipid material to be larger. This process is dependent on the glycerophospholipid disorder (severe) and can constitute the course of Phospholipidosis. increasing glycerophospholipid material [phospholipidosis - glycerophospholipid disorder (severe)] HOIP_0001318 HOIP:HOIP_0001319 NCBI-Human-GeneID:948 NCBI-Mouse-GeneID:12491 NCBI-Rat-GeneID:29184 PMID:15677505 PMID:16407588 PMID:18242221 PMID:21145849 PMID:27034954 CD36 [lipidosis] HOIP_0001319 NCBI-Human-GeneID:948 http://www.ncbi.nlm.nih.gov/gene/948 NCBI-Mouse-GeneID:12491 http://www.ncbi.nlm.nih.gov/gene/12491 NCBI-Rat-GeneID:29184 http://www.ncbi.nlm.nih.gov/gene/29184 PMID:16407588 Lipid metabolism and liver inflammation. I. Hepatic fatty acid uptake: possible role in steatosis. PMID:18242221 Hepatic fatty acid transporter Cd36 is a common target of LXR, PXR, and PPARgamma in promoting steatosis. Activation of LXR induced Cd36. Moreover, the hepatic steatosis induced by LXR agonists was largely abolished in Cd36 null mice. PXR can regulate Cd36 directly or through its activation of PPARgamma. Both LXR-mediated Cd36 regulation and PXR-mediated PPARgamma regulation are liver specific. PMID:21145849 AMPK activation promotes fatty acid uptake into the cell through the fatty acid transporter FAT/CD36 in addition to its stimulating role on mitochondrial fatty acid oxidation. PMID:27034954 VPA enhanced oleic acid- (OLA-) induced lipid accumulation in a dose-dependent manner in hepatocytes; this may be due to upregulated lipid uptake, triacylglycerol (TAG) synthesis, and lipid droplet formation. Following VPA treatment, the expression levels of genes encoding cluster of differentiation 36 (Cd36), low-density lipoprotein receptor-related protein 1 (Lrp1), diacylglycerol acyltransferase 2 (Dgat2), and perilipin 2 (Plin2) were increased. CD36 regulates lipid uptake in different cells via binding to different ligands including long-chain fatty acids and native/oxidized lipoproteins. Increased hepatic CD36 expression is highly correlated with human insulin resistance and nonalcoholic steatohepatitis (NASH) development HOIP:HOIP_0001321 AP-1 activation is a subtype of AP-1 activation: A process that changes the activity of the AP-1 to be higher by JNK. AP-1 activation by JNK HOIP_0001321 HOIP:HOIP_0001322 AP-1 activation is a subtype of AP-1 activation: A process that changes the activity of the AP-1 to be higher by JNK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. AP-1 activation [ER stress] HOIP_0001322 HOIP:HOIP_0001323 Hypofunction of hepatic metabolism is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient hepatic metabolism. hypofunction of hepatic metabolism HOIP_0001323 HOIP:HOIP_0001324 Hypofunction of protein metabolism is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient protein metabolism. hypofunction of protein metabolism HOIP_0001324 HOIP:HOIP_0001325 Hypofunction of lipid metabolism is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient lipid metabolism. hypofunction of lipid metabolism HOIP_0001325 HOIP:HOIP_0001326 Hypofunction of carbohydrate metabolism is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient carbohydrate metabolism. hypofunction of carbohydrate metabolism HOIP_0001326 HOIP:HOIP_0001327 Hypofunction of cholesterol biosynthesis is a subtype of hypofunction of lipid biosynthesis: A process that performs a decreased or insufficient cholesterol biosynthesis. hypofunction of cholesterol biosynthesis HOIP_0001327 HOIP:HOIP_0001330 Decreasing cholesterol concentration in blood is a subtype of decreasing concentration: A process that changes the concentration of the cholesterol in the blood to be lower. decreasing cholesterol concentration in blood HOIP_0001330 HOIP:HOIP_0001331 Hypofunction of albumin biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient albumin biosynthesis. hypofunction of albumin biosynthesis HOIP_0001331 HOIP:HOIP_0001332 Decreasing albumin concentration in blood is a subtype of decreasing concentration: A process that changes the concentration of the albumin in the blood to be lower. decreasing albumin concentration in blood HOIP_0001332 HOIP:HOIP_0001333 Decreasing blood osmotic pressure. is a subtype of decreasing osmotic pressure.: A process that changes the osmotic pressure to be lower. decreasing blood osmotic pressure. HOIP_0001333 HOIP:HOIP_0001334 An attribute inhering in a bearer by virtue of the bearer's participation in movement. movement attribute HOIP_0001334 HOIP:HOIP_0001335 Decreasing amount of circulating blood is a subtype of decreasing blood flow: A process that changes the amount of circulating blood to be smaller. decreasing amount of circulating blood HOIP_0001335 HOIP:HOIP_0001336 Decreasing renal blood flow is a subtype of decreasing flow: A process that changes the amount of renal flow to be lower. decreasing renal blood flow HOIP_0001336 HOIP:HOIP_0001337 Increasing creatinine concentration is a subtype of increasing concentration: A process that changes the creatinine concentration to be higher. increasing creatinine concentration HOIP_0001337 HOIP:HOIP_0001338 Renin-angiotensin activation is a subtype of activating: A process that changes the activity of the renin-angiotensin system, which regulates blood pressure and fluid balance, to be higher. renin-angiotensin activation HOIP_0001338 HOIP:HOIP_0001340 Hypofunction of retinol storage is a subtype of hypofunctioning: A process that performs a decreased or insufficient retinol storage. hypofunction of retinol storage HOIP_0001340 HOIP:HOIP_0001341 A role played by the molecule which transfers fatty acids. fatty acid transporter role HOIP_0001341 HOIP:HOIP_0001342 Hypofunction of liver's excretion is a subtype of hypofunction of removing: A process that performs a decreased or insufficient liver's excretion. hypofunction of liver's excretion HOIP_0001342 HOIP:HOIP_0001343 Bile acid biosynthetic malfunction is a subtype of organ malfunction: A process that does not perform a bile acid biosynthetic function correctly. bile acid biosynthetic malfunction HOIP_0001343 HOIP:HOIP_0001344 Bile secretion malfunction is a subtype of organ malfunction: A process that does not perform bile secretion function correctly. bile secretion malfunction HOIP_0001344 HOIP:HOIP_0001345 Cholestasis (primitive process) is a subtype of stagnating: A process that changes the bile flow to be slower due to obstruction. cholestasis (primitive process) HOIP_0001345 HOIP:HOIP_0001346 Inreasing blood ALP concentration is a subtype of increasing concentration: A process that changes the bilirubin concentration in the blood to be higher. http://purl.bioontology.org/ontology/MEDDRA/10001771 http://purl.bioontology.org/ontology/OMIM/MTHU010336 inreasing blood ALP concentration HOIP_0001346 HOIP:HOIP_0001347 Increasing γ-glutamyltransferase concentration in blood is a subtype of increasing concentration: A process that changes the γ-glutamyltransferase (GGT) concentration to be higher. increasing γ-glutamyltransferase concentration in blood HOIP_0001347 HOIP:HOIP_0001348 Hypofunction of bilirubin excretion is a subtype of hypofunction of liver's excretion: A process that performs a decreased or insufficient bilirubin excretion. hypofunction of bilirubin excretion HOIP_0001348 HOIP:HOIP_0001349 Increasing bilirubin concentration in blood is a subtype of increasing concentration: A process that changes the bilirubin concentration in the blood to be higher. increasing bilirubin concentration in blood HOIP_0001349 HOIP:HOIP_0001350 Jaundice is a changing process that generally changes the color of the skin or eyes into yellow. jaundice (Process) HOIP_0001350 HOIP:HOIP_0001351 A class of lipoproteins of large size (30-80 nm), very low density (0.93-1.006 g/ml) particles with a core composed mainly of triglycerides and a surface monolayer of phospholipids and cholesterol into which are imbedded the apolipoproteins B, E, and C. VLDL facilitate the transport of endogenously made triglycerides to extrahepatic tissues. very-low-density lipoproteins VLDL (canonical)[lipidosis] HOIP_0001351 HOIP:HOIP_0001352 Hypofunction of blood coagulation factor synthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient blood coagulation factor synthesis. hypofunction of blood coagulation factor synthesis HOIP_0001352 HOIP:HOIP_0001353 A process that emits blood. hemorrhage bleeding HOIP_0001353 HOIP:HOIP_0001354 Hypofunction of detoxification is a subtype of hypofunctioning: A process that performs a decreased or insufficient detoxification. hypofunction of detoxification HOIP_0001354 HOIP:HOIP_0001355 Increasing ammonia concentration in blood is a subtype of increasing concentration: A process that changes the ammonia concentration in the blood to be higher. increasing ammonia concentration in blood HOIP_0001355 HOIP:HOIP_0001356 The directed movement of VLDL, out of a hepatocyte. VLDL release from hepatocyte HOIP_0001356 HOIP:HOIP_0001358 Hepatic shunt formtion is a subtype of biological structure formation: A process that makes abnormal communications between the hepatic arteries, portal veins, and hepatic or systemic veins. It makes abnormal communications between the hepatic arteries, portal veins, and hepatic or systemic veins. It makes abnormal communications between the hepatic arteries, portal veins, and hepatic or systemic veins. hepatic shunt formtion HOIP_0001358 It makes abnormal communications between the hepatic arteries, portal veins, and hepatic or systemic veins. PMID:15143226 HOIP:HOIP_0001359 Increasing hepatic portal pressure is a subtype of increasing pressure: A process that changes the hepatic portal pressure to be higher. increasing hepatic portal pressure HOIP_0001359 HOIP:HOIP_0001360 Increasing size of the spleen is a subtype of increasing size: A process that changes the size of the of the spleen to be larger. splenomegaly increasing size of the spleen HOIP_0001360 HOIP:HOIP_0001361 Spleen hyperfunction is a subtype of hyperfunctioning: A process that performs an excessive spleen function. spleen hyperfunction HOIP_0001361 HOIP:HOIP_0001362 Decreasing hemoglobin concentration in blood is a subtype of decreasing concentration: A process that changes the concentration of the hemoglobin in the blood to be lower. decreasing hemoglobin concentration in blood HOIP_0001362 HOIP:HOIP_0001363 Bypass formation is a subtype of biological structure formation: A process that constructs an alternate passage of a bodily substancepassage carrying blood. bypass formation HOIP_0001363 HOIP:HOIP_0001364 Varicosity of veins formation is a subtype of biological structure formation: A process that have a varicosity of veins. PMID:18453484 varicosity of veins formation HOIP_0001364 HOIP:HOIP_0001365 Stomach congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the stomach. stomach congestion HOIP_0001365 HOIP:HOIP_0001366 Increasing hepatic venous pressure is a subtype of increasing pressure: A process that changes the hpatic venous pressure to be higher. increasing hepatic venous pressure HOIP_0001366 HOIP:HOIP_0001367 Hyperfunction of hepatic lymph production is a subtype of hyperfunction of biosynthesis: A process that performs an excessive hepatic lymph production. hyperfunction of hepatic lymph production HOIP_0001367 HOIP:HOIP_0001368 Hepatic lymph leakage is a subtype of leaking: A process that leaks lymph out from the liver lymphatic vessel. hepatic lymph leakage HOIP_0001368 HOIP:HOIP_0001369 Ascites (process) is a subtype of accumulation of fluids: A process that keeps fluid in the peritoneal cavity. ascites (process) HOIP_0001369 HOIP:HOIP_0001370 NRF2 activation by PERK is a subtype of NRF2 activation: A process that changes the activity of NRF2 (Nuclear Factor, Erythroid 2 Like 2) to be higher by PERK. NRF2 activation by PERK HOIP_0001370 HOIP:HOIP_0001371 The directed movement of VLDL, out of a hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). VLDL release from hepatocyte [lipidosis (normal course)] HOIP_0001371 HOIP:HOIP_0001372 Increasing aldosterone concentration in blood is a subtype of increasing concentration: A process that changes the aldosterone concentration in the blood to be higher. increasing aldosterone concentration in blood HOIP_0001372 HOIP:HOIP_0001373 A role played by a chemical compound exihibiting itself through the ability to induce damage to the kidney in animals. nephrotoxicant nephrotoxic agent HOIP_0001373 HOIP:HOIP_0001374 Edema is a subtype of accumulation of fluids: A process that keeps an excessive fluid in cells or intercellular tissues. HP:0000969 edema (process) HOIP_0001374 HP:0000969 Edema may be related to one or more of the following factors: 1) increased capillary hydrostatic pressure, 2) decreased osmotic pressure of plasma, 3) decreased tissue tension and lymphatic drainage, 4) increased osmotic pressure of tissue fluids, and 5) increased capillary permeability. HOIP:HOIP_0001375 Hypofunction of hormone metabolic process is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient hormone metabolic process. hypofunction of hormone metabolic process HOIP_0001375 HOIP:HOIP_0001376 Hypofunction of estrogen degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient estrogen degradation. hypofunction of estrogen degradation HOIP_0001376 HOIP:HOIP_0001377 Increasing estrogen concentration in blood is a subtype of increasing concentration: A process that changes the estrogen concentration in the blood to be higher. increasing estrogen concentration in blood HOIP_0001377 HOIP:HOIP_0001378 Hyperfunction of glutathione synthetic gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive glutathione synthetic gene expression. hyperfunction of glutathione synthetic gene expression HOIP_0001378 HOIP:HOIP_0001379 Lipid degradtion related gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature lipid degradation related gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). lipid degradation related gene expression [lipidosis (normal course)] HOIP_0001379 HOIP:HOIP_0001380 Leaking fluid from blood vessel is a subtype of leaking: A process that leaks fluid out from the blood vessel. leaking fluid from blood vessel HOIP_0001380 HOIP:HOIP_0001381 Lipid degradtion related gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature lipid degradation related gene product or products (proteins or RNA). lipid degradation related gene expression HOIP_0001381 HOIP:HOIP_0001382 growth factor family HOIP_0001382 HOIP:HOIP_0001383 Lipid synthesis gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature lipid synthesis gene product or products (proteins or RNA). lipid synthesis gene expression HOIP_0001383 HOIP:HOIP_0001384 MMP inactivation by TIMP1 is a subtype of inactivating: A process that changes the activity of the MMP to be lower by TIMP1. MMP inactivation by TIMP1 HOIP_0001384 HOIP:HOIP_0001385 Catalysis role of the transfer of an acyl group from one compound (donor) to another (acceptor). EC:2.3. GO:0008415 acyltransferase HOIP_0001385 HOIP:HOIP_0001386 Lipid synthesis gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature lipid synthesis gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). lipid synthesis gene expression [lipidosis (normal course)] HOIP_0001386 HOIP:HOIP_0001387 Fatty acid strorage is a subtype of accumulation of substances in a biological object: A process that keeps fatty acid in a biological object. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis by alcoholic liver injury. fatty acid strorage [hepatic fibrosis by alcoholic liver injury] HOIP_0001387 HOIP:HOIP_0001388 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid in the mitochondria. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). mitochondrial fatty acid beta-oxidation HOIP_0001388 HOIP:HOIP_0001389 Negative regulation of lipid transport from liver to peripheral tissue is a subtype of negative regulation of lipid transport: A process that stops, prevents, or reduces the frequency, rate or extent of lipid transport from liver to peripheral tissue. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. negative regulation of lipid transport from liver to peripheral tissue [hepatic fibrosis course] HOIP_0001389 HOIP:HOIP_0001390 A fatty acid oxidation process that results in the complete beta oxidation of a fatty acid in the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course) mitochondrial fatty acid beta-oxidation [lipidosis (normal course)] HOIP_0001390 HOIP:HOIP_0001391 Negative regulation of lipid transport is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. negative regulation of lipid transport HOIP_0001391 HOIP:HOIP_0001392 Bcl2 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into Bcl2. Bcl2 phosphorylation HOIP_0001392 HOIP:HOIP_0001393 A role played by the entity which transmits from A to B. transmitter role HOIP_0001393 HOIP:HOIP_0001394 NCBI-Human-GeneID:2194 PMID:10962028 FATTY Acid Synthase (canonical)[lipidosis] HOIP_0001394 NCBI-Human-GeneID:2194 http://www.ncbi.nlm.nih.gov/gene/2194 HOIP:HOIP_0001397 Catalysis role of the reaction: acetyl-CoA + histone = CoA + acetyl-histone. EC:2.3.1.48 acetyl-CoA:histone acetyltransferase histone acetylase related molecular function GO:0004402 histone acetyltransferase HOIP_0001397 HOIP:HOIP_0001398 CAD insertion into phospholipase binding site to lysosomal inner membrane is a subtype of binding: A process that CAD inserts and replaces the phospholipase binding site in the lysosomal inner membrane. Under normal conditions, lysosomal phospholipase A2 is bound through electrostatic charge interactions to the inner membranes of the lysosome. A cationic amphiphile, accumulates in the lysosome and inserts into the inner membrane decreasing or eliminating the anionic binding sites for the lipase. The lipase is no longer able to bind to its substrates and is potentially susceptible to degradation by lysosomal proteases. CAD insertion into phospholipase binding site to lysosomal inner membrane HOIP_0001398 HOIP:HOIP_0001399 CAD insertion into phospholipase binding site to lysosomal inner membrane is a subtype of binding: A process that CAD inserts and replaces the phospholipase binding site in the lysosomal inner membrane. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). PMID:22960355 CAD insertion into phospholipase binding site to lysosomal inner membrane [phospholipidosis (imbalance course)] HOIP_0001399 PMID:22960355 Under normal conditions, lysosomal phospholipase A2 is bound through electrostatic charge interactions to the inner membranes of the lysosome. A cationic amphiphile, accumulates in the lysosome and inserts into the inner membrane decreasing or eliminating the anionic binding sites for the lipase. The lipase is no longer able to bind to its substrates and is potentially susceptible to degradation by lysosomal proteases. HOIP:HOIP_0001400 increasing number of damaged lysosomes is a subtype of increasing number : A process that becomes larger in the number of damaged lysosomes. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). increasing number of damaged lysosomes [phospholipidosis (severe)] HOIP_0001400 HOIP:HOIP_0001401 NCBI-Human-GeneID:31 NCBI-Mouse-GeneID:107476 NCBI-Rat-GeneID:60581 PMID:28290443 ACC1 (canonical)[lipidosis] HOIP_0001401 NCBI-Human-GeneID:31 http://www.ncbi.nlm.nih.gov/gene/31 NCBI-Mouse-GeneID:107476 http://www.ncbi.nlm.nih.gov/gene/107476 NCBI-Rat-GeneID:60581 http://www.ncbi.nlm.nih.gov/gene/60581 HOIP:HOIP_0001402 Negative regulation of phospholipid binding is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid binding. negative regulation of phospholipid binding HOIP_0001402 HOIP:HOIP_0001403 Negative regulation of phospholipase-mediated phospholipid degradation by CAD is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase-mediated phospholipid deradation regulated by CAD. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). negative regulation of phospholipase-mediated phospholipid degradation by CAD [phospholipidosis (mild)] HOIP_0001403 HOIP:HOIP_0001404 Negative regulation of phospholipase binding to phospholipid by CAD is a subtype of negative regulation of phospholipid binding: A process that stops, prevents, or reduces the frequency, rate or extent of phosphholipid binding by phospholipase. negative regulation of phospholipase binding to phospholipid by CAD HOIP_0001404 HOIP:HOIP_0001406 The chemical reactions and pathways resulting in the breakdown of phospholipids, any lipid containing phosphoric acid as a mono- or diester. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). phospholipid degradation phospholipid catabolic process [phospholipidosis (normal course)] HOIP_0001406 HOIP:HOIP_0001407 Negative regulation of lipid transport from liver to peripheral tissue is a subtype of negative regulation of lipid transport: A process that stops, prevents, or reduces the frequency, rate or extent of lipid transport from liver to peripheral tissue. negative regulation of lipid transport from liver to peripheral tissue HOIP_0001407 HOIP:HOIP_0001408 Increasing production amount of acetaldehyde is a subtype of increasing quantity: A process that changes the production amount of acetaldehyde to be higher. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis by alcoholic liver injury. increasing production amount of acetaldehyde [hepatic fibrosis by alcoholic liver injury] HOIP_0001408 HOIP:HOIP_0001409 Increasing production amount of acetaldehyde is a subtype of increasing quantity: A process that changes the production amount of acetaldehyde to be higher. increasing production amount of acetaldehyde HOIP_0001409 HOIP:HOIP_0001410 Hyperfunction of phospholipid biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive phospholipid biosynthesis. hyperfunction of phospholipid biosynthesis HOIP_0001410 HOIP:HOIP_0001411 Hyperfunction of glycerophospholipid biosynthesis is a subtype of hyperfunction of phospholipid biosynthesis: A process that performs an excessive glycerophospholipid biosynthesis. hyperfunction of glycerophospholipid biosynthesis HOIP_0001411 HOIP:HOIP_0001412 Increasing number of macrophage derived foam cell is a subtype of increasing number of objects: A process that becomes larger in the number of foam cell, a type of macrophage containing lipids in small vacuoles, in the liver. increasing number of macrophage derived foam cell HOIP_0001412 HOIP:HOIP_0001413 Hypofunction of ceramide synthesis is a subtype of hypofunction of lipid biosynthesis: A process that performs a decreased or insufficient ceramide biosynthesis. hypofunction of ceramide biosynthesis HOIP_0001413 HOIP:HOIP_0001414 eIF2a translation regulation system is a subtype of pathway system. This entity has sub-parts and has a goal of regulating translation by eIF2a as a systemic context. eIF2a translation regulation system HOIP_0001414 HOIP:HOIP_0001415 Hyperfunction of choline transport is a subtype of hyperfunction of transport: A process that performs an excesssive choline transport. hyperfunction of choline transport HOIP_0001415 HOIP:HOIP_0001417 DGAT(mol) HOIP_0001417 HOIP:HOIP_0001418 Hypofunction of glycerophospholipid degradation is a subtype of hypofunction of phospholipid degradation: A process that performs a decreased or insufficient glycerophospholipid degradation. hypofunction of glycerophospholipid degradation HOIP_0001418 HOIP:HOIP_0001419 Increaseing production quantity of catecholamine is a subtype of increasing quantity: A process that changes the production amount of catecholamine to be higher. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. increaseing production quantity of catecholamine [hepatic fibrosis course] HOIP_0001419 HOIP:HOIP_0001420 Hypofunction of phosphatidylcholine degradation is a subtype of hypofunction of glycerophospholipid degradation: A process that performs a decreased or insufficient phosphatidylserine degradation. hypofunction of phosphatidylcholine degradation HOIP_0001420 HOIP:HOIP_0001421 Increaseing production quantity of catecholamine is a subtype of increasing quantity: A process that changes the production amount of catecholamine to be higher. increaseing production quantity of catecholamine HOIP_0001421 HOIP:HOIP_0001423 NCBI-Human-GeneID:8694 NCBI-Mouse-GeneID:13350 NCBI-Rat-GeneID:84497 DGAT1 (mol) HOIP_0001423 NCBI-Human-GeneID:8694 http://www.ncbi.nlm.nih.gov/gene/8694 NCBI-Mouse-GeneID:13350 http://www.ncbi.nlm.nih.gov/gene/13350 NCBI-Rat-GeneID:84497 http://www.ncbi.nlm.nih.gov/gene/84497 HOIP:HOIP_0001424 Fatty Acid Synthase FASN HOIP_0001424 HOIP:HOIP_0001426 Arole played by the entity that has both hydrophobic and hydrophilic properties with a charged cationic amine group. CADs exhibit the property of lysosomotropism, the property of a molecule to specifically associate with lysosomes. In theory, CADs could enter the lysosome through endocytosis, autophagy, or a drug-specific transporter. However, passive diffusion has been invoked as the major mechanism whereby CADs accumulate within the lysosome . CADs bind directly to phospholipids to result in indigestible drug–lipid complexes, which accumulate and are stored in the form of lysosomal lamellar bodies. Production of lamellar bodies was associated with inhibition of phospholipase activity; either due to direct inhibition or interaction of CAD at the phospholipid bilayer of the lysosome. CADs exhibit the property of lysosomotropism, the property of a molecule to specifically associate with lysosomes. In theory, CADs could enter the lysosome through endocytosis, autophagy, or a drug-specific transporter. However, passive diffusion has been invoked as the major mechanism whereby CADs accumulate within the lysosome . CADs bind directly to phospholipids to result in indigestible drug–lipid complexes, which accumulate and are stored in the form of lysosomal lamellar bodies. Production of lamellar bodies was associated with inhibition of phospholipase activity; either due to direct inhibition or interaction of CAD at the phospholipid bilayer of the lysosome. PMID:9061852 CAD role Cationic Amphiphilic Drug role HOIP_0001426 CADs exhibit the property of lysosomotropism, the property of a molecule to specifically associate with lysosomes. In theory, CADs could enter the lysosome through endocytosis, autophagy, or a drug-specific transporter. However, passive diffusion has been invoked as the major mechanism whereby CADs accumulate within the lysosome . CADs bind directly to phospholipids to result in indigestible drug–lipid complexes, which accumulate and are stored in the form of lysosomal lamellar bodies. Production of lamellar bodies was associated with inhibition of phospholipase activity; either due to direct inhibition or interaction of CAD at the phospholipid bilayer of the lysosome. PMID:16979167 PMID:9061852 Cationic amphiphilic drug-induced phospholipidosis. Xenobiotics or their metabolites that induce phospholipidosis. Each of these drugs shares several common physiochemical properties: hydrophobic ring structure on the molecule and a hydrophilic side chain with a charged cationic amine group, hence the class term cationic amphiphilic drugs (CADs). The hydrophobic structure enhances the molecule’s ability pass through plasma membranes when are they to not ionized. HOIP:HOIP_0001427 The multiplication or reproduction of cells, resulting in the rapid expansion of a cell population. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). cell proliferation [phospholipidosis (normal course)] HOIP_0001427 HOIP:HOIP_0001428 NCBI-Human-GeneID:19 NCBI-Mouse-GeneID:107476 NCBI-Rat-GeneID:60581 PMID:28290443 ATP Binding Cassette Subfamily A Member 1 [lipidosis] ABCA1 (canonical)[lipidosis] HOIP_0001428 NCBI-Human-GeneID:19 http://www.ncbi.nlm.nih.gov/gene/19 NCBI-Mouse-GeneID:107476 http://www.ncbi.nlm.nih.gov/gene/107476 NCBI-Rat-GeneID:60581 http://www.ncbi.nlm.nih.gov/gene/60581 HOIP:HOIP_0001429 CHOP gene expression regulation system is a subtype of pathway system. This entity has sub-parts and has a goal of regulating gene expressions by CHOP as a systemic context. CHOP gene expression regulation system HOIP_0001429 HOIP:HOIP_0001430 Hyperfunction of phospholipid degradation is a subtype of hyperfunction of decompoing: A process that performs an excessive phospholipid degradation. hyperfunction of phospholipid degradation HOIP_0001430 HOIP:HOIP_0001433 Dysfunction of protein refolding is a subtype of dysfunctioning: A process that performs an abnormal and incomplete protein refolding. dysfunction of protein refolding HOIP_0001433 HOIP:HOIP_0001434 Phospholipid metabolism balance is a subtype of maintaining balance: A process that keeps a balance of phospholipid metabolism. phospholipid metabolism balance HOIP_0001434 HOIP:HOIP_0001435 Phospholipid metabolism balance is a subtype of maintaining balance: A process that keeps a balance of phospholipid metabolism. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). phospholipid metabolism balance [phospholipidosis (normal course)] HOIP_0001435 HOIP:HOIP_0001436 ATF6 gene expression regulation system is a subtype of pathway system. This entity has sub-parts and has a goal of regulating gene expressions by ATF6 as a systemic context. ATF6 gene expression regulation system HOIP_0001436 HOIP:HOIP_0001437 The totality of all processes through which the phospholipidosis is realized. This causal process is heredity. phospholipidosis (genetic) HOIP_0001437 HOIP:HOIP_0001438 Loss of phospholipid degradation is a subtype of loss of function (process): A process that results in no longer having a phospholipid degradation function or the process that gradually loses it. loss of phospholipid degradation HOIP_0001438 HOIP:HOIP_0001440 Loss of structure is a subtype of changing structure: A process that lacks the structure or decreases structural parts. loss of structure HOIP_0001440 HOIP:HOIP_0001441 Genetic defect is a subtype of structural defect: A process in which a part of a chromosome or a sequence of DNA is lost during DNA replication. wikipedia: Deletion_(genetics) genetic defect HOIP_0001441 HOIP:HOIP_0001442 in vitro (human) 24hr HOIP_0001442 HOIP:HOIP_0001443 NCBI-Human-GeneID:19 OMIM:600046 ATP Binding Cassette Subfamily A Member 1 ABCA1 (mol) HOIP_0001443 NCBI-Human-GeneID:19 http://www.ncbi.nlm.nih.gov/gene/19 HOIP:HOIP_0001444 Phopholipase gene mutation is a subtype of gene mutation: A process thatchanges the sequence of a phospholipase gene. phopholipase gene mutation HOIP_0001444 HOIP:HOIP_0001445 Sphingomyelinase gene mutation is a subtype of phopholipase gene mutation: A process that changes the sequence of a sphingomyelinase gene. sphingomyelinase gene mutation HOIP_0001445 HOIP:HOIP_0001446 Sphingomyelinase gene mutation is a subtype of phopholipase gene mutation: A process that changes the sequence of a sphingomyelinase gene. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B. sphingomyelinase gene mutation [course of Niemann–Pick disease type A and type B] HOIP_0001446 HOIP:HOIP_0001447 Dysfunction of phospholipid degradation is a subtype of dysfunctioning: A process that performs an abnormal and incomplete phospholipid degradation. dysfunction of phospholipid degradation HOIP_0001447 HOIP:HOIP_0001449 Cell rupture is the tearing apart of a cell. This entity is a specific course-dependent process. This process can constitute the course of necrosis. cell rupture [necrosis (course)] HOIP_0001449 HOIP:HOIP_0001450 Hypofunction of mitochondrial fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient mitochondrial fatty acid beta-oxidation. This entity is a specific course-dependent process. This process can constitute the course of glutathione depletion. hypofunction of mitochondrial fatty acid beta-oxidation [glutathione depletion (course)] HOIP_0001450 HOIP:HOIP_0001451 A role played by the entity which enables the directed movement of cholesterol into, out of or within a cell, or between cells. cholesterol transporter role HOIP_0001451 HOIP:HOIP_0001453 Malfunctioning of intracellular signal transduction is a subtype of malfunctioning process: A process that cannot perform signaling appropriately or cannot realize it at all. malfunctioning of intracellular signal transduction HOIP_0001453 HOIP:HOIP_0001454 Malfunctioning of receptor function is a subtype of malfunctioning process: A process that cannot perform a receiving function appropriately or cannot realize it at all. malfunctioning of receptor function HOIP_0001454 HOIP:HOIP_0001455 Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:26481188 autophagy in response to ER stress positive regulation of autophagy [ER stress] HOIP_0001455 PMID:26481188 Blocking autophagy enhances meloxicam lethality to hepatocellular carcinoma by promotion of endoplasmic reticulum stress. Blocking autophagy by 3-methyladenine (3-MA) or Atg5 siRNA knock-down enhanced meloxicam lethality for HCC by activation of ER stress-related apoptosis. In addition, GRP78 seemed to lead to autophagic activation via the AMPK-mTOR signalling pathway. Blocking AMPK with a chemical inhibitor inhibited autophagy suggesting that meloxicam-regulated autophagy requires activation of AMPK. ER stress and autophagy were involved in cell death evoked by meloxicam in HCC cells. This inhibition of autophagy to enhance meloxicam lethality, suggests a novel therapeutic strategy against HCC. HOIP:HOIP_0001456 Changing membrane potential is a subtype of changing quality: A process that changes the electrical potential across a membrane. changing membrane potential HOIP_0001456 HOIP:HOIP_0001457 A release process of the cholesterol from hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). cholesterol efflux from hepatoyte [lipidosis (normal course)] HOIP_0001457 HOIP:HOIP_0001458 Hypofunction of cholesterol transport from hepatocyte is a subtype of hypofunction of transport: A process that performs a decreased or insufficient cholesterol transport from hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). hypofunction of cholesterol export from hepatoyte [lipidosis (imbalance course)] HOIP_0001458 HOIP:HOIP_0001459 A value in comparison to something else. relative value HOIP_0001459 HOIP:HOIP_0001460 A value which is greater in comparison to something else. relative large (value) HOIP_0001460 HOIP:HOIP_0001461 A value which is greater in comparison to something else. relative small (value) HOIP_0001461 HOIP:HOIP_0001462 The totality of all processes through which the Niemann–Pick disease type A or type B is realized. This causal process is heredity. Niemann–Pick disease type A and type B are inherited as autosomal recessive deficiency of the enzyme sphingomyelinase, in the lysosomes of the reticuloendothelial system. This results in the lysosomal storage of sphingomyelin. The liver and spleen are predominantly involved. Sherlock's Diseases of the Liver and Biliary System, 12th Edition Niemann–Pick disease type A and type B are inherited as autosomal recessive deficiency of the enzyme sphingomyelinase, in the lysosomes of the reticuloendothelial system. This results in the lysosomal storage of sphingomyelin. The liver and spleen are predominantly involved. Sherlock's Diseases of the Liver and Biliary System, 12th Edition PMID:20111001 https://ghr.nlm.nih.gov/condition/niemann-pick-disease course of Niemann–Pick disease type A and type B HOIP_0001462 Niemann–Pick disease type A and type B are inherited as autosomal recessive deficiency of the enzyme sphingomyelinase, in the lysosomes of the reticuloendothelial system. This results in the lysosomal storage of sphingomyelin. The liver and spleen are predominantly involved. Sherlock's Diseases of the Liver and Biliary System, 12th Edition Online ISBN:9781444341294 Print ISBN:9781405134897 PMID:20111001 Hsp70 stabilizes lysosomes and reverts Niemann-Pick disease-associated lysosomal pathology. HOIP:HOIP_0001463 Phopholipase gene mutation is a subtype of gene mutation: A process thatchanges the sequence of a phospholipase gene. This process is dependent on the genetic and can constitute the course of Phospholipidosis (genetic). phopholipase gene mutation [phospholipidosis (genetic)] HOIP_0001463 HOIP:HOIP_0001465 The chemical reactions and pathways resulting in the breakdown of sphingophospholipids. sphingophospholipid breakdown sphingophospholipid catacolism sphingophospholipid degradation sphingophospholipid catabolic process HOIP_0001465 HOIP:HOIP_0001466 Moving fatty axid to the hepatocyte is a subtype of moving A to the inside of B: A process of the movement of fatty acid into a hepatocyte. moving fatty acid to the hepatocyte HOIP_0001466 HOIP:HOIP_0001467 Increaing in fatty acid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the fatty acid inflow into the hepatocyte to be larger. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. increaing in fatty acid inflow into hepatocyte [hepatic fibrosis course] HOIP_0001467 HOIP:HOIP_0001468 The totality of all processes through which the Niemann–Pick disease type A is realized. This causal process is heredity. PMID:16434659 PMID:24488099 https://ghr.nlm.nih.gov/condition/niemann-pick-disease https://omim.org/entry/257200 course of Niemann–Pick disease type A HOIP_0001468 PMID:16434659 Natural history of type A Niemann-Pick disease: possible endpoints for therapeutic trials. Neurology 66: 228-232, 2006. The clinical course in Type A Niemann-Pick disease is similar among affected patients and is characterized by a relentless neurodegenerative course that leads to death, usually within 3 years. PMID:24488099 High sphingomyelin levels induce lysosomal damage and autophagy dysfunction in Niemann Pick disease type A. Niemann Pick disease type A (NPA), which is caused by loss of function mutations in the acid sphingomyelinase (ASM) gene, is a lysosomal storage disorder leading to neurodegeneration. Undegraded molecules build up in neurons of acid sphingomyelinase knockout mice and in fibroblasts from NPA patients in which autophagolysosomes accumulate. The latter is not due to alterations in autophagy initiation or autophagosome-lysosome fusion but because of inefficient autophago-lysosomal clearance. T his, in turn, can be explained by lysosomal membrane permeabilization leading to cytosolic release of Cathepsin B. High sphingomyelin (SM) levels account for these effects as they can be induced in control cells on addition of the lipid and reverted on SM-lowering strategies in ASM-deficient cells. These results unveil a relevant role for SM in autophagy modulation and characterize autophagy anomalies in NPA, opening new perspectives for therapeutic interventions. https://ghr.nlm.nih.gov/condition/niemann-pick-disease Niemann-Pick disease type A usually develop an enlarged liver and spleen (hepatosplenomegaly) by age 3 months and fail to gain weight and grow at the expected rate (failure to thrive). The affected children develop normally until around age 1 year when they experience a progressive loss of mental abilities and movement (psychomotor regression). Children with Niemann-Pick disease type A also develop widespread lung damage (interstitial lung disease) that can cause recurrent lung infections and eventually lead to respiratory failure. All affected children have an eye abnormality called a cherry-red spot, which can be identified with an eye examination. Children with Niemann-Pick disease type A generally do not survive past early childhood. HOIP:HOIP_0001469 The totality of all processes through which the Niemann–Pick disease type B is realized. This causal process is heredity. PMID:20111001 https://ghr.nlm.nih.gov/condition/niemann-pick-disease https://omim.org/entry/607616 course of Niemann–Pick disease type B HOIP_0001469 https://ghr.nlm.nih.gov/condition/niemann-pick-disease PMID:20111001 Kirkegaard et al. (2010) showed that Hsp70 (140550) stabilizes lysosomes by binding to an endolysosomal anionic phospholipid bis(monoacylglycero)phosphate (BMP), an essential cofactor for lysosomal sphingomyelin metabolism. In acidic environments Hsp70 binds with high affinity and specificity to BMP, thereby facilitating the BMP binding and activity of acid sphingomyelinase (ASM). The inhibition of the Hsp70-BMP interaction by BMP antibodies or a point mutation in Hsp70 (trp90 to phe), as well as the pharmacologic and genetic inhibition of ASM, effectively reverted the Hsp70-mediated stabilization of lysosomes. Notably, the reduced ASM activity in cells from patients with Niemann-Pick disease A (257200) and B, severe lysosomal storage disorders caused by mutations in the sphingomyelin phosphodiesterase-1 gene (SMPD1; 607616) encoding ASM, is also associated with a marked decrease in lysosomal stability, and this phenotype could be effectively corrected by treatment with recombinant Hsp70. Kirkegaard et al. (2010) concluded that, taken together, their data opened exciting possibilities for the development of new treatments for lysosomal storage disorders and cancer with compounds that enter the lysosomal lumen by the endocytic delivery pathway. https://omim.org/entry/607616 Hsp70 stabilizes lysosomes and reverts Niemann-Pick disease-associated lysosomal pathology. Nature 463: 549-553, 2010. [ https://ghr.nlm.nih.gov/condition/niemann-pick-disease Niemann-Pick disease type B usually presents in mid-childhood. The signs and symptoms of this type are similar to type A, but not as severe. People with Niemann-Pick disease type B often have hepatosplenomegaly, recurrent lung infections, and a low number of platelets in the blood (thrombocytopenia). They also have short stature and slowed mineralization of bone (delayed bone age). About one-third of affected individuals have the cherry-red spot eye abnormality or neurological impairment. People with Niemann-Pick disease type B usually survive into adulthood. HOIP:HOIP_0001470 Retinal degeneration is a subtype of changing material: A process that degenerates retinal photoreceptors and pigmented epithelial cells. Detinal degenration is usually caused by the progressive cell death. retinal degeneration HOIP_0001470 HOIP:HOIP_0001471 Retinal degeneration is a subtype of changing material: A process that degenerates retinal photoreceptors and pigmented epithelial cells. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick Disease Type A. retinal degeneration [course of Niemann–Pick disease type A] HOIP_0001471 HOIP:HOIP_0001472 Dysfunction of sphingomyelin degradation in the myelin sheath is a subtype of dysfunction of phosphosphingolipid degradation: A process that performs an abnormal and incomplete sphingomyelin degradation in the myelin sheath. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. dysfunction of sphingomyelin degradation in the myelin sheath [course of Niemann–Pick disease type A] HOIP_0001472 HOIP:HOIP_0001473 Dysfunction of sphingomyelin degradation in the myelin sheath is a subtype of dysfunction of phosphosphingolipid degradation: A process that performs an abnormal and incomplete sphingomyelin degradation in the myelin sheath. dysfunction of sphingomyelin degradation in the myelin sheath HOIP_0001473 HOIP:HOIP_0001474 Dysfunction of phosphosphingolipid degradation is a subtype of dysfunction of phospholipid degradation: A process that performs an abnormal and incomplete phosphosphingolipid degradation. dysfunction of phosphosphingolipid degradation HOIP_0001474 HOIP:HOIP_0001475 Dysfunction of sphingomyelin degradation is a subtype of dysfunction of phosphosphingolipid degradation: A process that performs an abnormal and incomplete sphingomyelin degradation. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B. dysfunction of sphingomyelin degradation [course of Niemann–Pick disease type A and type B] HOIP_0001475 HOIP:HOIP_0001476 A process that becomes lacking a homeostastasis balance of the sphingomyelin metabolism. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B. sphingomyelin metabolism imbalance [course of Niemann–Pick disease type A and type B] HOIP_0001476 HOIP:HOIP_0001477 Pulmonary infection is a subtype of pathogen colonization: A process that makes pathogen such as microorganism (bacteria, virus, mycoplasma, etc.) present in the lung to increase the number. pulmonary infection HOIP_0001477 HOIP:HOIP_0001478 Pulmonary infection is a subtype of pathogen colonization: A process that makes pathogen such as microorganism (bacteria, virus, mycoplasma, etc.) present in the lung to increase the number. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B. pulmonary infection [course of Niemann–Pick disease type A and type B] HOIP_0001478 HOIP:HOIP_0001479 Decrease in platelet count is a subtype of decreasing number of objects: A process that becomes smaller in platelet count. thrombocytopenia decrease in platelet count HOIP_0001479 HOIP:HOIP_0001480 Decrease in platelet count is a subtype of decreasing number of objects: A process that becomes smaller in platelet count. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick Disease Type B. decrease in platelet count [course of Niemann–Pick disease type B] HOIP_0001480 HOIP:HOIP_0001481 Pulmonary infection is a subtype of pathogen colonization: A process that makes pathogen such as microorganism (bacteria, virus, mycoplasma, etc.) present in the lung to increase the number. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. pulmonary infection [course of Niemann–Pick disease type A] HOIP_0001481 HOIP:HOIP_0001482 A process that becomes lacking a homeostastasis balance of the sphingomyelin metabolism. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. sphingomyelin metabolism imbalance [course of Niemann–Pick disease type A] HOIP_0001482 HOIP:HOIP_0001483 Hyperfunction of phospholipid removing is a subtype of hyperfunctioning: A process that performs an excessive removal of phospholipids. hyperfunction of phospholipid removing HOIP_0001483 HOIP:HOIP_0001484 Hyperfunction of phospholipid removing is a subtype of hyperfunctioning: A process that performs an excessive removal of phospholipids. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). hyperfunction of phospholipid removing [phospholipidosis (severe (excessive defense))] HOIP_0001484 HOIP:HOIP_0001485 lysophagy is a subtype of autophagy: A process that becomes larger in the number of autodigestion of abnormal lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course) . lysophagy [phospholipidosis (normal course)] HOIP_0001485 HOIP:HOIP_0001486 Hyperfunction of immune response is a subtype of hyperfunctioning: A process that performs an excessive immune response. hyperfunction of immune response HOIP_0001486 HOIP:HOIP_0001487 Hyperfunction of immune response is a subtype of hyperfunctioning: A process that performs an excessive immune response. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). PMID:26241657 hyperfunction of immune response [phospholipidosis (severe (excessive defense))] HOIP_0001487 HOIP:HOIP_0001488 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). iflammation [Phospholipidosis (excessive defense)] inflammatory response [phospholipidosis (severe (excessive defense))] HOIP_0001488 HOIP:HOIP_0001489 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). regulation of cell cycle [phospholipidosis (severe (excessive defense))] HOIP_0001489 HOIP:HOIP_0001490 The multiplication or reproduction of cells, resulting in the rapid expansion of a cell population. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). cell proliferation [phospholipidosis (severe (excessive defense)) ] HOIP_0001490 HOIP:HOIP_0001491 Tumor cell proliferation is a subtype of cell proliferation: A process of the multiplication or reproduction of tumor cells, resulting in the rapid expansion of a tumor cell population. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)) . PMID:12069817 PMID:12414665 tumor cell proliferation [[phospholipidosis (severe (excessive defense)) ] HOIP_0001491 PMID:12069817 Phosphoinositide 3-kinases in lysophosphatidic acid signaling: regulation and cross-talk with the Ras/mitogen-activated protein kinase pathway. HOIP:HOIP_0001492 EGFR signaling is a subtype of signaling that a signal is transmitted by the EGFR (epidermal growth factor receptor) on the surface of a cell, starting with a ligand binding to a EGFR http://purl.obolibrary.org/obo/GO_0007173 EGFR signaling HOIP_0001492 HOIP:HOIP_0001493 EGFR signaling is a subtype of signaling that a signal is transmitted by the EGFR (epidermal growth factor receptor) on the surface of a cell, starting with a ligand binding to a EGFR This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)) . EGFR signaling [phospholipidosis (severe (excessive defense)) ] HOIP_0001493 PMID:12414665 HOIP:HOIP_0001494 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). http://purl.obolibrary.org/obo/GO_0043491 PKB signaling AKT signaling HOIP_0001494 HOIP:HOIP_0001495 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). phosphatidylinositol 3-kinase signaling [phospholipidosis (severe (excessive defense))] HOIP_0001495 HOIP:HOIP_0001497 The spread or migration of cancer cells from one part of the body (the organ in which it first appeared) to another. The secondary tumor contains cells that are like those in the original (primary) tumor. [def-source: NCI] This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). metastasis [phospholipidosis (severe (excessive defense))] HOIP_0001497 HOIP:HOIP_0001498 NCBI-Human-GeneID:948 NCBI-Mouse-GeneID:12491 NCBI-Rat-GeneID:29184 PMID:15677505 PMID:16407588 PMID:18242221 PMID:21145849 PMID:27034954 CD36 -translocator role [lipidosis] HOIP_0001498 NCBI-Human-GeneID:948 http://www.ncbi.nlm.nih.gov/gene/948 NCBI-Mouse-GeneID:12491 http://www.ncbi.nlm.nih.gov/gene/12491 NCBI-Rat-GeneID:29184 http://www.ncbi.nlm.nih.gov/gene/29184 PMID:16407588 Lipid metabolism and liver inflammation. I. Hepatic fatty acid uptake: possible role in steatosis. PMID:18242221 Hepatic fatty acid transporter Cd36 is a common target of LXR, PXR, and PPARgamma in promoting steatosis. Activation of LXR induced Cd36. Moreover, the hepatic steatosis induced by LXR agonists was largely abolished in Cd36 null mice. PXR can regulate Cd36 directly or through its activation of PPARgamma. Both LXR-mediated Cd36 regulation and PXR-mediated PPARgamma regulation are liver specific. PMID:21145849 AMPK activation promotes fatty acid uptake into the cell through the fatty acid transporter FAT/CD36 in addition to its stimulating role on mitochondrial fatty acid oxidation. PMID:27034954 VPA enhanced oleic acid- (OLA-) induced lipid accumulation in a dose-dependent manner in hepatocytes; this may be due to upregulated lipid uptake, triacylglycerol (TAG) synthesis, and lipid droplet formation. Following VPA treatment, the expression levels of genes encoding cluster of differentiation 36 (Cd36), low-density lipoprotein receptor-related protein 1 (Lrp1), diacylglycerol acyltransferase 2 (Dgat2), and perilipin 2 (Plin2) were increased. CD36 regulates lipid uptake in different cells via binding to different ligands including long-chain fatty acids and native/oxidized lipoproteins. Increased hepatic CD36 expression is highly correlated with human insulin resistance and nonalcoholic steatohepatitis (NASH) development HOIP:HOIP_0001499 A role played by the molecule which transfers free fatty acids. free fatty acid transporter role HOIP_0001499 HOIP:HOIP_0001500 Hyperfunction of uptaking fatty acid into liver is a a process that performs an excesssive uptaking of fatty acids into the iver. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). hyperfunction of uptaking fatty acid [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001500 HOIP:HOIP_0001501 Hyperfunction of uptaking fatty acid into liver is a a process that performs an excesssive uptaking of fatty acids into the iver. hyperfunction of uptaking fatty acid HOIP_0001501 HOIP:HOIP_0001503 Finding is a subtype of data item that the result (output) of an investigation or an image finding, or some combination thereof. finding HOIP_0001503 HOIP:HOIP_0001505 Changing time length is a subtype of changing quality: A process that changes the length of time. changing time length HOIP_0001505 HOIP:HOIP_0001507 A pathological finding is a subtype of finding, which is observed as the lesion based on the pathological morphology. pathological finding HOIP_0001507 HOIP:HOIP_0001508 myelin figure [Liver PathologicalFindings] is a type of finding observed in the liver. Based on pathological morphology, lesions are observed as myelin-like layered structures under electron microscopy. membranous cytoplasmic body myelinsome [Liver PathologicalFindings] myeloid body [Liver PathologicalFindings] myelin figure [Liver Pathological Findings] HOIP_0001508 HOIP:HOIP_0001509 GO:0004879 nuclear receptor family HOIP_0001509 HOIP:HOIP_0001510 An attribute value of a tumor. This entity is a subtype of categorical value, which is non-quantitative and is dependent on tumors. tumor value HOIP_0001510 HOIP:HOIP_0001511 A value of the attribute of tumors that progress, invade surrounding tissues or metastasize. neoplastic (value) HOIP_0001511 HOIP:HOIP_0001512 An attribute value of a tumor that does not progress, not invade surrounding tissues or not metastasize. non-neoplastic (value) HOIP_0001512 HOIP:HOIP_0001513 Signal integration system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals and a gene regulation as a systemic context. signal integration system HOIP_0001513 HOIP:HOIP_0001514 continuousness (attribute) HOIP_0001514 HOIP:HOIP_0001515 Catalysis role of the transfer of a phosphate group, usually from ATP, to a substrate molecule. EC:2.7. related molecular function GO:0016301 kinase HOIP_0001515 HOIP:HOIP_0001516 Negative regulation ofglycosylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of glycosylation. negative regulation of glycosylation HOIP_0001516 HOIP:HOIP_0001517 NCBI-Human-GeneID:283 NCBI-Mouse-GeneID:11727 NCBI-Rat-GeneID:305843 Ang (mol) HOIP_0001517 NCBI-Human-GeneID:283 http://www.ncbi.nlm.nih.gov/gene/283 NCBI-Mouse-GeneID:11727 http://www.ncbi.nlm.nih.gov/gene/11727 NCBI-Rat-GeneID:305843 http://www.ncbi.nlm.nih.gov/gene/305843 HOIP:HOIP_0001519 sequestering of triglyceride (mild) is a subtype of lipid strorage in hepatocyte: A process that keeps triglycerides in hepatocytes. And the degree is mild. This entity is a specific course-dependent process. This process can constitute the course of simple steatosis. sequestering of triglyceride in hepatocyte (mild) [simple steatosis] HOIP_0001519 HOIP:HOIP_0001520 Changing pH is a subtype of changing quality: A process that changes the pH of the object, which denotes the acidity of a solution in terms of activity of hydrogen ions (H+). changing pH HOIP_0001520 HOIP:HOIP_0001522 sequestering of triglyceride in hepatocyte is a subtype of lipid strorage in hepatocyte: A process that keeps triglycerides in hepatocytes. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). sequestering of triglyceride in hepatocyte [lipidosis (imbalance course)] HOIP_0001522 HOIP:HOIP_0001525 A physical attribute inhering in a bearer by virtue of the bearer's rate of change of the position velocity attribute HOIP_0001525 HOIP:HOIP_0001527 JNK activation by IRE1 is a subtype of JNK activation: A process that changes the activity of the JNK to be higher by IRE1. JNK activation by IRE1 HOIP_0001527 HOIP:HOIP_0001528 NCBI-Human-GeneID:2081 NCBI-Mouse-GeneID:78943 NCBI-Rat-GeneID:498013 ERN1 IRE1 (mol) HOIP_0001528 NCBI-Human-GeneID:2081 http://www.ncbi.nlm.nih.gov/gene/2081 NCBI-Mouse-GeneID:78943 http://www.ncbi.nlm.nih.gov/gene/78943 NCBI-Rat-GeneID:498013 http://www.ncbi.nlm.nih.gov/gene/498013 HOIP:HOIP_0001529 PERK signal integration system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals and a gene regulation via PERK as a systemic context. PERK signal integration system HOIP_0001529 HOIP:HOIP_0001530 JNK activation by IRE1 is a subtype of JNK activation: A process that changes the activity of the JNK to be higher by IRE1. This entity is a specific course-dependent process. This process can constitute the course of ER stress. JNK activation by IRE1 [ER stress] HOIP_0001530 HOIP:HOIP_0001531 A role that represses the rate, timing and/or magnitude of transcription of genetic information. trannscriptional repressor HOIP_0001531 HOIP:HOIP_0001533 PERK-eIF2a-ATF4 signal integration system is a subtype of PERK pathway system. This entity has sub-parts and has a goal of transmitting signals and a gene regulation via PERK, eIF2a, and ATF4 as a systemic context. PERK-eIF2a-ATF4 signal integration system HOIP_0001533 HOIP:HOIP_0001534 Sorting cargo transport signal is a subtype of extractng: A process that obtains a necessary cargo transport signal. PMID:12914695 sorting cargo transport signal HOIP_0001534 PMID:12914695 Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi. Cell, 114, 299-310 (2003) HOIP:HOIP_0001535 The totality of all processes through which the Niemann–Pick disease type C is realized. This causal process is heredity. PMID:18953351 PMID:21502308 PMID:9211850 https://ghr.nlm.nih.gov/condition/niemann-pick-disease#genes https://omim.org/entry/257220 https://omim.org/entry/607623 https://omim.org/entry/607625 under construction Niemann–Pick disease type C HOIP_0001535 PMID:18953351 NPC1 is involved in sphingosine efflux from lysosomes, and that lysosomal sphingosine accumulation in NPC alters intracellular calcium concentration and causes abnormal endocytic trafficking Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium. Nature Med. 14: 1247-1255, 2008. PMID:9211850 Murine model of Niemann-Pick C disease: mutation in a cholesterol homeostasis gene. Science 277: 232-235, 1997. https://ghr.nlm.nih.gov/condition/niemann-pick-disease#genes Mutations in either the NPC1 or NPC2 gene cause Niemann-Pick disease type C. The proteins produced from these genes are involved in the movement of lipids within cells. Mutations in these genes lead to a shortage of functional protein, which prevents movement of cholesterol and other lipids, leading to their accumulation in cells. Because these lipids are not in their proper location in cells, many normal cell functions that require lipids (such as cell membrane formation) are impaired. The accumulation of lipids as well as the cell dysfunction eventually leads to cell death, causing the tissue and organ damage seen in Niemann-Pick disease types C1 and C2. HOIP:HOIP_0001536 An attribute in which events occur in sequence. time attribute HOIP_0001536 HOIP:HOIP_0001537 Lysosomal cholesterol storage is a subtype of cholesterol storage: A process that keeps cholesterol in the lysosome. lysosomal cholesterol storage HOIP_0001537 HOIP:HOIP_0001538 Lysosomal cholesterol storage is a subtype of cholesterol storage: A process that keeps cholesterol in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick Disease Type C. lysosomal cholesterol storage [Niemann–Pick disease type C] HOIP_0001538 HOIP:HOIP_0001539 dysfunction of mitochondrial fatty acid beta-oxidation (severe) is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient fatty acid beta-oxidation severely. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). dysfunction of mitochondrial fatty acid beta-oxidation (severe) [non-alcoholic steatohepatitis (course)] HOIP_0001539 HOIP:HOIP_0001540 Hypofunction of ATP biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient ATP biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. hypofunction of ATP biosynthesis [alcoholic fatty liver] HOIP_0001540 HOIP:HOIP_0001541 Overeating is a subtype of increasing quantity: A process that changes the ingestion amount of food to be larger. overeating HOIP_0001541 HOIP:HOIP_0001542 A behavioral process associated with the intake of food. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). feeding behavior [phospholipidosis (severe)] HOIP_0001542 HOIP:HOIP_0001544 Catalysis role of the reaction: anandamide + H2O <=> arachidonate + ethanolaminium(1+) Catalysis role of the reaction: anandamide + H2O <=> arachidonate + ethanolaminium(1+) GO:0103073 anandamide amidohydrolase HOIP_0001544 Catalysis role of the reaction: anandamide + H2O <=> arachidonate + ethanolaminium(1+) EC:3.5.1.99 HOIP:HOIP_0001545 Hypofunction of phosphoethanolamine degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient phosphoethanolamine degradation. Decreasing phosphoethanolamine degradation is a subtype of decreasing functioning process of breakdown of phosphoethanolamine. hypofunction of phosphoethanolamine degradation HOIP_0001545 HOIP:HOIP_0001546 Regulation of hepatocyte cell cycle is a subtype of regulation of cell cycle: A process that modulates the frequency, rate or extent of hepatocyte cell cycle. This entity is a specific course-dependent process. This process can constitute the course of Hypertrophy. regulation of hepatocyte cell cycle [Hypertrophy] HOIP_0001546 HOIP:HOIP_0001547 P53 signaling is a process that a signal is transmitted by p53. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). PMID:17090686 p53 signaling [phospholipidosis (severe (excessive defense))] HOIP_0001547 HOIP:HOIP_0001548 Catalysis role of the reaction: erythro-5-hydroxy-L-lysine + GTP = 5-phosphonooxy-L-lysine + GDP + 2 H(+) EC:2.7.1.81 PMID:22241472 hydroxylysine kinase HOIP_0001548 PMID:22241472 Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine. J. Biol. Chem. 287: 7246-7255, 2012. [ HOIP:HOIP_0001550 Hypofunction of drug metabolism phase I is a subtype of hypofunction of drug metabolism: A process that performs a decreased or insufficient drug metabolism phase I. hypofunction of drug metabolism phase I HOIP_0001550 HOIP:HOIP_0001551 Hyperfunction of drug metabolism phase I is a subtype of hyperfunction of drug metabolism: A process that performs an excesssive drug metabolism phase I. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). hyperfunction of drug metabolism phase I [phospholipidosis (imbalance course)] HOIP_0001551 HOIP:HOIP_0001552 Cyp1 is a subtype of cytochrome P450. Cyp1 HOIP_0001552 HOIP:HOIP_0001553 Cyp2 is a subtype of cytochrome P450. Cyp2 HOIP_0001553 HOIP:HOIP_0001554 Cyp3 is a subtype of cytochrome P450. Cyp3 HOIP_0001554 HOIP:HOIP_0001555 Cyp4 is a subtype of cytochrome P450. Cyp4 HOIP_0001555 HOIP:HOIP_0001556 Hypofunction of cholesterol transport from lysosome is a subtype of hypofunction of transport: A process that performs a decreased or insufficient cholestsrol transport from lysosomes. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick type C. hypofunction of cholesterol transport in lysosome [Niemann–Pick disease type C] . HOIP_0001556 HOIP:HOIP_0001557 Cholesteroltransport gene mutation is a subtype of gene mutation: A process thatchanges the sequence of a cholesterol transport gene. This process is dependent on the genetic and can constitute the course of Niemann Pick Type C. cholesterol transport gene mutation [Niemann–Pick disease type C] HOIP_0001557 HOIP:HOIP_0001558 IPR:001128 PMID:16584116 http://purl.obolibrary.org/obo/CHEBI_38559 Cytochrome P450 HOIP_0001558 PMID:16584116 AAPS J. 2006 Mar 10;8(1):E101-11. Cytochrome P450s and other enzymes in drug metabolism and toxicity. HOIP:HOIP_0001559 Drug metabolism phase I by Cytochrome P450 is a subtype of drug metabolism phase I: A process that is biotransformed by cytochrome P450 (CYP) superfamily . NCIT:C91423 PMID:16584116 https://reactome.org/PathwayBrowser/#/R-HSA-211945&SEL=R-HSA-211981&PATH=R-HSA-1430728,R-HSA-211859 drug metabolism phase I by Cytochrome P450 HOIP_0001559 HOIP:HOIP_0001561 A role played by the entity to repair the damaged DNA. DNA repair agent role HOIP_0001561 HOIP:HOIP_0001565 Amitriptyline metabolism is a subtype of drug metabolism phase I by Cytochrome P450: A process that that is biotransformed of amitriptyline by cytochrome P450 (CYP) superfamily (CYP2D6, CYP1A2, and CYP2C9. ) amitriptyline metabolism phase I HOIP_0001565 HOIP:HOIP_0001567 A length quality value which is greater than the normal or average. short (value) long (value) HOIP_0001567 HOIP:HOIP_0001569 Decreasing ceramide is a subtype of decreasing lipid: A process that changes the quantity of the ceramide to be lower. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. decreasing ceramide [sphingomyelin disorder (course)] HOIP_0001569 HOIP:HOIP_0001570 Hepatocyte cell division is a subtype of cell division: The process resulting in division and partitioning of components of a heoatocyte cell to form more cells. hepatocyte cell division HOIP_0001570 HOIP:HOIP_0001571 PPARalpha inactivation is a subtype of inactivating: A process that changes the activity of the activating PPAR alpha ( (Peroxisome Proliferator Activated Receptor Alpha)) with a nuclear receptor role to be lower. PPAR alpha inactivation inactivating peroxisome proliferator-activated receptor alpha PPARalpha inactivation HOIP_0001571 HOIP:HOIP_0001572 CHEBI:23981 MeSH:D004983 ethanoleamines HOIP_0001572 HOIP:HOIP_0001573 MeSH:D019856 ethanoleamine HOIP_0001573 HOIP:HOIP_0001574 A length quality value which is small. short (value) HOIP_0001574 HOIP:HOIP_0001575 PERK-eIF2a-ATF4 signal integration system signal integration system is a subtype of PERK pathway system. This entity has sub-parts and has a goal of transmitting signals and a gene regulation via PERK, eIF2a, ATF4, and CHOP as a systemic context. PERK-eIF2a-ATF4-CHOP signal integration system HOIP_0001575 HOIP:HOIP_0001576 Glycerophospholipid metabolism balance is a subtype of phospholipid metabolism balance: A process that keeps a balance of glycerophospholipid metabolism. glycerophospholipid metabolism balance HOIP_0001576 HOIP:HOIP_0001578 Heoatocyte growth is a subtype of cell growth: A process that The process in which a hepatocyte, the main structural component of the liver, increases in size. heoatocyte growth HOIP_0001578 HOIP:HOIP_0001579 Phosphatidylcholine metabolism balance is a subtype of glycerophospholipid metabolism balance: A process that keeps a balance of phosphatidylcholine metabolism. phosphatidylcholine metabolism balance HOIP_0001579 HOIP:HOIP_0001580 Regulation of hepatocyte cell cycle [hypertrophy] is a subtype of regulation of cell cycle: A process that modulates the frequency, rate or extent of hepatocyte cell cycle. regulation of hepatocyte cell cycle [hypertrophy] HOIP_0001580 HOIP:HOIP_0001581 Stagnating is a subtype of decreasing velocity: A process that changes the flow velocity to be slower or stops it in progress. stagnating HOIP_0001581 HOIP:HOIP_0001583 Increasing phosphatidylcholine material is a subtype of increasing glycerophospholipid material: A process that changes the amount of phosphatidylcholine material to be larger. increasing phosphatidylcholine material HOIP_0001583 HOIP:HOIP_0001584 The chemical reactions and pathways involving a drug, a substance used in the diagnosis, treatment or prevention of a disease; as used here antibiotic substances (see antibiotic metabolism) are considered to be drugs, even if not used in medical or veterinary practice. This entity is a specific course-dependent process. This process can constitute the course of Ground glass appearance. drug metabolic process [Ground glass appearance] HOIP_0001584 HOIP:HOIP_0001585 Phosphatidylcholine metabolism imbalance is a subtype of glycerophospholipid metabolism imbalance : A process that becomes lacking a homeostastasis balance of phosphatidylcholine metabolism. phosphatidylcholine metabolism imbalance HOIP_0001585 HOIP:HOIP_0001587 Hyperfunction of Phosphatidylcholine synthesis gene expression is a subtype of hyperfunction of glycerophospholipid synthesis gene expression: A process that performs an excesssive phosphatidylcholine ssynthetic gene expression. hyperfunction of Phosphatidylcholine synthesis gene expression HOIP_0001587 HOIP:HOIP_0001589 Nuclear receptor inactivation is a subtype of inactivation : A process that changes the activity of the molecule with a nuclear receptor role to be lower. nuclear receptor inactivation nuclear receptor inactivation HOIP_0001589 HOIP:HOIP_0001590 Increasing distance between hepatocytes is a subtype of increasing distance between cells: A process that places a distance between hepatocytes. separating between hepatocytes increasing distance between hepatocytes HOIP_0001590 HOIP:HOIP_0001591 Drug metabolism phase II is a subtype of drug metabolic process: A process that of biotransformation reactions involving conjugate enabling efficient excretion. http://purl.bioontology.org/ontology/MESH/D050217 drug metabolism phase II HOIP_0001591 HOIP:HOIP_0001592 Increasing phosphatidylethanolamine material is a subtype of increasing glycerophospholipid material: A process that changes the amount of phosphatidylethanolamine material to be larger. increasing phosphatidylethanolamine material HOIP_0001592 HOIP:HOIP_0001594 Phosphatidylethanolamine metabolism imbalance is a subtype of glycerophospholipid metabolism imbalance : A process that becomes lacking a homeostastasis balance of phosphatidylethanolamine metabolism. phosphatidylethanolamine metabolism imbalance HOIP_0001594 HOIP:HOIP_0001595 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. negative regulation of apoptotic process [Phospholipidosis-sphingomyelin disorder] HOIP_0001595 HOIP:HOIP_0001596 Hyperfunctioning of phosphatidylethanolamine synthesis gene expression is a subtype of hyperfunction of glycerophospholipid synthesis gene expression: A process that performs an excesssive phosphatidylethanolamine synthetic gene expression. hyperfunctioning of phosphatidylethanolamine synthesis gene expression HOIP_0001596 HOIP:HOIP_0001598 Negative regulation of phosphatidylethanolamine degradation is a subtype of Negative regulation of glycerophospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phosphatidylethanolamine degradation. negative regulation of phosphatidylethanolamine degradation HOIP_0001598 HOIP:HOIP_0001599 The modification of a xenobiotic substance by the conjugation of glucuronic acid. The resultant glucuronosides are often much more water-soluble than the xenobiotic precursor, enabling efficient excretion. This entity is a specific course-dependent process. This process can constitute the course of Ground glass appearance. In the liver, bilirubin is conjugated with glucuronic acid by the enzyme glucuronyltransferase, making it soluble in water: the conjugated version is the main form of bilirubin present in the "direct" bilirubin fraction. Much of it goes into the bile and thus out into the small intestine. In the liver, bilirubin is conjugated with glucuronic acid by the enzyme glucuronyltransferase, making it soluble in water: the conjugated version is the main form of bilirubin present in the "direct" bilirubin fraction. Much of it goes into the bile and thus out into the small intestine. UGT1A1 responsible for conjugating bilirubin is inducible by CAR activators such as phenobarbital and scoparone. UGT1A1 responsible for conjugating bilirubin is inducible by CAR activators such as phenobarbital and scoparone. xenobiotic glucuronidation [Ground glass appearance] HOIP_0001599 In the liver, bilirubin is conjugated with glucuronic acid by the enzyme glucuronyltransferase, making it soluble in water: the conjugated version is the main form of bilirubin present in the "direct" bilirubin fraction. Much of it goes into the bile and thus out into the small intestine. https://en.wikipedia.org/wiki/Bilirubin UGT1A1 responsible for conjugating bilirubin is inducible by CAR activators such as phenobarbital and scoparone. ISBN:0071769234 HOIP:HOIP_0001600 Hyperfunction of phosphatidylinositol biosynthesis is a subtype of hyperfunction of glycerophospholipid biosynthesis: A process that performs an excessive phosphatidylinositol biosynthesis. hyperfunction of phosphatidylinositol biosynthesis HOIP_0001600 HOIP:HOIP_0001601 Hyperfunction of phosphatidylethanolamine biosynthesis is a subtype of hyperfunction of glycerophospholipid biosynthesis: A process that performs an excessive phosphatidylethanolamine biosynthesis. hyperfunction of phosphatidylethanolamine biosynthesis HOIP_0001601 HOIP:HOIP_0001602 Hyperfunction of phosphatidylglycerol biosynthesis is a subtype of hyperfunction of glycerophospholipid biosynthesis: A process that performs an excessive phosphatidylglycerol biosynthesis. hyperfunction of phosphatidylglycerol biosynthesis HOIP_0001602 HOIP:HOIP_0001603 Hyperfunction of phosphatidylcholine biosynthesis is a subtype of hyperfunction of glycerophospholipid biosynthesis: A process that performs an excessive phosphatidylcholine biosynthesis. hyperfunction of phosphatidylcholine biosynthesis HOIP_0001603 HOIP:HOIP_0001604 Hyperfunction of phosphatidyl-L-serine biosynthesis is a subtype of hyperfunction of glycerophospholipid biosynthesis: A process that performs an excessive phosphatidyl-L-serine biosynthesis. hyperfunction of phosphatidyl-L-serine biosynthesis HOIP_0001604 HOIP:HOIP_0001606 Increasing phosphatidylglycerol material is a subtype of increasing glycerophospholipid material: A process that changes the amount of phosphatidylglycerol material to be larger. increasing phosphatidylglycerol material HOIP_0001606 HOIP:HOIP_0001608 Phosphatidylglycerol metabolism imbalance is a subtype of glycerophospholipid metabolism imbalance : A process that becomes lacking a homeostastasis balance of phosphatidylglycerol metabolism. phosphatidylglycerol metabolism imbalance HOIP_0001608 HOIP:HOIP_0001610 Hypofunction of phosphatidylglycerol degradation is a subtype of hypofunction of glycerophospholipid degradation: A process that performs a decreased or insufficient phosphatidylglycerol degradation. hypofunction of phosphatidylglycerol degradation HOIP_0001610 HOIP:HOIP_0001611 Gene expression of cytochrome p450 is a subtype of gene expression: The process in which a gene sequence is converted into a mature cytochrome p450 gene product or products (proteins or RNA) . gene expression of cytochrome p450 HOIP_0001611 HOIP:HOIP_0001612 Hyperfunction of phosphatidylglycerol synthesis gene expression is a subtype of hyperfunction of glycerophospholipid synthesis gene expression: A process that performs an excesssive phosphatidylglycerol synthetic gene expression. hyperfunction of phosphatidylglycerol synthesis gene expression HOIP_0001612 HOIP:HOIP_0001614 Negative regulation of phosphatidylglycerol degradation is a subtype of Negative regulation of glycerophospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phosphatidylglycerol degradation. negative regulation of phosphatidylglycerol degradation HOIP_0001614 HOIP:HOIP_0001615 Smooth endoplasmic reticulum membrane organization is a subtype of endoplasmic reticulum membrane organization: A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts of a smooth endoplasmic reticulum membrane. smooth endoplasmic reticulum membrane organization HOIP_0001615 HOIP:HOIP_0001616 Changing color is a subtype of changing quality: A process that chnges the color of the object. changing color HOIP_0001616 HOIP:HOIP_0001617 Increasing distance between cells is a subtype of increasing distance: A process that places a distance between cells. separating between cells increasing distance between cells HOIP_0001617 HOIP:HOIP_0001618 PPARalpha inactivation is a subtype of inactivation: A process that changes the activity of the activating PPAR alpha (Peroxisome Proliferator Activated Receptor Alpha) with a nuclear receptor role to be lower. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). Reactome The set of genes regulated by PPAR-alpha is not fully known in humans, however many examples have been found in mice. Genes directly activated by PPAR-alpha contain peroxisome proliferator receptor elements (PPREs) in their promoters and include: 1) genes involved in fatty acid oxidation and ketogenesis (Acox1, Cyp4a, Acadm, Hmgcs2); 2) genes involved in fatty acid transport (Cd36, , Slc27a1, Fabp1, Cpt1a, Cpt2); 3) genes involved in producing fatty acids and very low density lipoproteins (Me1, Scd1); 4) genes encoding apolipoproteins (Apoa1, Apoa2, Apoa5); 5) genes involved in triglyceride clearance ( Angptl4); 6) genes involved in glycerol metabolism (Gpd1 in mouse); PMID:25703085 PMID:25450203 PPAR alpha inactivation [non-alcoholic steatohepatitis (course)] HOIP_0001618 PMID:25450203 PMID:25450203 PMID:25703085 Liver PPARα expression negatively correlated with the presence of NASH (p=0.001) and with severity of steatosis (p=0.003), ballooning (p=0.001), NASH activity score (p=0.008) and fibrosis (p=0.003). HOIP:HOIP_0001620 Phosphatidic acid degradation is a subtype of glycerophospholipid catabolic process: A process of the chemical reactions resulting in the breakdown of phosphatidic acid. phosphatic acid breakdown phosphatidic acid catabolic process phosphatidic acid catabolism phosphatidic acid degradation HOIP_0001620 HOIP:HOIP_0001622 Hyperfunction of phosphatidic acid biosynthesis is a subtype of hyperfunction of glycerophospholipid biosynthesis: A process that performs an excessive phosphatidic acid biosynthesis. hyperfunction of phosphatidic acid biosynthesis HOIP_0001622 HOIP:HOIP_0001623 Hyperfunction of drug metabolism phase I by Cytochrome P450 is a subtype of hyperfunction of drug metabolism phase I: A process that performs an excesssive drug metabolism phase I by Cytochrome P450. hyperfunction of drug metabolism phase I by Cytochrome P450 HOIP_0001623 HOIP:HOIP_0001624 Hyperfunction of phosphosphingolipid biosynthesis is a subtype of hyperfunction of phospholipid biosynthesis: A process that performs an excessive phosphosphingolipid biosynthesis. hyperfunction of phosphosphingolipid biosynthesis HOIP_0001624 HOIP:HOIP_0001625 Hyperfunction of sphingomyelin biosynthesis is a subtype of hyperfunction of phosphosphingolipid biosynthesis: A process that performs an excessive sphingomyelin biosynthesis. hyperfunction of sphingomyelin biosynthesis HOIP_0001625 HOIP:HOIP_0001626 ER stress response gene expression via PERK is a subtype of gene expression: The process in which a gene sequence is converted into a mature ER stress response gene product or products (proteins or RNA) by PERK. ER stress response gene expression via PERK HOIP_0001626 HOIP:HOIP_0001628 Increasing phosphatidic acid material is a subtype of increasing glycerophospholipid material: A process that changes the amount of phosphatidic acid material to be larger. increasing phosphatidic acid material HOIP_0001628 HOIP:HOIP_0001630 Increasing phosphatidylserine material is a subtype of increasing glycerophospholipid material: A process that changes the amount of phosphatidylserine material to be larger. increasing phosphatidylserine material HOIP_0001630 HOIP:HOIP_0001631 Increasing amount of foreign substance is a subtype of increasing quantity: A process that changes the amount of foreign substance to be higher. increasing amount of foreign substance HOIP_0001631 HOIP:HOIP_0001632 NCBI-Human-GeneID:5465 NCBI-Mouse-GeneID:19013 NCBI-Rat-GeneID:25747 Peroxisome Proliferator-Activated Receptor Alpha [lipidosis] PPAR alpha (canonical) [lipidosis] HOIP_0001632 NCBI-Human-GeneID:5465 http://www.ncbi.nlm.nih.gov/gene/5465 NCBI-Mouse-GeneID:19013 http://www.ncbi.nlm.nih.gov/gene/19013 NCBI-Rat-GeneID:25747 http://www.ncbi.nlm.nih.gov/gene/25747 HOIP:HOIP_0001633 Increasing amount of xenobiotics is a subtype of increasing amount of foreign substance: A process that changes the amount of xenobiotics to be higher. increasing amount of xenobiotics HOIP_0001633 HOIP:HOIP_0001634 acetaldehyde [Lipidosis] HOIP_0001634 HOIP:HOIP_0001635 Increasing amount of drug is a subtype of increasing amount of xenobiotics: A process that changes the amount of drug to be higher. increasing amount of drug HOIP_0001635 HOIP:HOIP_0001636 AMPK inactivation is a subtype of molecular inactivation: A process that changes the activity of the AMPK (AMP-activated protein kinase) to be lower. AMPK inactivation HOIP_0001636 HOIP:HOIP_0001638 AMPK inactivation is a subtype of molecular inactivation: A process that changes the activity of the AMPK (AMP-activated protein kinase) to be lower. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. AMPK is sensitive to energy charge, which is activated by an increase in the ratio of AMP/ATP. PMID:17854140 AMPK inactivation [alcoholic fatty liver]] HOIP_0001638 PMID:17854140 When ethanol is added to cultured hepatoma cells that oxidize ethanol, it induces transcription of an SREBP-regulated promoter and increases the levels of the mature form of SREBP-1. AMPK regulates the ethanol-elicited SREBP-1 activation and the development of steatosis. The mechanism of ethanol-elicited SREBP-1 activation is also partly due to inhibition of the AMP-activated protein kinase (AMPK), described in greater detail below. AMPK catalyzes the phosphorylation of target enzymes, some of which are important rate-limiting enzymes in hepatic lipid metabolism. By inhibiting the activity of AMPK, ethanol relieves suppression of SREBP-1, causing its activation and increasing its levels in the nucleus. HOIP:HOIP_0001639 Decreasing amount of drug is a subtype of decreasing amount of xenobiotics: A process that changes the quantity of the drug to be lower. decreasing amount of drug HOIP_0001639 HOIP:HOIP_0001640 Phosphatidylserine metabolism imbalance is a subtype of glycerophospholipid metabolism imbalance : A process that becomes lacking a homeostastasis balance of phosphatidylserine metabolism. phosphatidylserine metabolism imbalance HOIP_0001640 HOIP:HOIP_0001641 Removing myelin figure by Kupffer cell or macrophage is a subtype of removing: A process that takes myelin figure from a cell by Kupffer cells or macrophages. removing myelin figure by Kupffer cell or macrophage HOIP_0001641 HOIP:HOIP_0001642 Phosphatidic acid metabolism imbalance is a subtype of glycerophospholipid metabolism imbalance : A process that becomes lacking a homeostastasis balance of phosphatidic acid metabolism. phosphatidic acid metabolism imbalance HOIP_0001642 HOIP:HOIP_0001643 Removing myelin figure by Kupffer cell or macrophage is a subtype of removing: A process that takes myelin figure from a cell by Kupffer cells or macrophages. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). removing myelin figure by Kupffer cell or macrophage [phospholipidosis (severe (excessive defense))] HOIP_0001643 HOIP:HOIP_0001644 Phosphatidylinositol metabolism imbalance is a subtype of glycerophospholipid metabolism imbalance : A process that becomes lacking a homeostastasis balance of phosphatidylinositol metabolism. phosphatidylinositol metabolism imbalance HOIP_0001644 HOIP:HOIP_0001645 Lipid accumulation in hepatocyte is a subtype of lipid strorage in hepatocyte: A process that keeps lipids in hepatocytes mildly. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. lipid accumulation in hepatocyte [phospholipidosis via obese] HOIP_0001645 HOIP:HOIP_0001646 Hyperfunction of Phosphatidylserine synthesis gene expression is a subtype of hyperfunction of glycerophospholipid synthesis gene expression: A process that performs an excesssive phosphatidylserine synthetic gene expression. hyperfunction of Phosphatidylserine synthesis gene expression HOIP_0001646 HOIP:HOIP_0001648 Hypofunction of phosphatidylserine degradation is a subtype of hypofunction of glycerophospholipid degradation: A process that performs a decreased or insufficient phosphatidylcholine degradation. hypofunction of phosphatidylserine degradation HOIP_0001648 HOIP:HOIP_0001649 Keeping amount of drug is a subtype of keeping amount: A process that maintains the amount of the drug at a constant level . keeping amount of drug HOIP_0001649 HOIP:HOIP_0001650 Negative regulation of phosphatidylserine degradation is a subtype of Negative regulation of glycerophospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phosphatidylserine degradation. negative regulation of phosphatidylserine degradation HOIP_0001650 HOIP:HOIP_0001651 Cell rupture is the tearing apart of a cell. cell rupture HOIP_0001651 HOIP:HOIP_0001652 AMPK is a highly evolutionarily conserved serine/threonine kinase, and orthologs of the AMPK subunits are found in all eukaryotic species. At the molecular level, AMPK is a heterotrimer complex comprising a catalytic alpha subunit, with a conventional serine/threonine protein kinase domain, and two regulatory subunits, beta and gamma. In mammals, each subunit is encoded by multiple genes (alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3), which results in 12 possible combinations of AMPK complex. The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008] NCBI-Human-GeneID:5562 NCBI-Mouse-GeneID:105787 NCBI-Rat-GeneID:65248 PRKAA1 AMPK (canonical)[lipidosis] HOIP_0001652 NCBI-Human-GeneID:5562 http://www.ncbi.nlm.nih.gov/gene/5562 NCBI-Mouse-GeneID:105787 http://www.ncbi.nlm.nih.gov/gene/105787 NCBI-Rat-GeneID:65248 http://www.ncbi.nlm.nih.gov/gene/65248 HOIP:HOIP_0001653 Increasing phosphatidylinositol material is a subtype of increasing glycerophospholipid material: A process that changes the amount of phosphatidylinositol material to be larger. increasing phosphatidylinositol material HOIP_0001653 HOIP:HOIP_0001655 Hyperfunction of phosphatidylinositol synthetic gene expression is a subtype of hyperfunction of glycerophospholipid synthesis gene expression: A process that performs an excesssive phosphatidylinositol synthetic gene expression. hyperfunction of phosphatidylinositol synthetic gene expression HOIP_0001655 HOIP:HOIP_0001656 Chemical homeostasis imbalance is a subtype of homeostasis imbalance: A process that becomes lacking a chemical homeostastasis balance. chemical homeostasis imbalance HOIP_0001656 HOIP:HOIP_0001657 Hypofunction of phosphatidylinositol degradation is a subtype of hypofunction of glycerophospholipid degradation: A process that performs a decreased or insufficient phosphatidylinositol degradation. hypofunction of phosphatidylinositol degradation HOIP_0001657 HOIP:HOIP_0001658 Changing balance of drug metabolism is a subtype of changing balance: A process that that changes the balance between break down and the continued presence of the drug. changing balance of drug metabolism HOIP_0001658 HOIP:HOIP_0001659 Negative regulation of phosphatidylinositol degradation is a subtype of Negative regulation of glycerophospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phosphatidylinositol degradation. negative regulation of phosphatidylinositol degradation HOIP_0001659 HOIP:HOIP_0001660 Changing balance of drug metabolism is a subtype of changing balance: A process that that changes the balance between break down and the continued presence of the drug. This entity is a specific course-dependent process. This process can constitute the course of Ground glass appearance. changing balance of drug metabolism [Ground glass appearance] HOIP_0001660 HOIP:HOIP_0001661 Drug metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of drug metabolism. drug metabolism imbalance HOIP_0001661 HOIP:HOIP_0001662 Hyperfunction of hosphatidic acid gene expression is a subtype of hyperfunction of glycerophospholipid synthesis gene expression: A process that performs an excesssive phosphatidic acid synthetic gene expression. hyperfunction of hosphatidic acid gene expression HOIP_0001662 HOIP:HOIP_0001664 Hypofunction of phosphatidic acid degradation is a subtype of hypofunction of glycerophospholipid degradation: A process that performs a decreased or insufficient phosphatidic acid degradation. hypofunction of phosphatidic acid degradation HOIP_0001664 HOIP:HOIP_0001666 Negative regulation of phosphatidic acid degradation is a subtype of Negative regulation of glycerophospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phosphatidic acid degradation. negative regulation of phosphatidic acid degradation HOIP_0001666 HOIP:HOIP_0001669 Increasing sphingophopholipid material is a subtype of increasing materials for lipid formation: A process that changes the amount of sphingophopholipid material to be larger. increasing sphingophopholipid material HOIP_0001669 HOIP:HOIP_0001670 Increasing sphingomyelin material is a subtype of increasing sphingophopholipid material: A process that changes the amount of sphingomyelin material to be larger. increasing sphingomyelin material HOIP_0001670 HOIP:HOIP_0001671 Increasing sphingomyelin material is a subtype of increasing sphingophopholipid material: A process that changes the amount of sphingomyelin material to be larger. This process is dependent on the genetic and can constitute the course of Phospholipidosis (genetic). increasing sphingomyelin material [phospholipidosis (genetic)] HOIP_0001671 HOIP:HOIP_0001672 Sphingomyelin metabolism imbalance is a subtype of sphingophopholipid metabolism imbalance: A process that becomes lacking a homeostastasis balance of sphingomyelin metabolism. sphingomyelin metabolism imbalance HOIP_0001672 HOIP:HOIP_0001673 Increase in fatty acid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the fatty acid inflow into the hepatocyte to be larger. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. increase in fatty acid inflow into hepatocyte [Phpspholipidosis] HOIP_0001673 HOIP:HOIP_0001674 Hyperfunction of sphingomyelin synthetic gene expression is a subtype of hyperfunction of sphingophospholipid synthesis gene expression: A process that performs an excesssive sphingomyelin synthetic gene expression. hyperfunction of sphingomyelin synthetic gene expression HOIP_0001674 HOIP:HOIP_0001676 Hypofunction of sphingomyelin degradation is a subtype of hypofunction of phosphosphingolipid degradation: A process that performs a decreased or insufficient sphingomyelin degradation. hypofunction of sphingomyelin degradation HOIP_0001676 HOIP:HOIP_0001678 Negative regulation of sphingophopholipid degradation is a subtype of negative regulation of phospholipid degradation: Any process that stops, prevents, or reduces the frequency, rate or extent of the sphingophospholipid catabolic process. negative regulation of sphingophopholipid degradation HOIP_0001678 HOIP:HOIP_0001680 Negative regulation of sphingomyelin catabolic process is a subtype of negative regulation of sphingophopholipid degradation: Any process that stops, prevents, or reduces the frequency, rate or extent of the sphingomyelin catabolic process. negative regulation of sphingomyelin catabolic process HOIP_0001680 HOIP:HOIP_0001681 Hyperfunction of moving A to the inside of B is a subtype of hyperfunctioning: A process that performs an excesssive moving A to the inside of B. hyperfunction of moving A to the inside of B HOIP_0001681 HOIP:HOIP_0001682 A role played by the entity which receives energy and transmits operand(s). energy sensor HOIP_0001682 HOIP:HOIP_0001683 Any process involved in the maintenance of an internal steady state of phospholipid within an organism or cell. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). maintaining phospholipid homeostasis [phospholipidosis (normal course)] HOIP_0001683 HOIP:HOIP_0001684 Moving drug to the inside of liver is a subtype of moving A to the inside of B: A process that of the movement of drug into hepatocytes. moving drug to inside of hepatocyte HOIP_0001684 HOIP:HOIP_0001685 The totality of all processes through which the sphingomyelin disorder is realized. This causal process is heredity. sphingomyelin disorder (genetic) HOIP_0001685 HOIP:HOIP_0001686 Dysfunction of sphingomyelin degradation is a subtype of dysfunction of phosphosphingolipid degradation: A process that performs an abnormal and incomplete sphingomyelin degradation. dysfunction of sphingomyelin degradation HOIP_0001686 HOIP:HOIP_0001687 Dysfunction of sphingomyelin degradation is a subtype of dysfunction of phosphosphingolipid degradation: A process that performs an abnormal and incomplete sphingomyelin degradation. This process is dependent on the sphingomyelin disorder and can constitute the course of Phospholipidosis. dysfunction of sphingomyelin degradation [sphingomyelin disorder (genetic)] HOIP_0001687 HOIP:HOIP_0001688 Sphingomyelinase gene mutation is a subtype of phopholipase gene mutation: A process that changes the sequence of a sphingomyelinase gene. This process is dependent on the genetic and can constitute the course of Phospholipidosis (genetic). sphingomyelinase gene mutation [sphingomyelin disorder (genetic)] HOIP_0001688 HOIP:HOIP_0001689 Increasing pressure is a subtype of changing pressure: A process that changes the pressure of the object to be higher. related quality: http://purl.obolibrary.org/obo/PATO_0001576 increasing pressure HOIP_0001689 HOIP:HOIP_0001690 Sphingomyelin accumulation in lysosome is a subtype of sphingophospholipid accumulation in lysosome: A process that keeps sphingomyelin in the lysosome. This process is dependent on the sphingomyelin disorder and can constitute the course of Phospholipidosis (genetic). sphingomyelin accumulation in lysosome [sphingomyelin disorder (genetic)] HOIP_0001690 HOIP:HOIP_0001691 Sphingomyelin accumulation in lysosome of nervous system is a subtype of sphingomyelin accumulation in lysosome: A process that keeps sphingomyelin in the lysosome of nervous system. sphingomyelin accumulation in lysosome of nervous system HOIP_0001691 HOIP:HOIP_0001692 Severe sphingomyelin accumulation in lysosome of nervous system is a subtype of sphingomyelin accumulation in lysosome of nervous system: A process that keeps sphingomyelin in the lysosome of nervous system severely. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A (severe). sphingomyelin accumulation in lysosome of nervous system (severe) [course of Niemann–Pick disease type A] HOIP_0001692 HOIP:HOIP_0001693 Protein binding by NAPQI is a subtype of protein binding: Interacting between a protein and NAPQI. protein binding by NAPQI HOIP_0001693 HOIP:HOIP_0001694 Compound accumulation in liver is a subtype of accumulation of xenobiotics: A process that keeps compound in the liver. chemical compound accumulation in liver HOIP_0001694 HOIP:HOIP_0001695 Compound accumulation in lysosome is a subtype of accumulation of xenobiotics: A process that keeps compound in the lysosome. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID:24003057 chemical compound accumulation in lysosome [phospholipidosis (severe)] HOIP_0001695 PMID:15342952 PMID:24003057 From the LOPAC library we found that a group of tricyclic analogs including imipramine, clomipramine, trimipramine and amitriptyline used as antidepressant in the clinic were correctly identified as PLD inducers. HOIP:HOIP_0001696 PERK signal transduction system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals via PERK as a systemic context. PERK signal transduction system HOIP_0001696 HOIP:HOIP_0001697 Glycerophospholipid accumulation in lysosome is a subtype of phospholipid accumulation in lysosome: A process that keeps glycerophospholipid in the lysosome. glycerophospholipid accumulation in lysosome HOIP_0001697 HOIP:HOIP_0001698 Increase in fatty acid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the fatty acid inflow into the hepatocyte to be larger. The degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). increaing in fatty acid inflow into hepatocyte [Phpspholipidosis (severe)] HOIP_0001698 HOIP:HOIP_0001699 Leaking is a subtype of moving A to the outside of B: A process that lets gas or liquid flow through. leaking HOIP_0001699 HOIP:HOIP_0001700 Increase in fatty acid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the fatty acid inflow into the hepatocyte to be larger. The digree is moderate. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. increase in fatty acid inflow into hepatocyte [Phpspholipidosis(moderate)] HOIP_0001700 HOIP:HOIP_0001701 Phosphatidic acid accumulation in lysosome is a subtype of glycerophospholipid accumulation in lysosome: A process that keeps phosphatidic acid in the lysosome. phosphatidic acid accumulation in lysosome HOIP_0001701 HOIP:HOIP_0001702 Increasing phospholipid material is a subtype of increasing quantity: A process that changes the amount of phospholipid material to be larger. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). increasing phospholipid material [phospholipidosis (moderate)] HOIP_0001702 HOIP:HOIP_0001703 Phosphatidylserine accumulation in lysosome is a subtype of glycerophospholipid accumulation in lysosome: A process that keeps phosphatidylserine in the lysosome. phosphatidylserine accumulation in lysosome HOIP_0001703 HOIP:HOIP_0001704 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of phospholipids. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). hyperfunction of phospholipid biosynthesis [phospholipidosis (moderate) ] HOIP_0001704 HOIP:HOIP_0001705 Phosphatidylcholine accumulation in lysosome is a subtype of glycerophospholipid accumulation in lysosome: A process that keeps phosphatidylcholine in the lysosome. phosphatidylcholine accumulation in lysosome HOIP_0001705 HOIP:HOIP_0001706 S1P inactivation is a subtype of molecular inactivation: A process that changes the activity of the S1P (Sphingosine-1-phosphate) to be lower. S1P inactivation HOIP_0001706 HOIP:HOIP_0001707 Phosphatidylglycerol accumulation in lysosome is a subtype of glycerophospholipid accumulation in lysosome: A process that keeps phosphatidylglycerol in the lysosome. phosphatidylglycerol accumulation in lysosome HOIP_0001707 HOIP:HOIP_0001708 Hyperfunction of phospholipid biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive phospholipid biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). hyperfunction of phospholipid biosynthesis [phospholipidosis (severe)] HOIP_0001708 HOIP:HOIP_0001709 Phosphatidylethanolamine accumulation in lysosome is a subtype of glycerophospholipid accumulation in lysosome: A process that keeps phosphatidylethanolamine in the lysosome. phosphatidylethanolamine accumulation in lysosome HOIP_0001709 HOIP:HOIP_0001710 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of phospholipids. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. positive regulation of phospholipid biosynthetic process [phospholipidosis (imbalance course)] HOIP_0001710 HOIP:HOIP_0001712 PERK-eIF2a signal transduction system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals via PERK and eIF2a as a systemic context. PERK-eIF2a signal transduction system HOIP_0001712 HOIP:HOIP_0001713 PERK signal transduction system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals via PERK as a systemic context. This entity is dependent on ER stress. PERK signal transduction system [ER stress] HOIP_0001713 HOIP:HOIP_0001715 Course dependent process is a subtype of primitive process: A process that can constitute the specific course. course dependent process HOIP_0001715 HOIP:HOIP_0001716 Phospholipidosis dependent process is a subtype of course dependent process: A process that can constitute the course of phospholipidosis . PMID:1697167 phospholipidosis dependent process HOIP_0001716 HOIP:HOIP_0001717 ER stress dependent process is a subtype of course dependent process: A process that can constitute the course of endoplasmic reticulum stress. ER stress dependent process HOIP_0001717 HOIP:HOIP_0001718 Malfunctioning of hepatic blood circulation is a subtype of malfunctioning process: A process that cannot perform hepatic blood circulation function appropriately or cannot realize it at all. malfunctioning of hepatic blood circulation HOIP_0001718 HOIP:HOIP_0001720 Hepatic steatosis dependent process is a subtype of course dependent process: A process that can constitute the course of hepatic steatosis (fatty degeneration). hepatic steatosis dependent process HOIP_0001720 HOIP:HOIP_0001721 MMP inactivation by TIMP1 is a subtype of inactivating: A process that changes the activity of the MMP to be lower by TIMP1. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. MMP inactivation by TIMP1 [hepatic fibrosis course] HOIP_0001721 HOIP:HOIP_0001722 Hypofunction of ATP biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient ATP biosynthesis. hypofunction of ATP biosynthesis HOIP_0001722 HOIP:HOIP_0001723 Hypofunction of phospholipid deradation by phospholipase is a subtype of hypofunction of phospholipid degradation: A process that performs a decreased or insufficient phospholipid deradation by phospholipase. hypofunction of phospholipid deradation by phospholipase HOIP_0001723 HOIP:HOIP_0001724 Hyperfunction of increasing is a subtype of hyperfunctioning: A process that performs an excessive function of increasing. hyperfunction of increasing HOIP_0001724 HOIP:HOIP_0001725 PERK-eIF2a signal transduction system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals via PERK and eIF2a as a systemic context. This entity is dependent on the translation attenuation of ER stress. PERK-eIF2a signal transduction system HOIP_0001725 HOIP:HOIP_0001726 Hyperfunction of phospholipid synthesis gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive phospholipid synthetic gene expression. hyperfunction of phospholipid synthesis gene expression HOIP_0001726 HOIP:HOIP_0001727 Cell death dependent process is a subtype of course dependent process: A process that can constitute the course of hepatocyte cell death. cell death dependent process HOIP_0001727 HOIP:HOIP_0001730 Oxidative stress dependent process is a subtype of course dependent process: A process that can constitute the course of oxidative stress. oxidative stress dependent process HOIP_0001730 HOIP:HOIP_0001731 Course dependent chemical entity is a subtype of chemical entity. This entity can participate in a specific course. Course dependent chemical entity HOIP_0001731 HOIP:HOIP_0001732 ATF6 signal transduction system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals via ATF6 as a systemic context. ATF6 signal transduction system HOIP_0001732 HOIP:HOIP_0001734 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is step 3: a state of balance between demand activity and defense (supply) processes. balance state HOIP_0001734 HOIP:HOIP_0001735 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand); 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity indicates step 3: a state of imbalance between demand and defense processes. imbalance state HOIP_0001735 HOIP:HOIP_0001736 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity indicates step 1: a state of functioning (supplying) for biological defense and maintaining homeostasis. state of functional supply HOIP_0001736 HOIP:HOIP_0001737 Cell part damage is a subtype of damaging: A process that injures the structure of the cellular part as the direct or indirect result of an external force. cell part damage HOIP_0001737 HOIP:HOIP_0001738 Membrane damage is a subtype of damaging: A process that injures the structure of the membrane as the direct or indirect result of an external force. membrane damage HOIP_0001738 HOIP:HOIP_0001739 Dysfunction of mitochondrial fatty acid beta-oxidation (severe) is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient fatty acid beta-oxidation severely. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. dysfunction of mitochondrial fatty acid degradation [alcoholic fatty liver] HOIP_0001739 HOIP:HOIP_0001740 The level of degree is very high in comparison to the medium. very high level HOIP_0001740 HOIP:HOIP_0001741 Dysfunction of lipid degradation is a subtype of dysfunctioning: A process that performs an abnormal and incomplete lipid degradation. dysfunction of lipid degradation HOIP_0001741 HOIP:HOIP_0001742 The level of degree is middle. medium level HOIP_0001742 HOIP:HOIP_0001743 The level of degree is lower than medium. low level HOIP_0001743 HOIP:HOIP_0001744 Inflammasome activation is a subtype of activating: A process that changes the activity of the inflammasome to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). PMID:20303873 inflammasome activation [non-alcoholic steatohepatitis (course)] HOIP_0001744 PMID:20303873 NLRP3 agonists tested, including ATP and particulate activators, induce ROS and ROS blockade by chemical scavengers suppresses inflammasome activation. The source of ROS is currently unclear, but one or several NADPH oxidases are implicated, as suppression of the common p22 subunit inhibits inflammasome activation (Dostert et al., 2008); alternatively, ROS may be of mitochondrial origin. HOIP:HOIP_0001746 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) 3) balance/imbalance between demand and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity indicates step 2: a state of functional demand. functional demand state HOIP_0001746 HOIP:HOIP_0001747 Malfunctioning of mitochondrial ATP synthesis coupled electron transfer is a subtype of malfunctioning process: A process that cannot perform a respiratory electron transport chain appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). PMID:23299992 malfunctioning of mitochondrial ATP synthesis coupled electron transfer [non-alcoholic steatohepatitis (course)] HOIP_0001747 PMID:23299992 Furthermore, enhanced mtFAO without concomitant up‐regulation of the mitochondrial respiratory chain (MRC) activity induces reactive oxygen species (ROS) overproduction within different MRC components upstream of cytochrome c oxidase. This event seems to play a significant role in the initiation of oxidative stress and subsequent development of nonalcoholic steatohepatitis (NASH) in some individuals. Experimental investigations also pointed to a progressive reduction of MRC activity during NAFLD, which could impair energy output and aggravate ROS overproduction by the damaged MRC. Furthermore, high glucose levels promote ROS overproduction within hepatocytes, thus favoring oxidative stress and mitochondrial dysfunction. It is likely that this event triggers a vicious cycle since mitochondrial ROS are able to oxidatively damage nearby MRC enzymes and mtDNA HOIP:HOIP_0001748 Negative regulation of respiratory electron transport chain is a subtype of negative regulation process: Any process that stops, prevents or reduces the frequency, rate or extent of mrespiratory electron transport chain. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. negative regulation of respiratory electron transport chain [alcoholic fatty liver] HOIP_0001748 HOIP:HOIP_0001749 Negative regulation of oxidative phosphorylation is a subtype of negative regulation process: Any process that stops, prevents or reduces the frequency, rate or extent of the oxidative phosphorylation. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. negative regulation of oxidative phosphorylation [alcoholic fatty liver] HOIP_0001749 HOIP:HOIP_0001750 ATF6 signal integration system is a subtype of pathway system. This entity has sub-parts and has a goal of transmitting signals and a gene regulation via ATF6 as a systemic context. ATF6 signal integration system HOIP_0001750 HOIP:HOIP_0001751 NAPQI accumulation is a subtype of accumulation of substances in a biological object: A process that keeps NAPQI (N-acetyl-p-benzoquinone imine) within a biological object(s). NAPQI is an intermediate metabolite of the paracetamol and plays a role as a toxic substance in the body. NAPQI accumulation HOIP_0001751 HOIP:HOIP_0001753 Preventing is a type of functioning process of meta-function of "ToPrevent". Two meta-functions "ToAllow" and "Toprevent" are concerned with the undesirable side effects of functions. A function fa having positive effects on the side effect of a function ft1 is said to have a meta-function “to allow the side-effects of ft1”. The “undesirable side effect” is defined in a relation with another function ft2 or the whole system. The “positive effect” means such a causal relation that increase of the focused attribute of fa causes decrease of the side effect. If a serious trouble (e.g., faults) will be caused in a function ft2 when a function fa is not achieved, function fa is said to have a meta-function “to prevent malfunction of ft2”. For example, the “to super-heat” function of the boiler prevents malfunction of the turbine, because the steam of low temperature would damage the turbine blade by water particles. For almost all fa performing a ToAllow meta-function for ft1, in general, there exists a ToPrevent meta-function for another function ft2. preventing HOIP_0001753 HOIP:HOIP_0001754 Providing is a subtype of metafunctioning process. When a function fa generates (or transfers) the materials which another function ft intentionally processes, the function fa is said to perform a meta-function “to provide material” for the function ft. The material of ft can be basically defined as input objects (entity or energy) which will be a part of the output objects on which the function ft focuses. providing HOIP_0001754 HOIP:HOIP_0001755 Abnormality of membrane is a subtype of changing abnormal cellular structure: A process that changes the membrane stucture abnormally. abnormality of membrane HOIP_0001755 HOIP:HOIP_0001756 Driving is a type of functioning process of meta-function. The function which generates or transfers a driving energy is said to have meta-function “driving”. For example, the “to heat water” function of the boiler has a ToDrive meta-function for the “to generate torque” function of the turbine , because the amount of the heat energy transferred by the heating has a proportional causal relation to the torque and is consumed by the rotation. driving HOIP_0001756 HOIP:HOIP_0001757 Enabling is a subtype of meta-functioning process. To enable is a meta-function that sets conditions for other functions to work correctly. enabling HOIP_0001757 HOIP:HOIP_0001758 Cytochrome P450 activation is a subtype of molecular activation: A process that changes the activity of the cytochrome P450 to be higher. p450 activaion cytochrome P450 activation HOIP_0001758 HOIP:HOIP_0001760 ATF6-CHOP signal integration system is a subtype of ATF6 pathway system. This entity has sub-parts and has a goal of transmitting signals and a gene regulation via ATF6 and CHOP as a systemic context. ATF6-CHOP signal integration system HOIP_0001760 HOIP:HOIP_0001761 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of phospholipids. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). positive regulation of phospholipid biosynthetic process [phospholipidosis (moderate) ] HOIP_0001761 HOIP:HOIP_0001762 Increasing phospholipid material is a subtype of increasing quantity: A process that changes the amount of phospholipid material to be larger. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. increasing phospholipid material [phospholipidosis (imbalance course)] HOIP_0001762 HOIP:HOIP_0001763 Sphingophospholipid accumulation in lysosome is a subtype of phospholipid accumulation in lysosome: A process that keeps sphingophospholipid in the lysosome. sphingophospholipid accumulation in lysosome HOIP_0001763 HOIP:HOIP_0001764 Sphingomyelin accumulation in lysosome is a subtype of sphingophospholipid accumulation in lysosome: A process that keeps sphingomyelin in the lysosome. sphingomyelin accumulation in lysosome HOIP_0001764 HOIP:HOIP_0001765 Calcium ion homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a calcium ion homeostastasis balance. calcium ion homeostasis imbalance HOIP_0001765 HOIP:HOIP_0001766 Hypofunction of xenobiotic glucuronidation is a subtype of decreasing function of: A process that performs a decreased or insufficient xenobiotic glucuronidation. hypofunction of glucuronic acid conjugation hypofunction of xenobiotic glucuronidation HOIP_0001766 HOIP:HOIP_0001768 A process that becomes lacking a homeostastasis balance of the sphingomyelin metabolism. This process is dependent on the genetic and can constitute the course of Phospholipidosis (genetic). sphingomyelin metabolism imbalance [sphingomyelin disorder (genetic)] HOIP_0001768 HOIP:HOIP_0001769 Hypofunction of phospholipase transport to lysosome is a subtype of hypofunction of transport: A process that performs a decreased or insufficient phospholipase transport to lysosome . hypofunction of phospholipase transport to lysosome HOIP_0001769 HOIP:HOIP_0001770 Changing abnormal cellular structure is a subtype of changing structure: A process that changes the structure of the cell abnormally. changing abnormal cellular structure HOIP_0001770 HOIP:HOIP_0001771 Negative regulation of oxidative phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of oxodative phosphorylation. negative regulation of oxidative phosphorylation HOIP_0001771 HOIP:HOIP_0001772 Keeping amount of phospholipid in lysosome is a subtype of keeping amount: A process that maintaining the amount of lysosomal phospholipid. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). keeping amount of phospholipid in lysosome [phospholipidosis (normal course)] HOIP_0001772 HOIP:HOIP_0001773 Glutathione deficiency is a subtype of malfunctioning process: A process that lacks performing the glutathione function required. glutathione deficiency HOIP_0001773 HOIP:HOIP_0001774 This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. NCBI-Human-GeneID:211 PMID:19710929 PMID:20018698 ALAS1 (human)[lipidosis] HOIP_0001774 This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. http://www.ncbi.nlm.nih.gov/gene/211 NCBI-Human-GeneID:211 http://www.ncbi.nlm.nih.gov/gene/211 PMID:19710929 Most of the genes commonly regulated in mouse and human were involved in lipid metabolism and many represented known PPARalpha targets, including CPT1A, HMGCS2, FABP1, ACSL1, and ADFP. Several genes were identified that were specifically induced by PPARalpha in human (MBL2, ALAS1, CYP1A1, TSKU) or mouse (Fbp2, lgals4, Cd36, Ucp2, Pxmp4). HOIP:HOIP_0001775 Hypofunction of glutathione conjugation is a subtype of hypofunction of drug metabolism: A process that performs a decreased or insufficient glutathione conjugation. hypofunction of glutathione conjugation HOIP_0001775 HOIP:HOIP_0001776 Phospholipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of phospholipid metabolism. This process is dependent on the genetic and can constitute the course of Phospholipidosis (genetic). phospholipid metabolism imbalance [phospholipidosis (genetic)] HOIP_0001776 HOIP:HOIP_0001777 Phospholipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of phospholipid metabolism. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). phospholipid metabolism imbalance [phospholipidosis (mild)] HOIP_0001777 HOIP:HOIP_0001778 Phospholipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of phospholipid metabolism. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). phospholipid metabolism imbalance [phospholipidosis (severe)] HOIP_0001778 HOIP:HOIP_0001779 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that includes step 1 to 4, and the demand level is higher (Very High, VH) than usual to imbalance and abnormal manifestations. imbalance VH (demand action) HOIP_0001779 HOIP:HOIP_0001780 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that inculdes step 1 to 3. The defense performance level and the functional demand level are high, as a result, keeping the balance. This state reflects the adaptation. balance H=H (maintining homeostasis at higher level) HOIP_0001780 HOIP:HOIP_0001781 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that inculdes step 1 to 4. The defense performance level is higher (H) than daily life; however, the functional demand level is Very high(VH), which leads to the imbalance and leads to abnormal manifestation. imbalance H<VH HOIP_0001781 HOIP:HOIP_0001782 Phospholipid metabolism balance is a subtype of maintaining balance: A process that keeps a balance of phospholipid metabolism. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis (excessive defense). phospholipid metabolism balance [Phospholipidosis (adaptation)] HOIP_0001782 HOIP:HOIP_0001785 Catalysis role of the reaction: H(2)O + sphingomyelin = ceramide + choline phosphate + H(+). EC 3.1.4.12 http://www.brenda-enzymes.org/ontology.php?ontology_id=1&f[id][value]=GO:0004767&f[id][type]=2&id_go=GO:0004767 http://www.genome.ad.jp/dbget-bin/www_bget?enzyme+3.1.4.12 sphingomyelinase sphingomyelin phosphodiesterase HOIP_0001785 HOIP:HOIP_0001787 Negative regulation of enzyme activation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of enzyme activation. negative regulation of enzyme activation HOIP_0001787 HOIP:HOIP_0001788 Negative regulation of sphingomyelin catabolic process is a subtype of negative regulation of sphingophopholipid degradation: Any process that stops, prevents, or reduces the frequency, rate or extent of the sphingomyelin catabolic process. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. negative regulation of sphingomyelin catabolic process [sphingomyelin disorder (course)] HOIP_0001788 HOIP:HOIP_0001790 Increasing free radical is a subtype of increasing quantity: A process that changes the amount of free radicals to be larger. increasing free radical HOIP_0001790 HOIP:HOIP_0001791 NCBI-Human-GeneID:1558 CYP2C8 (mol) HOIP_0001791 NCBI-Human-GeneID:1558 http://www.ncbi.nlm.nih.gov/gene/1558 HOIP:HOIP_0001792 Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the unfolded protein response (UPR) and in response to low amino acid availability. Converts phosphorylated eIF-2-alpha/EIF2S1 either in a global protein synthesis inhibitor, leading to a reduced overall utilization of amino acids, or to a translation initiation activator of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function. NCBI-Human-GeneID:9451 NCBI-Mouse-GeneID:13666 NCBI-Rat-GeneID:29702 http://www.uniprot.org/entry/Q9NZJ5 PERK (mol) HOIP_0001792 NCBI-Human-GeneID:9451 http://www.ncbi.nlm.nih.gov/gene/9451 NCBI-Mouse-GeneID:13666 http://www.ncbi.nlm.nih.gov/gene/13666 NCBI-Rat-GeneID:29702 http://www.ncbi.nlm.nih.gov/gene/29702 HOIP:HOIP_0001793 Generating signal is a subtype of generating: A process that produces a signal as an output. This entity is a specific course-dependent process. This process can constitute the course of Signaling pathway. generating signal [Signaling pathway] HOIP_0001793 HOIP:HOIP_0001794 Increasing glycerophospholipid material is a subtype of increasing materials for lipid formation: A process that changes the amount of glycerophospholipid material to be larger. This process is dependent on the sphingophospholipid disorder and can constitute the course of Phospholipidosis. increasing glycerophospholipid material [Phospholipidosis - sphingophospholipid disorder] HOIP_0001794 HOIP:HOIP_0001795 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). phosphatidylinositol 3-kinase signaling HOIP_0001795 HOIP:HOIP_0001796 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)) . AKT signaling [phospholipidosis (severe (excessive defense))] HOIP_0001796 HOIP:HOIP_0001807 Sphingomyelin accumulation in lysosome is a subtype of sphingophospholipid accumulation in lysosome: A process that keeps sphingomyelin in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B (severe). severe sphingomyelin accumulation in lysosome [course of Niemann–Pick disease type A and type B (severe)] HOIP_0001807 HOIP:HOIP_0001809 Sphingomyelin accumulation in lysosome is a subtype of sphingophospholipid accumulation in lysosome: A process that keeps sphingomyelin in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. severe sphingomyelin accumulation in lysosome [course of Niemann–Pick disease type B] HOIP_0001809 HOIP:HOIP_0001810 Malfunction of mitochondria is a subtype of malfunctioning process: A process that cannot perform a mitochondrial function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of ER stress. malfunction of mitochondria [ER stress] HOIP_0001810 HOIP:HOIP_0001811 A size change process in which the size of liver and spleen is increasing. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick Disease Type B. splenohepatomegaly [course of Niemann–Pick disease type B] HOIP_0001811 HOIP:HOIP_0001812 A size change process in which the size of liver and spleen is increasing. icreasing size of liver and spleen splenohepatomegaly HOIP_0001812 HOIP:HOIP_0001813 NCBI-Human-GeneID:5599 NCBI-Mouse-GeneID:26419 NCBI-Rat-GeneID:116554 JNK (canonical)[ER stress] HOIP_0001813 NCBI-Human-GeneID:5599 http://www.ncbi.nlm.nih.gov/gene/5599 NCBI-Mouse-GeneID:26419 http://www.ncbi.nlm.nih.gov/gene/26419 NCBI-Rat-GeneID:116554 http://www.ncbi.nlm.nih.gov/gene/116554 HOIP:HOIP_0001814 Pulmonary infection is a subtype of pathogen colonization: A process that makes pathogen such as microorganism (bacteria, virus, mycoplasma, etc.) present in the lung to increase the number. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. pulmonary infection [course of Niemann–Pick disease type B] HOIP_0001814 HOIP:HOIP_0001815 Sphingomyelin accumulation in lysosome is a subtype of sphingophospholipid accumulation in lysosome: A process that keeps sphingomyelin in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. severe sphingomyelin accumulation in lysosome [course of Niemann–Pick disease type A] HOIP_0001815 HOIP:HOIP_0001816 A process that becomes lacking a homeostastasis balance of the sphingomyelin metabolism. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. sphingomyelin metabolism imbalance [course of Niemann–Pick disease type B] HOIP_0001816 HOIP:HOIP_0001817 A size change process in which the size of liver and spleen is increasing. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick Disease Type A. splenohepatomegaly [course of Niemann–Pick disease type A] HOIP_0001817 HOIP:HOIP_0001818 Hypofunction of nervous system functioning is a subtype of hypofunctioning: A process that performs a decreased or insufficient nervous system functioning. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick Disease Type A. hypofunction of nervous system functioning [course of Niemann–Pick disease type A] HOIP_0001818 HOIP:HOIP_0001819 Hypofunction of nervous system functioning is a subtype of hypofunctioning: A process that performs a decreased or insufficient nervous system functioning. hypofunction of nervous system functioning HOIP_0001819 HOIP:HOIP_0001820 System dependent functional molecule is asubtype of chemical entity. This entity is dependent on a system for functioning. system dependent functional molecule HOIP_0001820 HOIP:HOIP_0001821 Signaling transduction system dependent molecule is a subtype of system dependeny functional molecule. This entity is dependent on a signal transduction system for functioning. signal transduction system dependent molecule HOIP_0001821 HOIP:HOIP_0001822 Lipid accumulation in hepatocyte is a subtype of lipid strorage in hepatocyte: A process that keeps lipids in hepatocytes. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). lipid accumulation in hepatocyte [Phospholipidosis(moderate)] HOIP_0001822 HOIP:HOIP_0001823 A process that becomes lacking a homeostastasis balance of the sphingomyelin metabolism. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. sphingomyelin metabolism imbalance [sphingomyelin disorder (course)] HOIP_0001823 HOIP:HOIP_0001824 Phospholipid accumulation in lysosome is a subtype of phospholipid accumulation: A process that keeps phospholipid in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). phospholipid accumulation in lysosome [phospholipidosis (mild)] HOIP_0001824 HOIP:HOIP_0001825 Hyperfunction of increasing the amount of drug is a subtype of hyperfunction of increasing: A process that performs an excessive increase in the amount of drug. hyperfunction of increasing the amount of drug HOIP_0001825 HOIP:HOIP_0001826 Receiving abnormal protein signal by PERK is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by PERK. This process is dependent on the refolding and can constitute the course of ER stress via protein refolding. receiving abnormal protein signal by PERK [ER stress - refolding] HOIP_0001826 HOIP:HOIP_0001828 Receptor molecule is a subtype of signaling dependent molecule. This entity is dependent on a signal transduction system and can participate in signaling process. receptor molecule [signal transduction system] HOIP_0001828 HOIP:HOIP_0001829 Hypofunction of ceramide degradation is a subtype of hypofunction of lipid degradation: A process that performs a decreased or insufficient ceramide degradation. hypofunction of ceramide degradation HOIP_0001829 HOIP:HOIP_0001830 Decreasing production quantity of protein is a subtype of decreasing quantity: A process that changes the production quantity of the protein to be lower. decreasing protein production decreasing production quantity of protein HOIP_0001830 HOIP:HOIP_0001831 Phosphatidylinositol accumulation in lysosome is a subtype of glycerophospholipid accumulation in lysosome: A process that keeps phosphatidylinositol in the lysosome. phosphatidylinositol accumulation in lysosome HOIP_0001831 HOIP:HOIP_0001832 Hyperfunction of decreasing is a subtype of hyperfunctioning: A process that performs an excesssive decreasing amount or decreasing number of objects. hyperfunction of decreasing HOIP_0001832 HOIP:HOIP_0001833 Signaling molecule is a subtype of signaling dependent molecule. This entity is dependent on a signal transduction system and can participate in signaling process. signaling molecule [signal transduction system] HOIP_0001833 HOIP:HOIP_0001834 Hyperfunction of decreasing the amount of drugs is a subtype of hyperfunction of decreasing: A process that performs an excesssive decreasing the amount of drugs. hyperfunction of decreasing the amount of drugs HOIP_0001834 HOIP:HOIP_0001835 Dissociation of PERK:BIP heterodimer is a subtype of detaching: A process that disaggregates PERK-BIP heterodimers into BIP and PERK. This process is dependent on the refolding and can constitute the course of ER stress. PMID:10854322 PMID:11907036 Reactome PathwayStep4038 Reactome:R-HSA-381086 PERK (EIF2AK3) is a single-pass transmembrane protein located in the Endoplasmic Reticulum (ER) membrane. PERK has an N-terminal luminal domain and a C-terminal cytosolic domain. It is maintained in an inactive state by association of its luminal domain with BiP, a chaperone in the ER. Because BiP also binds unfolded proteins, BiP dissociates from PERK when unfolded proteins exceed chaperone activity in the ER. Dissociation of PERK:BIP Heterodimer [ER stress - refolding] HOIP_0001835 Reactome PathwayStep4038 http://purl.obolibrary.org/obo/HINO_0006880 HOIP:HOIP_0001837 Receiving signal in PERK signal transduction pathway is a subtype of receiving signal: A process that recognizes another object and changes into a signal in a PERK signal transduction pathway. receiving signal in PERK signal transduction pathway HOIP_0001837 HOIP:HOIP_0001839 Dissociation of PERK:BIP heterodimer is a subtype of detaching: A process that disaggregates PERK-BIP heterodimers into BIP and PERK. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:10854322 PMID:11907036 Reactome PathwayStep4038 Reactome:R-HSA-381086 PERK (EIF2AK3) is a single-pass transmembrane protein located in the Endoplasmic Reticulum (ER) membrane. PERK has an N-terminal luminal domain and a C-terminal cytosolic domain. It is maintained in an inactive state by association of its luminal domain with BiP, a chaperone in the ER. Because BiP also binds unfolded proteins, BiP dissociates from PERK when unfolded proteins exceed chaperone activity in the ER. Dissociation of PERK:BIP Heterodimer [ER stress - apoptosis] HOIP_0001839 Reactome PathwayStep4038 http://purl.obolibrary.org/obo/HINO_0006880 HOIP:HOIP_0001841 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signal sensor (canonical)[Perk signalling system] HOIP_0001841 HOIP:HOIP_0001844 Lipid accumulation in hepatocyte is a subtype of lipid strorage in hepatocyte: A process that keeps lipids in hepatocytes. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). lipid accumulation in hepatocyte [Phospholipidosis(severe)] HOIP_0001844 HOIP:HOIP_0001845 S1P inactivation is a subtype of molecular inactivation: A process that changes the activity of the S1P (Sphingosine-1-phosphate) to be lower. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). S1P inactivation [phospholipidosis (severe)] HOIP_0001845 HOIP:HOIP_0001846 Malfunctioning of mitochondrial ATP synthesis coupled electron transpor is a subtype of malfunctioning process: A process that cannot perform a respiratory electron transport chain appropriately or cannot realize it at all. malfunctioning of mitochondrial ATP synthesis coupled electron transpor HOIP_0001846 HOIP:HOIP_0001847 Changing balance is a subtype of changing relationship between operands: A process that changes the balance between operands. changing balance HOIP_0001847 HOIP:HOIP_0001850 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). hepatic fibrosis [phospholipidosis (severe (excessive defense))] HOIP_0001850 HOIP:HOIP_0001851 Making existence of xenobiotics is a subtype of making existence of foreign substance: A process that makes xenobiotics to be present in a cell, organelle, or an organism. making existence of xenobiotics HOIP_0001851 HOIP:HOIP_0001852 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signaling factor (canonical)[Perk signalling system] HOIP_0001852 HOIP:HOIP_0001853 TGF beta receptor signaling is a subtype of signaling that a signal is transmitted by the TGF beta receptor (transforming growth factor beta receptor) on the surface of a cell, starting with a ligand binding to a TGFR. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). TGF beta receptor signaling [phospholipidosis (severe (excessive defense))] HOIP_0001853 HOIP:HOIP_0001854 TGF beta receptor signaling is a subtype of signaling that a signal is transmitted by the TGF beta receptor (transforming growth factor beta receptor) on the surface of a cell, starting with a ligand binding to a TGFR. TGF beta receptor signaling HOIP_0001854 HOIP:HOIP_0001855 Decreasing mitochondrial membrane potential is a subtype of decreasing membrane potential: A process that changes the electrical potential of a mitochondrial membrane to be lower. reduction of membrane potential decreasing mitochondrial membrane potential HOIP_0001855 HOIP:HOIP_0001856 The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). heme biosynthetic process [non-alcoholic steatohepatitis (course)] HOIP_0001856 HOIP:HOIP_0001858 Hypofunction of PPAR alpha regulated gene expression is a subtype of hyporfunction of gene expression: A process that performs an PPARa trgulated gene expression. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). hypofunction of PPARa regulated gene expression [non-alcoholic steatohepatitis (course)] HOIP_0001858 HOIP:HOIP_0001860 Hypofunction of PPARa regulated gene expression is a subtype of Hypofunction of phospholipase gene expression is a subtype of hypofunction of transcription, DNA-templated: A process that performs a decreased or insufficient PPARa regulated gene expression. hypofunction of PPARa regulated gene expression HOIP_0001860 HOIP:HOIP_0001861 A process that changes the activity of the target object by PERK. This entity is a specific course-dependent process. This process can constitute the course of PERK pathway. changing activity of target molecule by PERK [PERK pathway] HOIP_0001861 HOIP:HOIP_0001863 The process that results in the movement of mitochondriall DNA from the mitochondria. mtDNA stress release of DNA from mitochondria HOIP_0001863 HOIP:HOIP_0001864 The process that results in the movement of mitochondriall DNA from the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of lipidosis. PMID:30046112 release of DNA from mitochondria [non-alcoholic steatohepatitis (course)] HOIP_0001864 HOIP:HOIP_0001865 Catalysis role of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. rerlated molecular fuction GO:0004672 protein kinase HOIP_0001865 HOIP:HOIP_0001866 A role played by the entity which inhibits bile acid transport by BSEP. inhibitor role of BSEP bile acid transport HOIP_0001866 HOIP:HOIP_0001867 A role played by the entity which stops, prevents, or reduces the frequency, rate or extent of trasnport. negative regulator role of transport HOIP_0001867 HOIP:HOIP_0001874 Gene expression by CHOP (DDIT3, GADD153) is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by CHOP (DDIT3, GADD153). gene expression by CHOP (DDIT3, GADD153) HOIP_0001874 HOIP:HOIP_0001875 NCBI-Human-GeneID:3553 NCBI-Mouse-GeneID:16176 NCBI-Rat-GeneID:24494 IL-1B (canonical)[lipidosis] HOIP_0001875 NCBI-Human-GeneID:3553 http://www.ncbi.nlm.nih.gov/gene/3553 NCBI-Mouse-GeneID:16176 http://www.ncbi.nlm.nih.gov/gene/16176 NCBI-Rat-GeneID:24494 http://www.ncbi.nlm.nih.gov/gene/24494 HOIP:HOIP_0001876 NLRP3 is a inflammasome component NCBI-Human-GeneID:114548 NCBI-Mouse-GeneID:216799 NCBI-Rat-GeneID:287362 NLRP3 (canonical)[lipidosis] HOIP_0001876 NCBI-Human-GeneID:114548 http://www.ncbi.nlm.nih.gov/gene/114548 NCBI-Mouse-GeneID:216799 http://www.ncbi.nlm.nih.gov/gene/216799 NCBI-Rat-GeneID:287362 http://www.ncbi.nlm.nih.gov/gene/287362 HOIP:HOIP_0001878 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). IL-1beta production [non-alcoholic steatohepatitis (course)] HOIP_0001878 HOIP:HOIP_0001879 Increasing volume of mitochondria is a changing process to change the volume of the mitochondria to increase. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:25339807 increasing volume of mitochondria [mitochondrial disorder (course)] HOIP_0001879 PMID:25339807 TNF-α induces mitochondrial perturbations such as swelling with a lighter matrix and abnormal morphological alterations in the membrane. In addition, TNF-α-induced mitochondrial swelling causes a bursting of the membrane leading to an interference between respiratory chain complexes I and III. HOIP:HOIP_0001880 Generating energy is a subtype of generating: A process that produces energy as an output. generating energy HOIP_0001880 HOIP:HOIP_0001881 An attribute inhering in a bearer by an observation. findings attribute HOIP_0001881 HOIP:HOIP_0001882 Electrophiles formation is a subtype of biosynthetic process: A process that that generates electrophiles. Electrophile is a reagent that forms a bond to its reaction partner (the nucleophile) by accepting both bonding electrons from that reaction partner. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). A number of xenobiotics exert a toxic effect theough their metabolites. Electrophiles are molecules that contain an electron-deficient atom with a partial or full positive charge that can react by sharing electron pairs with electron rich atoms in nucleophiles. Electrophilic toxicants generally are detoxificated by conjugation of with the nucleophile, glutathione. This reaction can be facilitated by glutathione S-trasferases. electrophiles formation [non-alcoholic steatohepatitis (course)] HOIP_0001882 HOIP:HOIP_0001884 NCBI-Human-GeneID:26291 PMID:17550777 PMID:20451522 PMID:22009939 PMID:27690692 FGF21 (canonical)[lipidosis] HOIP_0001884 NCBI-Human-GeneID:26291 http://www.ncbi.nlm.nih.gov/gene/26291 PMID:17550777 Endocrine regulation of the fasting response by PPARα-mediated induction of fibroblast growth factor 21: FGF21 is induced directly by PPARalpha in liver in response to fasting and PPARalpha agonists. FGF21 in turn stimulates lipolysis in white adipose tissue and ketogenesis in liver. PPARalpha-FGF21 endocrine signaling pathway in regulating diverse metabolic and behavioral aspects of the adaptive response to starvation. PMID:20451522 Increased Fibroblast Growth Factor 21 in Obesity and Nonalcoholic Fatty Liver Disease:We found increased serum FGF21 levels in patients with either NAFLD or NASH and for the first time we report that FGF21 mRNA expression in human liver is significantly increased in NAFLD. PMID:22009939 ER stress and PPARα activation contribute to carcinogenesis in a fatty liver: a modest increase in the expression of lipoprotein lipase (LPL) and fibroblast growth factor 21 (FGF21) in both Acox1−/− and Acox1−/−/ob/ob mouse liver (Fig. 5A). Significant increases in microsomal triglyceride transfer protein (MTP) were found in Acox1−/−/ob/ob mouse liver (Supplemental Fig. S2B). MTP regulates hepatic lipid secretion and may play a role in the reduction of hepatic steatosis in these mice HOIP:HOIP_0001886 NCBI-Human-GeneID:29108 ASC [lipidosis] CARD5 [lipidosis] Caspase Recruitment Domain-Containing Protein 5 [lipidosis] PYD And CARD Domain Containing [lipidosis] PYCARD (canonical)[lipidosis] HOIP_0001886 NCBI-Human-GeneID:29108 https://www.ncbi.nlm.nih.gov/gene/29108 HOIP:HOIP_0001889 Cytochrome P450 inactivation is a subtype of molecular inactivation: A process that changes the activity of the Cytochrome P450 to be lower. cytochrome P450 inactivation HOIP_0001889 HOIP:HOIP_0001890 Cytochrome P450 inactivation is a subtype of molecular inactivation: A process that changes the activity of the Cytochrome P450 to be lower. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). PMID:28303724 Cytochrome P450 inactivation [non-alcoholic steatohepatitis (course)] HOIP_0001890 PMID:28303724 The cytokine-mediated down-regulation of CYP3A4 (Werk and Cascorbi, 2014) in the course of the inflammatory response via the JAK/STAT (Janus kinase/Signal Transducer and Activator of Transcription) pathway (Jover et al., 2002 ) seem to be clinically relevant in NAFLD and diabetic patients due to circulating cytokines. HOIP:HOIP_0001892 Negative regulation of bile acid and bile salts export from the hepatocyte is a subtype of negative regulation of transport: A process that stops, prevents, or reduces the frequency, rate or extent of bile acid and bile salts export from the hepatocyte. negative regulation of bile acid and bile salts export from the hepatocyte HOIP_0001892 HOIP:HOIP_0001894 The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). PMID:24132155 PMID:25132496 protein unfolding [non-alcoholic steatohepatitis (course)] HOIP_0001894 PMID:25132496 Both NASH and HCC development were dependent on TNF produced by inflammatory macrophages that accumulate in the MUP-uPA liver in response to hepatocyte ER stress. HOIP:HOIP_0001898 A role played by the entity which transmits signals. signal transducer HOIP_0001898 HOIP:HOIP_0001899 EIF2a phosphorylation is a subtype of phosphorylation: The process of introducing a phosphate group into eIF2a. eIF2a phosphorylation HOIP_0001899 HOIP:HOIP_0001900 A role played by the entity which enables the energy-independent passage of anions across a lipid bilayer down a concentration gradient. related molecular function GO:0005253 anion channel HOIP_0001900 HOIP:HOIP_0001901 A tumor necrosis factor that is encoded in the genome of human. NCBI-Human-GeneID:7124 NCBI-Mouse-GeneID:21926 NCBI-Rat-GeneID:24835 tumor necrosis factor alpha [lipidosis] TNF alpha (canonical)[lipidosis] HOIP_0001901 NCBI-Human-GeneID:7124 http://www.ncbi.nlm.nih.gov/gene/7124 NCBI-Mouse-GeneID:21926 http://www.ncbi.nlm.nih.gov/gene/21926 NCBI-Rat-GeneID:24835 http://www.ncbi.nlm.nih.gov/gene/24835 HOIP:HOIP_0001902 Gene regulation pathway is a subtype of pathway: Sequence of reactions to regulate genes following signaling. gene regulation pathway HOIP_0001902 HOIP:HOIP_0001904 ATF6 activation is a subtype of molecular activation: A process that changes the activity of the ATF6 (Activating Transcription Factor 6) to be higher. PMID:12376530 ATF6 activation HOIP_0001904 HOIP:HOIP_0001905 ATF6 activation is a subtype of molecular activation: A process that changes the activity of the ATF6 (Activating Transcription Factor 6) to be higher. This process is dependent on the refolding and can constitute the course of ER stress. ATF6 activation [ER stress - refolding] HOIP_0001905 HOIP:HOIP_0001906 Acumulation of bile pigment in bile canaliculus is a subtype of bile pigment deposition: The aggregation of bile pigmentin a particular location in a bile canaliculus. acumulation of bile pigment in bile canaliculus HOIP_0001906 HOIP:HOIP_0001907 NCBI-Human-GeneID:468 NCBI-Mouse-GeneID:11911 NCBI-Rat-GeneID:79255 ATF4 (canonical)[ER stress] HOIP_0001907 NCBI-Human-GeneID:468 http://www.ncbi.nlm.nih.gov/gene/468 NCBI-Mouse-GeneID:11911 http://www.ncbi.nlm.nih.gov/gene/11911 NCBI-Rat-GeneID:79255 http://www.ncbi.nlm.nih.gov/gene/79255 HOIP:HOIP_0001908 Negative regulation of phospholipase-mediated phospholipid degradation by CAD is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase-mediated phospholipid deradation regulated by CAD. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). negative regulation of phospholipase-mediated phospholipid degradation by CAD [phospholipidosis (latent course)] HOIP_0001908 HOIP:HOIP_0001909 A role played by the entity which stops, prevents, or reduces the frequency, rate or extent of translational initiation. related process GO:0036495 negative regulation of translation initiation in response to endoplasmic reticulum stress GO:0010998: regulation of translational initiation by eIF2 alpha phosphorylation (Any process that modulates the frequency, rate or extent of translation initiation in response to stress by the phosphorylation of eIF2 alpha.) GO:0036492 eiF2alpha phosphorylation in response to endoplasmic reticulum stress inverse of GO:0036497 eIF2alpha dephosphorylation in response to endoplasmic reticulum stress negative regulator role of translational initiation HOIP_0001909 HOIP:HOIP_0001910 Hypofunction of biosynthesis is a subtype of hypofunctioning: A process that performs a decreased or insufficient biosynthesis. hypofunction of biosynthesis HOIP_0001910 HOIP:HOIP_0001911 Hypofunction of transport is a subtype of hypofunctioning: A process that performs a decreased or insufficient transport. hypofunction of transport HOIP_0001911 HOIP:HOIP_0001912 Increasing blood glucose lebvel is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. hyperglycemia (process) increasing blood glucose level HOIP_0001912 HOIP:HOIP_0001913 Decresing pressure is a subtype of changing pressure: A process that changes the pressure of the object to be lower. decresing pressure HOIP_0001913 HOIP:HOIP_0001914 Increasing BUN concentration is a subtype of increasing concentration: A process that changes the Blood Urea Nitrogen (BUN) concentration to be higher. increasing BUN concentration HOIP_0001914 HOIP:HOIP_0001915 Glutathione depletion dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the course of glutathione depletion. glutathione depletion dependent chemical entity HOIP_0001915 HOIP:HOIP_0001916 Glutathione depletion dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of glutathione depletion as a gene product. Gene profile:Human/in vitro/Hepatocyte/ glutathione depletion dependent molecule (human in vitro) HOIP_0001916 HOIP:HOIP_0001920 Electrophiles formation is a subtype of biosynthetic process: A process that that generates electrophiles. Electrophile is a reagent that forms a bond to its reaction partner (the nucleophile) by accepting both bonding electrons from that reaction partner. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. A number of xenobiotics exert a toxic effect theough their metabolites. Electrophiles are molecules that contain an electron-deficient atom with a partial or full positive charge that can react by sharing electron pairs with electron rich atoms in nucleophiles. Electrophilic toxicants generally are detoxificated by conjugation of with the nucleophile, glutathione. This reaction can be facilitated by glutathione S-trasferases. PMID:21177773 electrophiles formation [glutathione depletion (course)] HOIP_0001920 HOIP:HOIP_0001921 Glutathione depletion dependent chemical compound is a subtype of course dependent chemical entity. This entity (drug) can participate in the course of glutathione depletion. glutathione depletion dependent chemical compound HOIP_0001921 HOIP:HOIP_0001922 Wikipedia:Acetaminophen Wikipedia:Paracetamol N-(4-hydroxyphenyl)acetamide paracetamol [glutathione depletion (course)] APAP Acetaminophen [glutathione depletion (course)] HOIP_0001922 HOIP:HOIP_0001923 Glutathione conjugation is a subtype of drug metabolism phase II: Glutathione conjugation is a detoxication reaction. Four types of activation reaction have been recognized: direct-acting compounds, conjugates that are activated through cysteine conjugate beta-lyase, conjugates that are activated through redox cycling and lastly conjugates that release the original reactive parent compound. The glutathione S-transferases have three connections with the formation of biactivated conjugatesto make them more soluble for excretion. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. glutathione conjugation [glutathione depletion (course)] HOIP_0001923 HOIP:HOIP_0001924 ISBN:0071769234 phorone [glutathione depletion (course)] HOIP_0001924 ISBN:0071769234 Michael acceptors such as diethyl maleate (DEA) and phorone are commonly used in vivo to deplete GSH levels in experimental animals. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0001925 Hyperfunction of glutathione conjugation is a subtype of hyperfunction of drug metabolism phase II: A process that performs an excessive glutathione conjugation. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of glutathione conjugation [glutathione depletion (course)] HOIP_0001925 HOIP:HOIP_0001927 Glutathione depletion dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of glutathione depletion as a gene product. Gene profile:Rat/Liver/ glutathione depletion dependent molecule (rat) HOIP_0001927 HOIP:HOIP_0001928 NCBI-Rat-GeneID:296271 PMID:20621112 Srxn1 (rat)[glutathione depletion (course)] HOIP_0001928 NCBI-Rat-GeneID:296271 http://www.ncbi.nlm.nih.gov/gene/296271 HOIP:HOIP_0001929 PMID:23856494 Glutathione Synthetase [glutathione depletion (course)] ATP dependent. GSS (canonical)[glutathione depletion (course)] HOIP_0001929 HOIP:HOIP_0001931 NCBI-Human-GeneID:2937 NCBI-Mouse-GeneID:14854 NCBI-Rat-GeneID:25458 Glutathione Synthetase GSS (mol) HOIP_0001931 NCBI-Human-GeneID:2937 http://www.ncbi.nlm.nih.gov/gene/2937 NCBI-Mouse-GeneID:14854 http://www.ncbi.nlm.nih.gov/gene/14854 NCBI-Rat-GeneID:25458 http://www.ncbi.nlm.nih.gov/gene/25458 HOIP:HOIP_0001933 Hyperfunction of glutathione synthetic gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive glutathione synthetic gene expression. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of glutathione synthetic gene expression [glutathione depletion (course)] HOIP_0001933 HOIP:HOIP_0001934 NCBI-Rat-GeneID:26760 PMID:20621112 PMID:21688283 Akr7a3 (rat)[glutathione depletion (course)] HOIP_0001934 NCBI-Rat-GeneID:26760 http://www.ncbi.nlm.nih.gov/gene/26760 PMID:21688283 Aldo-keto reductase-7A protects liver cells and tissues from acetaminophen-induced oxidative stress and hepatotoxicity: In response to APAP or NAPQI exposure, Akr7a3 mRNA and protein were significantly up-regulated in vitro in human HepG2 and LO2 cells. Similarly, strong induction was observed for Akr7a5 in mouse AML12 hepatocytes exposed to APAP. In vivo in wild-type rats, significant up-regulation of hepatic AKR7A1 protein was observed after administration of APAP. On the other hand, depletion of Nrf2 reduced the expression of Akr7a3, suggesting that Nrf2, indeed, contributes significantly to the induction of Akr7a. HOIP:HOIP_0001937 An enzyme that catalysis of the reaction: L-gamma-glutamyl-L-cysteine + ATP + glycine = ADP + glutathione + 2 H(+) + phosphate. glutathione synthase HOIP_0001937 HOIP:HOIP_0001941 ISBN:0071769234 DMA [glutathoine depletion] diethyl malate [glutathione depletion (course)] HOIP_0001941 ISBN:0071769234 Michael acceptors such as diethyl maleate (DEA) and phorone are commonly used in vivo to deplete GSH levels in experimental animals. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0001942 ISBN:0071769234 PMID:20463017 PMID:8097674 BSO [glutathione depletion (course)] HOIP_0001942 ISBN:0071769234 Inhibition of GSH is achieved by buthionine-S-sulfoximine (BSO), which inhbits ints gammma-GCL. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0001944 Any process that stops, prevents, or reduces the frequency, rate or extent of glutathione biosynthetic process. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. negative regulation of glutathione biosyntheric process [glutathione depletion (course)] HOIP_0001944 HOIP:HOIP_0001946 Any process that stops, prevents, or reduces the frequency, rate or extent of glutathione biosynthetic process. down regulation of glutathione anabolism down regulation of glutathione biosynthesis negative regulation of glutathione anabolism negative regulation of glutathione biosynthesis negative regulation of glutathione formation negative regulation of glutathione synthesis negative regulation of glutathione biosynthetic process HOIP_0001946 HOIP:HOIP_0001947 NCBI-Human-GeneID:2938 NCBI-Rat-GeneID:24422 GSTA1 (mol) HOIP_0001947 NCBI-Human-GeneID:2938 http://www.ncbi.nlm.nih.gov/gene/2938 NCBI-Rat-GeneID:24422 http://www.ncbi.nlm.nih.gov/gene/24422 HOIP:HOIP_0001951 PMID:23856494 GCLC - inactivated state (canonical)[glutathione depletion (course)] HOIP_0001951 PMID:23856494 GSH is synthesized by two successive enzymatic reactions (Fig. 1). The first reaction, catalyzed by glutamate cysteine ligase (GCL), couples L-glutamate to L-cysteine to form γ-glutamylcysteine (γ-GC) . HOIP:HOIP_0001953 NCBI-Rat-GeneID:246273 PMID:20621112 Trib3 (rat)[glutathione depletion (course)] HOIP_0001953 NCBI-Rat-GeneID:246273 http://www.ncbi.nlm.nih.gov/gene/246273 HOIP:HOIP_0001955 GCLC inactivation is a subtype of is a subtype of molecular inactivation: A process that changes the activity of the GCLC to be lower. This entity is a specific course-dependent process. This process can constitute the course of glutathione depletion. GCLC inactivation [glutathione depletion (course)] HOIP_0001955 HOIP:HOIP_0001956 Changing protein structure is a subtype of changing structure: A process that changes the stucture of the protein. This entity is a specific course-dependent process. This process can constitute the course of ER stress. changing protein structure [ER stress] HOIP_0001956 HOIP:HOIP_0001957 Hypofunction of forming disulfide bond is a subtype of hypofunction of assembling: A process that performs a decreased or insufficient forming disulfide bond. hypofunction of forming disulfide bond HOIP_0001957 HOIP:HOIP_0001958 Hypofunction of protein synthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient protein synthesis. hypofunction of protein synthesis HOIP_0001958 HOIP:HOIP_0001960 NCBI-Human-GeneID:7184 PMID:23334697 HSP90B1 (canonical)[ER stress] HOIP_0001960 NCBI-Human-GeneID:7184 http://www.ncbi.nlm.nih.gov/gene/7184 PMID:23334697 Toxicol Pathol. 2013 Feb;41(2):235-62. doi: 10.1177/0192623312470764. Epub 2013 Jan 18. Xenobiotic perturbation of ER stress and the unfolded protein response. HOIP:HOIP_0001961 NCBI-Human-GeneID:1374 https://www.ncbi.nlm.nih.gov/books/NBK1527/ CPT1 (canonical)[lipidosis] HOIP_0001961 NCBI-Human-GeneID:1374 http://www.ncbi.nlm.nih.gov/gene/1374 https://www.ncbi.nlm.nih.gov/books/NBK1527/ Carnitine palmitoyltransferase I (CPT I) is a mitochondrial membrane protein that converts long-chain fatty acyl-CoA molecules to their corresponding acylcarnitine molecules. The resulting acylcarnitines are then available for transport into the mitochondrial matrix where they can undergo fatty acid oxidation. Mitochondrial fatty acid oxidation by the liver provides an alternative source of fuel when glycogen reserves are significantly reduced, most often due to fasting or other intercurrent illness. The pathway fuels ketogenesis for metabolism in peripheral tissues that cannot oxidize fatty acids. copyright University of Washington HOIP:HOIP_0001962 Open TG-Gates compound_id:00A02 tunicamycin-protein glycosylation inhibitor [ER stress] HOIP_0001962 PMID:26977301 HOIP:HOIP_0001963 Hypofunction of protein glycosylation is a subtype of hypofunctioning: A process that performs a decreased or insufficient protein glycosylation. hypofunction of protein glycosylation HOIP_0001963 HOIP:HOIP_0001964 The totality of all processes through which the phospholipidosis is realized. This entity represents latent phospholipidosis, which describes the course of processes before abnormal manifestation. In the drug exposure situation in phospholipidosis, it is known that CADs affect biological functioning. CADs bind to lysosomal membranes and form a complex with phospholipids, which negatively regulates phospholipid degradation. Therefore, the defence system cannot perform a ‘high’ level, i.e. there is a lack of adaptation. Under normal conditions, although the cell system can maintain the balance between increasing and decreasing phospholipid at a ‘medium’ level, in this state, the cellular system is in what is called the latent stage. PMID:15342952 PMID:16979167 PMID:22960355 phospholipidosis (latent course) HOIP_0001964 PMID:15342952 The following four processes were involved in the induction of phospholipidosis; (1) Inhibition of lysosomal phospholipase activivity (2) Inhibition of lysosomal enzyme transport, as demonstrated by the down-regulation of genes involved in lysosomal enzyme transport (3) Enhanced phospholipid biosynthesis, which is supported by the up- regulation of fatty acid biosynthesis-related genes (4) Enhanced cholesterol biosynthesis, as shown by the up-regulation of cholesterol biosynthesis-related genes Increased cholesterol biosynthesis is considered to be an indirect trigger for the reasons: (1) The accumulation of sphingomyelin occurs concurrently with the increase in cholesterol in visceral tissues (e.g., spleen) in patients with Niemann-Pick type C disease (NPC), which is caused by a genetic defect in the cholesterol trafficking protein NPC1 or, in far fewer patients, the sterol regulating protein HE1 (Blanchette-Mackie, 2000; Harzer et al., 2003; Vanier, 1983). (2) The induction of lamellar myelin-like bodies and the accumulation of free cholesterol occur in cultured mouse macrophages that have been incubated with acetylated low density lipoprotein or acyl-CoA:cholesterol acyl- transferase inhibitor (McGookey and Anderson, 1983; Robenek and Schmitz, 1988). In addition, the up- or down-regulation of transporter genes (e.g., facilitated glucose transporter) and genes that control the cell cycle (e.g., cyclin G2) may also be involved. Increase in phospholipid synthesis and impaired membrane recycling and lysosomal enzyme sorting dynamics are also occured. HOIP:HOIP_0001965 Negative regulation ofglycosylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of glycosylation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. negative regulation of glycosylation [ER stress] HOIP_0001965 PMID:26977301 HOIP:HOIP_0001966 Catalysis role of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. EC:2.7.11.1 related molecular function GO:0004674 protein serine/threonine kinase HOIP_0001966 HOIP:HOIP_0001967 related molecular function GO:0004095 carnitine palmitoyltransferase HOIP_0001967 HOIP:HOIP_0001968 NCBI-Human-GeneID:7494 NCBI-Mouse-GeneID:22433 NCBI-Rat-GeneID:289754 PMID:25629003 XBP1 (canonical)[ER stress] HOIP_0001968 NCBI-Human-GeneID:7494 http://www.ncbi.nlm.nih.gov/gene/7494 NCBI-Mouse-GeneID:22433 http://www.ncbi.nlm.nih.gov/gene/22433 NCBI-Rat-GeneID:289754 http://www.ncbi.nlm.nih.gov/gene/289754 PMID:25629003 The Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer Therapeutics. HOIP:HOIP_0001969 A role played by the entity which determines the rate of a reaction by the slowest step. mitochondrial fatty acid βbeta-oxidation rate-limiting enzyme role HOIP_0001969 HOIP:HOIP_0001970 CPT1 inactivation is a subtype of is a subtype of molecular inactivation: A process that changes the activity of the activating CPT1 with a nuclear receptor role to be lower. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). Reactome The set of genes regulated by PPAR-alpha is not fully known in humans, however many examples have been found in mice. Genes directly activated by PPAR-alpha contain peroxisome proliferator receptor elements (PPREs) in their promoters and include: 1) genes involved in fatty acid oxidation and ketogenesis (Acox1, Cyp4a, Acadm, Hmgcs2); 2) genes involved in fatty acid transport (Cd36, , Slc27a1, Fabp1, Cpt1a, Cpt2); 3) genes involved in producing fatty acids and very low density lipoproteins (Me1, Scd1); 4) genes encoding apolipoproteins (Apoa1, Apoa2, Apoa5); 5) genes involved in triglyceride clearance ( Angptl4); 6) genes involved in glycerol metabolism (Gpd1 in mouse); PMID:21145849 CPT1 inactivation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001970 HOIP:HOIP_0001971 CPT1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the CPT1 to be lower. CPT1 inactivation HOIP_0001971 HOIP:HOIP_0001972 Negative regulation of mitochondrial beta oxidation is a subtype of negative regulation of decomposing: Any process that stops, prevents or reduces the frequency, rate or extent of mitochondrial fatty acid beta oxidation. negative regulation of mitochondrial beta oxidation HOIP_0001972 HOIP:HOIP_0001973 Negative regulation of mitochondrial beta oxidation is a subtype of negative regulation of decomposing: Any process that stops, prevents or reduces the frequency, rate or extent of mitochondrial fatty acid beta oxidation. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:21145849 negative regulation of mitochondrial beta oxidation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0001973 HOIP:HOIP_0001974 NCBI-Human-GeneID:1374 https://www.ncbi.nlm.nih.gov/books/NBK1527/ CPT1 -inactivation state(canonical)[lipidosis] HOIP_0001974 NCBI-Human-GeneID:1374 http://www.ncbi.nlm.nih.gov/gene/1374 https://www.ncbi.nlm.nih.gov/books/NBK1527/ Carnitine palmitoyltransferase I (CPT I) is a mitochondrial membrane protein that converts long-chain fatty acyl-CoA molecules to their corresponding acylcarnitine molecules. The resulting acylcarnitines are then available for transport into the mitochondrial matrix where they can undergo fatty acid oxidation. Mitochondrial fatty acid oxidation by the liver provides an alternative source of fuel when glycogen reserves are significantly reduced, most often due to fasting or other intercurrent illness. The pathway fuels ketogenesis for metabolism in peripheral tissues that cannot oxidize fatty acids. copyright University of Washington HOIP:HOIP_0001975 ISBN:0071769234 PMID:21145849 tamoxifen -fatty acid oxidation inhibitor [Lipidosis] HOIP_0001975 ISBN:0071769234 Drug-induced steatosis is mainly caused by compounds such as 4,4′- diethylaminoethoxyhexestrol, amiodarone, tamoxifen, perhexiline, etc., which accumulate in mitochondria and inhibit β-oxidation and mitochondrial respiration. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0001976 ISBN:0071769234 PMID:21145849 valproic acid - fatty acid oxidation inhibitor [Lipidosis] HOIP_0001976 ISBN:0071769234 Types of hepatobiliary injury: Fatty liver: Amiodarone, CCl4, ethanol, fialuridine, tamoxifen, valproic acid in Table 13-2. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0001977 Accumulation of abnormal proteins in ER is a subtype of accumulation of abnormal proteins: A process that keeps abnormal protein(s) in the ER (endoplasmic reticulum). This entity is a specific course-dependent process. This process can constitute the course of ER stress (mild). accumulation of abnormal proteins in ER [ER stress (mild) ] HOIP_0001977 HOIP:HOIP_0001978 A role played by the gene which has a characteristic profile of gene expression change in a specific toxic mechanism. feature gene role HOIP_0001978 HOIP:HOIP_0001979 Enterohepatic circulation is a subtype of changing between operands: Bile salts secreted by the liver pass into the intestine, are absorbed in large part by the ileum, and return to the liver by way of the portal vein. Bile salts (>90%) are absorbed along the small intestine and transported back by the portal blood to the liver. They are taken up into hepatocytes and re-secreted into the canaliculi. This round trip of bile salts between the intestine and the liver is termed enterohepatic circulation. MeSH:D004764 PMID:4627839 enterohepatic circulation HOIP_0001979 HOIP:HOIP_0001980 PMID:21888831 PMID:25937070 1,4-dithiothreitol [ER stress] DTT [ER stress] HOIP_0001980 HOIP:HOIP_0001981 Ccl4 [ER stress] HOIP_0001981 HOIP:HOIP_0001982 Meloxicam is a long acting nonsteroidal antiinflammatory drug (NSAID) available by prescription only and used in therapy of chronic arthritis. Meloxicam has been linked to rare instances of acute, clinically apparent liver injury. PMID:26481188 MLX [ER stress] meloxicam [ER stress] HOIP_0001982 HOIP:HOIP_0001983 ISBN:0071769234 PMID:21145849 amiodarone - fatty acid oxidation inhibitor HOIP_0001983 ISBN:0071769234 Drug-induced steatosis is mainly caused by compounds such as amiodarone, tamoxifen, which accumulate in mitochondria and inhibit β-oxidation and mitochondrial respiration. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0001984 Changing state is a subtype of changing an operand: A process that changes the state of the object. changing state HOIP_0001984 HOIP:HOIP_0001986 The totality of all processes through which mitochondrial disorder is realized. mitochondrial disorder (course) HOIP_0001986 HOIP:HOIP_0001987 Mitochondrial disorder dependent process is a subtype of course dependent process: A process that can constitute the course of mitochondrial disorder. mitochondrial disorder dependent process HOIP_0001987 HOIP:HOIP_0001988 ATP depletion is a subtype of depleting: A process that lessens markedly in the amount of adenosine triphosphate (ATP) . This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:25339807 PMID:31623280 ATP depletion [mitochondrial disorder (course)] HOIP_0001988 PMID:25339807 MPTP activation by a combination of elevated intramitochondrial Ca2+ and oxidative stress promotes the collapse of transmembrane ion gradients, resulting in membrane depolarization, uncoupling of oxidative phosphorylation and ATP depletion. Under conditions of low ATP levels, the cells are unable to maintain structural and functional integrity, including ion homeostasis. This results in outer membrane permeabilization and cytochrome c release into the cytoplasm to initiate pro-apoptotic signals. PMID:31623280 Consistent with this, high glucose induces mitochondrial fragmentation, ROS production, loss of mitochondrial membrane potential, and ATP depletion in several rodent and human cell models. Moreover, in vitro treatment of liver cells with saturated fatty acids (palmitic and stearic acids) reproduces mitochondrial dysfunction found in NASH, including decreasing cellular ATP content and mtDNA-encoded oxidative phosphorylation (OXPHOS) subunit expression, coupled with increased oxidative stress. In addition to its ability to promote de novo lipogenesis and block β-oxidation of fatty acids, fructose consumption seems to cause a drop in ATP and an elevation of uric acid, which can further induce mitochondrial oxidative stress. More precisely, dietary-induced hypercholesterolemia causes oxidative stress, loss of mitochondrial membrane potential, reduction in ATP content, loss of mitochondrial cristae, and hepatic steatosis in mice. HOIP:HOIP_0001989 Negative regulation of respiratory electron transport chain is a subtype of negative regulation process: Any process that stops, prevents or reduces the frequency, rate or extent of mrespiratory electron transport chain. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. negative regulation of respiratory electron transport chain [mitochondrial disorder (course)] HOIP_0001989 HOIP:HOIP_0001990 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:23299992 PMID:25339807 PMID:26571396 PMID:27151080 PMID:29222479 PMID:29335519 PMID:30232152 PMID:31623280 PMID:31649547 reactive oxygen species biosynthetic process [mitochondrial disorder (course)] HOIP_0001990 PMID:23299992 Furthermore, enhanced mtFAO without concomitant up‐regulation of the mitochondrial respiratory chain (MRC) activity induces reactive oxygen species (ROS) overproduction within different MRC components upstream of cytochrome c oxidase. This event seems to play a significant role in the initiation of oxidative stress and subsequent development of nonalcoholic steatohepatitis (NASH) in some individuals. Experimental investigations also pointed to a progressive reduction of MRC activity during NAFLD, which could impair energy output and aggravate ROS overproduction by the damaged MRC. Furthermore, high glucose levels promote ROS overproduction within hepatocytes, thus favoring oxidative stress and mitochondrial dysfunction. It is likely that this event triggers a vicious cycle since mitochondrial ROS are able to oxidatively damage nearby MRC enzymes and mtDNA PMID:25339807 These results suggest that the observed dysfunction of complex I in hepatic mitochondria from CDD animals could be attributed, at least in part, to ROS-induced cardiolipin alterations. Long-chain free fatty acids which accumulate in nonalcoholic fatty liver are considered the initial source of this ROS damaging cycle. These compounds have been shown to promote ROS production in mitochondria, although the mechanism(s) underlying this effect is still unclear. Thus, the CL-dependent alterations of the ETC organization in supercomplexes could be another factor contributing to ROS generation and to mitochondrial bioenergetic decay in NAFLD. PMID:26571396 During nonalcoholic fatty liver disease (NAFLD), mitochondria also produce ROS that damage hepatocytes, trigger inflammation, and contribute to insulin resistance. PMID:27151080 not reported in the liver. We found a consistent and significant increase of mitochondrial ROS along with a parallel increase of total cellular ROS levels specifically in mC9ORF72 cells compared to both healthy control and mTDP-43 fibroblasts (Fig. 2e-​-ff). PMID:29222479 Alcohol-mediated damage of mitochondrial DNA (mtDNA) also impairs cellular energy metabolism via enhanced formation of reactive oxygen species (ROS). Alcohol decreases the activity of the oxidative phosphorylation (OXPHOS) complexes and increases ROS production, leading to mitochondrial stress or dysfunction. PMID:29335519 Collectively, these data suggest that enforced PCK1 expression triggers glucose-deprived liver cancer cell death by causing truncated gluconeogenesis, energy crisis, TCA cycle cataplerosis and high ROS levels. PMID:30232152 not reported in liver Exogenous H2O2 activates AMPK indirectly in myotubes by decreasing the ATP/ADP ratio. We conclude that AMPK activity in response to redox changes is not due to direct action on AMPK itself, but is a secondary consequence of redox effects on other processes, such as mitochondrial ATP production. PMID:31623280 The imbalance of respiratory complex activity during the development of NAFLD and its progression to NASH leads to increased mitochondrial reactive oxygen species (ROS), causing oxidative mitochondrial DNA (mtDNA) damage, mitochondria structural abnormalities, and lipid peroxidation. Mitochondrial ROS (mtROS) and lipid peroxidation also trigger proinflammatory cytokines such as interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), interleukin 1 beta (IL-1β), which are critical mediators of inflammation in NASH. Mitochondrial-derived ROS activate mitogen-activated protein kinases (MAPKs) including c-Jun N-terminal kinase (JNK). Phosphorylated JNK translocates to the mitochondria, where it binds to scaffold proteins inhibiting the mitochondrial respiratory chain and further increasing ROS production. Mitochondrial-derived ROS also activate AMP-activated protein kinase (AMPK) secondary to redox changes and mitochondrial ATP production. Mitochondrial ROS and oxidative stress can disrupt ER function leading to inappropriate release of calcium in liver parenchymal cells. Consistent with this, high glucose induces mitochondrial fragmentation, ROS production, loss of mitochondrial membrane potential, and ATP depletion in several rodent and human cell models. Saturated fats promote fatty liver and accumulation of lipotoxic byproducts including ceramides and diacylglycerols is associated with hepatic inflammation and mitochondrial ROS production resulting in liver cell death. PMID:31649547 Accumulating evidence has shown that defective hepatic mitochondrial respiration characterized by damaged mitochondria accumulation can impair mitochondrial fatty acid β-oxidation, which sequentially causes various adverse consequences, such as excessive ROS, reduced ATP production, and hepatic fatty acid accumulation. In general, damaged mitochondria accumulation can cause excessive ROS production, which will destroy mitochondrial oxidative phosphorylation and substrate oxidation, thereby inhibiting fatty acid oxidative degradation and accelerating fatty acid accumulation . HOIP:HOIP_0001991 Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:21145849 PMID:23299992 PMID:25339807 positive regulation of mitochondrial membrane permeability [mitochondrial disorder (course)] HOIP_0001991 PMID:21145849 Table 1. PMID:23299992 Moreover, saturated FAs are able to activate c‐Jun N‐terminal kinase and trigger the mitochondrial membrane permeability transition, thus inducing mitochondrial release of cytochrome c and apoptosis. PMID:25339807 In fact, phospholipid peroxidation alters the structural organization of the mitochondrial bilayer, perturbing membrane fluidity and permeability. MPTP activation by a combination of elevated intramitochondrial Ca2+ and oxidative stress promotes the collapse of transmembrane ion gradients, resulting in membrane depolarization, uncoupling of oxidative phosphorylation and ATP depletion. Cardiolipin has been shown to be involved in several steps of the intrinsic pathway of the apoptotic process, including mitochondrial permeability transition pore (MPTP) and cytochrome c release from mitochondria. MPTP is defined as the sudden increase of mitochondrial inner membrane permeability to low molecular weight solutes (1.5 kDa) in response to many stimuli, including high levels of Ca2+ and oxidant stress. If MPTP opening is transient, the cell can recover; while in conditions of prolonged MPTP opening and ATP depletion, irreversible damage and cell death occur, predominantly through necrosis. In addition, CL oxidation seems to promote the permeabilization of the outer mitochondrial membrane, probably interacting with Bcl2 family proteins, such as Bax and Bid. Thus, oxidized CL may have a critical role in several steps of the apoptotic process such as: the translocation of t-Bid to mitochondria with subsequent oligomerization of Bax and Bak leading to membrane permeabilization; cytochrome c dissociation from the inner mitochondrial membrane; and activation of MPTP, followed by the release of this hemoprotein from the mitochondrial intermembrane space to the cytosol (Figure ​1). HOIP:HOIP_0001992 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:23299992 PMID:25339807 PMID:29335519 PMID:31623280 apoptotic process [mitochondrial disorder (course)] HOIP_0001992 PMID:23299992 Moreover, saturated FAs are able to activate c‐Jun N‐terminal kinase and trigger the mitochondrial membrane permeability transition, thus inducing mitochondrial release of cytochrome c and apoptosis. PMID:25339807 Oxidative stress may cause damage at cellular level, such as membrane lipid peroxidation, cell degeneration and necrosis, cell death by apoptosis, proinflammatory cytokine expression, liver stellate cell activation and fibrogenesis. In liver cells, mitochondrial dysfunction plays a critical role by amplifying the apoptotic signal and integrating both pathways into a final common pathway. PMID:29335519 Metabolic reprogramming by PCK1 promotes TCA cataplerosis, oxidative stress and apoptosis in liver cancer cells and suppresses hepatocellular carcinoma. Collectively, these data suggest that enforced PCK1 expression triggers glucose-deprived liver cancer cell death by causing truncated gluconeogenesis, energy crisis, TCA cycle cataplerosis and high ROS levels. PMID:31623280 Bellanti et al. showed through targeted lipidomic analysis that rats fed diets rich in cholesterol exhibited increased toxic hepatic triol, which induces apoptosis and impaired mitochondrial respiration in vitro. Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). HOIP:HOIP_0001993 Decreasing mitochondrial membrane potential is a subtype of decreasing membrane potential: A process that changes the electrical potential of a mitochondrial membrane to be lower. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:25339807 PMID:31623280 decreasing mitochondrial membrane potential [mitochondrial disorder (course)] HOIP_0001993 PMID:25339807 MPTP activation by a combination of elevated intramitochondrial Ca2+ and oxidative stress promotes the collapse of transmembrane ion gradients, resulting in membrane depolarization, uncoupling of oxidative phosphorylation and ATP depletion. PMID:31623280 Consistent with this, high glucose induces mitochondrial fragmentation, ROS production, loss of mitochondrial membrane potential, and ATP depletion in several rodent and human cell models. More precisely, dietary-induced hypercholesterolemia causes oxidative stress, loss of mitochondrial membrane potential, reduction in ATP content, loss of mitochondrial cristae, and hepatic steatosis in mice. HOIP:HOIP_0001995 Decreasing membrane potential is a subtype of changing membrane potential: A process that changes the electrical potential across a membrane to be lower. decreasing membrane potential HOIP_0001995 HOIP:HOIP_0001996 A substance that kills or slows the growth of Mycobacterium tuberculosis and is used in the treatment of tuberculosis. antitubercular agent HOIP_0001996 HOIP:HOIP_0001997 Malfunctioning of uncoupling is a subtype of malfunctioning process: A process that cannot perform uncoupling appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. malfunctioning of uncoupling [mitochondrial disorder (course)] HOIP_0001997 HOIP:HOIP_0001998 A role played by the entity which enables the facilitated diffusion of a chloride (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism. related molecular funcion GO:0005254 chloride channel HOIP_0001998 HOIP:HOIP_0001999 Negative regulation of mitochondrial gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial gene expression. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. negative regulation of mitochondrial gene expression [mitochondrial disorder (course)] HOIP_0001999 HOIP:HOIP_0002000 GCLC inactivation is a subtype of molecular inactivation: A process that changes the activity of the GCLC to be lower. GCLC inactivation HOIP_0002000 HOIP:HOIP_0002001 Negative regulation of mitochondrial gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial gene expression. The process in which a mitochondrial gene's sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. The process in which a mitochondrial gene's sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. PMID:28285835 negative regulation of mitochondrial gene expression negative regulation of mitochondrial gene expression HOIP_0002001 The process in which a mitochondrial gene's sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. PMID:27058308 HOIP:HOIP_0002002 Catalysis role of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. EC:2.7.12.1 ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating) related molecular function GO:0004712 protein serine/threonine/tyrosine kinase HOIP_0002002 HOIP:HOIP_0002004 Lipid storage in liver is a subtype of lipid storage: The accumulation and maintenance in cells or tissues of lipids in the liver. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:23299992 PMID:29222479 PMID:31623280 lipid storage in liver [mitochondrial disorder (course)] HOIP_0002004 PMID:23299992 However, several hormonal and metabolic adaptations are set up in order to restrain hepatic fat accumulation, such as increased mitochondrial fatty acid oxidation (mtFAO). The expansion of hepatic lipids can be limited by different hormonal and metabolic adaptations leading to increased peroxisomal and mitochondrial FAO, as well as enhanced VLDL secretion (arrow 2). PMID:29222479 As shown in Fig. 3c, H&E staining and Oil Red O staining showed that hepatic fat accumulation and immune cell infiltration were increased in alcohol-fed GDF15 KO mice compared to controls (Fig. 3c).  PMID:31623280 Recent studies also show that MAMs are important for hepatic insulin signaling, nutrient sensing, and glucose homeostasis. Therefore, disruption of ER-mitochondria contact sites could exacerbate hepatic lipid accumulation and miscommunication between organelles appears to be related to the pathology of hepatic metabolic diseases. Saturated fats promote fatty liver and accumulation of lipotoxic byproducts including ceramides and diacylglycerols is associated with hepatic inflammation and mitochondrial ROS production resulting in liver cell death. More precisely, dietary-induced hypercholesterolemia causes oxidative stress, loss of mitochondrial membrane potential, reduction in ATP content, loss of mitochondrial cristae, and hepatic steatosis in mice. Damaged mitochondria are usually eliminated by autophagy/mitophagy which is attenuated by lipid accumulation. HOIP:HOIP_0002005 Hypofunction of mitochondrial fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient fatty acid beta-oxidation. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. Mitochondria are responsible for beta oxidation of fatty acids.Inhibition of mitochondrial beta-oxidation leads to hepatic steatosis and/or hepatotoxicity. DRUG INDUCED LIVER DISEASE CHAPTER 5, 3rd Ed. Editors: Neil Kaplowitz Laurie DeLev Hardcover ISBN: 9780123878175 PMID:21145849 PMID:31623280 PMID:31649547 hypofunction of mitochondrial fatty acid beta-oxidation [mitochondrial disorder (course)] HOIP_0002005 PMID:21145849 Table 1. PMID:31623280 H2O2 produced by mitochondria induces antioxidant enzyme expression through AMPK-mediated activation of nuclear factor 2 (NRF2), and consistently, NRF2 knockout mice on a high-fat diet develop more severe NASH associated with decreased antioxidant response, reduced β-oxidation genes, and increased lipogenic genes. In addition to its ability to promote de novo lipogenesis and block β-oxidation of fatty acids, fructose consumption seems to cause a drop in ATP and an elevation of uric acid, which can further induce mitochondrial oxidative stress. PMID:31649547 Recent study has found that hepatic fatty acid accumulation can cause damaged mitochondria accumulation, which can impair mitochondrial respiratory chain function and fatty acid oxidative degradation. Accumulating evidence has shown that defective hepatic mitochondrial respiration characterized by damaged mitochondria accumulation can impair mitochondrial fatty acid β-oxidation, which sequentially causes various adverse consequences, such as excessive ROS, reduced ATP production, and hepatic fatty acid accumulation. In general, damaged mitochondria accumulation can cause excessive ROS production, which will destroy mitochondrial oxidative phosphorylation and substrate oxidation, thereby inhibiting fatty acid oxidative degradation and accelerating fatty acid accumulation. HOIP:HOIP_0002006 Hypofunction of lipid degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient lipid degradation. hypofunction of lipid degradation HOIP_0002006 HOIP:HOIP_0002007 Hypofunction of fatty acid degradation is a subtype of hypofunction of lipid degradation: A process that performs a decreased or insufficient fatty acid degradation. hypofunction of fatty acid degradation HOIP_0002007 HOIP:HOIP_0002008 Hypofunction of fatty acid beta-oxidation is a subtype of hypofunction of fatty acid oxidation: A process that performs a decreased or insufficient fatty acid beta-oxidation. hypofunction of fatty acid beta-oxidation HOIP_0002008 HOIP:HOIP_0002009 Changing iron ion concentration is a subtype of changing concentration: A process that changes the iron (Fe) concentration in the blood to be lower. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. changing iron ion concentration [mitochondrial disorder (course)] HOIP_0002009 HOIP:HOIP_0002010 Degradation of a mitochondrion by macroautophagy. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:22187934 PMID:22743996 PMID:27151080 mitohagy [mitochondrial disorder (course)] HOIP_0002010 PMID:27151080 not reported in the liver. We found evidence of autophagy/mitophagy in dynamic equilibrium with the biogenesis of novel mitochondria, particularly in mutant C9ORF72 fibroblasts where an increase of mitochondrial DNA content and mass, and of PGC1-α protein was observed. These results, together with electronic microscopy data showing few autophagic/mitophagic vacuoles in both mutant fibroblast groups (Fig. 1d), suggest an early activation of the autophagic process. HOIP:HOIP_0002011 C19H35N C1CCC(CC1)C(CC1CCCCN1)C1CCCCC1 DrugBank:DB01074 PMID:21145849 Wikipedia:Perhexiline perhexiline - fatty acid oxidation inhibitor [lipidosis] HOIP_0002011 HOIP:HOIP_0002012 Mitochondrial damage dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the course of mitochondrial damage. mitochondrial damage dependent chemical entity HOIP_0002012 HOIP:HOIP_0002013 C19H35N C1CCC(CC1)C(CC1CCCCN1)C1CCCCC1 DrugBank:DB01074 Wikipedia:Perhexiline perhexiline [lipidosis] HOIP_0002013 HOIP:HOIP_0002018 ACOT1 (Acyl-CoA Thioesterase 1) is a Protein Coding gene. Diseases associated with ACOT1 include Human Immunodeficiency Virus Infectious Disease. Among its related pathways are Metabolism and Fatty acid elongation. GO annotations related to this gene include hydrolase activity and palmitoyl-CoA hydrolase activity. An important paralog of this gene is ACOT2. https://www.ncbi.nlm.nih.gov/gene/641371 NCBI-Human-GeneID:641371 NCBI-Mouse-GeneID:26897 NCBI-Rat-GeneID:50559 http://omim.org/entry/614313 Acot1 (mol) HOIP_0002018 NCBI-Human-GeneID:641371 http://www.ncbi.nlm.nih.gov/gene/641371 NCBI-Mouse-GeneID:26897 http://www.ncbi.nlm.nih.gov/gene/26897 NCBI-Rat-GeneID:50559 http://www.ncbi.nlm.nih.gov/gene/50559 HOIP:HOIP_0002019 ISBN:0071769234 PMID:21145849 tamoxifen -mitochondrial respiratory chain inhibitor [Lipidosis] HOIP_0002019 ISBN:0071769234 Drug-induced steatosis is mainly caused by compounds such as 4,4′- diethylaminoethoxyhexestrol, amiodarone, tamoxifen, perhexiline, etc., which accumulate in mitochondria and inhibit β-oxidation and mitochondrial respiration. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0002026 ISBN:0071769234 PMID:21145849 amiodarone -mitochondrial respiratory chain inhibitor [lipidosis] HOIP_0002026 ISBN:0071769234 Drug-induced steatosis is mainly caused by compounds such as amiodarone, tamoxifen, which accumulate in mitochondria and inhibit β-oxidation and mitochondrial respiration. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0002030 C19H35N C1CCC(CC1)C(CC1CCCCN1)C1CCCCC1 DrugBank:DB01074 PMID:21145849 Wikipedia:Perhexiline pergexiline -mitochondrial respiratory chain inhibitor [lipidosis] HOIP_0002030 HOIP:HOIP_0002031 A role played by the entity which negative regulates the oxidative phosphorylation. oxidative phosphorylation inhibitor role HOIP_0002031 HOIP:HOIP_0002032 NCBI-Human-GeneID:2939 NCBI-Rat-GeneID:501110 GSTA2 (mol) HOIP_0002032 NCBI-Human-GeneID:2939 http://www.ncbi.nlm.nih.gov/gene/2939 NCBI-Rat-GeneID:501110 http://www.ncbi.nlm.nih.gov/gene/501110 HOIP:HOIP_0002033 The totality of all processes through which a given diabetes instance is realized. diabetes course HOIP_0002033 HOIP:HOIP_0002034 Hypofunction of electron transport coupled proton transport is a subtype of hypofunction of ion transport: A process that performs a decreased or insufficient electron transport coupled proton transport. hypofunction of electron transport coupled proton transport HOIP_0002034 HOIP:HOIP_0002035 ibuprofen [lipidosis] HOIP_0002035 HOIP:HOIP_0002036 ibuprofen - oxidative phosphorylation inhibitor [lipidosis] HOIP_0002036 HOIP:HOIP_0002037 A role played by the entity which regulates the glutathione conjugation. glutathione conjuation regulating agent role HOIP_0002037 HOIP:HOIP_0002038 Leaking proton ion is a subtype of leaking: A process that leaks the proton from the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. leaking proton ion [mitochondrial disorder (course)] HOIP_0002038 HOIP:HOIP_0002039 Enables the transfer of protons from mitochondrial intermembrane space into mitochondrial matrix, dissipating the proton gradient across the mitochondrial inner membrane established by the electron transport chain during the oxidative phosphorylation (proton leak). Proton leak uncouples the processes of electron transport/proton generation and ATP synthesis. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. Enables the transfer of protons from mitochondrial intermembrane space into mitochondrial matrix, dissipating the proton gradient across the mitochondrial inner membrane established by the electron transport chain during the oxidative phosphorylation (proton leak). Proton leak uncouples the processes of electron transport/proton generation and ATP synthesis. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:21145849 PMID:25339807 oxidative phosphorylation uncoupling [mitochondrial disorder (course)] HOIP_0002039 Enables the transfer of protons from mitochondrial intermembrane space into mitochondrial matrix, dissipating the proton gradient across the mitochondrial inner membrane established by the electron transport chain during the oxidative phosphorylation (proton leak). Proton leak uncouples the processes of electron transport/proton generation and ATP synthesis. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:15738989 PMID:16179945 PMID:21145849 Table 1. PMID:25339807 MPTP activation by a combination of elevated intramitochondrial Ca2+ and oxidative stress promotes the collapse of transmembrane ion gradients, resulting in membrane depolarization, uncoupling of oxidative phosphorylation and ATP depletion. HOIP:HOIP_0002040 Fatty acid strorage is a subtype of accumulation of substances in a biological object: A process that keeps fatty acid in a biological object. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:23299992 PMID:26571396 PMID:31649547 fatty acid strorage [mitochondrial disorder (course)] HOIP_0002040 PMID:23299992 A second mechanism is ROS generation due to CYP2E1 overexpression and reduced levels of mtGSH. Whereas CYP2E1 induction could be secondary to higher levels of glucagon, FAs and KBs, reduced mtGSH could result from higher mitochondrial levels of cholesterol. Some lipid derivatives such as FAs can directly inhibit several enzymes involved in MRC and OXPHOS. Moreover, saturated FAs are able to activate c‐Jun N‐terminal kinase and trigger the mitochondrial membrane permeability transition, thus inducing mitochondrial release of cytochrome c and apoptosis. Numerous studies showed increased expression of PPARα in fatty liver. Different cues such as FAs, leptin, and IL6 could activate PPARα and its target genes involved in mtFAO (CPT1, MCAD), peroxisomal FAO (acyl‐CoA oxidase), and VLDL production (microsomal triglyceride transfer protein). PMID:26571396 First, in murine livers, elevation of fatty acid delivery not only induced oxidative metabolism, but also amplified anaplerosis/cataplerosis and caused a proportional rise in oxidative stress and inflammation. Likewise, Pck1 knockdown did not cause lower fasting basal endogenous glucose production (Figure 4C) or GNG (Figure 4D) on a control diet, but it was sufficient to prevent the rise in these fluxes during a HFD. PMID:31649547 Recent study has found that hepatic fatty acid accumulation can cause damaged mitochondria accumulation, which can impair mitochondrial respiratory chain function and fatty acid oxidative degradation. Accumulating evidence has shown that defective hepatic mitochondrial respiration characterized by damaged mitochondria accumulation can impair mitochondrial fatty acid β-oxidation, which sequentially causes various adverse consequences, such as excessive ROS, reduced ATP production, and hepatic fatty acid accumulation. In general, damaged mitochondria accumulation can cause excessive ROS production, which will destroy mitochondrial oxidative phosphorylation and substrate oxidation, thereby inhibiting fatty acid oxidative degradation and accelerating fatty acid accumulation. HOIP:HOIP_0002041 PPARalpha activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating PPAR alpha ( (Peroxisome Proliferator Activated Receptor Alpha)) with a nuclear receptor role to be higher. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. Reactome The set of genes regulated by PPAR-alpha is not fully known in humans, however many examples have been found in mice. Genes directly activated by PPAR-alpha contain peroxisome proliferator receptor elements (PPREs) in their promoters and include: 1) genes involved in fatty acid oxidation and ketogenesis (Acox1, Cyp4a, Acadm, Hmgcs2); 2) genes involved in fatty acid transport (Cd36, , Slc27a1, Fabp1, Cpt1a, Cpt2); 3) genes involved in producing fatty acids and very low density lipoproteins (Me1, Scd1); 4) genes encoding apolipoproteins (Apoa1, Apoa2, Apoa5); 5) genes involved in triglyceride clearance ( Angptl4); 6) genes involved in glycerol metabolism (Gpd1 in mouse); PMID:23299992 PPARalpha activation [mitochondrial disorder (course)] HOIP_0002041 PMID:23299992 Numerous studies showed increased expression of PPARα in fatty liver. Different cues such as FAs, leptin, and IL6 could activate PPARα and its target genes involved in mtFAO (CPT1, MCAD), peroxisomal FAO (acyl‐CoA oxidase), and VLDL production (microsomal triglyceride transfer protein). mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). For instance, LCFA‐mediated PPARα activation increases the expression of the mitochondrial enzymes CPT1 and medium‐chain acyl‐CoA dehydrogenase (MCAD). HOIP:HOIP_0002042 nimesulide [lipidosis] HOIP_0002042 HOIP:HOIP_0002043 PMID:21145849 nimesulide [lipidosis - oxidative phosphorylation inhibitor] HOIP_0002043 HOIP:HOIP_0002044 A compound which plays an inhibition of glutathione conjugation. glutathione conjugation inhibotor role HOIP_0002044 HOIP:HOIP_0002045 Glutathione depletion dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of glutathione depletion as a gene product. Gene profile:caonical that described in textbooks or articles. glutathione depletion dependent molecule (canonical) HOIP_0002045 HOIP:HOIP_0002046 Changing force is a subtype of changing quality: A process that changes the force of the object. changing force HOIP_0002046 HOIP:HOIP_0002048 Hypofunction of carbohydrate transport is a subtype of hypofunction of transport: A process that performs a decreased or insufficient carbohydrate transport. hypofunction of carbohydrate transport HOIP_0002048 HOIP:HOIP_0002049 Hyperfunction of drug metabolism phase I is a subtype of hyperfunctioning of drug metabolism: A process that performs an excessive drug metabolism phase I. hyperfunction of drug metabolism phase I HOIP_0002049 HOIP:HOIP_0002050 Decreasing glycogen level is a subtype of decreasing quantity: A process that changes the amount of glycogen level to be lower. MPATH:50 glycogen depletion decreasing glycogen level HOIP_0002050 HOIP:HOIP_0002051 Hyperfunction of Cyp gene expression is a subtype of hyperfunction of drug metabolizing enzyme gene expression: A process that performs an excesssive gene expression of cytochrome p450. hyperfunction of Cyp gene expression HOIP_0002051 HOIP:HOIP_0002052 Hyperfunction of electron transport from NADH to cytochrome P450 is a subtype of hyperfunction of transport: A process that performs an excesssive electron transport from NADH to cytochrome P450. hyperfunction of electron transport from NADH to cytochrome P450 HOIP_0002052 HOIP:HOIP_0002053 Dioxins and dioxin-like compounds accumulation in liver is a subtype of compound accumulation in liver: A process that keeps dioxins and dioxin-like compoundsin the liver. dioxins and dioxin-like compounds accumulation in liver HOIP_0002053 HOIP:HOIP_0002054 Negative regulation of heat generation is a subtype of negative regulation process: Any process that stops, prevents, or reduces the rate or extent of heat generation. down regulation of heat generation down-regulation of heat generation downregulation of heat generation inhibition of heat generation negative regulation of heat generation HOIP_0002054 HOIP:HOIP_0002056 Any process that stops, prevents, or reduces the frequency, rate or extent of glutathione conjugation process. negative regulation of glutathione conjugation HOIP_0002056 HOIP:HOIP_0002057 Negative regulation of cell proliferation inhibitor expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of cell proliferation inhibitor expression. negative regulation of cell proliferation inhibitor expression HOIP_0002057 HOIP:HOIP_0002058 Hyperfunction of reduction is a subtype of hyperfunctioning: A process that performs an excesssive reduction. hyperfunction of reduction HOIP_0002058 HOIP:HOIP_0002059 Decreasing negative regulator of G1/S transition is a subtype of decreasing quantity: A process that chanes the quantity of the object with a negative regulator of G1/S role to be lower. decreasing negative regulator of G1/S transition HOIP_0002059 HOIP:HOIP_0002060 Insufficient detoxification is a subtype of making insufficient: A process that lacks in detoxification. insufficient detoxification HOIP_0002060 HOIP:HOIP_0002061 Antioxidant gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature antioxidant gene product or products (proteins or RNA). antioxidant gene expression HOIP_0002061 HOIP:HOIP_0002063 Hyprerfunction of anti-oxidative stress is a subtype of hyperfunctioning: A process that performs an excesssive response to oxidative stress. hyprerfunction of anti-oxidative stress HOIP_0002063 HOIP:HOIP_0002064 Decreasing proton motive force is a subtype of decreasing force: A process that changes the force of proton generated by electrochemical proton gradient to be lower. decreasing proton motive force HOIP_0002064 HOIP:HOIP_0002065 A chromenone having the keto group located at the 2-position. PMID:2922762 coumarin [glutathione depletion (course)] HOIP_0002065 HOIP:HOIP_0002066 CAR binding is a subtype of binding: Interacting with CAR (constitutive androstane receptor) . constitutive androstane receptor binding CAR binding HOIP_0002066 HOIP:HOIP_0002067 NCBI-Human-GeneID:2941 GSTA4 (mol) HOIP_0002067 NCBI-Human-GeneID:2941 http://www.ncbi.nlm.nih.gov/gene/2941 HOIP:HOIP_0002069 Dysfunction of phospholipid degradation is a subtype of dysfunctioning: A process that performs an abnormal and incomplete phospholipid degradation. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis (genetic). dysfunction of phospholipid degradation [phospholipidosis (genetic)] HOIP_0002069 HOIP:HOIP_0002070 Phospholipid accumulation in lysosome is a subtype of phospholipid accumulation: A process that keeps phospholipid in the lysosome. This process is dependent on the sphingomyelin disorder and can constitute the course of Phospholipidosis (genetic). phospholipid accumulation in lysosome [phospholipidosis (genetic)] HOIP_0002070 HOIP:HOIP_0002071 Liver malfunction is a subtype of organ malfunction: A process that does not perform liver function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick Disease Type A/ B. liver malfunction [course of Niemann–Pick disease type A and type B] HOIP_0002071 HOIP:HOIP_0002072 Spleen malfunction is a subtype of organ malfunction: A process that does not perform spleen function correctly. This entity is a specific course-dependent process. This process can constitute the course of Niemann-Pick Disease Type A/ B. spleen malfunction [course of Niemann–Pick disease type A and type B] HOIP_0002072 HOIP:HOIP_0002073 Organ malfunction is a subtype of malfunctioning process: A process that cannot perform organ(s) function appropriately or cannot realize it at all. organ malfunction HOIP_0002073 HOIP:HOIP_0002074 Liver malfunction is a subtype of organ malfunction: A process that does not perform liver function correctly or not functioning at all. liver malfunction HOIP_0002074 HOIP:HOIP_0002075 Spleen malfunction is a subtype of organ malfunction: A process that does not perform spleen function correctly. spleen malfunction HOIP_0002075 HOIP:HOIP_0002076 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. The defense performance level and the functional demand level are moderate (M) under the normal condition and keeping the balance. imbalance M=M (maintining homeostasis in the normal condition) HOIP_0002076 HOIP:HOIP_0002077 Compound excretion is a subtype of xenobiotics excretion: A process that takes a compound from a cell, organelle, or makes a clearance of it from the body. chemical compound excretion HOIP_0002077 HOIP:HOIP_0002078 Compound excretion is a subtype of xenobiotics excretion: A process that takes a compound from a cell, organelle, or makes a clearance of it from the body. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). chemical compound excretion [phospholipidosis (normal course)] HOIP_0002078 HOIP:HOIP_0002080 Decreasing demand is a subtype of decreasing quantity: A process that changes the quantity demanded to be lower. decreasing demand HOIP_0002080 HOIP:HOIP_0002081 Decreasing functional demand is a subtype of decreasing demand: A process that changes the functional demand to be lower. decreasing functional demand HOIP_0002081 HOIP:HOIP_0002082 Decreasing demand for phospholipid degradation is a subtype of decreasing functional demand: A process that changes the functional demand for the phospholipid degradation to be lower. decreasing demand for phospholipid degradation HOIP_0002082 HOIP:HOIP_0002084 Decreasing phospholipid is a subtype of decreasing lipid: A process that changes the quantity of the phospholipid to be lower. decreasing phospholipid HOIP_0002084 HOIP:HOIP_0002085 Decreasing phospholipid is a subtype of decreasing lipid: A process that changes the quantity of the phospholipid to be lower. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). decreasing phospholipid [phospholipidosis (normal course)] HOIP_0002085 HOIP:HOIP_0002086 Increasing lysosomal pH is a subtype of changing pH: A process that changes the pH in lysosome to be higher. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). increasing lysosomal pH [phospholipidosis (moderate) ] HOIP_0002086 HOIP:HOIP_0002087 A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid degradation. And the degree is mild. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). negative regulation of phospholipid degradation [phospholipidosis (mild)] HOIP_0002087 HOIP:HOIP_0002088 Hypofunction of phospholipid degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient phospholipid degradation. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). hypofunction of phospholipid degradation [phospholipidosis (mild)] HOIP_0002088 HOIP:HOIP_0002089 glutathione transferase family HOIP_0002089 HOIP:HOIP_0002091 Malfunctioning of phospholipid metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of phospholipid metabolism appropriately or cannot realize it at all. The degree is mild. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). malfunctioning of phospholipid metabolism [phospholipidosis (mild)] HOIP_0002091 HOIP:HOIP_0002092 Malfunctioning of phospholipid metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of phospholipid metabolism appropriately or cannot realize it at all. malfunctioning of phospholipid metabolism HOIP_0002092 HOIP:HOIP_0002093 NCBI-Human-GeneID:2944 NCBI-Mouse-GeneID:14863 NCBI-Rat-GeneID:24424 GSTM1 (mol) HOIP_0002093 NCBI-Human-GeneID:2944 http://www.ncbi.nlm.nih.gov/gene/2944 NCBI-Mouse-GeneID:14863 http://www.ncbi.nlm.nih.gov/gene/14863 NCBI-Rat-GeneID:24424 http://www.ncbi.nlm.nih.gov/gene/24424 HOIP:HOIP_0002094 Lysosome damage is a subtype of organelle damage. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID:23921551 lysosome damage [phospholipidosis (severe)] HOIP_0002094 HOIP:HOIP_0002095 Lysosomal enzyme leakage is a subtype of leaking: A process that leaks the enzyme out from the lysosome. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). lysosomal enzyme leakage [phospholipidosis (severe)] HOIP_0002095 HOIP:HOIP_0002096 Lysosomal enzyme leakage is a subtype of leaking: A process that leaks the enzyme out from the lysosome. lysosomal enzyme leakage HOIP_0002096 HOIP:HOIP_0002097 Autolysis is a subtype of dissolving: The disintegration of a cell by rupture of the cell membrane by the action of their own enzymes. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). autolysis [phospholipidosis (severe)] HOIP_0002097 HOIP:HOIP_0002098 Dysfunction of phospholipid degradation is a subtype of dysfunctioning: A process that performs an abnormal and incomplete phospholipid degradation severely. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). dysfunction of phospholipid degradation [phospholipidosis (severe)] HOIP_0002098 HOIP:HOIP_0002099 Increasing drug metabolite is a subtype of increasing quantity: A process that changes the amount of drug metabolites to be higher. This entity is a specific course-dependent process. This process can constitute the course of necrosis. increasing drug metabolite [necrosis (course)] HOIP_0002099 HOIP:HOIP_0002101 Negative regulation of insulin receptor signaling pathway is a subtype of negative regulation of signaling: Any process that stops, prevents, or reduces the frequency, rate or extent of insulin receptor signaling. This entity is a specific course-dependent process. This process can constitute the course of ER stress. negative regulation of insulin receptor signaling pathway [ER stress] HOIP_0002101 HOIP:HOIP_0002102 Negative regulation of insulin receptor signaling pathway is a subtype of negative regulation of signaling: Any process that stops, prevents, or reduces the frequency, rate or extent of insulin receptor signaling. negative regulation of insulin receptor signaling pathway HOIP_0002102 HOIP:HOIP_0002103 Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:25966993 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3126329/ negative regulation of AKT signaling [ER stress] HOIP_0002103 PMID:25966993 ER stress in hepatocytes induces PHLDA3 via IRE1-Xbp1s pathway, which facilitates liver injury by inhibiting Akt. HOIP:HOIP_0002104 NCBI-Human-GeneID:2946 NCBI-Mouse-GeneID:68312 NCBI-Rat-GeneID:81869 GSTM2 (mol) HOIP_0002104 NCBI-Human-GeneID:2946 http://www.ncbi.nlm.nih.gov/gene/2946 NCBI-Mouse-GeneID:68312 http://www.ncbi.nlm.nih.gov/gene/68312 NCBI-Rat-GeneID:81869 http://www.ncbi.nlm.nih.gov/gene/81869 HOIP:HOIP_0002105 NCBI-Human-GeneID:207 NCBI-Mouse-GeneID:11651 NCBI-Rat-GeneID:24185 AKT (canonical)[ER stress] HOIP_0002105 NCBI-Human-GeneID:207 http://www.ncbi.nlm.nih.gov/gene/207 NCBI-Mouse-GeneID:11651 http://www.ncbi.nlm.nih.gov/gene/11651 NCBI-Rat-GeneID:24185 http://www.ncbi.nlm.nih.gov/gene/24185 HOIP:HOIP_0002106 Unfolded protein is a subtype of substance with role. This entity participates in a unfolded protein response and plays a unfolded protein role. unfolded protein HOIP_0002106 HOIP:HOIP_0002107 Molecular complex is a subtype of object aggregates. This entity has sub-parts of molecules. molecular complex HOIP_0002107 HOIP:HOIP_0002108 Bip-stress sensor complex is a subtype of molecular complex. This entity has sub-parts of molecules, BIP/GRP78 and other molecule which has role of stress sensor. This entity is dependent on ER stress. BIP-STRESS sensor complex (canonical)[ER stress] HOIP_0002108 HOIP:HOIP_0002109 Bip-PERK sensor complex is a subtype of molecular complex. This entity has sub-parts of molecules, BIP/GRP78 and PERK which has role of stress sensor. This entity is dependent on ER stress. BIP-PERK complex (canonical)[ER stress] HOIP_0002109 HOIP:HOIP_0002110 BIP-ATF6 complex is a subtype of molecular complex. This entity has sub-parts of molecules, BIP/GRP78 and ATF6 which has role of stress sensor. This entity is dependent on ER stress. BIP-ATF6 complex (canonical)[ER stress] HOIP_0002110 HOIP:HOIP_0002111 BIP-IRE1 complex is a subtype of molecular complex. This entity has sub-parts of molecules, BIP/GRP78 and IRE1 which has role of stress sensor. This entity is dependent on ER stress. BIP-IRE1 complex (canonical)[ER stress] HOIP_0002111 HOIP:HOIP_0002112 Hypofunction of mitochondrial fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient mitochondrial fatty acid beta-oxidation. hypofunction of mitochondrial fatty acid beta-oxidation HOIP_0002112 HOIP:HOIP_0002113 Glutathione depletion is a subtype of depleting: A process that lessens markedly in the amount of glutathione. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:25931127 glutathione depletion [ER stress] HOIP_0002113 HOIP:HOIP_0002114 Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:26977301 positive regulation of apoptotic process [ER stress] HOIP_0002114 PMID:26977301 PMID:26977301 In liver, the lesions observed in tunicamycin‐intoxicated animals include steatosis, bile ductular hyperplasia, swollen hepatocytes, and the presence of apoptotic bodies (Finnie and O'Shea 1989; Finnie and O'Shea 1990b; Finnie et al. 2004; Rutkowski et al. 2008). HOIP:HOIP_0002115 Bip-unfolded protein is a subtype of a molecular complex. This entity has sub-parts of molecules: BIP/GRP78, and an unfolded protein. http://purl.obolibrary.org/obo/HINO_0017506 https://identifiers.org/reactome:R-HSA-381062 Bip-unfolded protein complex HOIP_0002115 HOIP:HOIP_0002116 A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:25931127 cell cycle arrest [ER stress] HOIP_0002116 PMID:25931127 Because of the role of glutathione in cell cycle progression and apoptosis, an important role for CHAC1 in regulating the redox potential, proliferation, and viability of cells following ER stress is suggested. CHAC1 induction may induce a biphasic signal, first for cell cycle arrest, allowing the cell time to adapt to the stress, followed by apoptosis if the stress is insurmountable. HOIP:HOIP_0002117 Forming disulfide bond is a subtype of binding: The interaction between molecules with interchain disulfide bonds. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:21091435 PMID:23198585 PMID:23637286 forming disulfide bond [ER stress] HOIP_0002117 PMID:21091435 The endoplasmic reticulum sulfhydryl oxidase Ero1beta drives efficient oxidative protein folding with loose regulation. PMID:23637286 Protein disulfide isomerase (PDI) is the first discovered, most abundant oxidoreductase in the ER. Depending on conditions, it catalyzes formation, isomerization, or reduction of disulfide bonds. Without oxidoreductase capacity in the ER, protein folding would be too slow and prone to disaster, with abundant aggregation and degradation favored. Considering that protein folding in principle is a spontaneous process and that chaperones guide the process, the formation of nonnative disulfide bonds during folding is a must. HOIP:HOIP_0002118 Forming disulfide bond is a subtype of binding: The interaction between molecules with interchain disulfide bonds. In chemistry, a disulfide refers to a functional group with the structure R−S−S−R′. The linkage is also called an SS-bond or sometimes a disulfide bridge and is usually derived by the coupling of two thiol groups. Occurrence in proteins Disulfide bonds play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium. Since most cellular compartments are reducing environments, in general, disulfide bonds are unstable in the cytosol, with some exceptions as noted below, unless a sulfhydryl oxidase is present. Disulfide bonds in proteins are formed between the thiol groups of cysteine residues by the process of oxidative folding. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds. A disulfide bond is typically denoted by hyphenating the abbreviations for cysteine, e.g., when referring to ribonuclease A the "Cys26–Cys84 disulfide bond", or the "26–84 disulfide bond", or most simply as "C26–C84"　where the disulfide bond is understood and does not need to be mentioned. The prototype of a protein disulfide bond is the two-amino-acid peptide cystine, which is composed of two cysteine amino acids joined by a disulfide bond (shown in Figure 3 in its unionized form). The structure of a disulfide bond can be described by its χss dihedral angle between the Cβ−Sγ−Sγ−Cβ atoms, which is usually close to ±90°. In chemistry, a disulfide refers to a functional group with the structure R−S−S−R′. The linkage is also called an SS-bond or sometimes a disulfide bridge and is usually derived by the coupling of two thiol groups. Occurrence in proteins Disulfide bonds play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium. Since most cellular compartments are reducing environments, in general, disulfide bonds are unstable in the cytosol, with some exceptions as noted below, unless a sulfhydryl oxidase is present. Disulfide bonds in proteins are formed between the thiol groups of cysteine residues by the process of oxidative folding. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds. A disulfide bond is typically denoted by hyphenating the abbreviations for cysteine, e.g., when referring to ribonuclease A the "Cys26–Cys84 disulfide bond", or the "26–84 disulfide bond", or most simply as "C26–C84"　where the disulfide bond is understood and does not need to be mentioned. The prototype of a protein disulfide bond is the two-amino-acid peptide cystine, which is composed of two cysteine amino acids joined by a disulfide bond (shown in Figure 3 in its unionized form). The structure of a disulfide bond can be described by its χss dihedral angle between the Cβ−Sγ−Sγ−Cβ atoms, which is usually close to ±90°. forming disulfide bond HOIP_0002118 In chemistry, a disulfide refers to a functional group with the structure R−S−S−R′. The linkage is also called an SS-bond or sometimes a disulfide bridge and is usually derived by the coupling of two thiol groups. Occurrence in proteins Disulfide bonds play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium. Since most cellular compartments are reducing environments, in general, disulfide bonds are unstable in the cytosol, with some exceptions as noted below, unless a sulfhydryl oxidase is present. Disulfide bonds in proteins are formed between the thiol groups of cysteine residues by the process of oxidative folding. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds. A disulfide bond is typically denoted by hyphenating the abbreviations for cysteine, e.g., when referring to ribonuclease A the "Cys26–Cys84 disulfide bond", or the "26–84 disulfide bond", or most simply as "C26–C84"　where the disulfide bond is understood and does not need to be mentioned. The prototype of a protein disulfide bond is the two-amino-acid peptide cystine, which is composed of two cysteine amino acids joined by a disulfide bond (shown in Figure 3 in its unionized form). The structure of a disulfide bond can be described by its χss dihedral angle between the Cβ−Sγ−Sγ−Cβ atoms, which is usually close to ±90°. https://en.wikipedia.org/wiki/Disulfide HOIP:HOIP_0002119 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signaling factor (canonical)[Perk-eIF2a signalling system] HOIP_0002119 HOIP:HOIP_0002120 NCBI-Human-GeneID:2948 NCBI-Mouse-GeneID:14865 NCBI-Rat-GeneID:499689 GSTM4 (mol) HOIP_0002120 NCBI-Human-GeneID:2948 http://www.ncbi.nlm.nih.gov/gene/2948 NCBI-Mouse-GeneID:14865 http://www.ncbi.nlm.nih.gov/gene/14865 NCBI-Rat-GeneID:499689 http://www.ncbi.nlm.nih.gov/gene/499689 HOIP:HOIP_0002121 NCBI-Human-GeneID:2949 NCBI-Mouse-GeneID:14862 NCBI-Rat-GeneID:24423 GSTM5 (mol) HOIP_0002121 NCBI-Human-GeneID:2949 http://www.ncbi.nlm.nih.gov/gene/2949 NCBI-Mouse-GeneID:14862 http://www.ncbi.nlm.nih.gov/gene/14862 NCBI-Rat-GeneID:24423 http://www.ncbi.nlm.nih.gov/gene/24423 HOIP:HOIP_0002122 Cell invasion into other cell is a subtype of moving A to the inside of B: A process of the movement of a cell into other different cells. This entity is a specific course-dependent process. This process can constitute the course of anoikis. cell invasion into other cell [anoikis (course)] HOIP_0002122 HOIP:HOIP_0002123 Cell invasion into other cell is a subtype of moving A to the inside of B: A process of the movement of a cell into other different cells. cell invasion into other cell HOIP_0002123 HOIP:HOIP_0002124 Negative regulation of tumor cell proliferation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of tumor cell proliferation. negative regulation of tumor cell proliferation HOIP_0002124 HOIP:HOIP_0002125 Negative regulation of tumor cell proliferation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of tumor cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. negative regulation of tumor cell proliferation [apoptosis (course)] HOIP_0002125 HOIP:HOIP_0002126 A series of molecular signals mediated by ATF6 (activating transcription factor 6). ATF6 signal transduction pathway HOIP_0002126 HOIP:HOIP_0002127 NCBI-Human-GeneID:9446 NCBI-Mouse-GeneID:14873 NCBI-Rat-GeneID:114846 GSTO1 (mol) HOIP_0002127 NCBI-Human-GeneID:9446 http://www.ncbi.nlm.nih.gov/gene/9446 NCBI-Mouse-GeneID:14873 http://www.ncbi.nlm.nih.gov/gene/14873 NCBI-Rat-GeneID:114846 http://www.ncbi.nlm.nih.gov/gene/114846 HOIP:HOIP_0002128 Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. negative regulation of autophagy [apoptosis (course)] HOIP_0002128 HOIP:HOIP_0002129 Metabolic dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete metabolic function. This entity is a specific course-dependent process. This process can constitute the course of necrosis. metabolic dysfunction [necrosis (course)] HOIP_0002129 HOIP:HOIP_0002130 Malfunctioning of metabolism is a subtype of malfunctioning process: A process that cannot perform a metabolism appropriately or cannot realize it at all. malfunctioning of metabolism HOIP_0002130 HOIP:HOIP_0002131 Metabolic dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete metabolic function. metabolic dysfunction HOIP_0002131 HOIP:HOIP_0002132 Changing fatty acid homeostasis is a subtype of changing balance: A process that changes the steady state of fatty acid within an organism or cell. changing fatty acid homeostasis HOIP_0002132 HOIP:HOIP_0002133 Changing fatty acid homeostasis in peroxisome is a subtype of changing balance: A process that changes the steady state of fatty acid within peroxisomes. changing fatty acid homeostasis in peroxisome HOIP_0002133 HOIP:HOIP_0002135 Regulation of gene expression by p53 is a subtype of regulation of gene expression: Any process that modulates the frequency, rate or extent of gene expression. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. regulation of gene expression by p53 [apoptosis (course)] HOIP_0002135 HOIP:HOIP_0002136 Regulation of gene expression by p53 is a subtype of regulation of gene expression: Any process that modulates the frequency, rate or extent of gene expression. regulation of gene expression by p53 HOIP_0002136 HOIP:HOIP_0002137 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. DNA repair [apoptosis (course)] HOIP_0002137 HOIP:HOIP_0002138 Membrane phospholipid catabolic process is a subtype of lipid catabolic process: The chemical reactions resulting in the breakdown of membrane phopholipids This entity is a specific course-dependent process. This process can constitute the course of cell death. membrane phospholipid catabolic process [cell death (course)] HOIP_0002138 HOIP:HOIP_0002139 Pathogen proliferation is a subtype of increasing number of objects: A process becomes larger in the number of pathogen such as microorganism (bacteria, virus, mycoplasma, etc.) present in the body. pathogen proliferation HOIP_0002139 HOIP:HOIP_0002140 Pathogen proliferation is a subtype of increasing number of objects: A process becomes larger in the number of pathogen such as microorganism (bacteria, virus, mycoplasma, etc.) present in the body. This entity is a specific course-dependent process. This process can constitute the course of pyroptosis. pathogen proliferation [pyroptosis (course)] HOIP_0002140 HOIP:HOIP_0002141 Hyperfunction of immune response is a subtype of hyperfunctioning: A process that performs an excessive immune response. This entity is a specific course-dependent process. This process can constitute the course of pyroptosis. hyperfunction of immune response [pyroptosis (course)] HOIP_0002141 HOIP:HOIP_0002142 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of necrosis. inflammatory response [necrosis (course)] HOIP_0002142 HOIP:HOIP_0002143 A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). This pathway is a specific course-dependent and can constitute the course of ER stress. A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). This pathway is a specific course-dependent and can constitute the course of ER stress. ATF6-mediated unfolded protein response [ER stress] HOIP_0002143 A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). This pathway is a specific course-dependent and can constitute the course of ER stress. PMID:22013210 HOIP:HOIP_0002144 A caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18. This entity is a specific course-dependent process. This process can constitute the course of pyroptosis. pyroptosis [pyroptosis (course)] HOIP_0002144 HOIP:HOIP_0002145 A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). This pathway is a specific course-dependent and can constitute the course of ER stress. PERK-mediated unfolded protein response [ER stress] HOIP_0002145 HOIP:HOIP_0002146 Decreasing proton motive force is a subtype of decreasing force: A process that changes the force of proton generated by electrochemical proton gradient to be lower. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. decreasing proton motive force [mitochondrial disorder (course)] HOIP_0002146 HOIP:HOIP_0002147 Hypofunction of fatty acid oxidation is a subtype of hypofunctioning of decomposing: A process that performs a decreased or insufficient fatty acid oxidation. hypofunction of fatty acid oxidation HOIP_0002147 1 HOIP:HOIP_0002148 Anoikis is a subtype of cell death triggered by inadequate or inappropriate adherence to substrate e.g. after disruption of the interactions between normal epithelial cells and the extracellular matrix. An adherent cell-restricted lethal cascade that is ignited by detachment from the matrix and that is characterized by (i) lack of beta1-integrin engagement, (ii) downregulation of EGFR expression, (iii) inhibition of extracellular-regulated kinase 1 (ERK1) signaling, and (iv) overexpression of the BCL-2 family member BIM. It should be noted that in most, if not all, instances, the cell death program ignited by anoikis is executed by the molecular machinery for intrinsic apoptosis. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ anoikis (course) HOIP_0002148 HOIP:HOIP_0002149 In response to several stimuli, neutrophils and eosinophils can release the so-called neutrophil extracellular traps (NETs), that is, microbicidal structures composed of nuclear chromatin, histones and granular antimicrobial proteins. Netotic cells exhibit massive vacuolization of the cytoplasm, rapid chromatin decondensation and breakdown of both the nuclear and granular membranes, which is required for proper NET formation. Netosis is insensitive to caspase inhibitors and necrostatin-1, further demonstrating that it constitutes a cell death subroutine distinct from apoptosis and regulated necrosis. Netosis might be defined as a cell death subroutine that is: (i) restricted to granulocytic cells; (ii) insensitive to (and perhaps dependent on)163 caspase inhibition; (iii) insensitive to necrostatin; (iv) dependent on NAPDH oxidase-mediated superoxide generation; and (v) dependent on (components of) the autophagic machinery https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ PMID:24009232 netosis HOIP_0002149 HOIP:HOIP_0002151 NCBI-Human-GeneID:119391 NCBI-Mouse-GeneID:68214 NCBI-Rat-GeneID:309465 GSTO2 (mol) HOIP_0002151 NCBI-Human-GeneID:119391 http://www.ncbi.nlm.nih.gov/gene/119391 NCBI-Mouse-GeneID:68214 http://www.ncbi.nlm.nih.gov/gene/68214 NCBI-Rat-GeneID:309465 http://www.ncbi.nlm.nih.gov/gene/309465 HOIP:HOIP_0002152 Collagenase inhibitor production is a subtype of protein production: A process that makes existent of a substance with collagenase inhibitor role due to biosynthesis or secretion resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. collagenase inhibitor production [hepatic fibrosis course] HOIP_0002152 HOIP:HOIP_0002153 Collagenase inhibitor production is a subtype of protein production: A process that makes existent of a substance with collagenase inhibitor role due to biosynthesis or secretion resulting in an increase in its levels. collagenase inhibitor production HOIP_0002153 HOIP:HOIP_0002154 A role of combining with a signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. related molecular function GO:0004675 transmembrane receptor protein serine/threonine kinase HOIP_0002154 HOIP:HOIP_0002155 A series of molecular signals mediated by IRE1 (Inositol-requiring transmembrane kinase/endonuclease). IRE1 signal transduction pathway HOIP_0002155 HOIP:HOIP_0002156 Malfunctioning of electron transport coupled proton transport is a subtype of malfunctioning process: A process that cannot perform an electron transport coupled proton transport appropriately or cannot realize it at all. malfunctioning of uncoupling HOIP_0002156 HOIP:HOIP_0002157 PERK-eIF2a signaling is a subtype of PERK signaling (integrated pathway): Sequence of linked reactions, which has PERK-eIF2a signaling and gene regulation pathway. This pathway is dependent on the translation attenuation and can constitute the course of ER stress. PERK-eIF2a signaling (integrated pathway)[ER stress - translation attenuation] HOIP_0002157 HOIP:HOIP_0002161 The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state. This entity is a specific course-dependent process. This process can constitute the course of ER stress. protein unfolding [ER stress] HOIP_0002161 HOIP:HOIP_0002162 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signaling factor (canonical)[ER stress - translation attenuation] HOIP_0002162 HOIP:HOIP_0002163 The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:18556558 PMID:26977301 lipid biosynthetic process [ER stress] HOIP_0002163 PMID:18556558 X-box binding protein 1 (XBP1), known as a key regulator of the unfolded protein response (UPR) secondary to ER stress, is a only recently characterized regulator of hepatic lipogenesis. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 2008; 320: 1492-1496. XBP1 protein expression in mice was elevated after feeding carbohydrates and corresponded with the induction of critical genes involved in fatty acid synthesis. Inducible, selective deletion of XBP1 in the liver resulted in marked hypocholesterolemia and hypotriglyceridemia, secondary to a decreased production of lipids from the liver. This phenotype was not accompanied by hepatic steatosis or compromise in protein secretory function. The identification of XBP1 as a regulator of lipogenesis has important implications for human dyslipidemias. HOIP:HOIP_0002164 NCBI-Rat-GeneID:192235 R-HSA-1791066.1 https://omim.org/entry/601746 Hyou1 (rat)[ER stress] HOIP_0002164 NCBI-Rat-GeneID:192235 http://www.ncbi.nlm.nih.gov/gene/192235 HOIP:HOIP_0002165 NCBI-Human-GeneID:4189 PMID:14559994 PMID:18400946 PMID:25146923 REACTOME: R-HSA-381038 https://omim.org/entry/602634 ERDJ4 [ER stress] IRE1->Xbp1->DNAJB9 DNAJB9 (human)[ER stress] HOIP_0002165 NCBI-Human-GeneID:4189 http://www.ncbi.nlm.nih.gov/gene/4189 PMID:14559994 XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. XBP-1-dependent UPR target genes: ERdj4, p58IPK, EDEM, RAMP-4, PDI-P5, and HEDJ, all of which appear to act in the ER and display Hsp40-like ATPase augmenting activity for the Hsp70 family chaperone proteins. PMID:18400946 ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. PMID:25146923 Genotoxic stress/p53-induced DNAJB9 inhibits the pro-apoptotic function of p53. DNAJB9 as an inducible gene of the tumor suppressor p53. DNAJB9 expression was induced by p53 or genotoxic stress in a p53-dependent manner, which was mediated by the Ras/Raf/ERK pathway. In addition, depletion of DNAJB9 by using siRNAs greatly increased genotoxic stress/p53-induced apoptosis, suggesting that DNAJB9 inhibits the pro-apoptotic function of p53. REACTOME: R-HSA-381038 XBP1(S) activates chaperone genes including DNAJB9, EDEM, RAMP4, p58IPK, and others. This results in an increase in protein folding activity in the ER. HOIP:HOIP_0002166 This gene encodes a member of the mammalian activation transcription factor/cAMP responsive element-binding (CREB) protein family of transcription factors. This gene is induced by a variety of signals, including many of those encountered by cancer cells, and is involved in the complex process of cellular stress response. Multiple transcript variants encoding different isoforms have been found for this gene. It is possible that alternative splicing of this gene may be physiologically important in the regulation of target genes. [provided by RefSeq, Apr 2011] stress induction ->ATF3 ->apotosis induction by activating pro-apoptic genesTNRSF1-B and BBC3 cancer development ->ATF3 ->apoptosis inhibition by repressing proapoptic genes CDKN1A Systems analysis of ATF3 in stress response and cancer reveals opposing effects on pro-apoptotic genes in p53 pathway. PMID:22046379 Stress-induced ATF3 binds to 40% of p53 targets and activates pro-apoptotic genes such as TNFRSF10B/DR5 and BBC3/PUMA. Cancer-associated ATF3, by contrast, represses these pro-apoptotic genes in addition to CDKN1A/p21. ATF3 has opposing, cell context-dependent effects on p53 target genes in DNA damage response and cancer development. NCBI-Human-GeneID:467 PMID:20485437 PMID:22046379 PMID:24939851 PMID:26917416 PMID:27484784 PMID:8622660 PERK->ATF4->ATF3 reactome ATF3 (human)[ER stress] HOIP_0002166 PMID:24217556 PMID:22046379 NCBI-Human-GeneID:467 http://www.ncbi.nlm.nih.gov/gene/467 PMID:20485437 Opposing roles for calcineurin and ATF3 in squamous skin cancer. Calcineurin/NFAT inhibition counteracts p53-dependent cancer cell senescence, thereby increasing tumorigenic potential. ATF3, a member of the 'enlarged' AP1 family, is selectively induced by calcineurin/NFAT inhibition, both under experimental conditions and in clinically occurring tumors, and increased ATF3 expression accounts for suppression of p53-dependent senescence and enhanced tumorigenic potential. PMID:22046379 Systems analysis of ATF3 in stress response and cancer reveals opposing effects on pro-apoptotic genes in p53 pathway. PMID:8622660 Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10 HOIP:HOIP_0002167 NCBI-Human-GeneID:1649 PMID:15601821 PMID:15775988 PMID:22761832 PMID:25904325 http://www.omim.org/entry/126337 CHOP [ER stress] DDIT3 (human)[ER stress] HOIP_0002167 NCBI-Human-GeneID:1649 http://www.ncbi.nlm.nih.gov/gene/1649 PMID:15775988 TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. HOIP:HOIP_0002168 NCBI-Human-GeneID:57761 PMID:12791994 PMID:15775988 PMID:17369260 PMID:23695665 http://omim.org/entry/607898 TRIB3 (human)[ER stress] HOIP_0002168 NCBI-Human-GeneID:57761 http://www.ncbi.nlm.nih.gov/gene/57761 PMID:15775988 TRB3 is a novel target of CHOP/ATF4 and downregulates its own induction by repression of CHOP/ATF4 functions, and that it is involved in CHOP-dependent cell death during ER stress. PMID:17369260 TRB3 inhibits the transcriptional activation of stress-regulated genes by a negative feedback on the ATF4 pathway. HOIP:HOIP_0002169 Elucidation of a novel phenformin derivative on glucose-deprived stress responses in HT-29 cells. 2-(2-chlorophenyl)ethylbiguanide (2-Cl-Phen) down-regulated expression of several ER stress-related genes, with the exception of GADD153. The expression levels of ATF6α, GRP78, MANF, and CRELD2 mRNA were almost completely decreased by 2-Cl-Phen. NCBI-Human-GeneID:79174 PMID:23956175 https://omim.org/entry/607171 CRELD2 (human)[ER stress] HOIP_0002169 NCBI-Human-GeneID:79174 http://www.ncbi.nlm.nih.gov/gene/79174 PMID:23956175 Armet/Manf and Creld2 are components of a specialized ER stress response provoked by inappropriate formation of disulphide bonds: implications for genetic skeletal diseases. HOIP:HOIP_0002170 Dysfunction of mitochondrial respiratory electron transport chain is a subtype of dysfunctioning: A process that performs an abnormal and incomplete functioning of respiratory electron transport chain. dysfunction of mitochondrial respiratory electron transport chain HOIP_0002170 HOIP:HOIP_0002171 Hypofunction of mitochondrial fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient mitochondrial fatty acid beta-oxidation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. hypofunction of mitochondrial fatty acid beta-oxidation [ER stress] HOIP_0002171 HOIP:HOIP_0002172 Lipid storage in liver is a subtype of lipid storage: The accumulation and maintenance in cells or tissues of lipids in the liver. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:18556558 PMID:26977301 PMID:27325692 lipid storage in liver [ER stress] HOIP_0002172 PMID:18556558 X-box binding protein 1 (XBP1), known as a key regulator of the unfolded protein response (UPR) secondary to ER stress, is a only recently characterized regulator of hepatic lipogenesis. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 2008; 320: 1492-1496. XBP1 protein expression in mice was elevated after feeding carbohydrates and corresponded with the induction of critical genes involved in fatty acid synthesis. Inducible, selective deletion of XBP1 in the liver resulted in marked hypocholesterolemia and hypotriglyceridemia, secondary to a decreased production of lipids from the liver. This phenotype was not accompanied by hepatic steatosis or compromise in protein secretory function. The identification of XBP1 as a regulator of lipogenesis has important implications for human dyslipidemias. PMID:26977301 In liver, the lesions observed in tunicamycin‐intoxicated animals include steatosis, bile ductular hyperplasia, swollen hepatocytes, and the presence of apoptotic bodies (Finnie and O'Shea 1989; Finnie and O'Shea 1990b; Finnie et al. 2004; Rutkowski et al. 2008). HOIP:HOIP_0002174 Receiving signal is a subtype of receiving: A process that recognizes another object and changes it into a signal. receiving signal HOIP_0002174 HOIP:HOIP_0002175 The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. This process persists for a certain period or over a long period. This entity is a specific course-dependent process. This process can constitute the course of ER stress (sustained) . protein refolding (sustained) [ER stress] HOIP_0002175 HOIP:HOIP_0002176 Dissociation of IRE1:BIP heterodimer is a subtype of detaching: A process that disaggregates IRE-1-BIP heterodimers into BIP and IRE1. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:10854322 Dissociation of IRE1:BIP Heterodimer [ER stress] HOIP_0002176 PMID:10854322 Perturbation of protein folding promotes reversible dissociation of BiP from the lumenal domains of PERK and IRE1. HOIP:HOIP_0002177 Protein refolding insufficiency is a subtype of malfunctioning process: A process that lacks performing the function of protein refolding required. This entity is a specific course-dependent process. This process can constitute the course of ER stress. protein refolding insufficiency [ER stress] HOIP_0002177 HOIP:HOIP_0002178 A role played by the entity within a toxicological context. toxicological role HOIP_0002178 HOIP:HOIP_0002179 NCBI-Human-GeneID:373156 NCBI-Mouse-GeneID:76263 NCBI-Rat-GeneID:297029 GSTK1 (mol) HOIP_0002179 NCBI-Human-GeneID:373156 http://www.ncbi.nlm.nih.gov/gene/373156 NCBI-Mouse-GeneID:76263 http://www.ncbi.nlm.nih.gov/gene/76263 NCBI-Rat-GeneID:297029 http://www.ncbi.nlm.nih.gov/gene/297029 HOIP:HOIP_0002180 NCBI-Human-GeneID:2950 NCBI-Mouse-GeneID:14870 NCBI-Rat-GeneID:24426 GSTP1 (mol) HOIP_0002180 NCBI-Human-GeneID:2950 http://www.ncbi.nlm.nih.gov/gene/2950 NCBI-Mouse-GeneID:14870 http://www.ncbi.nlm.nih.gov/gene/14870 NCBI-Rat-GeneID:24426 http://www.ncbi.nlm.nih.gov/gene/24426 HOIP:HOIP_0002181 NCBI-Human-GeneID:2952 GSTT1 (mol) HOIP_0002181 NCBI-Human-GeneID:2952 http://www.ncbi.nlm.nih.gov/gene/2952 HOIP:HOIP_0002182 Pancreatic beta cell damage is a subtype of cellular damage: A process that injuries the structure of the pancreatic beta cell as the direct or indirect result of an external force. pancreatic beta cell damage HOIP_0002182 HOIP:HOIP_0002183 Abnormal protein production is a subtype of protein production: A process that makes existent of an abnormal protein due to biosynthesis or secretion resulting in an increase in its levels. abnormal protein production HOIP_0002183 HOIP:HOIP_0002184 A role played by the entity which inhibits or decreases the frequency, rate or extent of the glycosylation of one or more amino acid residues within a protein. related process: GO:0060051 protein glycosylation inhibitor role HOIP_0002184 HOIP:HOIP_0002185 NCBI-Human-GeneID:2953 NCBI-Mouse-GeneID:14872 NCBI-Rat-GeneID:29487 GSTT2 (mol) HOIP_0002185 NCBI-Human-GeneID:2953 http://www.ncbi.nlm.nih.gov/gene/2953 NCBI-Mouse-GeneID:14872 http://www.ncbi.nlm.nih.gov/gene/14872 NCBI-Rat-GeneID:29487 http://www.ncbi.nlm.nih.gov/gene/29487 HOIP:HOIP_0002186 NCBI-Human-GeneID:653689 GSTT2B (mol) HOIP_0002186 NCBI-Human-GeneID:653689 https://www.ncbi.nlm.nih.gov/gene/653689 HOIP:HOIP_0002187 Accumulation of abnormal proteins in ER is a subtype of accumulation of abnormal proteins: A process that keeps abnormal protein(s) in the ER (endoplasmic reticulum). accumulation of abnormal proteins in ER HOIP_0002187 HOIP:HOIP_0002188 Hypofunction of carbohydrate metabolism is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient carbohydrate metabolism. This entity is a specific course-dependent process. This process can constitute the course of ER stress. hypofunction of carbohydrate metabolism [ER stress] HOIP_0002188 HOIP:HOIP_0002189 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. see quality : http://purl.obolibrary.org/obo/HP_0000855 decreasing isulin sensitivity insulin resistance (process) HOIP_0002189 HOIP:HOIP_0002190 Hypofunction of drug metabolism is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient drug metabolism. hypofunction of drug metabolism HOIP_0002190 HOIP:HOIP_0002191 Hypofunction of drug metabolism is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient drug metabolism. This entity is a specific course-dependent process. This process can constitute the course of ER stress. hypofunction of drug metabolism [ER stress] HOIP_0002191 HOIP:HOIP_0002192 Hypofunction of sequestering of calcium ion is a subtype of hypofunctioning: A process that performs a decreased or insufficient sequestering of calcium ion. hypofunction of sequestering of calcium ion HOIP_0002192 HOIP:HOIP_0002193 A role played by a process to maintain homeostasis and to protect the insult. adaptive response HOIP_0002193 HOIP:HOIP_0002194 Hypofunction of sequestering of calcium ion is a subtype of hypofunctioning: A process that performs a decreased or insufficient sequestering of calcium ion. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:27694578 hypofunction of sequestering of calcium ion [ER stress] HOIP_0002194 PMID:27694578 Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5. HOIP:HOIP_0002195 Hypofunction of lipid biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient lipid biosynthesis. hypofunction of lipid biosynthesis HOIP_0002195 HOIP:HOIP_0002196 A role played by the entity which regulates the formation of lipids. lipid synthesis regulator role HOIP_0002196 HOIP:HOIP_0002197 Malfunction of lipid biosynthesis is a subtype of malfunctioning: A process that cannot perform the lipid biosynthesis function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of ER stress. malfunction of lipid biosynthesis [ER stress] HOIP_0002197 HOIP:HOIP_0002198 Malfunctioning of cellular membrane is a subtype of malfunctioning process: A process that cannot perform a cellular membrane function appropriately or cannot realize it at all. malfunctioning of cellular membrane HOIP_0002198 HOIP:HOIP_0002199 Malfunctioning of cellular membrane is a subtype of malfunctioning process: A process that cannot perform a cellular membrane function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of ER stress. malfunctioning of cellular membrane [ER stress] HOIP_0002199 HOIP:HOIP_0002200 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of ER stress. necrosis [ER stress] HOIP_0002200 HOIP:HOIP_0002201 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of ER stress. insulin resistance (process) [ER stress] HOIP_0002201 HOIP:HOIP_0002202 Hepatic cirrhosis is a subtype of changing hardness: A process that changes the hardness of the liver to become hard due to the replacement of normal liver tissue to scar tissue. hepatic cirrhosis HOIP_0002202 HOIP:HOIP_0002203 Hepatic cirrhosis is a subtype of changing hardness: A process that changes the hardness of the liver to become hard due to the replacement of normal liver tissue to scar tissue. This entity is a specific course-dependent process. This process can constitute the course of ER stress. hepatic cirrhosis [ER stress] HOIP_0002203 HOIP:HOIP_0002204 The chemical reactions and pathways resulting in the breakdown of misfolded proteins transported from the endoplasmic reticulum and targeted to cytoplasmic proteasomes for degradation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. ER-associated misfolded protein catabolic process [ER stress] HOIP_0002204 HOIP:HOIP_0002205 NCBI-Human-GeneID:4257 NCBI-Mouse-GeneID:56615 NCBI-Rat-GeneID:171341 MGST1 (mol) HOIP_0002205 NCBI-Human-GeneID:4257 http://www.ncbi.nlm.nih.gov/gene/4257 NCBI-Mouse-GeneID:56615 http://www.ncbi.nlm.nih.gov/gene/56615 NCBI-Rat-GeneID:171341 http://www.ncbi.nlm.nih.gov/gene/171341 HOIP:HOIP_0002206 NCBI-Human-GeneID:4258 NCBI-Mouse-GeneID:211666 NCBI-Rat-GeneID:295037 MGST2 (mol) HOIP_0002206 NCBI-Human-GeneID:4258 http://www.ncbi.nlm.nih.gov/gene/4258 NCBI-Mouse-GeneID:211666 http://www.ncbi.nlm.nih.gov/gene/211666 NCBI-Rat-GeneID:295037 http://www.ncbi.nlm.nih.gov/gene/295037 HOIP:HOIP_0002207 The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. This entity is a specific course-dependent process. This process can constitute the course of ER stress (early stage). PMID:23637286 protein refolding [ER stress (early stage)] HOIP_0002207 HOIP:HOIP_0002208 NCBI-Human-GeneID:4259 NCBI-Mouse-GeneID:66447 NCBI-Rat-GeneID:289197 MGST3 (mol) HOIP_0002208 NCBI-Human-GeneID:4259 http://www.ncbi.nlm.nih.gov/gene/4259 NCBI-Mouse-GeneID:66447 http://www.ncbi.nlm.nih.gov/gene/66447 NCBI-Rat-GeneID:289197 http://www.ncbi.nlm.nih.gov/gene/289197 HOIP:HOIP_0002209 Hypofunction of ATP biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient ATP biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of ER stress. hypofunction of ATP biosynthesis [ER stress] HOIP_0002209 HOIP:HOIP_0002210 Increasing demand for protein refolding is a subtype of increasing functional demand: A process that changes the functional demand for protein refolding to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. increasing demand for protein refolding [ER stress] HOIP_0002210 HOIP:HOIP_0002211 Increasing demand for protein refolding is a subtype of increasing functional demand: A process that changes the functional demand for protein refolding to be higher. increasing demand for protein refolding HOIP_0002211 HOIP:HOIP_0002212 Accumulation of compound in ER is a subtype of accumulation of xenobiotics: A process that keeps compound in the ER (endoplasmic reticulum). accumulation of compound in ER HOIP_0002212 HOIP:HOIP_0002213 Dissociation of PERK:BIP heterodimer is a subtype of detaching: A process that disaggregates PERK-BIP heterodimers into BIP and PERK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:10854322 PMID:11907036 Reactome PathwayStep4038 Reactome:R-HSA-381086 http://www.reactome.org/PathwayBrowser/#/R-HSA-381119&SEL=R-HSA-381086&PATH=R-HSA-392499 PERK (EIF2AK3) is a single-pass transmembrane protein located in the Endoplasmic Reticulum (ER) membrane. PERK has an N-terminal luminal domain and a C-terminal cytosolic domain. It is maintained in an inactive state by association of its luminal domain with BiP, a chaperone in the ER. Because BiP also binds unfolded proteins, BiP dissociates from PERK when unfolded proteins exceed chaperone activity in the ER. Dissociation of PERK:BIP Heterodimer [ER stress] HOIP_0002213 Reactome PathwayStep4038 http://purl.obolibrary.org/obo/HINO_0006880 HOIP:HOIP_0002214 CAD accumulation in lysosome is a subtype of compound accumulation in lysosome: A process that keeps CAD (Cationic Amphiphilic Drugs cationic amphiphile drug) in the lysosome. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). CAD accumulation in lysosome [phospholipidosis (moderate) ] HOIP_0002214 HOIP:HOIP_0002215 The totality of all processes through which the phospholipidosis is realized. PMID:15342952 PMID:16979167 PMID:22960355 http://purl.bioontology.org/ontology/MEDDRA/10074564 phospholipidosis (imbalance course) HOIP_0002215 PMID:15342952 The following four processes were involved in the induction of phospholipidosis; (1) Inhibition of lysosomal phospholipase activivity (2) Inhibition of lysosomal enzyme transport, as demonstrated by the down-regulation of genes involved in lysosomal enzyme transport (3) Enhanced phospholipid biosynthesis, which is supported by the up- regulation of fatty acid biosynthesis-related genes (4) Enhanced cholesterol biosynthesis, as shown by the up-regulation of cholesterol biosynthesis-related genes Increased cholesterol biosynthesis is considered to be an indirect trigger for the reasons: (1) The accumulation of sphingomyelin occurs concurrently with the increase in cholesterol in visceral tissues (e.g., spleen) in patients with Niemann-Pick type C disease (NPC), which is caused by a genetic defect in the cholesterol trafficking protein NPC1 or, in far fewer patients, the sterol regulating protein HE1 (Blanchette-Mackie, 2000; Harzer et al., 2003; Vanier, 1983). (2) The induction of lamellar myelin-like bodies and the accumulation of free cholesterol occur in cultured mouse macrophages that have been incubated with acetylated low density lipoprotein or acyl-CoA:cholesterol acyl- transferase inhibitor (McGookey and Anderson, 1983; Robenek and Schmitz, 1988). In addition, the up- or down-regulation of transporter genes (e.g., facilitated glucose transporter) and genes that control the cell cycle (e.g., cyclin G2) may also be involved. Increase in phospholipid synthesis and impaired membrane recycling and lysosomal enzyme sorting dynamics are also occured. PMID:16979167 Phospholipidosis is the appearance of intracellular accumulation of phospholipids and lamellar bodies, most likely from an impaired phospholipid metabolism of the lysosome. In drug induced phospholipidosis, CAD induces its own specific phospho-lipid composition and selectively targets organs. PMID:22960355 Drug induced phospholipidosis: an acquired lysosomal storage disorder. Biochim Biophys Acta. 2013, 1831(3):602-11. HOIP:HOIP_0002216 A process that changes the activity of the NRF2 to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. NRF2 activation [glutathione depletion (course)] HOIP_0002216 HOIP:HOIP_0002217 A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid degradation severely. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). negative regulation of phospholipid degradation [phospholipidosis (severe)] HOIP_0002217 HOIP:HOIP_0002218 Negative regulation of phospholipase transcription is a subtype of negative regulation of transcription, DNA-templated: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase transcription. negative regulation of phospholipase transcription HOIP_0002218 HOIP:HOIP_0002219 Hypofunction of phospholipase gene expression is a subtype of hypofunction of phospholipase gene expression: A process that performs a decreased or insufficient phospholipase gene expression. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). hypofunction of phospholipase gene expression [phospholipidosis (severe)] HOIP_0002219 HOIP:HOIP_0002220 Lysosomal dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete lysosomal function. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). lysosomal dysfunction [phospholipidosis (severe)] HOIP_0002220 HOIP:HOIP_0002221 Lysosomal dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete lysosomal function. lysosomal dysfunction HOIP_0002221 HOIP:HOIP_0002222 Malfunctioning of cellular membrane is a subtype of malfunctioning process: A process that cannot perform a cellular membrane function appropriately or cannot realize it at all. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). malfunctioning of cellular membrane [phospholipidosis (severe)] HOIP_0002222 HOIP:HOIP_0002223 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of phospholipids. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). positive regulation of phospholipid biosynthetic process [phospholipidosis (severe)] HOIP_0002223 HOIP:HOIP_0002224 glutathione synthetic gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) involved in glutathione synthesis. glutathione synthetic gene expression HOIP_0002224 HOIP:HOIP_0002225 Phospholipid material transport is a subtype of molecule transport: A process that of the directed movement of phospholipid materials into a peroxisome. phospholipid material transport HOIP_0002225 HOIP:HOIP_0002226 Hyperfunction of phospholipid material transport is a subtype of hyperfunction of transport: A process that performs an excesssive phospholipid material transport. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). hyperfunction of phospholipid material transport [phospholipidosis (severe)] HOIP_0002226 HOIP:HOIP_0002227 Increase in intracellular calcium level is a subtype of increase in calcium level: A process that changes the calcium ion concentration within a cell to be higher. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). increase in intracellular calcium level [phospholipidosis (severe)] HOIP_0002227 HOIP:HOIP_0002228 In the imbalance model, the basic units are as follows: In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that inculdes step 1 to 3. The defense performance level and the functional demand level are low, as a result, keeping the balance. This state reflects the adaptation. balance L=L (maintining homeostasis at lower level) HOIP_0002228 HOIP:HOIP_0002229 Increasing uptake amount of mitochondrial calcium ion is a subtype of increasing quantity: A process that changes the uptake amount of mitochondrial calcium ion to be higher. increasing uptake amount of mitochondrial calcium ion HOIP_0002229 HOIP:HOIP_0002230 Hypofunction of ATP biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient ATP biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:24746669 PMID:28789970 PMID:29335519 PMID:30232152 PMID:30250064 PMID:31623280 PMID:31649547 hypofunction of ATP biosynthesis [mitochondrial disorder (course)] HOIP_0002230 PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). PMID:28789970 not reported in the liver. High-level exposures may result in increased fission, which blocks efficient ATP generation and limits rates of functional complementation, in addition to potentially leading to apoptosis. PMID:29335519 Supporting this notion, PCK1 expression in SK-Hep-1 dramatically reduced cellular ATP level by 4 folds in cells cultured in low glucose medium, but not in normal medium (Fig. 4c). In addition, supplement of dimethyl-α-KG may also increase cellular ATP level and alleviate energy stress, as indicated by the decreased phosphorylation of AMPKα1 and ACC (Fig. 5f). PMID:30232152 not reported in liver. Exogenous H2O2 activates AMPK indirectly in myotubes by decreasing the ATP/ADP ratio. We conclude that AMPK activity in response to redox changes is not due to direct action on AMPK itself, but is a secondary consequence of redox effects on other processes, such as mitochondrial ATP production. PMID:30250064 not reported in the liver. Strikingly, NEAT1-depleted single cell clones showed a consistent reduction in mitochondrial DNA (mtDNA) (Fig. 7a), reduced mitochondrial respiration (by detection of the oxygen consumption rate (OCR); Fig. 7b) and adenosine triphosphate (ATP) production (Fig. 7c), reduced OCR and extracellular acidification rate (ECAR) rate (Fig. 7d), suggesting that the aberrant NEAT1 expression could cause mitochondrial dysfunction. PMID:31623280 Mitochondrial-derived ROS also activate AMP-activated protein kinase (AMPK) secondary to redox changes and mitochondrial ATP production. PMID:31649547 Accumulating evidence has shown that defective hepatic mitochondrial respiration characterized by damaged mitochondria accumulation can impair mitochondrial fatty acid β-oxidation, which sequentially causes various adverse consequences, such as excessive ROS, reduced ATP production, and hepatic fatty acid accumulation. HOIP:HOIP_0002231 The directed movement of calcium from the lysosome. release of calcium ion from lysosome HOIP_0002231 HOIP:HOIP_0002232 Increasing uptake amount of mitochondrial calcium ion is a subtype of increasing quantity: A process that changes the uptake amount of mitochondrial calcium ion to be higher. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. increasing uptake amount of mitochondrial calcium ion [phospholipidosis (severe)] HOIP_0002232 HOIP:HOIP_0002233 Decreasing mitochondrial membrane potential is a subtype of decreasing membrane potential: A process that changes the electrical potential of a mitochondrial membrane to be lower. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). decreasing mitochondrial membrane potential [phospholipidosis (severe)] HOIP_0002233 HOIP:HOIP_0002234 Hypofunction of ATP biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient ATP biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). hypofunction of ATP biosynthesis [phospholipidosis (severe)] HOIP_0002234 HOIP:HOIP_0002235 Autolysis is a subtype of dissolving: The disintegration of a cell by rupture of the cell membrane by the action of their own enzymes. MeSH:D001329 autolysis HOIP_0002235 HOIP:HOIP_0002236 Stabilizing membrane structure is a subtype of keeping structure: A process that maintains the membrane structure. stabilizing membrane structure HOIP_0002236 HOIP:HOIP_0002237 Stabilizing lysosomal membrane structure is a subtype of stabilizing membrane structure: A process that maintains the membrane structure in the lysosome. stabilizing lysosomal membrane structure HOIP_0002237 HOIP:HOIP_0002238 Stabilizing lysosomal membrane structure is a subtype of stabilizing membrane structure: A process that maintains the membrane structure in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID:21281795 stabilizing lysosomal membrane structure [phospholipidosis (severe)] HOIP_0002238 PMID:21281795 Attenuation of the lysosomal death pathway by lysosomal cholesterol accumulation. HOIP:HOIP_0002239 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). Negative regulation of apoptotic process might be a defense process prevent the number of cells from decreasing too much. negative regulation of apoptotic process [phospholipidosis (severe (excessive defense))] HOIP_0002239 HOIP:HOIP_0002240 The directed movement of calcium from the lysosome. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. PMID:27977664 release of calcium ion from lysosome [phospholipidosis (severe)] HOIP_0002240 PMID:27977664 Lysosomal Re-acidification Prevents Lysosphingolipid-Induced Lysosomal Impairment and Cellular Toxicity: Neutralization can cause release of lysosomal Ca2+ and cathepsins: Ca2+ release could compromise cytoskeletal function and hence cell division, whereas cathepsin release and activation could initiate cell death. In addition, increasing lysosomal pH would be predicted to decrease function of any lysosomal enzymes evolutionarily optimized for function in an acidic environment. HOIP:HOIP_0002241 Obesity is a subtype of increasing weight: A process that changes the body weight to be higher. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. obesity [phospholipidosis via obese] HOIP_0002241 PMID:27800604 HOIP:HOIP_0002242 Negative regulation of inflammatory response is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. negative regulation of inflammatory response [phospholipidosis (imbalance course)] HOIP_0002242 HOIP:HOIP_0002245 Tumor growth is a subtype of cell growth: The process in which a tumor cell increases in size. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). tumor growth [phospholipidosis (severe (excessive defense))] HOIP_0002245 HOIP:HOIP_0002246 A role played by the entity involved in DNA repair processes including direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. DNA repair role HOIP_0002246 HOIP:HOIP_0002247 A role played by the entity which involves in regulating a cell cycle process. cell cycle regulator role HOIP_0002247 HOIP:HOIP_0002248 Increasing phospholipid metabolite is a subtype of increasing quantity: A process that changes the amount of phospholipid metabolites to be larger. increasing phospholipid metabolite HOIP_0002248 HOIP:HOIP_0002250 Any substance that inhibits the process of fibrosis. fibrosis inhibitor HOIP_0002250 HOIP:HOIP_0002252 Decreasing CAD in lysosomal membranes is a subtype of decreasing quantity: A process that changes the quantity of the Cationic Amphiphilic Drugs (CAD) in lysosomal membranes to be smaller. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). decreasing CAD in lysosomal membranes [phospholipidosis (normal course)] HOIP_0002252 HOIP:HOIP_0002253 Decreasing CAD in lysosomal membranes is a subtype of decreasing quantity: A process that changes the quantity of the Cationic Amphiphilic Drugs (CAD) in lysosomal membranes to be smaller. decreasing CAD in lysosomal membranes HOIP_0002253 HOIP:HOIP_0002254 glutathione synthetic gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) involved in glutathione synthesis. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. glutathione synthetic gene expression [glutathione depletion (course)] HOIP_0002254 HOIP:HOIP_0002255 Any process that increases the rate, frequency, or extent of phospholipid catabolism, the chemical reactions and pathways resulting in the breakdown of phospholipids, any lipid containing phosphoric acid as a mono- or diester. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). positive regulation of phospholipid catabolic process [phospholipidosis (normal course)] HOIP_0002255 HOIP:HOIP_0002256 Hyperfunction of phospholipase gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive phospholipase gene expression. hyperfunction of phospholipase gene expression HOIP_0002256 HOIP:HOIP_0002257 Hyperfunction of phospholipase gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive phospholipase gene expression. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). hyperfunction of phospholipase gene expression [phospholipidosis (normal course)] HOIP_0002257 HOIP:HOIP_0002258 Keeping acidic environment in lysosome is a subtype of keeping quality: A process that maintains the acidic environment within the interior of the lysosomes. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). keeping acidic environment in lysosome [phospholipidosis (normal course)] HOIP_0002258 HOIP:HOIP_0002259 Keeping acidic environment in lysosome is a subtype of keeping quality: A process that maintains the acidic environment within the interior of the lysosomes. keeping acidic environment in lysosome HOIP_0002259 HOIP:HOIP_0002261 A role played by the entity which positively regulates the process of tumor cell growth. positive regulator of tumor growth HOIP_0002261 HOIP:HOIP_0002262 A role played by the entity within a pharmacological context. drug-metabolizing enzyme role HOIP_0002262 HOIP:HOIP_0002263 Increasing number of macrophage derived foam cell (niemann pick cell) is a subtype of increasing number of objects: A process that becomes larger in the number of foam cell, a type of macrophage (niemann pick cell) containing lipids in small vacuoles, in the liver. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B. increasing number of macrophage derived foam cell (niemann pick cell) [course of Niemann–Pick disease type A and type B] HOIP_0002263 HOIP:HOIP_0002264 Hepatic cirrhosis is a subtype of changing hardness: A process that changes the hardness of the liver to become hard due to the replacement of normal liver tissue to scar tissue. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). hepatic cirrhosis [phospholipidosis (severe (excessive defense))] HOIP_0002264 HOIP:HOIP_0002265 Inflammatory cytokine gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). PMID:26241657 inflammatory cytokine gene expression [phospholipidosis (severe (excessive defense))] HOIP_0002265 PMID:26241657 HOIP:HOIP_0002266 Inflammatory cytokine gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA). inflammatory cytokine gene expression HOIP_0002266 HOIP:HOIP_0002269 A role played by the entity that positively regulates the process of cell cycle. positive regulator of cell cycle role HOIP_0002269 HOIP:HOIP_0002270 A role played by the entity that positively regulates the process of cell cycle arrest. positive regulator of cell cycle arrest role HOIP_0002270 HOIP:HOIP_0002271 A role played by the entity which positively regulates the process of cell proliferation. positive regulator of cell proliferation HOIP_0002271 HOIP:HOIP_0002272 A role played by the entity which positively regulates the process of tumor cell proliferation. positive regulator of tumor cell proliferation HOIP_0002272 HOIP:HOIP_0002273 Any process involved in the maintenance of an internal steady state of phospholipid within an organism or cell. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). maintaining phospholipid homeostasis [phospholipidosis (latent)] HOIP_0002273 HOIP:HOIP_0002274 Hyperfunction of biological defense function is a subtype of hyperfunction of defensive function: A process that performs an excessive biological defensive function. hyperfunction of biological defense function HOIP_0002274 HOIP:HOIP_0002275 Hyperfunction of cell survival is a subtype of hyperfunctioning: A process that performs an excesssive cell survival. hyperfunction of cell survival HOIP_0002275 HOIP:HOIP_0002276 Hyperfunction of cell survival is a subtype of hyperfunctioning: A process that performs an excesssive cell survival. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). hyperfunction of cell survival [phospholipidosis (severe (excessive defense))] HOIP_0002276 HOIP:HOIP_0002279 Hyperfunction of removing is a subtype of hyperfunctioning: A process that performs an excessive removal function. hyperfunction of removing HOIP_0002279 HOIP:HOIP_0002281 A pathologic process that involves the transformation of normal cells to a neoplastic state. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). carcinogenesis [phospholipidosis (severe (excessive defense))] HOIP_0002281 HOIP:HOIP_0002282 Converting type is a subtype of changing an operand: A process that changes the type, kind, or class of the operand. converting type HOIP_0002282 HOIP:HOIP_0002283 Catalysis role of the hydrolysis of a lipid or phospholipid. EC:3.1.1 related molecular function: GO:0016298 lipase HOIP_0002283 HOIP:HOIP_0002284 A role played by an entity that responds to immunity. immune responsor role HOIP_0002284 HOIP:HOIP_0002285 Glutathione depletion dependent gene is a subtype of course dependent chemical entity. This gene can participate in the course of glutathione depletion as a gene product. Gene profile:Mice glutathione depletion dependent gene [mouse] HOIP_0002285 HOIP:HOIP_0002286 A role played by the entity that ipositive regulates the cytokine production. cytokine production inducer HOIP_0002286 HOIP:HOIP_0002287 A role played by the entity that ipositive regulates the IL-2 production. IL-2 production inducer HOIP_0002287 HOIP:HOIP_0002289 A role played by the entity which inhibits the process of infmammatory response. inhibitor of immune response HOIP_0002289 HOIP:HOIP_0002291 NCBI-Mouse-GeneID:14864 PMID:22496397 PMID:25202346 Gstm3 (mouse)[glutathione depletion (course)] HOIP_0002291 NCBI-Mouse-GeneID:14864 http://www.ncbi.nlm.nih.gov/gene/14864 PMID:22496397 Coordinated regulation of hepatic phase I and II drug-metabolizing genes and transporters using AhR-, CAR-, PXR-, PPARα-, and Nrf2-null mice. PMID:25202346 GSTM3 overexpression sensitized the PLC/PRF/5R cells to radiation mainly though induction of apoptosis. GSTM3 increased the expression of cell cycle- and apoptosis-related genes (Bcl-2, Bax, p21, p27 and p53) in PRF/PLC/5R cells with irradiation HOIP:HOIP_0002292 Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. PTK related molecular function GO:0004713 protein tyrosine kinase HOIP_0002292 HOIP:HOIP_0002293 Phospholipid metabolism balance is a subtype of maintaining balance: A process that keeps a balance of phospholipid metabolism. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). phospholipid metabolism balance [phospholipidosis (latent) ] HOIP_0002293 HOIP:HOIP_0002295 Hypofunction of phospholipase gene expression is a subtype of hypofunction of transcription, DNA-templated: A process that performs a decreased or insufficient phospholipase gene expression. decreasing function of phospholipase transcription, DNA-templated hypofunction of phospholipase gene expression HOIP_0002295 HOIP:HOIP_0002297 Any process that stops, prevents, or reduces the frequency, rate or extent of endocytosis. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). negative regulation of endocytosis [phospholipidosis (severe)] HOIP_0002297 HOIP:HOIP_0002298 NCBI-Human-GeneID:5599 NCBI-Mouse-GeneID:26419 NCBI-Rat-GeneID:116554 JNK (canonical)[glutathione depletion (course)] HOIP_0002298 NCBI-Human-GeneID:5599 http://www.ncbi.nlm.nih.gov/gene/5599 NCBI-Mouse-GeneID:26419 http://www.ncbi.nlm.nih.gov/gene/26419 NCBI-Rat-GeneID:116554 http://www.ncbi.nlm.nih.gov/gene/116554 HOIP:HOIP_0002299 Catalysis role of the reaction: ATP + creatine = N-phosphocreatine + ADP + 2 H(+). In both mammals and birds, the creatine kinase (CK) family consists of four types of genes: cytosolic brain type (B-CK); cytosolic muscle type (M-CK); mitochondrial ubiquitous, acidic type (Mia-CK); and mitochondrial sarcomeric, basic type (Mib-CK). In both mammals and birds, the creatine kinase (CK) family consists of four types of genes: cytosolic brain type (B-CK); cytosolic muscle type (M-CK); mitochondrial ubiquitous, acidic type (Mia-CK); and mitochondrial sarcomeric, basic type (Mib-CK). EC:2.7.3.2 IMR:0002602 (obsolete) related molecular function GO:0004111 creatine kinase HOIP_0002299 In both mammals and birds, the creatine kinase (CK) family consists of four types of genes: cytosolic brain type (B-CK); cytosolic muscle type (M-CK); mitochondrial ubiquitous, acidic type (Mia-CK); and mitochondrial sarcomeric, basic type (Mib-CK). PMID:8662608 HOIP:HOIP_0002300 PMID:23856494 GCLM (canonical)[glutathione depletion (course)] HOIP_0002300 PMID:23856494 GSH is synthesized by two successive enzymatic reactions (Fig. 1). The first reaction, catalyzed by glutamate cysteine ligase (GCL), couples L-glutamate to L-cysteine to form γ-glutamylcysteine (γ-GC) . HOIP:HOIP_0002301 Increasing demand for response to mitochondrial oxidative stress is a subtype of increasing demand for response to oxidative stress: A process that changes the functional demand for the response to the mitochondrial oxidative stress to be higher. increasing demand for response to mitochondrial oxidative stress HOIP_0002301 HOIP:HOIP_0002302 Glutathione conjugation (supply) - function demand imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance between glutathione conjugation supply and demand. Glutathione conjugation (supply) - function demand imbalance HOIP_0002302 HOIP:HOIP_0002303 Hyperfunction of biological repair function is a subtype of hyperfunctioning: A process that performs an excessive biological repair function. hyperfunction of biological repair function HOIP_0002303 HOIP:HOIP_0002304 Hypofunction of xenobiotics conjugate excretion is a subtype of hypofunction of liver's excretion: A process that performs a decreased or insufficient xenobiotics conjugate excretion. hypofunction of xenobiotics conjugate excretion HOIP_0002304 HOIP:HOIP_0002305 Decreasing excretion quantity of bile acid is a subtype of decreasing quantity: A process that changes the excretion quantity of of bile acids to be lower. decreasing excretion quantity of the bile acid HOIP_0002305 HOIP:HOIP_0002306 Catalysis of the transfer of acyl groups from an acyl-CoA to lysophosphatidic acid to form phosphatidic acid. EC:2.3.1.51 Lysophosphatidic acid (LPA) acyltransferase (LPAAT), also known as 1-acyl sn-glycerol-3-phosphate acyltransferase (1-AGPAT) (EC 2.3.1.51), catalyzes the conversion of LPA to phosphatidic acid (PA). LPAAT related molecular function GO:0042171 lysophosphatidic acid acyltransferase HOIP_0002306 Lysophosphatidic acid (LPA) acyltransferase (LPAAT), also known as 1-acyl sn-glycerol-3-phosphate acyltransferase (1-AGPAT) (EC 2.3.1.51), catalyzes the conversion of LPA to phosphatidic acid (PA). PMID:11487472 HOIP:HOIP_0002307 Catalysis role of the reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate. Catalysis role of the reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate. cacordase activity cacordase activity glycerol ester hydrolase activity glycerol ester hydrolase activity glycerol-ester hydrolase activity glycerol-ester hydrolase activity triacylglycerol acylhydrolase activity triacylglycerol acylhydrolase activity triacylglycerol ester hydrolase activity triacylglycerol ester hydrolase activity triacylglycerol lipase activity triacylglycerol lipase activity tributyrin esterase activity tributyrin esterase activity tributyrinase activity tributyrinase activity related molecular finction GO:0004806 triglyceride lipase HOIP_0002307 Catalysis role of the reaction: triacylglycerol + H2O = diacylglycerol + a carboxylate. EC:3.1.1.3 cacordase activity EC:3.1.1.3 glycerol ester hydrolase activity EC:3.1.1.3 glycerol-ester hydrolase activity EC:3.1.1.3 triacylglycerol acylhydrolase activity EC:3.1.1.3 triacylglycerol ester hydrolase activity EC:3.1.1.3 triacylglycerol lipase activity EC:3.1.1.3 tributyrin esterase activity EC:3.1.1.3 tributyrinase activity EC:3.1.1.3 HOIP:HOIP_0002308 Phospholipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of phospholipid metabolism. phospholipid metabolism imbalance HOIP_0002308 HOIP:HOIP_0002310 Dysfunction of glycerophospholipid degradation is a subtype of dysfunction of phospholipid degradation: A process that performs an abnormal and incomplete glycerophospholipid degradation. dysfunction of glycerophospholipid degradation HOIP_0002310 HOIP:HOIP_0002312 Dysfunction ofphosphatidylinositol degradation is a subtype of dysfunction of glycerophospholipid degradation: A process that performs an abnormal and incomplete phosphatidylinositol degradation. dysfunction ofphosphatidylinositol degradation HOIP_0002312 HOIP:HOIP_0002313 Dysfunction of phosphatidylethanolamine degradation is a subtype of dysfunction of glycerophospholipid degradation: A process that performs an abnormal and incomplete phosphatidylethanolamine degradation. dysfunction of phosphatidylethanolamine degradation HOIP_0002313 HOIP:HOIP_0002314 Dysfunction of phosphatidylglycerol degradation is a subtype of dysfunction of glycerophospholipid degradation: A process that performs an abnormal and incomplete phosphatidylglycerol degradation. dysfunction of phosphatidylglycerol degradation HOIP_0002314 HOIP:HOIP_0002315 Dysfunction of phosphatidylcholine degradation is a subtype of dysfunction of glycerophospholipid degradation: A process that performs an abnormal and incomplete phosphatidylcholine degradation. dysfunction of phosphatidylcholine degradation HOIP_0002315 HOIP:HOIP_0002316 Dysfunction of phosphatidyl-L-serine degradation is a subtype of dysfunction of glycerophospholipid degradation: A process that performs an abnormal and incomplete phosphatidyl-L-serine degradation. dysfunction of phosphatidyl-L-serine degradation HOIP_0002316 HOIP:HOIP_0002317 Dysfunction of phosphatidic acid degradation is a subtype of dysfunction of glycerophospholipid degradation: A process that performs an abnormal and incomplete phosphatidic acid degradation. dysfunction of phosphatidic acid degradation HOIP_0002317 HOIP:HOIP_0002318 Hyperfunction of cell proliferation is a subtype of hyperfunction of increasing number: A process that performs an excessive cell proliferation. hyperfunction of cell proliferation HOIP_0002318 HOIP:HOIP_0002321 Hyperfunction of hepatocyte proliferation is a subtype of hyperfunction of cell proliferation: The multiplication or reproduction of hepatocytes, resulting in the expansion of a cell population. Hepatocytes form the main structural component of the liver. They are specialized epithelial cells that are organized into interconnected plates called lobules. hyperfunction of hepatocyte proliferation HOIP_0002321 HOIP:HOIP_0002324 Phospholipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of phospholipid metabolism. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). phospholipid metabolism imbalance [phospholipidosis (imbalance course)] HOIP_0002324 HOIP:HOIP_0002325 Accumulation of drug in hepatocyte is a subtype of accumulation of xenobiotics: A process that keeps compound in the hepatocyte. accumulation of drug in hepatocyte HOIP_0002325 HOIP:HOIP_0002326 Increasing demand for NAPQI metabolism is a subtype of increasing functional demand: A process changes the functional demand for the for NAPQI metabolism to be higher. increasing demand for NAPQI metabolism HOIP_0002326 HOIP:HOIP_0002327 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that inculdes step 1 to 4. The defense performance level is very low (L) than the moderate (M) in normal condition. Threfore even if the functional demand level is Moderatelevel (M) in the daily life in the helathy person, which leads to the imbalance and leads to abnormal manifestation. imbalance VL(defense) HOIP_0002327 HOIP:HOIP_0002328 The level of degree is very low. very low level HOIP_0002328 HOIP:HOIP_0002329 The totality of all processes through which hepatic fibrosis is realized. PMID:15690074 PMID:21497738 PMID:24966597 PMID:25869468 PMID:29391303 PMID:30002817 under construction hepatic fibrosis course HOIP_0002329 HOIP:HOIP_0002330 Hypofunction of drug metabolism phase II is a subtype of hypofunction of drug metabolism: A process that performs a decreased or insufficient drug metabolism phase II. hypofunction of drug metabolism phase II HOIP_0002330 HOIP:HOIP_0002331 NCBI-Human-GeneID:2729 NCBI-Mouse-GeneID:14629 NCBI-Rat-GeneID:25283 glutamate-cysteine ligase modifier subunit HOIP_0002331 NCBI-Human-GeneID:2729 http://www.ncbi.nlm.nih.gov/gene/2729 NCBI-Mouse-GeneID:14629 http://www.ncbi.nlm.nih.gov/gene/14629 NCBI-Rat-GeneID:25283 http://www.ncbi.nlm.nih.gov/gene/25283 HOIP:HOIP_0002332 Hyperfunction of drug metabolizing enzyme gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive drug metabolizing enzyme gene expression. hyperfunction of drug metabolizing enzyme gene expression HOIP_0002332 HOIP:HOIP_0002333 Increasing number of dead cells in liver is a subtype of cell proliferation: A process that becomes larger in the number of dead cells in the liver. This entity is a specific course-dependent process. This process can constitute the course of oxidative stress. increasing number of dead cells in liver [oxidative stress (course)] HOIP_0002333 HOIP:HOIP_0002334 Cel cycle related gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature cell cycle related gene product or products (proteins or RNA). cel cycle related gene expression HOIP_0002334 HOIP:HOIP_0002335 Hyperfunction of fatty acid biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive fatty acid biosynthesis. hyperfunction of fatty acid biosynthesis HOIP_0002335 HOIP:HOIP_0002336 Lipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of lipid metabolism. lipid metabolism imbalance HOIP_0002336 HOIP:HOIP_0002337 Hyperfunction of lipid biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive lipid biosynthesis. hyperfunction of lipid biosynthesis HOIP_0002337 HOIP:HOIP_0002338 Hyperfunction of lipid synthetic gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive lipid biosynthetic gene expression. hyperfunction of lipid synthetic gene expression HOIP_0002338 HOIP:HOIP_0002339 Lipid vacuole organization is a subtype of vacuole organization: A process that s carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid vacuole. lipid vacuole organization HOIP_0002339 HOIP:HOIP_0002341 Leaking proton ion is a subtype of leaking: A process that leaks the proton from the mitochondria. leaking proton ion HOIP_0002341 HOIP:HOIP_0002342 Negative regulation of respiratory electron transport chain is a subtype of negative regulation process: Any process that stops, prevents or reduces the frequency, rate or extent of mrespiratory electron transport chain. negative regulation of respiratory electron transport chain HOIP_0002342 HOIP:HOIP_0002343 Changing iron ion concentration is a subtype of changing concentration: A process that changes the iron (Fe) concentration in the blood to be lower. changing iron ion concentration HOIP_0002343 HOIP:HOIP_0002344 Hyperfunction of mitochondrial fatty acid beta-oxidation is a subtype of hyperfunction of fatty acid beta-oxidation: A process that performs an excessive mitochondrial fatty acid beta-oxidation. hyperfunction of mitochondrial fatty acid beta-oxidation HOIP_0002344 HOIP:HOIP_0002345 Hyperfunction of gene expression is a subtype of hyperfunctioning: A process that performs an excesssive gene expression. hyperfunction of gene expression HOIP_0002345 HOIP:HOIP_0002346 Hyperfunction of biosynthesis is a subtype of hyperfunctioning: A process that performs an excessive biosynthesis. hyperfunction of biosynthesis HOIP_0002346 HOIP:HOIP_0002347 Hyperfunction of drug metabolism is a subtype of hyperfunctioning of metabolism: A process that performs an excessive drug metabolism. hyperfunction of drug metabolism HOIP_0002347 HOIP:HOIP_0002348 Decreasing bile flow in bile canaliculus is a subtype of decreasing bile flow: A process that changes the amount of bile flow in bile canaliculus to be lower. decreasing bile flow in bile canaliculus HOIP_0002348 HOIP:HOIP_0002349 Hyperfunction of decompoing is a subtype of hyperfunctioning: A process that performs an excessive decomposition. hyperfunction of decompoing HOIP_0002349 HOIP:HOIP_0002350 A role played by the entity for peroxisome proliferation peroxisome proliferator HOIP_0002350 HOIP:HOIP_0002351 Hyperfunction of transport is a subtype of hyperfunctioning: A process that performs an excesssive transport. hyperfunction of transport HOIP_0002351 HOIP:HOIP_0002352 Hyperfunction of metabolism is a subtype of hyperfunctioning: A process that performs an excessive metabolism. hyperfunction of metabolism HOIP_0002352 HOIP:HOIP_0002353 A role played by the entity that activates or increases the frequency, rate or extent of feeding behavior. positive regulator role of feeding behavior HOIP_0002353 HOIP:HOIP_0002354 Hypofunction of metabolism is a subtype of hypofunction of changing between operands: A process that performs a decreased or insufficient metabolism. hypofunction of metabolism HOIP_0002354 HOIP:HOIP_0002355 Hypofunction of removing is a subtype of hypofunctioning: A process that performs a decreased or insufficient removing. hypofunction of removing HOIP_0002355 HOIP:HOIP_0002356 Hypofunction of transcription, DNA-templated is a subtype of hypofunctioning: A process that hypofunction of transcription, DNA-templated decreasing function of transcription, DNA-templated hypofunction of transcription, DNA-templated HOIP_0002356 HOIP:HOIP_0002357 PPARalpha inactivation is a subtype of inactivation: A process that changes the activity of the activating PPAR alpha (Peroxisome Proliferator Activated Receptor Alpha) with a nuclear receptor role to be lower. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. Reactome The set of genes regulated by PPAR-alpha is not fully known in humans, however many examples have been found in mice. Genes directly activated by PPAR-alpha contain peroxisome proliferator receptor elements (PPREs) in their promoters and include: 1) genes involved in fatty acid oxidation and ketogenesis (Acox1, Cyp4a, Acadm, Hmgcs2); 2) genes involved in fatty acid transport (Cd36, , Slc27a1, Fabp1, Cpt1a, Cpt2); 3) genes involved in producing fatty acids and very low density lipoproteins (Me1, Scd1); 4) genes encoding apolipoproteins (Apoa1, Apoa2, Apoa5); 5) genes involved in triglyceride clearance ( Angptl4); 6) genes involved in glycerol metabolism (Gpd1 in mouse); PMID:17854140 PPARalpha inactivation [alcoholic fatty liver] HOIP_0002357 PMID:17854140 Ethanol administration to rodents or ethanol exposure to ethanol-metabolizing cultured cells causes a general down-regulation of PPAR-α. Further, RXR-PPAR-α extracted from hepatoma cells previously exposed to ethanol or acetaldehyde binds poorly to an oligonucleotide containing peroxisome proliferator response elements, indicating that acetaldehyde is responsible for the action of ethanol. It is possible that acetaldehyde, because of its ability to covalently bind proteins can form adducts with the PPAR-α transcription complex, thereby preventing its ability to bind the promoter element(s). It is also noteworthy that ethanol-elicited inhibition of fatty acid oxidation can be reversed, as demonstrated by experiments in which ethanol-fed animals were co-treated with the PPAR-α agonist, WY14, 643. Fatty liver was blocked in these animals due to induction of PPAR-α, which, in turn, accelerated fatty acid oxidation thereby preventing ethanol-elicited fatty liver HOIP:HOIP_0002358 A role played by the entity which regulates lipid metabolic process. lipid metabolic regulator role HOIP_0002358 HOIP:HOIP_0002359 Hyperfunction of moving drug to the inside of liver is a subtype of hyperfunction of moving A to the inside of B: A process that performs an excesssive moving drug to the inside of liver. hyperfunction of moving drug to the inside of liver HOIP_0002359 HOIP:HOIP_0002360 Hyperfunction of defensive function is a subtype of hyperfunctioning: A process that performs an excessive defensive function. hyperfunction of defensive function HOIP_0002360 HOIP:HOIP_0002361 Mitochondrial dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete mitochondrial function. mitochondrial dysfunction HOIP_0002361 HOIP:HOIP_0002362 A role played by the entity which positively regulates the formation of phospholipids. phospholipid biosynthetic positive regulator role HOIP_0002362 HOIP:HOIP_0002363 Cell survial is a subtype of keeong quantity: A process that keeps the viability of a cell. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. cell survival [glutathione depletion (course)] HOIP_0002363 HOIP:HOIP_0002364 Increasing drug metabolite is a subtype of increasing quantity: A process that changes the amount of drug metabolites to be higher. increasing drug metabolite HOIP_0002364 HOIP:HOIP_0002366 Dissociation of Nrf2-Keap1 complex is a subtype of detaching: A process that disaggregates a Nrf2-Keap1 complexe into Nrf2 and Keap1. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. dissociation of Nrf2-Keap1 complex [glutathione depletion (course)] HOIP_0002366 HOIP:HOIP_0002367 Activation of thioredoxin pathway is a subtype of activating: A process that changes the activity of the thioredoxin pathway to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:20463017 activation of thioredoxin pathway [glutathione depletion (course)] HOIP_0002367 PMID:20463017 Under GSH deprivation, the cytosolic thioredoxin/thioredoxin reductase system plays an essential role for the cells to deal with the excess amount of intracellular cystine. HOIP:HOIP_0002368 Hyperfunction of anti-oxidative stress is a subtype of hyperfunctioning: A process that performs an excesssive response to oxidative stress. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of anti-oxidative stress [glutathione depletion (course)] HOIP_0002368 HOIP:HOIP_0002369 P53 signaling is a process that a signal is transmitted by p53. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. p53 signaling [glutathione depletion (course)] HOIP_0002369 HOIP:HOIP_0002370 Caspase signaling is a process that a signal is transmitted by the caspase. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. caspase signaling [glutathione depletion (course)] HOIP_0002370 HOIP:HOIP_0002371 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:19662025 apoptotic process [glutathione depletion (course)] HOIP_0002371 PMID:19662025 Cell Death and Differentiation (2009) 16, 1303–1314; Apoptosis and glutathione: beyond an antioxidant Glutathione (GSH) depletion is a common feature of apoptotic cell death triggered by a wide variety of stimuli including activation of death receptors, stress, environmental agents, and cytotoxic drugs. Although initial studies suggested that GSH depletion was only a byproduct of oxidative stress generated during cell death, recent discoveries suggest that GSH depletion and post-translational modifications of proteins through glutathionylation are critical regulators of apoptosis. GSH is essential for cell survival as the GSH-depleted knock-out mouse of γ-GCS dies from massive apoptotic cell death. As the availability of cysteine is the rate-limiting factor in GSH formation, cysteine starvation has been shown to induce apoptosis by GSH depletion. HOIP:HOIP_0002372 Increasing number of dead cells in liver is a subtype of cell proliferation: A process that becomes larger in the number of dead cells in the liver. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. increasing number of dead cells in liver [glutathione depletion (course)] HOIP_0002372 HOIP:HOIP_0002373 Liver dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete liver function. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. liver dysfunction [glutathione depletion (course)] HOIP_0002373 HOIP:HOIP_0002374 A role played by the entity that activates the activity of cytochrome P450 involved in catalysis of organic substances. p450 activator HOIP_0002374 HOIP:HOIP_0002375 JNK signaling is a process that a signal is transmitted by the JNK (a stress-activated protein kinase (SAPK) ). This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:18337250 JNK signaling [glutathione depletion (course)] HOIP_0002375 PMID:18931691 PMID:18337250 APAP-induced liver injury involves JNK activation, due to increased reactive oxygen species generated by GSH-depleted mitochondria, and translocation of activated JNK to mitochondria where JNK induces mitochondrial permeability transition and inhibits mitochondria bioenergetics. HOIP:HOIP_0002376 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. regulation of cell cycle [glutathione depletion (course)] HOIP_0002376 HOIP:HOIP_0002377 Keap1 oxidative modification by electrophiles is a subtype of protein binding: Interacting between a protein and electrophiles. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. Keap1 oxidative modification by electrophiles HOIP_0002377 HOIP:HOIP_0002378 A process that changes the activity of the eIF2a by PERK. This process is dependent on the PERK-eIF2A pathway and can constitute the course of ER stress. changing activity of eIF2a by PERK [ER stress PERK - eIF2A pathway] HOIP_0002378 HOIP:HOIP_0002379 A metabolic process that generates a pool of NADPH by the reduction of NADP+. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:24287781 NADPH regeneration [glutathione depletion (course)] HOIP_0002379 PMID:24287781 Nat Rev Drug Discov. 2013 Dec;12(12):931-47. doi: 10.1038/nrd4002. Modulation of oxidative stress as an anticancer strategy. Both GSH and TXN utilize NADPH to regenerate themselves once they have reduced reactive oxygen species (ROS). These are all upregulated by NRF2. HOIP:HOIP_0002380 Keap1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the Keap1 to be lower. Keap1 inactivation HOIP_0002380 HOIP:HOIP_0002381 Abnormality of membrane is a subtype of changing abnormal cellular structure: A process that changes the membrane stucture abnormally. The degree is severe. This entity is a specific course-dependent process. This process can constitute the course of necrosis. abnormality of membrane (severe) [necrosis (course)] HOIP_0002381 HOIP:HOIP_0002382 TP53 - cell cycle regulation factor (canonical) [cell death (course)] HOIP_0002382 HOIP:HOIP_0002384 Chaperon production is a subtype of protein production: A process that makes existent of a protein with a chaperon role due to biosynthesis or secretion resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Generating a chparon protein is a generating process to make a protein as an output in the course of ER stress. chaperon production [ER stress] HOIP_0002384 HOIP:HOIP_0002385 NCBI-Human-GeneID:3309 NCBI-Mouse-GeneID:14828 NCBI-Rat-GeneID:25617 PMID:12110171 PMID:8020977 BIP [ER stress] HEL-S-89n [ER stress] HSPA5 [ER stress] Heat Shock Protein Family A (Hsp70) Member 5 [ER stress] MIF2 [ER stress] GRP78 (canonical)[ER stress] HOIP_0002385 NCBI-Human-GeneID:3309 http://www.ncbi.nlm.nih.gov/gene/3309 NCBI-Mouse-GeneID:14828 http://www.ncbi.nlm.nih.gov/gene/14828 NCBI-Rat-GeneID:25617 http://www.ncbi.nlm.nih.gov/gene/25617 PMID:12110171 ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. PMID:8020977 Localization of the gene encoding human BiP/GRP78, the endoplasmic reticulum cognate of the HSP70 family, to chromosome 9q34. Genomics 20: 281-284, 1994. BiP/GRP78 is a member of the HSP70 family involved in the folding and assembly of proteins in the endoplasmic reticulum. HOIP:HOIP_0002387 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of necrosis. necrosis [necrosis (course)] HOIP_0002387 HOIP:HOIP_0002388 The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. REACT:1213.3 apoptotic DNA fragmentation [apoptosis (course)] HOIP_0002388 HOIP:HOIP_0002389 Increasing cell volume is a changing process to change the volume of the cell to increase. This entity is a specific course-dependent process. This process can constitute the course of necrosis. cell swelling [necrosis (course)] increasing cell volume [necrosis (course)] HOIP_0002389 HOIP:HOIP_0002390 reduced oxygenation of body tissues resulting in the decreased pressure of this component of body gases; commonly due to hypoxemia This entity is a specific course-dependent process. This process can constitute the course of cell death. hypoxia [cell death (course)] HOIP_0002390 HOIP:HOIP_0002392 NCBI-Human-GeneID:4780 NCBI-Mouse-GeneID:18024 NCBI-Rat-GeneID:83619 NRF2 (canonical)[glutathione depletion (course)] HOIP_0002392 NCBI-Human-GeneID:4780 http://www.ncbi.nlm.nih.gov/gene/4870 NCBI-Mouse-GeneID:18024 http://www.ncbi.nlm.nih.gov/gene/18024 NCBI-Rat-GeneID:83619 http://www.ncbi.nlm.nih.gov/gene/363735 HOIP:HOIP_0002393 Refolding gene expression by ATF6 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the protein refolding function by ATF6. This process is dependent on the refolding and can constitute the course of ER stress. PMID:11779464 PMID:17765679 PMID:27346803 refolding gene expression by ATF6 [ER stress - refolding] HOIP_0002393 PMID:27346803 PMID:18319259 PMID:27346803 PMID:11779464 PMID:17765679 PMID:11779464 The active form of ATF6 is produced faster than that of XBP1 in ER-stressed cells because the former is derived from preexisting precursor protein, whereas the latter must be newly translated from mRNA that is transcriptionally induced and then spliced. XBP1 can function in a more sustained fashion than ATF6 because, once produced, the spliced form of XBP1 can keep activating transcription by autoregulating its own transcription as far as IRE1 is activated. In contrast, ATF6 mRNA is not upregulated during ER stress. Low levels of ER stress may be dealt with only by proteolytic activation of ATF6, medium to high levels of ER stress may be handled by activating both ATF6 and IRE1-XBP1 systems, and extremely high levels of ER stress may be overcome by multiple rounds of activation of the XBP1 cycle. PMID:27346803 On release from BiP, ATF6α transfers to the Golgi compartment where it is processed by the Golgi enzymes site 1 protease (S1P) and S2P to produce a cytosolic p50 fragment that migrates to the nucleus. The p50 fragment activates the expression of genes encoding proteins that function to increase ER capacity and folding (including, BiP, GRP94, p58IPK (also known as DNAJC3) and XBP1), as well as the ERAD pathway HOIP:HOIP_0002394 A role played by the entity which is a first rate-limiting enzyme and regulates the glutathione biosynthetic process. glutathione biosynthetic limiting enzyme agent role HOIP_0002394 HOIP:HOIP_0002395 A role that stimulates a cell to grow or proliferate. Most growth factors have other actions besides the induction of cell growth or proliferation. Extracellular polypeptide signal molecule that can stimulate a cell grow or proliferate. Examples are EGF and PDGF. Most growth factors also have other actions. Extracellular polypeptide signal molecule that can stimulate a cell grow or proliferate. Examples are EGF and PDGF. Most growth factors also have other actions. GO:0008083 IMR:0000030 (obsolete) Growth Substance growth factor role HOIP_0002395 Extracellular polypeptide signal molecule that can stimulate a cell grow or proliferate. Examples are EGF and PDGF. Most growth factors also have other actions. ISBN:0815340729 HOIP:HOIP_0002396 A role played by the entity which involves in poritively regulating a gulutathione expression process. glutathione expression positive regulator role HOIP_0002396 HOIP:HOIP_0002397 A role played by the entity which induces the process of cell death. cell death inducer HOIP_0002397 HOIP:HOIP_0002398 CDK5R1(mol) HOIP_0002398 HOIP:HOIP_0002399 An enzyme inhibitor that interferes with the activity of p53. p53 inhibitor HOIP_0002399 HOIP:HOIP_0002400 A role played by the entity which positively regulates the glutathione biosynthetic process. glutathione biosynthetic promoting agent HOIP_0002400 HOIP:HOIP_0002401 A role played by small molecule that is formed in or released into the cytosol in response to an extracellular signal and helps to relay the signal to the interior of the cell. Examples include cAMP, IP3, and Ca++. second messenger HOIP_0002401 HOIP:HOIP_0002402 A role played by the entity which positively regulates the reduced glutathione biosynthetic process reduced glutathione biosynthetic promoting agent HOIP_0002402 HOIP:HOIP_0002403 The process that results in the movement of cytochrome c from the mitochondrial intermembrane space into the cytosol, which is part of the apoptotic signaling pathway and leads to caspase activation. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. release of cytochrome c from mitochondria [apoptosis (course)] HOIP_0002403 HOIP:HOIP_0002404 Keap1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the Keap1 to be lower. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. Keap1 inactivation [glutathione depletion (course)] HOIP_0002404 HOIP:HOIP_0002405 BIP-stress sensor complex is a subtype of molecular complex. This entity has sub-parts of molecules, BIP/GRP78 and other molecule which has role of stress sensor. BIP-stress sensor complex HOIP_0002405 HOIP:HOIP_0002406 A role played by the entity which regulates the process of cell death. cell death modulator role HOIP_0002406 HOIP:HOIP_0002407 Keap1 modification by electrophiles is a subtype of oxidation by electrophiles. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. Keap1 modification by electrophiles [glutathione depletion (course)] HOIP_0002407 HOIP:HOIP_0002409 Electrophiles formation is a subtype of biosynthetic process: A process that that generates electrophiles. Electrophile is a reagent that forms a bond to its reaction partner (the nucleophile) by accepting both bonding electrons from that reaction partner. This entity is a specific course-dependent process. This process can constitute the course of necrosis. A number of xenobiotics exert a toxic effect theough their metabolites. Electrophiles are molecules that contain an electron-deficient atom with a partial or full positive charge that can react by sharing electron pairs with electron rich atoms in nucleophiles. Electrophilic toxicants generally are detoxificated by conjugation of with the nucleophile, glutathione. This reaction can be facilitated by glutathione S-trasferases. electrophiles formation [necrosis (course)] HOIP_0002409 HOIP:HOIP_0002410 NCBI-Human-GeneID:7184 NCBI-Mouse-GeneID:22027 NCBI-Rat-GeneID:362862 HSP90B1 [ER stress] GRP94 (canonical)[ER stress] HOIP_0002410 NCBI-Human-GeneID:7184 http://www.ncbi.nlm.nih.gov/gene/7184 NCBI-Mouse-GeneID:22027 http://www.ncbi.nlm.nih.gov/gene/22027 NCBI-Rat-GeneID:362862 http://www.ncbi.nlm.nih.gov/gene/362862 HOIP:HOIP_0002411 NCBI-Human-GeneID:112476 NCBI-Mouse-GeneID:69017 NCBI-Rat-GeneID:361651 PKCΕ (canonical)[ER stress] HOIP_0002411 NCBI-Human-GeneID:112476 http://www.ncbi.nlm.nih.gov/gene/112476 NCBI-Mouse-GeneID:69017 http://www.ncbi.nlm.nih.gov/gene/69017 NCBI-Rat-GeneID:361651 http://www.ncbi.nlm.nih.gov/gene/361651 HOIP:HOIP_0002412 A process in which a signal to eIF2a is transduced by PERK. This process is dependent on the refolding and can constitute the course of ER stress. PERK signaling to eIF2a [ER stress - refolding] HOIP_0002412 HOIP:HOIP_0002413 An attribute related to the power or force. strength (attribute) HOIP_0002413 HOIP:HOIP_0002414 A physical attribute that inheres in a bearer by virtue of the proportion of the bearer's amount of matter. mass attribute HOIP_0002414 HOIP:HOIP_0002415 A 1-D extent attribute which is equal to the distance between two points. http://purl.obolibrary.org/obo/PATO_0000122 length attribute HOIP_0002415 HOIP:HOIP_0002416 A 3-D extent attribute related to amount of 3-dimensional space it occupies. volume attribute HOIP_0002416 HOIP:HOIP_0002417 A physical attribure of the thermal energy of a system. http://purl.obolibrary.org/obo/PATO_0000146 temperature attribute HOIP_0002417 HOIP:HOIP_0002418 A physical attribute relaeted to the amount of force per unit area the bearer exerts. pressure attribute HOIP_0002418 HOIP:HOIP_0002419 A physical attribute entity inhering in a bearer by virtue of the bearer's rate of change of momentum. http://purl.obolibrary.org/obo/PATO_0001035 force attribute HOIP_0002419 HOIP:HOIP_0002420 An attribute to the potential energy per unit charge associated with a static (time-invariant) electric field, also called the electrostatic potential. http://purl.obolibrary.org/obo/PATO_0001464 electric potential attribute HOIP_0002420 HOIP:HOIP_0002421 An attribute entity inhering in a cell's plasma membrane by virtue of the electrical potential difference across it. http://purl.obolibrary.org/obo/PATO_0001462 membrane potential attribute HOIP_0002421 HOIP:HOIP_0002422 A physical attribute inhering in a bearer by virtue the bearer's disposition to having an affinity for water; it is readily absorbing or dissolving in water. hydrophilicity attribute HOIP_0002422 HOIP:HOIP_0002423 A physical attribute inhering in a bearer by virtue the bearer's disposition to being water-repellent; tending to repel and not absorb water. hydrophobicity attribute HOIP_0002423 HOIP:HOIP_0002424 A time attribute inhering in a bearer by virtue of how long the bearer has existed. age attribute HOIP_0002424 HOIP:HOIP_0002425 An organismal attribute inhering in a bearer by virtue of the bearer's ability to undergo sexual reproduction in order to differentiate the individuals or types involved. http://purl.obolibrary.org/obo/PATO_0000047 biological sex (attribute) HOIP_0002425 HOIP:HOIP_0002426 An organismal value of an attribute inhering in a bearer by virtue of the bearer's ability to undergo sexual reproduction in order to differentiate the individuals or types involved. biological sex value HOIP_0002426 HOIP:HOIP_0002427 A biological sex value inhering in an individual or a population that only produces gametes that can be fertilised by male gametes. female value HOIP_0002427 HOIP:HOIP_0002428 A biological sex attribute inhering in an individual or a population whose sex organs contain only male gametes. male value HOIP_0002428 HOIP:HOIP_0002429 An attribute that inheres in a bearer in virtue of its realizing one of its functions. activity (attribute) activation (attribute) HOIP_0002429 HOIP:HOIP_0002430 Negative regulation of inflammatory response is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. negative regulation of inflammatory response [glutathione depletion (course)] HOIP_0002430 HOIP:HOIP_0002431 The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:20173742 autophagy dependent Keap1 catabolic process [glutathione depletion (course)] HOIP_0002431 PMID:20173742 Nrf2 target gene products, such as Gst-m1 and Gst-p1, were prominent proteins in autophagy-deficient liver. Surprisingly, Gst-m1 constituted 7.69 ± 1.25% of the cytosolic proteins in Atg7-deficient livers. HOIP:HOIP_0002432 The chemical reaction resulting in the breakdown of NRF2, which is mediated by the proteasome. proteasome-mediated ubiquitin-dependent NRF2 catabolic process HOIP_0002432 HOIP:HOIP_0002433 Gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by ATF4. gene expression by ATF4 HOIP_0002433 HOIP:HOIP_0002434 The chemical reaction resulting in the breakdown of NRF2, which is mediated by the proteasome. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. proteasome-mediated NRF2 degradation [glutathione depletion (course)] HOIP_0002434 HOIP:HOIP_0002435 Pancreatic beta cell damage is a subtype of cellular damage: A process that injuries the structure of the pancreatic beta cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of type 1 diabetes pancreatic beta cell damage [type 1 diabetes mellitus course] HOIP_0002435 HOIP:HOIP_0002436 Dysfunction of of insulin secretion is a subtype of dysfunctioning: A process that performs an abnormal and incomplete insulin secretion. dysfunction of insulin secretion HOIP_0002436 HOIP:HOIP_0002437 Dysfunction of insulin secretion is a subtype of dysfunctioning: A process that performs an abnormal and incomplete insulin secretion. This entity is a specific course-dependent process. This process can constitute the course of type 1 diabetes dysfunction of insulin secretion [type 1 diabetes mellitus course] HOIP_0002437 HOIP:HOIP_0002438 Changing concentration is a subtype of changing quality: A process that changes the concentration of the object. changing concentration HOIP_0002438 HOIP:HOIP_0002439 Decreasing blood glucose level in blood is a subtype of decreasing concentration: A process that changes the blood glucose concentration in the blood to be lower. decreasing blood glucose level in blood HOIP_0002439 HOIP:HOIP_0002440 A process in which a signal to eIF2a is transduced by PERK. This process is dependent on the apoptosis and can constitute the course of ER stress. PERK signaling to eIF2a [ER stress apoptosis] HOIP_0002440 HOIP:HOIP_0002441 Any process that stops, prevents, or reduces the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. negative regulation of proteasomal ubiquitin-dependent protein catabolic process HOIP_0002441 HOIP:HOIP_0002442 Any process that stops, prevents, or reduces the frequency, rate or extent of the breakdown of NRF2 by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. negative regulation of proteasomal ubiquitin-dependent NRF2 catabolic process HOIP_0002442 HOIP:HOIP_0002443 Overeating is a subtype of increasing quantity: A process that changes the ingestion amount of food to be larger. This entity is a specific course-dependent process. This process can constitute the course of Type II Diabetes mellitus. overeating [type 2 diabetes mellitus course] HOIP_0002443 HOIP:HOIP_0002444 Increasing insulin demand is a subtype of increasing functional demand: A process changes the demand for insulin to be higher. increasing insulin demand HOIP_0002444 HOIP:HOIP_0002445 The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation. autophagy dependent Keap1 catabolic process HOIP_0002445 HOIP:HOIP_0002446 Fatty acid homeostasis imbalance in peroxisome is a subtype of changing balance: A process that becomes lacking afatty acid homeostastasis balance. fatty acid homeostasis imbalance in peroxisome HOIP_0002446 HOIP:HOIP_0002447 Receiving abnormal protein signal by ATF6 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by ATF6. This process is dependent on the refolding and can constitute the course of ER stress. receiving abnormal protein signal by ATF6 [ER stress - refolding] HOIP_0002447 HOIP:HOIP_0002449 A process in which a signal to eIF2a is transduced by PERK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PERK signaling to eIF2a [ER stress] HOIP_0002449 HOIP:HOIP_0002452 The simplest member of the class of bromobenzenes, that is benzene in which a single hydrogen has been substituted by a bromine. A liquid at room temperature (m.p. -30degreeC; b.p.760 156degreeC), it is used as a solvent, particularly for large-scale crystallisations, and for the introduction of phenyl groups in organic synthesis. C6H5Br Brc1ccccc1 CAS:108-86-1 MetaCyc:BROMOBENZENE PMID:18078705 PMID:20621112 PMID:569914 Wikipedia:Bromobenzene bromobenzene [glutathione depletion (course)] HOIP_0002452 PMID:18078705 After 24h treatment with the hepatotoxins, there was evidence for the initiation of a late defence response. BB significantly increased both HO-1 and GCLC protein at this time point, CCl4 increased GCLC protein alone. PMID:569914 Synergistic effects of phorone on the hepatotoxicity of bromobenzene and paracetamol in mice. HOIP:HOIP_0002453 PMID:1784629 PMID:18078705 PMID:29039508 PMID:29549912 Gclc (mouse)[glutathione depletion (course)] HOIP_0002453 PMID:18078705 Significant GSH depletion was seen with APAP (9.6+/-1.7% of control levels) and BB (52.8+/-6.2% of control levels) 1h after administration, but not with FS and CCl4. Treatment with APAP for 1h caused a significant increase in the levels of haem oxygenase-1 (HO-1; 2.85-fold) and glutamate cysteine ligase (GCLC; 1.62-fold) mRNA. BB and FS did not affect the mRNA levels of either gene after 1h of treatment; however CCl4 significantly increased HO-1 mRNA at this time point. After 24h treatment with the hepatotoxins, there was evidence for the initiation of a late defence response. BB significantly increased both HO-1 and GCLC protein at this time point, CCl4 increased GCLC protein alone. HOIP:HOIP_0002454 Signaling molecule activation is a subtype of molecular activation: A process that changes the activity of the molecule with a signaling molecule role to be higher. signaling molecule activation HOIP_0002454 HOIP:HOIP_0002455 Excretion of glutathione conjugates from hepatocyte to bile tube is a subtype of compound excretion: A process that excretes the glutathione conjugates from the hepatocyte to to the bile tube. excretion of glutathione conjugates from hepatocyte to bile tube HOIP_0002455 HOIP:HOIP_0002456 Excretion of glutathione conjugates from hepatocyte to blood is a subtype of compound excretion: A process that excretes the glutathione conjugates from the hepatocyte to to blood. excretion of glutathione conjugates from hepatocyte to blood HOIP_0002456 HOIP:HOIP_0002457 glutathione export from hepatocyte to blood is a subtype of glutathione transport: A process that exports the glutathione from the hepatocyte to to the blood. glutathione export from hepatocyte to blood HOIP_0002457 HOIP:HOIP_0002458 Refolding-unfolding imbalance is a subtype of imbalance: A process that lacks a balance between protein refolding and unfolding. This entity is a specific course-dependent process. This process can constitute the course of ER stress (mild). refolding-unfolding imbalance [ER stress (mild) ] HOIP_0002458 HOIP:HOIP_0002459 Refolding-unfolding imbalance is a subtype of imbalance: A process that lacks a balance between protein refolding and unfolding. refolding-unfolding imbalance HOIP_0002459 HOIP:HOIP_0002460 Refolding-unfolding imbalance is a subtype of imbalance: A process that lacks a balance between protein refolding and unfolding. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of ER stress (moderate). refolding-unfolding imbalance [ER stress (moderate) ] HOIP_0002460 HOIP:HOIP_0002461 PERK-NRF2 signal integration system is a subtype of PERK pathway system. This entity has sub-parts and has a goal of transmitting signals and a gene regulation via PERK and NRF2 as a systemic context. PERK-NRF2 signal integration system HOIP_0002461 HOIP:HOIP_0002462 A physical attribute inhering in a bearer by virtue of the bearer's motion characteristic. flow rate attribute HOIP_0002462 HOIP:HOIP_0002463 A role of receiving a signal and transmitting it in the cell to initiate a change in cell activity. A signal is a physical entity or change in state that is used to transfer information in order to trigger a response. related molecular function GO:0004872 signaling receptor HOIP_0002463 HOIP:HOIP_0002464 Stress sensor activation, is a subtype of molecular activation: A process that changes the activity of the molecule with stress sensor role to be higher. stress sensor activation HOIP_0002464 HOIP:HOIP_0002465 Transport ATF-6 from the endoplasmic reticulum (ER) to the Golgi is a subtype of ER to Golgi transport: A process of the directed movement of ATF6 from the endoplasmic reticulum (ER) to the Golgi. Transport ATF-6 from the endoplasmic reticulum (ER) to the Golgi HOIP_0002465 HOIP:HOIP_0002466 Transport ATF-6 from the endoplasmic reticulum (ER) to the Golgi is a subtype of ER to Golgi transport: A process of the directed movement of ATF6 from the endoplasmic reticulum (ER) to the Golgi. This process is dependent on the refolding and can constitute the course of ER stress. PMID:11821395 PMID:12110171 PMID:15657421 Reactome:R-HSA-381186 http://purl.obolibrary.org/obo/HINO_0008859 The association between ATF6-alpha and BiP causes ATF6-alpha to be retained in the endoplasmic reticulum (ER). Once dissociated from BiP, the 2 Golgi Localization Sequences on ATF6-alpha are exposed and ATF6-alpha transits from the ER to the Golgi Apparatus. Transport ATF-6 from the endoplasmic reticulum (ER) to the Golgi [ER stress - refolding] HOIP_0002466 HOIP:HOIP_0002467 ATF6 processing is a subtype of protein processing: A process that ATF6 maturation process achieved by the cleavage of a peptide bond or bonds within ATF6 protein. This process is dependent on the refolding and can constitute the course of ER stress. ATF6 processing [ER stress - refolding] HOIP_0002467 HOIP:HOIP_0002468 ATF6F (canonical)[ER stress] HOIP_0002468 HOIP:HOIP_0002469 Increasing demand for protein refolding is a subtype of increasing functional demand: A process that changes the functional demand for protein refolding to be higher. This process persists for a certain period or over a long period. This entity is a specific course-dependent process. This process can constitute the course of ER stress (sustained). increasing demand for protein refolding [ER stress (sustained)] HOIP_0002469 HOIP:HOIP_0002470 Accumulation of abnormal proteins in ER is a subtype of accumulation of abnormal proteins: A process that keeps abnormal protein(s) in the ER (endoplasmic reticulum). And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of ER stress (moderate). accumulation of abnormal proteins in ER [ER stress (moderate) ] HOIP_0002470 HOIP:HOIP_0002471 Increasing demand for protein degradation is a subtype of increasing functional demand: A process that is subjected to increasing load of protein degradation. increasing demand for protein degradation HOIP_0002471 HOIP:HOIP_0002472 Increasing demand for abnormal protein degradation is a subtype of increasing demand of protein degradation: A process is subjected to increasing load of abnormal protein degradation. increasing demand for abnormal protein degradation HOIP_0002472 HOIP:HOIP_0002473 Increasing demand for abnormal protein degradation is a subtype of increasing demand of protein degradation: A process is subjected to increasing load of abnormal protein degradation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. increasing demand for abnormal protein degradation [ER stress] HOIP_0002473 HOIP:HOIP_0002474 Protein refolding insufficiency is a subtype of malfunctioning process: A process that lacks performing the function of protein refolding required. protein refolding insufficiency HOIP_0002474 HOIP:HOIP_0002475 Protein refolding insufficiency is a subtype of malfunctioning process: A process that lacks performing the function of protein refolding required. This process persists for a certain period or over a long period. This entity is a specific course-dependent process. This process can constitute the course of ER stress (sustained) . protein refolding insufficiency (sustained) [ER stress] HOIP_0002475 HOIP:HOIP_0002476 Protein degradation insufficiency is a subtype of malfunctioning process: A process that lacks performing the function of protein degradation required. protein degradation insufficiency HOIP_0002476 HOIP:HOIP_0002477 Protein degradation insufficiency is a subtype of malfunctioning process: A process that lacks performing the function of protein degradation required. This entity is a specific course-dependent process. This process can constitute the course of ER stress. protein degradation insufficiency [ER stress] HOIP_0002477 HOIP:HOIP_0002478 Abnormal protein production- degradation imbalance is a subtype of imbalance: A process that lacks a balance between abnormal protein production and degradation. abnormal protein production- degradation imbalance HOIP_0002478 HOIP:HOIP_0002479 Abnormal protein production- degradation imbalance is a subtype of imbalance: A process that lacks a balance between abnormal protein production and degradation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. abnormal protein production- degradation imbalance [ER stress] HOIP_0002479 HOIP:HOIP_0002480 glutathione export from hepatocyte to bile tube is a subtype of glutathione transport: A process that exports the glutathione from the hepatocyte to to the blood. glutathione export from hepatocyte to bile tube HOIP_0002480 HOIP:HOIP_0002482 A series of molecular signals mediated by Caspase family. http://purl.obolibrary.org/obo/IEV_0000128 caspase pathway HOIP_0002482 HOIP:HOIP_0002483 ATF4 gene regulation pathway is a subtype of gene regulation pathway: Sequence of reactions to regulate genes by ATF4. ATF4 gene regulation pathway HOIP_0002483 HOIP:HOIP_0002484 ATF4 gene regulation pathway is a subtype of gene regulation pathway: Sequence of reactions to regulate genes by ATF4. This pathway is dependent on the apoptosis and can constitute the course of ER stress. ATF4 gene regulation pathway [ER stress - apoptosis] HOIP_0002484 HOIP:HOIP_0002485 CHOP gene regulation pathway is a subtype of gene regulation pathway: Sequence of reactions to regulate genes by CHOP. CHOP gene regulation pathway HOIP_0002485 HOIP:HOIP_0002486 XBP1s gene regulation pathway is a subtype of gene regulation pathway: A series of process in which XBP1s regulates the gene expression. XBP1s gene regulation pathway HOIP_0002486 HOIP:HOIP_0002487 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB. A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB. IRE1-mediated unfolded protein response [ER stress] HOIP_0002487 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB. PMID:22013210 HOIP:HOIP_0002488 glutathione export from hepatocyte is a subtype of glutathione transport: A process that exports the glutathione from the hepatocyte. ISBN:0071769234 PMID:18786560 glutathione export from hepatocyte HOIP_0002488 ISBN:0071769234 GSH itself is often cotranported with other xenobiotics or xenobiotics metabolites, namely, by MRP2 into bile, and by MRP1,4,5 into blood. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition PMID:18786560 The Mrp proteins mediate not only GSH efflux, but they also export oxidized glutathione derivatives (e.g., glutathione disulfide (GSSG), S-nitrosoglutathione (GS-NO), and glutathione-metal complexes), as well as other glutathione S-conjugates. HOIP:HOIP_0002489 PI3K-AKT signaling is a subtype of integrated signaling pathway: Sequence of linked reactions, which has PI3 signaling and activation of the AKT gene. PI3K-AKT signaling HOIP_0002489 HOIP:HOIP_0002490 NRF2 signaling (integrated pathway) is a subtype of integrated signaling pathway: Sequence of linked reactions, which has NRF2 signaling and gene regulation pathway. nuclear factor erythroid 2 like 2 signaling pathway NRF2 signaling pathway HOIP_0002490 HOIP:HOIP_0002491 glutathione export from hepatocyte is a subtype of glutathione transport: A process that exports the glutathione from the hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. ISBN:0071769234 PMID:18786560 glutathione export from hepatocyte [glutathione depletion (course)] HOIP_0002491 ISBN:0071769234 ISBN:0071769234 ISBN:0071769234 ISBN:0071769234 GSH itself is often cotranported with other xenobiotics or xenobiotics metabolites, namely, by MRP2 into bile, and by MRP1,4,5 into blood. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition PMID:18786560 The Mrp proteins mediate not only GSH efflux, but they also export oxidized glutathione derivatives (e.g., glutathione disulfide (GSSG), S-nitrosoglutathione (GS-NO), and glutathione-metal complexes), as well as other glutathione S-conjugates. HOIP:HOIP_0002492 Dissociation of NF-kappaB -I-kappaB is a subtype of detaching: A process that disaggregates a NF-kappaB-I-kappaB to NF-kappaB dimers and I-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. GO:0008588 The release of NF-kappaB from specific molecules in the cytoplasm to which it was bound, thereby allowing its translocation into the nucleus. dissociation of NF-kappaB-I-kappaB HOIP_0002492 HOIP:HOIP_0002493 ABCC2 [glutathione depletion (course)] MRP2 (canonical)[glutathione depletion (course)] HOIP_0002493 HOIP:HOIP_0002494 NF-kappaB transport into nucleus is a subtype of nuclear transport: A process that of the directed movement of NF-kappaB from the cytoplasm to the nucleus. NF-kappaB transport into nucleus HOIP_0002494 HOIP:HOIP_0002495 The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. PMID:21772278 The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. PMID:21772278 GO:0007252 I-kappaB phosphorylation HOIP_0002495 The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. PMID:21772278 PMID:7594468 HOIP:HOIP_0002496 NCBI-Human-GeneID:1244 NCBI-Mouse-GeneID:12780 NCBI-Rat-GeneID:25303 ATP Binding Cassette Subfamily C Member 2 ATP-Binding Cassette, Sub-Family C (CFTR/MRP), Member 2 Canalicular Multispecific Organic Anion Transporter 1 MRP2 Multidrug Resistance-Associated Protein 2 ABCC2 (mol) HOIP_0002496 NCBI-Human-GeneID:1244 http://www.ncbi.nlm.nih.gov/gene/1244 NCBI-Mouse-GeneID:12780 http://www.ncbi.nlm.nih.gov/gene/12780 NCBI-Rat-GeneID:25303 http://www.ncbi.nlm.nih.gov/gene/25303 HOIP:HOIP_0002497 https://doi.org/10.1271/kagakutoseibutsu.50.484 ERO1 (canonical)[ER stress] HOIP_0002497 HOIP:HOIP_0002498 IGFBP1 gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature IGFBP1 product or products (proteins or RNA) by ATF4. This entity is a specific course-dependent process. This process can constitute the course of ER stress. IGFBP1 gene expression by ATF4 [ER stress] HOIP_0002498 HOIP:HOIP_0002499 Abnormal protein production is a subtype of protein production: A process that makes existent of an abnormal protein due to biosynthesis or secretion resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of ER stress. abnormal protein production [ER stress] HOIP_0002499 HOIP:HOIP_0002500 NCBI-Human-GeneID:4363 NCBI-Mouse-GeneID:17250 NCBI-Rat-GeneID:24565 ATP Binding Cassette Subfamily C Member 1 ATP-Binding Cassette, Sub-Family C (CFTR/MRP), Member 1 Leukotriene C(4) Transporter MRP1 Multidrug Resistance-Associated Protein 1 ABCC1 (mol) HOIP_0002500 NCBI-Human-GeneID:4363 http://www.ncbi.nlm.nih.gov/gene/4363 NCBI-Mouse-GeneID:17250 http://www.ncbi.nlm.nih.gov/gene/17250 NCBI-Rat-GeneID:24565 http://www.ncbi.nlm.nih.gov/gene/24565 HOIP:HOIP_0002501 NCBI-Human-GeneID:5465 NCBI-Mouse-GeneID:19013 NCBI-Rat-GeneID:25747 Peroxisome Proliferator-Activated Receptor Alpha [lipidosis] HOIP_0002501 NCBI-Human-GeneID:5465 http://www.ncbi.nlm.nih.gov/gene/5465 NCBI-Mouse-GeneID:19013 http://www.ncbi.nlm.nih.gov/gene/19013 NCBI-Rat-GeneID:25747 http://www.ncbi.nlm.nih.gov/gene/25747 HOIP:HOIP_0002502 Hyperfunction of protein unfolding is a subtype of hyperfunctioning: A process that performs an excesssive protein unfolding. This process persists for a certain period or over a long period. This entity is a specific course-dependent process. This process can constitute the course of ER stress (sustained) . hyperfunction of protein unfolding (sustained) [ER stress] HOIP_0002502 HOIP:HOIP_0002503 Accumulation of compound in ER is a subtype of accumulation of xenobiotics: A process that keeps compound in the ER (endoplasmic reticulum). This entity is a specific course-dependent process. This process can constitute the course of ER stress (severe) . accumulation of compound in ER [ER stress (severe) ] HOIP_0002503 HOIP:HOIP_0002504 Hyperfunction of repeated protein unfolding is a subtype of hyperfunctioning: A process that performs an excesssive protein unfolding. This entity is a specific course-dependent process. This process can constitute the course of ER stress. hyperfunction of repeated protein unfolding [ER stress] HOIP_0002504 HOIP:HOIP_0002505 Protein aggregation is a subtype of molecular assembly: The aggregation, arrangement and bonding together of molecules. This entity is a specific course-dependent process. This process can constitute the course of ER stress. accumulatiing protein aggregates Protein aggretates are often insoluble and tend to sequester Fe 2+ ions. Fe 2+ helps to produce ROS. protein aggregation [ER stress] HOIP_0002505 HOIP:HOIP_0002506 A process that changes the activity of the eIF2a by PERK. This process is dependent on the translation attenuation and can constitute the course of ER stress. changing activity of eIF2a by PERK [ER stress - translation attenuation] HOIP_0002506 HOIP:HOIP_0002507 Phosphorylation of eIF2-alpha by PERK is a subtype of eIF2a phosphorylation: A process that The process of introducing a phosphate group into eIF2a by PERK. This process is dependent on the translation attenuation and can constitute the course of ER stress. PMID:23334697 PMID:9930704 Reactome:R-HSA-381111 The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Phosphorylation of eIF2-alpha by PERK [ER stress - translation attenuation] HOIP_0002507 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Id:R-HSA-381111 HOIP:HOIP_0002508 Phosphorylation of eIF2-alpha by PERK is a subtype of eIF2a phosphorylation: A process that The process of introducing a phosphate group into eIF2a by PERK. This process is dependent on the refolding and can constitute the course of ER stress. PMID:23334697 PMID:9930704 Reactome:R-HSA-381111 The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Phosphorylation of eIF2-alpha by PERK [ER stress - refolding] HOIP_0002508 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Id:R-HSA-381111 HOIP:HOIP_0002509 Phosphorylation of eIF2-alpha by PERK is a subtype of eIF2a phosphorylation: A process that The process of introducing a phosphate group into eIF2a by PERK. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:23334697 PMID:9930704 Reactome:R-HSA-381111 The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Phosphorylation of eIF2-alpha by PERK [ER stress - apoptosis] HOIP_0002509 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Id:R-HSA-381111 HOIP:HOIP_0002510 Phosphorylation of eIF2-alpha by PERK is a subtype of eIF2a phosphorylation: A process that The process of introducing a phosphate group into eIF2a by PERK. This process is dependent on the inflammation and can constitute the course of ER stress. PMID:23334697 PMID:9930704 Reactome:R-HSA-381111 The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Phosphorylation of eIF2-alpha by PERK [ER stress - inflammation] HOIP_0002510 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Id:R-HSA-381111 HOIP:HOIP_0002511 Chaperone gene regulation pathway by ATF6 is a subtype of ATF6 gene regulation pathway: Sequence of reactions to regulate genes which have a chaperone role by ATF6. This process can constitute the course of ER stress. chaperone gene regulation pathway by ATF6 [ER stress] HOIP_0002511 HOIP:HOIP_0002512 MRP1 [glutathione depletion (course)] ABCC1(canonical)[glutathione depletion (course)] HOIP_0002512 HOIP:HOIP_0002513 PERK-eIF2a-ATF4 mediated pathway is a subtype of PERK-eIF2a signaling: Sequence of linked reactions, which has PERK-eIF2a signaling and gene regulation by ATF4. PERK-eIF2a-ATF4 mediated pathway HOIP_0002513 HOIP:HOIP_0002514 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. This process is dependent on the translation attenuation and can constitute the course of ER stress. PERK activation [ER stress - translation attenuation] HOIP_0002514 HOIP:HOIP_0002515 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. This process persists for a certain period or over a long period. This process is dependent on the apoptosis (sutained) and can constitute the course of ER stress. PERK activation [ER stress - apoptosis (sutained ) ] HOIP_0002515 HOIP:HOIP_0002516 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. This process is dependent on the refolding and can constitute the course of ER stress. PERK activation [ER stress - refolding] HOIP_0002516 HOIP:HOIP_0002517 A process that changes the activity of the eIF2a by PERK. This process is dependent on the apoptosis and can constitute the course of ER stress. changing activity of eIF2a by PERK [ER stress - apoptosis] HOIP_0002517 HOIP:HOIP_0002518 A process that changes the activity of the eIF2a by PERK. This process is dependent on the refolding and can constitute the course of ER stress. changing activity of eIF2a by PERK [ER stress - refolding] HOIP_0002518 HOIP:HOIP_0002519 PERK-eIF2a-ATF4-CHOP pathway is a subtype of PERK-eIF2a-ATF4 signaling: Sequence of linked reactions, which has PERK-eIF2a-ATF4 signaling and gene regulation by CHOP. This pathway is dependent on the apoptosis and can constitute the course of ER stress. PERK-ATF4-CHOP signaling [ER stress - apoptosis] HOIP_0002519 HOIP:HOIP_0002520 ATF6 gene regulation pathway is a subtype of gene regulation pathway: Sequence of reactions to regulate genes by ATF6. Reactome ID: 381183 https://www.wikipathways.org/index.php/Pathway:WP2655 ATF6 gene regulation pathway HOIP_0002520 HOIP:HOIP_0002521 The process in which a gene's sequence is converted into a mature gene product or products (proteins or RNA) by ATF6. is a subtype of Gene expression by transcriptional regulator: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by ATF6. gene expression by ATF6 The process in which a gene's sequence is converted into a mature gene product or products (proteins or RNA) by ATF6. HOIP_0002521 HOIP:HOIP_0002522 CAD accumulation in lysosome is a subtype of compound accumulation in lysosome: A process that keeps CAD (Cationic Amphiphilic Drugs) in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). CAD accumulation in lysosome [phospholipidosis (latent)] HOIP_0002522 HOIP:HOIP_0002526 NRF2 gene expression regulation system is a subtype of pathway system. This entity has sub-parts and has a goal of regulating gene expressions by NRF2 as a systemic context. NRf2 gene expression regulation system HOIP_0002526 HOIP:HOIP_0002527 NCBI-Human-GeneID:4780 NCBI-Mouse-GeneID:18024 NCBI-Rat-GeneID:83619 NRF2 (mol) HOIP_0002527 NCBI-Human-GeneID:4780 http://www.ncbi.nlm.nih.gov/gene/4780 NCBI-Mouse-GeneID:18024 http://www.ncbi.nlm.nih.gov/gene/18024 NCBI-Rat-GeneID:83619 http://www.ncbi.nlm.nih.gov/gene/83619 HOIP:HOIP_0002528 The totality of all processes through which endoplasmic reticulum (ER) stress is realized. 細胞、パスウェイレベルを導入。 今後、Reactome等外部とマッピング予定。 課題 ・どのレベルでマッピングするか ー再帰的なパスウェイの扱い ー外部パスウェイ間でパスウェイの領域、参加分子が異なる。 The ER stress is a cellular response that occurs after sustained pertubation of ER protein synthesis, folding, and export machinery. Tis is likely to be induced by oxidative or covalent modification of ER proteins, which leads to misfolding of proteins. The ER stress is a cellular response that occurs after sustained pertubation of ER protein synthesis, folding, and export machinery. Tis is likely to be induced by oxidative or covalent modification of ER proteins, which leads to misfolding of proteins. MeSH:D059865 PMID:17765679 PMID:22883813 PMID:23022383 PMID:23334697 PMID:26977301 ER stress (course) endoplasmic reticulum stress (course) HOIP_0002528 The ER stress is a cellular response that occurs after sustained pertubation of ER protein synthesis, folding, and export machinery. Tis is likely to be induced by oxidative or covalent modification of ER proteins, which leads to misfolding of proteins. Drug-Induced Liver Disease 3rd Edition Editors: Neil Kaplowitz Laurie DeLeve Academic Press 2013 HOIP:HOIP_0002529 Aggregated protein production- degradation imbalance is a subtype of imbalance: A process that lacks a balance between aggregated protein production and degradation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. aggregated protein production- degradation imbalance [ER stress] HOIP_0002529 HOIP:HOIP_0002530 Aggregated protein production- degradation imbalance is a subtype of imbalance: A process that lacks a balance between aggregated protein production and degradation. aggregated protein production- degradation imbalance HOIP_0002530 HOIP:HOIP_0002531 Increasing number of abnormal cells in liver is a subtype of cell proliferation: A process that becomes larger in the number of autodigestion of abnormal cells in the liver. increasing number of abnormal cells in liver HOIP_0002531 HOIP:HOIP_0002532 Increasing number of abnormal cells in liver is a subtype of cell proliferation: A process that becomes larger in the number of autodigestion of abnormal cells in the liver. This entity is a specific course-dependent process. This process can constitute the course of ER stress. increasing number of abnormal cells in liver [ER stress] HOIP_0002532 HOIP:HOIP_0002533 Hyperfunction of cell survival is a subtype of hyperfunctioning: A process that performs an excesssive cell survival. This entity is a specific course-dependent process. This process can constitute the course of ER stress. hyperfunction of cell survival[ER stress] HOIP_0002533 HOIP:HOIP_0002534 A pathologic process that involves the transformation of normal cells to a neoplastic state. This entity is a specific course-dependent process. This process can constitute the course of ER stress. carcinogenesis [ER stress] HOIP_0002534 HOIP:HOIP_0002535 Tumor cell proliferation is a subtype of cell proliferation: A process of the multiplication or reproduction of tumor cells, resulting in the rapid expansion of a tumor cell population. This entity is a specific course-dependent process. This process can constitute the course of ER stress. tumor cell proliferation [ER stress] HOIP_0002535 HOIP:HOIP_0002536 Increasing hepatocellular volume is a changing process to change the volume of the hepatocyte to increase. This entity is a specific course-dependent process. This process can constitute the course of ER stress. increasing hepatocellular volume [ER stress] HOIP_0002536 HOIP:HOIP_0002537 Negative regulation of increasing insulin resistance is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of insulin resistance. negative regulation of increasing insulin resistance HOIP_0002537 HOIP:HOIP_0002539 Protein quality control for misfolded or incompletely synthesized proteins is a subtype of keeping quality: A process that maintains the protein quality in an early stage of course. This entity is a specific course-dependent process. This process can constitute the course of ER stress (early stage). protein quality control for unfolded proteins [ER stress (early stage)] HOIP_0002539 HOIP:HOIP_0002540 BIP- chaperone [ER stress - refolding [early stage] HEL-S-89n- chaperone [ER stress - refolding [early stage] HSPA5- chaperone [ER stress - refolding [early stage] Heat Shock Protein Family A (Hsp70) Member 5- chaperone [ER stress - refolding [early stage] MIF2- chaperone [ER stress - refolding [early stage] GRP78 - chaperone (canonical)[ER stress - refolding [early stage] HOIP_0002540 HOIP:HOIP_0002541 Optional contribution processis a subtype of meta-functioning and it represents optional contribution to functioning. The “optional” means that the effect of fa is not mandatory to ft, that is, ft can be performed without the effect of fa. optional contribution process HOIP_0002541 HOIP:HOIP_0002542 Enhancing is a type of functioning process of meta-function. Both enhancing and improveing represents optional contribution to other function. The “optional” means that the effect of fa is not mandatory to ft, that is, the target function can be performed without improving or enhancing. The discrimination between improving and enhancing is made by whether augmentation of the output can be made without increase of the amount of the input energy or not. For example, the “to make low pressure” of the condenser contributes to the efficiency of the “to generate torque” function without increment of input energy, so its functioning is “Improving”. On the other hand, the “to super-heat” function of the boiler optionally increases the amount of the input energy to make a contribution. Its meta-function is “Enhancing” . enhancing HOIP_0002542 HOIP:HOIP_0002543 A chromosome that encodes the nuclear genome and is found in the nucleus of a eukaryotic cell during the cell cycle phases when the nucleus is intact. nuclear chromosome HOIP_0002543 HOIP:HOIP_0002544 Protein quality control for misfolded or incompletely synthesized proteins is a subtype of keeping quality: A process that maintains the protein quality. This entity is a specific course-dependent process. This process can constitute the course of ER stress. protein quality control for unfolded proteins [ER stress] HOIP_0002544 HOIP:HOIP_0002545 Regulation of lipolytic gene expression is a subtype of regulation of gene expression: A process that modulates the frequency, rate or extent of lipid degradation related gene expression. regulation of lipolytic gene expression HOIP_0002545 HOIP:HOIP_0002546 Refolding promoting gene expression by ATF6 is a subtype of gene expression: The process in which a gene sequence is converted into a mature refolding inducing gene product or products (proteins or RNA) by ATF6 . This entity is a specific course-dependent process. This process can constitute the course of ER stress. refolding promoting gene expression by ATF6 [ER stress] HOIP_0002546 HOIP:HOIP_0002547 Negative regulation of increasing insulin resistance is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of insulin resistance. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:27325692 negative regulation of increasing insulin resistance [ER stress] HOIP_0002547 PMID:27325692 XBP1s Is an Anti-lipogenic Protein: XBP1s reduces hepatic lipogenic gene expression and improves hepatosteatosis in mouse models of obesity and insulin resistance, which leads us to conclude that XBP1s has anti-lipogenic properties in the liver. HOIP:HOIP_0002548 ATF6 signaling (integrated pathway) is a subtype of integrated signaling pathway: Sequence of linked reactions, which has ATF6 signaling and gene regulation pathway. ATF6 signaling (integrated pathway) HOIP_0002548 HOIP:HOIP_0002549 ATF6 mediated chaperon gene regulation pathway is a subtype of ATF6 signaling (integrated pathway): Sequence of linked reactions, which has ATF6 signaling and gene regulation pathway. This process is dependent on the refolding and can constitute the course of ER stress. ATF6 mediated chaperon gene producion pathway [ER stress -refolding] HOIP_0002549 HOIP:HOIP_0002550 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. This process is dependent on the refolding and can constitute the course of ER stress. ATF6 signaling [ER stress - refolding] HOIP_0002550 HOIP:HOIP_0002551 Excretion of glutathione conjugates from hepatocyte is a subtype of compound excretion: A process that excretes the glutathione conjugates from the hepatocyte. excretion of glutathione conjugates from hepatocyte HOIP_0002551 HOIP:HOIP_0002552 Blood coagulation factor synthesis is a subtype of biosynthetic process: The chemical reactions resulting in the formation of substances with blood coagulation factor role. blood coagulation factor synthesis HOIP_0002552 HOIP:HOIP_0002554 Receiving signal in ATF6 signal transduction pathway is a subtype of receiving signal: A process that recognizes another object and changes into a signal in a ATF6 signal transduction pathway. receiving signal by ATF6 HOIP_0002554 ISBN 978-4-7581-0131-8 HOIP:HOIP_0002555 This gene encodes a eukaryotic translation initiation factor that catalyzes the formation of puromycin-sensitive 80 S preinitiation complexes and the poly(U)-directed synthesis of polyphenylalanine at low concentrations of Mg2+. This gene should not be confused with eIF2-alpha (EIF2S1, Gene ID: 1965), the alpha subunit of the eIF2 translation initiation complex. Although both of these proteins function in binding initiator tRNA to the 40 S ribosomal subunit, the encoded protein does so in a codon-dependent manner, whereas eIF2 complex requires GTP. Alternative splicing of this gene results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jan 2016] http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=Retrieve&dopt=full_report&list_uids=83939 phosphorylated eIF2A P-EIF2A - translation initiation inhibitor (canonical)[ER stress - translation attenuation] HOIP_0002555 HOIP:HOIP_0002556 http://www.ncbi.nlm.nih.gov/gene/83939 phosphorylated eIF2A -ATF4 promoting factor [ER stress - proteinrefolding] P-EIF2A -ATF4 promoting factor (canonical)[ER stress - proteinrefolding] HOIP_0002556 HOIP:HOIP_0002557 A role played by the entity which modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. translation regulator role HOIP_0002557 HOIP:HOIP_0002558 ATF4 - transcriptional regulator (canonical)[ER stress - apotosis] HOIP_0002558 HOIP:HOIP_0002559 ATF4 - transcriptional regulator (canonical)[ER stress - inflammation] HOIP_0002559 HOIP:HOIP_0002560 仮　要調査 ATF4 - transcriptional regulator (canonical)[ER stress - insulin resistance] HOIP_0002560 HOIP:HOIP_0002561 PERK-eIF2a-ATF4 mediated pathway is a subtype of PERK-eIF2a signaling: Sequence of linked reactions, which has PERK-eIF2a signaling and TRIB3 gene regulation by ATF4. This pathway is dependent on the insulin resistance and can constitute the course of ER stress. PERK-ATF4-TRIB3 signaling [ER stress - insulin resistance] HOIP_0002561 HOIP:HOIP_0002562 Trib3 gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence of Trib3 is converted into a mature gene product or products (proteins or RNA) related to the refolding by ATF4. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Trib3 gene expression by ATF4 [ER stress] HOIP_0002562 HOIP:HOIP_0002563 IRE1 signaling (integrated pathway) is a subtype of integrated signaling pathway: Sequence of linked reactions, which has IRE1 signaling and gene regulation pathway. IRE1 signaling (integrated pathway) HOIP_0002563 HOIP:HOIP_0002564 Excretion of glutathione conjugates from hepatocyte is a subtype of compound excretion: A process that excretes the glutathione conjugates from the hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. excretion of glutathione conjugates from hepatocyte [Glutathione depletion.] HOIP_0002564 HOIP:HOIP_0002565 Changing protein fold is a subtype of changing protein structure: A process that changes the folding stucture of the protein. changing protein fold HOIP_0002565 HOIP:HOIP_0002566 Changing structure is a subtype of changing an operand: A process that change sthe stucture of the operand. changing structure HOIP_0002566 HOIP:HOIP_0002567 Converting to information is a subtype of converting type: A process that changes a type of object to information. converting to information HOIP_0002567 HOIP:HOIP_0002568 Changing composition is a subtype of changing between operands: A process that changes the relationship of the overall components. changing composition HOIP_0002568 HOIP:HOIP_0002569 Combining is a subtype of assembling: A process that merges different parts into one. Each element can be recognized after combination. combining HOIP_0002569 HOIP:HOIP_0002570 Dissolving is a subtype of assembling: A process that creates a solvent-solute relationship between components. 溶質ー溶媒関係に着目した合成 出力混合物は溶媒−溶質関係となり、均一な状態となる dissolving HOIP_0002570 HOIP:HOIP_0002571 IRE1 signaling is a process that a signal is transmitted by the IRE1 (Inositol-requiring transmembrane kinase/endonuclease). IRE1 generally plays a endoplasmic reticulum membrane stress sensor role. This entity is a specific course-dependent process. This process can constitute the course of ER stress. IRE1 signaling [ER stress] HOIP_0002571 HOIP:HOIP_0002572 CAD insertion into phospholipase binding site to lysosomal inner membrane is a subtype of binding: A process that CAD inserts and replaces the phospholipase binding site in the lysosomal inner membrane. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). PMID:22960355 CAD insertion into phospholipase binding site to lysosomal inner membrane [phospholipidosis (latent course)] HOIP_0002572 PMID:22960355 Under normal conditions, lysosomal phospholipase A2 is bound through electrostatic charge interactions to the inner membranes of the lysosome. A cationic amphiphile, accumulates in the lysosome and inserts into the inner membrane decreasing or eliminating the anionic binding sites for the lipase. The lipase is no longer able to bind to its substrates and is potentially susceptible to degradation by lysosomal proteases. HOIP:HOIP_0002573 Mixing is a subtype of assembling: A process that combines two or more substances to a single element, and they cannot be distinguished. 出力混合物は共存関係となるが識別できず mixing HOIP_0002573 HOIP:HOIP_0002574 Composing is a subtype of assembling: A process that makes the different constituents into a connected whole. 異なる部分構成成分を組み合わせて１つのものをつくる。一体化する composing HOIP_0002574 HOIP:HOIP_0002575 Gathering is a subtype of assembling: A process that groups components of the same type. gathering HOIP_0002575 HOIP:HOIP_0002576 Splitting is a subtype of separating: A process that divides the whole object into the same kinds of parts. A + A+ A splitting is a dividing process to divide the whole operand into the same kinds of parts (operands) splitting HOIP_0002576 HOIP:HOIP_0002577 Taking is a subtype of separating: A process that separates and chooses an object . ある要素に注目して取るプロセス taking HOIP_0002577 HOIP:HOIP_0002578 Extracting is a subtype of taking: A process that obtains a necessary component from the whole object 異種成分の１つに注目して取り出すこと extracting HOIP_0002578 HOIP:HOIP_0002580 Decreasing distance is a subtype of changing distance: A process that brings object A close to object B. decreasing distance HOIP_0002580 HOIP:HOIP_0002581 Making contact between A and B is a subtype of decreasing distance: A process that brings object A close to object B to set the distance to 0. making contact between A and B HOIP_0002581 HOIP:HOIP_0002582 Glutathione conjugation (supply) - function demand imbalance (severe) is a subtype of imbalance: A process that becomes lacking a homeostastasis balance between glutathione conjugation supply and demand. The degree is severe This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. Glutathione conjugation (supply) - function demand imbalance (severe) [glutathione depletion (course)] HOIP_0002582 HOIP:HOIP_0002583 Keeping distance is a subtype of changing distance: A process that maintains the relative positional relationship between objects. keeping distance HOIP_0002583 HOIP:HOIP_0002584 Keeping adhesivity is a subtype of keeping distance: A process that maintains the relative positional relationship between objects with no distance. keeping adhesivity HOIP_0002584 HOIP:HOIP_0002585 Keeping distance (d>0) is a subtype of keeping distance: A process that maintains the relative positional relationship between objects with a certain distance (>0) . keeping distance (>0) HOIP_0002585 HOIP:HOIP_0002586 Changing the relationship between inside and outside is a subtype of changing position: A process that that changes the relative position between an inside object and an outside object. changing the relationship between inside and outside HOIP_0002586 HOIP:HOIP_0002587 Moving A to the inside of B is a subtype of changing the relationship between inside and outside: A process that that places an object from the outside to the inside of the boundary. moving A to the inside of B HOIP_0002587 HOIP:HOIP_0002588 Moving A to the outside of B is a subtype of changing the relationship between inside and outside: A process that that places an object from the inside to the outside of the boundary. 境界内側の対象物を外側に出す． 包含関係：AがBの内側．媒体A自身が対象物AとなりBの外側に． 必要か不要かは無関係． 例）水を出す 　対象物：水 　部分プロセス 　　水をためる（装置：タンク）→水を動かす（装置：パイプ） moving A to the outside of B HOIP_0002588 HOIP:HOIP_0002589 Discharging unnecessary object is a subtype of giving: A process that sends out an unnecessary object to an other medium. discharging unnecessary object HOIP_0002589 HOIP:HOIP_0002590 Changing material is a subtype of changing relationship between operands: A process that replaces the old material into new material. changing material HOIP_0002590 HOIP:HOIP_0002591 IRE1 activation is a subtype of molecular activation: A process that changes the activity of the IRE1 to be higher. This entity is a specific course-dependent process. This process can constitute the course of IRE1 pathway. IRE1 activation [IRE1 pathway] HOIP_0002591 HOIP:HOIP_0002592 XBP1 activation by IRE1 is a subtype of activation of transcription factor: A process that changes the activity of XBP1 (X-Box Binding Protein 1) to be higher by IRE1. This entity is a specific course-dependent process. This process can constitute the course of IRE1 pathway. Reactome:R-HSA-1791121.3 The XBP1 gene is transcribed to yield mRNA, which is spliced and translated to transcription factor Xbp(s). XBP1 activation by IRE1 [IRE1 pathway] HOIP_0002592 Reactome:R-HSA-1791121.3 http://www.reactome.org/PathwayBrowser/#/R-HSA-381183&SEL=R-HSA-1791121&PATH=R-HSA-392499,R-HSA-381119,R-HSA-381033 HOIP:HOIP_0002593 IRE1 signaling is a process that a signal is transmitted by the IRE1 (Inositol-requiring transmembrane kinase/endonuclease). IRE1 generally plays a endoplasmic reticulum membrane stress sensor role. This entity is a specific course-dependent process. This process can constitute the course of IRE1 pathway. IRE1 signaling [IRE1 pathway] HOIP_0002593 HOIP:HOIP_0002594 A process in which a signal to TRAF2 is transduced by the IRE1. This process is dependent on the inflammation and can constitute the course of ER stress. IRE1 signaling to TRAF2 [ER stress - inflammation] HOIP_0002594 HOIP:HOIP_0002595 IRE1 dimerization is a subtype of protein dimerization: The formation of a IRE1 dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. IRE1 dimerization HOIP_0002595 HOIP:HOIP_0002596 IRE1 dimerization is a subtype of protein dimerization: The formation of a IRE1 dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:11897784 PMID:16365312 PMID:23236464 Reactome:R-HSA-381109 IRE1 dimerization [ER stress] HOIP_0002596 HOIP:HOIP_0002597 IRE1 autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by IRE1 of one or more of its own amino acid residues (cis-autophosphorylation), or residues on IRE1 (trans-autophosphorylation). IRE1 autophosphorylation HOIP_0002597 HOIP:HOIP_0002598 IRE1 autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by IRE1 of one or more of its own amino acid residues (cis-autophosphorylation), or residues on IRE1 (trans-autophosphorylation). This entity is a specific course-dependent process. This process can constitute the course of ER stress. IRE1 autophosphorylation [ER stress] HOIP_0002598 HOIP:HOIP_0002599 IRE1-Traf2-ASK-JNK-AP1 pathway is a subtype of IRE1 signaling (integrated pathway): Sequence of linked reactions, which has IRE1-Traf2-ASK-JNK signaling and gene regulation by AP1. This pathway is dependent on the inflammation and can constitute the course of ER stress. IRE1-TRAF2-ASK1 complex A protein complex of the endoplasmic reticulum membrane that consists of IRE1 (Inositol-requiring enzyme-1), TRAF2 (TNF receptor-associated factor 2) and ASK1 (Apoptosis signal-regulating kinase 1, a MAP3K). http://purl.obolibrary.org/obo/GO_1990604 PMID:27346803 IRE1-Traf2-ASK-JNK-AP1 pathway [ER stress - inflammation] HOIP_0002599 PMID:27346803 The IRE1α–TRAF2 complex can, in addition to the activation of NF-κB, recruit ASK1( also known as MAP3K5) and can activate JNK, leading to the increased expression of pro-inflammatory genes through enhanced AP1 activity HOIP:HOIP_0002601 NCBI-Human-GeneID:2081 NCBI-Mouse-GeneID:78943 NCBI-Rat-GeneID:498013 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 (canonical)[ER stress] HOIP_0002601 NCBI-Human-GeneID:2081 http://www.ncbi.nlm.nih.gov/gene/2081 NCBI-Mouse-GeneID:78943 http://www.ncbi.nlm.nih.gov/gene/78943 NCBI-Rat-GeneID:498013 http://www.ncbi.nlm.nih.gov/gene/498013 HOIP:HOIP_0002602 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 - signal sensor (canonical)[IRE1 signalling system] HOIP_0002602 HOIP:HOIP_0002603 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 - signaling factor (canonical)[IRE1 signalling system] HOIP_0002603 HOIP:HOIP_0002604 Receiving signal in IRE1 signal transduction pathway is a subtype of receiving signal: A process that recognizes another object and changes into a signal in a IRE1 signal transduction pathway. receiving signal in IRE1 signal transduction pathway HOIP_0002604 HOIP:HOIP_0002605 XBP1 - transcriptional regulator (canonical)[ER stress -ERAD] HOIP_0002605 HOIP:HOIP_0002606 Gene expression by XBP1 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by XBP1. gene expression by XBP1 HOIP_0002606 HOIP:HOIP_0002607 Gene expression by XBP1 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by XBP1. This entity is a specific course-dependent process. This process can constitute the course of ER stress. gene expression by XBP1 [ER stress] HOIP_0002607 HOIP:HOIP_0002608 ERAD gene expression by XBP1 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA)related to the ER associated degradation (ERAD) by XBP1. This entity is a specific course-dependent process. This process can constitute the course of ER stress. ERAD gene expression by XBP1 [ER stress] HOIP_0002608 HOIP:HOIP_0002609 IRE1-XBP1 mediated pathway is a subtype of IRE1 signaling (integrated pathway): Sequence of linked reactions, which has IRE1 signaling and gene regulation by XBP1. This process is dependent on refolding and can constitute the course of ER stress. IRE1-XBP1 mediated pathway [ER stress - refolding] HOIP_0002609 HOIP:HOIP_0002610 IRE1-XBP1 mediated pathway is a subtype of IRE1 signaling (integrated pathway): Sequence of linked reactions, which has IRE1 signaling and gene regulation by XBP1. This process is dependent on ERAD and can constitute the course of ER stress. IRE1-XBP1 mediated pathway [ER stress - ERAD] HOIP_0002610 HOIP:HOIP_0002611 Hyou gene expression by XBP1 is a subtype of gene expression by transcriptional factor: The process in which a Hyou gene sequence is converted into a mature gene product or products (proteins or RNA) by XBP1. This process is dependent on the refolding and can constitute the course of ER stress. Hyou gene expression by XBP1 [ER stress - refolding] HOIP_0002611 HOIP:HOIP_0002612 DNAJB9 gene expression by XBP1 is a subtype of gene expression by transcriptional factor: The process in which a DNAJB9 gene sequence is converted into a mature gene product or products (proteins or RNA) by XBP1. This process is dependent on the refolding and can constitute the course of ER stress. DNAJB9 gene expression by XBP1 [ER stress - refolding] HOIP_0002612 HOIP:HOIP_0002613 Hyperfunctio of glutathione conjugates excretion from hepatocyte is a subtype of compound excretion: A process that excretes the glutathione conjugates from the hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of glutathione conjugates excretion from hepatocyte [glutathione depletion (course)] HOIP_0002613 HOIP:HOIP_0002617 Enabling translation is a subtype of enabling: A process that sets conditions for translation to work correctly. enabling translation HOIP_0002617 HOIP:HOIP_0002618 Antioxidant gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature antioxidant gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of ER stress. antioxidant gene expression [ER stress] HOIP_0002618 HOIP:HOIP_0002619 BIP HEL-S-89n HSPA5 Heat Shock Protein Family A (Hsp70) Member 5 MIF2 GRP78 - stress sensor inhibitor (canonical)[ER stress - proteinrefolding [short-term]] HOIP_0002619 HOIP:HOIP_0002620 A role played by the entity that inhibits or desensitizes the stress sensor. By dissociating this inhibitor from the sensor, it can be received the stress and converted into a molecular signal. negative regulator role of stress sensor HOIP_0002620 HOIP:HOIP_0002621 BIP- stress sensor inhibitor [ER stress - proteinrefolding [persist] -IRE1 pathway] HSPA5- stress sensor inhibitor [ER stress - proteinrefolding [persist] -IRE1 pathway] Heat Shock Protein Family A (Hsp70) Member 5 - stress sensor inhibitor [ER stress - proteinrefolding [persist] -IRE1 pathway] GRP78 - stress sensor inhibitor (canonical)[ER stress - proteinrefolding [persist] -IRE1 pathway] HOIP_0002621 HOIP:HOIP_0002622 BIP- stress sensor inhibitor[ER stress - proteinrefolding [persist] -ATF6 pathway] HEL-S-89n- stress sensor inhibitor [ER stress - proteinrefolding [persist] -ATF6 pathway] HSPA5- stress sensor inhibitor [ER stress - proteinrefolding [persist] -ATF6 pathway] Heat Shock Protein Family A (Hsp70) Member 5- stress sensor inhibitor [ER stress - proteinrefolding [persist] -ATF6 pathway] MIF2- stress sensor inhibitor[ER stress - proteinrefolding [persist] -ATF6 pathway] GRP78 - stress sensor inhibitor (canonical)[ER stress - proteinrefolding [persist] -ATF6 pathway] HOIP_0002622 HOIP:HOIP_0002623 nucleoside phosphate HOIP_0002623 HOIP:HOIP_0002624 PERK-eIF2a-ATF4 mediated pathway is a subtype of PERK-eIF2a signaling: Sequence of linked reactions, which has PERK-eIF2a signaling and gene regulation by ATF4. This pathway is dependent on the inflammation and can constitute the course of ER stress. PERK-eIF2a-ATF4 pathway [ER stress - inflammation] HOIP_0002624 HOIP:HOIP_0002625 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signal sensor (canonical)[ER stress - translation attenuation] HOIP_0002625 HOIP:HOIP_0002628 A role played by the entity which enables the transmembrane transfer of an ion by a channel that opens when a specific intracellular ligand has been bound by the channel complex or one of its constituent parts. IMR:0000746 (obsolete) related molecular function GO:0005217 intracellular ligand-gated ion channel HOIP_0002628 HOIP:HOIP_0002629 Autophagy regulator is a role played by any compound that regulates the process of autophagy (the self-digestion of one or more components of a cell through the action of enzymes originating within the same cell). autophagy regulator role HOIP_0002629 HOIP:HOIP_0002633 NF-kappaB transport into nucleus is a subtype of nuclear transport: A process that of the directed movement of NF-kappaB from the cytoplasm to the nucleus. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Translocation of NF-kappaB [ER stress] HOIP_0002633 HOIP:HOIP_0002648 Decreasing cross-sectional area is a subtype of decreasing area: A process that changes the cross-sectional area of the object to be smaller. decreasing cross-sectional area HOIP_0002648 HOIP:HOIP_0002653 Bile transport (import-export) imbalance is a subtype of imbalance: A process that lacks a balance between bile import and export. bile transport (import-export) imbalance HOIP_0002653 HOIP:HOIP_0002655 Biliary tract stenosis is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the biliary tract to be smaller. biliary tract stenosis HOIP_0002655 HOIP:HOIP_0002656 Changing topology is a subtype of changing structure: A process that changes the setting of the subsets of a topological space. changing topology HOIP_0002656 HOIP:HOIP_0002661 Protein aggregation is a subtype of molecular assembly: The aggregation, arrangement and bonding together of molecules. http://jglobal.jst.go.jp/en/detail?JGLOBAL_ID=200906073816740790 http://purl.jp/bio/4/id/200906073816740790 protein aggregation HOIP_0002661 HOIP:HOIP_0002665 Regulation of cell survival is a subtype of controlling: A process that modulates the frequency, rate or extent of cell survival. regulation of cell survival HOIP_0002665 HOIP:HOIP_0002667 Negative regulation of contractile movement of bile canaliculus is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of contractile movement of bile canaliculus. This entity is a specific course-dependent process. This process can constitute the course of Cholestasis. negative regulation of contractile movement of bile canaliculus [Cholestasis] HOIP_0002667 HOIP:HOIP_0002671 The totality of all processes through which a given type 1 diabetes instance is realized. type 1 diabetes mellitus course HOIP_0002671 HOIP:HOIP_0002672 Decreasing flow is a subtype of decreasing quantity: A process that changes the amount of flow to be lower. Decreasing flow is a deacreasing process to decrease the magnitude of the flow. decreasing flow HOIP_0002672 HOIP:HOIP_0002673 Decreasing bile flow is a subtype of decreasing flow: A process that changes the amount of bile flow to be lower. decreasing bile flow HOIP_0002673 HOIP:HOIP_0002677 PMID:12110171 PMID:18653895 PMID:8020977 BIP HEL-S-89n HSPA5 Heat Shock Protein Family A (Hsp70) Member 5 MIF2 GRP78 - chaperone (canonical)[ER stress - proteinrefolding (sustained)] HOIP_0002677 PMID:12110171 ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3: 99-111, 2002. ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor that activates the transcription of ER molecular chaperones. Upon ER stress, ATF6 translocates from the ER to the Golgi where it is processed to its active form. ER chaperone BiP/GRP78 binds ATF6 and dissociates in response to ER stress. BiP retains ATF6 in the ER by inhibiting its GLSs and that dissociation of BiP during ER stress allows ATF6 to be transported to the Golgi. PMID:18653895 ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321: 569-572, 2008. Misfolded or unassembled proteins are discarded by ER-associated degradation (ERAD), which involves their retrotranslocation into the cytosol. ERAD substrates frequently contain disulfide bonds that must be cleaved before their retrotranslocation. ER-resident protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins, and accelerated ERAD through its physical and functional associations with EDEM (ER degradation-enhancing alpha-mannosidase-like protein) and an ER-resident chaperone BiP. PMID:8020977 Localization of the gene encoding human BiP/GRP78, the endoplasmic reticulum cognate of the HSP70 family, to chromosome 9q34. Genomics 20: 281-284, 1994. BiP/GRP78 is a member of the HSP70 family involved in the folding and assembly of proteins in the endoplasmic reticulum. HOIP:HOIP_0002680 XBP1 activation by IRE1 is a subtype of activation of transcription factor: A process that changes the activity of XBP1 (X-Box Binding Protein 1) to be higher by IRE1. This entity is a specific course-dependent process. This process is dependent on the ERAD process and can constitute the course of ER stress. http://www.reactome.org/PathwayBrowser/#/R-HSA-381183&SEL=R-HSA-1791121&PATH=R-HSA-392499,R-HSA-381119,R-HSA-381033 The XBP1 gene is transcribed to yield mRNA, the mRNA is spliced to yield Xbp(s) mRNA, and the mRNA is translated to yield protein. XBP1 activation by IRE1 [ER stress - ERAD] HOIP_0002680 HOIP:HOIP_0002682 Negative regulation of transport is a subtype of negative regulation process: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. negative regulation of transport HOIP_0002682 HOIP:HOIP_0002683 Bile secretion is a subtype of moving A to the outside of B: A process of the release of the bile to the outside of the liver. bile secretion HOIP_0002683 HOIP:HOIP_0002684 IRE1 signaling is a process that a signal is transmitted by the IRE1 (Inositol-requiring transmembrane kinase/endonuclease). IRE1 generally plays a endoplasmic reticulum membrane stress sensor role. This entity is a specific course-dependent process. This process is dependent on ERAD and can constitute the course of ER stress. IRE1 signaling [ER stress - ERAD] HOIP_0002684 HOIP:HOIP_0002685 IRE1 activation is a subtype of molecular activation: A process that changes the activity of the IRE1 to be higher. This entity is a specific course-dependent process. This process is dependent on ERAD and can constitute the course of ER stress. IRE1 activation [ER stress - ERAD] HOIP_0002685 HOIP:HOIP_0002686 IRE1 activation is a subtype of molecular activation: A process that changes the activity of the IRE1 to be higher. This process is dependent on the refolding and can constitute the course of ER stress. IRE1 activation [ER stress - refolding] HOIP_0002686 HOIP:HOIP_0002687 IRE1 activation is a subtype of molecular activation: A process that changes the activity of the IRE1 to be higher. This process is dependent on the apoptosis and can constitute the course of ER stress. IRE1 activation [ER stress - apoptosis] HOIP_0002687 HOIP:HOIP_0002688 IRE1 activation is a subtype of molecular activation: A process that changes the activity of the IRE1 to be higher. This process is dependent on the inflammation and can constitute the course of ER stress. IRE1 activation [ER stress - inflammation] HOIP_0002688 HOIP:HOIP_0002689 XBP1 activation by IRE1 is a subtype of activation of transcription factor: A process that changes the activity of XBP1 (X-Box Binding Protein 1) to be higher by IRE1. This process is dependent on the refolding and can constitute the course of ER stress. http://www.reactome.org/PathwayBrowser/#/R-HSA-381183&SEL=R-HSA-1791121&PATH=R-HSA-392499,R-HSA-381119,R-HSA-381033 The XBP1 gene is transcribed to yield mRNA, the mRNA is spliced to yield Xbp(s) mRNA, and the mRNA is translated to yield protein. XBP1 activation by IRE1 [ER stress - refolding] HOIP_0002689 HOIP:HOIP_0002690 XBP1 activation by IRE1 is a subtype of activation of transcription factor: A process that changes the activity of XBP1 (X-Box Binding Protein 1) to be higher by IRE1. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Reactome:R-HSA-1791121.3 The XBP1 gene is transcribed to yield mRNA, the mRNA is spliced to yield Xbp(s) mRNA, and the mRNA is translated to yield protein. XBP1 activation by IRE1 [ER stress] HOIP_0002690 Reactome:R-HSA-1791121.3 http://www.reactome.org/PathwayBrowser/#/R-HSA-381183&SEL=R-HSA-1791121&PATH=R-HSA-392499,R-HSA-381119,R-HSA-381033 HOIP:HOIP_0002691 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. This process is dependent on ERAD and can constitute the course of ER stress. ATF6 signaling [ER stress - ERAD] HOIP_0002691 HOIP:HOIP_0002692 Bile secretion to bile canaliculus is a subtype of bile secretion: A process that of the release from one side of a hepatocyte plasma membrane to a bile canaliculus. Bile canaliculi are the thin tubes formed by hepatocyte membranes. bile secretion to bile canaliculus HOIP_0002692 HOIP:HOIP_0002693 Bile acid and bile salt transport to hepatocyte is a subtype of bile acid and bile salt transport: A process that transports bile acid and bile salts within a hepatocyte by means of some agent such as a transporter or pore. bile acid and bile salt transport to hepatocyte HOIP_0002693 HOIP:HOIP_0002694 A family of transmembrane proteins that usually function as dimers to hydrolyze ATP, which permits them to transport a wide variety of substrates across cellular membranes. These proteins consist of two distinct domains, a transmembrane domain and a nucleotide-binding domain. ATP binding is required for both dimerization and transporter activity. http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C17750 ATP-binding cassette Transporter ABC transporter HOIP_0002694 HOIP:HOIP_0002695 Contraction of bile canaliculus is a subtype of contraction: A process that generates the directed movement in which the bile canaliculus decreases in volume. PMID:2040644 PMID:7015506 contraction of bile canaliculus HOIP_0002695 HOIP:HOIP_0002696 ERAD related gene expression by XBP1s is a subtype of gene expression: The process in which a gene sequence is converted into a mature ER-associated degradation (ERAD) gene product or products (proteins or RNA) by XBP1s. This entity is a specific course-dependent process. This process can constitute the course of ER stress. ERAD related gene expression byXBP1s [ER stress] HOIP_0002696 HOIP:HOIP_0002699 Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2. NCBI-Human-GeneID:9695 NCBI-Mouse-GeneID:192193 NCBI-Rat-GeneID:297504 PMID:11375934 PMID:12610306 PMID:18653895 http://omim.org/entry/607673 EDEM (canonical)[ER stress] HOIP_0002699 NCBI-Human-GeneID:9695 http://www.ncbi.nlm.nih.gov/gene/9695 NCBI-Mouse-GeneID:192193 http://www.ncbi.nlm.nih.gov/gene/192193 NCBI-Rat-GeneID:297504 http://www.ncbi.nlm.nih.gov/gene/297504 PMID:18653895 ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321: 569-572, 2008. HOIP:HOIP_0002700 EDEM -ERAD promoting factor (canonical)[ER stress -ERAD] HOIP_0002700 HOIP:HOIP_0002701 Hyperfunctioning of glutathione conjugates excretion from hepatocyte is a subtype of hyperfunctioning: A process that performs an excessive excretion of the glutathione conjugates from the hepatocyte. hyperfunctioning of glutathione conjugates excretion from hepatocyte HOIP_0002701 HOIP:HOIP_0002703 Converting cell type is a subtype of converting type: A process that changes the type of the cell. converting cell type HOIP_0002703 HOIP:HOIP_0002704 Changing permeability is a subtype of changing quality: A process that changes the temperature of the object. changing permeability HOIP_0002704 HOIP:HOIP_0002705 Changing size is a subtype of changing quality: A process that changes the size of the object. changing size HOIP_0002705 HOIP:HOIP_0002706 Increasing canalicular membrane permeability is a subtype of increasing membrane permeabilization: A process that changes the permeability of the canalicular membrane to be higher. increasing canalicular membrane permeability HOIP_0002706 HOIP:HOIP_0002708 Hyperfunction of glutathione export from hepatocyte is a subtype of hyperfunction of transport: A process that performs an excesssive export of the glutathione from the hepatocyte. ISBN:0071769234 PMID:18786560 hyperfunction of glutathione export from hepatocyte HOIP_0002708 ISBN:0071769234 GSH itself is often cotranported with other xenobiotics or xenobiotics metabolites, namely, by MRP2 into bile, and by MRP1,4,5 into blood. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition PMID:18786560 The Mrp proteins mediate not only GSH efflux, but they also export oxidized glutathione derivatives (e.g., glutathione disulfide (GSSG), S-nitrosoglutathione (GS-NO), and glutathione-metal complexes), as well as other glutathione S-conjugates. HOIP:HOIP_0002709 A process in which a signal to XBP1 is transduced by the IRE1. This entity is a specific course-dependent process. This process is dependent on ERAD and can constitute the course of ER stress. IRE1 signaling to XBP1 [ER stress] HOIP_0002709 HOIP:HOIP_0002710 Receiving abnormal protein signal by IRE1 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by IRE1. This process is dependent on the ERAD and can constitute the course of ER stress. receiving abnormal protein signal by IRE1 [ER stress - ERAD] HOIP_0002710 HOIP:HOIP_0002711 Hyperfunction of glutathione export from hepatocyte is a subtype of hyperfunction of transport: A process that performs an excesssive export of the glutathione from the hepatocyte. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. ISBN:0071769234 PMID:18786560 hyperfunction of glutathione export from hepatocyte [glutathione depletion (course)] HOIP_0002711 ISBN:0071769234 GSH itself is often cotranported with other xenobiotics or xenobiotics metabolites, namely, by MRP2 into bile, and by MRP1,4,5 into blood. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition PMID:18786560 The Mrp proteins mediate not only GSH efflux, but they also export oxidized glutathione derivatives (e.g., glutathione disulfide (GSSG), S-nitrosoglutathione (GS-NO), and glutathione-metal complexes), as well as other glutathione S-conjugates. HOIP:HOIP_0002712 A role played by the entity which regulatess OATP bile acid transport process. regulator of OATP bile acid transport HOIP_0002712 HOIP:HOIP_0002713 Bile tube occlusion is a subtype of occlusion: Obstruction or a closure of bile tube. bile tube occlusion HOIP_0002713 HOIP:HOIP_0002714 Increasing bile level is a subtype of increasing quantity: A process that changes the amount of bile to be higher. increasing bile level HOIP_0002714 HOIP:HOIP_0002715 Increasing bile concentration in blood is a subtype of increasing concentration: A process that changes the concentration of the bile in the blood to be higher. increasing bile concentration in blood HOIP_0002715 HOIP:HOIP_0002716 Refolding promoting gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature refolding inducing gene product or products (proteins or RNA) . This entity is a specific course-dependent process. This process can constitute the course of ER stress. refolding promoting gene expression [ER stress] HOIP_0002716 HOIP:HOIP_0002717 Increasing vomume of bile canaliculus is a subtype of increasing volume: A process that changes the volume of the bile canaliculus to be higher. increasing vomume of bile canaliculus HOIP_0002717 HOIP:HOIP_0002718 Hyperfunction of protein unfolding is a subtype of hyperfunctioning: A process that performs an excesssive protein unfolding. hyperfunction of protein unfolding HOIP_0002718 HOIP:HOIP_0002721 ATF4 gene expression by eIF2a is a subtype of gene expression: The process in which a gene sequence is converted into a mature ATF4 gene product or products (proteins or RNA) by eIF2a. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:23334697 Reactome:R-HSA-381128 http://www.ncbi.nlm.nih.gov/pubmed/18426796 ATF4 gene expression by eIF2a [ER stress - apoptosis] HOIP_0002721 PMID:23334697 Under conditions of eIF2α phosphorylation, a subset of mRNAs with small upstream open reading frames (such as activating transcription factor 4 [ATF4]) or internal ribosome entry sites are preferentially translated. ATF4 is a bZIP transcription factor that controls the regulation of expression of pro-survival UPR-target genes (e.g., the chaperones glucose regulated protein [GRP]78 and GRP94) as well as genes involved in other functions such as redox homeostasis, amino acid metabolism, apoptosis, and autophagy. HOIP:HOIP_0002722 Chop expession by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a sequence of the Chop is converted into a mature gene product or products (proteins or RNA) by ATF4. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:26977301 Chop expression by ATF4 [ER stress] [ER stress - apoptosis] HOIP_0002722 HOIP:HOIP_0002727 Ubiquitination of IkB is a subtype of protein ubiquitination: The process in which one or more ubiquitin groups are added to IkB. PMID:12464174 http://purl.obolibrary.org/obo/HINO_0017767 ubiquitination of IkB HOIP_0002727 HOIP:HOIP_0002728 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signaling factor (canonical)[ER stress - apotosis] HOIP_0002728 HOIP:HOIP_0002729 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signaling factor (canonical)[ER stress - Refolding] HOIP_0002729 HOIP:HOIP_0002730 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signal sensor (canonical)[ER stress - apotosis] HOIP_0002730 HOIP:HOIP_0002731 Receiving abnormal protein signal by PERK is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by PERK. This process is dependent on the apoptosis and can constitute the course of ER stress via apoptosis. receiving abnormal protein signal by PERK [ER stress - apoptosis] HOIP_0002731 HOIP:HOIP_0002732 Positive regulation of bile export is a subtype of positive regulation process: A process that that activates or increases the frequency, rate or extent of bile acid secretion. positive regulation of bile export HOIP_0002732 HOIP:HOIP_0002733 Negative regulation of bile acid and bile salts export from the hepatocyte to bile tube is a subtype of negative regulation of transport: A process that stops, prevents, or reduces the frequency, rate or extent of bile acid and bile salts export from the hepatocyte to the bile tube. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. negative regulation of bile acid and bile salts export from the hepatocyte to bile tube [glutathione depletion (course)] HOIP_0002733 HOIP:HOIP_0002734 Cholestasis is a subtype of stagnating: A process that changes the bile flow to be slower due to obstruction. This entity is a specific course-dependent process. This process can constitute the course of glutathione depletion. cholestasis [glutathione depletion (course)] HOIP_0002734 HOIP:HOIP_0002735 PERK-Nrf2 mediated pathway is a subtype of PERK signaling (integrated pathway): Sequence of linked reactions, which has PERK signaling and gene regulation pathway. PERK-Nrf2 mediated pathway (integrated pathway) HOIP_0002735 HOIP:HOIP_0002736 A process that changes the activity of the NRF2 to be higher by PERK. PMID:14517290 NRF2 activation by PERK HOIP_0002736 PMID:14517290 Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. HOIP:HOIP_0002737 Dissociation of Nrf2-Keap1 complex is a subtype of detaching: A process that disaggregates a Nrf2-Keap1 complexe into Nrf2 and Keap1. dissociation of Nrf2-Keap1 complex HOIP_0002737 HOIP:HOIP_0002738 Dissociation of Nrf2-Keap1 complex by Perk is a subtype of detaching: A process that disaggregates a Nrf2-Keap1 complex into Nrf2 and Keap1 by Perk. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PERK activation->dissociation of Nrf2/Keap in ER stress PERK-dependent phosphorylation triggers dissociation of Nrf2/Keap1 complexes and inhibits reassociation of Nrf2/Keap1 complexes in vitro. PMID:14517290 dissociation of Nrf2-Keap1 complex by PERK [ER stress] HOIP_0002738 HOIP:HOIP_0002739 A process that changes the activity of the NRF2 to be higher by PERK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:14517290 NRF2 activation by PERK [ER stress] HOIP_0002739 PMID:14517290 Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. HOIP:HOIP_0002740 PERK-NRF2 mediated pathway is a subtype of PERK signaling (integrated pathway): Sequence of linked reactions, which has PERK-NRF2 signaling and gene regulation pathway. This pathway is a specific course-dependent process. This process can constitute the course of ER stress. PERK-Nrf2 mediated pathway HOIP_0002740 HOIP:HOIP_0002741 Receiving abnormal protein signal by PERK is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by PERK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. receiving abnormal protein signal by PERK [ER stress] HOIP_0002741 HOIP:HOIP_0002742 A process in which a signal to NRF2 is transduced PERK. This entity is a specific course-dependent process. This process can constitute the course of PERK - eIF2A pathway. PERK signaling to Nrf2 [PERK - eIF2A pathway] HOIP_0002742 HOIP:HOIP_0002743 A process in which a signal to NRF2 is transduced PERK . This entity is a specific course-dependent process. This process can constitute the course of ER stress. PERK signaling to Nrf2 [ER stress] HOIP_0002743 HOIP:HOIP_0002744 Antioxidant gene expression by NRF2 is a subtype of gene expression: The process in which an antioxidant gene sequence is converted into a mature antioxidant gene product or products (proteins or RNA) by NRF2. This entity is a specific course-dependent process. This process can constitute the course of ER stress. antioxidant gene expression by NRF2 [ER stress] HOIP_0002744 HOIP:HOIP_0002745 NCBI-Human-GeneID:4780 NCBI-Rat-GeneID:83619 NRF2 - transcriptional regulator (canonical)[ER stress] HOIP_0002745 NCBI-Human-GeneID:4780 http://www.ncbi.nlm.nih.gov/gene/4780 NCBI-Rat-GeneID:83619 http://www.ncbi.nlm.nih.gov/gene/83619 HOIP:HOIP_0002746 Any process that activates or increases the frequency, rate or extent of cellular response to oxidative stress. This entity is a specific course-dependent process. This process can constitute the course of ER stress. positive regulation of cellular response to oxidative stress [ER stress] HOIP_0002746 HOIP:HOIP_0002747 Oxidation-antioxidtion inbalance is a subtype of imbalance: A process that lacks a balance between oxidation and anti-oxidation that inhibits oxidation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. oxidation-antioxidtion inbalance [ER stress] HOIP_0002747 HOIP:HOIP_0002748 Oxidation-antioxidtion inbalance is a subtype of imbalance: A process that lacks a balance between oxidation and anti-oxidation that inhibits oxidation. PMID:24641954 oxidative stress oxidation-antioxidtion inbalance HOIP_0002748 HOIP:HOIP_0002749 Receiving oxidative signal by PERK is a subtype of receiving signal: A process that recognizes another object and changes into a oxidative signal by PERK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. receiving oxidative signal by PERK [ER stress] HOIP_0002749 HOIP:HOIP_0002750 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. This process is dependent on the antioxidation and can constitute the course of ER stress. PERK activation [ER stress - antioxidation] HOIP_0002750 HOIP:HOIP_0002751 Enabling translation is a subtype of enabling: A process that sets conditions for translation to work correctly. This entity is a specific course-dependent process. This process can constitute the course of ER stress. This entity refers to the process of restarting translation. During protein refolding, it is known that a translation attenuation is occurred temporarily to reduce the production of new proteins. enabling translation [ER stress] HOIP_0002751 HOIP:HOIP_0002752 The process of removing one or more phosphoric (ester or anhydride) residues from the eIF2a. This entity is a specific course-dependent process. This process can constitute the course of ER stress. dephosphorylation of eIF2a [ER stress] HOIP_0002752 HOIP:HOIP_0002753 Gene expression patheway dependent molecule is a subtype of system dependeny functional molecule. This entity is dependent on a gene expresion system for functioning. gene expression patheway dependent molecule HOIP_0002753 HOIP:HOIP_0002754 eIF2a gene regulation pathway is a subtype of gene regulation pathway: Sequence of reactions to regulate translation of genes by eIF2a. eIF2a gene regulation pathway HOIP_0002754 HOIP:HOIP_0002755 Regulation of translation by eIF2a is a subtype of regulation of translation: A process that modulates the frequency, rate or extent of eIF2 alpha mediated translation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. regulation of translation by eIF2a [ER stress] HOIP_0002755 HOIP:HOIP_0002756 Positive regulation of uORF dependent gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of uORF dependent gene expression. positive regulation of uORF dependent gene expression HOIP_0002756 HOIP:HOIP_0002757 Positive regulation of uORF dependent gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of uORF dependent gene expression. This entity is a specific eIF2a translational system depedent. positive regulation of uORF dependent gene expression [eIF2a [translation regulation] HOIP_0002757 HOIP:HOIP_0002758 Degradation of I-kappaB is a subtype of protein catabolic process: A process of the chemical reactions resulting in the breakdown of inhibitor of kappa B (I-kappaB) protein degradation of I-kappaB HOIP_0002758 HOIP:HOIP_0002759 Bile acid accumulation in hepatocyte is a subtype of accumulation of substances in a biological object: A process that keeps bile acid within the hepatocute in the liver (intrahepatic). This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. Bile acid accumulation in hepatocyte [glutathione depletion (course)] HOIP_0002759 HOIP:HOIP_0002760 Refolding promoting gene expression by XBP1s is a subtype of gene expression: The process in which a gene sequence is converted into a mature refolding inducing gene product or products (proteins or RNA) by XbP1s . This entity is a specific course-dependent process. This process can constitute the course of ER stress. refolding promoting gene expression by XBP1s [ER stress] HOIP_0002760 HOIP:HOIP_0002761 A process in which a signal to XBP1 is transduced by the IRE1. This process is dependent on the refolding and can constitute the course of ER stress. IRE1 signaling to XBP1 [ER stress - refolding] HOIP_0002761 HOIP:HOIP_0002762 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA by eIF2A in the course of ER stress. This process is dependent on the translation attenuation and can constitute the course of ER stress. regulation of translation by eIF2a [ER stress - translation attenuation] HOIP_0002762 HOIP:HOIP_0002763 Gene expression by NRF2 is a subtype of Gene expression by transcriptional regulator: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by NRF2. gene expression by NRF2 HOIP_0002763 HOIP:HOIP_0002764 Gene expression by NRF2 is a subtype of Gene expression by transcriptional regulator: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by NRF2. This entity is a specific course-dependent process. This process can constitute the course of PERK - NRF2 pathway. gene expression by NRF2 [PERK - NRF2 pathway] HOIP_0002764 HOIP:HOIP_0002765 Gene expression by NRF2 is a subtype of Gene expression by transcriptional regulator: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by NRF2. This entity is a specific course-dependent process. This process can constitute the course of ER stress. gene expression by NRF2 [ER stress] HOIP_0002765 HOIP:HOIP_0002766 Inflammatory cytokine gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:20303879 inflammatory cytokine gene expression [ER stress] HOIP_0002766 PMID:20303879 IRE1->JNK->AP-1->inflammatory response IRE1->XBP1s->IL6, IL8, MCP1 IRE1->IKK->NfkB ATF6->NfkB Perk->reducedIkB->NfkB HOIP:HOIP_0002767 Gene expression by CHOP (DDIT3, GADD153) is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by CHOP (DDIT3, GADD153). This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:26977301 gene expression by CHOP (DDIT3, GADD153) [ER stress - apoptosis] HOIP_0002767 HOIP:HOIP_0002768 NFKB - transcriptional regulator (canonical)[ER stress - inflammation] HOIP_0002768 HOIP:HOIP_0002769 NFKB (canonical)[ER stress] HOIP_0002769 HOIP:HOIP_0002770 Gene expression bu NF-kappaB is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by NF-kappaB. gene expression by NF-kappaB HOIP_0002770 HOIP:HOIP_0002771 NCBI-Human-GeneID:5034 NCBI-Mouse-GeneID:18453 NCBI-Rat-GeneID:25506 PMID:15158710 PMID:23198585 PMID:23637286 PDI (canonical)[ER stress] HOIP_0002771 NCBI-Human-GeneID:5034 http://www.ncbi.nlm.nih.gov/gene/5034 NCBI-Mouse-GeneID:18453 http://www.ncbi.nlm.nih.gov/gene/18453 NCBI-Rat-GeneID:25506 http://www.ncbi.nlm.nih.gov/gene/25506 PMID:23637286 Protein disulfide isomerase (PDI) is the first discovered, most abundant oxidoreductase in the ER. Depending on conditions, it catalyzes formation, isomerization, or reduction of disulfide bonds. Without oxidoreductase capacity in the ER, protein folding would be too slow and prone to disaster, with abundant aggregation and degradation favored. Considering that protein folding in principle is a spontaneous process and that chaperones guide the process, the formation of nonnative disulfide bonds during folding is a must. HOIP:HOIP_0002772 I-kappaB phosphorylation is a subtype of phosphorylation: The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. GO:0007252 PMID:12464174 PMID:15134788 PMID:21772278 I-kappaB phosphorylation [NfKB pathway] HOIP_0002772 HOIP:HOIP_0002773 XBP1 splicing is a subtype of removing: The process of removing sections of the XBP1 RNA transcript to remove sequences. This process is dependent on the inflammation and can constitute the course of ER stress. XBP1 splicing [ER stress - inflammation] HOIP_0002773 HOIP:HOIP_0002774 A series of molecular signals transduced with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. GO:0007249 NfkB gene regulation pathway HOIP_0002774 HOIP:HOIP_0002775 Inflammatory gene expression by NF-kappa B is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the inflammation by NF-kappa B. This process is dependent on the IRE1-TRAF2-NfkB pathway mediated inflammation and can constitute the course of ER stress. inflammatory gene expression by NF-kappa B [ER stress - inflammation - IRE1-TRAF-NfkB pathway] HOIP_0002775 HOIP:HOIP_0002776 NCBI-Human-GeneID:54431 NCBI-Mouse-GeneID:66861 NCBI-Rat-GeneID:295690 PMID:18653895 ERDJ5 (canonical)[ER stress] HOIP_0002776 NCBI-Human-GeneID:54431 http://www.ncbi.nlm.nih.gov/gene/54431 NCBI-Mouse-GeneID:66861 http://www.ncbi.nlm.nih.gov/gene/66861 NCBI-Rat-GeneID:295690 http://www.ncbi.nlm.nih.gov/gene/295690 HOIP:HOIP_0002777 Ubiquitination of IkB is a subtype of protein ubiquitination: The process in which one or more ubiquitin groups are added to IkB. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. PMID:12464174 http://purl.obolibrary.org/obo/HINO_0017767 ubiquitination of IkB [NfKB pathway] HOIP_0002777 HOIP:HOIP_0002778 Degradation of I-kappaB is a subtype of protein catabolic process: A process of the chemical reactions resulting in the breakdown of inhibitor of kappa B (I-kappaB) protein This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. degradation of IKB [NfkB pathway] HOIP_0002778 HOIP:HOIP_0002779 NF-kappaB transport into nucleus is a subtype of nuclear transport: A process that of the directed movement of NF-kappaB from the cytoplasm to the nucleus. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. Translocation of NF-kappaB [NfKB pathway] HOIP_0002779 HOIP:HOIP_0002780 IKK activation is a subtype of molecular activation: A process that changes the activity of the IKK (kappaB Kinase) to be higher. IKK activation HOIP_0002780 HOIP:HOIP_0002781 IKK activation is a subtype of molecular activation: A process that changes the activity of the IIKK (kappaB Kinase) to be higher. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. IKK activation [NfKB pathway] HOIP_0002781 HOIP:HOIP_0002782 NF-kappaB activation is a subtype of transcription factor activation: A process that changes the activity of the NF-kappaB to be higher. NF-kappaB activation HOIP_0002782 HOIP:HOIP_0002783 NF-kappaB activation is a subtype of transcription factor activation: A process that changes the activity of the NF-kappaB to be higher. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. NF-kappaB activation [NfKB pathway] HOIP_0002783 HOIP:HOIP_0002784 Regulation of gene expression by NfKB is a subtype of regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of gene expression by NfkB. regulation of gene expression by NfKB HOIP_0002784 HOIP:HOIP_0002785 Regulation of gene expression by NfKB is a subtype of regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of gene expression by NfkB. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. regulation of gene expression by NfKB [NfKB pathway] HOIP_0002785 HOIP:HOIP_0002786 Binding of NF-kappaB and I-kappaB in cytosol is a subtype of binding: The selective interaction of a inhibitory-kappaB (I-kappaB/IKB) protein with NF-kappaB. In the resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. http://purl.obolibrary.org/obo/IEV_0000214 (obsolete) Binding of NF-kappaB and I-kappaB in cytosol HOIP_0002786 HOIP:HOIP_0002787 PMID:23087145 MRP4 [glutathione depletion (course)] ABCC4 (canonical)[glutathione depletion (course)] HOIP_0002787 HOIP:HOIP_0002789 The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. cytoplasmic sequestering of NF-kappaB [NfKB pathway] HOIP_0002789 HOIP:HOIP_0002790 The selective interaction of a inhibitory-kappaB (I-kappaB/IKB) protein with NF-kappaB. In the resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. PMID:15134788 http://purl.obolibrary.org/obo/IEV_0000214 Binding of NF-kappaB and I-kappaB in cytosol [NfkB pathway] Binding of NF-kappaB and I-kappaB in cytosol [NfKB pathway] HOIP_0002790 HOIP:HOIP_0002791 Dissociation of NF-kappaB -I-kappaB is a subtype of detaching: A process that disaggregates a NF-kappaB-I-kappaB to NF-kappaB dimers and I-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. This entity is a specific course-dependent process. This process can constitute the course of NfKB pathway. PMID:15134788 http://purl.obolibrary.org/obo/IEV_0000215 dissociation of NF-kappaB - IkappaB [NfKB pathway] HOIP_0002791 HOIP:HOIP_0002792 MRP5 [glutathione depletion (course)] ABCC5 (canonical)[glutathione depletion (course)] HOIP_0002792 HOIP:HOIP_0002793 PERK-NFkB pathway is a subtype of PERK signaling (integrated pathway): Sequence of linked reactions, which has PERK signaling and gene regulation pathway. This pathway is dependent on the inflammation and can constitute the course of ER stress. PMID:12773372 PERK-NFkB pathway [ER stress - inflammation] HOIP_0002793 HOIP:HOIP_0002794 PERK-eIF2a-NFkB pathway is a subtype of PERK-eIF2a signaling: Sequence of linked reactions, which has PERK-eIF2a signaling and gene regulation by NF-kappa B. This pathway is dependent on the inflammation and can constitute the course of ER stress. PMID:15542827 PMID:20303879 PMID:28860159 PERK-eIF2a-NFkB pathway [ER stress - inflammation] HOIP_0002794 PMID:20303879 Both the IRE1α and PERK branches of the UPR can lead to activation of the NF-κB-IKK pathway. This pathway also plays a critical role in the induction of multiple inflammatory mediators and has been implicated in insulin resistance. PMID:28860159 phosphorylated eIF2α attenuates general mRNA translation, During translational attenuation, IκB, an inhibitor of NF-κB, is depleted (due to its short half-life) to activate NF-κB. HOIP:HOIP_0002795 IRE1-TRAF2-NFkB signal transduction pathway is a subtype of IRE1 signaling (integrated pathway): Sequence of linked reactions, which has IRE1-TRAF2 signaling and gene regulation by NF-kappaB. This pathway is dependent on the inflammation and can constitute the course of ER stress. PMID:12843613 PMID:20303879 PMID:25232821 IRE1-TRAF2-NFkB signal transduction pathway [ER stress - inflammation] HOIP_0002795 PMID:12843613 NF-kB was activated by ER stress-inducing agents, thapsigargin and tunicamycin. The activation was inhibited by a dominant-negative IRE1. In addition, a dominant-negative TRAF2 also suppressed the activation of NF-kB by ER stress. These results suggest that ER stress-induced NF-kB activation is also mediated by the IRE1- TRAF2 pathway, as well as JNK activation. Result indicates that the RNase domain of IRE1 in the C-terminus is necessary for the binding of IRE1 with TRAF2, and that ER stress-induced NF-kB activation is dependent on not only the interaction between IRE1 and TRAF2, but also the kinase activity of IRE1. PMID:20303879 Both the IRE1α and PERK branches of the UPR can lead to activation of the NF-κB-IKK pathway. This pathway also plays a critical role in the induction of multiple inflammatory mediators and has been implicated in insulin resistance. PMID:25232821 IRE-1 directly triggers IκB kinase and as such IκB phosphorylation, in a TNF receptor associated factor (TRAF)-2 dependent manne HOIP:HOIP_0002796 ATF6-NFkB signal transduction pathway is a subtype of ATF6 signaling (integrated pathway): Sequence of linked reactions, which has ATF6 signaling and gene regulation by NF-kappaB. This process is dependent on positive inflammation and can constitute the course of ER stress. PMID:20303879 ATF6-NFkB signal transduction pathway [ER stress - inflammation] HOIP_0002796 PMID:20303879 The ATF6 branch of the UPR has also been linked to NF-κB-IKK signaling, suggesting that specific inflammatory triggers may signal through different branches of the UPR. HOIP:HOIP_0002797 PERK-eIF2a signaling is a subtype of PERK signaling (integrated pathway): Sequence of linked reactions, which has PERK-eIF2a signaling and gene regulation pathway. This pathway is dependent on the inflammation and can constitute the course of ER stress. PERK-eIF2a signaling [ER stress - inflammation] HOIP_0002797 HOIP:HOIP_0002798 NF-kappaB activation is a subtype of transcription factor activation: A process that changes the activity of the NF-kappaB to be higher. This process is dependent on the inflammation and can constitute the course of ER stress. CHOP Knock Down resulted in reduced cytokine-induced NF-κB activity and expression of key NF-κB target genes involved in apoptosis and inflammation, including iNOS, FAS, IRF-7, IL-15, CCL5 and CXCL10. This was due to decreased IκB degradation and p65 translocation to the nucleus CHOP Knock Down resulted in reduced cytokine-induced NF-κB activity and expression of key NF-κB target genes involved in apoptosis and inflammation, including iNOS, FAS, IRF-7, IL-15, CCL5 and CXCL10. This was due to decreased IκB degradation and p65 translocation to the nucleus NF-kappaB activation [ER stress - inflammation] HOIP_0002798 CHOP Knock Down resulted in reduced cytokine-induced NF-κB activity and expression of key NF-κB target genes involved in apoptosis and inflammation, including iNOS, FAS, IRF-7, IL-15, CCL5 and CXCL10. This was due to decreased IκB degradation and p65 translocation to the nucleus PMID:22653339 HOIP:HOIP_0002799 Decreasing I-kappaB production is a subtype of decreasing production quantity of protein: A process that changes the quantity of the Iinhibitor of kappa B (I-kappaB) to be lower. decreasing I-kappaB production HOIP_0002799 HOIP:HOIP_0002800 Decreasing I-kappaB production is a subtype of decreasing production quantity of protein: A process that changes the quantity of the Iinhibitor of kappa B (I-kappaB) to be lower. This process is dependent on the Perk-eIF2a-NfkB pathway mediated inflammation and can constitute the course of ER stress. PMID:22249202 PMID:25232821 decreasing I-kappaB production [ER stress - inflammation -Perk-eIF2a-NfkB] HOIP_0002800 PMID:25232821 Activation of PERK and concomitant translational inhibition leads to a disequilibrium in the ratio of the short-lived IκB protein (inhibitor of NF-κB) to the longer-lived NF-κB protein, resulting in activation of NF-κB, independent of IκB phosphorylation https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4388558/figure/F4/ HOIP:HOIP_0002801 inhibitor of NF-kappaB [ER stress - inflammation] I-kappaB -NfkB inhibitor [ER stress - inflammation] HOIP_0002801 HOIP:HOIP_0002802 IKB HOIP_0002802 HOIP:HOIP_0002803 A role played by the entity which enables the energy-independent passage of cations across a lipid bilayer down a concentration gradient. related molecular function GO:0005261 cation channel HOIP_0002803 HOIP:HOIP_0002804 NF-kappaB transport into nucleus is a subtype of nuclear transport: A process that of the directed movement of NF-kappaB from the cytoplasm to the nucleus. This process is dependent on the inflammation and can constitute the course of ER stress. Translocation of NF-kappaB [ER stress - inflammation] HOIP_0002804 HOIP:HOIP_0002805 Inflammatory gene expression by NF-kappa B via PERK is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the inflammation by NF-kappa B via PERK. This process is dependent on the inflammation and can constitute the course of ER stress. inflammatory cytokine gene expression by NF-kappa B via PERK [ER stress - inflammation] HOIP_0002805 HOIP:HOIP_0002806 Inflammatory cytokine gene expression via JNK is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA) via JNK pathway. This process is dependent on the inflammation and can constitute the course of ER stress. inflammatory cytokine gene expression via JNK [ER stress - inflammation] HOIP_0002806 HOIP:HOIP_0002807 NF-kappaB activation is a subtype of transcription factor activation: A process that changes the activity of the NF-kappaB to be higher. This process is dependent on the IRE1-TRAF2-IkB-NfkB pathway mediated inflammation and can constitute the course of ER stress. NF-kappaB activation [ER stress - inflammation - IRE1-TRAF2-IkB-NfkB pathway] HOIP_0002807 HOIP:HOIP_0002808 I-kappaB phosphorylation is a subtype of phosphorylation: The process of introducing a phosphate group into an inhibitor of kappa B (I-kappaB) protein. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing bound NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. This process is dependent on the IRE1-NfkB pathway mediated inflammation and can constitute the course of ER stress. GO:0007252 PMID:12464174 PMID:15134788 PMID:21772278 I-kappaB phosphorylation [ER stress - inflammation - IRE1-NfkB pathway] HOIP_0002808 HOIP:HOIP_0002809 Ubiquitination of IkB is a subtype of protein ubiquitination: The process in which one or more ubiquitin groups are added to IkB. This process is dependent on the IRE1-NfkB pathway mediated inflammation and can constitute the course of ER stress. PMID:12464174 http://purl.obolibrary.org/obo/HINO_0017767 ubiquitination of IkB [ER stress - inflammation - IRE1-NfKB pathway] HOIP_0002809 HOIP:HOIP_0002810 Degradation of I-kappaB is a subtype of protein catabolic process: A process of the chemical reactions resulting in the breakdown of inhibitor of kappa B (I-kappaB) protein. This process is dependent on the IRE1-NfkB pathway mediated inflammation and can constitute the course of ER stress. degradation of I-kappaB [ER stress] HOIP_0002810 HOIP:HOIP_0002811 Inflammatory gene expression by NF-kappa B via IRE1 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the inflammation by NF-kappa B via IRE1. This process is dependent on the inflammation and can constitute the course of ER stress. inflammatory cytokine gene expression by NF-kappa B via IRE1 [ER stress - inflammation] HOIP_0002811 HOIP:HOIP_0002812 Regulation of gene expression by NfKB is a subtype of regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of gene expression by NfkB. This process is dependent on the PERK-eIF2a-NfkB pathway mediated inflammation and can constitute the course of ER stress. PMID:20303879 regulation of gene expression by NfKB [ER stress - inflammation - PERK-eIF2a-NfkB pathway] HOIP_0002812 HOIP:HOIP_0002813 Regulation of gene expression by NfKB is a subtype of regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of gene expression by NfkB. This process is dependent on the IRE1-TARF2-NfkB pathway mediated inflammation and can constitute the course of ER stress. regulation of gene expression by NfKB [ER stress - inflammation - IRE1-Traf2-NfkB pathway] HOIP_0002813 HOIP:HOIP_0002814 Translocation of NF-kappaB from the Cytosol to the Nucleus is a subtype of nuclear transport: A process that of the directed movement of NF-kappaB from the cytoplasm to the nucleus. This process is dependent on the Perk-eIF2a-NfkB pathway mediated inflammation and can constitute the course of ER stress. Translocation of NF-kappaB from the Cytosol to the Nucleus [ER stress - inflammation - Perk-eIF2a-NfkB pathway] HOIP_0002814 HOIP:HOIP_0002815 Translocation of NF-kappaB from the Cytosol to the Nucleus is a subtype of nuclear transport: A process that of the directed movement of NF-kappaB from the cytoplasm to the nucleus. This process is dependent on the IRE1-TRAF2-NfkB pathway mediated inflammation and can constitute the course of ER stress. Translocation of NF-kappaB from the Cytosol to the Nucleus [ER stress - inflammation - IRE1-TRAF2-NfkB pathway] HOIP_0002815 HOIP:HOIP_0002816 TRAF2 activation by IRE1 is a subtype of molecular activation: A process that changes the activity of the TARF2 to be higher by IRE1. This process is dependent on the IRE1-TRAF2-IKK-NfkB pathway mediated inflammation and can constitute the course of ER stress. PMID:25232821 TRAF2 activation by IRE1 [ER stress - inflammation - IRE1-TRAF2-IKK-NfkB pathway] HOIP_0002816 PMID:25232821 IRE-1 directly triggers IκB kinase and as such IκB phosphorylation, in a TNF receptor associated factor (TRAF)-2 dependent manner HOIP:HOIP_0002817 IKK activation is a subtype of molecular activation: A process that changes the activity of the IIKK (kappaB Kinase) to be higher. This process is dependent on the IRE1-TRAF2-NfkB pathway mediated inflammation and can constitute the course of ER stress. PMID:12843613 PMID:25232821 IKK activation [ER stress - inflammation - IRE1-TRAF2-NfkB pathway] HOIP_0002817 PMID:25232821 IRE-1 directly triggers IκB kinase and as such IκB phosphorylation, in a TNF receptor associated factor (TRAF)-2 dependent manner. HOIP:HOIP_0002818 NCBI-Human-GeneID:7186 NCBI-Mouse-GeneID:22030 NCBI-Rat-GeneID:311786 TRAF2 (canonical)[ER stress] HOIP_0002818 NCBI-Human-GeneID:7186 http://www.ncbi.nlm.nih.gov/gene/7186 NCBI-Mouse-GeneID:22030 http://www.ncbi.nlm.nih.gov/gene/22030 NCBI-Rat-GeneID:311786 http://www.ncbi.nlm.nih.gov/gene/311786 HOIP:HOIP_0002819 TRAF2 -IRE1 adaptor protein (canonical)[ER stress - inflammation -IRE1-NfkB] HOIP_0002819 HOIP:HOIP_0002820 TRAF2 activation by IRE1 is a subtype of molecular activation: A process that changes the activity of the TARF2 to be higher by IRE1. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:25232821 TRAF2 activation by IRE1 [ER stress] HOIP_0002820 PMID:25232821 IRE-1 directly triggers IκB kinase and as such IκB phosphorylation, in a TNF receptor associated factor (TRAF)-2 dependent manner HOIP:HOIP_0002821 TRAF2 activation by IRE1 is a subtype of molecular activation: A process that changes the activity of the TARF2 to be higher by IRE1. This process is dependent on the IRE1-TRAF2-ASK-JNK pathway mediated inflammation and can constitute the course of ER stress. PMID:25232821 TRAF2 activation by IRE1 [ER stress - inflammation - IRE1-TRAF2-ASK-JNK pathway] HOIP_0002821 PMID:25232821 IRE-1 also mediates phosphorylation of JNK in a TRAF2-ASK dependent pathway18, which was linked to insulin receptor substrate (IRS)-1 phosphorylation and the development of insulin resistance in type II diabetes HOIP:HOIP_0002822 TRAF2 -IRE1 adaptor protein (canonical)[ER stress - inflammation -IRE1-JNK] HOIP_0002822 HOIP:HOIP_0002823 ASK activation is a subtype of molecular activation: A process that changes the activity of one of the ASK (apoptosis signal-regulating kinase) family to be higher. This process is dependent on the inflammation and can constitute the course of ER stress. PMID:12843613 PMID:25232821 ASK activation [ER stress - inflammation] HOIP_0002823 PMID:25232821 IRE-1 also mediates phosphorylation of JNK in a TRAF2-ASK dependent pathway, which was linked to insulin receptor substrate (IRS)-1 phosphorylation and the development of insulin resistance in type II diabetes. HOIP:HOIP_0002824 ASK activation is a subtype of molecular activation: A process that changes the activity of one of the ASK (apoptosis signal-regulating kinase) family to be higher. This entity is a specific course-dependent process. This process can constitute the course of IRE-TRAF2-ASK-JNK pathway. ASK activation [IRE-TRAF2-ASK-JNK pathway] HOIP_0002824 HOIP:HOIP_0002825 ASK activation is a subtype of molecular activation: A process that changes the activity of one of the ASK （apoptosis signal-regulating kinase) family to be higher. ASK activation HOIP_0002825 HOIP:HOIP_0002826 JNK activation is a subtype of molecular activation: A process that changes the activity of the JNK to be higher. This entity is a specific course-dependent process. This process can constitute the course of JNK pathway. JNK activation [JNK pathway] HOIP_0002826 HOIP:HOIP_0002827 JNK activation is a subtype of molecular activation: A process that changes the activity of the JNK to be higher. This process is dependent on the IRE1-TRAF2-ASK-JNK pathway mediated inflammation and can constitute the course of ER stress. PMID:25232821 JNK activation [ER stress - inflammation - IRE1-TRAF2-ASK-JNK pathway] HOIP_0002827 PMID:25232821 IRE-1 also mediates phosphorylation of JNK in a TRAF2-ASK dependent pathway18, which was linked to insulin receptor substrate (IRS)-1 phosphorylation and the development of insulin resistance in type II diabetes HOIP:HOIP_0002828 JNK activation is a subtype of molecular activation: A process that changes the activity of the JNK to be higher. JNK activation HOIP_0002828 HOIP:HOIP_0002829 AP-1 activation is a subtype of AP-1 activation: A process that changes the activity of the AP-1 to be higher by JNK. This process is dependent on the IRE1-TRAF2-ASK-JNK pathway mediated inflammation and can constitute the course of ER stress. AP-1 activation by JNK [ER stress - inflammation - IRE1-TRAF2-ASK-JNK pathway] HOIP_0002829 HOIP:HOIP_0002830 Inflammatory gene expression by XBP1s is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the inflammation by XBP1s. This process is dependent on the inflammation and can constitute the course of ER stress. inflammatory cytokine gene expression by XBP1s [ER stress - inflammation] HOIP_0002830 HOIP:HOIP_0002831 A process in which a signal to XBP1 is transduced by the IRE1. This process is dependent on the inflammation and can constitute the course of ER stress. IRE1 signaling to XBP1 [ER stress - inflammation] HOIP_0002831 HOIP:HOIP_0002832 XBP1 activation by IRE1 is a subtype of activation of transcription factor: A process that changes the activity of XBP1 (X-Box Binding Protein 1) to be higher by IRE1. This process is dependent on the inflammation and can constitute the course of ER stress. http://www.reactome.org/PathwayBrowser/#/R-HSA-381183&SEL=R-HSA-1791121&PATH=R-HSA-392499,R-HSA-381119,R-HSA-381033 The XBP1 gene is transcribed to yield mRNA, the mRNA is spliced to yield Xbp(s) mRNA, and the mRNA is translated to yield protein. XBP1 activation by IRE1 [ER stress - inflammation] HOIP_0002832 HOIP:HOIP_0002833 Inflammatory gene expression by AP-1 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the inflammation by AP-1. This process is dependent on the inflammation and can constitute the course of ER stress. PMID:22883813 inflammatory cytokine gene expression by AP-1 [ER stress - inflammation] HOIP_0002833 PMID:22883813 The IRE1a branch of the UPR is responsible for AP-1 activation. Genes tran- scribed by AP-1 include those encoding tumor necrosis factor (TNF), keratinocyte growth factor (KGF), granulo- cyte macrophage colony-stimulating factor (GM-CSF), in- terleukin (IL)-8, and certain cytokine receptors . HOIP:HOIP_0002834 A process in which a signal to TRAF2 is transduced by the IRE1. This process is dependent on the IRE1-TRAF2-IKK-NfkB pathway mediated inflammation and can constitute the course of ER stress. IRE1 signaling to TRAF2 [ER stress - inflammation - IRE1-TRAF2-IKK-NfkB pathway] HOIP_0002834 HOIP:HOIP_0002835 A process in which a signal to TRAF2 is transduced by the IRE1. This process is dependent on the IRE1-TRAF2-ASK-JNK pathway mediated inflammation and can constitute the course of ER stress. IRE1 signaling to TRAF2 [ER stress - inflammation - IRE1-TRAF2-ASK-JNK pathway] HOIP_0002835 HOIP:HOIP_0002836 IRE1-XBP1 mediated pathway is a subtype of IRE1 signaling (integrated pathway): Sequence of linked reactions, which has IRE1 signaling and gene regulation by XBP1. This process is dependent on inflammation and can constitute the course of ER stress. IRE1-XBP1 mediated pathway [ER stress - inflammation] HOIP_0002836 HOIP:HOIP_0002837 Translocation of NF-kappaB from the Cytosol to the Nucleus is a subtype of nuclear transport: A process that of the directed movement of NF-kappaB from the cytoplasm to the nucleus. This process is dependent on the ATF6-NfkB pathway mediated inflammation and can constitute the course of ER stress. Translocation of NF-kappaB from the Cytosol to the Nucleus [ER stress - inflammation - ATF6-NfkB pathway] HOIP_0002837 HOIP:HOIP_0002838 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. This process is dependent on the inflammation and can constitute the course of ER stress. ATF6 signaling [ER stress - inflammation] HOIP_0002838 HOIP:HOIP_0002839 PERK - stress sensor (canonical)[ER stress - translation attenuation] HOIP_0002839 HOIP:HOIP_0002840 Regulation of gene expression by NfKB is a subtype of regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of gene expression by NfkB. This process is dependent on the ATF6-NfkB Pathway mediated inflammation and can constitute the course of ER stress. regulation of gene expression by NfKB [ER stress - inflammation - ATF6-NfkB Pathway] HOIP_0002840 HOIP:HOIP_0002841 NF-kappaB activation is a subtype of transcription factor activation: A process that changes the activity of the NF-kappaB to be higher. This process is dependent on the ATF6-NfkB pathway mediated inflammation and can constitute the course of ER stress. NF-kappaB activation [ER stress - inflammation - ATF6-NfkB] HOIP_0002841 HOIP:HOIP_0002842 Decreasing I-kappaB production is a subtype of decreasing production quantity of protein: A process that changes the quantity of the Iinhibitor of kappa B (I-kappaB) to be lower. This process is dependent on the ATF6-NfkB pathway mediated inflammation and can constitute the course of ER stress. PMID:22249202 PMID:25232821 decreasing I-kappaB production [ER stress -inflmmation- ATF6-NfkB] HOIP_0002842 PMID:25232821 Activation of PERK and concomitant translational inhibition leads to a disequilibrium in the ratio of the short-lived IκB protein (inhibitor of NF-κB) to the longer-lived NF-κB protein, resulting in activation of NF-κB, independent of IκB phosphorylation https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4388558/figure/F4/ HOIP:HOIP_0002843 Inflammatory cytokine gene expression by NF-kappaB via ATF6 is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA) by NF-kappaB via ATF6 signaling. This process is dependent on the inflammation and can constitute the course of ER stress. inflammatory cytokine gene expression by NF-kappa B via ATF6 [ER stress - inflammation] HOIP_0002843 HOIP:HOIP_0002844 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. This process is dependent on the ATF6-NfkB pathway mediated inflammation and can constitute the course of ER stress. ATF6 signaling [ER stress - inflammation - ATF6-NfkB pathway] HOIP_0002844 HOIP:HOIP_0002845 PERK - stress sensor (canonical)[ER stress - apotosis] HOIP_0002845 HOIP:HOIP_0002846 PERK - stress sensor (canonical)[ER stress - inflammation] HOIP_0002846 HOIP:HOIP_0002847 Receiving abnormal protein signal by PERK is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by PERK. This process is dependent on the inflammation and can constitute the course of ER stress via inflammation. receiving abnormal protein signal by PERK [ER stress - inflammation] HOIP_0002847 HOIP:HOIP_0002848 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signal sensor (canonical)[ER stress - inflammation] HOIP_0002848 HOIP:HOIP_0002849 A process in which a signal to eIF2a is transduced by PERK. This process is dependent on the inflammation and can constitute the course of ER stress. PERK signaling to eIF2a [ER stress - inflammation] HOIP_0002849 HOIP:HOIP_0002850 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signaling factor (canonical)[ER stress - inflammation] HOIP_0002850 HOIP:HOIP_0002851 XBP1 splicing is a subtype of removing: The process of removing sections of the XBP1 RNA transcript to remove sequences. This process is dependent on the refolding process and can constitute the course of ER stress. XBP1 splicing [ER stress - refolding] HOIP_0002851 HOIP:HOIP_0002852 A process that changes the activity of the eIF2a by PERK. This process is dependent on the inflammation and can constitute the course of ER stress. changing activity of eIF2a by PERK [ER stress - inflammation] HOIP_0002852 HOIP:HOIP_0002853 Any process that stops, prevents, or reduces the frequency, rate or extent of I-Kappa B translation by eIF2a. This process is dependent on the inflammation and can constitute the course of ER stress. attenuation of I-kappaB translation by eIF2a [ER stress - inflammation] HOIP_0002853 HOIP:HOIP_0002854 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. This process is dependent on the inflammation and can constitute the course of ER stress. PERK activation [ER stress - inflammation] HOIP_0002854 HOIP:HOIP_0002855 PERK dimerization is a subtype of protein dimerization: The formation of a PERK dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This process is dependent on the inflammation and can constitute the course of ER stress. Reactome:R-HSA-381087 http://www.ncbi.nlm.nih.gov/pubmed/11907036 PERK dimerization [ER stress - inflammation] HOIP_0002855 HOIP:HOIP_0002856 PERK - kinase (canonical)[ER stress - inflammation] HOIP_0002856 HOIP:HOIP_0002857 PERK - kinase (canonical)[ER stress - translation attenuation] HOIP_0002857 HOIP:HOIP_0002858 PERK - autophosphorylation kinase (canonical)[ER stress - translation attenuation] HOIP_0002858 HOIP:HOIP_0002859 PERK - autophosphorylation kinase (canonical)[ER stress - inflammation] HOIP_0002859 HOIP:HOIP_0002860 PERK - autophosphorylation kinase (canonical)[ER stress - apotosis] HOIP_0002860 HOIP:HOIP_0002861 PERK - autophosphorylation kinase (canonical)[ER stress - Refolding] HOIP_0002861 HOIP:HOIP_0002862 PERK - kinase (canonical)[ER stress - apotosis] HOIP_0002862 HOIP:HOIP_0002863 PERK - kinase (canonical)[ER stress - Refolding] HOIP_0002863 HOIP:HOIP_0002864 PERK - stress sensor (canonical)[ER stress - Refolding] HOIP_0002864 HOIP:HOIP_0002865 Dissociation of PERK:BIP heterodimer is a subtype of detaching: A process that disaggregates PERK-BIP heterodimers into BIP and PERK. This process is dependent on the inflammation and can constitute the course of ER stress. PMID:10854322 PMID:11907036 Reactome:R-HSA-381086 PERK (EIF2AK3) is a single-pass transmembrane protein located in the Endoplasmic Reticulum (ER) membrane. PERK has an N-terminal luminal domain and a C-terminal cytosolic domain. It is maintained in an inactive state by association of its luminal domain with BiP, a chaperone in the ER. Because BiP also binds unfolded proteins, BiP dissociates from PERK when unfolded proteins exceed chaperone activity in the ER. Dissociation of PERK:BIP Heterodimer [ER stress - inflammation] HOIP_0002865 HOIP:HOIP_0002866 PERK dimerization is a subtype of protein dimerization: The formation of a PERK dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This process is dependent on the apoptosis and can constitute the course of ER stress. Reactome:R-HSA-381087 http://www.ncbi.nlm.nih.gov/pubmed/11907036 PERK dimerization [ER stress - apoptosis] HOIP_0002866 HOIP:HOIP_0002867 PERK dimerization is a subtype of protein dimerization: The formation of a PERK dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This process is dependent on the refolding and can constitute the course of ER stress. Reactome:R-HSA-381087 http://www.ncbi.nlm.nih.gov/pubmed/11907036 PERK dimerization [ER stress - refolding] HOIP_0002867 HOIP:HOIP_0002868 PERK autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by PERK of one or more of its own amino acid residues (cis-autophosphorylation), or residues on PERK (trans-autophosphorylation). This process is dependent on the inflammation and can constitute the course of ER stress. PERK autophosphorylation [ER stress - inflammation] HOIP_0002868 HOIP:HOIP_0002869 PERK autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by PERK of one or more of its own amino acid residues (cis-autophosphorylation), or residues on PERK (trans-autophosphorylation). This process is dependent on the apoptosis and can constitute the course of ER stress. PERK autophosphorylation [ER stress - apoptosis] HOIP_0002869 HOIP:HOIP_0002870 PERK autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by PERK of one or more of its own amino acid residues (cis-autophosphorylation), or residues on PERK (trans-autophosphorylation). This process is dependent on the refolding and can constitute the course of ER stress. PERK autophosphorylation [ER stress - refolding] HOIP_0002870 HOIP:HOIP_0002871 XBP1 splicing is a subtype of removing: The process of removing sections of the XBP1 RNA transcript to remove sequences. This entity is a specific course-dependent process. This process is dependent on the ERAD process and can constitute the course of ER stress. XBP1 splicing [ER stress - ERAD] HOIP_0002871 HOIP:HOIP_0002872 TRAF2 activation by IRE1 is a subtype of molecular activation: A process that changes the activity of the TARF2 to be higher by IRE1. PMID:25232821 TRAF2 activation by IRE1 HOIP_0002872 PMID:25232821 IRE-1 directly triggers IκB kinase and as such IκB phosphorylation, in a TNF receptor associated factor (TRAF)-2 dependent manner HOIP:HOIP_0002873 A duration quality of a process inhering in a bearer by virtue of the bearer's having slow progressive course of indefinite duration. http://purl.obolibrary.org/obo/PATO_0001863 chronic HOIP_0002873 HOIP:HOIP_0002874 Regulation of translation by eIF2a is a subtype of regulation of translation: A process that modulates the frequency, rate or extent of eIF2 alpha mediated translation. regulation of translation by eIF2a HOIP_0002874 HOIP:HOIP_0002875 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). This process is dependent on the apoptosis that can constitute the course of ER stress. IRE1 pathway [ER stress - apoptosis] HOIP_0002875 HOIP:HOIP_0002876 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). This process is dependent on the inflammation via IRE1-XBP1 pathway that can constitute the course of ER stress. IRE1 pathway [ER stress - inflammation - IRE1-XBP1 pathway] HOIP_0002876 HOIP:HOIP_0002877 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). This process is dependent on the inflammation that can constitute the course of ER stress. IRE1 pathway [ER stress - ERAD] HOIP_0002877 HOIP:HOIP_0002878 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). This process is dependent on the inflammation via IRE1-JNK pathway that can constitute the course of ER stress. IRE1 pathway [ER stress - inflammation - IRE1-JNK pathway] HOIP_0002878 HOIP:HOIP_0002879 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). This process is dependent on the inflammation via IRE1-NfkB pathway that can constitute the course of ER stress. IRE1 pathway [ER stress - inflammation - IRE1-NfkB pathway] HOIP_0002879 HOIP:HOIP_0002880 NCBI-Human-GeneID:9451 NCBI-Mouse-GeneID:13666 NCBI-Rat-GeneID:29702 http://omim.org/entry/604032 EIF2AK3 PERK dimer (canonical)[ER stress] HOIP_0002880 NCBI-Human-GeneID:9451 http://www.ncbi.nlm.nih.gov/gene/9451 NCBI-Mouse-GeneID:13666 http://www.ncbi.nlm.nih.gov/gene/13666 NCBI-Rat-GeneID:29702 http://www.ncbi.nlm.nih.gov/gene/29702 HOIP:HOIP_0002881 PERK dimer (canonical)[ER stress - Refolding] HOIP_0002881 HOIP:HOIP_0002882 PERK dimer (canonical)[ER stress - inflammation] HOIP_0002882 HOIP:HOIP_0002883 PERK dimer (canonical)[ER stress - apotosis] HOIP_0002883 HOIP:HOIP_0002884 PERK dimer (canonical)[ER stress - translation attenuation] HOIP_0002884 HOIP:HOIP_0002885 Dissociation of IRE1:BIP heterodimer is a subtype of detaching: A process that disaggregates IRE-1-BIP heterodimers into BIP and IRE1. This process is dependent on the inflammation and can constitute the course of ER stress. Dissociation of IRE1:BIP Heterodimer [ER stress - inflammation] HOIP_0002885 HOIP:HOIP_0002886 IRE - stress sensor (canonical)[ER stress - inflammation] HOIP_0002886 HOIP:HOIP_0002887 Receiving abnormal protein signal by IRE1 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by IRE1. This process is dependent on the inflammation and can constitute the course of ER stress. receiving abnormal protein signal by IRE1 [ER stress - inflammation] HOIP_0002887 HOIP:HOIP_0002888 Receiving abnormal protein signal by IRE1 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by IRE1. This process is dependent on the IRE1-TRAF2-ASK-JNK pathway mediated inflammation and can constitute the course of ER stress. receiving abnormal protein signal by IRE1 [ER stress - inflammation - IRE1-TRAF2-ASK-JNK pathway] HOIP_0002888 HOIP:HOIP_0002889 Receiving abnormal protein signal by IRE1 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by IRE1. This process is dependent on the IRE1-TRAF2-IKK-NfkB pathway mediated inflammation and can constitute the course of ER stress. receiving abnormal protein signal by IRE1 [ER stress - inflammation - IRE1-TRAF2-IKK-NfkB pathway] HOIP_0002889 HOIP:HOIP_0002890 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 - signal sensor (canonical)[ER stress - inflammation] HOIP_0002890 HOIP:HOIP_0002891 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 - signaling factor (canonical)[ER stress - inflammation] HOIP_0002891 HOIP:HOIP_0002892 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 - signaling factor (canonical)[ER stress -ERAD] HOIP_0002892 HOIP:HOIP_0002893 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 - signaling factor (canonical)[ER stress - inflammation -Xbp1] HOIP_0002893 HOIP:HOIP_0002894 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 - signaling factor (canonical)[ER stress - inflammation -TRAF2] HOIP_0002894 HOIP:HOIP_0002895 Receiving abnormal protein signal by IRE1 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by IRE1. This process is dependent on the IRE1-XBP1 pathway mediated inflammation and can constitute the course of ER stress. receiving abnormal protein signal by IRE1 [ER stress - inflammation - IRE1-XBP1 pathway] HOIP_0002895 HOIP:HOIP_0002896 phosphorylated eIF2A - translation initiation inhibitor [ER stress - inflammation] P-EIF2A - translation initiation inhibitor (canonical)[ER stress - inflammation] HOIP_0002896 HOIP:HOIP_0002897 PMID:8107808 CALR [ER stress] CALRETICULIN (canonical)[ER stress] HOIP_0002897 PMID:8107808 Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. HOIP:HOIP_0002898 PMID:27698029 PMID:8107808 http://omim.org/entry/109091 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=Retrieve&dopt=full_report&list_uids=811 CALR - chaperone [ER stress -Refolding [persist]] CALRETICULIN - chaperone (canonical)[ER stress -Refolding [persist]] HOIP_0002898 PMID:27698029 Calnexin and calreticulin promote the efficient folding of glycoproteins by: (1) stabilizing folding events or slowing the folding process in a domain specific manner; (2) preventing aggregation and turnover; (3) retaining nonnative substrates in the ER to support additional attempts for proper folding; (4) facilitating the formation of disulfide bond formation through their association with the oxidoreductase ERp57 ; (5) perhaps facilitating Pro isomerization through association with the PPIase CypB PMID:8107808 Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. HOIP:HOIP_0002899 ATF6 - transcriptional factor (canonical)[ER stress - Refolding] HOIP_0002899 HOIP:HOIP_0002900 ATF6 - stress sensor (canonical)[ER stress - Refolding] HOIP_0002900 HOIP:HOIP_0002901 ATF6 - signaling factor (canonical)[ER stress - Refolding] HOIP_0002901 HOIP:HOIP_0002902 ATF6 - signaling factor (canonical)[ER stress - inflammation] HOIP_0002902 HOIP:HOIP_0002903 Dissociation of ATF6:BIP heterodimer is a subtype of detaching: A process that disaggregates ATF6-BIP heterodimers into BIP and ATF6. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Dissociation of ATF6-alpha:BIP Complex [ER stress] HOIP_0002903 HOIP:HOIP_0002904 Dissociation of ATF6:BIP heterodimer is a subtype of detaching: A process that disaggregates ATF6-BIP heterodimers into BIP and ATF6. This process is dependent on the refolding and can constitute the course of ER stress. Dissociation of ATF6-alpha:BIP Complex [ER stress - refolding] HOIP_0002904 HOIP:HOIP_0002905 Bip-unfolded protein is a subtype of a molecular complex. This entity has sub-parts of molecules: BIP/GRP78, and an unfolded protein. This entity can participate in the infmallation of ER stress via PERK pathway. Bip-unfolded protein complex 1 [ER stress - refolding] HOIP_0002905 HOIP:HOIP_0002906 Bip-unfolded protein is a subtype of a molecular complex. This entity has sub-parts of molecules: BIP/GRP78, and an unfolded protein. This entity can participate in the protein refolding of ER stress. Bip-Unfolded Protein complex 2 [ER stress - refolding] HOIP_0002906 HOIP:HOIP_0002907 Bip-unfolded protein is a subtype of a molecular complex. This entity has sub-parts of molecules: BIP/GRP78, and an unfolded protein. This entity can participate in the inflammation of ER stress via IRE1 pathway. Bip-unfolded protein complex 3 [ER stress - inflammation] HOIP_0002907 HOIP:HOIP_0002908 ATF6 mediated proapoptic gene production pathway is a subtype of ATF6 signaling (integrated pathway): Sequence of linked reactions, which has ATF6 signaling and gene regulation pathway. This process is dependent on positive regulation of apoptosis and can constitute the course of ER stress. ATF6 mediated proapoptic gene production pathway [ER stress - apoptosis] HOIP_0002908 HOIP:HOIP_0002909 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. This process is dependent on the apoptosis and can constitute the course of ER stress. ATF6 signaling [ER stress - apoptosis] HOIP_0002909 HOIP:HOIP_0002910 ATF6 - signaling factor (canonical)[ER stress - apotosis] HOIP_0002910 HOIP:HOIP_0002911 ATF6 activation is a subtype of molecular activation: A process that changes the activity of the ATF6 (Activating Transcription Factor 6) to be higher. This process is dependent on the apoptosis and can constitute the course of ER stress. ATF6 activation [ER stress - apoptosis] HOIP_0002911 HOIP:HOIP_0002912 Refolding gene expression by ATF6 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the apoptosis by ATF6. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:23334697 PMID:26960794 apoptotic gene expression by ATF6 [ER stress - apoptosis] HOIP_0002912 PMID:233334697 PMID:26960794 These findings support the idea that PERK/ATF6 cross-talk is a primary driver of CHOP expression within the liver ( A previous study of CHO and COS-1 cell lines suggested that ATF6 can contribute to CHOP expression by an ER-stress element situated in the CHOP promoter (Ma et al., 2002 blue right-pointing triangle). We addressed the role played by ATF6 in CHOP expression in Hepa1-6 cells by depleting ATF6 using shRNA, followed by treatment with 2 μM tunicamycin. Loss of ATF6 led to reductions in the expression of well-defined ATF6-target genes, including ER chaperone BiP (GRP78/HSPA5) and XBP1t and its spliced variant XBP1s (Figure 2A; Yoshida et al., 2001 blue right-pointing triangle; Baumeister et al., 2005 blue right-pointing triangle). ATF4 mRNA levels were also modestly reduced in the ATF6-depleted cells treated with tunicamycin, but there was no measurable reduction in ATF4 protein levels (Figure 2, A and B). Of importance, depletion of ATF6 sharply lowered the induction of CHOP mRNA and protein upon ER stress in the Hepa1-6 cells. The CHOP protein levels were reduced by 76 and 51% at 3 and 6 h, respectively. These results suggest that ATF6 can be a major contributor to CHOP expression, especially during ER stress. To address whether other ATF transcription factors regulated by PERK can effect CHOP expression, we depleted ATF5 expression in Hepa1-6 cells using shRNA and found no changes in induced expression of CHOP protein by ER stress (Figure 2C). These findings indicate that the requirement of ATF6 for induced CHOP expression in the Hepa1-6 hepatocytes is not broadly shared among other transcription factors controlled by PERK. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4850040/ HOIP:HOIP_0002913 ATF6 - transcriptional factor (canonical)[ER stress - apotosis] HOIP_0002913 HOIP:HOIP_0002914 NCBI-Human-GeneID:1649 NCBI-Mouse-GeneID:13198 NCBI-Rat-GeneID:29467 PMID:15601821 PMID:15775988 PMID:22761832 PMID:25904325 DDIT3 [ER stress] CHOP (canonical)[ER stress] HOIP_0002914 NCBI-Human-GeneID:1649 http://www.ncbi.nlm.nih.gov/gene/1649 NCBI-Mouse-GeneID:13198 http://www.ncbi.nlm.nih.gov/gene/13198 NCBI-Rat-GeneID:29467 http://www.ncbi.nlm.nih.gov/gene/29467 PMID:15775988 TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. HOIP:HOIP_0002915 PMID:15601821 PMID:15775988 PMID:22761832 PMID:25904325 http://www.omim.org/entry/126337 DDIT3 [ER stress - apoptosis - apoptosis inducer ] CHOP - apotosis inducing factor (canonical)[ER stress - apotosis] HOIP_0002915 PMID:15775988 TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. HOIP:HOIP_0002916 Apoptosis inducing gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature apoptosis inducing gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of ER stress. apoptosis promoting gene expression [ER stress] HOIP_0002916 HOIP:HOIP_0002917 Apoptosis inducing gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature apoptosis inducing gene product or products (proteins or RNA). apoptosis promoting gene expression HOIP_0002917 HOIP:HOIP_0002918 ATF6 activation is a subtype of molecular activation: A process that changes the activity of the ATF6 (Activating Transcription Factor 6) to be higher. This process is dependent on ERAD and can constitute the course of ER stress. ATF6 activation [ER stress - ERAD] HOIP_0002918 HOIP:HOIP_0002919 Refolding gene expression by XBP1 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the protein refolding function by XBP1. This process is dependent on the refolding and can constitute the course of ER stress. refolding gene expression by XBP1 [ER stress - refolding] HOIP_0002919 HOIP:HOIP_0002920 PMID:10837345 PMID:14674765 PMID:20942857 R-HSA-1791066.1 https://omim.org/entry/601746 GRP170 - chaperone [ER stress - Refolding] HYOU1 - chaperone (canonical)[ER stress - Refolding] HOIP_0002920 PMID:20942857 A comprehensive review of GRP170 as a putative GRP78 co-chaperone is available. HOIP:HOIP_0002921 NCBI-Human-GeneID:10525 NCBI-Mouse-GeneID:12282 NCBI-Rat-GeneID:192235 PMID:10037731 PMID:10837345 R-HSA-1791066.1 https://omim.org/entry/601746 grp170 [ER stress] HYOU1 (canonical)[ER stress] HOIP_0002921 NCBI-Human-GeneID:10525 http://www.ncbi.nlm.nih.gov/gene/10525 NCBI-Mouse-GeneID:12282 http://www.ncbi.nlm.nih.gov/gene/12282 NCBI-Rat-GeneID:192235 http://www.ncbi.nlm.nih.gov/gene/192235 PMID:10037731 150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death. HOIP:HOIP_0002922 A role played by the entity that assists chaperon and ensures correct protein folding. co-chaperone HOIP_0002922 HOIP:HOIP_0002923 XBP1 - transcriptional regulator (canonical)[ER stress - Refolding] HOIP_0002923 HOIP:HOIP_0002924 ATF6 activation is a subtype of molecular activation: A process that changes the activity of the ATF6 (Activating Transcription Factor 6) to be higher. This process is dependent on the inflammation and can constitute the course of ER stress. ATF6 activation [ER stress - inflammation] HOIP_0002924 HOIP:HOIP_0002925 Positive regulation of gene expression via JNK signaling is a subtype of positive regulation of gene expression: A process that that activates or increases the frequency, rate or extent of gene expression via JNK signaling. This entity is a specific course-dependent process. This process can constitute the course of ER stress. positive regulation of gene expression via JNK signaling [ER stress] HOIP_0002925 HOIP:HOIP_0002926 Receiving abnormal protein signal by IRE1 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by IRE1. This process is dependent on the apoptosis and can constitute the course of ER stress. receiving abnormal protein signal by IRE1 [ER stress - apoptosis] HOIP_0002926 HOIP:HOIP_0002927 JNK - kinase (canonical)[ER stress - inflammation] HOIP_0002927 HOIP:HOIP_0002928 JNK - kinase (canonical)[ER stress - apotosis] HOIP_0002928 HOIP:HOIP_0002929 JNK - signalling factor (canonical)[ER stress - apotosis] HOIP_0002929 HOIP:HOIP_0002930 JNK - signalling factor (canonical)[ER stress - inflammation] HOIP_0002930 HOIP:HOIP_0002931 P-EIF2A - translation initiation inhibitor (canonical)[ER stress - translation] HOIP_0002931 HOIP:HOIP_0002932 EIF2A - translation initiation factor (canonical)[ER stress - translation] HOIP_0002932 HOIP:HOIP_0002933 A role played by the entity that activates, or increases the frequency, rate or extent of translation initiation positive regulator role of translational initiation HOIP_0002933 HOIP:HOIP_0002934 NCBI-Human-GeneID:23645 NCBI-Mouse-GeneID:17872 NCBI-Rat-GeneID:171071 GADD34 (canonical)[ER stress] HOIP_0002934 NCBI-Human-GeneID:23645 http://www.ncbi.nlm.nih.gov/gene/23645 NCBI-Mouse-GeneID:17872 http://www.ncbi.nlm.nih.gov/gene/17872 NCBI-Rat-GeneID:171071 http://www.ncbi.nlm.nih.gov/gene/171071 HOIP:HOIP_0002935 http://omim.org/entry/611048 http://www.ncbi.nlm.nih.gov/gene/23645 GADD34 - phosphatase (canonical)[ER stress - translation] HOIP_0002935 HOIP:HOIP_0002936 IRE1-Traf2-ASK-JNK-Bcl2 pathway is a subtype of IRE1 signaling (integrated pathway): Sequence of linked reactions, which has IRE1-Traf2-ASK-JNK-BCL2 pathway and gene regulation. This pathway is dependent on the apoptosis and can constitute the course of ER stress. IRE1-TRAF2-ASK1 complex A protein complex of the endoplasmic reticulum membrane that consists of IRE1 (Inositol-requiring enzyme-1), TRAF2 (TNF receptor-associated factor 2) and ASK1 (Apoptosis signal-regulating kinase 1, a MAP3K). http://purl.obolibrary.org/obo/GO_1990604 IRE1-Traf2-ASK-JNK-Bcl2 pathway [ER stress - apoptosis] HOIP_0002936 HOIP:HOIP_0002937 TRAF2 activation by IRE1 is a subtype of molecular activation: A process that changes the activity of the TARF2 to be higher by IRE1. This process is dependent on the IRE1−TRAF2-ASK-JNK-Bcl2 pathway mediated apoptosis and can constitute the course of ER stress. PMID:25232821 TRAF2 activation by IRE1 [ER stress - apoptosis - IRE1−TRAF2-ASK-JNK-Bcl2 pathway] HOIP_0002937 PMID:25232821 IRE-1 also mediates phosphorylation of JNK in a TRAF2-ASK dependent pathway18, which was linked to insulin receptor substrate (IRS)-1 phosphorylation and the development of insulin resistance in type II diabetes HOIP:HOIP_0002938 TRAF2 -IRE1 adaptor protein (canonical)[ER stress - apotosis -IRE1-JNK] HOIP_0002938 HOIP:HOIP_0002939 ASK activation is a subtype of molecular activation: A process that changes the activity of one of the ASK (apoptosis signal-regulating kinase) family to be higher. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:12843613 PMID:25232821 ASK activation [ER stress - apoptosis - IRE1-TRAF2-ASK-JNK-Bcl2 pathway] HOIP_0002939 PMID:25232821 IRE-1 also mediates phosphorylation of JNK in a TRAF2-ASK dependent pathway, which was linked to insulin receptor substrate (IRS)-1 phosphorylation and the development of insulin resistance in type II diabetes. HOIP:HOIP_0002940 JNK activation is a subtype of molecular activation: A process that changes the activity of the JNK to be higher. This process is dependent on the IRE1−TRAF2-ASK-JNK-Bcl2 pathway mediated apoptosis and can constitute the course of ER stress. PMID:25232821 JNK activation [ER stress - apoptosis - IRE1−TRAF2-ASK-JNK-Bcl2 pathway] HOIP_0002940 PMID:25232821 IRE-1 also mediates phosphorylation of JNK in a TRAF2-ASK dependent pathway18, which was linked to insulin receptor substrate (IRS)-1 phosphorylation and the development of insulin resistance in type II diabetes HOIP:HOIP_0002941 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 IRE1 - signaling factor (canonical)[ER stress - apotosis] HOIP_0002941 HOIP:HOIP_0002942 NCBI-Human-GeneID:10926 NCBI-Mouse-GeneID:27214 NCBI-Rat-GeneID:312046 ASK (canonical)[ER stress] HOIP_0002942 NCBI-Human-GeneID:10926 http://www.ncbi.nlm.nih.gov/gene/10926 NCBI-Mouse-GeneID:27214 http://www.ncbi.nlm.nih.gov/gene/27214 NCBI-Rat-GeneID:312046 http://www.ncbi.nlm.nih.gov/gene/312046 HOIP:HOIP_0002943 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 ASK - signaling factor (canonical)[ER stress - inflammation] HOIP_0002943 HOIP:HOIP_0002944 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 ASK - signaling factor (canonical)[ER stress - inflammation -TRAF2] HOIP_0002944 HOIP:HOIP_0002945 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 ASK - signaling factor (canonical)[ER stress - apotosis -TRAF2] HOIP_0002945 HOIP:HOIP_0002946 A process that changes the activity of the Bcl2 to be lower by JNK. This process is dependent on the IRE1-TRAF2-JNK pathway mediated apoptosis and can constitute the course of ER stress. Inhibition of anti-apoptotic factor Bcl-2 results in the promotion of apoptosis. Bcl2 inactivation by JNK [ER stress - apoptosis - IRE1-TRAF2-JNK pathway] HOIP_0002946 HOIP:HOIP_0002947 Bcl2 inactivation by JNK is a subtype of inactivating: A process that changes the activity of the Bcl2 to be lower by JNK. Bcl2 inactivation by JNK HOIP_0002947 HOIP:HOIP_0002948 BIM activation is a subtype of molecular activation: A process that changes the activity of the BIM (BCL2L11), BH3-only BCL-2 family, to be higher. This process is dependent on the IRE1−TRAF2-JNK-Bcl2 pathway mediated apoptosis and can constitute the course of ER stress. PMID:12818176 BIM activation [ER stress - apoptosis - IRE1−TRAF2-JNK-Bcl2 pathway] HOIP_0002948 PMID:12818176 JNK-mediated BIM phosphorylation potentiates BAX-dependent apoptosis HOIP:HOIP_0002949 BIM activation is a subtype of molecular activation: A process that changes the activity of the BIM (BCL2L11), BH3-only BCL-2 family, to be higher. BIM activation HOIP_0002949 HOIP:HOIP_0002950 Bcl2 phosphorylation by JNK is a subtype of Bcl2 phosphorylation: A process that The process of introducing a phosphate group into Bcl2 by JNK. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:23334697 PMID:9930704 Reactome:R-HSA-381111 The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Bcl2 phosphorylation by JNK [ER stress - apoptosis] HOIP_0002950 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. R-HSA-381111 HOIP:HOIP_0002951 Bcl2 phosphorylation by JNK is a subtype of Bcl2 phosphorylation: A process that The process of introducing a phosphate group into Bcl2 by JNK. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:23334697 Reactome:R-HSA-381111 Bcl2 phosphorylation by JNK [ER stress] HOIP_0002951 PMID:23334697 IRE1 can bind to the adaptor protein TRAF2 to initiate the activation of ASK1 and JNK signaling pathways. JNK can then phosphorylate BCL-2 to reduce its antiapoptotic activity and phosphorylate the pro-apoptotic protein BIM (BCL2-interacting mediator of cell death) resulting in BCL-2-associated X protein (BAX)-dependent apoptosis. HOIP:HOIP_0002952 Bcl2 phosphorylation by JNK is a subtype of Bcl2 phosphorylation: A process that The process of introducing a phosphate group into Bcl2 by JNK. Bcl2 phosphorylation by JNK HOIP_0002952 HOIP:HOIP_0002953 IRE1 signaling is a process that a signal is transmitted by the IRE1 (Inositol-requiring transmembrane kinase/endonuclease). IRE1 generally plays a endoplasmic reticulum membrane stress sensor role. This process is dependent on the apoptosis and can constitute the course of ER stress. IRE1 signaling [ER stress - apoptosis] HOIP_0002953 HOIP:HOIP_0002954 BIM (canonical)[ER stress - apotosis] HOIP_0002954 HOIP:HOIP_0002955 NCBI-Human-GeneID:10018 NCBI-Mouse-GeneID:12125 NCBI-Rat-GeneID:64547 BIM (canonical)[ER stress] HOIP_0002955 NCBI-Human-GeneID:10018 http://www.ncbi.nlm.nih.gov/gene/10018 NCBI-Mouse-GeneID:12125 http://www.ncbi.nlm.nih.gov/gene/12125 NCBI-Rat-GeneID:64547 http://www.ncbi.nlm.nih.gov/gene/64547 HOIP:HOIP_0002956 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). This process is dependent on the protein refolding that can constitute the course of ER stress. IRE1 pathway [ER stress - refolding] HOIP_0002956 HOIP:HOIP_0002957 Receiving abnormal protein signal by IRE1 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by IRE1. This entity is a specific course-dependent process. This process can constitute the course of ER stress via protein refolding. receiving abnormal protein signal by IRE1 [ER stress - refolding] HOIP_0002957 HOIP:HOIP_0002958 ATF6 - signaling factor (canonical)[ER stress -ERAD] HOIP_0002958 HOIP:HOIP_0002959 XBP1s gene regulation pathway is a subtype of gene regulation pathway: A series of process in which XBP1s regulates the gene expression. This process is dependent on the protein refolding and can constitute the course of ER stress. XBP1s gene regulation pathway [ER stress - refolding] HOIP_0002959 HOIP:HOIP_0002960 XBP1s gene regulation pathway is a subtype of gene regulation pathway: A series of process in which XBP1s regulates the gene expression. This process is dependent on the inflammation that can constitute the course of ER stress. XBP1s gene regulation pathway [ER stress - ERAD] HOIP_0002960 HOIP:HOIP_0002961 CHOP gene regulation pathway is a subtype of gene regulation pathway: Sequence of reactions to regulate genes by CHOP. This pathway is dependent on the apoptosis and can constitute the course of ER stress. CHOP gene regulation pathway [ER stress - apoptosis] HOIP_0002961 HOIP:HOIP_0002962 NRF2 signaling (integrated pathway) is a subtype of integrated signaling pathway: Sequence of linked reactions, which has NRF2 signaling and gene regulation pathway. This pathway is a specific course-dependent process. This process can constitute the course of ER stress. NRF2 gene regulation pathway [ER stress] HOIP_0002962 HOIP:HOIP_0002963 Refolding gene regulation pathway by ATF4 is a subtype of ATF4 gene regulation pathway: Sequence of reactions to regulate refolding genes by ATF4. This pathway can constitute the course of ER stress. Refolding gene regulation pathway by ATF4 [ER stress] HOIP_0002963 HOIP:HOIP_0002964 Refolding gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the refolding by ATF4. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:26977301 refolding gene expression by ATF4 [ER stress] HOIP_0002964 HOIP:HOIP_0002965 ATF4 - transcriptional regulator (canonical)[ER stress - Refolding] HOIP_0002965 HOIP:HOIP_0002966 Inflammatiory gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to apoptosis by ATF4. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:26977301 apoptotic gene expression by ATF4 [ER stress - apoptosis] HOIP_0002966 HOIP:HOIP_0002967 Carbohydrate metabolism related gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related carbohydrate metabolism by ATF4. This entity is a specific course-dependent process. This process can constitute the course of ER stress. carbohydrate metabolism gene expression by ATF4 [ER stress] HOIP_0002967 HOIP:HOIP_0002968 Lipid metabolism gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the lipid metabolism by ATF4. This entity is a specific course-dependent process. This process can constitute the course of ER stress. lipid metabolism gene expression by ATF4 [ER stress] HOIP_0002968 HOIP:HOIP_0002969 ATF4 - transcriptional regulator (canonical)[ER stress - glucose metabolism disorder] HOIP_0002969 HOIP:HOIP_0002970 ATF4 - transcriptional regulator (canonical)[ER stress - dyslipidemia] HOIP_0002970 HOIP:HOIP_0002971 IRE1 dimerization is a subtype of protein dimerization: The formation of a IRE1 dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This process is dependent on the refolding and can constitute the course of ER stress. PMID:11897784 PMID:23236464 Reactome:R-HSA-381109 IRE1 dimerization [ER stress - refolding] HOIP_0002971 HOIP:HOIP_0002972 NCBI-Human-GeneID:2081 NCBI-Mouse-GeneID:78943 NCBI-Rat-GeneID:498013 http://omim.org/entry/604032 ERN1 dimer [ER stress] IRE1 dimer (canonical)[ER stress] HOIP_0002972 NCBI-Human-GeneID:2081 http://www.ncbi.nlm.nih.gov/gene/2081 NCBI-Mouse-GeneID:78943 http://www.ncbi.nlm.nih.gov/gene/78943 NCBI-Rat-GeneID:498013 http://www.ncbi.nlm.nih.gov/gene/498013 HOIP:HOIP_0002973 IRE1 dimer (canonical)[ER stress - Refolding] HOIP_0002973 HOIP:HOIP_0002974 IRE1 dimer (canonical)[ER stress -ERAD] HOIP_0002974 HOIP:HOIP_0002975 IRE1 dimerization is a subtype of protein dimerization: The formation of a IRE1 dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This entity is a specific course-dependent process. This process is dependent on ERAD and can constitute the course of ER stress. PMID:11897784 PMID:23236464 Reactome:R-HSA-381109 IRE1 dimerization [ER stress - ERAD] HOIP_0002975 HOIP:HOIP_0002976 IRE1 autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by IRE1 of one or more of its own amino acid residues (cis-autophosphorylation), or residues on IRE1 (trans-autophosphorylation). This process is dependent on the refolding and can constitute the course of ER stress. IRE1 autophosphorylation [ER stress - refolding] HOIP_0002976 HOIP:HOIP_0002977 IRE1 autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by IRE1 of one or more of its own amino acid residues (cis-autophosphorylation), or residues on IRE1 (trans-autophosphorylation). This process is dependent on the ERAD and can constitute the course of ER stress. IRE1 autophosphorylation [ER stress - ERAD] HOIP_0002977 HOIP:HOIP_0002978 IRE1 - autophosphorylation kinase (canonical)[ER stress - Refolding] HOIP_0002978 HOIP:HOIP_0002979 IRE1 - autophosphorylation kinase (canonical)[ER stress -ERAD] HOIP_0002979 HOIP:HOIP_0002980 Translocation of XBP1s from the cytosol to the nucleus is a subtype of nuclear transport: A process that of the directed movement of XBP1s from the cytoplasm to the nucleus. Translocation of XBP1s from the cytosol to the nucleus HOIP_0002980 HOIP:HOIP_0002981 Translocation of XBP1s from the cytosol to the nucleus is a subtype of nuclear transport: A process that of the directed movement of XBP1s from the cytoplasm to the nucleus. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Translocation of XBP1s from the cytosol to the nucleus [ER stress] HOIP_0002981 HOIP:HOIP_0002982 Translocation of XBP1s from the cytosol to the nucleus is a subtype of nuclear transport: A process that of the directed movement of XBP1s from the cytoplasm to the nucleus. This process is dependent on the refolding and can constitute the course of ER stress. Translocation of XBP1s from the cytosol to the nucleus [ER stress - refolding] HOIP_0002982 HOIP:HOIP_0002983 Translocation of XBP1s from the cytosol to the nucleus is a subtype of nuclear transport: A process that of the directed movement of XBP1s from the cytoplasm to the nucleus. This entity is a specific course-dependent process. This process is dependent on the ERAD and can constitute the course of ER stress. Translocation of XBP1s from the cytosol to the nucleus [ER stress - ERAD] HOIP_0002983 HOIP:HOIP_0002984 XBP1s gene regulation pathway is a subtype of gene regulation pathway: A series of process in which XBP1s regulates the gene expression. This pathway is dependent on the inflammation and can constitute the course of ER stress. XBP1s gene regulation pathway[ER stress - inflammation] HOIP_0002984 HOIP:HOIP_0002985 Translocation of XBP1s from the cytosol to the nucleus is a subtype of nuclear transport: A process that of the directed movement of XBP1s from the cytoplasm to the nucleus. This process is dependent on the inflammation and can constitute the course of ER stress. Translocation of XBP1s from the cytosol to the nucleus [ER stress - inflammation] HOIP_0002985 HOIP:HOIP_0002986 PERK-eIF2a-CyclinD1 pathway is a subtype of PERK-eIF2a signaling: Sequence of linked reactions, which has PERK-eIF2a signaling and CyclinD1 gene regulation. This pathway is dependent on the cell cycle arrest and can constitute the course of ER stress. PERK-eIF2a-CyclinD1 pathway [ER stress - cell cycle arrest] HOIP_0002986 HOIP:HOIP_0002987 Regulation of cell cycle related gene expression is a subtype of regulation of gene expression: A process that modulates the frequency, rate or extent of cel cycle related gene expression. This entity is a specific course-dependent process. This process can constitute the course of ER stress. regulation of cell cycle related gene expression [ER stress] HOIP_0002987 HOIP:HOIP_0002988 Negative regulation of formation of cytoplasmic translation initiation complex is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of formation of cytoplasmic translation initiation complex. This process is dependent on the inflammation and can constitute the course of ER stress. PMID:23334697 PMID:9930704 negative regulation of formation of cytoplasmic translation initiation complex by eIF2a [ER stress - inflammation] HOIP_0002988 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. HOIP:HOIP_0002989 Any process that stops, prevents, or reduces the frequency, rate or extent of Cyclin D1 translation by eIF2a. This entity is a specific course-dependent process. This process can constitute the course of ER stress. attenuation of Cyclin D1 translation by eIF2a [ER stress] HOIP_0002989 HOIP:HOIP_0002990 Negative regulation of cell cycle regulator gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of cell cycle regulator gene expression. This entity is a specific course-dependent process. This process can constitute the course of ER stress. negative regulation of cell cycle regulator gene expression [ER stress] HOIP_0002990 HOIP:HOIP_0002991 A process in which a signal to eIF2a is transduced by PERK. This process is dependent on the cell cycle arrest and can constitute the course of ER stress. PERK signaling to eIF2a [ER stress - cell cycle arrest] HOIP_0002991 HOIP:HOIP_0002992 Receiving abnormal protein signal by PERK is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by PERK. This entity is a specific course-dependent process. This process can constitute the course of ER stress via cell cycle arrest. receiving abnormal protein signal by PERK [ER stress - cell cycle arrest] HOIP_0002992 HOIP:HOIP_0002993 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signal sensor (canonical)[ER stress - cell cycle arrest] HOIP_0002993 HOIP:HOIP_0002994 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signal sensor (canonical)[ER stress - Refolding] HOIP_0002994 HOIP:HOIP_0002995 Dissociation of PERK:BIP heterodimer is a subtype of detaching: A process that disaggregates PERK-BIP heterodimers into BIP and PERK. This process is dependent on the cell cycle arrest and can constitute the course of ER stress. PMID:10854322 PMID:11907036 Reactome PathwayStep4038 PERK (EIF2AK3) is a single-pass transmembrane protein located in the Endoplasmic Reticulum (ER) membrane. PERK has an N-terminal luminal domain and a C-terminal cytosolic domain. It is maintained in an inactive state by association of its luminal domain with BiP, a chaperone in the ER. Because BiP also binds unfolded proteins, BiP dissociates from PERK when unfolded proteins exceed chaperone activity in the ER. Dissociation of PERK:BIP Heterodimer [ER stress - cell cycle arrest] HOIP_0002995 Reactome PathwayStep4038 http://purl.obolibrary.org/obo/HINO_0006880 HOIP:HOIP_0002996 PERK - stress sensor (canonical)[ER stress - cell cycle arrest] HOIP_0002996 HOIP:HOIP_0002997 PERK autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by PERK of one or more of its own amino acid residues (cis-autophosphorylation), or residues on PERK (trans-autophosphorylation). This process is dependent on the cell cycle arrest and can constitute the course of ER stress. PERK autophosphorylation [ER stress - cell cycle arrest] HOIP_0002997 HOIP:HOIP_0002998 PERK - autophosphorylation kinase (canonical)[ER stress - cell cycle arrest] HOIP_0002998 HOIP:HOIP_0002999 PERK - kinase (canonical)[ER stress - cell cycle arrest] HOIP_0002999 HOIP:HOIP_0003000 Phosphorylation of eIF2-alpha by PERK is a subtype of eIF2a phosphorylation: A process that The process of introducing a phosphate group into eIF2a by PERK. This process is dependent on the cell cycle arrest and can constitute the course of ER stress. PMID:23334697 PMID:9930704 Reactome:R-HSA-381111 The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Phosphorylation of eIF2-alpha by PERK [ER stress - cell cycle arrest] HOIP_0003000 PMID:23334697 Activated PERK phosphorylates the eIF2α at serine 51, resulting in inactivation of eIF2α, preventing assembly of the preinitiation ribosome complex. This attenuates general mRNA translation. ATF4 which has a subset of mRNAs with small upstream open reading frames or internal ribosome entry sites are translated. PMID:9930704 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1. Id:R-HSA-381111 HOIP:HOIP_0003001 A process that changes the activity of the eIF2a by PERK. This process is dependent on the cell cycle arrest and can constitute the course of ER stress. changing activity of eIF2a by PERK [ER stress - cell cycle arrest] HOIP_0003001 HOIP:HOIP_0003002 PERK activation is a subtype of Molecular activation: A process that changes the activity of PERK to be higher. This process is dependent on the cell cycle arrest and can constitute the course of ER stress. PERK activation [ER stress - cell cycle arrest] HOIP_0003002 HOIP:HOIP_0003003 http://purl.obolibrary.org/obo/UniProt_Q9NZJ5 http://www.uniprot.org/entry/Q9NZJ5 PERK - signaling factor (canonical)[ER stress - cell cycle arrest] HOIP_0003003 HOIP:HOIP_0003004 PERK dimerization is a subtype of protein dimerization: The formation of a PERK dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This entity is a specific course-dependent process. This process is dependent on the process of cell cycle arrest and can constitute the course of ER stress. Reactome:R-HSA-381087 http://www.ncbi.nlm.nih.gov/pubmed/11907036 PERK dimerization [ER stress - cell cycle arrest] HOIP_0003004 HOIP:HOIP_0003005 PERK dimer (canonical)[ER stress - cell cycle arrest] HOIP_0003005 HOIP:HOIP_0003006 G1-S期特異的。 PMID:10411905 PMID:23334697 CYCLIND1 (canonical)[ER stress] HOIP_0003006 PMID:23334697 Activated PERK can phosphorylate eIF2α. Phospho-eIF2α leads to translation attenuation with immediate effects on proteins with short half-lives Cyclin D1 which results in immediate cell cycle arrest. HOIP:HOIP_0003007 Changing calcium ion concentration is a subtype of changing concentration: A process that changes the calcium ion concentration in the blood. changing calcium ion concentration HOIP_0003007 HOIP:HOIP_0003008 Changing calcium ion concentration in ER is a subtype of changing calcium ion concentration: A process that changes the calcium ion concentration in the endoplasmic reticulum (ER). This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:16672378 PMID:23334697 changing calcium ion concentration in ER [ER stress] HOIP_0003008 PMID:233334697 PMID:16672378 PMID:23334697 PMID:23334697 PMID:23334697 PMID:23334697 Ritonavir and lopinavir may also have effects on ER Ca2+ levels by inhibition of SERCA HOIP:HOIP_0003009 Changing calcium ion concentration in ER is a subtype of changing calcium ion concentration: A process that changes the calcium ion concentration in the endoplasmic reticulum (ER). changing calcium ion concentration in ER HOIP_0003009 HOIP:HOIP_0003012 ER stress dependent chemical compound is a subtype of course dependent chemical entity. This entity (drug) can participate in the course of ER stress. ER stress dependent chemical compound HOIP_0003012 HOIP:HOIP_0003013 Negative regulation of SERCA gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of SERCA gene expression. negative regulation of SERCA gene expression HOIP_0003013 HOIP:HOIP_0003014 Negative regulation of SERCA gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of SERCA gene expression. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:22407670 PMID:23334697 negative regulation of SERCA gene expression [ER stress] HOIP_0003014 PMID:23334697 PMID:23334697 PMID:22407670 In alcohol plus RIT and LOP, alcohol synergistically increased the HIV drug-induced GRP78 and ratio of spliced sXbp1 to Xbp1. In addition, RIT and LOP inhibited protein expression of the Sarco/ER Calcium-ATPase (SERCA) which was further inhibited in the presence of alcohol. CYP2E1 was not significantly affected in response to any of these acute treatments. An increased alcohol exposure induces oxidative stress and/or hyperhomocysteinmia, which disturb SERCA further and exacerbate the HIV drug-induced ER stress leading to hepatic steatosis and fibrosis PMID:23334697 Ritonavir and lopinavir may also have effects on ER Ca2+ levels by inhibition of SERCA HOIP:HOIP_0003015 PMID:19444596 PMID:20587749 PMID:29142472 PMID:30254132 PMID:30396238 thapsigargin [ER stress] HOIP_0003015 PMID:19444596 Reduced endoplasmic reticulum luminal calcium links saturated fatty acid-mediated endoplasmic reticulum stress and cell death in liver cells. HOIP:HOIP_0003016 Negative regulation of endoplasmic reticulum-associated degradation is a subtype of negative regulation of protein catabolic process: A process that stops, prevents, or reduces the frequency, rate or extent of endoplasmic reticulum-associated degradation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. negative regulation of endoplasmic reticulum-associated degradation [ER stress] HOIP_0003016 HOIP:HOIP_0003017 Any process that stops, prevents or reduces the frequency, rate or extent of proteasomal protein catabolic process. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:19520899 negative regulation of proteasomal protein catabolic process [ER stress] HOIP_0003017 PMID:19520899 Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors (MG-132): a consequence of endoplasmic reticulum (ER) stress induction, activation of PERK and general control nonderepressible-2 eIF2alpha kinase (GCN2), and global translational shutoff. HOIP:HOIP_0003018 NCBI-Human-GeneID:10057 NCBI-Mouse-GeneID:27416 NCBI-Rat-GeneID:116721 ATP Binding Cassette Subfamily C Member 5 ATP-Binding Cassette, Sub-Family C (CFTR/MRP), Member 5 MRP5 Multi-Specific Organic Anion Transporter C Multidrug Resistance-Associated Protein 5 ABCC5 (mol) HOIP_0003018 NCBI-Human-GeneID:10057 http://www.ncbi.nlm.nih.gov/gene/10057 NCBI-Mouse-GeneID:27416 http://www.ncbi.nlm.nih.gov/gene/27416 NCBI-Rat-GeneID:116721 http://www.ncbi.nlm.nih.gov/gene/116721 HOIP:HOIP_0003019 NCBI-Human-GeneID:10257 NCBI-Mouse-GeneID:239273 NCBI-Rat-GeneID:170924 ATP Binding Cassette Subfamily C Member 4 ATP-Binding Cassette, Sub-Family C (CFTR/MRP), Member 4 MOATB MRP/CMOAT-Related ABC Transporter MRP4 Multidrug Resistance-Associated Protein 4 ABCC4 (mol) HOIP_0003019 NCBI-Human-GeneID:10257 http://www.ncbi.nlm.nih.gov/gene/10257 NCBI-Mouse-GeneID:239273 http://www.ncbi.nlm.nih.gov/gene/239273 NCBI-Rat-GeneID:170924 http://www.ncbi.nlm.nih.gov/gene/170924 HOIP:HOIP_0003020 PMID:19520899 MG-132 [ER stress] HOIP_0003020 PMID:19520899 Marked (approximately 4-fold) MG132 concentration-dependent PERK autophosphorylation, along with an 8-fold increase in eIF2alpha-phosphorylation was found. MG132 also activated GCN2 [general control nonderepressible-2 (EIF2AK4)] eIF2alpha kinase in a concentration-dependent manner, but not the heme-regulated inhibitor eIF2alpha kinase [(EIF2AK1)]. Pulse-chase, immunoprecipitation/immunoblotting analyses documented the consequently dramatic translational shutoff of total hepatic protein, including but not limited to CYP3A and tryptophan 2,3-dioxygenase protein syntheses. These findings reveal that at high concentrations, MG132 is indeed cytotoxic and can suppress CYP3A synthesis, a result confirmed by confocal immunofluorescence analyses of MG132-treated hepatocytes HOIP:HOIP_0003021 C19H25BN4O4 CC(C)C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)c1cnccn1)B(O)O PMID: 23877657 PMID: 28588081 PMID:29980790 Wikipedia:Bortezomib bortezomib [ER stress] HOIP_0003021 PMID: 28588081 Intercellular transmission of the unfolded protein response promotes survival and drug resistance in cancer cells. HOIP:HOIP_0003022 NCBI-Human-GeneID:5465 NCBI-Mouse-GeneID:19013 NCBI-Rat-GeneID:25747 Peroxisome Proliferator-Activated Receptor Alpha - inactivated[lipidosis] PPARA - inactivated (canonical)[lipidosis] HOIP_0003022 NCBI-Human-GeneID:5465 http://www.ncbi.nlm.nih.gov/gene/5465 NCBI-Mouse-GeneID:19013 http://www.ncbi.nlm.nih.gov/gene/19013 NCBI-Rat-GeneID:25747 http://www.ncbi.nlm.nih.gov/gene/25747 HOIP:HOIP_0003023 nelfinavir [ER stress] HOIP_0003023 HOIP:HOIP_0003024 PMID:18006837 PMID:23973637 atazanavir [ER stress] HOIP_0003024 PMID:18006837 HIV-1 protease inhibitors nelfinavir and atazanavir induce malignant glioma death by triggering endoplasmic reticulum stress. HOIP:HOIP_0003025 PMID:25501753 PMID:25901709 PMID:26546044 sorafenib [ER stress] HOIP_0003025 PMID:25501753 New therapeutic strategy for hepatocellular carcinoma by molecular targeting agents via inhibition of cellular stress defense mechanisms. PMID:25901709 RACK1 modulates apoptosis induced by sorafenib in HCC cells by interfering with the IRE1/XBP1 axis. PMID:26546044 Alpha-fetoprotein is a biomarker of unfolded protein response and altered proteostasis in hepatocellular carcinoma cells exposed to sorafenib. Sorafenib activated the Regulated Inositol-Requiring Enzyme-1α (IRE-1α) and the PKR-like ER Kinase (PERK)-dependent arms of the Unfolded Protein Response (UPR). The inhibition of IRE-1α partially restored the mRNA levels of AFP upon treatment with sorafenib. The inhibition of both pathways partially prevented the drop in the production of AFP induced by sorafenib. HOIP:HOIP_0003026 Intrinsic apoptosis signaling is a subtype of biological signaling: A process in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The process starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.). This process is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP). This entity is a specific course-dependent process. This process can constitute the course of apoptosis. Reactome:R-HSA-109606.3 intrinsic apotosis signaling[apoptosis (course)] HOIP_0003026 HOIP:HOIP_0003028 PMID:29438776 PMID:29457838 PMID:30538632 STF-083010 [ER stress] HOIP_0003028 PMID:29457838 Quercetin ameliorates HFD-induced NAFLD by promoting hepatic VLDL assembly and lipophagy via the IRE1a/XBP1s pathway. PMID:30538632 Hepatic MCP1, CTGF, P4HA1, Col1α1, and Mmp9, target genes of miR-122, were upregulated in CCl4-treated mice. Interestingly, STF-083010 reversed CCl4-induced hepatic miR-122 downregulation. STF-083010 inhibited CCl4-induced upregulation of miR-122 target genes. Therefore, STF-083010 alleviated CCl4-induced liver injury and thus protected against liver fibrosis associated with hepatic miR-122. HOIP:HOIP_0003030 Receiving abnormal protein signal by ATF6 is a subtype of receiving signal: A process that recognizes another object and changes into an abnormal protein (e.g., misfolded protein, etc.) signal by ATF6. This process is dependent on the apoptosis and can constitute the course of ER stress. receiving abnormal protein signal by ATF6 [ER stress - apoptosis] HOIP_0003030 HOIP:HOIP_0003031 Dissociation of ATF6:BIP heterodimer is a subtype of detaching: A process that disaggregates ATF6-BIP heterodimers into BIP and ATF6. This process is dependent on the apoptosis and can constitute the course of ER stress. Dissociation of ATF6-alpha:BIP Complex [ER stress - apoptosis] HOIP_0003031 HOIP:HOIP_0003032 ATF6 - stress sensor (canonical)[ER stress - apotosis] HOIP_0003032 HOIP:HOIP_0003033 Proapoptic gene regulation pathway by ATF6 is a subtype of ATF6 gene regulation pathway: Sequence of reactions to regulate genes which have a proapoptosis inducer role by ATF6. This process can constitute the course of ER stress. proapoptic gene regulation pathway by ATF6 [ER stress] HOIP_0003033 HOIP:HOIP_0003034 PMID:23334697 HSP90B1 - chaperone (canonical)[ER stress -Refolding [persist]] HOIP_0003034 PMID:23334697 Xenobiotic perturbation of ER stress and the unfolded protein response. HOIP:HOIP_0003035 ATF4 gene expression by eIF2a is a subtype of gene expression: The process in which a gene sequence is converted into a mature ATF4 gene product or products (proteins or RNA) by eIF2a. This process is dependent on the inflammation and can constitute the course of ER stress. Reactome:R-HSA-381128 http://www.ncbi.nlm.nih.gov/pubmed/18426796 ATF4 gene expression by eIF2a [ER stress - inflammation] HOIP_0003035 HOIP:HOIP_0003036 Inflammatiory gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the induction of inflammation by ATF4. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:26086088 PMID:27346803 PMID:28860159 inflammatory gene expression by ATF4 [ER stress] HOIP_0003036 PMID:26086088 Expression of NLRP1, a core inflammasome component, is specifically up-regulated during severe ER stress conditions in human cell lines. Both IRE1α and PERK, but not the ATF6 pathway, modulate NLRP1 gene expression. ATF4 transcription factor directly binds to NLRP1 promoter during ER stress. PMID:27346803 The PERK pathway has been shown to induce inflammation through the direct binding of ATF4 to the Il6 promoter PMID:28860159 ATF4 increases expression of inflammatory cytokines, including IL-6and monocyte chemoattractant protein-1 (MCP-1), by inducing transcription of the NACHT, LRR, and PYD domain-containing protein 1 (NLRP1), a core component of the inflammasome. I HOIP:HOIP_0003037 NCBI-Human-GeneID:3569 NCBI-Mouse-GeneID:16193 NCBI-Rat-GeneID:24498 IL-6 (canonical)[ER stress] HOIP_0003037 NCBI-Human-GeneID:3569 http://www.ncbi.nlm.nih.gov/gene/3569 NCBI-Mouse-GeneID:16193 http://www.ncbi.nlm.nih.gov/gene/16193 NCBI-Rat-GeneID:24498 http://www.ncbi.nlm.nih.gov/gene/24498 HOIP:HOIP_0003038 PMID:23990363 IL-6 - inflammatory cytokine (canonical)[ER stress - inflammation -ATF4 pathway] HOIP_0003038 PMID:23990363 Chronic inflammation is a molecular element of the metabolic syndrome and type 2 diabetes. Saturated fatty acids (SFAs) are considered to be an important proinflammatory factor. ATF 4, a transcription factor that is induced downstream of metabolic stresses including endoplasmic reticulum (ER) stress, plays critical roles in SFA-induced interleukin-6 (Il6) expression. ATF4 exerts its proinflammatory effects through at least two different mechanisms: ATF4 is involved in SFA-induced nuclear factor-κB activation; and ATF4 directly activates the Il6 promoter. HOIP:HOIP_0003039 NLRP1 is a inflammasome component NCBI-Human-GeneID:22861 PMID:22634126 PMID:25879280 PMID:27662089 NLRP1 (canonical)[ER stress] HOIP_0003039 NCBI-Human-GeneID:22861 http://www.ncbi.nlm.nih.gov/gene/22861 HOIP:HOIP_0003040 NLRP1 is a inflammasome component NLRP1・炎症関連分子＠＠炎症＠ERStress NLRP1 - inflammatory substance (canonical)[ER stress] HOIP_0003040 HOIP:HOIP_0003041 A role played by the entity that has inflammatory effects. inflammatory substance role HOIP_0003041 HOIP:HOIP_0003042 The totality of all processes through which a type2 diabetes instance is realized. type 2 diabetes course HOIP_0003042 HOIP:HOIP_0003043 Inflammatory cytokine gene expression via ATF4 is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA) via ATF4. This process is dependent on the inflammation and can constitute the course of ER stress. inflammatory cytokine gene expression via ATF4 [ER stress - inflammation] HOIP_0003043 HOIP:HOIP_0003044 ATF6-CREBPH-APR pathway is a subtype of ATF6 signaling (integrated pathway): Sequence of linked reactions, which has ATF6 signaling and gene regulation pathway. This process is dependent on positive inflammation and can constitute the course of ER stress. ATF6-CREBPH-APR pathway [ER stress - inflammation] HOIP_0003044 HOIP:HOIP_0003045 APR gene expression by ATF6. is a subtype of Gene expression by transcriptional regulator: The process in which the sequence of APR is converted into a mature gene product or products (proteins or RNA) by ATF6. This process is dependent on the ATF6-ARP mediated inflammation and can constitute the course of ER stress. PMID:16469704 PMID:23334697 APR gene expression by ATF6 [ER stress - inflammation - ATF6-ARP] HOIP_0003045 PMID:233334697 PMID:16469704 PMID:16469704 In this study,(1) expression of CREBH is liver specific and is induced by proinflammatory cytokines; (2) ER stress induces cleavage of CREBH to release an N-terminal fragment that traffics to the nucleus to activate transcription; (3) CREBH activation requires processing by Golgi-localized proteases S1P and S2P; (4) CREBH does not contribute to the classical UPR induction but is required for the APR by regulating transcription of the CRP and SAP genes; (5) CREBH and ATF6 bind to a conserved promoter element in the specific APR genes; (6) CREBH and ATF6 interact and synergistically activate transcription of target genes in hepatocytes upon ER stress; and (7) proinflammatory cytokines induce cleavage of CREBH and activate the APR and the UPR in the liver in vivo. HOIP:HOIP_0003046 ATF6 - transcriptional factor (canonical)[ER stress - inflammation] HOIP_0003046 HOIP:HOIP_0003047 ATF6 -APR transcriptional factor (canonical)[ER stress - inflammation -APR] HOIP_0003047 HOIP:HOIP_0003048 PMID:16469704 PMID:23317820 Acute Phase Response molecule [ER stress] APR gene (canonical)[ER stress] HOIP_0003048 PMID:16469704 CREBH and ATF6 activate transcription from the SAP (E) and CRP promoters. PMID:23317820 ER stress in hepatocytes, ATF6α and CREBH traffic to the Golgi to undergo S1P- and S2P–mediated cleavage; the cytosolic active transcription factors that are released induce the expression of APR genes, including those encoding C-reactive protein and serum amyloid P component HOIP:HOIP_0003049 GRP94 - chaperone (canonical)[proteinrefolding [persist]] HOIP_0003049 HOIP:HOIP_0003050 XBP1 - transcriptional regulator (canonical)[ER stress - Refolding -ATF6 pathway] HOIP_0003050 HOIP:HOIP_0003051 Refolding promotor is a role played by any substance that promotes the process of refolding. Yuki Y. 2018.08.31 refolding promoting factor role HOIP_0003051 HOIP:HOIP_0003052 Bipと結合、コシャペロンの働きをする NCBI-Human-GeneID:5611 NCBI-Mouse-GeneID:100037258 NCBI-Rat-GeneID:63880 http://omim.org/entry/601184 ERdj6 [ER stress] p58IPK [ER stress] DNAJC3 (canonical)[ER stress] HOIP_0003052 NCBI-Human-GeneID:5611 http://www.ncbi.nlm.nih.gov/gene/5611 NCBI-Mouse-GeneID:100037258 http://www.ncbi.nlm.nih.gov/gene/100037258 NCBI-Rat-GeneID:63880 http://www.ncbi.nlm.nih.gov/gene/63880 HOIP:HOIP_0003053 p58IPK [ER stress] DNAJC3 -cochaperone (canonical)[ER stress -Refolding [persist]] HOIP_0003053 HOIP:HOIP_0003054 ATF4 gene expression by eIF2a is a subtype of gene expression: The process in which a gene sequence is converted into a mature ATF4 gene product or products (proteins or RNA) by eIF2a. This process is dependent on the retranslation process and can constitute the course of ER stress. PMID:23334697 Reactome:R-HSA-381128 http://www.ncbi.nlm.nih.gov/pubmed/18426796 ATF4 gene expression by eIF2a [ER stress - translation] HOIP_0003054 PMID:23334697 Under conditions of eIF2α phosphorylation, a subset of mRNAs with small upstream open reading frames (such as activating transcription factor 4 [ATF4]) or internal ribosome entry sites are preferentially translated. ATF4 is a bZIP transcription factor that controls the regulation of expression of pro-survival UPR-target genes (e.g., the chaperones glucose regulated protein [GRP]78 and GRP94) as well as genes involved in other functions such as redox homeostasis, amino acid metabolism, apoptosis, and autophagy. HOIP:HOIP_0003055 ATF4 - transcriptional regulator (canonical)[ER stress - translation] HOIP_0003055 HOIP:HOIP_0003056 Tranlation promotion gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the translation promotion by ATF4. This process is dependent on the retranslation process and can constitute the course of ER stress. PMID:11564868 PMID:27346803 tranlation promotion gene expression by ATF4 [ER stress] HOIP_0003056 PMID:27346803 Perk->eIF2a-> translation attenuation Perk -> eIF2a->ATF4->GADD34 expression->eIF2a inactivation (dephosphorylation) by GADD34-> restoring translation GAA34 is a regulatory subunit of protein posphatase 1 (PP1). HOIP:HOIP_0003057 GADD34 gene expression by ATF4 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence of GADD34 is converted into a mature gene product or products (proteins or RNA) by ATF4. This process is dependent on the retranslation process and can constitute the course of ER stress. PMID:27346803 GADD34 gene expression by ATF4 [ER stress] HOIP_0003057 HOIP:HOIP_0003058 PERK-eIF2a-ATF4 mediated pathway is a subtype of PERK-eIF2a signaling: Sequence of linked reactions, which has PERK-eIF2a signaling and GADD34 gene regulation by ATF4. This pathway is dependent on the retranslation and can constitute the course of ER stress. PERK-ATF4-GADD34 signaling [ER stress - retranslation] HOIP_0003058 HOIP:HOIP_0003059 A process in which a signal to eIF2a is transduced by PERK. This process is dependent on the translation and can constitute the course of ER stress. PERK signaling to eIF2a [ER stress - translation] HOIP_0003059 HOIP:HOIP_0003061 A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with a ligand binding to a death domain receptor on the cell surface, and ends when the execution phase of apoptosis is triggered. This pathway is a specific course-dependent and can constitute the course of apoptosis. PMID:21525013 extrinsic apoptotic signaling pathway via death domain receptors [apoptosis (course)] HOIP_0003061 PMID:21525013 Gene products that may be annotated to this term include: 1) ligands such as FASL; 2) receptors such as FAS/CD95 (though care should be taken because FAS can also act as a non-apoptotic signal transducer); 3) signaling molecules such as FADD (FAS-associated protein with a death domain), cIAPs (cellular inhibitor of apoptosis proteins), c-FLIPs and caspases 8 and 10. Examples are TWEAK (TNF12) and FN14 (TNFRSF12A) (UniProt symbols O43508 and Q9NP84) HOIP:HOIP_0003062 NCBI-Human-GeneID:7076 NCBI-Mouse-GeneID:21857 NCBI-Rat-GeneID:116510 TIMP1 (canonical)[Fibrosis] HOIP_0003062 NCBI-Human-GeneID:7076 http://www.ncbi.nlm.nih.gov/gene/7076 NCBI-Mouse-GeneID:21857 http://www.ncbi.nlm.nih.gov/gene/21857 NCBI-Rat-GeneID:116510 http://www.ncbi.nlm.nih.gov/gene/116510 HOIP:HOIP_0003063 ATF6 processing is a subtype of protein processing: A process that ATF6 maturation process achieved by the cleavage of a peptide bond or bonds within ATF6 protein. ATF6 processing HOIP_0003063 HOIP:HOIP_0003064 IRE1 autophosphorylation is a subtype of protein autophosphorylation: The phosphorylation by IRE1 of one or more of its own amino acid residues (cis-autophosphorylation), or residues on IRE1 (trans-autophosphorylation). This entity is a specific course-dependent process. This process is dependent on RODD and can constitute the course of ER stress. IRE1 autophosphorylation [ER stress - RIDD] HOIP_0003064 HOIP:HOIP_0003065 Inflammatory gene expression by XBP1 is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the inflammation by XBP1. This process is dependent on the inflammation and can constitute the course of ER stress. PMID:27346803 inflammatory gene expression by XBP1 [ER stress - inflammation] HOIP_0003065 PMID:27347803 HOIP:HOIP_0003066 XBP1 - transcriptional regulator (canonical)[ER stress - inflammation] HOIP_0003066 HOIP:HOIP_0003067 PMID:23990363 IL-6 - inflammatory cytokine (canonical)[ER stress - inflammation -XBP1 pathway] HOIP_0003067 PMID:23990363 Chronic inflammation is a molecular element of the metabolic syndrome and type 2 diabetes. Saturated fatty acids (SFAs) are considered to be an important proinflammatory factor. ATF 4, a transcription factor that is induced downstream of metabolic stresses including endoplasmic reticulum (ER) stress, plays critical roles in SFA-induced interleukin-6 (Il6) expression. ATF4 exerts its proinflammatory effects through at least two different mechanisms: ATF4 is involved in SFA-induced nuclear factor-κB activation; and ATF4 directly activates the Il6 promoter. HOIP:HOIP_0003068 ARP related gene expression via ATF6 is a subtype of gene expression: The process in which a gene sequence is converted into a mature ARP gene product or products (proteins or RNA) ia ATF6. This entity is a specific course-dependent process. This process can constitute the course of ER stress. ARP related gene expression via ATF6 [ER stress] HOIP_0003068 HOIP:HOIP_0003069 NCBI-Human-GeneID:1401 NCBI-Mouse-GeneID:12944 NCBI-Rat-GeneID:25419 https://omim.org/entry/123260 https://www.ncbi.nlm.nih.gov/gene/1401 C-reactive protein [ER stress] PTX1 [ER stress] CRP (canonical)[ER stress] HOIP_0003069 NCBI-Human-GeneID:1401 http://www.ncbi.nlm.nih.gov/gene/1401 NCBI-Mouse-GeneID:12944 http://www.ncbi.nlm.nih.gov/gene/12944 NCBI-Rat-GeneID:25419 http://www.ncbi.nlm.nih.gov/gene/25419 HOIP:HOIP_0003070 C-reactive protein C-reactive protein - inflammatory substance [ER stress] CRP - inflammatory substance (canonical)[ER stress] HOIP_0003070 HOIP:HOIP_0003071 ARP related gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature ARP gene product or products (proteins or RNA) by PERK. ARP related gene expression HOIP_0003071 HOIP:HOIP_0003072 ATF6 signaling is a process that a signal is transmitted by the ATF6 (activating transcription factor 6). ATF6 generally plays a endoplasmic reticulum membrane stress sensor role. This process is dependent on the ATF6-ARP mediated inflammation and can constitute the course of ER stress. PMID:16469704 ATF6 signaling [ER stress - inflammation - ATF6-ARP] HOIP_0003072 HOIP:HOIP_0003073 ATF6 activation is a subtype of molecular activation: A process that changes the activity of the ATF6 (Activating Transcription Factor 6) to be higher. This process is dependent on the ARP mediated inflammation and can constitute the course of ER stress. ATF6 activation [ER stress - inflammation - ARP] HOIP_0003073 HOIP:HOIP_0003074 ATF6 processing is a subtype of protein processing: A process that ATF6 maturation process achieved by the cleavage of a peptide bond or bonds within ATF6 protein. This process is dependent on the inflammation and can constitute the course of ER stress. ATF6 processing [ER stress - inflammation] HOIP_0003074 HOIP:HOIP_0003075 Cleavage of CREB by S1P is a subtype of proteolysis: A process in which CREB is cleaved by endopeptidase S1P( MBTPS1). This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:27346803 cleavage of CREB by S1P [ER stress] HOIP_0003075 HOIP:HOIP_0003076 Cleavage of CREB by S1P is a subtype of proteolysis: A process in which CREB is cleaved by endopeptidase S1P( MBTPS1). cleavage of CREB by S1P HOIP_0003076 HOIP:HOIP_0003077 Cleavage of CREB by S2P is a subtype of proteolysis: A process in which CREB is cleaved by endopeptidase S2P( MBTPS2). Site-2 cleavage comes after site-1 cleavage cleavage of CREB by S2P HOIP_0003077 HOIP:HOIP_0003078 Cleavage of CREB by S2P is a subtype of proteolysis: A process in which CREB is cleaved by endopeptidase S2P( MBTPS2). Site-2 cleavage comes after site-1 cleavage This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:10564271 PMID:11163209 PMID:15299016 Reactome:R-HSA-420818 http://purl.obolibrary.org/obo/HINO_0008876 cleavage of CREB by S2P [ER stress] HOIP_0003078 HOIP:HOIP_0003079 CERB processing is a subtype of protein processing: CREB maturation process achieved by the cleavage of a peptide bond or bonds within CREB protein. This process is dependent on the ARP mediated inflammation and can constitute the course of ER stress. CERB processing [ER stress - inflammation -ARP] HOIP_0003079 HOIP:HOIP_0003080 CREB3L3 activation is a subtype of molecular activation: A process that changes the activity of the CREBL3 to be higher. This process is dependent on the rinflammation and can constitute the course of ER stress. PMID:16469704 CREB3L3 activation [ER stress - inflammation - ARP] HOIP_0003080 HOIP:HOIP_0003081 CREB3L3 signaling is a subtype of signaling that a signal is transmitted by CREB3L3. This entity is a specific course-dependent process. This process can constitute the course of ER stress. CREB3L3 signaling [ER stress - inflammation] HOIP_0003081 HOIP:HOIP_0003082 CRBPH (canonical)[ER stress] HOIP_0003082 HOIP:HOIP_0003083 CREBPH - signaling factor (canonical)[ER stress - inflammation] HOIP_0003083 HOIP:HOIP_0003084 ARP gene regulation pathway by ATF6 is a subtype of ATF6 gene regulation pathway: Sequence of reactions to regulate acute response protein (ARP) genes by ATF6. This process can constitute the course of ER stress. ARP gene regulation pathway by ATF6 [ER stress] HOIP_0003084 HOIP:HOIP_0003085 Creb3l3 PMID:16469704 CREBPH -APR transcriptional factor (canonical)[ER stress - inflammation -APR] HOIP_0003085 HOIP:HOIP_0003086 NCBI-Human-GeneID:325 NCBI-Mouse-GeneID:20219 NCBI-Rat-GeneID:29339 https://omim.org/entry/104770 APCS [ER stress] serum amyloid P-component [ER stress] SAP (canonical)[ER stress] HOIP_0003086 NCBI-Human-GeneID:325 http://www.ncbi.nlm.nih.gov/gene/325 NCBI-Mouse-GeneID:20219 http://www.ncbi.nlm.nih.gov/gene/20219 NCBI-Rat-GeneID:29339 http://www.ncbi.nlm.nih.gov/gene/29339 HOIP:HOIP_0003087 serum amyloid P-component - inflammatory factor [ER stress] SAP - inflammatory factor (canonical)[ER stress] HOIP_0003087 HOIP:HOIP_0003088 IRE1 - autophosphorylation kinase (canonical)[ER stress -RIDD] HOIP_0003088 HOIP:HOIP_0003089 IRE1 dimerization is a subtype of protein dimerization: The formation of a IRE1 dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. This entity is a specific course-dependent process. This process is dependent on RIDD and can constitute the course of ER stress. PMID:11897784 PMID:23236464 Reactome:R-HSA-381109 IRE1 dimerization [ER stress - RIDD] HOIP_0003089 HOIP:HOIP_0003090 IRE1 dimer (canonical)[ER stress -RIDD] HOIP_0003090 HOIP:HOIP_0003091 Caspase 12 signaling is a process that a signal is transmitted by the caspase 12. This process is dependent on the apoptosis and can constitute the course of ER stress. caspase 12 signaling [ER stress - apoptosis] HOIP_0003091 HOIP:HOIP_0003092 Caspase 4 signaling is a process that a signal is transmitted by the caspase 4. This process is dependent on the apoptosis and can constitute the course of ER stress. ミトコンドリア(intrinsic)と独立のパスウェイ caspase 4 signaling [ER stress - apoptosis] HOIP_0003092 HOIP:HOIP_0003093 Caspase-12 activation is a subtype of caspase activation: A process that changes the activity of the caspase-12, intracellular cysteine endopeptidase family members, to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:11278723 caspase-12 activation [ER stress] HOIP_0003093 HOIP:HOIP_0003094 Caspase-4 activation is a subtype of caspase activation: A process that changes the activity of the caspase-4, intracellular cysteine endopeptidase family members, to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. caspase-4 activation [ER stress] HOIP_0003094 PMID:23334697 HOIP:HOIP_0003095 Caspase activation is a subtype of molecular activation: A process that changes the activity of the caspase, intracellular cysteine endopeptidase family members, to be higher. caspase activation HOIP_0003095 HOIP:HOIP_0003096 Caspase-9 activation is a subtype of caspase activation: A process that changes the activity of the caspase-9, intracellular cysteine endopeptidase family members, to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. caspase-9 activation [ER stress] HOIP_0003096 PMID:23334697 HOIP:HOIP_0003097 Caspase-3 activation is a subtype of caspase activation: A process that changes the activity of the caspase-3, intracellular cysteine endopeptidase family members, to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:29335519 caspase-3 activation [ER stress] HOIP_0003097 PMID:29335519 Expression of catalytic inactive PCK1(C288S) mutant reduced, but not completely inhibited the cleavage of caspase-3.  HOIP:HOIP_0003098 Caspase-3 activation is a subtype of caspase activation: A process that changes the activity of the caspase-3, intracellular cysteine endopeptidase family members, to be higher. caspase-3 activation HOIP_0003098 HOIP:HOIP_0003099 Caspase-9 activation is a subtype of caspase activation: A process that changes the activity of the caspase-9, intracellular cysteine endopeptidase family members, to be higher. caspase-9 activation HOIP_0003099 HOIP:HOIP_0003100 Caspase-12 activation is a subtype of caspase activation: A process that changes the activity of the caspase-12, intracellular cysteine endopeptidase family members, to be higher. caspase-12 activation HOIP_0003100 HOIP:HOIP_0003101 Caspase-4 activation is a subtype of caspase activation: A process that changes the activity of the caspase-4, intracellular cysteine endopeptidase family members, to be higher. caspase-4 activation HOIP_0003101 HOIP:HOIP_0003102 A series of molecular signals mediated by Caspase family. This pathway is a specific course-dependent and can constitute the course of ER stress. This pathway is dependent on the apoptosis and can constitute the course of ER stress. caspase pathway [ER stress - apoptosis] HOIP_0003102 HOIP:HOIP_0003103 Caspase 9 signaling is a process that a signal is transmitted by the caspase 9. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:19737514 PMID:23334697 caspase 9 signaling [ER stress - apoptosis] HOIP_0003103 HOIP:HOIP_0003104 Caspase 3 signaling is a process that a signal is transmitted by the caspase 3. This process is dependent on the apoptosis and can constitute the course of ER stress. PMID:19737514 caspase 3 signaling [ER stress - apoptosis] HOIP_0003104 HOIP:HOIP_0003105 The process that results in the movement of cytochrome c from the mitochondrial intermembrane space into the cytosol, which is part of the apoptotic signaling pathway and leads to caspase activation. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Permeabilization of the outer mitochondrial membrane by pro-apoptotic BCL2 family proteins, such as BAK and BAX, allows cytochrome c eflux from the mitochondrial intermembrane space into the cytosol (Arnoult et al. 2003). ミトコンドリアから細胞質へチトクロームcが放出、Apaf-1に結合し、Apaf複合体形成。チトクロームc/Apaf-1複合体はカスパーゼ9を活性化、次にカスパーゼ3を活性化、アポトーシスが起こる。 Reactome:R-HSA-114284 release of cytochrome c from mitochondria [ER stress] HOIP_0003105 HOIP:HOIP_0003106 BAK activation is a subtype of molecular activation: A process that changes the activity of the BAK1 (BCL2 Antagonist/Killer 1), BCL-2 family, to be higher. BAK activation HOIP_0003106 HOIP:HOIP_0003107 BAK activation is a subtype of molecular activation: A process that changes the activity of the BAK1 (BCL2 Antagonist/Killer 1), BCL-2 family, to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:23334697 BAK activation [ER stress] HOIP_0003107 PMID:23334697 HOIP:HOIP_0003108 BAX activation is a subtype of molecular activation: A process that changes the activity of the BAX (BCL2 Associated X, Apoptosis Regulator), BCL-2 family, to be higher. BAX activation HOIP_0003108 HOIP:HOIP_0003109 BAX activation is a subtype of molecular activation: A process that changes the activity of the BAX (BCL2 Associated X, Apoptosis Regulator), BCL-2 family, to be higher. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:23334697 BAX activation [ER stress] HOIP_0003109 HOIP:HOIP_0003110 The aggregation, arrangement and bonding together of the apoptosome, a multisubunit protein complex involved in the signaling phase of the apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Apoptosome formation in cytosol apoptosome assembly [ER stress] HOIP_0003110 HOIP:HOIP_0003111 A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP). This pathway is a specific course-dependent and can constitute the course of apoptosis. Reactome:Id: R-HSA-109606.3 intrinsic apoptotic signaling pathway [apoptosis (course)] HOIP_0003111 Reactome:Id: R-HSA-109606.3 https://reactome.org/PathwayBrowser/#/R-HSA-109606&PATH=R-HSA-5357801,R-HSA-109581 HOIP:HOIP_0003112 Preventing is a type of functioning process of meta-function of "ToPrevent". Two meta-functions "ToAllow" and "ToPrevent" are concerned with the undesirable side effects of functions. A function fa having positive effects on the side effect of a function ft1 is said to have a meta-function “to allow the side-effects of ft1”. The “undesirable side effect” is defined in a relation with another function ft2 or the whole system. The “positive effect” means such a causal relation that increase of the focused attribute of fa causes decrease of the side effect. If a serious trouble (e.g., faults) will be caused in a function ft2 when a function fa is not achieved, function fa is said to have a meta-function “to prevent malfunction of ft2”. For example, the “to super-heat” function of the boiler prevents malfunction of the turbine, because the steam of low temperature would damage the turbine blade by water particles. For almost all fa performing a ToAllow meta-function for ft1, in general, there exists a ToPrevent meta-function for another function ft2. allowing HOIP_0003112 HOIP:HOIP_0003113 Bax/Bak complex formation is a subtype of protein complex assembly: A process that forms a complex consisting of BAX/BAK, a member of the Bcl-2 family. This entity is a specific course-dependent process. This process can constitute the course of ER stress. BAX and BAK homo-oligomerize at the ER membrane, leading to its permeabilization and the release of ER luminal proteins to the cytosol. BAX and BAK homo-oligomerize at the ER membrane, leading to its permeabilization and the release of ER luminal proteins to the cytosol. BAX/BAK formed a protein complex with the cytosolic domain of IRE1alpha that was essential for IRE1alpha activation. Thus, BAX and BAK function at the ER membrane to activate IRE1alpha signaling and to provide a physical link between members of the core apoptotic pathway and the UPR. BAX/BAK formed a protein complex with the cytosolic domain of IRE1alpha that was essential for IRE1alpha activation. Thus, BAX and BAK function at the ER membrane to activate IRE1alpha signaling and to provide a physical link between members of the core apoptotic pathway and the UPR. Mitochondrial cytochrome c release can also be mediated by BAK and BAX which oligomerize and form a pore in the outer mitochondrial membrane, given the appropriate pro-apoptotic signals. BAX and BAK can also insert into the ER membrane to mediate Ca2+ release into the cytosol activating calpains. Mitochondrial cytochrome c release can also be mediated by BAK and BAX which oligomerize and form a pore in the outer mitochondrial membrane, given the appropriate pro-apoptotic signals. BAX and BAK can also insert into the ER membrane to mediate Ca2+ release into the cytosol activating calpains. PMID:29472455 Bax/Bak complex formation [ER stress] HOIP_0003113 BAX and BAK homo-oligomerize at the ER membrane, leading to its permeabilization and the release of ER luminal proteins to the cytosol. PMID:28622296 BAX/BAK formed a protein complex with the cytosolic domain of IRE1alpha that was essential for IRE1alpha activation. Thus, BAX and BAK function at the ER membrane to activate IRE1alpha signaling and to provide a physical link between members of the core apoptotic pathway and the UPR. PMID:16645094 Mitochondrial cytochrome c release can also be mediated by BAK and BAX which oligomerize and form a pore in the outer mitochondrial membrane, given the appropriate pro-apoptotic signals. BAX and BAK can also insert into the ER membrane to mediate Ca2+ release into the cytosol activating calpains. PMID:23334697 HOIP:HOIP_0003114 Bax-Bak complex formation is a subtype of protein complex assembly: A process that forms a complex consisting of BAX/BAK, a member of the Bcl-2 family. Bax-Bak complex formation HOIP_0003114 HOIP:HOIP_0003116 Positive regulation of gene expression via JNK signaling is a subtype of positive regulation of gene expression: A process that that activates or increases the frequency, rate or extent of gene expression via JNK signaling. positive regulation of gene expression via JNK signaling HOIP_0003116 HOIP:HOIP_0003117 Binding to bile canaliculus membrane transporter by drug is a subtype of protein binding: Interacting process with the membrane transporter of bile canaliculus by the drug. binding to bile canaliculus membrane transporter by drug HOIP_0003117 HOIP:HOIP_0003119 NCBI-Human-GeneID:9971 NCBI-Mouse-GeneID:20186 NCBI-Rat-GeneID:60351 PMID:30013008 FXR (mol) HOIP_0003119 NCBI-Human-GeneID:9971 http://www.ncbi.nlm.nih.gov/gene/9971 NCBI-Mouse-GeneID:20186 http://www.ncbi.nlm.nih.gov/gene/20186 NCBI-Rat-GeneID:60351 http://www.ncbi.nlm.nih.gov/gene/60351 HOIP:HOIP_0003120 NCBI-Human-GeneID:8856 NCBI-Mouse-GeneID:18171 NCBI-Rat-GeneID:84385 PXR (mol) HOIP_0003120 NCBI-Human-GeneID:8856 http://www.ncbi.nlm.nih.gov/gene/8856 NCBI-Mouse-GeneID:18171 http://www.ncbi.nlm.nih.gov/gene/18171 NCBI-Rat-GeneID:84385 http://www.ncbi.nlm.nih.gov/gene/84385 HOIP:HOIP_0003121 NCBI-Human-GeneID:2908 NCBI-Mouse-GeneID:14815 NCBI-Rat-GeneID:24413 http://omim.org/entry/138040 GR (mol) HOIP_0003121 NCBI-Human-GeneID:2908 http://www.ncbi.nlm.nih.gov/gene/2908 NCBI-Mouse-GeneID:14815 http://www.ncbi.nlm.nih.gov/gene/14815 NCBI-Rat-GeneID:24413 http://www.ncbi.nlm.nih.gov/gene/24413 HOIP:HOIP_0003122 Back-flow is a subtype of changing direction: A process that changes the flow to the opposite direction. back-flow HOIP_0003122 HOIP:HOIP_0003123 BAK activation is a subtype of molecular activation: A process that changes the activity of the BAK1 (BCL2 Antagonist/Killer 1), BCL-2 family, to be higher. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. BAK activation [apoptosis (course)] HOIP_0003123 HOIP:HOIP_0003124 Import substances into hepatocyte vascular side (sinusoidal side) membrane is a subtype of transport: A process of the directed movement of substances into hepatocyte vascular side (sinusoidal side) membrane. import substances into hepatocyte vascular side (sinusoidal side) membrane HOIP_0003124 HOIP:HOIP_0003126 Negative regularuion of bile acid and bile salt transport is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of a bile acid and bile salts transport . negative regularuion of bile acid and bile salt transport HOIP_0003126 HOIP:HOIP_0003128 CAS:7723-14-0 Inchikey:OAICVXFJPJFONN-UHFFFAOYSA-N phosphorus phosphorus atom HOIP_0003128 HOIP:HOIP_0003129 Contraction is a subtype of generating motion: A process that generates the directed movement in which the object decreases in volume. contraction HOIP_0003129 HOIP:HOIP_0003130 Bile accumulation is a subtype of accumulation of substances in a biological object: A process that keeps bile within the liver (intrahepatic), or outside the liver (extrahepatic) in the bile duct system. bile accumulation HOIP_0003130 HOIP:HOIP_0003138 Regulation of transporter gene expression by cytokine is a subtype of regulation of transporter gene expression: A process that changes the the gene expression level of the transporter by cytokines. IL-1beta, TNF-alpha or IL-6 alters human hepatic transporters expression. Bile salt transporters as well as sinusoidal solute carrier transporters are usually repressed, whereas ATP-binding cassette drug efflux pumps remain unchanged or are either downregulated or upregulated. They maight alter drug pharmacokinetics, impairment of bile salt secretion and cholestasis caused by inflammation in humans. IL-1beta, TNF-alpha or IL-6 alters human hepatic transporters expression. Bile salt transporters as well as sinusoidal solute carrier transporters are usually repressed, whereas ATP-binding cassette drug efflux pumps remain unchanged or are either downregulated or upregulated. They maight alter drug pharmacokinetics, impairment of bile salt secretion and cholestasis caused by inflammation in humans. regulation of transporter gene expression by cytokine HOIP_0003138 IL-1beta, TNF-alpha or IL-6 alters human hepatic transporters expression. Bile salt transporters as well as sinusoidal solute carrier transporters are usually repressed, whereas ATP-binding cassette drug efflux pumps remain unchanged or are either downregulated or upregulated. They maight alter drug pharmacokinetics, impairment of bile salt secretion and cholestasis caused by inflammation in humans. PMID:19785515 HOIP:HOIP_0003139 Regulation of transporter gene expression is a subtype of regulation of gene expression: A process that changes the the gene expression level of the transporter. regulation of transporter gene expression HOIP_0003139 HOIP:HOIP_0003140 Decreasing bile acid production level is a subtype of decreasing quantity: A process that changes the production amount of bile acid to be lower. decreasing bile acid production level HOIP_0003140 HOIP:HOIP_0003141 Bile thrombus formation is a subtype of biological structure formation: A process that constructs bile thrombus. bile thrombus formation HOIP_0003141 HOIP:HOIP_0003142 Bile thrombus formation in bile canaliculus is a subtype of bile thrombus formation: A process that constructs bile thrombus in bile canaliculus. bile thrombus formation in bile canaliculus HOIP_0003142 HOIP:HOIP_0003143 Farnesoid X receptor activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating FxR (farnesoid X receptor) with a nuclear receptor role to be higher. Farnesoid X Receptor activation FxR activating activating FXR farnesoid X receptor activation HOIP_0003143 HOIP:HOIP_0003144 Increasing materials for bile formation is a subtype of increasing quantity: A process that changes the amount of bile formation material to be higher. increasing materials for bile formation HOIP_0003144 HOIP:HOIP_0003145 Farnesoid X Receptor Pathway is a subtype of gene regulation pathway: Sequence of reactions to regulate genes by nuclear receptor Farnesoid X Receptor. http://www.wikipathways.org/index.php/Pathway:WP2879 Farnesoid X Receptor Pathway HOIP_0003145 HOIP:HOIP_0003146 Gene expression by farnesoid X receptor is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) by Farnesoid X receptor (FXR). gene expression by FXR gene expression by farnesoid X receptor HOIP_0003146 HOIP:HOIP_0003149 Farnesoid X Receptor Pathway is a subtype of gene regulation pathway: Sequence of reactions to regulate genes by nuclear receptor Farnesoid X Receptor. This entity is a specific course-dependent process. This process can constitute the course of cholestasis. Farnesoid X receptor (FXR, a.k.a. NR1H4) is a nuclear receptor that responds to levels of bile acids present in the body and regulates many processes related to bile acids synthesis and transport. http://www.wikipathways.org/index.php/Pathway:WP2879 Farnesoid X Receptor Pathway [cholestasis] HOIP_0003149 HOIP:HOIP_0003150 Acumulation of bile pigment in hepatocyte is a subtype of bile pigment deposition: The aggregation of bile pigmentin a particular location in a hepatocyte. acumulation of bile pigment in hepatocyte HOIP_0003150 HOIP:HOIP_0003151 Increasing glutathione is a subtype of increasing quantity: A process that changes the amount of glutathione to be higher. increasing glutathione HOIP_0003151 HOIP:HOIP_0003152 Excretion of drug metabolite from hepatocyte to bile tube is a subtype of compound excretion: A process that excretes the drug metabolite from the hepatocyte to to the bile tube. excretion of drug metabolite from hepatocyte to bile tube HOIP_0003152 HOIP:HOIP_0003153 Drug export from the hepatocyte to to bile tube is a subtype of compound excretion: A process that excretes the drug from the hepatocyte to the bile tube. drug export from the hepatocyte to to bile tube HOIP_0003153 HOIP:HOIP_0003155 Negative regulation of contractile movement of bile canaliculus is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of contractile movement of bile canaliculus. negative regulation of contractile movement of bile canaliculus HOIP_0003155 HOIP:HOIP_0003156 A role played by a process that consitutes the course. constituent of course HOIP_0003156 HOIP:HOIP_0003157 Bip-unfolded protein is a subtype of a molecular complex. This entity has sub-parts of molecules: BIP/GRP78, and an unfolded protein. This entity is dependent on ER stress. http://purl.obolibrary.org/obo/HINO_0017506 https://identifiers.org/reactome:R-HSA-381062 Bip-unfolded protein complex [ER stress] HOIP_0003157 HOIP:HOIP_0003158 catenin HOIP_0003158 HOIP:HOIP_0003159 A role played by the entity which regulates the process of cell proliferation. regulator of cell proliferation HOIP_0003159 HOIP:HOIP_0003160 Hypofunction of glycogen degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient glycogen degradation. hypofunction of glycogen degradation HOIP_0003160 HOIP:HOIP_0003161 A role played by the entity which enables the facilitated diffusion of a calcium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism. IMR:0000499 (obsolete) related molecular function GO:0005262 calcium channel HOIP_0003161 HOIP:HOIP_0003162 NCBI-Human-GeneID:3725 NCBI-Mouse-GeneID:16476 NCBI-Rat-GeneID:24516 PMID:14967141 PMID:18931691 JUN (canonical)[glutathione depletion (course)] HOIP_0003162 NCBI-Human-GeneID:3725 http://www.ncbi.nlm.nih.gov/gene/3725 NCBI-Mouse-GeneID:16476 http://www.ncbi.nlm.nih.gov/gene/16476 NCBI-Rat-GeneID:24516 http://www.ncbi.nlm.nih.gov/gene/24516 PMID:14967141 JNK suppresses apoptosis via phosphorylation of the proapoptotic Bcl-2 family protein BAD. PMID:18931691 JNK can promote apoptosis by two distinct mechanisms. In the first mechanism targeted at the nuclear events, activated JNK translocates to the nucleus and transactivates c-Jun and other target transcription factors (TF). JNK can promote apoptosis by increasing the expression of pro-apoptotic genes through the transactivation of c-Jun/AP1-dependent or p53/73 protein-dependent mechanisms HOIP:HOIP_0003163 Activation and oligomerization of BAK protein is a subtype of molecular subpathway. This entity is a specific course-dependent process. This process can constitute the course of cell death. Mitochondrial cytochrome c release can also be mediated by BAK and BAX which oligomerize and form a pore in the outer mitochondrial membrane, given the appropriate pro-apoptotic signals. BAX and BAK can also insert into the ER membrane to mediate Ca2+ release into the cytosol activating calpains. Mitochondrial cytochrome c release can also be mediated by BAK and BAX which oligomerize and form a pore in the outer mitochondrial membrane, given the appropriate pro-apoptotic signals. BAX and BAK can also insert into the ER membrane to mediate Ca2+ release into the cytosol activating calpains. Reactome:R-HSA-114294.2 tBID binds to its mitochondrial partner BAK to release cytochrome c. Activated tBID results in an allosteric activation of BAK. This may induce its intramembranous oligomerization into a pore for cytochrome c efflux. PMID:29472455 Activation and oligomerization of BAK protein [cell death (course)] HOIP_0003163 Mitochondrial cytochrome c release can also be mediated by BAK and BAX which oligomerize and form a pore in the outer mitochondrial membrane, given the appropriate pro-apoptotic signals. BAX and BAK can also insert into the ER membrane to mediate Ca2+ release into the cytosol activating calpains. PMID:23334697 HOIP:HOIP_0003164 A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides. CHEBI:16856 5-L-Glutamyl-L-cysteinylglycine GSH L-Glutathione Reduced glutathione GLUTATHIONE (canonical)[glutathione depletion (course)] HOIP_0003164 HOIP:HOIP_0003165 GSHC [glutathione depletion (course)] GSHPx-1 [glutathione depletion (course)] Glutathione peroxidase 1 [glutathione depletion (course)] glutathione peroxidase monomer GLUTATHIONE peroxidase (canonical)[glutathione depletion (course)] HOIP_0003165 HOIP:HOIP_0003166 NCBI-Human-GeneID:836 NCBI-Mouse-GeneID:12367 NCBI-Rat-GeneID:25402 CASPASE 3 (canonical)[glutathione depletion (course)] HOIP_0003166 NCBI-Human-GeneID:836 http://www.ncbi.nlm.nih.gov/gene/836 NCBI-Mouse-GeneID:12367 http://www.ncbi.nlm.nih.gov/gene/12367 NCBI-Rat-GeneID:25402 http://www.ncbi.nlm.nih.gov/gene/25402 HOIP:HOIP_0003167 NFKB (canonical)[glutathione depletion (course)] HOIP_0003167 HOIP:HOIP_0003168 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. inflammatory response [glutathione depletion (course)] HOIP_0003168 HOIP:HOIP_0003169 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hepatic fibrosis [glutathione depletion (course)] HOIP_0003169 HOIP:HOIP_0003170 NCBI-Human-GeneID:1571 NCBI-Mouse-GeneID:13106 NCBI-Rat-GeneID:25086 PMID:21177773 CYP2E1 (canonical)[glutathione depletion (course)] HOIP_0003170 NCBI-Human-GeneID:1571 http://www.ncbi.nlm.nih.gov/gene/1571 NCBI-Mouse-GeneID:13106 http://www.ncbi.nlm.nih.gov/gene/13106 NCBI-Rat-GeneID:25086 http://www.ncbi.nlm.nih.gov/gene/25086 PMID:21177773 Cytochrome P450 (CYP) enzymes, including CYP2E1, CYP1A2, and CYP3A4, convert 5–9% of acetaminophen to a highly reactive metabolite, N-acetyl-p-benzoquinonimine (NAPQI) (Corcoran et al., 1980; Dahlin et al., 1984). HOIP:HOIP_0003171 NCBI-Human-GeneID:1576 PMID:21177773 CYP3A4 (canonical)[glutathione depletion (course)] HOIP_0003171 NCBI-Human-GeneID:1576 http://www.ncbi.nlm.nih.gov/gene/1576 PMID:21177773 Cytochrome P450 (CYP) enzymes, including CYP2E1, CYP1A2, and CYP3A4, convert 5–9% of acetaminophen to a highly reactive metabolite, N-acetyl-p-benzoquinonimine (NAPQI) (Corcoran et al., 1980; Dahlin et al., 1984). HOIP:HOIP_0003172 NCBI-Human-GeneID:3569 NCBI-Mouse-GeneID:16193 NCBI-Rat-GeneID:24498 IL-6 - inflammatory cytokine (canonical)[glutathione depletion (course)] HOIP_0003172 NCBI-Human-GeneID:3569 http://www.ncbi.nlm.nih.gov/gene/3569 NCBI-Mouse-GeneID:16193 http://www.ncbi.nlm.nih.gov/gene/16193 NCBI-Rat-GeneID:24498 http://www.ncbi.nlm.nih.gov/gene/24498 HOIP:HOIP_0003173 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. ROS biosynthetic process [glutathione depletion (course)] reactive oxygen species biosynthetic process [glutathione depletion (course)] HOIP_0003173 HOIP:HOIP_0003174 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. increasing demand for response to oxidative stress [glutathione depletion (course)] HOIP_0003174 HOIP:HOIP_0003175 Increasing anti-oxidation demand is a subtype of increasing functional demand: A process changes the functional demand of oxidation to be higher. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. increasing anti-oxidation demand [glutathione depletion (course)] HOIP_0003175 HOIP:HOIP_0003176 Increasing anti-oxidation demand is a subtype of increasing functional demand: A process changes the functional demand of oxidation to be higher. increasing anti-oxidation demand HOIP_0003176 HOIP:HOIP_0003177 Oxidation-antioxidtion inbalance is a subtype of imbalance: A process that lacks a balance between oxidation and anti-oxidation that inhibits oxidation. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. oxidation-antioxidtion inbalance [glutathione depletion (course)] HOIP_0003177 HOIP:HOIP_0003178 ROS accumulation is a subtype of accumulation of substances in a biological object: A process that keeps ROS (Reactive Oxygen Species) in a biological object. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. ROS accumulation [glutathione depletion (course)] ROS accumulation [glutathione depletion (course)] HOIP_0003178 HOIP:HOIP_0003179 ROS accumulation is a subtype of accumulation of substances in a biological object: A process that keeps ROS (Reactive Oxygen Species) in a biological object. ROS accumulation HOIP_0003179 HOIP:HOIP_0003180 Hyperfunction of peroxisomal fatty acid beta-oxidation is a subtype of hyperfunction of fatty acid beta-oxidation: A process that performs an excessive peroxisomal fatty acid beta-oxidation. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hyperfunction of peroxisomal fatty acid beta-oxidation [glutathione depletion (course)] HOIP_0003180 HOIP:HOIP_0003181 The chemical reaction resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. ATP biosynthetic process [glutathione depletion (course)] HOIP_0003181 HOIP:HOIP_0003182 Iron accumulation is a subtype of accumulation of substances in a biological object: A process that keeps iron in an organism, tissue, organelle, or cell. iron accumulation HOIP_0003182 HOIP:HOIP_0003183 Iron accumulation is a subtype of accumulation of substances in a biological object: A process that keeps iron in an organism, tissue, organelle, or cell. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:21373260 PMID:24200681 iron accumulation [glutathione depletion (course)] HOIP_0003183 HOIP:HOIP_0003184 Kupffer cell activation is a subtype of macrophage activation: A change in morphology and behavior of a kupffer cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. kupffer cell activation HOIP_0003184 HOIP:HOIP_0003185 Kupffer cell activation is a subtype of macrophage activation: A change in morphology and behavior of a kupffer cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. Chronic ethanol exposure increases the gut permeability, resulting in translocation of gut endotoxin/LPS to liver. In liver, LPS leads to KCs activation via activating NOX and the TLR-4 pathway. The activated KCs then produce a large amount of reactive oxygen species (ROS), pro-inflammatory cytokines, and chemokines, which finally lead to liver injury kupffer cell activation [glutathione depletion (course)] HOIP_0003185 Chronic ethanol exposure increases the gut permeability, resulting in translocation of gut endotoxin/LPS to liver. In liver, LPS leads to KCs activation via activating NOX and the TLR-4 pathway. The activated KCs then produce a large amount of reactive oxygen species (ROS), pro-inflammatory cytokines, and chemokines, which finally lead to liver injury PMID:27965666 HOIP:HOIP_0003186 Accumulation of ethanol in intestine is a subtype of accumulation of xenobiotics: A process that keeps ethanol in the intestine. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. accumulation of ethanol in intestine [glutathione depletion (course)] HOIP_0003186 HOIP:HOIP_0003187 Accumulation of ethanol in intestine is a subtype of accumulation of xenobiotics: A process that keeps ethanol in the intestine. accumulation of ethanol in intestine HOIP_0003187 HOIP:HOIP_0003188 LPS translocation from gut to liver is a subtype of transmitting: A process that of the directed movement of LPS from the gut to the liver. chronic ethanol-induced activation of KCs is attributed to gut-sourced LPS, which is a major component of outer membrane of Gram-negative bacteria and passes through the intestinal epithelial barrier. Chronic ethanol exposure can increase translocation of LPS from gut to liver by enhancing the intestinal permeability and altering the gut microflora. LPS translocation from gut to liver HOIP_0003188 chronic ethanol-induced activation of KCs is attributed to gut-sourced LPS, which is a major component of outer membrane of Gram-negative bacteria and passes through the intestinal epithelial barrier. Chronic ethanol exposure can increase translocation of LPS from gut to liver by enhancing the intestinal permeability and altering the gut microflora. PMID:27965666 HOIP:HOIP_0003189 LPS translocation from gut to liver is a subtype of transmitting: A process that of the directed movement of LPS from the gut to the liver. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. chronic ethanol-induced activation of KCs is attributed to gut-sourced LPS, which is a major component of outer membrane of Gram-negative bacteria and passes through the intestinal epithelial barrier. Chronic ethanol exposure can increase translocation of LPS from gut to liver by enhancing the intestinal permeability and altering the gut microflora. LPS translocation from gut to liver [glutathione depletion (course)] HOIP_0003189 chronic ethanol-induced activation of KCs is attributed to gut-sourced LPS, which is a major component of outer membrane of Gram-negative bacteria and passes through the intestinal epithelial barrier. Chronic ethanol exposure can increase translocation of LPS from gut to liver by enhancing the intestinal permeability and altering the gut microflora. PMID:27965666 HOIP:HOIP_0003190 NCBI-Human-GeneID:581 NCBI-Mouse-GeneID:12028 NCBI-Rat-GeneID:24887 BAX (canonical)[glutathione depletion (course)] HOIP_0003190 NCBI-Human-GeneID:581 http://www.ncbi.nlm.nih.gov/gene/581 NCBI-Mouse-GeneID:12028 http://www.ncbi.nlm.nih.gov/gene/12028 NCBI-Rat-GeneID:24887 http://www.ncbi.nlm.nih.gov/gene/24887 HOIP:HOIP_0003191 NCBI-Human-GeneID:3553 NCBI-Mouse-GeneID:16176 NCBI-Rat-GeneID:24494 IL-1B (canonical)[glutathione depletion (course)] HOIP_0003191 NCBI-Human-GeneID:3553 http://www.ncbi.nlm.nih.gov/gene/3553 NCBI-Mouse-GeneID:16176 http://www.ncbi.nlm.nih.gov/gene/16176 NCBI-Rat-GeneID:24494 http://www.ncbi.nlm.nih.gov/gene/24494 HOIP:HOIP_0003192 A class 2 cytokine, IL-10 type that is a translation product of the human IL10 gene or a 1:1 ortholog thereof. Active interleukin-10 inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T cells. Structurally, IL-10 is a protein of about 160 amino acids that contains four conserved cysteines involved in disulfide bonds. NCBI-Human-GeneID:3586 NCBI-Mouse-GeneID:16153 NCBI-Rat-GeneID:25325 IL-10 (canonical)[glutathione depletion (course)] HOIP_0003192 NCBI-Human-GeneID:3586 http://www.ncbi.nlm.nih.gov/gene/3586 NCBI-Mouse-GeneID:16153 http://www.ncbi.nlm.nih.gov/gene/16153 NCBI-Rat-GeneID:25325 http://www.ncbi.nlm.nih.gov/gene/25325 HOIP:HOIP_0003193 A protein that is a translation product of the human IL4 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3565 NCBI-Mouse-GeneID:16189 NCBI-Rat-GeneID:287287 IL-4 (canonical)[glutathione depletion (course)] HOIP_0003193 NCBI-Human-GeneID:3565 http://www.ncbi.nlm.nih.gov/gene/3565 NCBI-Mouse-GeneID:16189 http://www.ncbi.nlm.nih.gov/gene/16189 NCBI-Rat-GeneID:287287 http://www.ncbi.nlm.nih.gov/gene/287287 HOIP:HOIP_0003194 A tumor necrosis factor that is encoded in the genome of human. NCBI-Human-GeneID:7124 NCBI-Mouse-GeneID:21926 NCBI-Rat-GeneID:24835 TNF-A (canonical)[glutathione depletion (course)] HOIP_0003194 NCBI-Human-GeneID:7124 http://www.ncbi.nlm.nih.gov/gene/7124 NCBI-Mouse-GeneID:21926 http://www.ncbi.nlm.nih.gov/gene/21926 NCBI-Rat-GeneID:24835 http://www.ncbi.nlm.nih.gov/gene/24835 HOIP:HOIP_0003195 Cell death dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of cell death as a gene product. Gene profile:caonical that described in textbooks or articles. cell death dependent dependent molecule (canonical) HOIP_0003195 HOIP:HOIP_0003196 NCBI-Human-GeneID:317 NCBI-Mouse-GeneID:11783 NCBI-Rat-GeneID:78963 APAF1 (canonical)[apotosis] HOIP_0003196 NCBI-Human-GeneID:317 http://www.ncbi.nlm.nih.gov/gene/317 NCBI-Mouse-GeneID:11783 http://www.ncbi.nlm.nih.gov/gene/11783 NCBI-Rat-GeneID:78963 http://www.ncbi.nlm.nih.gov/gene/78963 HOIP:HOIP_0003197 NCBI-Human-GeneID:572 NCBI-Mouse-GeneID:12015 NCBI-Rat-GeneID:64639 BAD (canonical)[apotosis] HOIP_0003197 NCBI-Human-GeneID:572 http://www.ncbi.nlm.nih.gov/gene/572 NCBI-Mouse-GeneID:12015 http://www.ncbi.nlm.nih.gov/gene/12015 NCBI-Rat-GeneID:64639 http://www.ncbi.nlm.nih.gov/gene/64639 HOIP:HOIP_0003198 NCBI-Human-GeneID:578 NCBI-Mouse-GeneID:12018 NCBI-Rat-GeneID:116502 BAK1 (canonical)[apotosis] HOIP_0003198 NCBI-Human-GeneID:578 http://www.ncbi.nlm.nih.gov/gene/578 NCBI-Mouse-GeneID:12018 http://www.ncbi.nlm.nih.gov/gene/12018 NCBI-Rat-GeneID:116502 http://www.ncbi.nlm.nih.gov/gene/116502 HOIP:HOIP_0003199 NCBI-Human-GeneID:637 NCBI-Mouse-GeneID:12122 NCBI-Rat-GeneID:64625 BID (canonical)[apotosis] HOIP_0003199 NCBI-Human-GeneID:637 http://www.ncbi.nlm.nih.gov/gene/637 NCBI-Mouse-GeneID:12122 http://www.ncbi.nlm.nih.gov/gene/12122 NCBI-Rat-GeneID:64625 http://www.ncbi.nlm.nih.gov/gene/64625 HOIP:HOIP_0003200 NCBI-Human-GeneID:355 NCBI-Mouse-GeneID:14102 NCBI-Rat-GeneID:246097 FAS (canonical)[apotosis] HOIP_0003200 NCBI-Human-GeneID:355 http://www.ncbi.nlm.nih.gov/gene/355 NCBI-Mouse-GeneID:14102 http://www.ncbi.nlm.nih.gov/gene/14102 NCBI-Rat-GeneID:246097 http://www.ncbi.nlm.nih.gov/gene/246097 HOIP:HOIP_0003201 A tumor necrosis factor that is encoded in the genome of human. NCBI-Human-GeneID:7124 NCBI-Mouse-GeneID:21926 NCBI-Rat-GeneID:24835 TNF (canonical)[apotosis] HOIP_0003201 NCBI-Human-GeneID:7124 http://www.ncbi.nlm.nih.gov/gene/7124 NCBI-Mouse-GeneID:21926 http://www.ncbi.nlm.nih.gov/gene/21926 NCBI-Rat-GeneID:24835 http://www.ncbi.nlm.nih.gov/gene/24835 HOIP:HOIP_0003202 NCBI-Human-GeneID:7157 NCBI-Rat-GeneID:24842 TP53 (canonical)[apotosis] HOIP_0003202 NCBI-Human-GeneID:7157 http://www.ncbi.nlm.nih.gov/gene/7157 NCBI-Rat-GeneID:24842 http://www.ncbi.nlm.nih.gov/gene/24842 HOIP:HOIP_0003203 NCBI-Human-GeneID:8717 NCBI-Mouse-GeneID:71609 NCBI-Rat-GeneID:246756 TRADD (canonical)[apotosis] HOIP_0003203 NCBI-Human-GeneID:8717 http://www.ncbi.nlm.nih.gov/gene/8717 NCBI-Mouse-GeneID:71609 http://www.ncbi.nlm.nih.gov/gene/71609 NCBI-Rat-GeneID:246756 http://www.ncbi.nlm.nih.gov/gene/246756 HOIP:HOIP_0003204 NCBI-Human-GeneID:841 NCBI-Mouse-GeneID:12370 NCBI-Rat-GeneID:64044 CASP8 (canonical)[apotosis] HOIP_0003204 NCBI-Human-GeneID:841 http://www.ncbi.nlm.nih.gov/gene/841 NCBI-Mouse-GeneID:12370 http://www.ncbi.nlm.nih.gov/gene/12370 NCBI-Rat-GeneID:64044 http://www.ncbi.nlm.nih.gov/gene/64044 HOIP:HOIP_0003205 NCBI-Human-GeneID:836 NCBI-Mouse-GeneID:12367 NCBI-Rat-GeneID:25402 CASPASE-3 (canonical)[apotosis] HOIP_0003205 NCBI-Human-GeneID:836 http://www.ncbi.nlm.nih.gov/gene/836 NCBI-Mouse-GeneID:12367 http://www.ncbi.nlm.nih.gov/gene/12367 NCBI-Rat-GeneID:25402 http://www.ncbi.nlm.nih.gov/gene/25402 HOIP:HOIP_0003206 NCBI-Human-GeneID:7187 NCBI-Mouse-GeneID:22031 NCBI-Rat-GeneID:362788 TRAF3 (canonical)[apotosis] HOIP_0003206 NCBI-Human-GeneID:7187 http://www.ncbi.nlm.nih.gov/gene/7187 NCBI-Mouse-GeneID:22031 http://www.ncbi.nlm.nih.gov/gene/22031 NCBI-Rat-GeneID:362788 http://www.ncbi.nlm.nih.gov/gene/362788 HOIP:HOIP_0003208 Inflammatory cytokine gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. inflammatory cytokine gene expression [glutathione depletion (course)] HOIP_0003208 HOIP:HOIP_0003209 A pathologic process that involves the transformation of normal cells to a neoplastic state and resulting in polyclonal or monoclonal neoplastic cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. PMID:29558368 tumorigenesis [glutathione depletion (course)] HOIP_0003209 PMID:29558368 HOIP:HOIP_0003214 Osgin1 - apotosis inducing factor (rat) [cell death (course)] HOIP_0003214 HOIP:HOIP_0003215 Osgin1 - cancer repressor (rat) [cell death (course)] HOIP_0003215 HOIP:HOIP_0003216 Osgin1 - oxidative stress response protein (rat) [cell death (course)] HOIP_0003216 HOIP:HOIP_0003217 TP53 - apotosis inducing factor (canonical) [cell death (course)] HOIP_0003217 HOIP:HOIP_0003218 Negative regulation of cytokine gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of inflammatory cytokine gene expression. negative regulation of cytokine gene expression HOIP_0003218 HOIP:HOIP_0003220 A role played by the entity that competitively inhibits the catalysis of the hydrolysis of a phospholipid. conpetitive inhibitor of phospholipase HOIP_0003220 HOIP:HOIP_0003221 AMPK is a highly evolutionarily conserved serine/threonine kinase, and orthologs of the AMPK subunits are found in all eukaryotic species. At the molecular level, AMPK is a heterotrimer complex comprising a catalytic alpha subunit, with a conventional serine/threonine protein kinase domain, and two regulatory subunits, beta and gamma. In mammals, each subunit is encoded by multiple genes (alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3), which results in 12 possible combinations of AMPK complex. AMPK is a highly evolutionarily conserved serine/threonine kinase, and orthologs of the AMPK subunits are found in all eukaryotic species. At the molecular level, AMPK is a heterotrimer complex comprising a catalytic alpha subunit, with a conventional serine/threonine protein kinase domain, and two regulatory subunits, beta and gamma. In mammals, each subunit is encoded by multiple genes (alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3), which results in 12 possible combinations of AMPK complex. AMPK is a highly evolutionarily conserved serine/threonine kinase, and orthologs of the AMPK subunits are found in all eukaryotic species. At the molecular level, AMPK is a heterotrimer complex comprising a catalytic alpha subunit, with a conventional serine/threonine protein kinase domain, and two regulatory subunits, beta and gamma. In mammals, each subunit is encoded by multiple genes (alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3), which results in 12 possible combinations of AMPK complex. IMR:0002775 (obsolete) NCBI-Human-GeneID:5562 NCBI-Mouse-GeneID:105787 NCBI-Rat-GeneID:65248 gene name: PRKAA2 AMPK (mol) HOIP_0003221 AMPK is a highly evolutionarily conserved serine/threonine kinase, and orthologs of the AMPK subunits are found in all eukaryotic species. At the molecular level, AMPK is a heterotrimer complex comprising a catalytic alpha subunit, with a conventional serine/threonine protein kinase domain, and two regulatory subunits, beta and gamma. In mammals, each subunit is encoded by multiple genes (alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3), which results in 12 possible combinations of AMPK complex. PMID:16644800 PMID:17307971 PMID:18977694 NCBI-Human-GeneID:5562 http://www.ncbi.nlm.nih.gov/gene/5562 NCBI-Mouse-GeneID:105787 http://www.ncbi.nlm.nih.gov/gene/105787 NCBI-Rat-GeneID:65248 http://www.ncbi.nlm.nih.gov/gene/65248 HOIP:HOIP_0003222 A set or series of molecular interactions. molecular subpathway HOIP_0003222 HOIP:HOIP_0003223 PI3K (mol) HOIP_0003223 HOIP:HOIP_0003224 A combining role with a signal and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II. IMR:0000085 (obsolete) hasrelated molecular function GO:0004879 nuclear receptor HOIP_0003224 HOIP:HOIP_0003230 A role played by the entity which involves in regulating a process. process regulator role HOIP_0003230 HOIP:HOIP_0003235 The activation, translocation and oligomerization of BAX involved in the apoptosis. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. As a result of binding to Bid, Bax oligomerizes and integrates in the outer mitochondrial membrane that triggers cytochrome c release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis (Eskes et al., 2000) As a result of binding to Bid, Bax oligomerizes and integrates in the outer mitochondrial membrane that triggers cytochrome c release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis (Eskes et al., 2000) Reactome:R-HSA-114294.2 Activation, translocation and oligomerization of BAX [apoptosis (course)] HOIP_0003235 As a result of binding to Bid, Bax oligomerizes and integrates in the outer mitochondrial membrane that triggers cytochrome c release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis (Eskes et al., 2000) Reactome:R-HSA-114294.2 HOIP:HOIP_0003236 NCBI-Human-GeneID:581 NCBI-Mouse-GeneID:12028 NCBI-Rat-GeneID:24887 BAX (canonical)[cell death] HOIP_0003236 NCBI-Human-GeneID:581 http://www.ncbi.nlm.nih.gov/gene/581 NCBI-Mouse-GeneID:12028 http://www.ncbi.nlm.nih.gov/gene/12028 NCBI-Rat-GeneID:24887 http://www.ncbi.nlm.nih.gov/gene/24887 HOIP:HOIP_0003237 Intrinsic apoptosis signaling is a subtype of signaling that an intracellular signal is conveyed to trigger the apoptotic death of a cell. The process starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.). This process is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP). intrinsic apoptosis signaling HOIP_0003237 HOIP:HOIP_0003239 cyclin dependent kinase 1 NCBI-Human-GeneID:983 NCBI-Mouse-GeneID:12534 NCBI-Rat-GeneID:54237 OMIM:116940 Cdk1 (mol) HOIP_0003239 NCBI-Human-GeneID:983 http://www.ncbi.nlm.nih.gov/gene/983 NCBI-Mouse-GeneID:12534 http://www.ncbi.nlm.nih.gov/gene/12534 NCBI-Rat-GeneID:54237 http://www.ncbi.nlm.nih.gov/gene/54237 HOIP:HOIP_0003241 GO:0004693 Cyclin-dependent kinase CDK (family) HOIP_0003241 HOIP:HOIP_0003251 A role played by the entity which enables the transfer of drugs. drug transporter HOIP_0003251 HOIP:HOIP_0003254 NCBI-Human-GeneID:5830 NCBI-Mouse-GeneID:19305 NCBI-Rat-GeneID:312703 PEX5 (mol) HOIP_0003254 NCBI-Human-GeneID:5830 http://www.ncbi.nlm.nih.gov/gene/5830 NCBI-Mouse-GeneID:19305 http://www.ncbi.nlm.nih.gov/gene/19305 NCBI-Rat-GeneID:312703 http://www.ncbi.nlm.nih.gov/gene/312703 HOIP:HOIP_0003256 Farnesoid X receptor inactivation is a subtype of inactivating nuclear receptor: A process that changes the activity of the inactivating FxR (farnesoid X receptor) with a nuclear receptor role to be lower. FXR inactivation Farnesoid X Receptor inactivation farnesoid X receptor inactivation HOIP_0003256 HOIP:HOIP_0003257 Hyperfunction of drug transporter gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive drug transporter gene expression. hyperfunction of drug transporter gene expression HOIP_0003257 HOIP:HOIP_0003259 Hyperfunction of bile acid transport is a subtype of hyperfunction of transport: A process that performs an excesssive bile acid transport. hyperfunction of bile acid transport HOIP_0003259 HOIP:HOIP_0003264 Farnesoid X receptor inactivation is a subtype of inactivating nuclear receptor: A process that changes the activity of the activating FxR (farnesoid X receptor) with a nuclear receptor role to be lower. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:15146238 PMID:21286345 FXR inactivation [non-alcoholic fatty liver disease (NAFLD)] Farnesoid X Receptor inactivation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003264 HOIP:HOIP_0003265 Bile salts activate a bile sil sensor, FXR (bile acid receptor; NR1H4) in hepatocytes. https://omim.org/entry/603826 NCBI-Human-GeneID:9971 NCBI-Mouse-GeneID:20186 NCBI-Rat-GeneID:60351 PMID:26888176 UniProt:Q96RI1 http://purl.bioontology.org/ontology/MESH/C094063 http://www.ncbi.nlm.nih.gov/gene/9971 farnesoid x-activated receptor [lipidosis] FXR (canonical)[lipidosis] HOIP_0003265 NCBI-Human-GeneID:9971 http://www.ncbi.nlm.nih.gov/gene/9971 NCBI-Mouse-GeneID:20186 http://www.ncbi.nlm.nih.gov/gene/20186 NCBI-Rat-GeneID:60351 http://www.ncbi.nlm.nih.gov/gene/60351 PMID:26888176 Mutations in the nuclear bile acid receptor FXR cause progressive familial intrahepatic cholestasis. Clinical features of severe, NR1H4-related cholestasis include neonatal onset with rapid progression to end-stage liver disease, vitamin K-independent coagulopathy, low-to-normal serum gamma-glutamyl transferase activity, elevated serum alpha-fetoprotein and undetectable liver bile salt export pump (ABCB11) expression. HOIP:HOIP_0003266 Bile salts activate a bile sil sensor, FXR (bile acid receptor; NR1H4) in hepatocytes. https://omim.org/entry/603826 NCBI-Human-GeneID:9971 NCBI-Mouse-GeneID:20186 NCBI-Rat-GeneID:60351 PMID:26888176 UniProt:Q96RI1 http://purl.bioontology.org/ontology/MESH/C094063 http://www.ncbi.nlm.nih.gov/gene/9971 bile acid receptor [cholestasis] farnesoid x-activated receptor -inactivated state [lipidosis] FXR -inactivated state (canonical)[lipidosis] HOIP_0003266 NCBI-Human-GeneID:9971 http://www.ncbi.nlm.nih.gov/gene/9971 NCBI-Mouse-GeneID:20186 http://www.ncbi.nlm.nih.gov/gene/20186 NCBI-Rat-GeneID:60351 http://www.ncbi.nlm.nih.gov/gene/60351 PMID:26888176 Mutations in the nuclear bile acid receptor FXR cause progressive familial intrahepatic cholestasis. Clinical features of severe, NR1H4-related cholestasis include neonatal onset with rapid progression to end-stage liver disease, vitamin K-independent coagulopathy, low-to-normal serum gamma-glutamyl transferase activity, elevated serum alpha-fetoprotein and undetectable liver bile salt export pump (ABCB11) expression. HOIP:HOIP_0003267 Malfunction of biosynthesis is a subtype of malfunctioning: A process that cannot perform the biosynthesis function appropriately or cannot realize it at all. malfunction of biosynthesis HOIP_0003267 HOIP:HOIP_0003268 Malfunction of lipid biosynthesis is a subtype of malfunctioning: A process that cannot perform the lipid biosynthesis function appropriately or cannot realize it at all. malfunction of lipid biosynthesis HOIP_0003268 HOIP:HOIP_0003269 Hypofunction of phospholipid transport from ER to mitochondrial membrane is a subtype of hypofunction of transport: A process that performs a decreased or insufficient phospholipid transport from ER to mitochondrial membrane. hypofunction of phospholipid transport from ER to mitochondrial membrane HOIP_0003269 HOIP:HOIP_0003270 Hypofunction of phospholipid transport from ER to mitochondrial membrane is a subtype of hypofunction of transport: A process that performs a decreased or insufficient phospholipid transport from ER to mitochondrial membrane. This entity is a specific course-dependent process. This process can constitute the course of ER stress hypofunction of phospholipid transport from ER to mitochondrial membrane [ER stress] HOIP_0003270 HOIP:HOIP_0003274 ER stress and PPARα activation contribute to carcinogenesis in a fatty liver. PMID:22009939 Hepatosteatosis in peroxisome deficient liver despite increased beta-oxidation capacity and impaired lipogenesis. Biochimie (2011) 93:1828–38. FGF21-FGFR1 coordinates phospholipid homeostasis, lipid droplet function and ER stress in obesity.Endocrinology. 2016 PMID:27690692 Fibroblast growth factor 21 (FGF21) is an endocrine growth factor, a regulator of fatty acids and glucose metabolism. Recently, it has been reported that FGF21 expression is regulated by activating transcription factor 4 (ATF4), a transcription factor activated by various stimuli such as endoplasmic reticulum (ER) stress. PMID:27010621 Endoplasmic reticulum stress induces up-regulation of hepatic beta-Klotho expression through ATF4 signaling pathway. PMID:25727012 NCBI-Mouse-GeneID:56636 PMID:17550777 PMID:22009939 PMID:25727012 PMID:27010621 PMID:27690692 Fgf21 (mouse)[ER stress] HOIP_0003274 PMID:24217556 NCBI-Mouse-GeneID:56636 http://www.ncbi.nlm.nih.gov/gene/56636 PMID:17550777 Endocrine regulation of the fasting response by PPARα-mediated induction of fibroblast growth factor 21: FGF21 is induced directly by PPARalpha in liver in response to fasting and PPARalpha agonists. FGF21 in turn stimulates lipolysis in white adipose tissue and ketogenesis in liver. PPARalpha-FGF21 endocrine signaling pathway in regulating diverse metabolic and behavioral aspects of the adaptive response to starvation. PMID:22009939 ER stress and PPARα activation contribute to carcinogenesis in a fatty liver. PMID:27010621 FGF21 expression is regulated by activating transcription factor 4 (ATF4), a transcription factor activated by various stimuli such as endoplasmic reticulum (ER) stress. PMID:27690692 FGF21 is regulated by PPARa: Hepatic fibroblast growth factor 21 is regulated by PPARα and is a key mediator of hepatic lipid metabolism in ketotic states. HOIP:HOIP_0003275 Malfunction of phospholipid biosynthesis is a subtype of malfunctioning: A process that cannot perform the phospholipid biosynthesis function appropriately or cannot realize it at all. malfunction of phospholipid biosynthesis HOIP_0003275 HOIP:HOIP_0003276 Malfunction of phospholipid biosynthesis is a subtype of malfunctioning: A process that cannot perform the phospholipid biosynthesis function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of ER stress. malfunction of phospholipid biosynthesis [ER stress] HOIP_0003276 HOIP:HOIP_0003277 PMID:10818100 PMID:21091435 PMID:23334697 PMID:24469402 http://www.uniprot.org/uniprot/Q86YB8#function https://omim.org/entry/615437 Ero1lb (mouse)[ER stress] HOIP_0003277 PMID:21091435 The endoplasmic reticulum sulfhydryl oxidase Ero1-beta drives efficient oxidative protein folding with loose regulation. PMID:23334697 Xenobiotic perturbation of ER stress and the unfolded protein response. PMID:24469402 Deregulation of Pancreas-Specific Oxidoreductin ERO1β in the Pathogenesis of Diabetes Mellitus HOIP:HOIP_0003282 Hypofunction of phospholipid degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient phospholipid degradation. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). hypofunction of phospholipid degradation [phospholipidosis (moderate)] HOIP_0003282 HOIP:HOIP_0003283 NCBI-Human-GeneID:4864 NCBI-Mouse-GeneID: 18145 NCBI-Rat-GeneID:266732 OMIM: 607623 PMID:18772377 NPC Intracellular Cholesterol Transporter 1 [Niemann Pick Type C] NPC1 (canonical)[Niemann Pick Type C] HOIP_0003283 NCBI-Human-GeneID:4864 http://www.ncbi.nlm.nih.gov/gene/4864 NCBI-Mouse-GeneID: 18145 http://www.ncbi.nlm.nih.gov/gene/18145 NCBI-Rat-GeneID:266732 http://www.ncbi.nlm.nih.gov/gene/266732 HOIP:HOIP_0003284 NCBI-Human-GeneID:4864 NCBI-Mouse-GeneID: 18145 NCBI-Rat-GeneID:266732 OMIM: 607623 NPC Intracellular Cholesterol Transporter 1 NPC1 (mol) HOIP_0003284 NCBI-Human-GeneID:4864 http://www.ncbi.nlm.nih.gov/gene/4864 NCBI-Mouse-GeneID: 18145 http://www.ncbi.nlm.nih.gov/gene/18145 NCBI-Rat-GeneID:266732 http://www.ncbi.nlm.nih.gov/gene/266732 HOIP:HOIP_0003285 NCBI-Human-GeneID:10577 NCBI-Mouse-GeneID: 67963 NCBI-Rat-GeneID:286898 PMID:18772377 NPC Intracellular Cholesterol Transporter 2 [Niemann-Pick Type C] NPC2 (canonical)[Niemann-Pick Type C] HOIP_0003285 NCBI-Human-GeneID:10577 http://www.ncbi.nlm.nih.gov/gene/10577 NCBI-Mouse-GeneID: 67963 http://www.ncbi.nlm.nih.gov/gene/67963 NCBI-Rat-GeneID:286898 http://www.ncbi.nlm.nih.gov/gene/286898 PMID:18772377 Because of its ability to bind cholesterol, NPC2 can transfer cholesterol from one liposome to another. This transfer is accelerated in the presence of anionic phospholipids such as bis(monooleoylglycero)phosphate (BMP) and phosphatidyl inositol, which are found in lysosomes HOIP:HOIP_0003287 NCBI-Human-GeneID:10577 NCBI-Mouse-GeneID: 67963 NCBI-Rat-GeneID:286898 PMID:18772377 NPC Intracellular Cholesterol Transporter 2 [Niemann-Pick Type C] NPC2 (mol) HOIP_0003287 NCBI-Human-GeneID:10577 http://www.ncbi.nlm.nih.gov/gene/10577 NCBI-Mouse-GeneID: 67963 http://www.ncbi.nlm.nih.gov/gene/67963 NCBI-Rat-GeneID:286898 http://www.ncbi.nlm.nih.gov/gene/286898 HOIP:HOIP_0003288 Hypofunction of alcohol metabolism is a subtype of hyperfunctioning: A process that performs a decreased or insufficient glutathione conjugation. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. hypofunction of glutathione conjugation [glutathione depletion (course)] HOIP_0003288 HOIP:HOIP_0003289 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required. This entity is a specific course-dependent process. This process can constitute the course of diabetes. insulin deficiency [diabetes course] HOIP_0003289 HOIP:HOIP_0003290 Increasing blood glucose level is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of diabetes. hyperglycemia increasing blood glucose level [diabetes coruse] HOIP_0003290 HOIP:HOIP_0003291 The totality of all processes through which a given diabetic retinopathy instance is realized. diabetic retinopathy course HOIP_0003291 HOIP:HOIP_0003292 Mcrovascular dysfunction is a subtype of organ malfunction: A process that does not perform microvascular function correctly or not functioning at all. microvascular dysfunction HOIP_0003292 HOIP:HOIP_0003293 Narrowing of the retinal artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the retinal arteries to be smaller. narrowing of the retinal artery HOIP_0003293 HOIP:HOIP_0003294 Narrowing of the retinal artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the retinal arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of diabetic retinopathy. narrowing of the retinal artery [diabetic retinopathy course] HOIP_0003294 HOIP:HOIP_0003295 Retinal degeneration is a subtype of changing material: A process that degenerates retinal photoreceptors and pigmented epithelial cells. This entity is a specific course-dependent process. This process can constitute the course of diabetic retinopathy. retinal degeneration [diabetic retinopathy course] HOIP_0003295 HOIP:HOIP_0003301 Mitochondria proliferation in hepatocyte is a subtype of hepatocyte organelle proliferation: A process that becomes larger in the number of mitochondria in hepatocyte(s). mitochondria proliferation in hepatocyte HOIP_0003301 HOIP:HOIP_0003303 Hepatocyte organelle proliferation is a subtype of increasing number of organelle: A process that becomes larger in the number of organelles in hepatocyte(s). hepatocyte organelle proliferation HOIP_0003303 HOIP:HOIP_0003306 Increasing osmotic pressure is a subtype of increasing pressure: A process that changes the osmotic pressure of the object to be higher. increasing osmotic pressure. HOIP_0003306 HOIP:HOIP_0003307 Decreasing osmotic pressure. is a subtype of decresing pressure: A process that changes the osmotic pressure to be lower. decreasing osmotic pressure. HOIP_0003307 HOIP:HOIP_0003308 Increasing osmotic pressure in cell is a subtype of increasing osmotic pressure.: A process that changes the osmotic pressure of the cell to be higher. increasing osmotic pressure in cell HOIP_0003308 HOIP:HOIP_0003311 Improving is a type of functioning process of meta-function. Both enhancing and improveing represents optional contribution to other function. The “optional” means that the effect of fa is not mandatory to ft, that is, the target function can be performed without improving or enhancing. The discrimination between improving and enhancing is made by whether augmentation of the output can be made without increase of the amount of the input energy or not. For example, the “to make low pressure” of the condenser contributes to the efficiency of the “to generate torque” function without increment of input energy, so its functioning is “Improving”. On the other hand, the “to super-heat” function of the boiler optionally increases the amount of the input energy to make a contribution. Its meta-function is “Enhancing” . improving HOIP_0003311 HOIP:HOIP_0003313 Accumulation of substance in hepatocyte is a subtype of accumulation of substances in a biological object: A process that keeps substances in the hepatocyte. accumulation of substance in hepatocyte HOIP_0003313 HOIP:HOIP_0003315 Decreasing retinal blood flow is a subtype of decreasing flow: A process that changes the amount of retinal blood flow to be lower. decreasing retinal blood flow HOIP_0003315 HOIP:HOIP_0003317 Decreasing retinal blood flow is a subtype of decreasing flow: A process that changes the amount of retinal flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of diabetic retinopathy. decreasing retinal blood flow [diabetic retinopathy course] HOIP_0003317 HOIP:HOIP_0003318 Moving water to the inside of cell is a subtype of moving A to the inside of B: A process of the movement of water into a cell. moving water to the inside of cell HOIP_0003318 HOIP:HOIP_0003321 Catalysis role of the reaction: N-acylsphingosine + H2O = a fatty acid + sphingosine. ceramidase HOIP_0003321 HOIP:HOIP_0003326 Catalysis of the reaction: fatty acid (C-16 or longer) + 2-C = fatty acid (C-16 or longer + 2-C). related molecular function GO:0009922 fatty acid elongase HOIP_0003326 HOIP:HOIP_0003328 Catalysis role of the reaction: acyl-CoA + reduced acceptor + O2 = desaturated-acyl-CoA + acceptor + 2 H2O EC:1.14.19 related molecular function GO:0016215 acyl-coA desaturase HOIP_0003328 HOIP:HOIP_0003329 Catalysis role of the reaction: stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + H2O. EC:1.14.19.1 related molecular function GO:0004768 stearoyl-CoA 9-desaturase HOIP_0003329 HOIP:HOIP_0003331 Combining role with a cytokine and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. IMR:0000095 (obsolete) related molecular function GO:0004896 cytokine receptor HOIP_0003331 HOIP:HOIP_0003336 A role played by the entity which enables the transfer of the hexose monosaccharide glucose from one side of a membrane to the other. glucose permease related molecular function GO:0005355 glucose transmembrane transporter HOIP_0003336 HOIP:HOIP_0003338 A role played by the entity which transfers long-chain fatty acids from one side of a membrane to the other. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22 EC:3.6.3.47 PMID:15249972 related molecular function GO:0005324 long-chain fatty acid transporter HOIP_0003338 PMID:15249972 Effect of liver fatty acid binding protein (FABP) T94A missense mutation on plasma lipoprotein responsiveness to treatment with fenofibrate. Fenofibrate, a peroxisome proliferated activated receptor alpha (PPARalpha) agonist, has been shown to decrease plasma triglyceride (TG) and increase plasma high-density lipoprotein (HDL) cholesterol levels despite a large interindividual variation in the response. Fenofibrate-activated PPARalpha binds to a DNA sequence element termed PPAR response element (PPRE) present in regulatory regions of target genes. A PPRE has been identified in the proximal 5' flanking region of the gene encoding the liver fatty acid binding protein (LFABP). LFABP is a small cytosolic protein of 14 kDa present in the liver and the intestine and is a member of the superfamily of the fatty acid binding proteins (FABPs). FABPs play a role in the solubilization of long-chain fatty acids (LCFAs) and their CoA-ester to various intracellular organelles. FABPs serves as intracellular acceptors of LCFAs, and they may also have an impact in ligand-dependent transactivation of PPARs in trafficking LCFAs to the nucleus. Since PPARs are known to regulate the transcription of many genes involved in lipid metabolism, the importance of LFABP in fatty acid uptake has to be considered. The aim of this study was to verify whether genetic variations in the LFABP gene may impact on plasma lipoprotein/lipid levels in the fasting state as well as on the response to a lipid-lowering therapy with fenofibrate on plasma lipids and obesity variables. We also wanted to verify whether the presence of the PPARalpha L162V mutation interacts with genetic variants in LFABP gene. To achieve this goal, we first determined the genomic structure of the human LFABP gene and then designed intronic primers to sequence the coding regions, all exon-intron splicing boundaries, and the promoter region of the gene in 24 patients showing divergent plasma lipoprotein/lipid response to fenofibrate. Sequence analysis revealed the presence of a T94A missense mutation in exon 3. Interspecies comparison revealed that threonine 94 is conserved among species. We subsequently screened another sample of 130 French Canadian subjects treated with fenofibrate for the presence of the LFABP T94A mutation. Carriers of the A94 allele were at increased risk to exhibit plasma TG levels above 2.00 mmol/l after treatment with fenofibrate [2.75 (1.03-7.34); OR 95% confidence interval (CI)]. In addition, carriers of the A94 allele were characterized by higher baseline plasma-free fatty acid levels (FFA) ( p=0.01) and by a lower body mass index (BMI) ( p=0.05) and waist circumference ( p=0.005) than T94 homozygotes. Moreover, PPARalpha L162V and LFABP T94A showed to have a synergistic effect on BMI ( p interaction = 0.03). These results suggest that the LFABP T94A missense mutation could influence obesity indices as well as the risk to exhibit residual hypertriglyceridmia following a lipid-lowering therapy with fenofibrate. HOIP:HOIP_0003340 Increasing blood glucose lebvel is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of diabetic retinopathy. increasing blood glucose level [diabetic retinopathy course] HOIP_0003340 HOIP:HOIP_0003341 NCBI-Human-GeneID:1958 NCBI-Mouse-GeneID:13653 NCBI-Rat-GeneID:24330 PMID:15752369 PMID:16344600 PMID:24619556 PMID:25122760 PMID:25737480 PMID:29607419 http://omim.org/entry/128990 http://www.ncbi.nlm.nih.gov/gene/1958 EGR1 (human)[ER stress] HOIP_0003341 NCBI-Human-GeneID:1958 http://www.ncbi.nlm.nih.gov/gene/1958 NCBI-Mouse-GeneID:13653 http://www.ncbi.nlm.nih.gov/gene/13653 NCBI-Rat-GeneID:24330 http://www.ncbi.nlm.nih.gov/gene/24330 PMID:15752369 Liver X receptor agonists inhibit tissue factor expression in macrophages. PMID:16344600 Ethanol-induced liver injury: potential roles for egr-1. PMID:24619556 E2F1 is a novel fibrogenic gene that regulates cholestatic liver fibrosis through the Egr-1/SHP/EID1 network. PMID:25122760 ATF3 epigenetically suppresses expression of EGR-1, a non-canonical pro-inflammatory transcriptional modulator crucial to cancer chemokine induction. PMID:25737480 Loss of Egr-1 sensitizes pancreatic beta-cells to palmitate-induced ER stress and apoptosis. PMID:29607419 Role of early growth response 1 in liver metabolism and liver cancer. HOIP:HOIP_0003342 Diabetes dependent process is a subtype of disease course dependent process: A process that can constitute the course of diabetes. Diabetes dependent process [diabetes course] HOIP_0003342 HOIP:HOIP_0003343 Process of binding by which electrophiles interact with DNA (deoxyribonucleic acid). binding to DNA by electrophiles HOIP_0003343 HOIP:HOIP_0003344 Process of binding by which electrophiles interact with DNA (deoxyribonucleic acid). This entity is a specific course-dependent process. This process can constitute the course of necrosis. binding to DNA by electrophiles [necrosis (course)] HOIP_0003344 HOIP:HOIP_0003348 Catalysis role of the reaction: linoleoyl-CoA + reduced acceptor + O2 = gamma-linolenoyl-CoA + acceptor + 2 H2O. EC:1.14.19.3 PMID:7212717 related molecular function GO:0016213 linoleoyl-CoA desaturase role HOIP_0003348 HOIP:HOIP_0003351 A role played by the entity that ihibits the insulin resistance. inhibitor of insulin resistance HOIP_0003351 HOIP:HOIP_0003352 Negative regulation of increasing insulin resistance is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of insulin resistance. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. negative regulation of increasing insulin resistance [phospholipidosis (imbalance course)] HOIP_0003352 HOIP:HOIP_0003353 Substance with substance with cationic amphiphilic drug role is a subtype of substance with role. This entity is participating in a biological process and playing a cationic amphiphilic drug role. PMID:9061852 This entity is inferred from Description Logic. substance with cationic amphiphilic drug role HOIP_0003353 HOIP:HOIP_0003354 lysosomal enzyme transport to lysosome is a subtype of transport: A process that of the transfer of a lysosomal enzyme (from the ribosome to the lysosome). This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). lysosomal enzyme transport (to lysosome) [phospholipidosis (normal course)] HOIP_0003354 HOIP:HOIP_0003355 lysosomal enzyme transport (from ribosome to lysosome) is a subtype of transport: A process that of the transfer of a lysosomal enzyme (from the ribosome to the lysosome). transportng lysosomal enzyme from ribosome to lysosome HOIP_0003355 HOIP:HOIP_0003356 Phospholipidosis (normal course) is a subtype of process sequences: The courses of processes through which phospholipid homeostasis balance is keeping. phospholipidosis (normal course) HOIP_0003356 HOIP:HOIP_0003357 Keeping amount of phospholipid in lysosome is a subtype of keeping amount: A process that maintaining the amount of lysosomal phospholipid. keeping amount of phospholipid in lysosome HOIP_0003357 HOIP:HOIP_0003359 The totality of all processes through which the phospholipidosis is realized. The severity is mild. PMID:15342952 PMID:16979167 PMID:22960355 phospholipidosis (mild) HOIP_0003359 PMID:15342952 The following four processes were involved in the induction of phospholipidosis; (1) Inhibition of lysosomal phospholipase activivity (2) Inhibition of lysosomal enzyme transport, as demonstrated by the down-regulation of genes involved in lysosomal enzyme transport (3) Enhanced phospholipid biosynthesis, which is supported by the up- regulation of fatty acid biosynthesis-related genes (4) Enhanced cholesterol biosynthesis, as shown by the up-regulation of cholesterol biosynthesis-related genes Increased cholesterol biosynthesis is considered to be an indirect trigger for the reasons: (1) The accumulation of sphingomyelin occurs concurrently with the increase in cholesterol in visceral tissues (e.g., spleen) in patients with Niemann-Pick type C disease (NPC), which is caused by a genetic defect in the cholesterol trafficking protein NPC1 or, in far fewer patients, the sterol regulating protein HE1 (Blanchette-Mackie, 2000; Harzer et al., 2003; Vanier, 1983). (2) The induction of lamellar myelin-like bodies and the accumulation of free cholesterol occur in cultured mouse macrophages that have been incubated with acetylated low density lipoprotein or acyl-CoA:cholesterol acyl- transferase inhibitor (McGookey and Anderson, 1983; Robenek and Schmitz, 1988). In addition, the up- or down-regulation of transporter genes (e.g., facilitated glucose transporter) and genes that control the cell cycle (e.g., cyclin G2) may also be involved. Increase in phospholipid synthesis and impaired membrane recycling and lysosomal enzyme sorting dynamics are also occured. HOIP:HOIP_0003361 Dysfunction of fatty acid degradation is a subtype of hypofunctioning: A process that performs a decreased or insufficient lipid degradation. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). dysfunction of fatty acid degradation [non-alcoholic steatohepatitis (course)] HOIP_0003361 HOIP:HOIP_0003362 CAD insertion into phospholipase binding site to lysosomal inner membrane is a subtype of binding: A process that CAD inserts and replaces the phospholipase binding site in the lysosomal inner membrane. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). PMID:22960355 CAD insertion into phospholipase binding site to lysosomal inner membrane [phospholipidosis (mild)] HOIP_0003362 PMID:22960355 Under normal conditions, lysosomal phospholipase A2 is bound through electrostatic charge interactions to the inner membranes of the lysosome. A cationic amphiphile, accumulates in the lysosome and inserts into the inner membrane decreasing or eliminating the anionic binding sites for the lipase. The lipase is no longer able to bind to its substrates and is potentially susceptible to degradation by lysosomal proteases. HOIP:HOIP_0003363 Forming a complex of CAD and phospholipid is a subtype of forming a complex of drugs and biological substance: A process that forms a complex consisiting phospholipids and CAD (Cationic Amphiphilic Drug) in the lysosomal membrane, which causes structural change of the membrane. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). forming a complex of CAD and phospholipid [phospholipidosis (imbalance course)] HOIP_0003363 HOIP:HOIP_0003364 Forming a complex of CAD (Cationic Amphiphilic Drugs) and phospholipid is a subtype of forming a complex of drugs and biological substance: A process that forms a complex consisiting phospholipids and CAD in the lysosomal membrane, which causes structural change of the membrane. CAD decreases phospholipid release for cell membrane repair from lysosome. forming a complex of CAD and phospholipid HOIP_0003364 HOIP:HOIP_0003365 Forming a complex of CAD and phospholipid is a subtype of forming a complex of drugs and biological substance: A process that forms a complex consisiting phospholipids and CAD (Cationic Amphiphilic Drugs cationic amphiphile drug) in the lysosomal membrane, which causes structural change of the membrane. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). forming a complex of CAD and phospholipid [phospholipidosis (severe)] HOIP_0003365 HOIP:HOIP_0003366 Hypofunction of phospholipid export from lysosome is a subtype of hypofunction of export: A process that performs a decreased or insufficient phospholipid export from lysosome. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). hypofunction of phospholipid export from lysosome [phospholipidosis (moderate) ] HOIP_0003366 HOIP:HOIP_0003367 CAD accumulation in lysosome is a subtype of compound accumulation in lysosome: A process that keeps CAD (Cationic Amphiphilic Drug) in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). CAD accumulation in lysosome [phospholipidosis (imbalance course)] HOIP_0003367 HOIP:HOIP_0003368 CAD insertion into phospholipase binding site to lysosomal inner membrane is a subtype of binding: A process that CAD inserts and replaces the phospholipase binding site in the lysosomal inner membrane. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). PMID:22960355 CAD insertion into phospholipase binding site to lysosomal inner membrane [phospholipidosis (moderate) ] HOIP_0003368 PMID:22960355 Under normal conditions, lysosomal phospholipase A2 is bound through electrostatic charge interactions to the inner membranes of the lysosome. A cationic amphiphile, accumulates in the lysosome and inserts into the inner membrane decreasing or eliminating the anionic binding sites for the lipase. The lipase is no longer able to bind to its substrates and is potentially susceptible to degradation by lysosomal proteases. HOIP:HOIP_0003369 The totality of all processes through which the phospholipidosis is realized. The severity is moderate. PMID:15342952 PMID:16979167 PMID:22960355 phospholipidosis (moderate) HOIP_0003369 PMID:15342952 The following four processes were involved in the induction of phospholipidosis; (1) Inhibition of lysosomal phospholipase activivity (2) Inhibition of lysosomal enzyme transport, as demonstrated by the down-regulation of genes involved in lysosomal enzyme transport (3) Enhanced phospholipid biosynthesis, which is supported by the up- regulation of fatty acid biosynthesis-related genes (4) Enhanced cholesterol biosynthesis, as shown by the up-regulation of cholesterol biosynthesis-related genes Increased cholesterol biosynthesis is considered to be an indirect trigger for the reasons: (1) The accumulation of sphingomyelin occurs concurrently with the increase in cholesterol in visceral tissues (e.g., spleen) in patients with Niemann-Pick type C disease (NPC), which is caused by a genetic defect in the cholesterol trafficking protein NPC1 or, in far fewer patients, the sterol regulating protein HE1 (Blanchette-Mackie, 2000; Harzer et al., 2003; Vanier, 1983). (2) The induction of lamellar myelin-like bodies and the accumulation of free cholesterol occur in cultured mouse macrophages that have been incubated with acetylated low density lipoprotein or acyl-CoA:cholesterol acyl- transferase inhibitor (McGookey and Anderson, 1983; Robenek and Schmitz, 1988). In addition, the up- or down-regulation of transporter genes (e.g., facilitated glucose transporter) and genes that control the cell cycle (e.g., cyclin G2) may also be involved. Increase in phospholipid synthesis and impaired membrane recycling and lysosomal enzyme sorting dynamics are also occured. HOIP:HOIP_0003370 Phospholipid homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). phospholipid homeostasis imbalance [phospholipidosis (moderate) ] HOIP_0003370 HOIP:HOIP_0003371 Phospholipid accumulation in lysosome is a subtype of phospholipid accumulation: A process that keeps phospholipid in the lysosome. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). phospholipid accumulation in lysosome [phospholipidosis (moderate) ] HOIP_0003371 HOIP:HOIP_0003372 Phospholipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of phospholipid metabolism. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). phospholipid metabolism imbalance [phospholipidosis (moderate) ] HOIP_0003372 HOIP:HOIP_0003373 Glycerophospholipid accumulation in lysosome is a subtype of phospholipid accumulation in lysosome: A process that keeps glycerophospholipid in the lysosome. And the degree is moderate. This process is dependent on the glycerophospholipid disorder (moderate) and can constitute the course of Phospholipidosis. glycerophospholipid accumulation in lysosome [Phospholipidosis - glycerophospholipid disorder ] HOIP_0003373 HOIP:HOIP_0003374 A process that keeps phosphatidylinositol in the lysosome. This process can constitute the course of Phospholipidosis (phosphatidylinositol disorder ). phosphatidylinositol accumulation in lysosome [Phospholipidosis - phosphatidylinositol disorder] HOIP_0003374 HOIP:HOIP_0003375 A process that keeps phosphatidylethanolamine in the lysosome. This process can constitute the course of Phospholipidosis (phosphatidylethanolamine disorder). phosphatidylethanolamine accumulation in lysosome [Phospholipidosis - phosphatidylethanolamine disorder] HOIP_0003375 HOIP:HOIP_0003376 A process that keeps phosphatidylglycerol in the lysosome. This process can constitute the course of Phospholipidosis (phosphatidylglycerol disorder ). phosphatidylglycerol accumulation in lysosome [Phospholipidosis - phosphatidylglycerol disorder] HOIP_0003376 HOIP:HOIP_0003377 A process that keeps phosphatidylcholine in the lysosome. This process can constitute the course of Phospholipidosis (phosphatidylethanolamine disorder). phosphatidylcholine accumulation in lysosome [Phospholipidosis - phosphatidylcholine disorder] HOIP_0003377 HOIP:HOIP_0003378 A process that keeps phosphatidylserine in the lysosome. This process can constitute the course of Phospholipidosis (phosphatidylserine disorder). phosphatidylserine accumulation in lysosome [Phospholipidosis - phosphatidylserine disorder ] HOIP_0003378 HOIP:HOIP_0003379 A process that keeps phosphatidic acid in the lysosome. This process can constitute the course of Phospholipidosis　phosphatidic acid disorder). phosphatidic acid accumulation in lysosome [Phospholipidosis - phosphatidic acid disorder] HOIP_0003379 HOIP:HOIP_0003381 Sphingomyelin accumulation in lysosome is a subtype of phospholipid accumulation in lysosome: A process that keeps sphingomyelin in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. sphingomyelin accumulation in lysosome [sphingomyelin disorder (course)] HOIP_0003381 HOIP:HOIP_0003382 Phosphoipidosis is a subtype of process sequences: The courses of processes through which phospholipidosis is realized. PMID:15342952 PMID:16979167 PMID:22960355 phospholipidosis (course) HOIP_0003382 HOIP:HOIP_0003383 Phosholipase gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature phospholipase gene product or products (proteins or RNA). phosholipase gene expression HOIP_0003383 HOIP:HOIP_0003384 Phosholipase gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature phospholipase gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). phosholipase gene expression [phospholipidosis (normal course)] HOIP_0003384 HOIP:HOIP_0003385 Hyperfunction of phospholipid synthesis gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive phospholipid synthetic gene expression. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). hyperfunction of phospholipid synthesis gene expression [phospholipidosis (normal course)] HOIP_0003385 HOIP:HOIP_0003386 Increasing phospholipid is a subtype of increasing quantity: A process that changes the amount of phospholipid to be larger. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). increasing phospholipid [phospholipidosis (normal course)] HOIP_0003386 HOIP:HOIP_0003387 The chemical reactions and pathways resulting in the formation of phospholipids, any lipid containing phosphoric acid as a mono- or diester. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). phospholipid biosynthetic process [phospholipidosis (normal course)] HOIP_0003387 HOIP:HOIP_0003388 Phospholipid transport from lysosome into cytosol is a subtype of phospholipid transfer to membrane: A process of the transfer of a phospholipid from the lysosome to the plasma membrane. phospholipid transport from lysosome HOIP_0003388 HOIP:HOIP_0003390 Decreasing number of cells is a subtype of decreasing number of objects: A process that becomes smaller in number of cells. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). decreasing number of cells [phospholipidosis (normal course)] HOIP_0003390 HOIP:HOIP_0003391 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. PMID:17090686 apoptotic process [phospholipidosis (normal course)] HOIP_0003391 PMID:17090686 Sphingosine-1-phosphate lyase potentiates apoptosis via p53- and p38-dependent pathways and is down-regulated in colon cancer. HOIP:HOIP_0003392 Hyperfunctioning of apoptotic process is a subtype of hyperfunctioning: A process that performs an excesssive apoptosis. hyperfunctioning of apoptotic process HOIP_0003392 HOIP:HOIP_0003393 Decreasing number of lysosomes is a subtype of decreasing number of objects: A process that becomes smaller in number of lysosomes. decreasing number of lysosomes HOIP_0003393 HOIP:HOIP_0003394 Decreasing number of lysosomes is a subtype of decreasing number of objects: A process that becomes smaller in number of lysosomes. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). decreasing number of lysosomes [phospholipidosis (normal course)] HOIP_0003394 HOIP:HOIP_0003395 Removing phospholipid by Kupffer cell or macrophage is a subtype of removing: A process that takes a phospholipid from a cell by Kupffer cells or macrophages . This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). removing phospholipid by Kupffer cell or macrophage [phospholipidosis (normal course)] HOIP_0003395 HOIP:HOIP_0003396 Removing phospholipid by Kupffer cell or macrophage is a subtype of removing: A process that takes a phospholipid from a cell by Kupffer cells or macrophages . removing phospholipid by Kupffer cell or macrophage HOIP_0003396 HOIP:HOIP_0003397 Phospholipid synthesis gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature phospholipid synthesis gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). phospholipid synthesis gene expression [phospholipidosis (normal course)] HOIP_0003397 HOIP:HOIP_0003398 Phospholipid synthesis gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature phospholipid synthesis gene product or products (proteins or RNA). phospholipid synthesis gene expression HOIP_0003398 HOIP:HOIP_0003400 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of phospholipids. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). positive regulation of phospholipid biosynthetic process [phospholipidosis (normal course)] HOIP_0003400 HOIP:HOIP_0003401 Moving phopholipid to lysosome is a subtype of moving A to the inside of B: A process that of the movement of phospholipids into lysosomes. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). moving phopholipid to lysosome [phospholipidosis (normal course)] HOIP_0003401 HOIP:HOIP_0003402 Moving phopholipid to lysosome is a subtype of moving A to the inside of B: A process that of the movement of phospholipids into lysosomes. moving phopholipid to lysosome HOIP_0003402 HOIP:HOIP_0003403 Increasing phospholipid material is a subtype of increasing quantity: A process that changes the amount of phospholipid material to be larger. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). increasing phospholipid material [phospholipidosis (normal course)] HOIP_0003403 HOIP:HOIP_0003404 Phosphholipid binding by phospholipase is a subtype of phospholipid binding: Interacting selectively and non-covalently with phospholipids byphospholipases. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). ホスホリパーゼによるリン脂質結合 phosphholipid binding by phospholipase [phospholipidosis (normal course)] HOIP_0003404 HOIP:HOIP_0003405 IL-2 signaling is a process that a signal is transmitted by the cytokine IL-2. This process is dependent on the inflammation and can constitute the course of phospholipidosis (severe (excessive defense)) . PMID:28732506 Reactome:R-HSA-451927.2 IL-2 signaling [phospholipidosis (severe (excessive defense)) - inflammation ] HOIP_0003405 PMID:28732506 Blimp-1 is also crucial for inducing cytokine production by inflammatory T helper cells and effector Treg cells. The gene encoding IL-2 is one of the most important genes targeted by Blimp-1 in T cells, because IL-2 production is indispensable for T cell proliferation and differentiation HOIP:HOIP_0003406 IL-2 signaling is a process that a signal is transmitted by the cytokine IL-2. This process is dependent on the apoptosis inhibition and can constitute the course of phospholipidosis (severe (excessive defense)) . Reactome:R-HSA-451927.2 IL-2 signaling [phospholipidosis (severe (excessive defense))- apoptosis inhibition ] HOIP_0003406 PMID:9108028 HOIP:HOIP_0003407 IL-2 signaling is a process that a signal is transmitted by the cytokine IL-2. This process is dependent on the cell cycle arrest and can constitute the course of phospholipidosis (severe (excessive defense)) . Reactome:R-HSA-451927.2 IL-2 signaling [phospholipidosis (severe (excessive defense)) - cell cycle arrest ] HOIP_0003407 PMID:9108028 HOIP:HOIP_0003410 Phospholipid hydrolysis is a subtype of hydrolysis: A chemical reaction that uses water to break down a phospholipid. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). phospholipase activity http://purl.obolibrary.org/obo/GO_0004620 phospholipid hydrolysis [phospholipidosis (normal course)] HOIP_0003410 HOIP:HOIP_0003411 Phospholipid hydrolysis is a subtype of hydrolysis: A chemical reaction that uses water to break down a phospholipid. phospholipid hydrolysis HOIP_0003411 HOIP:HOIP_0003412 A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid hydrolysis mildly. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). negative regulation of phospholipid hydrolysis [phospholipidosis (mild)] HOIP_0003412 HOIP:HOIP_0003413 Negative regulation of phospholipid degradation is a subtype of negative regulation of phospholipid hydrolysis: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid hydrolysis. negative regulation of phospholipid hydrolysis HOIP_0003413 HOIP:HOIP_0003414 Negative regulation of phospholipase-mediated phospholipid degradation by CAD is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase-mediated phospholipid deradation regulated by CAD. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). negative regulation of phospholipase-mediated phospholipid degradation by CAD [phospholipidosis (imbalance course)] HOIP_0003414 HOIP:HOIP_0003415 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). This process is dependent on the cell proliferation and can constitute the course of phospholipidosis (severe (excessive defense)) . AKT signaling [phospholipidosis (severe (excessive defense)) - cell proliferation ] HOIP_0003415 HOIP:HOIP_0003416 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). This process is dependent on the tumor cell proliferation and can constitute the course of phospholipidosis (severe (excessive defense)) . AKT signaling [phospholipidosis (severe (excessive defense))- tumor cell proliferation ] HOIP_0003416 HOIP:HOIP_0003418 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). This process is dependent on the cell proliferation and can constitute the course of phospholipidosis (severe (excessive defense)) . phosphatidylinositol 3-kinase signaling [phospholipidosis (severe (excessive defense)) - cell proliferation ] HOIP_0003418 HOIP:HOIP_0003421 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). This process is dependent on the tumor cell proliferation and can constitute the course ofphospholipidosis (severe (excessive defense)) . phosphatidylinositol 3-kinase signaling [phospholipidosis (severe (excessive defense)) - tumor cell proliferation ] HOIP_0003421 HOIP:HOIP_0003422 EGFR signaling is a subtype of signaling that a signal is transmitted by the EGFR (epidermal growth factor receptor) on the surface of a cell, starting with a ligand binding to a EGFR This process is dependent on the cell proliferation and can constitute the course of phospholipidosis (severe (excessive defense)) . EGFR signaling [phospholipidosis (severe (excessive defense)) - cell proliferation ] HOIP_0003422 PMID:12414665 HOIP:HOIP_0003423 EGFR signaling is a subtype of signaling that a signal is transmitted by the EGFR (epidermal growth factor receptor) on the surface of a cell, starting with a ligand binding to a EGFR This process is dependent on the tumor cell proliferation and can constitute the course of phospholipidosis (severe (excessive defense)) . EGFR signaling [phospholipidosis (severe (excessive defense)) - tumor cell proliferation ] HOIP_0003423 PMID:12414665 HOIP:HOIP_0003430 Kupffer cell differentiation is a subtype of macrophage differentiation: The process that acquires the specialized features of a kupffer cell. The process in which a relatively unspecialized monocyte acquires the specialized features of a Kupffer cell. kupffer cell differentiation HOIP_0003430 HOIP:HOIP_0003431 Hyperfunction of phospholipid phagocytosis by Kupffer cells is a subtype of hyperfunctioning: A process that performs an excessive phospholipid phagocytosis by Kupffer cells. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). hyperfunction of phospholipid phagocytosis by Kupffer cells [Phospholipidosis (excessive defense)] HOIP_0003431 HOIP:HOIP_0003432 Hyperfunction of phospholipid phagocytosis by Kupffer cells is a subtype of hyperfunctioning: A process that performs an excessive phospholipid phagocytosis by Kupffer cells. hyperfunction of phospholipid phagocytosis by Kupffer cells HOIP_0003432 HOIP:HOIP_0003433 Hyperfunction of cell differentiation is a subtype of hyperfunctioning: A process that performs an excesssive cell differentiation. hyperfunction of cell differentiation HOIP_0003433 HOIP:HOIP_0003434 Hyperfunction of Kupffer cell differentiation is a subtype of hyperfunction of cell differentiation: A process that performs an excesssive kupffer cell differentiation. hyperfunction of Kupffer cell differentiation HOIP_0003434 HOIP:HOIP_0003435 Phospholipid homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). phospholipid homeostasis imbalance [phospholipidosis (severe)] HOIP_0003435 HOIP:HOIP_0003436 Decreasing lysosomal membrane permeability is a subtype of decreasing membrane permeability: A process that changes the permeability of the lysosomal membrane to be lower. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). decreasing lysosomal membrane permeability [phospholipidosis (severe)] HOIP_0003436 HOIP:HOIP_0003437 in vitro (human) 8hr HOIP_0003437 HOIP:HOIP_0003438 Decreasing lysosomal membrane permeability is a subtype of decreasing membrane permeability: A process that changes the permeability of the lysosomal membrane to be lower. decreasing lysosomal membrane permeability HOIP_0003438 HOIP:HOIP_0003439 Decreasing membrane permeability is a subtype of changing permeability: A process that changes the permeability of the membrane to be lower. decreasing membrane permeability HOIP_0003439 HOIP:HOIP_0003440 Hyperfunction of phospholipid material transport is a subtype of hyperfunction of transport: A process that performs an excesssive phospholipid material transport. hyperfunction of phospholipid material transport HOIP_0003440 HOIP:HOIP_0003441 Combining role with a pathogen-associated molecular pattern (PAMP), a structure conserved among microbial species, or damage-associated molecular pattern (DAMP), an endogenous molecule released from damaged cells), to initiate a change in cell activity. Receptors of the innate immune system that recognize pathogen associated molecular patterns (PAMPs, e.g. LPS) are called pattern recognition receptors (PRRs). Receptors of the innate immune system that recognize pathogen associated molecular patterns (PAMPs, e.g. LPS) are called pattern recognition receptors (PRRs). IMR:0001791 (obsolete) PRR related molecular function GO:0038187 pattern recognition receptor HOIP_0003441 Receptors of the innate immune system that recognize pathogen associated molecular patterns (PAMPs, e.g. LPS) are called pattern recognition receptors (PRRs). PMID:11724812 PMID:16697918 HOIP:HOIP_0003442 Negative regulation of phospholipase-mediated phospholipid degradation by CAD is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase-mediated phospholipid deradation regulated by CAD. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). negative regulation of phospholipase-mediated phospholipid degradation by CAD [phospholipidosis (moderate) ] HOIP_0003442 HOIP:HOIP_0003443 A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid hydrolysis moderately. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). hydrolysis of a phospholipid ホスホリパーゼ (phospholipase) は、リン脂質を脂肪酸とその他の親油性物質に加水分解する phospholipase activity - Gene Ontology (GO) http://purl.obolibrary.org/obo/GO_0004620 negative regulation of phospholipid hydrolysis [phospholipidosis (moderate) ] HOIP_0003443 HOIP:HOIP_0003444 A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid degradation. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). negative regulation of phospholipid degradation [phospholipidosis (moderate) ] HOIP_0003444 HOIP:HOIP_0003445 Hypofunction of ceramide degradation is a subtype of hypofunction of lipid degradation: A process that performs a decreased or insufficient ceramide degradation. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. hypofunction of ceramide degradation [sphingomyelin disorder (course)] HOIP_0003445 HOIP:HOIP_0003446 Negative regulation of phospholipase-mediated phospholipid degradation by CAD is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid deradation by phospholipase. negative regulation of phospholipase-mediated phospholipid degradation by CAD HOIP_0003446 HOIP:HOIP_0003447 A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid hydrolysis severely. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). Phospholipases hydrolyze phospholipids into fatty acids and other lipophilic substances. This entity indicates mainly to the process of inhibiting phospholipases. negative regulation of phospholipid hydrolysis [phospholipidosis (severe)] HOIP_0003447 HOIP:HOIP_0003448 Negative regulation of phospholipid hydrolysis is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid hydrolysis. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. negative regulation of phospholipid hydrolysis [phospholipidosis (imbalance course)] HOIP_0003448 HOIP:HOIP_0003449 CAD insertion into phospholipase binding site to lysosomal inner membrane is a subtype of binding: A process that CAD inserts and replaces the phospholipase binding site in the lysosomal inner membrane. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID:22960355 CAD insertion into phospholipase binding site to lysosomal inner membrane [phospholipidosis (severe)] HOIP_0003449 PMID:22960355 Under normal conditions, lysosomal phospholipase A2 is bound through electrostatic charge interactions to the inner membranes of the lysosome. A cationic amphiphile, accumulates in the lysosome and inserts into the inner membrane decreasing or eliminating the anionic binding sites for the lipase. The lipase is no longer able to bind to its substrates and is potentially susceptible to degradation by lysosomal proteases. HOIP:HOIP_0003450 Negative regulation of phospholipase-mediated phospholipid degradation by CAD is a subtype of negative regulation of phospholipid degradation: A process that stops, prevents, or reduces the frequency, rate or extent of phospholipase-mediated phospholipid deradation regulated by CAD. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). negative regulation of phospholipase-mediated phospholipid degradation by CAD [phospholipidosis (severe)] HOIP_0003450 HOIP:HOIP_0003451 CAD accumulation in lysosome is a subtype of compound accumulation in lysosome: A process that keeps CAD (Cationic Amphiphilic Drugs cationic amphiphile drug) in the lysosome. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). CAD accumulation in lysosome [phospholipidosis (severe)] HOIP_0003451 HOIP:HOIP_0003452 The totality of all processes through which the phospholipidosis is realized. The severity is severe. PMID:15342952 PMID:16979167 PMID:22960355 phospholipidosis (severe) HOIP_0003452 PMID:15342952 The following four processes were involved in the induction of phospholipidosis; (1) Inhibition of lysosomal phospholipase activivity (2) Inhibition of lysosomal enzyme transport, as demonstrated by the down-regulation of genes involved in lysosomal enzyme transport (3) Enhanced phospholipid biosynthesis, which is supported by the up- regulation of fatty acid biosynthesis-related genes (4) Enhanced cholesterol biosynthesis, as shown by the up-regulation of cholesterol biosynthesis-related genes Increased cholesterol biosynthesis is considered to be an indirect trigger for the reasons: (1) The accumulation of sphingomyelin occurs concurrently with the increase in cholesterol in visceral tissues (e.g., spleen) in patients with Niemann-Pick type C disease (NPC), which is caused by a genetic defect in the cholesterol trafficking protein NPC1 or, in far fewer patients, the sterol regulating protein HE1 (Blanchette-Mackie, 2000; Harzer et al., 2003; Vanier, 1983). (2) The induction of lamellar myelin-like bodies and the accumulation of free cholesterol occur in cultured mouse macrophages that have been incubated with acetylated low density lipoprotein or acyl-CoA:cholesterol acyl- transferase inhibitor (McGookey and Anderson, 1983; Robenek and Schmitz, 1988). In addition, the up- or down-regulation of transporter genes (e.g., facilitated glucose transporter) and genes that control the cell cycle (e.g., cyclin G2) may also be involved. Increase in phospholipid synthesis and impaired membrane recycling and lysosomal enzyme sorting dynamics are also occured. HOIP:HOIP_0003453 Compound accumulation in lysosome is a subtype of accumulation of xenobiotics: A process that keeps compound in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). compound accumulation in lysosome [phospholipidosis (mild)] HOIP_0003453 HOIP:HOIP_0003454 Compound accumulation in lysosome is a subtype of accumulation of xenobiotics: A process that keeps compound in the lysosome. And the degree is moderate. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (moderate). compound accumulation in lysosome [phospholipidosis (moderate) ] HOIP_0003454 HOIP:HOIP_0003455 Negative regulation of cell cycle regulator gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of cell cycle regulator gene expression. negative regulation of cell cycle gene expression HOIP_0003455 HOIP:HOIP_0003462 Increasing size of the spleen is a subtype of increasing size: A process that changes the size of the of the spleen to be larger. This entity is a specific course-dependent process. This process can constitute the course of hepatic blood circulatory disorder. increasing size of the spleen [hepatic blood circulatory disorder] HOIP_0003462 HOIP:HOIP_0003465 Intestine congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the intestine. intestine congestion HOIP_0003465 HOIP:HOIP_0003467 Varicosity of veins formation is a subtype of biological structure formation: A process that have a varicosity of veins. This entity is a specific course-dependent process. This process can constitute the course of hepatic blood circulatory disorder. varicosity of veins formation [hepatic blood circulatory disorder] HOIP_0003467 HOIP:HOIP_0003468 Sphingomyelinase gene mutation is a subtype of phopholipase gene mutation: A process that changes the sequence of a sphingomyelinase gene. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. sphingomyelinase gene mutation [course of Niemann–Pick disease type A] HOIP_0003468 HOIP:HOIP_0003471 NCBI-Human-GeneID:4189 PMID:25146923 PMID:28452953 ERDJ4 DNAJB9 - apotosis repressor -vitro (human)[ER stress] HOIP_0003471 NCBI-Human-GeneID:4189 http://www.ncbi.nlm.nih.gov/gene/4189 PMID:25146923 Genotoxic stress/p53-induced DNAJB9 inhibits the pro-apoptotic function of p53. DNAJB9 as an inducible gene of the tumor suppressor p53. DNAJB9 expression was induced by p53 or genotoxic stress in a p53-dependent manner, which was mediated by the Ras/Raf/ERK pathway. In addition, depletion of DNAJB9 by using siRNAs greatly increased genotoxic stress/p53-induced apoptosis, suggesting that DNAJB9 inhibits the pro-apoptotic function of p53. PMID:28452953 DNABJ9 suppresses apoptosis in response to chemotherapeutic agents by forming a negative regulatory loop with p53. HOIP:HOIP_0003473 Sphingomyelinase gene mutation is a subtype of phopholipase gene mutation: A process that changes the sequence of a sphingomyelinase gene. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. sphingomyelinase gene mutation [course of Niemann–Pick disease type B] HOIP_0003473 HOIP:HOIP_0003474 Dysfunction of sphingomyelin degradation is a subtype of dysfunction of phosphosphingolipid degradation: A process that performs an abnormal and incomplete sphingomyelin degradation. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. dysfunction of sphingomyelin degradation [course of Niemann–Pick disease type A] HOIP_0003474 HOIP:HOIP_0003475 Dysfunction of sphingomyelin degradation is a subtype of dysfunction of phosphosphingolipid degradation: A process that performs an abnormal and incomplete sphingomyelin degradation. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. dysfunction of sphingomyelin degradation [course of Niemann–Pick disease type B] HOIP_0003475 HOIP:HOIP_0003476 Lipid accumulation in hepatocyte (severe) is a subtype of lipid strorage in hepatocyte: A process that keeps lipids in hepatocytes. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). lipid storage in hepatocyte (severe) [Lipidosis] lipid accumulation in hepatocyte (severe) [non-alcoholic steatohepatitis (course)] HOIP_0003476 HOIP:HOIP_0003478 Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). positive regulation of autophagy [non-alcoholic steatohepatitis (course)] HOIP_0003478 HOIP:HOIP_0003480 Increasing hepatocellular volume is a changing process to change the volume of the hepatocyte to increase. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). increasing hepatocellular volume [non-alcoholic steatohepatitis (course)] HOIP_0003480 HOIP:HOIP_0003481 Hyperfunction of glucose transport to liver is a subtype of hyperfunction of transport: A process that performs an excesssive glucose transport to liver. hyperfunction of glucose transport to liver HOIP_0003481 HOIP:HOIP_0003482 Hyperfunction of glucose transport to liver is a subtype of hyperfunction of transport: A process that performs an excesssive glucose transport to liver. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). hyperfunction of glucose transport to liver [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003482 HOIP:HOIP_0003483 Hypofunction of triglyceride transport from hepatocyte to extrahepatic is a subtype of hypofunction of transport: A process that performs a decreased or insufficient triglyceride transport from hepatocyte to extrahepatic. hypofunction of triglyceride transport from hepatocyte to extrahepatic HOIP_0003483 HOIP:HOIP_0003484 Hypofunction of triglyceride transport from hepatocyte to extrahepatic is a subtype of hypofunction of transport: A process that performs a decreased or insufficient triglyceride transport from hepatocyte to extrahepatic. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). hypofunction of triglyceride transport from hepatocyte to extrahepatic [lipidosis (imbalance course)] HOIP_0003484 HOIP:HOIP_0003485 HSP90B1 - apotosis repressor -vitro (human)[ER stress] HOIP_0003485 HOIP:HOIP_0003486 Triglyceride transport from hepatocyte to extrahepatic is a subtype of triglyceride transport: A process that of the transfer of a triglyceride from the hepatocyte to the exrrahepatic tissues. triglyceride transport from hepatocyte to extrahepatic HOIP_0003486 HOIP:HOIP_0003487 Triglyceride transport from hepatocyte to extrahepatic is a subtype of triglyceride transport: A process that of the transfer of a triglyceride from the hepatocyte to the exrrahepatic tissues. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (normal course). triglyceride transport from hepatocyte to extrahepatic [lipidosis (normal course)] HOIP_0003487 HOIP:HOIP_0003488 Lipid homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a lipid homeostastasis balance. lipid homeostasis imbalance lipid homeostasis imbalance HOIP_0003488 HOIP:HOIP_0003489 GRP78 - apotosis repressor (canonical)[ER stress] HOIP_0003489 HOIP:HOIP_0003490 Tumor cell survial is a subtype of cell survival: A process that keeps the viability of a tumor cell. This entity is a specific course-dependent process. This process can constitute the course of ER stress. tumor cell survial [ER stress] HOIP_0003490 HOIP:HOIP_0003491 Lipid homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a lipid homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of llipidosis (imbalance course)]. lipid homeostasis imbalance [lipidosis (imbalance course)] HOIP_0003491 HOIP:HOIP_0003492 Increaing in fatty acid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the fatty acid inflow into the hepatocyte to be larger. increaing in fatty acid inflow into hepatocyte HOIP_0003492 HOIP:HOIP_0003493 Increase in lipid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the lipid inflow into the hepatocyte to be larger. increase in lipid inflow into hepatocyte HOIP_0003493 HOIP:HOIP_0003494 Increase in lipid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the lipid inflow into the hepatocyte to be larger. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course) increase in lipid inflow into hepatocyte [lipidosis (imbalance course)] HOIP_0003494 HOIP:HOIP_0003495 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). necrosis [non-alcoholic steatohepatitis (course)] HOIP_0003495 HOIP:HOIP_0003496 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:26006114 insulin resistance (process) [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003496 PMID:26006114 Insulin resistance alters hepatic ethanol metabolism: studies in mice and children with non-alcoholic fatty liver disease. HOIP:HOIP_0003498 The totality of all processes through which non-alcoholic fatty liver disease (NAFLD) is realized. PMID:24133660 PMID:26962021 PMID:30642126 non-alcoholic fatty liver disease (NAFLD) HOIP_0003498 HOIP:HOIP_0003499 Fatty change [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed as lipid droplets consisting of neutral fat in the hepatocyte based on pathological morphology. This finding is observable in the course of lipidosis. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. vacuolation [Liver Pathological Findings] [lipidosis (imbalance course)]] HOIP_0003499 A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0003501 Eosinophilic granular degeneration [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed in the form that the cytoplasm presents eosinophilic granules based on pathological morphology. FI-L510 eosinophilic granular degeneration [Liver Pathological Findings] HOIP_0003501 HOIP:HOIP_0003502 Hypertrophy [liver findings] is a type of finding observed in the liver. An increase in size (volume) of hepatocytes is observed based on pathological morphology. It is sometimes accompanied by an increase in the number of cells. hepatocellular hypertrophy [Liver Pathological Findings] HOIP_0003502 HOIP:HOIP_0003503 Cholestasis [liver findings] is a type of finding observed in the liver. A pathological findings caused by obstruction in intrahepatic or extrahepatic biliary system. Bile thrombus appears in the intrahepatic bile duct, and in general, bile pigment is observed in hepatocytes and Kupffer cells. Open TG-Gates:FI-L0360 cholestasis [Liver Pathological Findings] HOIP_0003503 HOIP:HOIP_0003504 Hyperplasia [ [Liver PathologicalFindings] is a type of finding observed in the liver. An increase in cell number is observed based on pathological morphology. Open TG-Gates:FI-L0910 hyperplasia [Liver Pathological Findings] HOIP_0003504 HOIP:HOIP_0003505 Hepatic fibrosis [Liver PathologicalFindings] is a type of finding observed in the liver. Lesions are observed as a proliferation of fibrous tissue in the liver based on pathological morphology. FI-L0780 hepatic fibrosis [Liver Pathological Findings] HOIP_0003505 HOIP:HOIP_0003506 Hypofunction of lipoprotein biosynthesis is a subtype of hypofunction of protein synthesis: A process that performs a decreased or insufficient lipoprotein biosynthesis. hypofunction of lipoprotein biosynthesis HOIP_0003506 HOIP:HOIP_0003507 Hypofunction of lipoprotein biosynthesis is a subtype of hypofunction of protein synthesis: A process that performs a decreased or insufficient lipoprotein biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of lipidosis (imbalance course). 肝臓で生成されたTGが血中に放出される場合、タンパクと重合し、ＶＬＤＬリポ蛋白となる。栄養障害でタンパク質が不足してくると、脂質と重合するタンパク質が不足、リポタンパク産生が低下する。→脂質放出できず。 hypofunction of lipoprotein biosynthesis [lipidosis (imbalance course)] HOIP_0003507 HOIP:HOIP_0003508 Lipidosis dependent chemical compound is a subtype of course dependent chemical entity. This entity (drug) can participate in the course of lipidosis. lipidosis dependent chemical compound HOIP_0003508 HOIP:HOIP_0003509 ISBN:0071769234 CCL4 [Lipidosis] HOIP_0003509 ISBN:0071769234 Types of hepatobiliary injury: Fatty liver: Amiodarone, CCl4, ethanol, fialuridine, tamoxifen, valproic acid in Table 13-2. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0003510 Increasing demand for response to oxidative stress is a subtype of increasing the demand for stress response : A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). Because the mitochondrial pathway is saturated, fatty acids are metabolized in peroxisomes, and Cyp2E1 enzyme induction occurs, resulting in oxidative stress. Because the mitochondrial pathway is saturated, fatty acids are metabolized in peroxisomes, and Cyp2E1 enzyme induction occurs, resulting in oxidative stress. increasing demand for response to oxidative stress [non-alcoholic steatohepatitis (course)] HOIP_0003510 Because the mitochondrial pathway is saturated, fatty acids are metabolized in peroxisomes, and Cyp2E1 enzyme induction occurs, resulting in oxidative stress. ISBN:4890133267 HOIP:HOIP_0003511 Malfunctioning of cellular membrane is a subtype of malfunctioning process: A process that cannot perform a cellular membrane function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). malfunctioning of cellular membrane [non-alcoholic steatohepatitis (course)] HOIP_0003511 HOIP:HOIP_0003512 Cellular membrane lipoperoxidation is a subtype of lipoperoxidation: A process that the degradation of lipids of cellular membrane caused by an oxidative attack from free radicals. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course) cellular membrane lipoperoxidation [non-alcoholic steatohepatitis (course) HOIP_0003512 HOIP:HOIP_0003513 Cellular membrane lipoperoxidation is a subtype of lipoperoxidation: A process that the degradation of lipids of cellular membrane caused by an oxidative attack from free radicals. cellular membrane lipoperoxidation HOIP_0003513 HOIP:HOIP_0003514 Lipoperoxidation is a subtype of lipid oxidation: The degradation of lipids caused by an oxidative attack from free radicals. http://purl.obolibrary.org/obo/NCIT_C81870 lipoperoxidation HOIP_0003514 HOIP:HOIP_0003515 Eosinophilic change [Liver PathologicalFindings] is a type of finding observed in hepatocyte cytoplasm. Based on pathological morphology, lesions are stained with eosin. · Stained with eosinophilic (eosinophilic) dye of hepatic cytoplasm. · Generally, it is caused by diffuse or focal increase of cytoplasmic organelle or excessive accumulation of eosinophilic substance. · Eosinophilic staining area: It often corresponds to mitochondria, smooth endoplasmic reticulum, or peroxisome. · Changes over the entire cytoplasm: granule degeneration, eosinophilic granular change, glute-like change · Cytoplasmic local changes: vitreous, eosinophilic inclusion bodies etc. · Stained with eosinophilic (eosinophilic) dye of hepatic cytoplasm. · Generally, it is caused by diffuse or focal increase of cytoplasmic organelle or excessive accumulation of eosinophilic substance. · Eosinophilic staining area: It often corresponds to mitochondria, smooth endoplasmic reticulum, or peroxisome. · Changes over the entire cytoplasm: granule degeneration, eosinophilic granular change, glute-like change · Cytoplasmic local changes: vitreous, eosinophilic inclusion bodies etc. acidophilic change eosinophilic change [Liver Pathological Findings] HOIP_0003515 · Stained with eosinophilic (eosinophilic) dye of hepatic cytoplasm. · Generally, it is caused by diffuse or focal increase of cytoplasmic organelle or excessive accumulation of eosinophilic substance. · Eosinophilic staining area: It often corresponds to mitochondria, smooth endoplasmic reticulum, or peroxisome. · Changes over the entire cytoplasm: granule degeneration, eosinophilic granular change, glute-like change · Cytoplasmic local changes: vitreous, eosinophilic inclusion bodies etc. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0003516 Lipidosis dependent molecule is a subtype of course dependent chemical entity. This molecule can participate in the course of lipidosis as a gene product. Gene profile:caonical that described in textbooks or articles. lipidosis dependent molecule (canonical) HOIP_0003516 HOIP:HOIP_0003517 The protein encoded by this gene is a major apoprotein of the chylomicron. It binds to a specific liver and peripheral cell receptor, and is essential for the normal catabolism of triglyceride-rich lipoprotein constituents. This gene maps to chromosome 19 in a cluster with the related apolipoprotein C1 and C2 genes. Mutations in this gene result in familial dysbetalipoproteinemia, or type III hyperlipoproteinemia (HLP III), in which increased plasma cholesterol and triglycerides are the consequence of impaired clearance of chylomicron and VLDL remnants. [provided by RefSeq, Jun 2016] NCBI-Human-GeneID:348 NCBI-Mouse-GeneID:11816 NCBI-Rat-GeneID:25728 http://omim.org/entry/107741 APOE (canonical)[Lipidosis] HOIP_0003517 NCBI-Human-GeneID:348 http://www.ncbi.nlm.nih.gov/gene/348 NCBI-Mouse-GeneID:11816 http://www.ncbi.nlm.nih.gov/gene/11816 NCBI-Rat-GeneID:25728 http://www.ncbi.nlm.nih.gov/gene/25728 HOIP:HOIP_0003518 An affinity inhering in a tissue constituent by virtue of the bearer exhibiting a molecular interaction for acidic dyes under specific ph conditions. acidophilic HOIP_0003518 HOIP:HOIP_0003520 Metabolic intermediate accumulation is a subtype of accumulation of substances in a biological object: A process that keeps intermediate(s) of metabolism in an organism, tissue, organelle, or cell. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. metabolic intermediate accumulation [glutathione depletion (course)] HOIP_0003520 HOIP:HOIP_0003521 A physical attribute inhering in a bearer by virtue of the bearer's rate of doing work. power (attribute) HOIP_0003521 HOIP:HOIP_0003522 Ground glass appearance [Liver PathologicalFindings] is a type of finding observed in hepatocyte cytoplasm. Based on the pathological morphology, lesions are observed as a frosted-like change in whole or most of the hepatocytes. This finding is observable in the course of ground glass appearance. ground glass appearance [Liver Pathological Findings] [Ground glass appearance (course)] HOIP_0003522 HOIP:HOIP_0003523 Eosinophilic granular degeneration [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed in the form that the cytoplasm presents eosinophilic granules based on pathological morphology. This finding is observable as a result of increasing peroxisome caused by PPAR. eosinophilic granular degeneration [Liver Pathological Findings] [eosinogranular degeneration (course) ] HOIP_0003523 HOIP:HOIP_0003524 Fatty change [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed as lipid droplets consisting of neutral fat in the hepatocyte based on pathological morphology. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. Open TG-Gates:FI-L1580 fatty degeneration [Liver PathologicalFindings] steatosis [Liver PathologicalFindings] vacuolation [Liver PathologicalFindings] fatty change [Liver Pathological Findings] HOIP_0003524 A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0003525 Fatty change [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed as lipid droplets consisting of neutral fat in the hepatocyte based on pathological morphology. This finding is observable in the course of phospholipidosis. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. vacuolation [Liver Pathological Findings][phospholipidosis (severe)] HOIP_0003525 A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0003526 myelin figure in lysosome [Liver Pathological Findings] is a type of finding observed in the liver. Based on pathological morphology, lesions are observed as myelin-like layered structures under electron microscopy. This finding is observable in the course of phospholipidosis. The presence of phospholipid inclusions are characterized by the presence of cytoplasmic vacuoles seen under the electron microscope as dense cytoplasmic myelin-like bodies showing a concentric lamellar structure with a periodicity of 4-4.5 nm along with an amorphorous matrix within a single membrane-bound lysosomal space. Histopathology of preclinical toxicity studies : interpretation and relevance in drug safety studies, Peter Greaves. 4th ed. Amsterdam ; Boston : Elsevier/AP, 2012. The presence of phospholipid inclusions are characterized by the presence of cytoplasmic vacuoles seen under the electron microscope as dense cytoplasmic myelin-like bodies showing a concentric lamellar structure with a periodicity of 4-4.5 nm along with an amorphorous matrix within a single membrane-bound lysosomal space. Histopathology of preclinical toxicity studies : interpretation and relevance in drug safety studies, Peter Greaves. 4th ed. Amsterdam ; Boston : Elsevier/AP, 2012. myelin figure in lysosome [phospholipidosis] HOIP_0003526 The presence of phospholipid inclusions are characterized by the presence of cytoplasmic vacuoles seen under the electron microscope as dense cytoplasmic myelin-like bodies showing a concentric lamellar structure with a periodicity of 4-4.5 nm along with an amorphorous matrix within a single membrane-bound lysosomal space. Histopathology of preclinical toxicity studies : interpretation and relevance in drug safety studies, Peter Greaves. 4th ed. Amsterdam ; Boston : Elsevier/AP, 2012. https://www.worldcat.org/title/histopathology-of-preclinical-toxicity-studies-interpretation-and-relevance-in-drug-safety-evaluation/oclc/778774101 HOIP:HOIP_0003527 Moderate accumulation of abnormal proteins in ER is a subtype of accumulation of abnormal proteins in ER: A process that keeps abnormal protein(s) in the ER (endoplasmic reticulum) moderately. moderate accumulation of abnormal proteins in ER HOIP_0003527 HOIP:HOIP_0003528 Severe accumulation of abnormal proteins in ER is a subtype of accumulation of abnormal proteins in ER: A process that keeps abnormal protein(s) in the ER (endoplasmic reticulum) severely. severe accumulation of abnormal proteins in ER HOIP_0003528 HOIP:HOIP_0003532 Refolding-unfolding imbalance (mild) is a subtype of refolding-unfolding imbalance: A process that lacks a balance between protein refolding and unfolding mildly. refolding-unfolding imbalance (mild) HOIP_0003532 HOIP:HOIP_0003533 Refolding-unfolding imbalance (moderate) is a subtype of refolding-unfolding imbalance: A process that lacks a balance between protein refolding and unfolding moderately. refolding-unfolding imbalance (moderate) HOIP_0003533 HOIP:HOIP_0003534 A role played by the entity which regulates the process of tumor cell proliferation. regulator of tumor cell proliferation HOIP_0003534 HOIP:HOIP_0003535 Eosinophilic granular degeneration [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed in the form that the cytoplasm presents eosinophilic granules based on pathological morphology. The degree is mild. This finding is observable as a result of increasing peroxisome caused by PPAR. eosinophilic granular degeneration [Liver Pathological Findings] [eosinogranular degeneration (mild) ] HOIP_0003535 HOIP:HOIP_0003536 Eosinophilic granular degeneration [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed in the form that the cytoplasm presents eosinophilic granules based on pathological morphology. The degree is moderate. This finding is observable as a result of increasing peroxisome caused by PPAR. eosinophilic granular degeneration [Liver Pathological Findings] [eosinogranular degeneration (moderate) ] HOIP_0003536 HOIP:HOIP_0003537 Eosinophilic granular degeneration [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed in the form that the cytoplasm presents eosinophilic granules based on pathological morphology. The degree is severe. This finding is observable as a result of increasing peroxisome caused by PPAR. eosinophilic granular degeneration [Liver Pathological Findings] [eosinogranular degeneration (severe) ] HOIP_0003537 HOIP:HOIP_0003538 Fatty change [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed as lipid droplets consisting of neutral fat in the hepatocyte based on pathological morphology. This finding is observable in the course of lipidosis. The degree is mild. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. vacuolation [Liver Pathological Findings][simple steatosis] HOIP_0003538 A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0003539 Phosphatidylcholine efflux is a subtype of moving A to the outside of B: A process that excretes phosphatidylcholine to the outside of a cell or organelle. phosphatidylcholine efflux HOIP_0003539 HOIP:HOIP_0003540 Fatty change [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed as lipid droplets consisting of neutral fat in the hepatocyte based on pathological morphology. This finding is observable in the course of lipidosis. The degree is moderate. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. vacuolation [Liver Pathological Findings][Lipidosis(moderate)] HOIP_0003540 A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0003541 Fatty change [Liver PathologicalFindings] is a type of finding observed in hepatocytes. Lesions are observed as lipid droplets consisting of neutral fat in the hepatocyte based on pathological morphology. This finding is observable in the course of lipidosis. The degree is severe. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. vacuolation [Liver Pathological Findings][non-alcoholic steatohepatitis (course)] HOIP_0003541 A metabolic disorder of neutral fat causes fatty change. Lipid droplets consisting of large and small neutral fats (triglycerides) increase in the cytoplasm of hepatocytes. In the case of large lipid droplets, the uneven distribution of nuclei is observed, but in the case of small loose droplets (microvesicular fatty change), uneven distribution of nuclei is not observed. According to the distribution, it classifies into centrilobular, periportal, and diffuse type. http://webcatplus.nii.ac.jp/webcatplus/details/book/isbn/4890134719.html?txt_isbn=4890134719 HOIP:HOIP_0003542 Ground glass appearance [Liver PathologicalFindings] is a type of finding observed in hepatocyte cytoplasm. Based on the pathological morphology, lesions are observed as a frosted-like change in whole or most of the hepatocytes. This finding is observable in the course of ground glass appearance. The degree is severe. ground glass appearance [Liver Pathological Findings] [Ground glass appearance (severe)] HOIP_0003542 HOIP:HOIP_0003544 Changing cell survival-cell death balance is a subtype of changing balance: A process that changes the steady state of cell number between cell death and cell survival within an organ or an organism. changing cell survival-cell death balance HOIP_0003544 HOIP:HOIP_0003545 Maintaining cell survival-cell death balance is a subtype of maintaining balance: A process that keeps a balance between cell death and cell survival within an organ or an organism. maintaining cell survival - cell death balance HOIP_0003545 HOIP:HOIP_0003546 Cell survival-cell death imbalance is a subtype is a subtype of imbalance: A process that lacks a balance between cell death and cell survival within an organ or an organism. cell survival-cell death imbalance HOIP_0003546 HOIP:HOIP_0003547 Cell survival-cell death imbalance is a subtype is a subtype of imbalance: A process that lacks a balance between cell death and cell survival within an organ or an organism. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). cell survival-cell death imbalance [phospholipidosis (severe)] HOIP_0003547 HOIP:HOIP_0003549 Maintaining cell survival-cell death balance is a subtype of maintaining balance: A process that keeps a balance between cell death and cell survival within an organ or an organism. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). maintaining cell survival-cell death balance [phospholipidosis (normal course)] HOIP_0003549 HOIP:HOIP_0003550 PMID:26481188 GRP78 - tumor cell enhanced survlival factor (canonical)[ER stress - tumor survival] HOIP_0003550 HOIP:HOIP_0003551 Changing cell homeostasis is a subtype of changing balance: A process that changes the steady state of cell within an organ or an organism. changing cell homeostasis HOIP_0003551 HOIP:HOIP_0003552 Any process involved in the maintenance of an internal steady state of cell within an organ or an organism. maintaining cell homeostasis HOIP_0003552 HOIP:HOIP_0003553 Cell homeostasis imbalance is a subtype of homeostasis imbalance: A process that becomes lacking a cell homeostastasis balance. cell homeostasis imbalance HOIP_0003553 HOIP:HOIP_0003555 NCBI-Human-GeneID:5319 NCBI-Mouse-GeneID:18778 NCBI-Rat-GeneID:29526 PMID:15528384 PMID:16005851 PLA2G1B(mol) HOIP_0003555 NCBI-Human-GeneID:5319 http://www.ncbi.nlm.nih.gov/gene/5319 NCBI-Mouse-GeneID:18778 http://www.ncbi.nlm.nih.gov/gene/18778 NCBI-Rat-GeneID:29526 http://www.ncbi.nlm.nih.gov/gene/29526 HOIP:HOIP_0003561 Combining role with an extracellular signal and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex. IMR:0000137 (obsolete) Wikipedia:GPCR GPCR related molecular function GO:0004930 G-Protein Coupled Receptor HOIP_0003561 HOIP:HOIP_0003562 A role played by the entity that positively regulates the process ofof G1/S transition of mitotic cell cycle role. G1/S transition of mitotic cell cycle HOIP_0003562 HOIP:HOIP_0003563 An affinity which is relatively high. increased affinity HOIP_0003563 HOIP:HOIP_0003564 A role played by the entity that positively regulates the process of cell cycle phase transition. positive regulator of cell cycle phase transition role HOIP_0003564 HOIP:HOIP_0003565 Forming a complex of CAD and phospholipid is a subtype of forming a complex of drugs and biological substance: A process that forms a complex consisiting phospholipids and CAD (Cationic Amphiphilic Drug) in the lysosomal membrane, which causes structural change of the membrane. The degree is mild. forming a complex of CAD and phospholipid (mild) HOIP_0003565 HOIP:HOIP_0003566 Forming a complex of CAD and phospholipid is a subtype of forming a complex of drugs and biological substance: A process that forms a complex consisiting phospholipids and CAD (Cationic Amphiphilic Drug) in the lysosomal membrane, which causes structural change of the membrane. The degree is moderate. forming a complex of CAD and phospholipid (moderate) HOIP_0003566 HOIP:HOIP_0003567 Forming a complex of CAD and phospholipid is a subtype of forming a complex of drugs and biological substance: A process that forms a complex consisiting phospholipids and CAD (Cationic Amphiphilic Drug) in the lysosomal membrane, which causes structural change of the membrane. The degree is severe. forming a complex of CAD and phospholipid (severe) HOIP_0003567 HOIP:HOIP_0003568 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder]. PMID:31623280 cell death [mitochondrial disorder (course)] HOIP_0003568 PMID:31623280 Emerging evidence suggests that mitochondrial dysfunction or maladaptation contributes to detrimental effects on hepatocyte bioenergetics, reactive oxygen species (ROS) homeostasis, endoplasmic reticulum (ER) stress, inflammation, and cell death leading to NASH and HCC. HOIP:HOIP_0003569 Glutathione depletion is a subtype of depleting: A process that lessens markedly in the amount of glutathione. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:25339807 glutathione depletion [mitochondrial disorder (course)] HOIP_0003569 PMID:25339807 Depletion of mitochondrial GSH levels could also be due to its reduced uptake by mitochondria as a result of enhanced levels of cholesterol within the inner mitochondrial membrane and the decrease in synthesis of S-adenosylmethionine, the major methyl donor in liver and precursor to GSH. HOIP:HOIP_0003572 A role played by the entity which positivey regulates the process of infmammatory response. positive regulator of immune response HOIP_0003572 HOIP:HOIP_0003575 Substance with cytokine role is a subtype of substance with role. This entity is inferred from Description Logic. substance with cytokine role HOIP_0003575 HOIP:HOIP_0003576 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of type II diabetes. PMID:26006114 Insulin resistance (process) [type 2 diabetes mellitus course] HOIP_0003576 PMID:26006114 Insulin resistance alters hepatic ethanol metabolism: studies in mice and children with non-alcoholic fatty liver disease. HOIP:HOIP_0003577 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required absolutely. This entity is a specific course-dependent process. This process can constitute the course of type 1 diabetes. insulin absolute deficiency [type 1 diabetes mellitus course] HOIP_0003577 HOIP:HOIP_0003578 A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid hydrolysis. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). negative regulation of phospholipid hydrolysis [phospholipidosis (latent course)] HOIP_0003578 HOIP:HOIP_0003579 The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. sphingomyelin anabolism sphingomyelin biosynthesis sphingomyelin formation sphingomyelin synthesis sphingomyelin biosynthetic process [course of Niemann–Pick disease type A] HOIP_0003579 The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. ISBN:0198506732 HOIP:HOIP_0003580 The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. sphingomyelin anabolism sphingomyelin biosynthesis sphingomyelin formation sphingomyelin synthesis sphingomyelin biosynthetic process[course of Niemann–Pick disease type B] HOIP_0003580 The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. ISBN:0198506732 HOIP:HOIP_0003581 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required. This entity is a specific course-dependent process. This process can constitute the course of type II diabetes. insulin relative deficiency [type 2 diabetes mellitus course] HOIP_0003581 HOIP:HOIP_0003583 Hyperfunction of phospholipid degradation (severe) is a subtype of hyperfunction of phospholipid degradation: A process that performs an excessive phospholipid degradation severely. hyperfunction of phospholipid degradation (severe) HOIP_0003583 HOIP:HOIP_0003584 Increasing phospholipid inflow (severe) is a subtype of increase in phospholipid inflow: A process that changes the phospholipid inflow into the hepatocyte to be larger. increasing phospholipid inflow (severe) HOIP_0003584 HOIP:HOIP_0003588 EIF2A - cell cycle arresr inducer (canonical)[ER stress - translation] HOIP_0003588 HOIP:HOIP_0003589 Cell homeostasis imbalance is a subtype of homeostasis imbalance: A process that becomes lacking a cell homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). cell homeostasis imbalance [phospholipidosis (severe)] HOIP_0003589 HOIP:HOIP_0003590 Changing cell homeostasis is a subtype of changing balance: A process that changes the steady state of cell within an organ or an organism. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. changing cell homeostasis [phospholipidosis (course)] HOIP_0003590 HOIP:HOIP_0003591 Any process involved in the maintenance of an internal steady state of cell within an organ or an organism. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. maintaining cell homeostasis [Phospholiipidosis] HOIP_0003591 HOIP:HOIP_0003592 Increasing energy is a subtype of increasing quantity: A process that changes the amount of energy to be larger. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). increasing energy [Phospholipidosis(severe)] HOIP_0003592 HOIP:HOIP_0003593 Increasing energy is a subtype of increasing quantity: A process that changes the amount of energy to be larger. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. increasing energy [phospholipidosis (imbalance course)] HOIP_0003593 HOIP:HOIP_0003594 Energy supply is a subtype of providing process to perform a meta-function “to provide energy. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). energy supply [phospholipidosis(severe)] HOIP_0003594 HOIP:HOIP_0003595 Energy supply is a subtype of providing process to perform a meta-function “to provide energy. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. energy supply [phospholipidosis (imbalance course)] HOIP_0003595 HOIP:HOIP_0003596 Increasing number of dead cells in liver is a subtype of cell proliferation: A process that becomes larger in the number of dead cells in the liver. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). increasing number of dead cells in liver [phospholipidosis (severe)] HOIP_0003596 HOIP:HOIP_0003598 Cell survival-cell death imbalance is a subtype is a subtype of imbalance: A process that lacks a balance between cell death and cell survival within an organ or an organism. This entity is a specific course-dependent process. This process can constitute the course of ER stress. maintaining cell survival-cell death balance [ER stress] HOIP_0003598 HOIP:HOIP_0003600 Any intermediate or product resulting from phospholipid metabolism. phospholipid metabolite HOIP_0003600 HOIP:HOIP_0003601 Decreasing ceramide is a subtype of decreasing lipid: A process that changes the quantity of the ceramide to be lower. decreasing ceramide HOIP_0003601 HOIP:HOIP_0003603 Mitochondrial damage dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of Mitochondrial damage as a gene product. Gene profile:Human/in vitro/Hepatocyte/ mitochondrial damage dependent molecule (human in vitro) HOIP_0003603 HOIP:HOIP_0003609 Oranic anion export is a subtype of moving A to the outside of B: A process of the directed movement of organic anions into, out of a cell, or an organelle, by means of some agent such as a transporter or pore. oranic anion export HOIP_0003609 HOIP:HOIP_0003610 PMID:30894684, Hepatocarcinoma cell NCBI-Human-GeneID:6347 PMID:30894684 CCL2(human) [mitochondrial damage] HOIP_0003610 NCBI-Human-GeneID:6347 http://www.ncbi.nlm.nih.gov/gene/6347 PMID:30894684 CCL2 is a multifunctional factor involved in various aspects of liver disease pathogenesis, including cirrhosis and hepatocarcinogenesis. Previous studies have shown that CCL2 promotes the accumulation and polarization of macrophages by CCR2 receptor signaling pathway. Our study demonstrated that CCL2 was a critical mediator to link the cytosolic mtDNA stress in HCC cells and TAM infiltration. HOIP:HOIP_0003611 NCBI-Human-GeneID:983 PMID:24746669 CDK1 (human) [mitochondrial damage] HOIP_0003611 NCBI-Human-GeneID:983 http://www.ncbi.nlm.nih.gov/gene/983 PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. HOIP:HOIP_0003613 NCBI-Human-GeneID:9518 PMID:29222479 GDF15 (human) [mitochondrial damage] HOIP_0003613 NCBI-Human-GeneID:9518 http://www.ncbi.nlm.nih.gov/gene/9518 PMID:29222479 Treatment with alcohol also increased the levels of secreted GDF15 in supernatants of cultured hepatocytes. We next investigated the effect of mitochondrial dysfunction on GDF15 expression in hepatocytes. Inhibition of the mitochondrial OXPHOS complex using oligomycin or rotenone significantly increased Gdf15 expression and GDF15 secretion by cultured hepatocytes. Hepatic Gdf15 expression and serum levels of GDF15 were remarkably increased in alcohol-fed mice. HOIP:HOIP_0003615 Severe sphingomyelin accumulation in lysosome of nervous system is a subtype of sphingomyelin accumulation in lysosome of nervous system: A process that keeps sphingomyelin in the lysosome of nervous system severely. severe sphingomyelin accumulation in lysosome of nervous system HOIP_0003615 HOIP:HOIP_0003616 Spleen hyperfunction is a subtype of hyperfunctioning: A process that performs an excessive spleen function. This entity is a specific course-dependent process. This process can constitute the course of hepatic blood circulatory disorder. spleen hyperfunction [hepatic blood circulatory disorder] HOIP_0003616 HOIP:HOIP_0003620 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis. PMID:20303879 PMID:21038418 PMID:22883813 PMID:25232821 PMID:26609140 PMID:27346803 PMID:27814504 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2887297/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2887297/figure/F1/ inflammatory response [non-alcoholic steatohepatitis (course)] HOIP_0003620 PMID:20303879 IRE1->JNK->AP-1->inflammatory response IRE1->XBP1s->IL6, IL8, MCP1 IRE1->IKK->NfkB ATF6->NfkB Perk->reducedIkB->NfkB PMID:21038418 Inflammation Preceding Steatosis. Simple hepatic steatosis, which is benign and nonprogressive in the majority of patients, and NASH may reflect different disease entities. Inflammation results in a stress response of hepatocytes, may lead to lipid accumulation, and therefore could precede steatosis in NASH. PMID:22883813 When activated, all three sensors of the unfolded protein response (UPR), PERK, IRE1, and ATF6, participate in upregulating inflammatory processes. ER stress in various cells plays an important role in the pathogenesis of several diseases, including obesity, type 2 diabetes, cancer, and intestinal bowel and airway diseases. HOIP:HOIP_0003621 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). hepatic fibrosis [non-alcoholic steatohepatitis (course)] HOIP_0003621 HOIP:HOIP_0003622 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the  outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis. inflammatory cell infiltration [non-alcoholic steatohepatitis (course)] HOIP_0003622 HOIP:HOIP_0003623 Lipid accumulation in hepatocyte is a subtype of lipid storage: A process that keeps lipids in hepatocytes. lipid accumulation in hepatocyte HOIP_0003623 HOIP:HOIP_0003624 Lipid accumulation in hepatocyte (mild) is a subtype of lipid strorage in hepatocyte: A process that keeps lipids in hepatocytes mildly. This entity is a specific course-dependent process. This process can constitute the course of simple steatosis. lipid strorage in hepatocyte [Lipidosis (mild)] lipid accumulation in hepatocyte (mild) [simple steatosis] HOIP_0003624 HOIP:HOIP_0003625 An cross-sectional area which is relatively low. decreased cross-sectional area HOIP_0003625 HOIP:HOIP_0003626 A 2-D extent attribute of the bearer which has been cut off to an axis. cross-sectional area HOIP_0003626 HOIP:HOIP_0003627 Balooning [Liver PathologicalFindings] is a type of finding observed in the liver. On the basis of pathological morphology, the cytoplasm becomes enlarged like balloons accompanied by the vacuolation. balooning [Liver Pathological Findings] HOIP_0003627 HOIP:HOIP_0003628 Balooning [Liver PathologicalFindings] is a type of finding observed in the liver. On the basis of pathological morphology, the cytoplasm becomes enlarged like balloons accompanied by the vacuolation . This finding is observable in the course of lipidosis. balooning [Liver Pathological Findings] [Lipidosis] HOIP_0003628 HOIP:HOIP_0003629 Hypofunction of peroxisomal fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient fatty acid degradation. hypofunction of peroxisomal fatty acid beta-oxidation HOIP_0003629 HOIP:HOIP_0003630 CCL3 Cl[C](Cl)Cl CCL3 [lipidosis] trichloromethyl(.) [NASH] HOIP_0003630 HOIP:HOIP_0003631 in vitro (human) 2hr HOIP_0003631 HOIP:HOIP_0003632 This course is categorized from the viewpoint of the findings of fatty change. This entity is inferred from Description Logic. course based on fatty change HOIP_0003632 HOIP:HOIP_0003633 NCBI-Human-GeneID:1544 NCBI-Mouse-GeneID:13077 NCBI-Rat-GeneID:24297 Cyp1A2 (mol) HOIP_0003633 NCBI-Human-GeneID:1544 http://www.ncbi.nlm.nih.gov/gene/1544 NCBI-Mouse-GeneID:13077 http://www.ncbi.nlm.nih.gov/gene/13077 NCBI-Rat-GeneID:24297 http://www.ncbi.nlm.nih.gov/gene/24297 HOIP:HOIP_0003634 A physical quality inhering in a fluid (liquid or gas) by virtue of the amount of fluid which passes through a given surface per unit time. fluid flow rate HOIP_0003634 HOIP:HOIP_0003636 Regulation of transmitting is a subtype of controlling: A process that modulates the frequency, rate or extent of transmitting. regulation of transmitting HOIP_0003636 HOIP:HOIP_0003637 Regulation of bile acid and bile salt transport is a subtype of regulation of transport (biology): Any process that modulates the frequency, rate or extent of the directed movement of bile acid and bile salts . regulation of bile acid and bile salt transport HOIP_0003637 HOIP:HOIP_0003638 A role which enables the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells. related molecular function GO:0005215 transporter HOIP_0003638 HOIP:HOIP_0003639 A role enables the energy-independent facilitated diffusion, mediated by passage of a solute through a transmembrane aqueous pore or channel. Stereospecificity is not exhibited but this transport may be specific for a particular molecular species or class of molecules. related molecular function GO:0015267 channel HOIP_0003639 HOIP:HOIP_0003640 Phosphholipid binding by phospholipase is a subtype of phospholipid binding: Interacting selectively and non-covalently with phospholipids byphospholipases. phosphholipid binding by phospholipase HOIP_0003640 HOIP:HOIP_0003641 Protein dimerization is a subtype of protein polymerization: The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. protein dimerization HOIP_0003641 HOIP:HOIP_0003643 NFKB (canonical)[Fibrosis] HOIP_0003643 HOIP:HOIP_0003644 A role played by the entity that regulates transcriptional elongation by enabling the transition from transcription initiation to elongation or by altering the elongation properties of the enzyme during the elongation phase of transcription. transcriptional elongation factor related molecular function GO:0003711 transcription elongation regulation factor HOIP_0003644 HOIP:HOIP_0003645 A role played by the entity to initiate or regulate transcription. IMR:0000368 (obsolete) This term is sometimes used for both gene regulatory proteins as well as the general transcription factors. transcription factor HOIP_0003645 HOIP:HOIP_0003646 An early local inflammatory reaction to insult or injury that consists of fever, an increase in inflammatory humoral factors, and an increased synthesis by hepatocytes of a number of proteins or glycoproteins usually found in the plasma. http://purl.bioontology.org/ontology/MEDDRA/10048998 http://purl.bioontology.org/ontology/MESH/D000210 acute phase responses by cytokines HOIP_0003646 HOIP:HOIP_0003647 A role played by the entity which regulates the formation of phospholipids. phospholipid metabolic regulator role HOIP_0003647 HOIP:HOIP_0003648 A role played by the entity which regulates fatty acid metabolic process. fatty accid metabolic regulator role HOIP_0003648 HOIP:HOIP_0003649 NCBI-Human-GeneID:6772 NCBI-Mouse-GeneID:20846 NCBI-Rat-GeneID:25124 STAT1 (canonical)[Fibrosis] HOIP_0003649 NCBI-Human-GeneID:6772 http://www.ncbi.nlm.nih.gov/gene/6772 NCBI-Mouse-GeneID:20846 http://www.ncbi.nlm.nih.gov/gene/20846 NCBI-Rat-GeneID:25124 http://www.ncbi.nlm.nih.gov/gene/25124 HOIP:HOIP_0003650 A role played by the entity which involves in regulating a gene expression process. gene expression regulator role HOIP_0003650 HOIP:HOIP_0003651 Phospholipid metabolism balance is a subtype of maintaining balance: A process that keeps a balance of phospholipid metabolism at small level. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis (excessive defense). phospholipid metabolism balance [Phospholipidosis (adaptation2)] HOIP_0003651 HOIP:HOIP_0003652 Dysfunction of fatty acid degradation is a subtype of dysfunctioning: A process that performs an abnormal and incomplete fatty acid degradation. dysfunction of fatty acid degradation HOIP_0003652 HOIP:HOIP_0003653 A traditional grouping of drugs said to have a soothing or calming effect on mood, thought or behaviour. tranquilizing drug HOIP_0003653 HOIP:HOIP_0003654 A role played by the entity which regulates the glutathione synthesis. glutathione synthesis regulating agent role HOIP_0003654 HOIP:HOIP_0003655 A role played by the entity which enables the facilitated diffusion of a potassium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism. related molecular function GO:0005267 potassium channel HOIP_0003655 HOIP:HOIP_0003656 A role played by the entity which enables the facilitated diffusion of a sodium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism. related molecular function GO:0005272 sodium channel HOIP_0003656 HOIP:HOIP_0003657 A role played by the entity that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way. General term for proteins in intracellular signaling pathways that link different proteins in the pathway directly together. General term for proteins in intracellular signaling pathways that link different proteins in the pathway directly together. IMR:0000333 (obsolete) anchoring protein docking protein scaffold protein adaptor protein role HOIP_0003657 General term for proteins in intracellular signaling pathways that link different proteins in the pathway directly together. ISBN:0815340729 PMID:9405336 HOIP:HOIP_0003658 Antipsychotic drugs are agents that control agitated psychotic behaviour, alleviate acute psychotic states, reduce psychotic symptoms, and exert a quieting effect. major tranquilizers neuroleptic antipsychotic agent HOIP_0003658 HOIP:HOIP_0003659 Antipsychotic drugs which can have different modes of action but which tend to be more likely than second generation antipsychotics to cause extrapyramidal motor control disabilities such as body rigidity or Parkinson's disease-type movements; such body movements can become permanent even after treatment has ceased. Wikipedia:Typical_antipsychotic first generation antipsychotic HOIP_0003659 HOIP:HOIP_0003660 Protein that catalyze a specific chemical reaction. Protein that catalyze a specific chemical reaction. IMR:0000207 (obsolete) related molecular function GO:0003824 enzyme role HOIP_0003660 Protein that catalyze a specific chemical reaction. ISBN:0815340729 HOIP:HOIP_0003661 phenothiazine antipsychotic drug HOIP_0003661 HOIP:HOIP_0003662 Catalysis role of the reaction: NTP + H2O = NDP + phosphate, to drive the unwinding of a DNA or RNA helix. IMR:0010034 (obsolete) related molecular function: GO:0004386 helicase HOIP_0003662 HOIP:HOIP_0003663 Catalysis role of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3. EC:3.-.-.- IMR:0010044 (obsolete) related molecular function GO:0016787 hydrolase HOIP_0003663 HOIP:HOIP_0003664 Catalysis role of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction. IMR:0000918 (obsolete) ATP hydrolase ATP hydrolase adenosine 5'-triphosphatase adenosine 5'-triphosphatase adenosine triphosphatase adenosine triphosphatase complex V (mitochondrial electron transport) related molecular function GO:0016887 ATPase HOIP_0003664 ATP hydrolase EC:3.6.1.3 adenosine 5'-triphosphatase EC:3.6.1.3 adenosine triphosphatase EC:3.6.1.3 HOIP:HOIP_0003665 A narcotic or opioid substance, synthetic or semisynthetic agent producing profound analgesia, drowsiness, and changes in mood. opioid analgesic HOIP_0003665 HOIP:HOIP_0003666 Catalysis role of the hydrolysis of any glycosyl bond. EC:3.2.-.- IMR:0010049 (obsolete) glycosylase HOIP_0003666 HOIP:HOIP_0003667 Catalysis role of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site. Catalysis role of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site. EC:3.2.2 DNA glycosylase DNA N-glycosylase HOIP_0003667 Catalysis role of the removal of damaged bases by cleaving the N-C1' glycosidic bond between the target damaged DNA base and the deoxyribose sugar. The reaction releases a free base and leaves an apurinic/apyrimidinic (AP) site. PMID:11554296 HOIP:HOIP_0003668 Catalysis role of the reaction: GTP + H2O = GDP + phosphate. EC:3.6.5.- IMR:0000960 (obsolete) related moleular function: GO:0003924 GTPase HOIP_0003668 HOIP:HOIP_0003669 A role of the RAS superfamily of GTP (guanosine triphosphate) hydrolysis-coupled signal transduction relay protein. It can be subclassified into RAS, RHO, RAB, and ARF families, as well as the closely related G alpha family. The members of each family can, in turn, be arranged into evolutionarily conserved branches. These groupings reflect structural, biochemical, and functional conservation. A role of the RAS superfamily of GTP (guanosine triphosphate) hydrolysis-coupled signal transduction relay protein. It can be subclassified into RAS, RHO, RAB, and ARF families, as well as the closely related G alpha family. The members of each family can, in turn, be arranged into evolutionarily conserved branches. These groupings reflect structural, biochemical, and functional conservation. EC:3.6.5.2 small G-protein small GTP-binding protein small GTPase Ras superfamily small GTPase HOIP_0003669 A role of the RAS superfamily of GTP (guanosine triphosphate) hydrolysis-coupled signal transduction relay protein. It can be subclassified into RAS, RHO, RAB, and ARF families, as well as the closely related G alpha family. The members of each family can, in turn, be arranged into evolutionarily conserved branches. These groupings reflect structural, biochemical, and functional conservation. PMID:15367757 PMID:15731001 HOIP:HOIP_0003670 Catalysis role of the reaction: histone N6-acetyl-L-lysine + H2O = histone L-lysine + acetate. This reaction represents the removal of an acetyl group from a histone, a class of proteins complexed to DNA in chromatin and chromosomes. Catalysis role of the reaction: histone N6-acetyl-L-lysine + H2O = histone L-lysine + acetate. This reaction represents the removal of an acetyl group from a histone, a class of proteins complexed to DNA in chromatin and chromosomes. IMR:0001166 (obsolete) related molecule fuction GO:0004407 HDAC histone deacetylase HOIP_0003670 Catalysis role of the reaction: histone N6-acetyl-L-lysine + H2O = histone L-lysine + acetate. This reaction represents the removal of an acetyl group from a histone, a class of proteins complexed to DNA in chromatin and chromosomes. EC:3.5.1.98 PMID:9893272 HOIP:HOIP_0003671 Catalysis role of the hydrolysis of a glycerophospholipid. EC:3.1.1 IMR:0000281 (obsolete) related molecular fuction : GO:0004620 phospholipase HOIP_0003671 Catalysis role of the hydrolysis of a glycerophospholipid. ISBN:0198506732 HOIP:HOIP_0003672 Catalysis role of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group. EC:3.1.4.- PDE phosphodiesterase related molecular function GO:0008081 phosphoric diester hydrolase HOIP_0003672 HOIP:HOIP_0003673 Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate. EC:3.1.3. EC:3.1.3.41 IMR:0000517 (obsolete) phosphoric monoester hydrolase activity NPPase activity related molecular function GO:0016791 phosphatase HOIP_0003673 HOIP:HOIP_0003674 Catalysis role of the reaction: D-glucopyranose 6-phosphate + H2O = D-glucose + phosphate. D-glucopyranose is also known as D-glucose 6-phosphate. Catalysis role of the reaction: D-glucopyranose 6-phosphate + H2O = D-glucose + phosphate. D-glucopyranose is also known as D-glucose 6-phosphate. EC:3.1.3.9 IMR:0010260 (obsolete) D-glucose-6-phosphate phosphohydrolase activity D-glucose-6-phosphate phosphohydrolase activity G-6-Pase G6Pase glucose 6-phosphate phosphatase activity glucose 6-phosphate phosphatase activity glucose-6-phosphatase HOIP_0003674 Catalysis role of the reaction: D-glucopyranose 6-phosphate + H2O = D-glucose + phosphate. D-glucopyranose is also known as D-glucose 6-phosphate. EC:3.1.3.9 D-glucose-6-phosphate phosphohydrolase activity EC:3.1.3.9 glucose 6-phosphate phosphatase activity EC:3.1.3.9 HOIP:HOIP_0003675 Catalysis role of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity. Catalysis role of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity. IMR:0000272 (obsolete) phosphoprotein phosphohydrolase phosphoprotein phosphohydrolase protein phosphatase protein phosphatase protein phosphatase-2A related molecular function GO:0004721 phosphoprotein phosphatase HOIP_0003675 Catalysis role of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity. EC:3.1.3.16 phosphoprotein phosphohydrolase EC:3.1.3.16 protein phosphatase EC:3.1.3.16 HOIP:HOIP_0003676 Catalysis role of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate. EC:3.1.3.16 IMR:0000277 (obsolete) serine/threonine specific protein phosphatase related molecular function GO:0004722 protein serine/threonine phosphatase HOIP_0003676 HOIP:HOIP_0003677 Catalysis role of the reactions: protein serine + H2O = protein serine + phosphate; protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate. IMR:0100208 (obsolete) related molecular function GO:0008138 Note that this term applies only to free amino acids. protein serine/threonine/tyrosine phosphatase HOIP_0003677 HOIP:HOIP_0003678 Compound accumulation in lysosome is a subtype of accumulation of xenobiotics: A process that keeps compound in the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). compound accumulation in lysosome [phospholipidosis (latent)] HOIP_0003678 HOIP:HOIP_0003679 Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate. EC:3.1.3.48 PPT-phosphatase PTPase [phosphotyrosine]protein phosphatase phosphoprotein phosphatase (phosphotyrosine) phosphotyrosine histone phosphatase phosphotyrosine phosphatase phosphotyrosine protein phosphatase phosphotyrosylprotein phosphatase protein-tyrosine-phosphate phosphohydrolase tyrosine O-phosphate phosphatase tyrosylprotein phosphatase related molecular function GO:0004725 protein tyrosine phosphatase HOIP_0003679 Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate. EC:3.1.3.48 HOIP:HOIP_0003680 A role played by the entity which enables the transmembrane transfer of an ion by a channel that opens when a specific ligand has been bound by the channel complex or one of its constituent parts. related molecular function GO:0015276 ligand-gated ion channel HOIP_0003680 HOIP:HOIP_0003681 A role played by the entity interacting selectively and non-covalently and simultaneously with one or more signal transduction molecules, usually acting as a scaffold to bring these molecules into close proximity either using their own SH2/SH3 domains (e.g. Grb2) or those of their target molecules (e.g. SAM68). This term refers to the adaptor proteins that possesses both SH2 and SH3 domains, such as Grb2, Nck and Crk, and does not include adaptor proteins that contain only SH2 or PTB domains, such as the Shc family and the IRS family. This term refers to the adaptor proteins that possesses both SH2 and SH3 domains, such as Grb2, Nck and Crk, and does not include adaptor proteins that contain only SH2 or PTB domains, such as the Shc family and the IRS family. IMR:0000334 (obsolete) related molecular function GO:0005070 SH2/SH3 adaptor protein role HOIP_0003681 This term refers to the adaptor proteins that possesses both SH2 and SH3 domains, such as Grb2, Nck and Crk, and does not include adaptor proteins that contain only SH2 or PTB domains, such as the Shc family and the IRS family. PMID:10393272 HOIP:HOIP_0003682 A role played by the entity interacting selectively and non-covalently and simultaneously with one or more signal transduction molecules, usually acting as a scaffold to bring these molecules into close using Death Domains. IMR:0000742 (obsolete) death domain-containing adaptor protein DD-containing adaptor protein role HOIP_0003682 HOIP:HOIP_0003683 An attribute of morphology inhering in a bearer by virtue of the bearer's physical magnitude. size (attribute) HOIP_0003683 HOIP:HOIP_0003684 A role played by the entity that acts as docking sites for multiple signaling molecules. A role played by the entity that acts as docking sites for multiple signaling molecules. IMR:0000345 (obsolete) docking protein HOIP_0003684 A role played by the entity that acts as docking sites for multiple signaling molecules. PMID:11057895 PMID:9405336 HOIP:HOIP_0003685 A role of involving the initiation of ribosome-mediated translation of mRNA into a polypeptide. related molecular function GO:0003743 translation initiation factor HOIP_0003685 HOIP:HOIP_0003686 Lipid Mediator role is played by a lipid having bioactivity, which is transiently produced locally, acts on a cell membrane receptor located in its place, transmits a signal, and usually is decomposed promptly. IMR:0100181 (obsolete) lipid mediator HOIP_0003686 HOIP:HOIP_0003687 The role of a molecule that contributes to the structural integrity of the ribosome. IMR:0100710 (obsolete) ribosomal protein reated molecular function GO:0003735 structural constituent of ribosome HOIP_0003687 HOIP:HOIP_0003688 A role played by the molecule to mediate adhesion of the cell to the external substrate or to another cell. IMR:0000166 (obsolete) cell adhesion mediator related molecular function GO:0098631 adhesion molecule HOIP_0003688 HOIP:HOIP_0003689 The role played by the molecule that contributes to the structural integrity of a cytoskeletal structure. IMR:0000185(obsolete) related molecular function GO:0005200 cytoskeletal protein HOIP_0003689 HOIP:HOIP_0003690 A role played by the entity that catalyses the generation of force resulting either in movement along a microfilament or microtubule, or in torque resulting in membrane scission, coupled to the hydrolysis of a nucleoside triphosphate. molecular motor IMR:0000518 (obsolete) related molecular function GO:0003774 motor protein HOIP_0003690 HOIP:HOIP_0003691 The role of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell. IMR:0000950 (obsolete) related molecular function GO:0005198 structural molecule HOIP_0003691 HOIP:HOIP_0003692 The role played by the molecule that contributes to the structural integrity of an microfilament (actin filament). Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells actin filament protein related cellular component GO:0005884 microfilament protein HOIP_0003692 HOIP:HOIP_0003693 The role played by the molecule that contributes to the structural integrity of the intermediate filaments. IMR:0000496 (obsolete) related cellular component GO:0005882 intermediate filament protein HOIP_0003693 HOIP:HOIP_0003694 The role played by the molecule that contributes to the structural integrity of cytoskeletal fibers. related cellular component GO:0099513 cytoskeletal fiber protein HOIP_0003694 HOIP:HOIP_0003695 The role of a molecule that contributes to the structural integrity of the extracellular matrix. IMR:0000540 (obsolete) ECM protein related molecular function GO:0005201 extracellular matrix structural constituent role HOIP_0003695 HOIP:HOIP_0003696 A role played by the entity of transport systems. This type enable facilitated diffusion of water (by an energy-independent process) by passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism. IMR:0000656 (obsolete) relate molecular function GO:0015250 water channel HOIP_0003696 HOIP:HOIP_0003697 A role played by the entity which enables the transfer of amino acids from one side of a membrane to the other. Amino acids are organic molecules that contain an amino group and a carboxyl group. IMR:0000929 (obsolete) related molecular function GO:0015171 amino acid transmembrane transporter HOIP_0003697 HOIP:HOIP_0003698 A role played by the entity which enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other. related molecular function GO:0022857 transmembrane transporter HOIP_0003698 HOIP:HOIP_0003699 A role played by the entity which enables the directed movement of lipids into, out of or within a cell, or between cells. related molecular function GO:0005319 lipid transportor HOIP_0003699 HOIP:HOIP_0003700 A role played by the entity which enables the directed movement of phospholipids into, out of or within a cell, or between cells. Phospholipids are a class of lipids containing phosphoric acid as a mono- or diester. related molecular function GO:0005548 phospholipid transporter HOIP_0003700 HOIP:HOIP_0003701 A role played by the entity which enables the transfer of a sugar from one side of a membrane to the other. A sugar is any member of a class of sweet, water-soluble, crystallizable carbohydrates, which are the monosaccharides and smaller oligosaccharides. A role played by the entity which enables the transfer of a sugar from one side of a membrane to the other. A sugar is any member of a class of sweet, water-soluble, crystallizable carbohydrates, which are the monosaccharides and smaller oligosaccharides. sugar transmembrane transporter HOIP_0003701 A role played by the entity which enables the transfer of a sugar from one side of a membrane to the other. A sugar is any member of a class of sweet, water-soluble, crystallizable carbohydrates, which are the monosaccharides and smaller oligosaccharides. ISBN:0815340729 HOIP:HOIP_0003702 A role played by the entity which enables the transfer of an ion from one side of a membrane to the other up the solute's concentration gradient. This is carried out by binding the solute and undergoing a series of conformational changes. Transport works equally well in either direction. related molecular finction GO:0015075 ion transmembrane transporter HOIP_0003702 HOIP:HOIP_0003703 A role played by the entity which enables the transfer of bile acid from one side of a membrane to the other. Bile acids are any of a group of steroid carboxylic acids occurring in bile, where they are present as the sodium salts of their amides with glycine or taurine. Reactome:REACT_10072 Reactome:REACT_10091 Reactome:REACT_10124 related molecular function GO:0015125 bile acid transmembrane transporter HOIP_0003703 Reactome:REACT_10072 Transport (influx) of bile salts and acids by OATP-A, Homo sapiens Reactome:REACT_10091 Transport (influx) of glycocholate and taurocholate by OATP-C, Homo sapiens Reactome:REACT_10124 Transport (influx) of glycocholate and taurocholate by OATP-8, Homo sapiens HOIP:HOIP_0003704 A role played by the entity which enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: bile acid(out) + Na+(out) = bile acid(in) + Na+(in). sodium/bile acid symporter related molecular function GO:0008508 bile acid:sodium symporter HOIP_0003704 HOIP:HOIP_0003705 A role played by the entity which changes the size of the operand(s). role related to changing size HOIP_0003705 HOIP:HOIP_0003706 IMR:0000914 (obsolete) G-protein re;ated molecular function GO:0005525 GTP-binding protein HOIP_0003706 HOIP:HOIP_0003707 The entity of the alpha, beta, and gamma subunits (or beta-gamma dimers) of heterotrimeric guanine nucleotide binding (G) proteins. It is an intracellular membrane-associated protein activated by various receptors (e.g., beta adrenergic). It serves as transducers of the receptor-initiated response linked to intracellular elements, such as enzymes, that generate second messengers to initiate an effect. G-protein heterotrimeric G-protein trimeric GTP-binding protein trimeric G-protein HOIP_0003707 HOIP:HOIP_0003708 A role played by the entity which changes the quality of the operand(s). role related to changing quality HOIP_0003708 HOIP:HOIP_0003709 A role played by the entity to make multiple components to an assembly role related to assembling HOIP_0003709 HOIP:HOIP_0003710 role related to regulating regulator role HOIP_0003710 HOIP:HOIP_0003711 A role played by the entity that inhibits molecular activity. molecular inhibitor HOIP_0003711 HOIP:HOIP_0003712 role related to changing A role played by the entity involved in changing process. changer role HOIP_0003712 HOIP:HOIP_0003713 A role played by the entity which regulates molecular activities. molecular (activity) regulator HOIP_0003713 HOIP:HOIP_0003714 A role played by the entity that activates molecular activity. molecular activator HOIP_0003714 HOIP:HOIP_0003715 type converter is a role played by the entity to change the type of the operand(s) type converter HOIP_0003715 HOIP:HOIP_0003716 A role played by the entity that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to either activate or repress the transcription of specific genes. Coregulators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. A third class modulates interactions of DNA-binding transcription factor with other transcription coregulators. related molecular function GO:0003712 transcription coregulator HOIP_0003716 HOIP:HOIP_0003717 A role played by the entity that interacts specifically and non-covalently with a DNA-bound DNA-binding transcription factor to activate the transcription of specific genes. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP-dependent class modifies the conformation of chromatin. Another type of coregulator activity is the bridging of a DNA-binding transcription factor to the basal transcription machinery. The Mediator complex, which bridges transcription factors and RNA polymerase, is also a transcription coactivator. IMR:0000424 (obsolete) related molecular function GO:0003713 transcriptional co-activator HOIP_0003717 HOIP:HOIP_0003718 lysosomal process HOIP_0003718 HOIP:HOIP_0003719 mitochondrial procress HOIP_0003719 HOIP:HOIP_0003720 A role of the entity which positively/negatively regulates a signaling pathway or metabolic pathway. IMR:0000428 (obsolete) pathway regulator HOIP_0003720 HOIP:HOIP_0003721 IMR:0001160 (obsolete) inhibitor of Wnt signaling pathway negative regulator of Wnt signaling pathway HOIP_0003721 HOIP:HOIP_0003722 A role played by the entity which binds to and modulates the activity of an enzyme. IMR:0000429 (obsolete) related molecular function GO:0030234 catalytic regulator enzyme modulator enzyme regulator HOIP_0003722 HOIP:HOIP_0003723 A role of the entity of binding to a specific ion or molecule and delivering it either to an acceptor molecule or to a specific location. related molecular function GO:0140104 molecular carrier HOIP_0003723 HOIP:HOIP_0003724 A role played by the entity which positively regulates the process of tumorigenesis. positive regulator of tumorigenesis role HOIP_0003724 HOIP:HOIP_0003725 A role played by the entity that regulates the activity of tumor cells. regulator of tumor cell activity role HOIP_0003725 HOIP:HOIP_0003727 A role played by the entity of funtion as realizable entity. functional role HOIP_0003727 HOIP:HOIP_0003728 receiver role related to receiving HOIP_0003728 HOIP:HOIP_0003729 A physical attribute inhering in a bearer by virtue of the bearer's resistance to pressure, being broken, or pierced hardness (attribute) HOIP_0003729 HOIP:HOIP_0003730 A role played by the entity involved in changing some state. changing state role HOIP_0003730 HOIP:HOIP_0003731 A role played by the entity that contributes to keep the structural integrity. keeping structure role HOIP_0003731 HOIP:HOIP_0003732 A role played by the entity which assists the molecule activity. molecular (activity) co-regulator HOIP_0003732 HOIP:HOIP_0003733 Keeping structure is a subtype of changing structure: A process that maintains the structure of the object at a constant level . keeping structure HOIP_0003733 HOIP:HOIP_0003734 GRP94 - tumor cell enhanced survlival factor (canonical)[ER stress] HOIP_0003734 HOIP:HOIP_0003735 PMID:25463537 HSP90B1 - tumor cell production promoting factor (human)[ER stress] HOIP_0003735 PMID:25463537 PMID:25463537 Endoplasmic reticulum heat shock protein gp96 maintains liver homeostasis and promotes hepatocellular carcinogenesis. Inhibition of gp96 in human HCCs perturbed multiple growth signals, and attenuated proliferation and expansion. HOIP:HOIP_0003736 ER stress dependent process (molecular level) is a subtype of ER stress dependent process: A process that can constitute the course of endoplasmic reticulum stress and specifies the molecular level. ER stress dependent process (molecular level) HOIP_0003736 HOIP:HOIP_0003737 The aggregation, arrangement and bonding together of the apoptosome, a multisubunit protein complex involved in the signaling phase of the apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. apoptosome assembly [apoptosis (course)] HOIP_0003737 HOIP:HOIP_0003738 NCBI-Human-GeneID:10053 NCBI-Mouse-GeneID:11768 NCBI-Rat-GeneID:367038 PMID:2335054 Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP1M2 (canonical)[Lipidosis] HOIP_0003738 NCBI-Human-GeneID:10053 http://www.ncbi.nlm.nih.gov/gene/10053 NCBI-Mouse-GeneID:11768 http://www.ncbi.nlm.nih.gov/gene/11768 NCBI-Rat-GeneID:367038 http://www.ncbi.nlm.nih.gov/gene/367038 HOIP:HOIP_0003739 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. This entity is a specific course-dependent process. This process can constitute the course of Cholestasis. leaking content from cell [Cholestasis] HOIP_0003739 HOIP:HOIP_0003740 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of Cholestasis. inflammatory cell infiltration [Cholestasis] HOIP_0003740 HOIP:HOIP_0003741 Increasing organelle volume is a subtype of increasing volume: A process that changes the volume of the organelle to be higher. increasing organelle volume HOIP_0003741 HOIP:HOIP_0003742 Hepatic fibrosis dependent process is a subtype of course dependent process: A process that can constitute the course of hepatic fibrosis. hepatic fibrosis dependent process HOIP_0003742 HOIP:HOIP_0003743 Kupffer cell activation is a subtype of macrophage activation: A change in morphology and behavior of a kupffer cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. kupffer cell activation [hepatic fibrosis course] HOIP_0003743 HOIP:HOIP_0003744 It is an attribute of structure inhering in a bearer by virtue of the bearer's disposition to being permeated or pervaded by a gas or liquid (as by osmosis or diffusion). permeability (attribute) HOIP_0003744 HOIP:HOIP_0003745 The regulated release of cytokines from a cell. Cytokines are any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. cytokine secretion [hepatic fibrosis course] HOIP_0003745 HOIP:HOIP_0003746 A change in the morphology or behavior of a hepatic stellate cell resulting from exposure to a cytokine, chemokine, hormone, cellular ligand or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. hepatic stellate cell activation [hepatic fibrosis course] HOIP_0003746 HOIP:HOIP_0003747 A physical attribute inhering in a fluid (liquid or gas) by virtue of the amount of fluid which passes through a given surface per unit time. fluid flow rate (attribute) HOIP_0003747 HOIP:HOIP_0003748 ISBN:0071769234 CCL4 [NASH] HOIP_0003748 ISBN:0071769234 Types of hepatobiliary injury: Fatty liver: Amiodarone, CCl4, ethanol, fialuridine, tamoxifen, valproic acid in Table 13-2. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition HOIP:HOIP_0003749 Hepatic fibrosis dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the course of hepatic fibrosis. hepatic fibrosis dependent chemical entity HOIP_0003749 HOIP:HOIP_0003750 Hepatic fibrosis dependent gene is a subtype of course dependent chemical entity. This gene can participate in the course of hepatic fibrosis as a gene product. Gene profile:caonical that described in textbooks or articles. hepatic fibrosis dependent molecule (canonical) HOIP_0003750 HOIP:HOIP_0003751 NCBI-Human-GeneID: NCBI-Mouse-GeneID: NCBI-Rat-GeneID: TGFB1 (canonical)[Fibrosis] HOIP_0003751 NCBI-Human-GeneID: http://www.ncbi.nlm.nih.gov/gene/7040 NCBI-Mouse-GeneID: http://www.ncbi.nlm.nih.gov/gene/21803 NCBI-Rat-GeneID: http://www.ncbi.nlm.nih.gov/gene/59086 HOIP:HOIP_0003752 PDGF (canonical)[Fibrosis] HOIP_0003752 HOIP:HOIP_0003753 Counting numbers of objects and how many times an event happens are essential not to individuals in them but to collectives of objects or events. counting quality HOIP_0003753 HOIP:HOIP_0003754 Addition of xenobiotics is a subtype of addition of foreign substance: A process that xenobiotics to make an addition to a cell, organelle, or an organism. addition of xenobiotics HOIP_0003754 HOIP:HOIP_0003755 The multiplication or reproduction of hepatic stellate cells, resulting in the expansion of a hepatic stellate cell population. Hepatic stellate cells are found in the perisinusoidal space of the liver, and are capable of multiple roles including storage of retinol, presentation of antigen to T cells (including CD1d-restricted NKT cells), and upon activation, production of extracellular matrix components. This cell type comprises approximately 8-15% of total cells in the liver. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. hepatic stellate cell proliferation [hepatic fibrosis course] HOIP_0003755 HOIP:HOIP_0003756 Increasing drug metabolite is a subtype of increasing quantity: A process that changes the amount of drug metabolites to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). Increasing drug metabolite [non-alcoholic steatohepatitis (course)] HOIP_0003756 HOIP:HOIP_0003757 The process in which a relatively unspecialized cell acquires specialized features of a myoblast. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into striated muscle fibers. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. myoblast differentiation [hepatic fibrosis course] HOIP_0003757 HOIP:HOIP_0003758 A number quality which is relatively few. decreased number (quality) HOIP_0003758 HOIP:HOIP_0003759 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures in the space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane, and also covers the host cell environment outside an intracellular parasite. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. extracellular matrix organization [hepatic fibrosis course] HOIP_0003759 HOIP:HOIP_0003760 Liver Enriched Antimicrobial Peptide 2 This gene encodes a cysteine-rich cationic antimicrobial peptide that is expressed predominantly in the liver. The mature peptide has activity against gram-positive bacteria and yeasts. [provided by RefSeq, Sep 2014] NCBI-Human-GeneID:116842 NCBI-Mouse-GeneID:259301 NCBI-Rat-GeneID:497901 PMID:27335344 http://www.ncbi.nlm.nih.gov/gene/116842 LEAP2 (human)[Fibrosis] HOIP_0003760 NCBI-Human-GeneID:116842 http://www.ncbi.nlm.nih.gov/gene/116842 NCBI-Mouse-GeneID:259301 http://www.ncbi.nlm.nih.gov/gene/259301 NCBI-Rat-GeneID:497901 http://www.ncbi.nlm.nih.gov/gene/497901 PMID:27335344 These findings suggest a model in which LEAP2 could act at the extracellular level as a modulator of FGF and activin signals in relation with cellular processes such as cell differentiation and migration. HOIP:HOIP_0003761 Any process that decreases the rate, frequency or extent of extracellular matrix disassembly. Extracellular matrix disassembly is a process that results in the breakdown of the extracellular matrix. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. negative regulation of extracellular matrix disassembly [hepatic fibrosis course] HOIP_0003761 HOIP:HOIP_0003762 High Mobility Group AT-Hook 1 This gene encodes a chromatin-associated protein involved in the regulation of gene transcription, integration of retroviruses into chromosomes, and the metastatic progression of cancer cells. The encoded protein preferentially binds to the minor groove of AT-rich regions in double-stranded DNA. Multiple transcript variants encoding different isoforms have been found for this gene. Pseudogenes of this gene have been identified on multiple chromosomes. [provided by RefSeq, Jan 2016] https://omim.org/entry/600701 NCBI-Human-GeneID:3159 NCBI-Mouse-GeneID:15361 NCBI-Rat-GeneID:117062 PMID:27001612  PMID:27855356 http://www.ncbi.nlm.nih.gov/gene/3159 HMGA1 (human)[Fibrosis] HOIP_0003762 NCBI-Human-GeneID:3159 http://www.ncbi.nlm.nih.gov/gene/3159 NCBI-Mouse-GeneID:15361 http://www.ncbi.nlm.nih.gov/gene/15361 NCBI-Rat-GeneID:117062 http://www.ncbi.nlm.nih.gov/gene/117062 PMID:27001612  The High Mobility Group A1 (HMGA1) gene is highly overexpressed in human uterine serous carcinomas and carcinosarcomas and drives Matrix Metalloproteinase-2 (MMP-2) in a subset of tumors. PMID:27855356 HMGA1 Expression in Human Hepatocellular Carcinoma Correlates with Poor Prognosis and Promotes Tumor Growth and Migration in in vitro Models. HMGA1 is frequently expressed in cirrhotic tissues and HCCs and its expression is associated with worse prognosis in HCC. HOIP:HOIP_0003763 This course is categorized from the viewpoint of pathological findings derived by inference. course based on pathological findings HOIP_0003763 HOIP:HOIP_0003766 CERB processing is a subtype of protein processing: CREB maturation process achieved by the cleavage of a peptide bond or bonds within CREB protein. CERB processing HOIP_0003766 HOIP:HOIP_0003767 NCBI-Human-GeneID:1906 NCBI-Mouse-GeneID:13614 NCBI-Rat-GeneID:24323 ET-1 (canonical)[Fibrosis] HOIP_0003767 NCBI-Human-GeneID:1906 http://www.ncbi.nlm.nih.gov/gene/1906 NCBI-Mouse-GeneID:13614 http://www.ncbi.nlm.nih.gov/gene/13614 NCBI-Rat-GeneID:24323 http://www.ncbi.nlm.nih.gov/gene/24323 HOIP:HOIP_0003768 NCBI-Human-GeneID:6347 NCBI-Mouse-GeneID:20296 NCBI-Rat-GeneID:24770 CCL2 (canonical)[Fibrosis] HOIP_0003768 NCBI-Human-GeneID:6347 http://www.ncbi.nlm.nih.gov/gene/6347 NCBI-Mouse-GeneID:20296 http://www.ncbi.nlm.nih.gov/gene/20296 NCBI-Rat-GeneID:24770 http://www.ncbi.nlm.nih.gov/gene/24770 HOIP:HOIP_0003769 acetaldehyde [Fibrosis] HOIP_0003769 HOIP:HOIP_0003770 The chemical reactions resulting in the breakdown of misfolded proteins in the cytoplasm, which are targeted to cytoplasmic proteasomes for degradation. cytoplasm-associated proteasomal ubiquitin-dependent protein catabolism cytoplasm-associated proteasomal ubiquitin-dependent protein degradation See also the biological process terms 'unfolded protein response ; GO:0030968' and 'retrograde protein transport, ER to cytosol ; GO:0030970'. cytoplasm protein quality control by the ubiquitin-proteasome system HOIP_0003770 HOIP:HOIP_0003771 Hepatic fibrosis dependent chemical compound is a subtype of course dependent chemical entity. This entity (drug) can participate in the course of hepatic fibrosis. hepatic fibrosis dependent chemical compound HOIP_0003771 HOIP:HOIP_0003772 CCL4 [Fibrosis] HOIP_0003772 HOIP:HOIP_0003773 NCBI-Human-GeneID:4318 NCBI-Mouse-GeneID:17395 NCBI-Rat-GeneID:81687 MMP9 (canonical)[Fibrosis] HOIP_0003773 NCBI-Human-GeneID:4318 http://www.ncbi.nlm.nih.gov/gene/4318 NCBI-Mouse-GeneID:17395 http://www.ncbi.nlm.nih.gov/gene/17395 NCBI-Rat-GeneID:81687 http://www.ncbi.nlm.nih.gov/gene/81687 HOIP:HOIP_0003774 A protein with a core domain composition consisting of a propeptide region and an Interleukin-1 / 18 domain. NCBI-Human-GeneID:3552 NCBI-Mouse-GeneID:16175 NCBI-Rat-GeneID:24493 IL-1 (canonical)[Fibrosis] HOIP_0003774 NCBI-Human-GeneID:3552 http://www.ncbi.nlm.nih.gov/gene/3552 NCBI-Mouse-GeneID:16175 http://www.ncbi.nlm.nih.gov/gene/16175 NCBI-Rat-GeneID:24493 http://www.ncbi.nlm.nih.gov/gene/24493 HOIP:HOIP_0003775 NCBI-Human-GeneID:3569 NCBI-Mouse-GeneID:16193 NCBI-Rat-GeneID:24498 IL-6 (canonical)[Fibrosis] HOIP_0003775 NCBI-Human-GeneID:3569 http://www.ncbi.nlm.nih.gov/gene/3569 NCBI-Mouse-GeneID:16193 http://www.ncbi.nlm.nih.gov/gene/16193 NCBI-Rat-GeneID:24498 http://www.ncbi.nlm.nih.gov/gene/24498 HOIP:HOIP_0003776 A tumor necrosis factor that is encoded in the genome of human. NCBI-Human-GeneID:7124 NCBI-Mouse-GeneID:21926 NCBI-Rat-GeneID:24835 TNFΑ (canonical)[Fibrosis] HOIP_0003776 NCBI-Human-GeneID:7124 http://www.ncbi.nlm.nih.gov/gene/7124 NCBI-Mouse-GeneID:21926 http://www.ncbi.nlm.nih.gov/gene/21926 NCBI-Rat-GeneID:24835 http://www.ncbi.nlm.nih.gov/gene/24835 HOIP:HOIP_0003777 NCBI-Human-GeneID:4313 NCBI-Mouse-GeneID:17390 NCBI-Rat-GeneID:81686 MMP2 (canonical)[Fibrosis] HOIP_0003777 NCBI-Human-GeneID:4313 http://www.ncbi.nlm.nih.gov/gene/4313 NCBI-Mouse-GeneID:17390 http://www.ncbi.nlm.nih.gov/gene/17390 NCBI-Rat-GeneID:81686 http://www.ncbi.nlm.nih.gov/gene/81686 HOIP:HOIP_0003778 NCBI-Human-GeneID:2833 NCBI-Mouse-GeneID:12766 NCBI-Rat-GeneID:84475 CXCR3 (canonical)[Fibrosis] HOIP_0003778 NCBI-Human-GeneID:2833 http://www.ncbi.nlm.nih.gov/gene/2833 NCBI-Mouse-GeneID:12766 http://www.ncbi.nlm.nih.gov/gene/12766 NCBI-Rat-GeneID:84475 http://www.ncbi.nlm.nih.gov/gene/84475 HOIP:HOIP_0003779 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. necrosis [hepatic fibrosis course] HOIP_0003779 HOIP:HOIP_0003780 CCL3 production is a subtype of generating a substance : A process that synthesizes trichloromethyl(.) as output. CCL3 production HOIP_0003780 HOIP:HOIP_0003781 Decreasing blood flow is a subtype of decreasing flow: A process that changes the blood flow to be smaller. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. decreasing blood flow [hepatic fibrosis course] HOIP_0003781 HOIP:HOIP_0003782 Scarring is a subtype of changing material: A process of keeping area replaced into fibrous tissue by injury. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. scarring [hepatic fibrosis course] HOIP_0003782 HOIP:HOIP_0003783 The process in which the anatomical structures of the nodule are generated and organized. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. nodule formation [hepatic fibrosis course] HOIP_0003783 HOIP:HOIP_0003784 NCBI-Human-GeneID:7077 TIMP2 (mol) HOIP_0003784 NCBI-Human-GeneID:7077 http://www.ncbi.nlm.nih.gov/gene/7076 HOIP:HOIP_0003785 TIMP2 (canonical)[Fibrosis] HOIP_0003785 HOIP:HOIP_0003786 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. negative regulation of apoptotic process [hepatic fibrosis course] HOIP_0003786 HOIP:HOIP_0003787 CCL3 production is a subtype of generating a substance : A process that synthesizes trichloromethyl(.) as output. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). PMID:12708612 CCL3 production [non-alcoholic steatohepatitis (course)] HOIP_0003787 PMID:12708612 CCl4 is activated by cytochrome (CYP)2E1, CYP2B1 or CYP2B2, and possibly CYP3A, to form the trichloromethyl radical, CCl3*. HOIP:HOIP_0003789 Decreasing stored glycogen is a subtype of decreasing glycogen level: A process that changes the stored amount of glycogen level to be lower. decreasing stored glycogen HOIP_0003789 HOIP:HOIP_0003792 NCBI-Human-GeneID:1571 NCBI-Mouse-GeneID:13106 NCBI-Rat-GeneID:25086 CYP2E1 (canonical)[Lipidosis] HOIP_0003792 NCBI-Human-GeneID:1571 http://www.ncbi.nlm.nih.gov/gene/1571 NCBI-Mouse-GeneID:13106 http://www.ncbi.nlm.nih.gov/gene/13106 NCBI-Rat-GeneID:25086 http://www.ncbi.nlm.nih.gov/gene/25086 HOIP:HOIP_0003794 Prevention of degradation of mRNA molecules. In the absence of compensating changes in other processes, the slowing of mRNA degradation can result in an overall increase in the population of active mRNA molecules. http://purl.obolibrary.org/obo/GO_0048255 negative regulation of mRNA degradation HOIP_0003794 HOIP:HOIP_0003797 Changing cycle phase is a subtype of changing quality: A process that changes the cycle phase. changing periodicity changing cycle phase HOIP_0003797 HOIP:HOIP_0003798 Maintaining cyclicity is a subtype of changing cyclicity: A process that keepss the repeating values in regular cycles (periods). maintaining cyclicity HOIP_0003798 HOIP:HOIP_0003799 Cytochrome P450 activation is a subtype of molecular activation: A process that changes the activity of the cytochrome P450 to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). PMID:2708612 Cytochrome P450 activation [glutathione depletion (course)] P450 activation [glutathione depletion (course)] Cytochrome P450 activation [non-alcoholic steatohepatitis (course)] HOIP_0003799 PMID:26456005 HOIP:HOIP_0003800 Extracellular matrix production- degradation imbalance is a subtype of imbalance: A process that lacks a balance between extracellular matrix production and degradation. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. extracellular matrix production- degradation imbalance [hepatic fibrosis course] HOIP_0003800 HOIP:HOIP_0003801 Extracellular matrix production- degradation imbalance is a subtype of imbalance: A process that lacks a balance between extracellular matrix production and degradation. extracellular matrix production- degradation imbalance HOIP_0003801 HOIP:HOIP_0003802 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. hepatic fibrosis [hepatic fibrosis course] HOIP_0003802 HOIP:HOIP_0003803 The totality of all processes through which hepatic fibrosis is realized by alcoholic liver injury. under construction hepatic fibrosis by alcoholic liver injury HOIP_0003803 HOIP:HOIP_0003805 NCBI-Human-GeneID:1544 NCBI-Mouse-GeneID:13077 NCBI-Rat-GeneID:24297 PMID:19590965 PMID:21177773 CYP1A2(canonical) [glutathione depletion (course)] HOIP_0003805 NCBI-Human-GeneID:1544 http://www.ncbi.nlm.nih.gov/gene/1544 NCBI-Mouse-GeneID:13077 http://www.ncbi.nlm.nih.gov/gene/13077 NCBI-Rat-GeneID:24297 http://www.ncbi.nlm.nih.gov/gene/24297 PMID:19590965 The critically reactive metabolite of AFB1 is the exo 8,9-epoxide formed by a two-electron oxidation mainly catalyzed by CYP3A4, with contribution from CYP1A2 and other CYPs. PMID:21177773 Cytochrome P450 (CYP) enzymes, including CYP2E1, CYP1A2, and CYP3A4, convert 5–9% of acetaminophen to a highly reactive metabolite, N-acetyl-p-benzoquinonimine (NAPQI) (Corcoran et al., 1980; Dahlin et al., 1984). HOIP:HOIP_0003806 Overeating is a subtype of increasing quantity: A process that changes the ingestion amount of food to be larger. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). overeating [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003806 HOIP:HOIP_0003807 Increasing fatty acid synthesis substrate is a subtype of increasing quantity: A process that changes the production amount of the substrate of the fatty acid synthesis. This entity is a specific course-dependent process. This process can constitute the course of [non-alcoholic fatty liver disease (NAFLD)]. increasing fatty acid synthesis substrate [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003807 HOIP:HOIP_0003808 Converting to acetyl CoA is a subtype of metabolic process. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). converting to acetyl CoA [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003808 HOIP:HOIP_0003809 Increasing amount of carbohydrate is a subtype of increasing quantity: A process that changes the amount of carbohydrates to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). increasing amount of carbohydrate [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003809 HOIP:HOIP_0003810 Increase in lipid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the lipid inflow into the hepatocyte to be larger. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). increase in lipid inflow into hepatocyte [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003810 HOIP:HOIP_0003811 Increaing in fatty acid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the fatty acid inflow into the hepatocyte to be larger. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). increaing in fatty acid inflow into hepatocyte [non-alcoholic fatty liver disease (NAFLD)] HOIP_0003811 HOIP:HOIP_0003812 NCBI-Human-GeneID:6720 NCBI-Mouse-GeneID:20787 NCBI-Rat-GeneID:78968 PMID:10962028 PMID:20817607 PMID:21286345 SREBP1C (canonical)[Lipidosis] HOIP_0003812 NCBI-Human-GeneID:6720 http://www.ncbi.nlm.nih.gov/gene/6720 NCBI-Mouse-GeneID:20787 http://www.ncbi.nlm.nih.gov/gene/20787 NCBI-Rat-GeneID:78968 http://www.ncbi.nlm.nih.gov/gene/78968 HOIP:HOIP_0003813 Negative regulation of adherens junction assembly is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of adherens junction assembly. negative regulation of adherens junction assembly HOIP_0003813 HOIP:HOIP_0003814 A role played by the entity to transmit something to be detected. signal role HOIP_0003814 HOIP:HOIP_0003815 Molecular assembly is a subtype of assembling: The aggregation, arrangement and bonding together of molecules. molecular assembly HOIP_0003815 HOIP:HOIP_0003816 A role played by the entity to transmit the stress to be detected. stress signal role HOIP_0003816 HOIP:HOIP_0003817 NCBI-Human-GeneID:3690 NCBI-Mouse-GeneID:16416 NCBI-Rat-GeneID:29302 ITGB3 (mol) HOIP_0003817 NCBI-Human-GeneID:3690 https://www.ncbi.nlm.nih.gov/gene/3690 NCBI-Mouse-GeneID:16416 https://www.ncbi.nlm.nih.gov/gene/16416 NCBI-Rat-GeneID:29302 https://www.ncbi.nlm.nih.gov/gene/29302 HOIP:HOIP_0003818 Open TG-Gates compound_id:00A02 PMID:26977301 tunicamycin - apoptosis inducer [ER stress] HOIP_0003818 PMID:26977301 HOIP:HOIP_0003819 Open TG-Gates compound_id:00A02 PMID:26977301 tunicamycin - lipidosis inducer [ER stress] HOIP_0003819 HOIP:HOIP_0003820 Lipofuscin (age pigment) is a brown-yellow, electron-dense, autofluorescent material that accumulates progressively over time in lysosomes. lipofuscin HOIP_0003820 HOIP:HOIP_0003821 Melanin granule is a sutype of pigment granule melanin granule HOIP_0003821 HOIP:HOIP_0003822 A role played by the entity which involves in inducing lipidosis lipidosis inducer role steatosis inducer role HOIP_0003822 HOIP:HOIP_0003823 NCBI-Human-GeneID:1385 CREB1 (mol) HOIP_0003823 NCBI-Human-GeneID:1385 http://www.ncbi.nlm.nih.gov/gene/1385 HOIP:HOIP_0003824 Lysosomal cholesterol storage is a subtype of cholesterol storage: A process that keeps cholesterol in the lysosome severely. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. lysosomal cholesterol storage (severe) [phospholipidosis (severe) HOIP_0003824 PMID:23921551 HOIP:HOIP_0003825 Inflammasome activation is a subtype of activating: A process that changes the activity of the inflammasome to be higher. This entity is a specific course-dependent process. This process can constitute the course of pyroptosis. PMID:18667412 PMID:21760595 inflammasome activation [pyroptosis (course)] HOIP_0003825 HOIP:HOIP_0003826 NCBI-Human-GeneID:834 PMID:20303873 CASP1 (canonical)[pyroptopsis] HOIP_0003826 NCBI-Human-GeneID:834 http://www.ncbi.nlm.nih.gov/gene/834 HOIP:HOIP_0003827 Inflammatory cytokine gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of pyroptosis. inflammatory cytokine gene expression [pyroptosis (course)] HOIP_0003827 HOIP:HOIP_0003828 NCBI-Human-GeneID:3553 NCBI-Mouse-GeneID:16176 NCBI-Rat-GeneID:24494 PMID:21760595 IL-1B (canonical)[pyroptosis] HOIP_0003828 NCBI-Human-GeneID:3553 http://www.ncbi.nlm.nih.gov/gene/3553 NCBI-Mouse-GeneID:16176 http://www.ncbi.nlm.nih.gov/gene/16176 NCBI-Rat-GeneID:24494 http://www.ncbi.nlm.nih.gov/gene/24494 HOIP:HOIP_0003829 Compound accumulation in liver is a subtype of accumulation of xenobiotics: A process that keeps compound in the liver. This entity is a specific course-dependent process. This process can constitute the course of necrosis. compound accumulation in liver [necrosis (course)] HOIP_0003829 HOIP:HOIP_0003830 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of pyroptosis. inflammatory response [pyroptosis (course)] HOIP_0003830 HOIP:HOIP_0003831 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course-dependent process. This process can constitute the course of pyroptosis. inflammatory cell infiltration [pyroptosis (course)] HOIP_0003831 HOIP:HOIP_0003832 NCBI-Human-GeneID:6819 NCBI-Mouse-GeneID:69083 NCBI-Rat-GeneID:171072 SULT1C2 (mol) HOIP_0003832 NCBI-Human-GeneID:6819 https://www.ncbi.nlm.nih.gov/gene/6819 NCBI-Mouse-GeneID:69083 https://www.ncbi.nlm.nih.gov/gene/69083 NCBI-Rat-GeneID:171072 https://www.ncbi.nlm.nih.gov/gene/171072 HOIP:HOIP_0003833 NCBI-Human-GeneID:166785 NCBI-Mouse-GeneID:109136 NCBI-Rat-GeneID:291939 PMID:15523652 MMAA (mol) HOIP_0003833 NCBI-Human-GeneID:166785 https://www.ncbi.nlm.nih.gov/gene/166785 NCBI-Mouse-GeneID:109136 https://www.ncbi.nlm.nih.gov/gene/109136 NCBI-Rat-GeneID:291939 https://www.ncbi.nlm.nih.gov/gene/291939 HOIP:HOIP_0003834 NCBI-Human-GeneID:10417 NCBI-Mouse-GeneID:100689 NCBI-Rat-GeneID:171569 https://omim.org/entry/605918 SPON2 (mol) HOIP_0003834 NCBI-Human-GeneID:10417 https://www.ncbi.nlm.nih.gov/gene/10417 NCBI-Mouse-GeneID:100689 https://www.ncbi.nlm.nih.gov/gene/100689 NCBI-Rat-GeneID:171569 https://www.ncbi.nlm.nih.gov/gene/171569 HOIP:HOIP_0003835 NCBI-Human-GeneID:91543 NCBI-Mouse-GeneID:58185 NCBI-Rat-GeneID:65190 RSAD2 (mol) HOIP_0003835 NCBI-Human-GeneID:91543 https://www.ncbi.nlm.nih.gov/gene/91543 NCBI-Mouse-GeneID:58185 https://www.ncbi.nlm.nih.gov/gene/58185 NCBI-Rat-GeneID:65190 https://www.ncbi.nlm.nih.gov/gene/65190 HOIP:HOIP_0003836 NCBI-Human-GeneID:1579 NCBI-Rat-GeneID:24306 https://omim.org/entry/601310 CYP4A11 (mol) HOIP_0003836 NCBI-Human-GeneID:1579 https://www.ncbi.nlm.nih.gov/gene/1579 NCBI-Rat-GeneID:24306 https://www.ncbi.nlm.nih.gov/gene/24306 HOIP:HOIP_0003837 NCBI-Human-GeneID:57600 NCBI-Mouse-GeneID:329679 NCBI-Rat-GeneID:310538 FNIP2 (mol) HOIP_0003837 NCBI-Human-GeneID:57600 https://www.ncbi.nlm.nih.gov/gene/57600 NCBI-Mouse-GeneID:329679 https://www.ncbi.nlm.nih.gov/gene/329679 NCBI-Rat-GeneID:310538 https://www.ncbi.nlm.nih.gov/gene/310538 HOIP:HOIP_0003838 NCBI-Human-GeneID:5570 NCBI-Mouse-GeneID:18768 NCBI-Rat-GeneID:24678 https://omim.org/entry/606914 PKIB (mol) HOIP_0003838 NCBI-Human-GeneID:5570 https://www.ncbi.nlm.nih.gov/gene/5570 NCBI-Mouse-GeneID:18768 https://www.ncbi.nlm.nih.gov/gene/18768 NCBI-Rat-GeneID:24678 https://www.ncbi.nlm.nih.gov/gene/24678 HOIP:HOIP_0003839 NCBI-Human-GeneID:3778 NCBI-Mouse-GeneID:16531 NCBI-Rat-GeneID:83731 KCNMA1 (mol) HOIP_0003839 NCBI-Human-GeneID:3778 https://www.ncbi.nlm.nih.gov/gene/3778 NCBI-Mouse-GeneID:16531 https://www.ncbi.nlm.nih.gov/gene/16531 NCBI-Rat-GeneID:83731 https://www.ncbi.nlm.nih.gov/gene/83731 HOIP:HOIP_0003840 NCBI-Human-GeneID:443 NCBI-Mouse-GeneID:11484 NCBI-Rat-GeneID:79251 ASPA (mol) HOIP_0003840 NCBI-Human-GeneID:443 https://www.ncbi.nlm.nih.gov/gene/443 NCBI-Mouse-GeneID:11484 https://www.ncbi.nlm.nih.gov/gene/11484 NCBI-Rat-GeneID:79251 https://www.ncbi.nlm.nih.gov/gene/79251 HOIP:HOIP_0003841 NCBI-Human-GeneID:1601 NCBI-Mouse-GeneID:13132 NCBI-Rat-GeneID:79128 DAB2 (mol) HOIP_0003841 NCBI-Human-GeneID:1601 https://www.ncbi.nlm.nih.gov/gene/1601 NCBI-Mouse-GeneID:13132 https://www.ncbi.nlm.nih.gov/gene/13132 NCBI-Rat-GeneID:79128 https://www.ncbi.nlm.nih.gov/gene/79128 HOIP:HOIP_0003842 NCBI-Human-GeneID:374383 NCBI-Rat-GeneID:691092 PMID:19528259 https://omim.org/entry/613714 NCR3LG1 (mol) HOIP_0003842 NCBI-Human-GeneID:374383 https://www.ncbi.nlm.nih.gov/gene/374383 NCBI-Rat-GeneID:691092 https://www.ncbi.nlm.nih.gov/gene/691092 PMID:19528259 The B7 family member B7-H6 is a tumor cell ligand for the activating natural killer cell receptor NKp30 in humans. HOIP:HOIP_0003854 Making existence of drug is a subtype of making existence of xenobiotics: A process that makes a drug to be present in in a cell, organelle, or an organism. making existence of drug HOIP_0003854 HOIP:HOIP_0003862 9970 NCBI-Human-GeneID:9970 NCBI-Mouse-GeneID:12355 NCBI-Rat-GeneID:65035 Constitutive Androstane Receptor NR1I3 CAR (mol) HOIP_0003862 NCBI-Human-GeneID:9970 http://www.ncbi.nlm.nih.gov/gene/9970 NCBI-Mouse-GeneID:12355 http://www.ncbi.nlm.nih.gov/gene/12355 NCBI-Rat-GeneID:65035 http://www.ncbi.nlm.nih.gov/gene/65035 HOIP:HOIP_0003863 A role played by the entity which receives xenobiotics (signal) and transmits operand(s). xenosensor HOIP_0003863 HOIP:HOIP_0003867 Clonal expansion of preneoplastic cell is a subtype of clonal expansion: A process that becomes larger in the number of preneoplastic cells by cell division of a population of identical cells descended from a single progenitor. clonal expansion of preneoplastic cell HOIP_0003867 HOIP:HOIP_0003877 Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). PMID:27398911 positive regulation of autophagy [phospholipidosis (severe (excessive defense))] HOIP_0003877 HOIP:HOIP_0003880 A role played by the entity which positively regulates the tumor metastasis. tumor metastasis inducer HOIP_0003880 HOIP:HOIP_0003882 Negative regulation of arachidonic acid metabolic process is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the arachidonic acid metabolism. negative regulation of arachidonic acid metabolic process HOIP_0003882 HOIP:HOIP_0003883 Hyperfunctioning of apoptotic process is a subtype of hyperfunctioning: A process that performs an excesssive autophagy. hyperfunctioning of autophagy HOIP_0003883 HOIP:HOIP_0003884 The chemical reactions and pathways involving arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer. The chemical reactions and pathways involving arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer. Wikipedia:Arachidonic_acid arachidonic acid metabolism HOIP_0003884 The chemical reactions and pathways involving arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer. ISBN:0198506732 HOIP:HOIP_0003885 The chemical reactions and pathways by which arachidonic acid is converted to other compounds initially by omega-hydroxylation. The chemical reactions and pathways by which arachidonic acid is converted to other compounds initially by omega-hydroxylation. omega-hydroxylase P450 pathway HOIP_0003885 The chemical reactions and pathways by which arachidonic acid is converted to other compounds initially by omega-hydroxylation. PMID:10681399 HOIP:HOIP_0003886 Negative regulation of arachidonic acid metabolic process is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the arachidonic acid metabolism. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). negative regulation of arachidonic acid metabolic process [phospholipidosis (severe)] HOIP_0003886 HOIP:HOIP_0003887 fatty acid omega-hydroxylase activity HOIP_0003887 HOIP:HOIP_0003888 A role played by the entity which inhibits the tumor progression. tumor progression inhibitor HOIP_0003888 HOIP:HOIP_0003889 Hyperfunctioning of apoptotic process is a subtype of hyperfunctioning: A process that performs an excesssive apoptosis. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)) . PMID:17090686 Hyperfunctioning of apoptotic process [phospholipidosis (severe (excessive defense)) ] HOIP_0003889 PMID:17090686 Sphingosine-1-phosphate lyase potentiates apoptosis via p53- and p38-dependent pathways and is down-regulated in colon cancer. HOIP:HOIP_0003890 TGFbeta signaling is a process that a signal is transmitted by the cytokine TGFbeta. This process is dependent on the apoptosis inhibition and can constitute the course of phospholipidosis (severe (excessive defense)). TGF beta receptor signaling [phospholipidosis (severe (excessive defense)) - apoptosis inhibition ] HOIP_0003890 PMID:9108028 HOIP:HOIP_0003898 Degradation of Dab2 is a subtype of protein catabolic process: A process of the chemical reactions resulting in the breakdown of Dab2. degradation of Dab2 HOIP_0003898 HOIP:HOIP_0003899 Degradation of Dab2 is a subtype of protein catabolic process: A process of the chemical reactions resulting in the breakdown of Dab2. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). degradation of Dab2 [phospholipidosis (severe (excessive defense))] HOIP_0003899 HOIP:HOIP_0003911 A role of the entity which negatively regulates the EGFR signaling pathway. EGFR pathway negative regulator role HOIP_0003911 HOIP:HOIP_0003917 Translocation of CAR from the cytosol to the nucleus is a subtype of nuclear transport: A process that of the directed movement of CAR from the cytoplasm to the nucleus. Translocation of CAR from the cytosol to the nucleus HOIP_0003917 HOIP:HOIP_0003920 Hypofunction of gluconeogenesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient gluconeogenesis. hypofunction of gluconeogenesis HOIP_0003920 HOIP:HOIP_0003928 A role played by the entity involved in gluconeogenesis. gluconeogenic factor HOIP_0003928 HOIP:HOIP_0003929 A role played by the entity which inhibits gluconeogenesis. gluconeogenesis inhibitor role HOIP_0003929 HOIP:HOIP_0003934 A role played by the entity that activates AMPK activity. AMPK activator HOIP_0003934 HOIP:HOIP_0003935 FOXO1 inactivation is a subtype of inactivating: A process that changes the activity of the FOXO1 to be lower. FOXO1 inactivation HOIP_0003935 HOIP:HOIP_0003937 Regulation of gluconeogenesis gene expression is a subtype of regulation of gene expression: A process that modulates the frequency, rate or extent of gluconeogenesis gene expression. regulation of gluconeogenesis gene expression HOIP_0003937 HOIP:HOIP_0003938 Negative regulation of gluconeogenesis gene expression is a subtype of regulation of gluconeogenesis gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of gluconeogenesis gene expression. negative regulation of gluconeogenesis gene expression HOIP_0003938 HOIP:HOIP_0003939 Negative regulation of gluconeogenesis gene expression is a subtype of regulation of gluconeogenesis gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of gluconeogenesis gene expression. This entity is a specific course-dependent process. This process can constitute the course of Ground glass appearance. negative regulation of gluconeogenesis gene expression [Ground glass appearance] HOIP_0003939 HOIP:HOIP_0003940 Negative regulation of G6Pase expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of G6Pase expression. negative regulation of G6Pase expression HOIP_0003940 HOIP:HOIP_0003946 A role that represses the rate, timing and/or magnitude of transcription of FOXO1. trannscriptional repressor of FOXO1 HOIP_0003946 HOIP:HOIP_0003947 A role that activates, or increases the rate, timing and/or magnitude of transcription of gluconeogenic gene. positive regulator of gluconeogenic gene transcription role HOIP_0003947 HOIP:HOIP_0003949 A role played by the entity which regulates carbohydrate metabolic process. carbohydrate sysnthesis regulator role HOIP_0003949 HOIP:HOIP_0003950 Increasing AMP/ATP ratio is a subtype of increasing ratio: A process that changes the ratio of AMP to ATP to be higher. increasing AMP/ATP ratio HOIP_0003950 HOIP:HOIP_0003959 SREBP1 inactivation is a subtype of inactivating: A process that changes the activity of the SREBP1 to be lower. SREBP1 inactivation HOIP_0003959 HOIP:HOIP_0003962 Decreasing hepatic triglyceride is a subtype of decreasing lipid: A process that changes the quantity of the hepatic triglyceride in lysosomal membranes to be lower. decreasing hepatic triglyceride HOIP_0003962 HOIP:HOIP_0003963 Decreasing cholesterol is a subtype of decreasing lipid: A process that changes the amount of cholesterol to be lower. decreasing cholesterol HOIP_0003963 HOIP:HOIP_0003966 NCBI-Human-GeneID:6720 NCBI-Mouse-GeneID:20787 NCBI-Rat-GeneID:78968 SREBP1 Sterol Regulatory Element Binding Transcription Factor 1 http://omim.org/entry/184756 SREBF1 (mol) HOIP_0003966 NCBI-Human-GeneID:6720 http://www.ncbi.nlm.nih.gov/gene/6720 NCBI-Mouse-GeneID:20787 http://www.ncbi.nlm.nih.gov/gene/20787 NCBI-Rat-GeneID:78968 http://www.ncbi.nlm.nih.gov/gene/78968 HOIP:HOIP_0003967 A role played by the entity which positively regulates the formation of lipids. lipid synthesis positive regulator role HOIP_0003967 HOIP:HOIP_0003968 A role played by the entity which positively regulates the formation of cholesterol. cholesterol synthesis positive regulator role HOIP_0003968 HOIP:HOIP_0003970 Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. Multiple alternatively spliced transcript variants divergent in the 5' sequence and encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008] NCBI-Human-GeneID:31 NCBI-Mouse-GeneID:107476 NCBI-Rat-GeneID:60581 ACC (mol) HOIP_0003970 NCBI-Human-GeneID:31 http://www.ncbi.nlm.nih.gov/gene/31 NCBI-Mouse-GeneID:107476 http://www.ncbi.nlm.nih.gov/gene/107476 NCBI-Rat-GeneID:60581 http://www.ncbi.nlm.nih.gov/gene/60581 HOIP:HOIP_0003973 A role played by the entity which positively regulates the formation of fatty acid. fatty acid synthesis positive regulator role HOIP_0003973 HOIP:HOIP_0003974 ACACB (mol) HOIP_0003974 HOIP:HOIP_0003978 Negative regulation of ATP consuming is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of ATP consuming. negative regulation of ATP consuming HOIP_0003978 HOIP:HOIP_0003981 NUAK Family Kinase NUAK HOIP_0003981 HOIP:HOIP_0003982 9891 NUAK1 (mol) HOIP_0003982 HOIP:HOIP_0003984 Sphingomyelin homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. This process is dependent on the genetic and can constitute the course of sphingomyelin disorder (genetic). sphingomyelin homeostasis imbalance [sphingomyelin disorder (genetic)] HOIP_0003984 HOIP:HOIP_0003985 Phospholipid homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. This process is dependent on the genetic and can constitute the course of Phospholipidosis (genetic). phospholipid homeostasis imbalance [phospholipidosis (genetic)] HOIP_0003985 HOIP:HOIP_0003986 Sphingomyelin homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. sphingomyelin homeostasis imbalance [course of Niemann–Pick disease type A] HOIP_0003986 HOIP:HOIP_0003987 Sphingomyelin homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type B. sphingomyelin homeostasis imbalance [course of Niemann–Pick disease type B] HOIP_0003987 HOIP:HOIP_0003988 Sphingomyelin homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B. sphingomyelin homeostasis imbalance [course of Niemann–Pick disease type A and type B] HOIP_0003988 HOIP:HOIP_0003989 A role played by the entity that diminishes the rate of a chemical reaction competitively. http://purl.obolibrary.org/obo/SBO_0000206 competitive inhibitor HOIP_0003989 HOIP:HOIP_0003990 Leukocyte infiltration is a subtype of inflammatory cell inflow: A process that that moves the outside leukocyte cell to the inside. leukocyte infiltration HOIP_0003990 HOIP:HOIP_0003991 Glutathione conjugation is a detoxication reaction. Four types of activation reaction have been recognized: direct-acting compounds, conjugates that are activated through cysteine conjugate beta-lyase, conjugates that are activated through redox cycling and lastly conjugates that release the original reactive parent compound. The glutathione S-transferases have three connections with the formation of biactivated conjugatesto make them more soluble for excretion. Glutathione conjugation is a detoxication reaction. Four types of activation reaction have been recognized: direct-acting compounds, conjugates that are activated through cysteine conjugate beta-lyase, conjugates that are activated through redox cycling and lastly conjugates that release the original reactive parent compound. The glutathione S-transferases have three connections with the formation of biactivated conjugatesto make them more soluble for excretion. Glutathione S-Transferases (GSTs; EC 2.5.1.18) are another major set of phase II conjugation enzymes. They can be found in the cytosol as well as being microsomal membrane-bound. Cytosolic GSTs are encoded by at least 5 gene families (alpha, mu, pi, theta and zeta GST) whereas membrane-bound enzymes are encoded by single genes. Soluble GSTs are homo- or hetero-dimeric enzymes (approximately 25KDa subunits) which can act on a wide range of endogenous and exogenous electrophiles. GSTs mediate conjugation using glutathione (GSH), a tripeptide synthesized from its precursor amino acids gamma-glutamate, cysteine and glycine. A generalized reaction isRX + GSH -> HX + GSRGlutathione conjugates are excreted in bile and converted to cysteine and mercapturic acid conjugates in the intestine and kidneys. GSH is the major, low molecular weight, non-protein thiol synthesized de novo in mammalian cells. As well as taking part in conjugation reactions, GSH also has antioxidant ability and can metabolize endogenous and exogenous compounds. The nucleophilic GSH attacks the electrophilic substrate forming a thioether bond between the cysteine residue of GSH and the electrophile. The result is generally a less reactive and more water-soluble conjugate that can be easily excreted. In some cases, GSTs can activate compounds to reactive species such as certain haloalkanes and haloalkenes. Substrates for GSTs include epoxides, alkenes and compounds with electrophilic carbon, sulfur or nitrogen centres. There are two types of conjugation reaction with glutathione: displacement reactions where glutathione displaces an electron-withdrawing group and addition reactions where glutathione is added to activated double bond structures or strained ring systems. Glutathione S-Transferases (GSTs; EC 2.5.1.18) are another major set of phase II conjugation enzymes. They can be found in the cytosol as well as being microsomal membrane-bound. Cytosolic GSTs are encoded by at least 5 gene families (alpha, mu, pi, theta and zeta GST) whereas membrane-bound enzymes are encoded by single genes. Soluble GSTs are homo- or hetero-dimeric enzymes (approximately 25KDa subunits) which can act on a wide range of endogenous and exogenous electrophiles. GSTs mediate conjugation using glutathione (GSH), a tripeptide synthesized from its precursor amino acids gamma-glutamate, cysteine and glycine. A generalized reaction isRX + GSH -> HX + GSRGlutathione conjugates are excreted in bile and converted to cysteine and mercapturic acid conjugates in the intestine and kidneys. GSH is the major, low molecular weight, non-protein thiol synthesized de novo in mammalian cells. As well as taking part in conjugation reactions, GSH also has antioxidant ability and can metabolize endogenous and exogenous compounds. The nucleophilic GSH attacks the electrophilic substrate forming a thioether bond between the cysteine residue of GSH and the electrophile. The result is generally a less reactive and more water-soluble conjugate that can be easily excreted. In some cases, GSTs can activate compounds to reactive species such as certain haloalkanes and haloalkenes. Substrates for GSTs include epoxides, alkenes and compounds with electrophilic carbon, sulfur or nitrogen centres. There are two types of conjugation reaction with glutathione: displacement reactions where glutathione displaces an electron-withdrawing group and addition reactions where glutathione is added to activated double bond structures or strained ring systems. PMID:6339228 https://reactome.org/content/detail/R-HSA-156590 glutathione conjugation HOIP_0003991 Glutathione conjugation is a detoxication reaction. Four types of activation reaction have been recognized: direct-acting compounds, conjugates that are activated through cysteine conjugate beta-lyase, conjugates that are activated through redox cycling and lastly conjugates that release the original reactive parent compound. The glutathione S-transferases have three connections with the formation of biactivated conjugatesto make them more soluble for excretion. PMID:11154735 Glutathione S-Transferases (GSTs; EC 2.5.1.18) are another major set of phase II conjugation enzymes. They can be found in the cytosol as well as being microsomal membrane-bound. Cytosolic GSTs are encoded by at least 5 gene families (alpha, mu, pi, theta and zeta GST) whereas membrane-bound enzymes are encoded by single genes. Soluble GSTs are homo- or hetero-dimeric enzymes (approximately 25KDa subunits) which can act on a wide range of endogenous and exogenous electrophiles. GSTs mediate conjugation using glutathione (GSH), a tripeptide synthesized from its precursor amino acids gamma-glutamate, cysteine and glycine. A generalized reaction isRX + GSH -> HX + GSRGlutathione conjugates are excreted in bile and converted to cysteine and mercapturic acid conjugates in the intestine and kidneys. GSH is the major, low molecular weight, non-protein thiol synthesized de novo in mammalian cells. As well as taking part in conjugation reactions, GSH also has antioxidant ability and can metabolize endogenous and exogenous compounds. The nucleophilic GSH attacks the electrophilic substrate forming a thioether bond between the cysteine residue of GSH and the electrophile. The result is generally a less reactive and more water-soluble conjugate that can be easily excreted. In some cases, GSTs can activate compounds to reactive species such as certain haloalkanes and haloalkenes. Substrates for GSTs include epoxides, alkenes and compounds with electrophilic carbon, sulfur or nitrogen centres. There are two types of conjugation reaction with glutathione: displacement reactions where glutathione displaces an electron-withdrawing group and addition reactions where glutathione is added to activated double bond structures or strained ring systems. Reactome: R-HSA-156590 HOIP:HOIP_0003992 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that inculdes step 1 to 4. composite state of imbalance HOIP_0003992 HOIP:HOIP_0003995 A role played by the oncogene that is altered forms of normal cellular genes. Many proto-oncogenes are homologous to viral oncogenes and involved in the control of cell proliferation or differentiation. Mutations, amplifications or rearrangements of proto-oncogenes lead to upregulated or deregulated cell growth and allow them to function as oncogenes. http://purl.bioontology.org/ontology/MESH/D011519 http://purl.bioontology.org/ontology/SNOMEDCT/1496005 Normal cellular genes at a stage prior to carcinogenesis. The products of proto-oncogenes are important regulators of biological processes and appear to be involved in the events that serve to maintain the ordered procession through the cell cycle. Proto-oncogenes have names of the form c-onc. protooncogene role HOIP_0003995 Normal cellular genes at a stage prior to carcinogenesis. The products of proto-oncogenes are important regulators of biological processes and appear to be involved in the events that serve to maintain the ordered procession through the cell cycle. Proto-oncogenes have names of the form c-onc. MeSH: D011519 HOIP:HOIP_0003997 A role of the cytoplasmic proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. Chaperone proteins do not covalently bind to their targets and do not form part of the finished product. Heat-shock proteins are an important sub set of chaperones. Three major families are recognised, the chaperonins (groEL and hsp60), the hsp70 family and the hsp90 family. Outside these major families are other proteins with similar functions including nucleoplasmin, secB and T-cell receptor associated protein. chaperone role HOIP_0003997 HOIP:HOIP_00040000 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a cysteine nucleophile. cysteine protease HOIP_00040000 HOIP:HOIP_0004001 Recycling endosome dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete recycling endosomal function. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID:18216768 PMID:23625997 PMID:26574506 recycling endososomal dysfunction [phospholipidosis (severe)] HOIP_0004001 HOIP:HOIP_0004002 Recycling endosome dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete recycling endosomal function. And the degree is severe. recycling endosome dysfunction HOIP_0004002 HOIP:HOIP_0004003 This gene encodes the mitochondrial enzyme which is catalyzes the rate-limiting step in heme (iron-protoporphyrin) biosynthesis. NCBI-Mouse-GeneID:11655 PMID:20018698 PMID:22070747 Alas1 (mouse) [Lipidosis] HOIP_0004003 PMID:20018698 NCBI-Mouse-GeneID:11655 http://www.ncbi.nlm.nih.gov/gene/11655 PMID:22070747 It has been shown that insulin blunts hepatocyte ALAS1 induction, by disrupting the interaction of FOXO1 (forkhead box O1) and PGC-1α (peroxisome-proliferator-activated receptor γ co-activator 1α). HOIP:HOIP_0004004 Hyperfunction of phospholipid biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive heme biosynthesis. hyperfunction of heme biosynthesis HOIP_0004004 HOIP:HOIP_0004008 Tumor tissue is a subtype of abnormal cellular tissue that consists of tumor cells . tumor tissue HOIP_0004008 HOIP:HOIP_0004009 Hypofunction of eidocytic recycling from ER to mitochondrial membrane is a subtype of hypofunction of transport: A process that performs a decreased or insufficient endocytic recycling. hypofunction of endocytic recycling HOIP_0004009 HOIP:HOIP_0004010 Hypofunction of eidocytic recycling from ER to mitochondrial membrane is a subtype of hypofunction of transport: A process that performs a decreased or insufficient endocytic recycling. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). hypofunction of endocytic recycling [phospholipidosis (severe)] HOIP_0004010 HOIP:HOIP_0004011 NCBI-Mouse-GeneID:11522 ADH1 (mol) HOIP_0004011 NCBI-Mouse-GeneID:11522 https://www.ncbi.nlm.nih.gov/gene/11522 HOIP:HOIP_0004012 NCBI-Mouse-GeneID:11522 Adh1 (mouse)[lipidosis] HOIP_0004012 NCBI-Mouse-GeneID:11522 https://www.ncbi.nlm.nih.gov/gene/11522 HOIP:HOIP_0004014 Negative regulation of release of arachidonic acid from cell membrane is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the release of arachidonic acid from cell membrane. negative regulation of release of arachidonic acid from cell membrane HOIP_0004014 HOIP:HOIP_0004015 Dissociation of FLCN:FNIP complex is a subtype of detaching: A process that disaggregates the FLCN:FNIP complex. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID:25775561 Dissociation of FLCN:FNIP complex [phospholipidosis (severe)] HOIP_0004015 HOIP:HOIP_0004016 Dissociation of FLCN:FNIP complex is a subtype of detaching: A process that disaggregates the FLCN:FNIP complex. Dissociation of FLCN:FNIP complex HOIP_0004016 HOIP:HOIP_0004023 A role played by the entity which regulates the metabolism. metabolic regulator role HOIP_0004023 HOIP:HOIP_0004028 TOR signaling is a process that a signal is transmitted by the TOR (Target of rapamycin) . TOR signaling HOIP_0004028 HOIP:HOIP_0004032 Negative regulation of release of arachidonic acid from cell membrane is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the release of arachidonic acid from cell membrane. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). negative regulation of release of arachidonic acid from cell membrane [phospholipidosis (severe)] HOIP_0004032 HOIP:HOIP_0004034 TOR signaling is a process that a signal is transmitted by the TOR (Target of rapamycin) . This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). TOR signaling　[phospholipidosis (severe)] HOIP_0004034 HOIP:HOIP_0004035 The directed movement of tumor inhibitor from the lysosome. release of tumor inhibitor from lysosome HOIP_0004035 HOIP:HOIP_0004040 The directed movement of tumor inhibitor from the lysosome. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). release of tumor inhibitor from lysosome [phospholipidosis (severe)] HOIP_0004040 HOIP:HOIP_0004043 A role played by the entity which negatively regulates the process of tumor cell proliferation. negative regulator of tumor cell proliferation HOIP_0004043 HOIP:HOIP_0004045 A role played by the entity which negatively regulates the process of cell proliferation. negative regulator of cell proliferation HOIP_0004045 HOIP:HOIP_0004046 Forming adduct is a subtype of having extra parts: A process that changes to have connection or association with another entity. forming adduct HOIP_0004046 HOIP:HOIP_0004047 Abnormal cell tissue is a subtype of cellular tissue that consists of abnormal cells and tissues. abnormal cell tissue HOIP_0004047 HOIP:HOIP_0004048 The chemical reaction resulting in the breakdown of FNIP2, which is mediated by the proteasome. proteasome-mediated ubiquitin-dependent FNIP2 catabolic process HOIP_0004048 HOIP:HOIP_0004049 The chemical reaction resulting in the breakdown of FNIP2, which is mediated by the proteasome. This entity is a specific course-dependent process. This process can constitute the course of [phospholipidosis (severe). proteasome-mediated FNIP2 degradation [[phospholipidosis (severe)] HOIP_0004049 HOIP:HOIP_0004053 PPARalpha activation is a subtype of activating nuclear receptor: A process that changes the activity of the activating PPAR alpha ( (Peroxisome Proliferator Activated Receptor Alpha)) with a nuclear receptor role to be higher. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). PMID:27816970 PPARalpha activation [phospholipidosis (severe)] HOIP_0004053 PMID:27816970 HOIP:HOIP_0004065 The chemical reactions and pathways resulting in the formation of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). PMID:21502324 PMID:24140022 PMID:31442404 ketone anabolism ketone biosynthesis ketone formation ketone synthesis ketone biosynthetic process [phospholipidosis (severe (excessive defense))] HOIP_0004065 PMID:24140022 The key irreversible step in ketogenesis is synthesis of 3-hydroxy-3-methylglutaryl-CoA by HMGCS2. Conversely, the rate limiting step in ketolysis is conversion of acetoacetate to acetoacetyl-CoA by OXCT1. HMGCS2 transcription is heavily regulated by FOXA2, mTOR, PPARα, and FGF21. ketogenic diets suppress fatty acid synthesis enzymes including SCD1. Instead, PPARα, a regulator of ketogenic genes, is strongly induced, as is one of its crucial downstream targets, FGF21, resulting in increased transcription of ketogenic enzymes, such as HMGCS2. HOIP:HOIP_0004066 Hypofunction of anti-oxidative stress is a subtype of hypofunctioning: A process that performs a decreased or insufficient anti-oxidative stress function. hypofunction of anti-oxidative stress HOIP_0004066 HOIP:HOIP_0004069 Hypofunction of anti-oxidative stress is a subtype of hypofunctioning: A process that performs a decreased or insufficient anti-oxidative stress function. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). hypofunction of anti-oxidative stress [phospholipidosis (severe)] HOIP_0004069 HOIP:HOIP_0004077 Energy supply is a subtype of providing process to perform a meta-function “to provide energy. energy supply HOIP_0004077 HOIP:HOIP_0004079 Any process that increases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death. positive regulation of cell death HOIP_0004079 HOIP:HOIP_0004081 Any process that stops, prevents or reduces the frequency, rate or extent of tmitochondrial electron transport, ubiquinol to cytochrome c negative regulation of mitochondrial electron transport, ubiquinol to cytochrome c HOIP_0004081 HOIP:HOIP_0004082 Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death. negative regulation of cell death HOIP_0004082 HOIP:HOIP_0004084 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). negative regulation of potassium ion transport [phospholipidosis (severe)] HOIP_0004084 HOIP:HOIP_0004088 Malfunctioning of insulin signaling is a subtype of malfunctioning process: A process that cannot perform insulin signaling appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis via obese. 白色脂肪組織では発現減少． PMID:27800604 malfunctioning of insulin signaling [phospholipidosis via obese] HOIP_0004088 PMID:27800604 kcnma1 expression is downregulated in white adipose tissue of mice fed a high-fat diet and in hypertrophied adipocytes. Furthermore, inhibition of kcnma1 expression or treatment with a BK channel blocker attenuated insulin-induced Akt phosphorylation in mature adipocytes. These results strongly indicate that KCNMA1 contributes to the regulation of insulin signalling in mature adipocytes. HOIP:HOIP_0004096 The process in which one or more ubiquitin groups are added to a protein. protein ubiquitinylation protein ubiquitylation protein ubiquitination HOIP_0004096 HOIP:HOIP_0004097 genetic information carrier role is a subtype of role dependent on transmitting genetic information process genetic information carrier role HOIP_0004097 HOIP:HOIP_0004098 Any process that activates or increases the frequency, rate or extent of glutathione biosynthetic process. This entity is a specific course-dependent process. This process can constitute the course of Glutathione depletion. positive regulation of glutathione biosynthetic process [glutathione depletion (course)] HOIP_0004098 HOIP:HOIP_0004099 Any process that stops, prevents or reduces the frequency, rate or extent of the transfer of electrons from succinate to ubiquinone. negative regulation of mitochondrial electron transport, succinate to ubiquinone HOIP_0004099 HOIP:HOIP_0004100 Malfunctioning of cobalamin biosynthetic process is a subtype of malfunctioning process: A process that cannot perform cobalamin biosynthetic process appropriately or cannot realize it at all. malfunctioning of cobalamin biosynthetic process HOIP_0004100 HOIP:HOIP_0004101 Malfunctioning of cobalamin biosynthetic process is a subtype of malfunctioning process: A process that cannot perform cobalamin biosynthetic process appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of Phosphoipidosis (severe). malfunctioning of cobalamin biosynthetic process [phospholipidosis (severe)] HOIP_0004101 HOIP:HOIP_0004104 A protein that is a translation product of the human IL32 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:9235 IL32 (human)[Phospholipidosis] HOIP_0004104 NCBI-Human-GeneID:9235 http://www.ncbi.nlm.nih.gov/gene/9235 HOIP:HOIP_0004107 A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to a target protein. protein modification by small protein conjugation HOIP_0004107 HOIP:HOIP_0004109 Any process that stops, prevents or reduces the frequency, rate or extent of mitochondrial electron transport, NADH to ubiquinone. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. negative regulation of mitochondrial electron transport, NADH to ubiquinone [mitochondrial disorder (course)] HOIP_0004109 HOIP:HOIP_0004110 A process that results in the assembly, arrangement of constituent parts of a lipid droplet. adiposome formation lipid droplet formation HOIP_0004110 HOIP:HOIP_0004111 A process that results in the assembly, arrangement of constituent parts of a lipid droplet. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis via obese. adiposome formation lipid droplet formation [phospholipidosis via obese] HOIP_0004111 HOIP:HOIP_0004113 The orderly movement of a macrophage from one site to another. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). macrophage migration [phospholipidosis (severe (excessive defense))] HOIP_0004113 HOIP:HOIP_0004115 A role played by the entity which negatively regulates the tumor metastasis. tumor metastasis inhibitor HOIP_0004115 HOIP:HOIP_0004117 Hyperfunction of drug metabolism phase II is a subtype of hyperfunction of drug metabolism: A process that performs an excessive drug metabolism phase II. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). hyperfunction of drug metabolism phase II [phospholipidosis (imbalance course)] HOIP_0004117 HOIP:HOIP_0004119 Any process that stops, prevents or reduces the frequency, rate or extent of the transfer of electrons from succinate to ubiquinone. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. negative regulation of mitochondrial electron transport, succinate to ubiquinone [mitochondrial disorder (course)] HOIP_0004119 HOIP:HOIP_0004120 Any process that stops, prevents or reduces the frequency, rate or extent of tmitochondrial electron transport, ubiquinol to cytochrome c. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. negative regulation of mitochondrial electron transport, ubiquinol to cytochrome c [mitochondrial disorder (course)] HOIP_0004120 HOIP:HOIP_0004121 Drug-, radiation-induced, or spontaneous injuries to DNA that introduce deviations from its normal double-helical conformation. These changes include structural distortions that interfere with replication and transcription, as well as point mutations that disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. If the damage is minor, it can often be repaired (DNA repair); extensive damage can induce apoptosis. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:21145849 PMID:23299992 PMID:29222479 PMID:31623280 DNA damage [mitochondrial disorder (course)] HOIP_0004121 PMID:21145849 For instance APAP and troglitazone can induce mtDNA strand breaks which eventually lead to a reduction of mtDNA levels. Indeed, damaged mtDNA molecules harboring numerous strand breaks can be rapidly degraded by mitochondrial endonucleases. Table 1. PMID:23299992 NAFLD has been associated with higher hepatic expression of the inducible nitric oxide (NO) synthase (iNOS), mainly as a consequence of tumor necrosis factor‐α (TNF‐α) overproduction by the Kupffer cells. NO can readily react with the superoxide anion, thus generating the RNS peroxynitrite, which has deleterious effects on mitochondrial function and genome. It is likely that this event triggers a vicious cycle since mitochondrial ROS are able to oxidatively damage nearby MRC enzymes and mtDNA TNF‐α is able to impair MRC activity, possibly by inducing hypoxia inducible factor‐1α (HIF‐1α) and mtDNA damage. In addition to ROS, reactive nitrogen species (RNS) and lipid peroxidation products are able to damage mtDNA. PMID:29222479 Alcohol-mediated damage of mitochondrial DNA (mtDNA) also impairs cellular energy metabolism via enhanced formation of reactive oxygen species (ROS). PMID:31623280 Just like in NASH, oxidative stress, mitochondrial dysfunction, and oxidized mtDNA also contribute to the progression of HCC through influences on inflammation, cell death, and ER stress. Moreover, a diet rich in fructose is associated with increased oxidative mtDNA lesions in rat liver coupled with reduced mitochondrial repair capacity and rats consuming a diet high in fat and rich in fructose have increased hepatocyte damage, inflammation, and lipid peroxidation coupled with impaired mitochondrial respiration and activity. HOIP:HOIP_0004122 Any process that increases the rate or frequency of tumor cell death. positive regulation of tumor cell death HOIP_0004122 HOIP:HOIP_0004123 Any process that increases the rate or frequency of tumor cell death. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). positive regulation of tumor cell death [phospholipidosis (severe)] HOIP_0004123 HOIP:HOIP_0004124 Negative regulation of heat generation is a subtype of negative regulation process: Any process that stops, prevents, or reduces the rate or extent of heat generation. This process can constitute the course of Mitochondrial disorder. down regulation of heat generation [mitochondrial disorder (course)] down-regulation of heat generation [mitochondrial disorder (course)] downregulation of heat generation [mitochondrial disorder (course)] inhibition of heat generation [mitochondrial disorder (course)] negative regulation of heat generation [mitochondrial disorder (course)] HOIP_0004124 HOIP:HOIP_0004125 Negative regulation of oxidative phosphorylation is a subtype of negative regulation process: Any process that stops, prevents or reduces the frequency, rate or extent of the oxidative phosphorylation. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:24746669 PMID:29222479 PMID:30250064 PMID:31649547 negative regulation of oxidative phosphorylation [mitochondrial disorder (course)] HOIP_0004125 PMID:29222479 PMID:23299992 Some lipid derivatives such as FAs can directly inhibit several enzymes involved in MRC and OXPHOS. PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). PMID:29222479 Chronic alcohol consumption alters mitochondrial oxidative phosphorylation in the liver by suppressing the synthesis of respiratory complex proteins. PMID:30250064 not reported in the liver. Strikingly, NEAT1-depleted single cell clones showed a consistent reduction in mitochondrial DNA (mtDNA) (Fig. 7a), reduced mitochondrial respiration (by detection of the oxygen consumption rate (OCR); Fig. 7b) and adenosine triphosphate (ATP) production (Fig. 7c), reduced OCR and extracellular acidification rate (ECAR) rate (Fig. 7d), suggesting that the aberrant NEAT1 expression could cause mitochondrial dysfunction. PMID:31649547 In general, damaged mitochondria accumulation can cause excessive ROS production, which will destroy mitochondrial oxidative phosphorylation and substrate oxidation, thereby inhibiting fatty acid oxidative degradation and accelerating fatty acid accumulation. HOIP:HOIP_0004126 Malfunctioning of TCA cycle is a subtype of malfunctioning of metabolism: A process that cannot perform a tricarboxylic acid cycle appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:26571396 PMID:29335519 malfunctioning of TCA cycle [mitochondrial disorder (course)] HOIP_0004126 PMID:26571396 Mitochondrial metabolism mediates oxidative stress and inflammation in fatty liver. Here, we provide several lines of evidence indicating that induction of biosynthesis through hepatic anaplerotic/cataplerotic pathways is energetically backed by elevated oxidative metabolism and hence contributes to oxidative stress and inflammation during NAFLD. First, in murine livers, elevation of fatty acid delivery not only induced oxidative metabolism, but also amplified anaplerosis/cataplerosis and caused a proportional rise in oxidative stress and inflammation. Second, loss of anaplerosis/cataplerosis via genetic knockdown of phosphoenolpyruvate carboxykinase 1 (Pck1) prevented fatty acid-induced rise in oxidative flux, oxidative stress, and inflammation. Though all tissues support minor activities of anaplerosis and cataplerosis, these pathways are a major function of liver TCA cycle, where anaplerosis and cataplerosis are required for shuttling reducing equivalents (RE) and biosynthetic substrates related to ureagenesis, amino acid synthesis, lipogenesis, and most prominently, gluconeogenesis (GNG) (1) On the whole, the data indicate that increased flux through anaplerotic/cataplerotic pathways not only contributes to dysregulation of downstream nutrients (e.g., glycemia and lipidemia), but also triggers oxidative metabolism and altered antioxidant capacity that contribute to the development of oxidative stress, inflammation, and insulin resistance (Figure 8B and Supplemental Table 2). PMID:29335519 Metabolic reprogramming by PCK1 promotes TCA cataplerosis, oxidative stress and apoptosis in liver cancer cells and suppresses hepatocellular carcinoma. Supporting this notion, PCK1 expression in SK-Hep-1 dramatically reduced cellular ATP level by 4 folds in cells cultured in low glucose medium, but not in normal medium (Fig. 4c). In addition, supplement of dimethyl-α-KG may also increase cellular ATP level and alleviate energy stress, as indicated by the decreased phosphorylation of AMPKα1 and ACC (Fig. 5f). HOIP:HOIP_0004127 Increasing acetyl CoA is a subtype of increasing quantity: A process that changes the amount of acetyl CoA to be larger. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder]. PMID:23299992 increasing acetyl CoA [mitochondrial disorder (course)] HOIP_0004127 PMID:23299992 Hepatic ketogenesis was also augmented in mice fed a high‐fat diet (HFD), thus suggesting that higher acetyl‐CoA generation by way of mtFAO is followed by efficient KB production. HOIP:HOIP_0004128 Increasing volume of mitochondria is a changing process to change the volume of the mitochondria to increase. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). increasing volume of mitochondria [non-alcoholic steatohepatitis (course)] HOIP_0004128 HOIP:HOIP_0004129 Any biological process that results in permanent cessation of tumor cells. tumor cell death HOIP_0004129 HOIP:HOIP_0004130 Increasing uptake amount of mitochondrial proton is a subtype of increasing quantity: A process that changes the uptake amount of mitochondrial proton to be higher. increasing uptake amount of mitochondrial proton ion HOIP_0004130 HOIP:HOIP_0004131 Increasing uptake amount of mitochondrial proton is a subtype of increasing quantity: A process that changes the uptake amount of mitochondrial proton to be higher. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. increasing uptake amount of mitochondrial proton ion [mitochondrial disorder (course)] HOIP_0004131 HOIP:HOIP_0004132 Negative regulation of tumor cell proliferation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of tumor cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). negative regulation of tumor cell proliferation [[phospholipidosis (severe)] HOIP_0004132 HOIP:HOIP_0004133 Any process that enables the transfer of protons from mitochondrial intermembrane space into mitochondrial matrix, dissipating the proton gradient across the mitochondrial inner membrane established by the electron transport chain during the oxidative phosphorylation (proton leak). Proton leak uncouples the processes of electron transport/proton generation and ATP synthesis. oxidative phosphorylation uncoupling HOIP_0004133 HOIP:HOIP_0004134 Any process that activates or increases the frequency, rate or extent of oxidative phosphorylation uncoupling. Oxidative phosphorylation uncoupling is a process that enables the transfer of protons from mitochondrial intermembrane space into mitochondrial matrix, dissipating the proton gradient across the mitochondrial inner membrane established by the electron transport chain during the oxidative phosphorylation (proton leak). Proton leak uncouples the processes of electron transport/proton generation and ATP synthesis. positive regulation of oxidative phosphorylation uncoupling HOIP_0004134 HOIP:HOIP_0004135 Any process that activates or increases the frequency, rate or extent of oxidative phosphorylation uncoupling. Oxidative phosphorylation uncoupling is a process that enables the transfer of protons from mitochondrial intermembrane space into mitochondrial matrix, dissipating the proton gradient across the mitochondrial inner membrane established by the electron transport chain during the oxidative phosphorylation (proton leak). Proton leak uncouples the processes of electron transport/proton generation and ATP synthesis. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. positive regulation of oxidative phosphorylation uncoupling [mitochondrial disorder (course)] HOIP_0004135 HOIP:HOIP_0004136 Energy supply is a subtype of providing process to perform a meta-function “to provide energy. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). energy supply [phospholipidosis (normal course)] HOIP_0004136 HOIP:HOIP_0004137 Increasing energy is a subtype of increasing quantity: A process that changes the amount of energy to be larger. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (normal course). increasing energy [phospholipidosis (normal course)] HOIP_0004137 HOIP:HOIP_0004138 Decreasing energy is a subtype of decreasing quantity: A process that changes the amount of energy to be smaller. decreasing energy HOIP_0004138 HOIP:HOIP_0004139 Decreasing energy is a subtype of decreasing quantity: A process that changes the amount of energy to be smaller. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. decreasing energy [phospholipidosis (imbalance course)] HOIP_0004139 HOIP:HOIP_0004141 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B. PMID:22102288 hepatic fibrosis [course of Niemann–Pick disease type A and type B] HOIP_0004141 PMID:22102288 Cathepsin B Overexpression Due to Acid Sphingomyelinase Ablation Promotes Liver Fibrosis in Niemann-Pick Disease HOIP:HOIP_0004143 ceramide accumulation is a subtype of accumulation of substances in a biological object: A process that keeps ceramide in an organism, tissue, organelle, or cell. ceramide acumulation HOIP_0004143 HOIP:HOIP_0004144 A process that results in the breakdown of the extracellular matrix. This entity is a specific course-dependent process. This process can constitute the course of [phospholipidosis (severe (excessive defense)). PMID:1540143 PMID:3458210 extracellular matrix disassembly [phospholipidosis (severe (excessive defense))] HOIP_0004144 PMID:3458210 Cathepsin B: association with plasma membrane in metastatic tumors. Localization of hydrolytic enzymes in the plasma membrane of metastatic tumor cells could result in focal dissolution of the extracellular matrix and thereby invasion and metastasis. HOIP:HOIP_0004145 A process that performs a decreased or insufficient cholesterol efflux hypofunction of cholesterol efflux from hepatoyte HOIP_0004145 HOIP:HOIP_0004146 A process that performs a decreased or insufficient cholesterol export. This entity is a specific course-dependent process. This process can constitute the course of Niemann–Pick disease type A and type B. PMID:29249985 hypofunction of cholesterol efflux [course of Niemann–Pick disease type A and type B] HOIP_0004146 PMID:29249985 Although tissues from mice or patients with NPA and NPB disease accumulate SM primarily in endolysosomes, cholesterol also increases as a secondary consequence (Huang and Feigenson, 1999; Radhakrishnan et al., 2000; Ridgway, 2000). While the underlying mechanism of cholesterol loading is not well understood, it is known that SM and cholesterol exhibit a high affinity for each other. Indeed, SM binds cholesterol with high affinity (Slotte, 1999; Ridgway, 2000), resulting in the sequestration and subsequent decrease in the efflux of cholesterol out of lysosomes, impairing the esterification of cholesterol by acyl-CoA:cholesterol acyl transferase in the ER. These events are in line with findings in macrophages from ASMase−/− mice or in macrophages from wild type mice enriched with exogenous SM, which results in increased lysosomal cholesterol content because of decreased cholesterol efflux (Leventhal et al., 2001). Interestingly, it has been described that ASMase is not only active in lysosomes, but it exhibits a secretory form that acts on the plasma membrane to generate ceramide from SM hydrolysis in response to stress (Falcone et al., 2004; Charruyer et al., 2005). This event, in turn, reorganizes membrane lipid domains, called “rafts,” which trigger downstream signaling events. These observations have led to the suggestion that in addition to lysosomal dysfunction produced by SM accumulation, part of the pathogenesis of NPA and NPB is related to alterations in signaling pathways at the plasma membrane. HOIP:HOIP_0004148 A process that forms myelin-like layered structures. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe). The presence of phospholipid inclusions are characterized by the presence of cytoplasmic vacuoles seen under the electron microscope as dense cytoplasmic myelin-like bodies showing a concentric lamellar structure with a periodicity of 4-4.5 nm along with an amorphorous matrix within a single membrane-bound lysosomal space. Histopathology of preclinical toxicity studies : interpretation and relevance in drug safety studies, Peter Greaves. 4th ed. Amsterdam ; Boston : Elsevier/AP, 2012. The presence of phospholipid inclusions are characterized by the presence of cytoplasmic vacuoles seen under the electron microscope as dense cytoplasmic myelin-like bodies showing a concentric lamellar structure with a periodicity of 4-4.5 nm along with an amorphorous matrix within a single membrane-bound lysosomal space. Histopathology of preclinical toxicity studies : interpretation and relevance in drug safety studies, Peter Greaves. 4th ed. Amsterdam ; Boston : Elsevier/AP, 2012. lamellar body formation in lysosome [phospholipidosis (severe)] myelin figureformation in lysosome [phospholipidosis (severe)] HOIP_0004148 The presence of phospholipid inclusions are characterized by the presence of cytoplasmic vacuoles seen under the electron microscope as dense cytoplasmic myelin-like bodies showing a concentric lamellar structure with a periodicity of 4-4.5 nm along with an amorphorous matrix within a single membrane-bound lysosomal space. Histopathology of preclinical toxicity studies : interpretation and relevance in drug safety studies, Peter Greaves. 4th ed. Amsterdam ; Boston : Elsevier/AP, 2012. https://www.worldcat.org/title/histopathology-of-preclinical-toxicity-studies-interpretation-and-relevance-in-drug-safety-evaluation/oclc/778774101 HOIP:HOIP_0004150 Removing ceramide by Kupffer cell or macrophage is a subtype of removing: A process that takes ceramide from a cell by Kupffer cells or macrophages . Removing ceramide by Kupffer cell or macrophage HOIP_0004150 HOIP:HOIP_0004151 Hyperfunction of ceramide phagocytosis by Kupffer cell or macrophage is a subtype of hyperfunctioning: A process that performs an excessive ceramide phagocytosis by Kupffer cells or macrophages. hyperfunction of ceramide phagocytosis by Kupffer cell or macrophage HOIP_0004151 HOIP:HOIP_0004152 Acid ceramidase inactivation is a subtype of molecular inactivation: A process that changes the activity of the acid ceramidase to be lower. acid ceramidase inactivation HOIP_0004152 HOIP:HOIP_0004154 Increasing number of macrophage derived foam cell is a subtype of increasing number of objects: A process that becomes larger in the number of foam cell, a type of macrophage containing lipids in small vacuoles, in the liver. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (severe (excessive defense)). increasing number of macrophage derived foam cell [phospholipidosis (severe (excessive defense))] HOIP_0004154 HOIP:HOIP_0004155 Phospholipid homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. And the degree is mild. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (mild). phospholipid homeostasis imbalance [phospholipidosis (mild) ] HOIP_0004155 HOIP:HOIP_0004157 The totality of all processes through which the sphingomyelin disorder is realized. sphingomyelin disorder (course) HOIP_0004157 HOIP:HOIP_0004158 Lysosomal cholesterol storage is a subtype of cholesterol storage: A process that keeps cholesterol in the lysosome moderately. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis(moderate). lysosomal cholesterol storage (moderate) [phospholipidosis (moderate)] HOIP_0004158 HOIP:HOIP_0004159 Sphingomyelin homeostasis imbalance is a subtype of phospholipid homeostasis imbalance: A process that becomes lacking asphingomyelin homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. sphingomyelin homeostasis imbalance [sphingomyelin disorder (course)] HOIP_0004159 HOIP:HOIP_0004160 Any process that increases the rate, frequency or extent of macrophage derived foam cell differentiation. Macrophage derived foam cell differentiation is the process in which a macrophage acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. positive regulation of macrophage derived foam cell differentiation [sphingomyelin disorder (course)] HOIP_0004160 HOIP:HOIP_0004161 Increasing number of macrophage derived foam cell is a subtype of increasing number of objects: A process that becomes larger in the number of foam cell, a type of macrophage containing lipids in small vacuoles, in the liver. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. increasing number of macrophage derived foam cell [sphingomyelin disorder (course)] HOIP_0004161 HOIP:HOIP_0004162 Dysfunction of sphingomyelin degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient sphingomyelin degradation. This entity is a specific course-dependent process. This process can constitute the course of sphingomyelin disorder. hypofunction of sphingomyelin degradation [sphingomyelin disorder (course)] HOIP_0004162 HOIP:HOIP_0004171 NCBI-Human-GeneID:203228 C9orf72(human) [mitochondrial damage] HOIP_0004171 NCBI-Human-GeneID:203228 http://www.ncbi.nlm.nih.gov/gene/203228 HOIP:HOIP_0004177 NCBI-Human-GeneID:283131 NEAT1 (human) [mitochondrial damage] HOIP_0004177 NCBI-Human-GeneID:283131 http://www.ncbi.nlm.nih.gov/gene/283131 HOIP:HOIP_0004207 Lipid metabolism imbalance is a subtype of imbalance: A process that becomes lacking a homeostastasis balance of lipid metabolism. The degree is severe. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. lipid metabolism imbalance (severe) [alcoholic fatty liver] HOIP_0004207 HOIP:HOIP_0004208 The deree level is a subtype of qualitative value. The extent or measure of the condition/action. degree level HOIP_0004208 HOIP:HOIP_0004209 Lipid homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a lipid homeostastasis balance. The degree is severe. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. lipid homeostasis imbalance (severe) [alcoholic fatty liver] HOIP_0004209 HOIP:HOIP_0004210 Lipid accumulation in hepatocyte (severe) is a subtype of lipid strorage in hepatocyte: A process that keeps lipids in hepatocytes. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. lipid storage in hepatocyte (severe) [Lipidosis] lipid accumulation in hepatocyte (severe) [alcoholic fatty liver] HOIP_0004210 HOIP:HOIP_0004211 An attribute of the finding of bodily harm due to the poisonous effects of something. toxicity (attribute) HOIP_0004211 HOIP:HOIP_0004212 Any process that stops, prevents, or reduces the frequency, rate or extent of protein-containing complex assembly. down regulation of protein-containing complex assembly down-regulation of protein-containing complex assembly downregulation of protein-containing complex assembly inhibition of protein-containing complex assembly negative regulation of protein-containing complex assembly HOIP_0004212 HOIP:HOIP_0004213 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex assembly. negative regulation of mitochondrial respiratory chain complex assembly HOIP_0004213 HOIP:HOIP_0004214 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex I assembly. negative regulation of mitochondrial respiratory chain complex I assembly HOIP_0004214 HOIP:HOIP_0004215 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex II assembly. negative regulation of mitochondrial respiratory chain complex II assembly HOIP_0004215 HOIP:HOIP_0004216 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex III assembly. negative regulation of mitochondrial respiratory chain complex III assembly HOIP_0004216 HOIP:HOIP_0004217 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex IV assembly. negative regulation of mitochondrial respiratory chain complex IV assembly HOIP_0004217 HOIP:HOIP_0004218 A pathologic process that involves the transformation of normal cells to a neoplastic state and resulting in polyclonal or monoclonal neoplastic cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:25181692 PMID:30894684 PMID:31623280 tumorigenesis [mitochondrial disorder (course)] HOIP_0004218 PMID:25181692 Tumor-Associated Macrophages Produce Interleukin 6 and Signal via STAT3 to Promote Expansion of Human Hepatocellular Carcinoma Stem Cells TAMs produce IL6, which promotes expansion of these CSCs and tumorigenesis. Levels of IL6 in human HCC samples correlate with tumor stage and markers of CSCs. We have identified that STAT3 signaling in HCC cells following TAM interaction is critical to increased CSC expansion and increased tumor growth. PMID:30894684 Our data demonstrated that increased mitochondrial fission induced release of mtDNA into the cytosol in HCC cells, which is commonly recognized as cytosolic mtDNA stress, suggesting a potentially critical role of mitochondrial fission-regulated mtDNA hemostasis in hepatocarcinogenesis. CCL2 is a multifunctional factor involved in various aspects of liver disease pathogenesis, including cirrhosis and hepatocarcinogenesis. Previous studies have shown that CCL2 promotes the accumulation and polarization of macrophages by CCR2 receptor signaling pathway. Our study demonstrated that CCL2 was a critical mediator to link the cytosolic mtDNA stress in HCC cells and TAM infiltration. HOIP:HOIP_0004220 NCBI-Human-GeneID:891 PMID:24746669 CCNB1 (human) [mitochondrial disorder (course)] HOIP_0004220 NCBI-Human-GeneID:891 http://www.ncbi.nlm.nih.gov/gene/891 PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. HOIP:HOIP_0004222 NCBI-Mouse-GeneID:23886 PMID:29222479 PMID:29956733 GDF15(mouse)[mitochondrial disorder (course)] HOIP_0004222 NCBI-Mouse-GeneID:23886 http://www.ncbi.nlm.nih.gov/gene/23886 PMID:29222479 Treatment with alcohol also increased the levels of secreted GDF15 in supernatants of cultured hepatocytes. We next investigated the effect of mitochondrial dysfunction on GDF15 expression in hepatocytes. Inhibition of the mitochondrial OXPHOS complex using oligomycin or rotenone significantly increased Gdf15 expression and GDF15 secretion by cultured hepatocytes. Hepatic Gdf15 expression and serum levels of GDF15 were remarkably increased in alcohol-fed mice. Liver-infiltrating monocytes and neutrophils were also increased in the GDF15 KO mice during liver fibrogenesis. These changes in hepatic immune cells were associated with increased tissue inflammation and fibrosis. As shown in Fig. 3c, H&E staining and Oil Red O staining showed that hepatic fat accumulation and immune cell infiltration were increased in alcohol-fed GDF15 KO mice compared to controls (Fig. 3c). In addition, collagen deposition was significantly increased in the livers of GDF15 KO mice treated with CCl4 (Fig. 4c). Furthermore, Tnf-α and fibrotic mediators such as type 1 collagen 1 alpha 1 (Col1a1) and alpha smooth muscle actin (Acta2) were upregulated in the livers of GDF15 KO mice treated with CCl4 (Fig. 4d). These data demonstrate that GDF15 deficiency induces hepatic inflammation and fibrosis in the CCl4-induced model of liver fibrosis. HOIP:HOIP_0004223 PMID:29222479 GDF15 - inactive form (mouse)[mitochondrial disorder (course)] HOIP_0004223 PMID:29222479 Treatment with alcohol also increased the levels of secreted GDF15 in supernatants of cultured hepatocytes. We next investigated the effect of mitochondrial dysfunction on GDF15 expression in hepatocytes. Inhibition of the mitochondrial OXPHOS complex using oligomycin or rotenone significantly increased Gdf15 expression and GDF15 secretion by cultured hepatocytes. Hepatic Gdf15 expression and serum levels of GDF15 were remarkably increased in alcohol-fed mice (Fig. 1j–l). Liver-infiltrating monocytes and neutrophils were also increased in the GDF15 KO mice during liver fibrogenesis. These changes in hepatic immune cells were associated with increased tissue inflammation and fibrosis. As shown in Fig. 3c, H&E staining and Oil Red O staining showed that hepatic fat accumulation and immune cell infiltration were increased in alcohol-fed GDF15 KO mice compared to controls (Fig. 3c). In addition, collagen deposition was significantly increased in the livers of GDF15 KO mice treated with CCl4 (Fig. 4c). Furthermore, Tnf-α and fibrotic mediators such as type 1 collagen 1 alpha 1 (Col1a1) and alpha smooth muscle actin (Acta2) were upregulated in the livers of GDF15 KO mice treated with CCl4 (Fig. 4d). These data demonstrate that GDF15 deficiency induces hepatic inflammation and fibrosis in the CCl4-induced model of liver fibrosis. HOIP:HOIP_0004224 NCBI-Mouse-GeneID:16193 IL-6 (mouse)[mitochondrial disorder (course)] HOIP_0004224 NCBI-Mouse-GeneID:16193 http://www.ncbi.nlm.nih.gov/gene/16193 HOIP:HOIP_0004225 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex assembly. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:23299992 PMID:29222479 PMID:31623280 Negative regulation of respiratory complex proteins synthesis HOIP_0004225 PMID:23299992 Finally, higher FOXO1 activity and oxidative stress could be involved, by way of impaired mitochondrial biogenesis. Indeed, FoxO1 activation is able to reduce the content of different MRC polypeptides, possibly by decreasing heme synthesis and impairing PGC1α activity. Reduced PGC1α activity could also be secondary to oxidative stress and inflammation, as previously mentioned (Fig. 4). PMID:29222479 Chronic alcohol consumption alters mitochondrial oxidative phosphorylation in the liver by suppressing the synthesis of respiratory complex proteins. PMID:31623280 Moreover, in vitro treatment of liver cells with saturated fatty acids (palmitic and stearic acids) reproduces mitochondrial dysfunction found in NASH, including decreasing cellular ATP content and mtDNA-encoded oxidative phosphorylation (OXPHOS) subunit expression, coupled with increased oxidative stress. HOIP:HOIP_0004226 Mitochondrial damage dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of Mitochondrial damage as a gene product. Gene profile:Mouse mitochondrial damage dependent molecule (mouse) HOIP_0004226 HOIP:HOIP_0004228 NCBI-Human-GeneID:1277 NCBI-Mouse-GeneID:12842 NCBI-Rat-GeneID:29393 COL1A1 (mol) HOIP_0004228 NCBI-Human-GeneID:1277 http://www.ncbi.nlm.nih.gov/gene/1277 NCBI-Mouse-GeneID:12842 http://www.ncbi.nlm.nih.gov/gene/12842 NCBI-Rat-GeneID:29393 http://www.ncbi.nlm.nih.gov/gene/29393 HOIP:HOIP_0004229 NCBI-Human-GeneID:1571 NCBI-Mouse-GeneID:13106 NCBI-Rat-GeneID:25086 PMID:23299992 PMID:29222479 CYP2E1 (canonical)[mitochondrial disorder (course)] HOIP_0004229 NCBI-Human-GeneID:1571 http://www.ncbi.nlm.nih.gov/gene/1571 NCBI-Mouse-GeneID:13106 http://www.ncbi.nlm.nih.gov/gene/13106 NCBI-Rat-GeneID:25086 http://www.ncbi.nlm.nih.gov/gene/25086 PMID:23299992 A second mechanism is ROS generation due to CYP2E1 overexpression and reduced levels of mtGSH. Whereas CYP2E1 induction could be secondary to higher levels of glucagon, FAs and KBs, reduced mtGSH could result from higher mitochondrial levels of cholesterol. PMID:29222479 Moreover, the radicals produced by cytochrome P450 2E1-mediated CCl4 metabolism bind to mtDNA directly and also promote lipid peroxidation, which results in degradation of mtDNA. HOIP:HOIP_0004230 NCBI-Human-GeneID:5599 NCBI-Mouse-GeneID:26419 NCBI-Rat-GeneID:116554 PMID:23299992 PMID:29222479 PMID:30898010 PMID:31623280 PMID:31649547 JNK (canonical)[mitochondrial disorder (course)] HOIP_0004230 NCBI-Human-GeneID:5599 http://www.ncbi.nlm.nih.gov/gene/5599 NCBI-Mouse-GeneID:26419 http://www.ncbi.nlm.nih.gov/gene/26419 NCBI-Rat-GeneID:116554 http://www.ncbi.nlm.nih.gov/gene/116554 PMID:23299992 Moreover, saturated FAs are able to activate c‐Jun N‐terminal kinase and trigger the mitochondrial membrane permeability transition, thus inducing mitochondrial release of cytochrome c and apoptosis. PMID:29222479 Furthermore, NF-kB, JNK, and p38 signaling pathways, which are closely associated with hepatic inflammation and fibrosis, were inhibited by treatment with rGDF15 in a mouse model of liver fibrosis (Fig. 6). PMID:30898010 In addition, there is more pronounced WAT remodeling with more adipose tissue-associated macrophages infiltration, more M1 macrophage polarization and thus an elevated inflammatory response. Mechanistically, hyperactivation of MAPK/JNK leads to insulin insensitivity, which can be inhibited by knocking out Mapk8/Jnk1 in fundc1 KO mice. PMID:31623280 Mitochondrial-derived ROS activate mitogen-activated protein kinases (MAPKs) including c-Jun N-terminal kinase (JNK). Phosphorylated JNK translocates to the mitochondria, where it binds to scaffold proteins inhibiting the mitochondrial respiratory chain and further increasing ROS production. Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. PMID:31649547 They have also demonstrated that impaired mitophagy can promote macrophage infiltration to activate MAPK signal pathway and inflammatory response to impair mitochondrial quality control, subsequently causing insulin resistance and hepatic steatosis. HOIP:HOIP_0004231 NCBI-Human-GeneID:10059 NCBI-Mouse-GeneID:74006 NCBI-Rat-GeneID:114114 DRP1 (mol) DNM1L (mol) HOIP_0004231 NCBI-Human-GeneID:10059 http://www.ncbi.nlm.nih.gov/gene/10059 NCBI-Mouse-GeneID:74006 http://www.ncbi.nlm.nih.gov/gene/74006 NCBI-Rat-GeneID:114114 http://www.ncbi.nlm.nih.gov/gene/114114 HOIP:HOIP_0004232 PMID:30894684, Hepatocarcinoma cell NCBI-Human-GeneID:10059 DRP1(human)[mitochondrial disorder (course)] DNM1L(human)[mitochondrial disorder (course)] HOIP_0004232 NCBI-Human-GeneID:10059 http://www.ncbi.nlm.nih.gov/gene/10059 HOIP:HOIP_0004234 PMID:30250064 NEAT1 - inactive form (human) [mitochondrial damage] HOIP_0004234 PMID:30250064 not reported in the liver. Strikingly, NEAT1-depleted single cell clones showed a consistent reduction in mitochondrial DNA (mtDNA) (Fig. 7a), reduced mitochondrial respiration (by detection of the oxygen consumption rate (OCR); Fig. 7b) and adenosine triphosphate (ATP) production (Fig. 7c), reduced OCR and extracellular acidification rate (ECAR) rate (Fig. 7d), suggesting that the aberrant NEAT1 expression could cause mitochondrial dysfunction. HOIP:HOIP_0004235 A Toll-like receptor 9 that is encoded in the genome of human. NCBI-Human-GeneID:54106 PMID:30894684 PMID:31623280 Toll-like receptor 9 (human) TLR9(human)[mitochondrial disorder (course)] HOIP_0004235 NCBI-Human-GeneID:54106 http://www.ncbi.nlm.nih.gov/gene/54106 PMID:30894684 Drp1-mediated mitochondrial fission induced the cytosolic mtDNA stress to enhance the CCL2 secretion from HCC cells by TLR9-mediated NF-κB signaling pathway, and thus promoted the TAM recruitment and polarization. PMID:31623280 Mitochondrial DAMPs (MTDs) activate pattern recognition receptors (PRRs), such as Toll-like receptor (TLR)9. After binding to TLR9, mitochondrial DAMPs trigger numerous downstream pathways, including nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), the nucleotide binding oligomerization domain (NOD)-like receptor family, pyrin domain containing 3 (NLRP3), and interferon regulatory factor-dependent type 1 to promote inflammation. HOIP:HOIP_0004238 cyclin B1-CDK1 complex (human) [mitochondrial disorder (course)] HOIP_0004238 HOIP:HOIP_0004239 PMID:24746669 cyclin B1-CDK1 complex - inactive form (canonical)[mitochondrial disorder (course)] HOIP_0004239 PMID:24746669 Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. not reported in the liver. HOIP:HOIP_0004240 cyclin B1-CDK1 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin B1-CDK1 complex to be lower. cyclin B1-CDK1 complex inactivation HOIP_0004240 HOIP:HOIP_0004241 cyclin B1-CDK1 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin B1-CDK1 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 cyclin B1-CDK1 complex inactivation [mitochondrial disorder (course)] HOIP_0004241 PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. HOIP:HOIP_0004242 ACTA2 production is a subtype of Actin production: A process that makes existent of ACTA2 due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 ACTA2 production [mitochondrial disorder (course)] HOIP_0004242 PMID:29222479 Furthermore, Tnf-α and fibrotic mediators such as type 1 collagen 1 alpha 1 (Col1a1) and alpha smooth muscle actin (Acta2) were upregulated in the livers of GDF15 KO mice treated with CCl4 (Fig. 4d). These data demonstrate that GDF15 deficiency induces hepatic inflammation and fibrosis in the CCl4-induced model of liver fibrosis. HOIP:HOIP_0004243 The appearance of chemokine (C-C motif) ligand 2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PID:30894684 CCL2 production [mitochondrial disorder (course)] HOIP_0004243 PID:30894684 Drp1-mediated mitochondrial fission induced the cytosolic mtDNA stress to enhance the CCL2 secretion from HCC cells by TLR9-mediated NF-κB signaling pathway, and thus promoted the TAM recruitment and polarization. HOIP:HOIP_0004244 Process of binding by which free radicals interact with DNA (deoxyribonucleic acid). binding to DNA by free radicals HOIP_0004244 HOIP:HOIP_0004245 COL1A1 production is a subtype of collagen production: A process that makes existent of a ollagen due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 COL1A1 production [mitochondrial disorder (course)] HOIP_0004245 PMID:29222479 In addition, collagen deposition was significantly increased in the livers of GDF15 KO mice treated with CCl4 (Fig. 4c). Furthermore, Tnf-α and fibrotic mediators such as type 1 collagen 1 alpha 1 (Col1a1) and alpha smooth muscle actin (Acta2) were upregulated in the livers of GDF15 KO mice treated with CCl4 (Fig. 4d). These data demonstrate that GDF15 deficiency induces hepatic inflammation and fibrosis in the CCl4-induced model of liver fibrosis. HOIP:HOIP_0004246 Negative regulation of cell cycle G2/M phase transition is a subtype of negative regulation of cell cycle: Any process that stops, prevents or reduces the frequency, rate or extent of cell cycle G2/M phase transition. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 negative regulation of cell cycle G2/M phase transition [mitochondrial disorder (course)] HOIP_0004246 PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0004247 GDF15 inactivation is a subtype of molecular inactivation: A process that changes the activity of the GDF15 (Growth differentiation factor 15) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 GDF15 inactivation [mitochondrial disorder (course)] HOIP_0004247 PMID:29222479 Liver-infiltrating monocytes and neutrophils were also increased in the GDF15 KO mice during liver fibrogenesis. These changes in hepatic immune cells were associated with increased tissue inflammation and fibrosis. As shown in Fig. 3c, H&E staining and Oil Red O staining showed that hepatic fat accumulation and immune cell infiltration were increased in alcohol-fed GDF15 KO mice compared to controls (Fig. 3c). In addition, collagen deposition was significantly increased in the livers of GDF15 KO mice treated with CCl4 (Fig. 4c). Furthermore, Tnf-α and fibrotic mediators such as type 1 collagen 1 alpha 1 (Col1a1) and alpha smooth muscle actin (Acta2) were upregulated in the livers of GDF15 KO mice treated with CCl4 (Fig. 4d). These data demonstrate that GDF15 deficiency induces hepatic inflammation and fibrosis in the CCl4-induced model of liver fibrosis. Furthermore, NF-kB, JNK, and p38 signaling pathways, which are closely associated with hepatic inflammation and fibrosis, were inhibited by treatment with rGDF15 in a mouse model of liver fibrosis (Fig. 6). HOIP:HOIP_0004248 GDF15 inactivation is a subtype of molecular inactivation: A process that changes the activity of the GDF15 (Growth differentiation factor 15) to be lower. GDF15 inactivation HOIP_0004248 HOIP:HOIP_0004249 JNK signaling is a process that a signal is transmitted by the JNK (a stress-activated protein kinase (SAPK) ). This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:29222479 PMID:30898010 PMID:31623280 PMID:31649547 JNK signaling [mitochondrial disorder (course)] HOIP_0004249 PMID:23299992 Moreover, saturated FAs are able to activate c‐Jun N‐terminal kinase and trigger the mitochondrial membrane permeability transition, thus inducing mitochondrial release of cytochrome c and apoptosis. PMID:29222479 Furthermore, NF-kB, JNK, and p38 signaling pathways, which are closely associated with hepatic inflammation and fibrosis, were inhibited by treatment with rGDF15 in a mouse model of liver fibrosis (Fig. 6). PMID:30898010 In addition, there is more pronounced WAT remodeling with more adipose tissue-associated macrophages infiltration, more M1 macrophage polarization and thus an elevated inflammatory response. Mechanistically, hyperactivation of MAPK/JNK leads to insulin insensitivity, which can be inhibited by knocking out Mapk8/Jnk1 in fundc1 KO mice. PMID:31623280 Mitochondrial-derived ROS activate mitogen-activated protein kinases (MAPKs) including c-Jun N-terminal kinase (JNK). Phosphorylated JNK translocates to the mitochondria, where it binds to scaffold proteins inhibiting the mitochondrial respiratory chain and further increasing ROS production. Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. PMID:31649547 They have also demonstrated that impaired mitophagy can promote macrophage infiltration to activate MAPK signal pathway and inflammatory response to impair mitochondrial quality control, subsequently causing insulin resistance and hepatic steatosis. HOIP:HOIP_0004250 NEAT1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NEAT1 (nuclear paraspeckle assembly transcript 1) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:30250064 NEAT1 inactivation [mitochondrial disorder (course)] HOIP_0004250 PMID:30250064 not reported in the liver. Strikingly, NEAT1-depleted single cell clones showed a consis- tent reduction in mitochondrial DNA (mtDNA) (Fig. 7a), reduced mitochondrial respiration (by detection of the oxygen consumption rate (OCR); Fig. 7b) and adenosine triphosphate (ATP) production (Fig. 7c), reduced OCR and extracellular acidification rate (ECAR) rate (Fig. 7d), suggesting that the aberrant NEAT1 expression could cause mitochondrial dysfunction. HOIP:HOIP_0004251 NfkB signaling is a subtype of signaling that in which a signal is transduced with the regulation of transcription of target genes by NF-kappaB. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 PMID:30894684 PMID:31623280 NfkB signaling [mitochondrial disorder (course)] HOIP_0004251 PMID:29222479 Furthermore, NF-kB, JNK, and p38 signaling pathways, which are closely associated with hepatic inflammation and fibrosis, were inhibited by treatment with rGDF15 in a mouse model of liver fibrosis (Fig. 6). PMID:30894684 Drp1-mediated mitochondrial fission induced the cytosolic mtDNA stress to enhance the CCL2 secretion from HCC cells by TLR9-mediated NF-κB signaling pathway, and thus promoted the TAM recruitment and polarization. PMID:31623280 After binding to TLR9, mitochondrial DAMPs trigger numerous downstream pathways, including nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), the nucleotide binding oligomerization domain (NOD)-like receptor family, pyrin domain containing 3 (NLRP3), and interferon regulatory factor-dependent type 1 to promote inflammation. HOIP:HOIP_0004252 p38 signaling is a process that a signal is transmitted by the p38 (a Mitogen-Activated Protein Kinase). This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 p38 signaling [mitochondrial disorder (course)] HOIP_0004252 PMID:29222479 Furthermore, NF-kB, JNK, and p38 signaling pathways, which are closely associated with hepatic inflammation and fibrosis, were inhibited by treatment with rGDF15 in a mouse model of liver fibrosis (Fig. 6). HOIP:HOIP_0004253 TLR9 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 9. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:30894684 PMID:31623280 TLR9 signaling [mitochondrial disorder (course)] HOIP_0004253 PMID:30894684 Drp1-mediated mitochondrial fission induced the cytosolic mtDNA stress to enhance the CCL2 secretion from HCC cells by TLR9-mediated NF-κB signaling pathway, and thus promoted the TAM recruitment and polarization. PMID:31623280 Mitochondrial DAMPs (MTDs) activate pattern recognition receptors (PRRs), such as Toll-like receptor (TLR)9. After binding to TLR9, mitochondrial DAMPs trigger numerous downstream pathways, including nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), the nucleotide binding oligomerization domain (NOD)-like receptor family, pyrin domain containing 3 (NLRP3), and interferon regulatory factor-dependent type 1 to promote inflammation. HOIP:HOIP_0004254 The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 PMID:29222479 PMID:31623280 tumor necrosis factor production [mitochondrial disorder (course)] HOIP_0004254 PMID:23299992 NAFLD has been associated with higher hepatic expression of the inducible nitric oxide (NO) synthase (iNOS), mainly as a consequence of tumor necrosis factor‐α (TNF‐α) overproduction by the Kupffer cells. NO can readily react with the superoxide anion, thus generating the RNS peroxynitrite, which has deleterious effects on mitochondrial function and genome. TNF‐α is able to impair MRC activity, possibly by inducing hypoxia inducible factor‐1α (HIF‐1α) and mtDNA damage. PMID:25339807 TNF-α induces mitochondrial perturbations such as swelling with a lighter matrix and abnormal morphological alterations in the membrane. PMID:29222479 Furthermore, Tnf-α and fibrotic mediators such as type 1 collagen 1 alpha 1 (Col1a1) and alpha smooth muscle actin (Acta2) were upregulated in the livers of GDF15 KO mice treated with CCl4 (Fig. 4d). These data demonstrate that GDF15 deficiency induces hepatic inflammation and fibrosis in the CCl4-induced model of liver fibrosis. PMID:31623280 Mitochondrial ROS (mtROS) and lipid peroxidation also trigger proinflammatory cytokines such as interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), interleukin 1 beta (IL-1β), which are critical mediators of inflammation in NASH. HOIP:HOIP_0004255 A moving process of alcohol from the outside to the inside of a body. This entity is a specific course dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 PMID:29222479 alcohol intake [mitochondrial disorder (course)] HOIP_0004255 PMID:25339807 NO and other RNS are increased in response to chronic alcohol consumption through induction of iNOS. PMID:29222479 Chronic alcohol consumption alters mitochondrial oxidative phosphorylation in the liver by suppressing the synthesis of respiratory complex proteins. Alcohol-mediated damage of mitochondrial DNA (mtDNA) also impairs cellular energy metabolism via enhanced formation of reactive oxygen species (ROS). GDF15 is essential for the regulation of alcohol-mediated liver injury and steatosis. HOIP:HOIP_0004256 The appearance of interleukin-6 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:31623280 interleukin-6 production [mitochondrial disorder (course)] HOIP_0004256 PMID:23299992 mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). PMID:31623280 Mitochondrial ROS (mtROS) and lipid peroxidation also trigger proinflammatory cytokines such as interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), interleukin 1 beta (IL-1β), which are critical mediators of inflammation in NASH. HOIP:HOIP_0004257 Process of binding by which radicals interact with mtDNA (mitochondrial deoxyribonucleic acid). This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 binding to mtDNA by radicals [mitochondrial disorder (course)]] HOIP_0004257 PMID:29222479 Moreover, the radicals produced by cytochrome P450 2E1-mediated CCl4 metabolism bind to mtDNA directly and also promote lipid peroxidation, which results in degradation of mtDNA. HOIP:HOIP_0004258 Increasing free radical is a subtype of increasing quantity: A process that changes the amount of free radicals to be larger. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 increasing free radical [mitochondrial disorder (course)] HOIP_0004258 PMID:29222479 Moreover, the radicals produced by cytochrome P450 2E1-mediated CCl4 metabolism bind to mtDNA directly and also promote lipid peroxidation, which results in degradation of mtDNA. HOIP:HOIP_0004259 The process that results in the movement of mitochondriall DNA from the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:30894684 release of DNA from mitochondria [mitochondria disorder] HOIP_0004259 PMID:30894684 PMID:30894684 Drp1-mediated mitochondrial fission induced the cytosolic mtDNA stress to enhance the CCL2 secretion from HCC cells by TLR9-mediated NF-κB signaling pathway, and thus promoted the TAM recruitment and polarization. HOIP:HOIP_0004260 Decreasing mtDNA level is a subtype of decreasing quantity: A process that changes the amount of glycogen level to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:21145849 PMID:25339807 PMID:30250064 decreasing mtDNA level [mitochondrial disorder (course)] HOIP_0004260 PMID:21145849 Table 1. Both tamoxifen and tacrine reduce mtDNA synthesis by interacting with the mitochondrial topoisomerases. Fourthly, drugs can impair mitochondrial FAO and induce microvesicular steatosis by reducing mtDNA levels (Table 1). Indeed, profound mtDNA depletion induces MRC impairment and secondary inhibition of FAO. This has been shown for the antiviral fialuridine (FIAU), AZT, d4T, and ddI, which all inhibit the mtDNA polymerase γ. PMID:25339807 MtDNA depletion in hepatocytes impairs mitochondrial function and causes hepatic steatosis and other liver injury. Reduced levels of mtDNA have also been reported in patients with NASH that seem to be responsible for the impairment of mitochondrial function and development and progression of liver steatosis and other liver injuries. Reduced expression of mtDNA-encoded polypeptides has been reported in patients with NASH, further supporting a role for mtDNA depletion in mitochondrial dysfunction. PMID:30250064 not reported in the liver. Strikingly, NEAT1-depleted single cell clones showed a consistent reduction in mitochondrial DNA (mtDNA) (Fig. 7a), reduced mitochondrial respiration (by detection of the oxygen consumption rate (OCR); Fig. 7b) and adenosine triphosphate (ATP) production (Fig. 7c), reduced OCR and extracellular acidification rate (ECAR) rate (Fig. 7d), suggesting that the aberrant NEAT1 expression could cause mitochondrial dysfunction. HOIP:HOIP_0004261 The division of a mitochondrion within a cell to form two or more separate mitochondrial compartments. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. The division of a mitochondrion within a cell to form two or more separate mitochondrial compartments. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:28789970 PMID:30894684 mitochondria fission [mitochondrial disorder (course)] HOIP_0004261 The division of a mitochondrion within a cell to form two or more separate mitochondrial compartments. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:11038192 PMID:28789970 Fission permits distribution of mitochondria throughout a cell (e.g., transport down axons or to permit allocation prior to cell division), and facilitates apoptosis via release of cytochrome C under some circumstances (Mishra and Chan 2014). High-level exposures may result in increased fission, which blocks efficient ATP generation and limits rates of functional complementation, in addition to potentially leading to apoptosis. PMID:30894684 In the present study, our data demonstrated that increased mitochondrial fission induced release of mtDNA into the cytosol in HCC cells, which is commonly recognized as cytosolic mtDNA stress, suggesting a potentially critical role of mitochondrial fission-regulated mtDNA hemostasis in hepatocarcinogenesis. Drp1-mediated mitochondrial fission induced the cytosolic mtDNA stress to enhance the CCL2 secretion from HCC cells by TLR9-mediated NF-κB signaling pathway, and thus promoted the TAM recruitment and polarization. HOIP:HOIP_0004262 The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 mitochondrial DNA catabolic process [mitochondrial disorder (course)] HOIP_0004262 PMID:29222479 Moreover, the radicals produced by cytochrome P450 2E1-mediated CCl4 metabolism bind to mtDNA directly and also promote lipid peroxidation, which results in degradation of mtDNA. HOIP:HOIP_0004263 The process that results in the movement of cytochrome c from the mitochondrial intermembrane space into the cytosol, which is part of the apoptotic signaling pathway and leads to caspase activation. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:23299992 PMID:25339807 PMID:28789970 release of cytochrome c from mitochondria [mitochondrial disorder (course)] HOIP_0004263 PMID:23299992 Moreover, saturated FAs are able to activate c‐Jun N‐terminal kinase and trigger the mitochondrial membrane permeability transition, thus inducing mitochondrial release of cytochrome c and apoptosis. PMID:25339807 Mitochondrial dysfunction results in the release of several proapoptotic proteins into the cytosol, including cytochrome c. Cardiolipin has been shown to be involved in several steps of the intrinsic pathway of the apoptotic process, including mitochondrial permeability transition pore (MPTP) and cytochrome c release from mitochondria. Another consequence of cytochrome c release from mitochondria is that it interferes with electron transport through ETC, resulting in ROS formation and triggering a new vicious cycle, which will worsen the disturbance. PMID:28789970 Fission permits distribution of mitochondria throughout a cell (e.g., transport down axons or to permit allocation prior to cell division), and facilitates apoptosis via release of cytochrome C under some circumstances (Mishra and Chan 2014). HOIP:HOIP_0004264 Energy metabolic dysfunction is a subtype of Metabolic dysfunctioning: A process that performs an abnormal and incomplete energy metabolic function. This entity is a specific course-dependent process. This process can constitute the Mitochondrial disorder. PMID:23299992 PMID:24746669 PMID:29222479 PMID:29335519 PMID:31623280 metabolic dysfunction of precursor metabolites and energy generation [mitochondrial disorder (course)] HOIP_0004264 PMID:23299992 Experimental investigations also pointed to a progressive reduction of MRC activity during NAFLD, which could impair energy output and aggravate ROS overproduction by the damaged MRC. PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). PMID:29222479 Alcohol-mediated damage of mitochondrial DNA (mtDNA) also impairs cellular energy metabolism via enhanced formation of reactive oxygen species (ROS). PMID:29335519 Metabolic reprogramming by PCK1 promotes TCA cataplerosis, oxidative stress and apoptosis in liver cancer cells and suppresses hepatocellular carcinoma. PMID:31623280 Emerging evidence suggests that mitochondrial dysfunction or maladaptation contributes to detrimental effects on hepatocyte bioenergetics, reactive oxygen species (ROS) homeostasis, endoplasmic reticulum (ER) stress, inflammation, and cell death leading to NASH and HCC. HOIP:HOIP_0004265 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex IV assembly. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:29222479 Negative regulation of respiratory complex IV proteins synthesis [mitochondrial disorder (course)] HOIP_0004265 PMID:29222479 Additionally, carbon tetrachloride (CCl4) reduces mitochondrial respiratory chain complex IV activity and depletes mtDNA in the liver. HOIP:HOIP_0004266 The orderly movement of a monocyte from one site to another. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 monocyte migration [mitochondrial disorder (course)] HOIP_0004266 PMID:29222479 Liver-infiltrating monocytes and neutrophils were also increased in the GDF15 KO mice during liver fibrogenesis. These changes in hepatic immune cells were associated with increased tissue inflammation and fibrosis. HOIP:HOIP_0004267 Increasing uptake amount of mitochondrial calcium ion is a subtype of increasing quantity: A process that changes the uptake amount of mitochondrial calcium ion to be higher. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. increasing uptake amount of mitochondrial calcium ion [mitochondrial disorder (course)] HOIP_0004267 HOIP:HOIP_0004268 The orderly movement of a neutrophil from one site to another. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 neutrophil migration [mitochondrial disorder (course)] HOIP_0004268 PMID:29222479 Liver-infiltrating monocytes and neutrophils were also increased in the GDF15 KO mice during liver fibrogenesis. These changes in hepatic immune cells were associated with increased tissue inflammation and fibrosis. HOIP:HOIP_0004269 The synthesis or release of a cytokine following a inflammatory stimulus as part of an inflammatory response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 PMID:29222479 PMID:31623280 cytokine production involved in inflammatory response [mitochondrial disorder (course)] HOIP_0004269 PMID:25339807 Oxidative stress may cause damage at cellular level, such as membrane lipid peroxidation, cell degeneration and necrosis, cell death by apoptosis, proinflammatory cytokine expression, liver stellate cell activation and fibrogenesis. PMID:29222479 GDF15 may regulate the hepatic immune microenvironment by inhibiting pro-inflammatory cytokine production from liver-resident macrophages. PMID:31623280 Mitochondrial ROS (mtROS) and lipid peroxidation also trigger proinflammatory cytokines such as interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), interleukin 1 beta (IL-1β), which are critical mediators of inflammation in NASH. HOIP:HOIP_0004270 Inflammatory cytokine gene expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature inflammatory cytokine gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. inflammatory cytokine gene expression [mitochondrial disorder (course)] HOIP_0004270 HOIP:HOIP_0004271 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:26571396 PMID:29222479 PMID:31623280 PMID:31649547 Inflammatory response [mitochondrial disorder (course)] HOIP_0004271 PMID:26571396 Mitochondrial metabolism mediates oxidative stress and inflammation in fatty liver. Second, loss of anaplerosis/cataplerosis via genetic knockdown of phosphoenolpyruvate carboxykinase 1 (Pck1) prevented fatty acid-induced rise in oxidative flux, oxidative stress, and inflammation. Figure 8 Histological data support a role for oxidative metabolism in NAFLD in humans. PMID:29222479 Liver-infiltrating monocytes and neutrophils were also increased in the GDF15 KO mice during liver fibrogenesis. These changes in hepatic immune cells were associated with increased tissue inflammation and fibrosis. PMID:31623280 Emerging evidence suggests that mitochondrial dysfunction or maladaptation contributes to detrimental effects on hepatocyte bioenergetics, reactive oxygen species (ROS) homeostasis, endoplasmic reticulum (ER) stress, inflammation, and cell death leading to NASH and HCC. Saturated fats promote fatty liver and accumulation of lipotoxic byproducts including ceramides and diacylglycerols is associated with hepatic inflammation and mitochondrial ROS production resulting in liver cell death. PMID:31649547 lipotoxicity and inflammation can interfere with insulin signaling pathway to cause hepatic insulin resistance; HOIP:HOIP_0004272 Cellular damage is a subtype of damaging: A process that injuries the structure of the cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 PMID:31623280 cellular damage [mitochondrial disorder (course)] HOIP_0004272 PMID:29222479 Hepatocytes display an eosinophilic cytoplasm upon hematoxylin-eosin staining, reflecting abundant mitochondria. Thus, it is not surprising that mitochondrial dysfunction promotes cellular damage and is linked to liver diseases. PMID:31623280 Moreover, TNF-α and IL-6 promote iron accumulation, which further fuels oxidative stress-driven cell toxicity and can activate fibrogenesis and carcinogenesis in metabolic syndrome. HOIP:HOIP_0004273 Tumor-associated macrophage (TAM) activation is a subtype of macrophage activation: A change in morphology and behavior of TAMs resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:30894684 Tumor-associated macrophage activation[mitochondrial disorder (course)] HOIP_0004273 PMID:30894684 Tumor-associated macrophages (TAMs) contribute to hepatocellular carcinoma (HCC) progression. Drp1-mediated mitochondrial fission induced the cytosolic mtDNA stress to enhance the CCL2 secretion from HCC cells by TLR9-mediated NF-κB signaling pathway, and thus promoted the TAM recruitment and polarization. HOIP:HOIP_0004274 The orderly movement of a TAM macrophage from one site to another. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:30894684 tumor-associated macrophage migration [mitochondrial disorder (course)] HOIP_0004274 PMID:30894684 Drp1-mediated mitochondrial fission induced the cytosolic mtDNA stress to enhance the CCL2 secretion from HCC cells by TLR9-mediated NF-κB signaling pathway, and thus promoted the TAM recruitment and polarization. HOIP:HOIP_0004275 The orderly movement of a TAM macrophage from one site to another. TAM recruitment tumor-associated macrophage migration HOIP_0004275 HOIP:HOIP_0004277 Tumor-associated macrophage (TAM) activation is a subtype of macrophage activation: A change in morphology and behavior of TAMs resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. Tumor-associated macrophage polarization Tumor-associated macrophage activation HOIP_0004277 HOIP:HOIP_0004278 Lipoperoxidation is a subtype of lipid oxidation: The degradation of lipids caused by an oxidative attack from free radicals. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:29222479 PMID:31623280 lipoperoxidation [mitochondrial disorder (course)] HOIP_0004278 PMID:23299992 Other mechanisms leading to impaired MRC activity could include higher levels of different lipid intermediates including free FAs, increased generation of lipid peroxidation products such as 4‐HNE, and reduced adiponectin action. In addition to ROS, reactive nitrogen species (RNS) and lipid peroxidation products are able to damage mtDNA. Several MRC complexes including COX are sensitive to ROS and RNS. In addition, COX can be inhibited by low levels of NO and inactivated by 4‐hydroxynonenal (4‐HNE), a reactive aldehyde generated during lipid peroxidation. PMID:29222479 Moreover, the radicals produced by cytochrome P450 2E1-mediated CCl4 metabolism bind to mtDNA directly and also promote lipid peroxidation, which results in degradation of mtDNA. PMID:31623280 The imbalance of respiratory complex activity during the development of NAFLD and its progression to NASH leads to increased mitochondrial reactive oxygen species (ROS), causing oxidative mitochondrial DNA (mtDNA) damage, mitochondria structural abnormalities, and lipid peroxidation. Mitochondrial ROS (mtROS) and lipid peroxidation also trigger proinflammatory cytokines such as interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), interleukin 1 beta (IL-1β), which are critical mediators of inflammation in NASH. HOIP:HOIP_0004279 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 PMID:29222479 PMID:31623280 hepatic fibrosis [mitochondrial disorder (course)] HOIP_0004279 PMID:25339807 Oxidative stress may cause damage at cellular level, such as membrane lipid peroxidation, cell degeneration and necrosis, cell death by apoptosis, proinflammatory cytokine expression, liver stellate cell activation and fibrogenesis. PMID:29222479 Liver-infiltrating monocytes and neutrophils were also increased in the GDF15 KO mice during liver fibrogenesis. These changes in hepatic immune cells were associated with increased tissue inflammation and fibrosis. Recombinant GDF15 attenuates CCl4-induced liver fibrosis by suppressing the hepatic inflammatory response. In addition, collagen deposition was significantly increased in the livers of GDF15 KO mice treated with CCl4 (Fig. 4c). Furthermore, Tnf-α and fibrotic mediators such as type 1 collagen 1 alpha 1 (Col1a1) and alpha smooth muscle actin (Acta2) were upregulated in the livers of GDF15 KO mice treated with CCl4 (Fig. 4d). These data demonstrate that GDF15 deficiency induces hepatic inflammation and fibrosis in the CCl4-induced model of liver fibrosis. PMID:31623280 Moreover, TNF-α and IL-6 promote iron accumulation, which further fuels oxidative stress-driven cell toxicity and can activate fibrogenesis and carcinogenesis in metabolic syndrome. HOIP:HOIP_0004281 Liver malfunction is a subtype of organ malfunction: A process that does not perform liver function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 PMID:26571396 PMID:29222479 liver malfunction [mitochondrial disorder (course)] HOIP_0004281 PMID:25339807 MtDNA depletion in hepatocytes impairs mitochondrial function and causes hepatic steatosis and other liver injury. PMID:26571396 During nonalcoholic fatty liver disease (NAFLD), mitochondria also produce ROS that damage hepatocytes, trigger inflammation, and contribute to insulin resistance. Figure 8 Histological data support a role for oxidative metabolism in NAFLD in humans. PMID:29222479 Hepatocytes display an eosinophilic cytoplasm upon hematoxylin-eosin staining, reflecting abundant mitochondria. Thus, it is not surprising that mitochondrial dysfunction promotes cellular damage and is linked to liver diseases. HOIP:HOIP_0004282 Scleroprotein production is a subtype of protein production: A process that makes existent of scleroprotein due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. Scleroprotein production HOIP_0004282 HOIP:HOIP_0004283 Collagen production is a subtype of scleroprotein production: A process that makes existent of collagen due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. Collagen production HOIP_0004283 HOIP:HOIP_0004284 COL1A1 production is a subtype of collagen production: A process that makes existent of a ollagen due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. COL1A1 production HOIP_0004284 HOIP:HOIP_0004285 cytoskeletal protein production is a subtype of protein production: A process that makes existent of cytoskeletal protein due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. cytoskeletal protein production HOIP_0004285 HOIP:HOIP_0004286 Actin production is a subtype of cytoskeletal protein production: A process that makes existent of actin due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. actin production HOIP_0004286 HOIP:HOIP_0004287 ACTA2 production is a subtype of Actin production: A process that makes existent of ACTA2 due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. ACTA2 production HOIP_0004287 HOIP:HOIP_0004290 NCBI-Human-GeneID:59 NCBI-Mouse-GeneID:11475 NCBI-Rat-GeneID:81633 ACTA2 (mol) HOIP_0004290 NCBI-Human-GeneID:59 http://www.ncbi.nlm.nih.gov/gene/59 NCBI-Mouse-GeneID:11475 http://www.ncbi.nlm.nih.gov/gene/11475 NCBI-Rat-GeneID:81633 http://www.ncbi.nlm.nih.gov/gene/81633 HOIP:HOIP_0004292 PMID:29222479 p38(canonical) [mitochondrial disorder (course)] HOIP_0004292 PMID:29222479 Furthermore, NF-kB, JNK, and p38 signaling pathways, which are closely associated with hepatic inflammation and fibrosis, were inhibited by treatment with rGDF15 in a mouse model of liver fibrosis (Fig. 6). HOIP:HOIP_0004293 Mitochondrial damage dependent molecule is a subtype of course dependent chemical entity. This gene can participate in the course of Mitochondrial damage as a gene product. Gene profile:caonical that described in textbooks or articles. mitochondrial damage dependent molecule (canonical) HOIP_0004293 HOIP:HOIP_0004294 The chemical reactions and pathways involving carbon tetrachloride, a toxic, carcinogenic compound which is used as a general solvent in industrial degreasing operations. It is also used as grain fumigant and a chemical intermediate in the production of refrigerants. http://purl.obolibrary.org/obo/GO_0018885 carbon tetrachloride metabolic process HOIP_0004294 HOIP:HOIP_0004295 The chemical reactions and pathways involving carbon tetrachloride, a toxic, carcinogenic compound which is used as a general solvent in industrial degreasing operations. It is also used as grain fumigant and a chemical intermediate in the production of refrigerants. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 http://purl.obolibrary.org/obo/GO_0018885 carbon tetrachloride metabolic process [mitochondrial disorder (course)] HOIP_0004295 PMID:29222479 Moreover, the radicals produced by cytochrome P450 2E1-mediated CCl4 metabolism bind to mtDNA directly and also promote lipid peroxidation, which results in degradation of mtDNA. HOIP:HOIP_0004296 A role played by the entity which receives DNA and transmits operand(s). DNA sensor HOIP_0004296 HOIP:HOIP_0004297 NEAT1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NEAT1 (nuclear paraspeckle assembly transcript 1) to be lower. NEAT1 inactivation HOIP_0004297 HOIP:HOIP_0004300 TLR9 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 9. TLR9 signaling HOIP_0004300 HOIP:HOIP_0004301 TLR signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor. TLR signaling HOIP_0004301 HOIP:HOIP_0004303 p38 signaling is a process that a signal is transmitted by the p38 (a Mitogen-Activated Protein Kinase). p38 signaling HOIP_0004303 HOIP:HOIP_0004305 energy metabolic dysfunction is a subtype of Metabolic dysfunctioning: A process that performs an abnormal and incomplete energy metabolic function. metabolic dysfunction of precursor metabolites and energy generation HOIP_0004305 HOIP:HOIP_0004306 The aggregation of collagen in a particular location in an organism, tissue or cell, occurring in response to some external stimulus. collagen deposition HOIP_0004306 HOIP:HOIP_0004307 The aggregation of collagen in a particular location in an organism, tissue or cell, occurring in response to some external stimulus. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29222479 collagen deposition [mitochondrial disorder (course)] HOIP_0004307 PMID:29222479 In addition, collagen deposition was significantly increased in the livers of GDF15 KO mice treated with CCl4 (Fig. 4c). Furthermore, Tnf-α and fibrotic mediators such as type 1 collagen 1 alpha 1 (Col1a1) and alpha smooth muscle actin (Acta2) were upregulated in the livers of GDF15 KO mice treated with CCl4 (Fig. 4d). These data demonstrate that GDF15 deficiency induces hepatic inflammation and fibrosis in the CCl4-induced model of liver fibrosis. HOIP:HOIP_0004308 Process of binding by which radicals interact with mtDNA (mitochondrial deoxyribonucleic acid). binding to mtDNA by radicals HOIP_0004308 HOIP:HOIP_0004310 Decreasing mtDNA level is a subtype of decreasing quantity: A process that changes the amount of mtDNA level to be lower. decreasing mtDNA level HOIP_0004310 HOIP:HOIP_0004312 mitochondrial disorder dependent chemical compound is a subtype of course dependent chemical entity. This entity (drug) can participate in the course of mitochondrial disorder. mitochondria disorder dependent chemical compound HOIP_0004312 HOIP:HOIP_0004314 A role played by the entity which negative regulates the respiratory chain. respiratory chain inhibitor role HOIP_0004314 HOIP:HOIP_0004316 PMID:29222479 CCL4 [mitochondrial disorder (course)] HOIP_0004316 PMID:29222479 Additionally, carbon tetrachloride (CCl4) reduces mitochondrial respiratory chain complex IV activity and depletes mtDNA in the liver. HOIP:HOIP_0004317 A molecular entity possessing an unpaired electron. free radical radicals [mitochondrial disorder (course)] HOIP_0004317 HOIP:HOIP_0004318 NCBI-Human-GeneID: PMID:25181692 STAT3(human)[mitochondrial disorder (course)] HOIP_0004318 NCBI-Human-GeneID: http://www.ncbi.nlm.nih.gov/gene/6774 PMID:25181692 Tumor-Associated Macrophages Produce Interleukin 6 and Signal via STAT3 to Promote Expansion of Human Hepatocellular Carcinoma Stem Cells TAMs produce IL6, which promotes expansion of these CSCs and tumorigenesis. Levels of IL6 in human HCC samples correlate with tumor stage and markers of CSCs. We have identified that STAT3 signaling in HCC cells following TAM interaction is critical to increased CSC expansion and increased tumor growth. HOIP:HOIP_0004319 NCBI-Human-GeneID:3569 PMID:25181692 PMID:31623280 IL-6(human)[mitochondrial disorder (course)] HOIP_0004319 NCBI-Human-GeneID:3569 http://www.ncbi.nlm.nih.gov/gene/3569 PMID:25181692 Tumor-Associated Macrophages Produce Interleukin 6 and Signal via STAT3 to Promote Expansion of Human Hepatocellular Carcinoma Stem Cells. PMID:31623280 Moreover, TNF-α and IL-6 promote iron accumulation, which further fuels oxidative stress-driven cell toxicity and can activate fibrogenesis and carcinogenesis in metabolic syndrome. HOIP:HOIP_0004320 An attribute of the finding of bodily injury due to the poisonous effects of drugs. drug toxicity HOIP_0004320 HOIP:HOIP_0004321 An attribute of the finding of liver injury due to the poisonous effects of drugs. drug liver toxicity HOIP_0004321 HOIP:HOIP_0004322 toxicity value HOIP_0004322 HOIP:HOIP_0004323 From Drug Induced Liver Injury Rank (DILIrank) Dataset. DILIrank consists of 1,036 FDA-approved drugs that are divided into four classes according to their potential for causing drug-induced liver injury (DILI). Most-DILI-Concern HOIP_0004323 HOIP:HOIP_0004324 IL6 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to Interleukin 6. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25181692 PMID:31623280 IL6 signaling [mitochondrial disorder (course)] HOIP_0004324 PMID:23299992 Numerous studies showed increased expression of PPARα in fatty liver. Different cues such as FAs, leptin, and IL6 could activate PPARα and its target genes involved in mtFAO (CPT1, MCAD), peroxisomal FAO (acyl‐CoA oxidase), and VLDL production (microsomal triglyceride transfer protein). mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). PMID:25181692 Tumor-Associated Macrophages Produce Interleukin 6 and Signal via STAT3 to Promote Expansion of Human Hepatocellular Carcinoma Stem Cells. PMID:31623280 Mitochondrial ROS (mtROS) and lipid peroxidation also trigger proinflammatory cytokines such as interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), interleukin 1 beta (IL-1β), which are critical mediators of inflammation in NASH. Moreover, TNF-α and IL-6 promote iron accumulation, which further fuels oxidative stress-driven cell toxicity and can activate fibrogenesis and carcinogenesis in metabolic syndrome. HOIP:HOIP_0004325 STAT3 activation is a subtype of molecular activation: A process that changes the activity of the STAT3 to be higher. This entity is a specific course-dependent process. This process can constitute the course of Mitochondrial disorder. PMID:25181692 STAT3 activation[mitochondrial disorder (course)] HOIP_0004325 PMID:23334697 PMID:25181692 Tumor-Associated Macrophages Produce Interleukin 6 and Signal via STAT3 to Promote Expansion of Human Hepatocellular Carcinoma Stem Cells HOIP:HOIP_0004326 STAT3 activation is a subtype of molecular activation: A process that changes the activity of the STAT3 to be higher. STAT3 activation HOIP_0004326 HOIP:HOIP_0004327 IL-6 signaling is a process that a signal is transmitted by the cytokine IL-6. IL-6 signaling HOIP_0004327 HOIP:HOIP_0004328 reactive aldehyde HOIP_0004328 HOIP:HOIP_0004329 mitochondrial respiratory chain complex I subunit HOIP_0004329 HOIP:HOIP_0004330 C19H35N C1CCC(CC1)C(CC1CCCCN1)C1CCCCC1 DrugBank:DB01074 PMID:21145849 Wikipedia:Perhexiline perhexiline [mitochondrial disorder (course)] HOIP_0004330 PMID:21145849 Table 1. HOIP:HOIP_0004331 PMID:21145849 Wikipedia:Acetaminophen Wikipedia:Paracetamol N-(4-hydroxyphenyl)acetamide paracetamol [mitochondrial disorder (course)] APAP Acetaminophen [mitochondrial disorder (course)] HOIP_0004331 PMID:21145849 For instance APAP and troglitazone can induce mtDNA strand breaks which eventually lead to a reduction of mtDNA levels. Indeed, damaged mtDNA molecules harboring numerous strand breaks can be rapidly degraded by mitochondrial endonucleases. Table 1. HOIP:HOIP_0004332 ISBN:0071769234 PMID:21145849 amiodarone [mitochondrial disorder (course)]] HOIP_0004332 ISBN:0071769234 Drug-induced steatosis is mainly caused by compounds such as amiodarone, tamoxifen, which accumulate in mitochondria and inhibit β-oxidation and mitochondrial respiration. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition PMID:21145849 Table 1. HOIP:HOIP_0004333 PMID:21145849 Wikipedia:Alpidem alpidem [mitochondrial disorder (course)] HOIP_0004333 PMID:21145849 Table 1. HOIP:HOIP_0004334 PMID:21145849 Wikipedia:Disulfiram disulfiram [mitochondrial disorder (course)] HOIP_0004334 PMID:21145849 Table 1. HOIP:HOIP_0004335 PMID:21145849 PMID:24003057 tamoxifen [mitochondrial disorder (course)] HOIP_0004335 PMID:21145849 Table 1. HOIP:HOIP_0004336 PMID:21145849 Wikipedia:Tetracycline tetracycline [mitochondrial disorder (course)] HOIP_0004336 PMID:21145849 Table 1. HOIP:HOIP_0004337 A chromane that has formula C24H27NO5S. Direct competition of troglitazone metabolites with conjugated bilirubin at the level of MRP2 could result in conjugated hyperbilirubinemia. Direct competition of troglitazone metabolites with conjugated bilirubin at the level of MRP2 could result in conjugated hyperbilirubinemia. Rifampicin, bosentan, and troglitazone directly inhibit bile salt export pump (BSEP). Rifampicin, bosentan, and troglitazone directly inhibit bile salt export pump (BSEP). ATC:A10BG01 PMID:11717175 PMID:21145849 troglitazone [mitochondrial disorder (course)] HOIP_0004337 ISBN:0071769234 ISBN:0123878179 Direct competition of troglitazone metabolites with conjugated bilirubin at the level of MRP2 could result in conjugated hyperbilirubinemia. PMID:21480339 Rifampicin, bosentan, and troglitazone directly inhibit bile salt export pump (BSEP). ISBN:0071769234 PMID:21145849 Table 1. For instance APAP and troglitazone can induce mtDNA strand breaks which eventually lead to a reduction of mtDNA levels. Indeed, damaged mtDNA molecules harboring numerous strand breaks can be rapidly degraded by mitochondrial endonucleases. HOIP:HOIP_0004338 PMID:21145849 Wikipedia:Nilutamide nilutamide [mitochondrial disorder (course)] HOIP_0004338 PMID:21145849 Table 1. HOIP:HOIP_0004339 PMID:21145849 Wikipedia:Buprenorphine buprenorphine [mitochondrial disorder (course)] HOIP_0004339 PMID:21145849 Table 1. HOIP:HOIP_0004340 Increasing demand for response to ER stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the endoplasmic reticulum (ER) stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 increasing demand for response to ER stress [mitochondrial disorder (course)] HOIP_0004340 PMID:31623280 Emerging evidence suggests that mitochondrial dysfunction or maladaptation contributes to detrimental effects on hepatocyte bioenergetics, reactive oxygen species (ROS) homeostasis, endoplasmic reticulum (ER) stress, inflammation, and cell death leading to NASH and HCC. HOIP:HOIP_0004341 cardiolipin peroxidation is a subtype of phospholipid oxidation: The degradation of cardiolipin caused by an oxidative attack from free radicals. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 PMID:25339807 cardiolipin peroxidation [mitochondrial disorder (course)] HOIP_0004341 PMID:25339807 Cardiolipin peroxidation has been associated with mitochondrial dysfunction in multiple tissues in several physiopathological conditions, including NAFLD. Indeed, in mitochondria lacking CL, a respiratory supercomplex formed by complex III and IV is destabilized. Similarly, dimeric organization of ADP/ATP carrier and other ADP/ATP carrier-containing supercomplexes are destabilized in CL-deficient mitochondria. These results suggest that the observed dysfunction of complex I in hepatic mitochondria from CDD animals could be attributed, at least in part, to ROS-induced cardiolipin alterations. Cardiolipin has been shown to be involved in several steps of the intrinsic pathway of the apoptotic process, including mitochondrial permeability transition pore (MPTP) and cytochrome c release from mitochondria. In addition, CL oxidation seems to promote the permeabilization of the outer mitochondrial membrane, probably interacting with Bcl2 family proteins, such as Bax and Bid. Thus, oxidized CL may have a critical role in several steps of the apoptotic process such as: the translocation of t-Bid to mitochondria with subsequent oligomerization of Bax and Bak leading to membrane permeabilization; cytochrome c dissociation from the inner mitochondrial membrane; and activation of MPTP, followed by the release of this hemoprotein from the mitochondrial intermembrane space to the cytosol (Figure ​1). HOIP:HOIP_0004342 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 PMID:31623280 necrosis [mitochondrial disorder (course)] HOIP_0004342 PMID:25339807 Oxidative stress may cause damage at cellular level, such as membrane lipid peroxidation, cell degeneration and necrosis, cell death by apoptosis, proinflammatory cytokine expression, liver stellate cell activation and fibrogenesis. If MPTP opening is transient, the cell can recover; while in conditions of prolonged MPTP opening and ATP depletion, irreversible damage and cell death occur, predominantly through necrosis. PMID:31623280 Reduced mitophagy results in the accumulation of severely damaged mitochondria, leading to cell necrosis releasing mitochondrial damage-associated molecular patterns (DAMPs) that can promote liver inflammation and NASH development. Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). HOIP:HOIP_0004343 Cellular membrane lipoperoxidation is a subtype of lipoperoxidation: A process that the degradation of lipids of cellular membrane caused by an oxidative attack from free radicals. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 cellular membrane lipoperoxidation [mitochondrial disorder (course)] HOIP_0004343 PMID:25339807 Oxidative stress may cause damage at cellular level, such as membrane lipid peroxidation, cell degeneration and necrosis, cell death by apoptosis, proinflammatory cytokine expression, liver stellate cell activation and fibrogenesis. HOIP:HOIP_0004344 A change in the morphology or behavior of a hepatic stellate cell resulting from exposure to a cytokine, chemokine, hormone, cellular ligand or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 hepatic stellate cell activation [mitochondrial disorder (course)] HOIP_0004344 PMID:25339807 Oxidative stress may cause damage at cellular level, such as membrane lipid peroxidation, cell degeneration and necrosis, cell death by apoptosis, proinflammatory cytokine expression, liver stellate cell activation and fibrogenesis. HOIP:HOIP_0004345 mitochondrial membrane morphology changes is a subtype of mitochondria morphology changes: A process that changes the morphology of the mitochondrial membrane. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. mitochondrial membrane morphology changes [mitochondrial disorder (course)] HOIP_0004345 HOIP:HOIP_0004346 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 IL-1beta production [mitochondrial disorder (course)] HOIP_0004346 PMID:31623280 Mitochondrial ROS (mtROS) and lipid peroxidation also trigger proinflammatory cytokines such as interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), interleukin 1 beta (IL-1β), which are critical mediators of inflammation in NASH. HOIP:HOIP_0004347 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 PMID:31649547 Insulin resistance (process) [mitochondrial disorder (course)] HOIP_0004347 PMID:31623280 Recent studies also show that MAMs are important for hepatic insulin signaling, nutrient sensing, and glucose homeostasis. Therefore, disruption of ER-mitochondria contact sites could exacerbate hepatic lipid accumulation and miscommunication between organelles appears to be related to the pathology of hepatic metabolic diseases. PMID:31649547 lipotoxicity and inflammation can interfere with insulin signaling pathway to cause hepatic insulin resistance; In conclusion, mitochondrial dysfunction gives rise to hepatic fatty acid accumulation, which ultimately impairs insulin signal pathway and causes hepatic insulin resistance. HOIP:HOIP_0004348 Calcium ion homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a calcium ion homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Calcium ion homeostasis imbalance [mitochondrial disorder (course)] HOIP_0004348 PMID:31623280 Mitochondrial ROS and oxidative stress can disrupt ER function leading to inappropriate release of calcium in liver parenchymal cells. HOIP:HOIP_0004349 Hypofunction of sequestering of calcium ion in ER is a subtype of hypofunctioning: A process that performs a decreased or insufficient sequestering of calcium ion in ER. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder.. PMID:31623280 Hypofunction of sequestering of calcium ion in ER [mitochondrial disorder (course)] HOIP_0004349 PMID:31623280 Mitochondrial ROS and oxidative stress can disrupt ER function leading to inappropriate release of calcium in liver parenchymal cells. Moreover, oxidative stress and ROS lead to the release of calcium by the endoplasmic reticulum, further increasing mitochondria ROS production and potentiating proapoptotic pathways. HOIP:HOIP_0004350 mitochondria morphology changes is a subtype of changing shape: A process that changes the morphology of the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:27151080 PMID:31623280 mitochondria morphology change [mitochondrial disorder (course)] HOIP_0004350 PMID:27151080 In the present study we showed that mutations in TARDBP and C9ORF72 genes, associated to defects in RNA metabolism in ALS and FTD neurodegenerative diseases, affect mitochondria functionality by altering several morphological and bioenergetics parameters in a gene-specific manner. These results suggest that an altered balance of fission and fusion processes may account for the mitochondria morphology changes observed in mTDP-43 and mC9ORF72 fibroblasts. not reported in the liver. PMID:31623280 The imbalance of respiratory complex activity during the development of NAFLD and its progression to NASH leads to increased mitochondrial reactive oxygen species (ROS), causing oxidative mitochondrial DNA (mtDNA) damage, mitochondria structural abnormalities, and lipid peroxidation. Consistent with this, high glucose induces mitochondrial fragmentation, ROS production, loss of mitochondrial membrane potential, and ATP depletion in several rodent and human cell models. More precisely, dietary-induced hypercholesterolemia causes oxidative stress, loss of mitochondrial membrane potential, reduction in ATP content, loss of mitochondrial cristae, and hepatic steatosis in mice. HOIP:HOIP_0004351 Any process that results in a change in state of redox. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:30232152 PMID:31623280 redox changes [mitochondrial disorder (course)] HOIP_0004351 PMID:30232152 not reported in the liver. Exogenous H2O2 activates AMPK indirectly in myotubes by decreasing the ATP/ADP ratio. We conclude that AMPK activity in response to redox changes is not due to direct action on AMPK itself, but is a secondary consequence of redox effects on other processes, such as mitochondrial ATP production. PMID:31623280 Mitochondrial-derived ROS also activate AMP-activated protein kinase (AMPK) secondary to redox changes and mitochondrial ATP production. Thus, accumulating evidences suggest that cholesterol overload in mitochondria induces redox imbalances leading to oxidative stress and cell death associated with steatohepatitis. HOIP:HOIP_0004352 PMID:21145849 Wikipedia:Salicylic_acid salicylic acid [mitochondrial disorder (course)] HOIP_0004352 PMID:21145849 Table 1. HOIP:HOIP_0004353 A monocarboxylic acid consisting of phenylacetic acid having a (2,6-dichlorophenyl)amino group at the 2-position. ATC:D11AX18 ATC:M01AB05 ATC:M02AA15 ATC:S01BC03 PMID:21145849 Wikipedia:Diclofenac diclofenac [mitochondrial disorder (course)] HOIP_0004353 PMID:21145849 Table 1. HOIP:HOIP_0004354 PMID:21145849 nimesulide [mitochondrial disorder (course)] HOIP_0004354 PMID:21145849 Table 1. HOIP:HOIP_0004355 NCBI-Human-GeneID:578 NCBI-Mouse-GeneID:12018 NCBI-Rat-GeneID:116502 PMID:25339807 BAK1(canonical) [mitochondrial disorder (course)] HOIP_0004355 NCBI-Human-GeneID:578 http://www.ncbi.nlm.nih.gov/gene/578 NCBI-Mouse-GeneID:12018 http://www.ncbi.nlm.nih.gov/gene/12018 NCBI-Rat-GeneID:116502 http://www.ncbi.nlm.nih.gov/gene/116502 PMID:25339807 In addition, CL oxidation seems to promote the permeabilization of the outer mitochondrial membrane, probably interacting with Bcl2 family proteins, such as Bax and Bid. Thus, oxidized CL may have a critical role in several steps of the apoptotic process such as: the translocation of t-Bid to mitochondria with subsequent oligomerization of Bax and Bak leading to membrane permeabilization; cytochrome c dissociation from the inner mitochondrial membrane; and activation of MPTP, followed by the release of this hemoprotein from the mitochondrial intermembrane space to the cytosol (Figure ​1). HOIP:HOIP_0004356 NCBI-Human-GeneID:581 NCBI-Mouse-GeneID:12028 NCBI-Rat-GeneID:24887 PMID:25339807 BAX(canonical) [mitochondrial disorder (course)] HOIP_0004356 NCBI-Human-GeneID:581 http://www.ncbi.nlm.nih.gov/gene/581 NCBI-Mouse-GeneID:12028 http://www.ncbi.nlm.nih.gov/gene/12028 NCBI-Rat-GeneID:24887 http://www.ncbi.nlm.nih.gov/gene/24887 PMID:25339807 In addition, CL oxidation seems to promote the permeabilization of the outer mitochondrial membrane, probably interacting with Bcl2 family proteins, such as Bax and Bid. Thus, oxidized CL may have a critical role in several steps of the apoptotic process such as: the translocation of t-Bid to mitochondria with subsequent oligomerization of Bax and Bak leading to membrane permeabilization; cytochrome c dissociation from the inner mitochondrial membrane; and activation of MPTP, followed by the release of this hemoprotein from the mitochondrial intermembrane space to the cytosol (Figure ​1). HOIP:HOIP_0004357 NCBI-Human-GeneID:637 NCBI-Mouse-GeneID:12122 NCBI-Rat-GeneID:64625 PMID:25339807 BID(canonical) [mitochondrial disorder (course)] HOIP_0004357 NCBI-Human-GeneID:637 http://www.ncbi.nlm.nih.gov/gene/637 NCBI-Mouse-GeneID:12122 http://www.ncbi.nlm.nih.gov/gene/12122 NCBI-Rat-GeneID:64625 http://www.ncbi.nlm.nih.gov/gene/64625 PMID:25339807 In addition, CL oxidation seems to promote the permeabilization of the outer mitochondrial membrane, probably interacting with Bcl2 family proteins, such as Bax and Bid. Thus, oxidized CL may have a critical role in several steps of the apoptotic process such as: the translocation of t-Bid to mitochondria with subsequent oligomerization of Bax and Bak leading to membrane permeabilization; cytochrome c dissociation from the inner mitochondrial membrane; and activation of MPTP, followed by the release of this hemoprotein from the mitochondrial intermembrane space to the cytosol (Figure ​1). HOIP:HOIP_0004358 ISBN:0071769234 PMID:21145849 valproic acid [mitochondrial disorder (course)] HOIP_0004358 ISBN:0071769234 Types of hepatobiliary injury: Fatty liver: Amiodarone, CCl4, ethanol, fialuridine, tamoxifen, valproic acid. Casarett & Doull's Toxicology: The Basic Science of Poisons, Eighth Edition PMID:21145849 Table 1. HOIP:HOIP_0004359 Any process that activates or decreases the frequency, rate or extent of mitophagy. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 PMID:31649547 nagative regulation of mitophagy [mitochondrial disorder (course)] HOIP_0004359 PMID:31623280 Damaged mitochondria are usually eliminated by autophagy/mitophagy which is attenuated by lipid accumulation. Prevention of autophagy further leads to accumulation of damaged mitochondria that can release inflammatory DAMPs and cytochrome C to promote cell death, and/or exacerbate endoplasmic reticulum (ER) stress. Reduced mitophagy results in the accumulation of severely damaged mitochondria, leading to cell necrosis releasing mitochondrial damage-associated molecular patterns (DAMPs) that can promote liver inflammation and NASH development. PMID:31649547 Wu et al. (2019) have found that impaired mitophagy can accelerate macrophage infiltration in white adipose tissue in high-fat diet–fed mice with FUNDC1 knockout. They have also demonstrated that impaired mitophagy can promote macrophage infiltration to activate MAPK signal pathway and inflammatory response to impair mitochondrial quality control, subsequently causing insulin resistance and hepatic steatosis. HOIP:HOIP_0004360 A fatty acid oxidation process that results in the complete beta oxidation of a fatty acid in the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 mitochondrial fatty acid beta-oxidation [mitochondrial disorder (course)] HOIP_0004360 PMID:23299992 However, several hormonal and metabolic adaptations are set up in order to restrain hepatic fat accumulation, such as increased mitochondrial fatty acid oxidation (mtFAO). Furthermore, enhanced mtFAO without concomitant up‐regulation of the mitochondrial respiratory chain (MRC) activity induces reactive oxygen species (ROS) overproduction within different MRC components upstream of cytochrome c oxidase. HOIP:HOIP_0004361 PMID:21145849 Wikipedia:Amineptine amineptine [mitochondrial disorder (course)] HOIP_0004361 PMID:21145849 Table 1. HOIP:HOIP_0004362 PMID:21145849 ibuprofen [mitochondrial disorder (course)] HOIP_0004362 PMID:21145849 Table 1. HOIP:HOIP_0004363 PMID:21145849 Wikipedia:Panadiplon panadiplon [mitochondrial disorder (course)] HOIP_0004363 PMID:21145849 Table 1. HOIP:HOIP_0004364 PMID:21145849 Wikipedia:Pirprofen pirprofen [mitochondrial disorder (course)] HOIP_0004364 PMID:21145849 Table 1. HOIP:HOIP_0004365 PMID:21145849 Wikipedia:Tacrine tacrine [mitochondrial disorder (course)] HOIP_0004365 PMID:21145849 Table 1. HOIP:HOIP_0004366 Hyperfunction of CYP2E1 gene expression is a subtype of hyperfunction of cytochrome 450 gene expression: A process that performs an excesssive gene expression of CYP2E1. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 hyperfunction of CYP2E1 gene expression [mitochondrial disorder (course)] HOIP_0004366 PMID:23299992 A second mechanism is ROS generation due to CYP2E1 overexpression and reduced levels of mtGSH. Whereas CYP2E1 induction could be secondary to higher levels of glucagon, FAs and KBs, reduced mtGSH could result from higher mitochondrial levels of cholesterol. HOIP:HOIP_0004367 Hyperfunction of glucose biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive glucose biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. hyperfunction of gluconeogenesis [mitochondrial disorder (course)] HOIP_0004367 HOIP:HOIP_0004368 Increasing damaged mitochondria is a subtype of decreasing quantity: A process that changes the amount of damaged mitochondria to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 PMID:31649547 Increasing damaged mitochondria [mitochondrial disorder (course)] HOIP_0004368 PMID:31623280 Prevention of autophagy further leads to accumulation of damaged mitochondria that can release inflammatory DAMPs and cytochrome C to promote cell death, and/or exacerbate endoplasmic reticulum (ER) stress. Reduced mitophagy results in the accumulation of severely damaged mitochondria, leading to cell necrosis releasing mitochondrial damage-associated molecular patterns (DAMPs) that can promote liver inflammation and NASH development. PMID:31649547 Recent study has found that hepatic fatty acid accumulation can cause damaged mitochondria accumulation, which can impair mitochondrial respiratory chain function and fatty acid oxidative degradation. Accumulating evidence has shown that defective hepatic mitochondrial respiration characterized by damaged mitochondria accumulation can impair mitochondrial fatty acid β-oxidation, which sequentially causes various adverse consequences, such as excessive ROS, reduced ATP production, and hepatic fatty acid accumulation. In general, damaged mitochondria accumulation can cause excessive ROS production, which will destroy mitochondrial oxidative phosphorylation and substrate oxidation, thereby inhibiting fatty acid oxidative degradation and accelerating fatty acid accumulation. HOIP:HOIP_0004369 Increasing CPT1 level is a subtype of increasing quantity: A process that changes the amount of CPT1 level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 increasing CPT1 level [mitochondrial disorder (course)] HOIP_0004369 PMID:23299992 For instance, LCFA‐mediated PPARα activation increases the expression of the mitochondrial enzymes CPT1 and medium‐chain acyl‐CoA dehydrogenase (MCAD). Increased mtFAO capacity in ob/ob liver was associated with enhanced CPT activity and/or CPT1 expression, and higher expression of other mtFAO enzymes. HOIP:HOIP_0004370 Hypofunction of anti-oxidative stress is a subtype of hypofunctioning: A process that performs a decreased or insufficient anti-oxidative stress function. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 hypofunction of anti-oxidative stress[mitochondrial disorder (course)] HOIP_0004370 PMID:23299992 Reduced ROS detoxification could also favor oxidative stress. Indeed, several studies showed lower GSH levels in NAFLD, including within the mitochondria. Decreased expression and/or activity of antioxidant enzymes such as GPx and SODs could also occur, in particular at the mitochondrial level. HOIP:HOIP_0004371 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:26571396 Reactome:R-HSA-70263 glucose biosynthesis glucose biosynthetic process gluconeogenesis [mitochondrial disorder (course)] HOIP_0004371 PMID:26571396 Though all tissues support minor activities of anaplerosis and cataplerosis, these pathways are a major function of liver TCA cycle, where anaplerosis and cataplerosis are required for shuttling reducing equivalents (RE) and biosynthetic substrates related to ureagenesis, amino acid synthesis, lipogenesis, and most prominently, gluconeogenesis (GNG) (1) On the whole, the data indicate that increased flux through anaplerotic/cataplerotic pathways not only contributes to dysregulation of downstream nutrients (e.g., glycemia and lipidemia), but also triggers oxidative metabolism and altered antioxidant capacity that contribute to the development of oxidative stress, inflammation, and insulin resistance (Figure 8B and Supplemental Table 2). Reactome:R-HSA-70263 Gluconeogenesis, Homo sapiens HOIP:HOIP_0004372 The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:26571396 PMID:31623280 lipogenesis lipid biosynthetic process [mitochondrial disorder (course)] HOIP_0004372 PMID:26571396 Though all tissues support minor activities of anaplerosis and cataplerosis, these pathways are a major function of liver TCA cycle, where anaplerosis and cataplerosis are required for shuttling reducing equivalents (RE) and biosynthetic substrates related to ureagenesis, amino acid synthesis, lipogenesis, and most prominently, gluconeogenesis (GNG) (1) On the whole, the data indicate that increased flux through anaplerotic/cataplerotic pathways not only contributes to dysregulation of downstream nutrients (e.g., glycemia and lipidemia), but also triggers oxidative metabolism and altered antioxidant capacity that contribute to the development of oxidative stress, inflammation, and insulin resistance (Figure 8B and Supplemental Table 2). PMID:31623280 In addition to its ability to promote de novo lipogenesis and block β-oxidation of fatty acids, fructose consumption seems to cause a drop in ATP and an elevation of uric acid, which can further induce mitochondrial oxidative stress. HOIP:HOIP_0004373 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 PMID:26571396 PMID:31623280 increasing demand for response to oxidative stress [mitochondrial disorder (course)] HOIP_0004373 PMID:23299992 Furthermore, high glucose levels promote ROS overproduction within hepatocytes, thus favoring oxidative stress and mitochondrial dysfunction. Reduced ROS detoxification could also favor oxidative stress. Indeed, several studies showed lower GSH levels in NAFLD, including within the mitochondria. Decreased expression and/or activity of antioxidant enzymes such as GPx and SODs could also occur, in particular at the mitochondrial level. PMID:25339807 MPTP is defined as the sudden increase of mitochondrial inner membrane permeability to low molecular weight solutes (1.5 kDa) in response to many stimuli, including high levels of Ca2+ and oxidant stress. PMID:26571396 Mitochondrial metabolism mediates oxidative stress and inflammation in fatty liver. Second, loss of anaplerosis/cataplerosis via genetic knockdown of phosphoenolpyruvate carboxykinase 1 (Pck1) prevented fatty acid-induced rise in oxidative flux, oxidative stress, and inflammation. Figure 8 Histological data support a role for oxidative metabolism in NAFLD in humans. PMID:31623280 Just like in NASH, oxidative stress, mitochondrial dysfunction, and oxidized mtDNA also contribute to the progression of HCC through influences on inflammation, cell death, and ER stress. Mitochondrial ROS and oxidative stress can disrupt ER function leading to inappropriate release of calcium in liver parenchymal cells. Moreover, in vitro treatment of liver cells with saturated fatty acids (palmitic and stearic acids) reproduces mitochondrial dysfunction found in NASH, including decreasing cellular ATP content and mtDNA-encoded oxidative phosphorylation (OXPHOS) subunit expression, coupled with increased oxidative stress. In addition to its ability to promote de novo lipogenesis and block β-oxidation of fatty acids, fructose consumption seems to cause a drop in ATP and an elevation of uric acid, which can further induce mitochondrial oxidative stress. More precisely, dietary-induced hypercholesterolemia causes oxidative stress, loss of mitochondrial membrane potential, reduction in ATP content, loss of mitochondrial cristae, and hepatic steatosis in mice. Thus, accumulating evidences suggest that cholesterol overload in mitochondria induces redox imbalances leading to oxidative stress and cell death associated with steatohepatitis. Moreover, TNF-α and IL-6 promote iron accumulation, which further fuels oxidative stress-driven cell toxicity and can activate fibrogenesis and carcinogenesis in metabolic syndrome. HOIP:HOIP_0004374 ketone body biosynthetic process is a subtype of generating: A process that synthesizes ketone body resulting in having output (s). This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 ketogenesis ketone body biosynthetic process [mitochondrial disorder (course)] HOIP_0004374 PMID:23299992 During fasting, acetyl‐CoA moieties are mainly used to generate KB by way of ketogenesis. Hepatic ketogenesis was also augmented in mice fed a high‐fat diet (HFD),80 thus suggesting that higher acetyl‐CoA generation by way of mtFAO is followed by efficient KB production. HOIP:HOIP_0004375 Negative regulation of mitochondrial respiratory chain complex I subunit phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex I subunit phosphorylation. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 Negative regulation of mitochondrial respiratory chain complex I subunit phosphorylation [mitochondrial disorder (course)] HOIP_0004375 PMID:24746669 not reported in the liver. The CyclinB1/Cdk1-mediated CI subunit phosphorylation enhances CI activity, whereas deficiency of such phosphorylation in each of the relevant CI subunits results in impairment of CI function. The mutation of Cdk1 consensus motifs severely diminished their phosphorylation. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0004376 A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 cell cycle arrest [mitochondrial disorder (course)] HOIP_0004376 PMID:24746669 not reported in the liver. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0004377 Increasing HMGB1 level is a subtype of increasing quantity: A process that changes the amount of HMGB1 level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Increasing HMGB1 level [mitochondrial disorder (course)] HOIP_0004377 PMID:31623280 Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. HOIP:HOIP_0004378 TLR4 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 4. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 TLR4 signaling [mitochondrial disorder (course)] HOIP_0004378 PMID:31623280 Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. HOIP:HOIP_0004379 Malfunctioning of insulin signaling is a subtype of malfunctioning process: A process that cannot perform insulin signaling appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 PMID:31649547 Malfunctioning of insulin signaling [mitochondrial disorder (course)] HOIP_0004379 PMID:31623280 Recent studies also show that MAMs are important for hepatic insulin signaling, nutrient sensing, and glucose homeostasis. Therefore, disruption of ER-mitochondria contact sites could exacerbate hepatic lipid accumulation and miscommunication between organelles appears to be related to the pathology of hepatic metabolic diseases. PMID:31649547 lipotoxicity and inflammation can interfere with insulin signaling pathway to cause hepatic insulin resistance; As a result, fatty acids especially diacylglycerol and ceramide may excessively accumulate in liver tissue. Previous report has shown that diacylglycerol can activate PKC to impair insulin signal pathway. Moreover, ceramide also activates PKC to suppress protein kinase AKT and further inhibits insulin signal pathway. In conclusion, mitochondrial dysfunction gives rise to hepatic fatty acid accumulation, which ultimately impairs insulin signal pathway and causes hepatic insulin resistance. HOIP:HOIP_0004380 Inflammasome activation is a subtype of activating: A process that changes the activity of the inflammasome to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 inflammasome activation [mitochondrial disorder (course)] HOIP_0004380 PMID:31623280 After binding to TLR9, mitochondrial DAMPs trigger numerous downstream pathways, including nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), the nucleotide binding oligomerization domain (NOD)-like receptor family, pyrin domain containing 3 (NLRP3), and interferon regulatory factor-dependent type 1 to promote inflammation. HOIP:HOIP_0004381 A tumor necrosis factor that is encoded in the genome of human. NCBI-Human-GeneID:7124 NCBI-Mouse-GeneID:21926 NCBI-Rat-GeneID:24835 TNFΑ (canonical)[mitochondrial disorder (course)] HOIP_0004381 NCBI-Human-GeneID:7124 http://www.ncbi.nlm.nih.gov/gene/7124 NCBI-Mouse-GeneID:21926 http://www.ncbi.nlm.nih.gov/gene/21926 NCBI-Rat-GeneID:24835 http://www.ncbi.nlm.nih.gov/gene/24835 HOIP:HOIP_0004382 HIF1A activation is a subtype of molecular activation: A process that changes the activity of the HIF1A (hypoxia inducible factor 1 subunit alpha) to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 HIF1A activation [mitochondrial disorder (course)] HOIP_0004382 PMID:23299992 TNF‐α is able to impair MRC activity, possibly by inducing hypoxia inducible factor‐1α (HIF‐1α) and mtDNA damage. PMID:25339807 TNF-α may also alter electron transport chain (ETC) by inducing hypoxia-inducible factor -1α and mtDNA damage. HOIP:HOIP_0004383 iNOS production is a subtype of protein production: A process that makes existent of iNOS ( inducible nitric oxide synthase) due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 inducible nitric oxide synthase production [mitochondrial disorder (course)] HOIP_0004383 PMID:23299992 NAFLD has been associated with higher hepatic expression of the inducible nitric oxide (NO) synthase (iNOS), mainly as a consequence of tumor necrosis factor‐α (TNF‐α) overproduction by the Kupffer cells. NO can readily react with the superoxide anion, thus generating the RNS peroxynitrite, which has deleterious effects on mitochondrial function and genome. PMID:25339807 NO and other RNS are increased in response to chronic alcohol consumption through induction of iNOS. HOIP:HOIP_0004384 HOR O[*] alcohol [mitochondrial disorder (course)] HOIP_0004384 HOIP:HOIP_0004385 NCBI-Human-GeneID:3569 NCBI-Mouse-GeneID:16193 NCBI-Rat-GeneID:24498 PMID:23299992 IL-6(canonical) [mitochondrial disorder (course)] HOIP_0004385 NCBI-Human-GeneID:3569 http://www.ncbi.nlm.nih.gov/gene/3569 NCBI-Mouse-GeneID:16193 http://www.ncbi.nlm.nih.gov/gene/16193 NCBI-Rat-GeneID:24498 http://www.ncbi.nlm.nih.gov/gene/24498 PMID:23299992 Numerous studies showed increased expression of PPARα in fatty liver. Different cues such as FAs, leptin, and IL6 could activate PPARα and its target genes involved in mtFAO (CPT1, MCAD), peroxisomal FAO (acyl‐CoA oxidase), and VLDL production (microsomal triglyceride transfer protein). mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). HOIP:HOIP_0004386 PMID:21145849 Wikipedia:Didanosine ddI didanosine [mitochondrial disorder (course)] HOIP_0004386 PMID:21145849 Table 1. HOIP:HOIP_0004387 PMID:21145849 Wikipedia:Zidovudine AZT zidovudine [mitochondrial disorder (course)] HOIP_0004387 PMID:21145849 Table 1. HOIP:HOIP_0004388 PMID:21145849 Wikipedia:Stavudine stavudine [mitochondrial disorder (course)] HOIP_0004388 PMID:21145849 Table 1. HOIP:HOIP_0004389 PMID:21145849 Wikipedia:Fialuridine FIAU fialuridine [mitochondrial disorder (course)] HOIP_0004389 PMID:21145849 Table 1. HOIP:HOIP_0004390 Hypofunction of PPARGC1A gene expression is a subtype of hypofunction of transcription, DNA-templated: A process that performs a decreased or insufficient PPARGC1A gene expression. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:31623280 Hypofunction of PPARGC1A gene expression [mitochondrial disorder (course)] HOIP_0004390 PMID:23299992 Finally, higher FOXO1 activity and oxidative stress could be involved, by way of impaired mitochondrial biogenesis. Indeed, FoxO1 activation is able to reduce the content of different MRC polypeptides, possibly by decreasing heme synthesis and impairing PGC1α activity. Interestingly, oxidative stress and inflammation are able to reduce PGC1α expression. PMID:31623280 Decreased mitochondrial biogenesis is associated with a reduction of PGC-1α, transcription factor A, mitochondrial (TFAM), or PPARs in fatty livers. HOIP:HOIP_0004393 Increasing production amount of reactive aldehyde is a subtype of increasing quantity: A process that changes the production amount of reactive aldehyde to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 increasing production amount of reactive aldehyde [mitochondrial disorder (course)] HOIP_0004393 PMID:23299992 Several MRC complexes including COX are sensitive to ROS and RNS. In addition, COX can be inhibited by low levels of NO and inactivated by 4‐hydroxynonenal (4‐HNE), a reactive aldehyde generated during lipid peroxidation. PMID:25339807 These compounds may undergo fragmentation to produce several reactive intermediates, among them, malondialdehyde and the most reactive 4-hydroxy-trans-2-nonenal. These two by-products of lipid peroxidation have been shown to interact with and inactivate ETC components, including cytochrome c oxidase, by forming adducts with this enzyme[, contributing to triggering mitochondrial dysfunction in NASH. HOIP:HOIP_0004397 Iron accumulation is a subtype of accumulation of substances in a biological object: A process that keeps iron in an organism, tissue, organelle, or cell. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Iron accumulation [mitochondrial disorder (course)] HOIP_0004397 PMID:31623280 Moreover, TNF-α and IL-6 promote iron accumulation, which further fuels oxidative stress-driven cell toxicity and can activate fibrogenesis and carcinogenesis in metabolic syndrome. HOIP:HOIP_0004398 Increasing ACSL1 level is a subtype of increasing quantity: A process that changes the amount of ACSL1 level to be higher. Increasing ACSL1 level HOIP_0004398 HOIP:HOIP_0004399 NCBI-Human-GeneID:2180 NCBI-Mouse-GeneID:14081 NCBI-Rat-GeneID:25288 ACSL1 (mol) HOIP_0004399 NCBI-Human-GeneID:2180 http://www.ncbi.nlm.nih.gov/gene/2180 NCBI-Mouse-GeneID:14081 http://www.ncbi.nlm.nih.gov/gene/14081 NCBI-Rat-GeneID:25288 http://www.ncbi.nlm.nih.gov/gene/25288 HOIP:HOIP_0004405 Increasing ACSL4 level is a subtype of increasing quantity: A process that changes the amount of ACSL4 level to be higher. Increasing ACSL4 level HOIP_0004405 HOIP:HOIP_0004406 NCBI-Human-GeneID:2182 NCBI-Mouse-GeneID:50790 NCBI-Rat-GeneID:113976 ACSL4 (mol) HOIP_0004406 NCBI-Human-GeneID:2182 http://www.ncbi.nlm.nih.gov/gene/2182 NCBI-Mouse-GeneID:50790 http://www.ncbi.nlm.nih.gov/gene/50790 NCBI-Rat-GeneID:113976 http://www.ncbi.nlm.nih.gov/gene/113976 HOIP:HOIP_0004411 Increasing AGGF1 level is a subtype of increasing quantity: A process that changes the amount of AGGF1 level to be higher. Increasing AGGF1 level HOIP_0004411 HOIP:HOIP_0004416 Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31649547 negative regulation of AKT signaling [mitochondrial disorder (course)] HOIP_0004416 PMID:31649547 Moreover, ceramide also activates PKC to suppress protein kinase AKT and further inhibits insulin signal pathway. HOIP:HOIP_0004423 A series of molecular signals mediated by APC (Activated protein C). APC signal transduction pathway HOIP_0004423 HOIP:HOIP_0004424 APC signaling is a process that a signal is transmitted by APC. APC signaling HOIP_0004424 HOIP:HOIP_0004425 Any process that stops, prevents, or reduces the frequency, rate or extent of APC signaling, a series of reactions mediated by APC. negative regulation of APC signaling HOIP_0004425 HOIP:HOIP_0004428 ATF4 inactivation is a subtype of molecular inactivation: A process that changes the activity of the ATF4 (activating transcription factor 4) to be lower. ATF4 inactivation HOIP_0004428 HOIP:HOIP_0004435 Negative regulation of ATP transport is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ATP into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Negative regulation of ATP transpot HOIP_0004435 HOIP:HOIP_0004436 Negative regulation of ATP transport is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ATP into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 Negative regulation of ATP transport [mitochondrial disorder (course)] HOIP_0004436 PMID:25339807 Similarly, dimeric organization of ADP/ATP carrier and other ADP/ATP carrier-containing supercomplexes are destabilized in CL-deficient mitochondria. HOIP:HOIP_0004437 Increasing BCL-2 level is a subtype of increasing quantity: A process that changes the amount of BCL-2 level to be higher. Increasing BCL-2 level HOIP_0004437 HOIP:HOIP_0004439 C9ORF72 inactivation is a subtype of molecular inactivation: A process that changes the activity of the C9ORF72 (C9orf72-SMCR8 complex subunit) to be lower. C9ORF72 inactivation HOIP_0004439 HOIP:HOIP_0004440 C9ORF72 inactivation is a subtype of molecular inactivation: A process that changes the activity of the C9ORF72 (C9orf72-SMCR8 complex subunit) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:27151080 C9ORF72 inactivation [mitochondrial disorder (course)] HOIP_0004440 PMID:27151080 not reported in the liver. We found evidence of autophagy/mitophagy in dynamic equilibrium with the biogenesis of novel mitochondria, particularly in mutant C9ORF72 fibroblasts where an increase of mitochondrial DNA content and mass, and of PGC1-α protein was observed. The autophagic process is also partially activated in mC9ORF72 as evidenced by electron microscopy data and p62 protein down-regulation. We observed a significant depolarization of mitochondria in mTDP-43 fibroblasts, where the median MMP value was approximately 80 % compared to control group, whereas in mC9ORF72 fibroblasts the median MMP value significantly increased to 129 %, indicating hyperpolarized mitochondria (Fig. 2a). We found a consistent and significant increase of mitochondrial ROS along with a parallel increase of total cellular ROS levels specifically in mC9ORF72 cells compared to both healthy control and mTDP-43 fibroblasts (Fig. 2e-​-ff). HOIP:HOIP_0004441 NCBI-Human-GeneID:203228 PMID:27151080 C9orf72_inactivated (human) [mitochondrial damage] HOIP_0004441 NCBI-Human-GeneID:203228 http://www.ncbi.nlm.nih.gov/gene/203228 PMID:27151080 not reported in the liver. In the present study we showed that mutations in TARDBP and C9ORF72 genes, associated to defects in RNA metabolism in ALS and FTD neurodegenerative diseases, affect mitochondria functionality by altering several morphological and bioenergetics parameters in a gene-specific manner. HOIP:HOIP_0004442 Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:27151080 positive regulation of autophagy [mitochondrial disorder (course)] HOIP_0004442 PMID:27151080 not reported in the liver. We found evidence of autophagy/mitophagy in dynamic equilibrium with the biogenesis of novel mitochondria, particularly in mutant C9ORF72 fibroblasts where an increase of mitochondrial DNA content and mass, and of PGC1-α protein was observed. The autophagic process is also partially activated in mC9ORF72 as evidenced by electron microscopy data and p62 protein down-regulation. HOIP:HOIP_0004443 Any process that activates or increases the frequency, rate or extent of mitophagy. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:27151080 positive regulation of mitophagy [mitochondrial disorder (course)] HOIP_0004443 PMID:27151080 not reported in the liver. We found evidence of autophagy/mitophagy in dynamic equilibrium with the biogenesis of novel mitochondria, particularly in mutant C9ORF72 fibroblasts where an increase of mitochondrial DNA content and mass, and of PGC1-α protein was observed. These results, together with electronic microscopy data showing few autophagic/mitophagic vacuoles in both mutant fibroblast groups (Fig. 1d), suggest an early activation of the autophagic process. HOIP:HOIP_0004444 Dysregulation of mitochondrion organization is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of mitochondrion organization appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:27151080 Dysregulation of mitochondrion organization HOIP_0004444 PMID:27151080 not reported in the liver. These results suggest that an altered balance of fission and fusion processes may account for the mitochondria morphology changes observed in mTDP-43 and mC9ORF72 fibroblasts. HOIP:HOIP_0004445 Increasing mitochondrial membrane potential is a subtype of increasing membrane potential: A process that changes the electrical potential of a mitochondrial membrane to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:27151080 Increasing mitochondrial membrane potential [mitochondrial disorder (course)] HOIP_0004445 PMID:27151080 not reported in the liver. We observed a significant depolarization of mitochondria in mTDP-43 fibroblasts, where the median MMP value was approximately 80 % compared to control group, whereas in mC9ORF72 fibroblasts the median MMP value significantly increased to 129 %, indicating hyperpolarized mitochondria (Fig. 2a). The increased oxygen consumption rate may reflect an efficient and tightly coupled ETC activity in mC9ORF72 fibroblasts, thus accounting for the observed higher ATP content, while the increased MMP may favour electron slippage and trigger ROS production as sustained by our experimental data. HOIP:HOIP_0004446 CAR activation is a subtype of molecular activation: A process that changes the activity of the CAR (constitutive active/androstane receptor) to be higher. CAR activation HOIP_0004446 HOIP:HOIP_0004451 CCL2 signaling is a process that a signal is transmitted by CCL2. CCL2 signaling HOIP_0004451 HOIP:HOIP_0004456 Increasing CCND1 level is a subtype of increasing quantity: A process that changes the amount of CCND1 level to be higher. Increasing CCND1 level HOIP_0004456 HOIP:HOIP_0004460 CDK1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the CDK1 (cyclin dependent kinase 1) to be lower. CDK1 inactivation HOIP_0004460 HOIP:HOIP_0004461 CDK1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the CDK1 (cyclin dependent kinase 1) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 CDK1 inactivation [mitochondrial disorder (course)] HOIP_0004461 PMID:24746669 not reported in the liver. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0004462 NCBI-Human-GeneID:983 PMID:24746669 CDK1 - inactive form (human) [mitochondrial damage] HOIP_0004462 NCBI-Human-GeneID:983 http://www.ncbi.nlm.nih.gov/gene/983 PMID:24746669 As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0004463 Increasing CDK2 level is a subtype of increasing quantity: A process that changes the amount of CDK2 level to be higher. Increasing CDK2 level HOIP_0004463 HOIP:HOIP_0004466 CDT1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the CDT1 (chromatin licensing and DNA replication factor 1) to be lower. CDT1 inactivation HOIP_0004466 HOIP:HOIP_0004467 NCBI-Human-GeneID:81620 NCBI-Mouse-GeneID:67177 NCBI-Rat-GeneID:292071 CDT1 (mol) HOIP_0004467 NCBI-Human-GeneID:81620 http://www.ncbi.nlm.nih.gov/gene/81620 NCBI-Mouse-GeneID:67177 http://www.ncbi.nlm.nih.gov/gene/67177 NCBI-Rat-GeneID:292071 http://www.ncbi.nlm.nih.gov/gene/292071 HOIP:HOIP_0004471 Increasing COX-2 level is a subtype of increasing quantity: A process that changes the amount of COX-2 level to be higher. Increasing COX-2 level HOIP_0004471 HOIP:HOIP_0004473 Increasing CPT1 level is a subtype of increasing quantity: A process that changes the amount of CPT1 level to be higher. increasing CPT1 level HOIP_0004473 HOIP:HOIP_0004474 NCBI-Human-GeneID:1374 NCBI-Mouse-GeneID:12894 NCBI-Rat-GeneID:25757 PMID:23299992 CPT1(canonical) [mitochondrial disorder (course)] HOIP_0004474 NCBI-Human-GeneID:1374 http://www.ncbi.nlm.nih.gov/gene/1374 NCBI-Mouse-GeneID:12894 https://www.ncbi.nlm.nih.gov/gene/12894 NCBI-Rat-GeneID:25757 https://www.ncbi.nlm.nih.gov/gene/25757 PMID:23299992 For instance, LCFA‐mediated PPARα activation increases the expression of the mitochondrial enzymes CPT1 and medium‐chain acyl‐CoA dehydrogenase (MCAD). Increased mtFAO capacity in ob/ob liver was associated with enhanced CPT activity and/or CPT1 expression, and higher expression of other mtFAO enzymes. HOIP:HOIP_0004481 CXCR3 signaling is a process that a signal is transmitted by CXCR3. CXCR3 signaling HOIP_0004481 HOIP:HOIP_0004484 A series of molecular signals mediated by CXCR3 (CXC chemokine receptor 3). CXCR3 signal transduction pathway HOIP_0004484 HOIP:HOIP_0004485 Increasing CXCR4 level is a subtype of increasing quantity: A process that changes the amount of CXCR4 level to be higher. Increasing CXCR4 level HOIP_0004485 HOIP:HOIP_0004486 NCBI-Human-GeneID:7852 NCBI-Mouse-GeneID:12767 NCBI-Rat-GeneID:60628 CXCR4 (mol) HOIP_0004486 NCBI-Human-GeneID:7852 http://www.ncbi.nlm.nih.gov/gene/7852 NCBI-Mouse-GeneID:12767 http://www.ncbi.nlm.nih.gov/gene/12767 NCBI-Rat-GeneID:60628 http://www.ncbi.nlm.nih.gov/gene/60628 HOIP:HOIP_0004493 Hyperfunction of CYP2E1 gene expression is a subtype of hyperfunction of cytochrome 450 gene expression: A process that performs an excesssive gene expression of CYP2E1. Hyperfunction of CYP2E1 gene expression HOIP_0004493 HOIP:HOIP_0004494 A series of molecular signals mediated by Cx (Connexin). Connexin signal transduction pathway HOIP_0004494 HOIP:HOIP_0004495 Connexin signaling is a process that a signal is transmitted by connexin. connexin signaling HOIP_0004495 HOIP:HOIP_0004496 Any process that stops, prevents, or reduces the frequency, rate or extent of connexin signaling, a series of reactions mediated by connexin. negative regulation of connexin signaling HOIP_0004496 HOIP:HOIP_0004499 Removing damaged DNA stress is a subtype of removing damaged object: A process that takes a damaged DNA from an organism or tissue. Removing damaged DNA stress HOIP_0004499 HOIP:HOIP_0004500 The process of a structure formation, in n which a chemical is attatched to a segement of DNA. formation of DNA adducts HOIP_0004500 HOIP:HOIP_0004515 Hyperfunction of DNA biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive DNA biosynthesis. Hyperfunction of DNA biosynthesis HOIP_0004515 HOIP:HOIP_0004520 Increasing DNMT1 level is a subtype of increasing quantity: A process that changes the amount of DNMT1 level to be higher. Increasing DNMT1 level HOIP_0004520 HOIP:HOIP_0004521 NCBI-Human-GeneID:1786 NCBI-Mouse-GeneID:13433 NCBI-Rat-GeneID:84350 DNA methyltransferase 1 DNMT1 (mol) HOIP_0004521 NCBI-Human-GeneID:1786 http://www.ncbi.nlm.nih.gov/gene/1786 NCBI-Mouse-GeneID:13433 https://www.ncbi.nlm.nih.gov/gene/13433 NCBI-Rat-GeneID:84350 https://www.ncbi.nlm.nih.gov/gene/84350 HOIP:HOIP_0004524 Increasing DPYD level is a subtype of increasing quantity: A process that changes the amount of DPYD level to be higher. Increasing DPYD level HOIP_0004524 HOIP:HOIP_0004530 A series of molecular signals mediated by EPCR (Endothelial protein C receptor). EPCR signal transduction pathway HOIP_0004530 HOIP:HOIP_0004531 EPCR signaling is a process that a signal is transmitted by EPCR. EPCR signaling HOIP_0004531 HOIP:HOIP_0004532 Any process that stops, prevents, or reduces the frequency, rate or extent of EPCR signaling, a series of reactions mediated by EPCR. negative regulation of EPCR signaling HOIP_0004532 HOIP:HOIP_0004534 A series of molecular signals mediated by ERK (extracellular receptor kinase). ERK signal transduction pathway HOIP_0004534 HOIP:HOIP_0004535 ERK signaling is a process that a signal is transmitted by ERK. ERK signaling HOIP_0004535 HOIP:HOIP_0004539 Grp78 signaling is a process that a signal is transmitted by Grp78. Grp78 signaling HOIP_0004539 HOIP:HOIP_0004540 A series of molecular signals mediated by Grp78 (Glucose-regulated protein 78). Grp78 signal transduction pathway HOIP_0004540 HOIP:HOIP_0004544 A series of molecular signals mediated by FAK (focal adhesion kinase). FAK signal transduction pathway HOIP_0004544 HOIP:HOIP_0004545 FAK signaling is a process that a signal is transmitted by FAK. FAK signaling HOIP_0004545 HOIP:HOIP_0004548 FAS signaling is a process that a signal is transmitted by FAS. FAS signaling HOIP_0004548 HOIP:HOIP_0004549 FAS signaling is a process that a signal is transmitted by FAS. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 FAS signaling [mitochondrial disorder (course)] HOIP_0004549 PMID:31623280 Moreover, mitochondrial-free cholesterol sensitizes liver cells to TNFα- and Fas-mediated steatohepatitis and causes mitochondrial-reduced glutathione (mGSH) depletion, which is also reported in animal models and patients with NASH. HOIP:HOIP_0004550 Increasing FGF21 level is a subtype of increasing quantity: A process that changes the amount of FGF21 level to be higher. increasing FGF21 level HOIP_0004550 HOIP:HOIP_0004551 Increasing FGF21 level is a subtype of increasing quantity: A process that changes the amount of FGF21 level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 increasing FGF21 level [mitochondrial disorder (course)] HOIP_0004551 PMID:23299992 mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). HOIP:HOIP_0004552 NCBI-Human-GeneID:26291 NCBI-Mouse-GeneID:56636 NCBI-Rat-GeneID:170580 PMID:23299992 FGF21(canonical) [mitochondrial disorder (course)] HOIP_0004552 NCBI-Human-GeneID:26291 http://www.ncbi.nlm.nih.gov/gene/26291 NCBI-Mouse-GeneID:56636 https://www.ncbi.nlm.nih.gov/gene/56636 NCBI-Rat-GeneID:170580 https://www.ncbi.nlm.nih.gov/gene/170580 PMID:23299992 mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). HOIP:HOIP_0004553 A series of molecular signals mediated by FGF2. FGF2 signal transduction pathway HOIP_0004553 HOIP:HOIP_0004554 FGF2 signaling is a process that a signal is transmitted by FGF2. FGF2 signaling HOIP_0004554 HOIP:HOIP_0004558 FOXO1 activation is a subtype of molecular activation: A process that changes the activity of the FOXO1 (forkhead box O1) to be higher. FOXO1 activation HOIP_0004558 HOIP:HOIP_0004559 FOXO1 activation is a subtype of molecular activation: A process that changes the activity of the FOXO1 (forkhead box O1) to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 FOXO1 activation [mitochondrial disorder (course)] HOIP_0004559 PMID:23299992 Finally, higher FOXO1 activity and oxidative stress could be involved, by way of impaired mitochondrial biogenesis. Indeed, FoxO1 activation is able to reduce the content of different MRC polypeptides, possibly by decreasing heme synthesis and impairing PGC1α activity. Reduced PGC1α activity could also be secondary to oxidative stress and inflammation, as previously mentioned (Fig. 4). Interestingly, oxidative stress and inflammation are able to reduce PGC1α expression. HOIP:HOIP_0004561 Hypofunction of heme biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient heme biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 Hypofunction of heme biosynthesis [mitochondrial disorder (course)] HOIP_0004561 PMID:23299992 Finally, higher FOXO1 activity and oxidative stress could be involved, by way of impaired mitochondrial biogenesis. Indeed, FoxO1 activation is able to reduce the content of different MRC polypeptides, possibly by decreasing heme synthesis and impairing PGC1α activity. Reduced PGC1α activity could also be secondary to oxidative stress and inflammation, as previously mentioned (Fig. 4). HOIP:HOIP_0004562 frizzled class receptor FZD HOIP_0004562 HOIP:HOIP_0004563 G protein-coupled receptors GPCR HOIP_0004563 HOIP:HOIP_0004565 NCBI-Human-GeneID:10912 NCBI-Mouse-GeneID:23882 NCBI-Rat-GeneID:291005 GADD45G (mol) HOIP_0004565 NCBI-Human-GeneID:10912 http://www.ncbi.nlm.nih.gov/gene/10912 NCBI-Mouse-GeneID:23882 http://www.ncbi.nlm.nih.gov/gene/23882 NCBI-Rat-GeneID:291005 http://www.ncbi.nlm.nih.gov/gene/291005 HOIP:HOIP_0004569 Increasing GDF15 level is a subtype of increasing quantity: A process that changes the amount of GDF15 level to be higher. Increasing GDF15 level HOIP_0004569 HOIP:HOIP_0004572 Negative regulation of gap-junctional intercellular communication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of gap-junctional intercellular communication. negative regulation of GJIC negative regulation of gap-junctional intercellular communication HOIP_0004572 HOIP:HOIP_0004575 A series of molecular signals mediated by GSK3beta (glycogen synthase kinase 3 beta). GSK3beta signal transduction pathway HOIP_0004575 HOIP:HOIP_0004576 GSK3beta signaling is a process that a signal is transmitted by GSK3beta. GSK3beta signaling HOIP_0004576 HOIP:HOIP_0004578 NCBI-Human-GeneID:3309 NCBI-Mouse-GeneID:14828 NCBI-Rat-GeneID:25617 PMID:28240761 BIP [ER stress] HEL-S-89n [ER stress] HSPA5 [ER stress] Heat Shock Protein Family A (Hsp70) Member 5 [ER stress] MIF2 [ER stress] GRP78 (canonical)[hepatocarcinogenesis] HOIP_0004578 NCBI-Human-GeneID:3309 http://www.ncbi.nlm.nih.gov/gene/3309 NCBI-Mouse-GeneID:14828 http://www.ncbi.nlm.nih.gov/gene/14828 NCBI-Rat-GeneID:25617 http://www.ncbi.nlm.nih.gov/gene/25617 PMID:28240761 It has been also shown that the overexpression of IP-10, which induced by liver graft injury, may lead to cisplatin resistance via ATF6/Grp78 ER stress signaling pathway in HCC; IP-10 neutralizing antibody could be a potential adjuvant therapy to sensitize HCC-cisplatin treatment. HOIP:HOIP_0004580 Increasing HBEGF level is a subtype of increasing quantity: A process that changes the amount of HBEGF level to be higher. Increasing HBEGF level HOIP_0004580 HOIP:HOIP_0004581 NCBI-Human-GeneID:1839 NCBI-Mouse-GeneID:15200 NCBI-Rat-GeneID:25433 HBEGF (mol) HOIP_0004581 NCBI-Human-GeneID:1839 http://www.ncbi.nlm.nih.gov/gene/1839 NCBI-Mouse-GeneID:15200 http://www.ncbi.nlm.nih.gov/gene/15200 NCBI-Rat-GeneID:25433 http://www.ncbi.nlm.nih.gov/gene/25433 HOIP:HOIP_0004599 HGFR signaling is a process that a signal is transmitted by HGFR. HGFR signaling HOIP_0004599 HOIP:HOIP_0004604 NCBI-Human-GeneID:3082 NCBI-Mouse-GeneID:15234 NCBI-Rat-GeneID:24446 HGF (mol) HOIP_0004604 NCBI-Human-GeneID:3082 http://www.ncbi.nlm.nih.gov/gene/3082 NCBI-Mouse-GeneID:15234 http://www.ncbi.nlm.nih.gov/gene/15234 NCBI-Rat-GeneID:24446 http://www.ncbi.nlm.nih.gov/gene/24446 HOIP:HOIP_0004605 Increasing HGF level is a subtype of increasing quantity: A process that changes the amount of HGF level to be higher. Increasing HGF level HOIP_0004605 HOIP:HOIP_0004607 HHIP inactivation is a subtype of molecular inactivation: A process that changes the activity of the HHIP (hedgehog interacting protein) to be lower. HHIP inactivation HOIP_0004607 HOIP:HOIP_0004608 NCBI-Human-GeneID:64399 NCBI-Mouse-GeneID:15245 NCBI-Rat-GeneID:291936 hedgehog interacting protein HHIP (mol) HOIP_0004608 NCBI-Human-GeneID:64399 http://www.ncbi.nlm.nih.gov/gene/64399 NCBI-Mouse-GeneID:15245 https://www.ncbi.nlm.nih.gov/gene/15245 NCBI-Rat-GeneID:291936 https://www.ncbi.nlm.nih.gov/gene/291936 HOIP:HOIP_0004612 HIF1A activation is a subtype of molecular activation: A process that changes the activity of the HIF1A (hypoxia inducible factor 1 subunit alpha) to be higher. HIF1A activation HOIP_0004612 HOIP:HOIP_0004614 NCBI-Human-GeneID:3091 NCBI-Mouse-GeneID:15251 NCBI-Rat-GeneID:29560 PMID:23299992 PMID:25339807 HIF1A - activation state (canonical)[mitochondrial disorder (course)] HOIP_0004614 NCBI-Human-GeneID:3091 http://www.ncbi.nlm.nih.gov/gene/3091 NCBI-Mouse-GeneID:15251 http://www.ncbi.nlm.nih.gov/gene/15251 NCBI-Rat-GeneID:29560 http://www.ncbi.nlm.nih.gov/gene/29560 PMID:23299992 TNF‐α is able to impair MRC activity, possibly by inducing hypoxia inducible factor‐1α (HIF‐1α) and mtDNA damage. PMID:25339807 TNF-α may also alter electron transport chain (ETC) by inducing hypoxia-inducible factor -1α and mtDNA damage. HOIP:HOIP_0004615 Increasing HILPDA level is a subtype of increasing quantity: A process that changes the amount of HILPDA level to be higher. Increasing HILPDA level HOIP_0004615 HOIP:HOIP_0004618 Increasing HMGB1 level is a subtype of increasing quantity: A process that changes the amount of HMGB1 level to be higher. Increasing HMGB1 level HOIP_0004618 HOIP:HOIP_0004619 NCBI-Human-GeneID:3146 NCBI-Mouse-GeneID:15289 PMID:31623280 HMGB1 (human) [mitochondrial disorder (course)] HOIP_0004619 NCBI-Human-GeneID:3146 http://www.ncbi.nlm.nih.gov/gene/3146 NCBI-Mouse-GeneID:15289 http://www.ncbi.nlm.nih.gov/gene/15289 PMID:31623280 Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. HOIP:HOIP_0004620 HNF4A inactivation is a subtype of molecular inactivation: A process that changes the activity of the HNF4A (hepatocyte nuclear factor 4 alpha) to be lower. HNF4A inactivation HOIP_0004620 HOIP:HOIP_0004621 NCBI-Human-GeneID:3172 NCBI-Mouse-GeneID:15378 NCBI-Rat-GeneID:25735 HNF4A (mol) HOIP_0004621 NCBI-Human-GeneID:3172 http://www.ncbi.nlm.nih.gov/gene/3172 NCBI-Mouse-GeneID:15378 http://www.ncbi.nlm.nih.gov/gene/15378 NCBI-Rat-GeneID:25735 http://www.ncbi.nlm.nih.gov/gene/25735 HOIP:HOIP_0004623 NCBI-Human-GeneID:728655 hepatocellular carcinoma up-regulated long non-coding RNA HULC HOIP_0004623 NCBI-Human-GeneID:728655 https://www.ncbi.nlm.nih.gov/gene/728655 HOIP:HOIP_0004624 Increasing HULC level is a subtype of increasing quantity: A process that changes the amount of HULC level to be higher. Increasing HULC level HOIP_0004624 HOIP:HOIP_0004628 A series of molecular signals mediated by Hedgehog (HH). Hedgehog signal transduction pathway HOIP_0004628 HOIP:HOIP_0004629 Hedgehog signaling is a process that a signal is transmitted by Hedgehog. Hedgehog signaling HOIP_0004629 HOIP:HOIP_0004635 A series of molecular signals mediated by Hippo (Mst1 and Mst2 in mammals). Hippo signal transduction pathway HOIP_0004635 HOIP:HOIP_0004637 Hippo signaling is a process that a signal is transmitted by Hippo. Hippo signaling HOIP_0004637 HOIP:HOIP_0004641 UHRF1 production is a subtype of protein production: A process that makes existent of a UHRF1 protein due to biosynthesis or secretion resulting in an increase in its levels. UHRF1 production HOIP_0004641 HOIP:HOIP_0004642 IFN alpha inactivation is a subtype of molecular inactivation: A process that changes the activity of the IFN alpha (interferon alpha) to be lower. IFN alpha inactivation HOIP_0004642 HOIP:HOIP_0004644 IGFBP3 inactivation is a subtype of molecular inactivation: A process that changes the activity of the IGFBP3 (insulin-like growth factor-binding protein 3) to be lower. IGFBP3 inactivation HOIP_0004644 HOIP:HOIP_0004645 NCBI-Human-GeneID:3486 NCBI-Mouse-GeneID:16009 NCBI-Rat-GeneID:24484 insulin like growth factor binding protein 3 IGFBP3 (mol) HOIP_0004645 NCBI-Human-GeneID:3486 http://www.ncbi.nlm.nih.gov/gene/3486 NCBI-Mouse-GeneID:16009 https://www.ncbi.nlm.nih.gov/gene/16009 NCBI-Rat-GeneID:24484 https://www.ncbi.nlm.nih.gov/gene/24484 HOIP:HOIP_0004648 NCBI-Human-GeneID:3553 NCBI-Mouse-GeneID:16176 NCBI-Rat-GeneID:24494 PMID:31623280 IL-1B(canonical) [mitochondrial disorder (course)] HOIP_0004648 NCBI-Human-GeneID:3553 http://www.ncbi.nlm.nih.gov/gene/3553 NCBI-Mouse-GeneID:16176 http://www.ncbi.nlm.nih.gov/gene/16176 NCBI-Rat-GeneID:24494 http://www.ncbi.nlm.nih.gov/gene/24494 PMID:31623280 Mitochondrial ROS (mtROS) and lipid peroxidation also trigger proinflammatory cytokines such as interleukin 6 (IL-6), tumor necrosis factor α (TNF-α), interleukin 1 beta (IL-1β), which are critical mediators of inflammation in NASH. HOIP:HOIP_0004649 IL-6 inactivation is a subtype of molecular inactivation: A process that changes the activity of the IL-6 (interleukin 6) to be lower. IL-6 inactivation HOIP_0004649 HOIP:HOIP_0004657 IL1 signaling is a process that a signal is transmitted by the cytokine IL1. IL1 signaling HOIP_0004657 HOIP:HOIP_0004662 A series of molecular signals mediated by IP-10 (Interferon Gamma Induced Protein 10kDa). IP-10 signal transduction pathway HOIP_0004662 HOIP:HOIP_0004663 IP-10 signaling is a process that a signal is transmitted by IP-10. IP-10 signaling HOIP_0004663 HOIP:HOIP_0004666 A series of molecular signals mediated by JAK (Janus kinase). JAK signal transduction pathway HOIP_0004666 HOIP:HOIP_0004667 JAK signaling is a process that a signal is transmitted by the JAK (Janus kinase) . JAK signaling HOIP_0004667 HOIP:HOIP_0004668 Increasing JUN level is a subtype of increasing quantity: A process that changes the amount of JUN level to be higher. Increasing JUN level HOIP_0004668 HOIP:HOIP_0004671 The process of removing one or more methyl groups from JUN gene promoter. JUN gene promoter demethylation HOIP_0004671 HOIP:HOIP_0004672 The process of removing one or more methyl groups from proto-oncogene promoter. proto-oncogene promoter demethylation HOIP_0004672 HOIP:HOIP_0004677 KIAA0101 inactivation is a subtype of molecular inactivation: A process that changes the activity of the KIAA0101 (PCLAF, PCNA clamp associated factor) to be lower. KIAA0101 inactivation HOIP_0004677 HOIP:HOIP_0004680 Increasing KIAA0101 level is a subtype of increasing quantity: A process that changes the amount of KIAA0101 level to be higher. Increasing KIAA0101 level HOIP_0004680 HOIP:HOIP_0004685 NCBI-Human-GeneID:753 NCBI-Mouse-GeneID:52662 NCBI-Rat-GeneID:679578 LDLRAD4 (mol) HOIP_0004685 NCBI-Human-GeneID:753 http://www.ncbi.nlm.nih.gov/gene/753 NCBI-Mouse-GeneID:52662 http://www.ncbi.nlm.nih.gov/gene/52662 NCBI-Rat-GeneID:679578 http://www.ncbi.nlm.nih.gov/gene/679578 HOIP:HOIP_0004688 The covalent transfer of a methyl group to LDLRAD4 gene promoter. LDLRAD4 gene promoter methylation HOIP_0004688 HOIP:HOIP_0004690 Increasing MIR135A level is a subtype of increasing quantity: A process that changes the amount of MIR135A level to be higher. Increasing MIR135A level HOIP_0004690 HOIP:HOIP_0004694 A series of molecular signals mediated by MMP7 (matrix metallopeptidase 7). MMP7 signal transduction pathway HOIP_0004694 HOIP:HOIP_0004696 MMP7 signaling is a process that a signal is transmitted by MMP7. MMP7 signaling HOIP_0004696 HOIP:HOIP_0004697 Increasing MYC level is a subtype of increasing quantity: A process that changes the amount of MYC level to be higher. Increasing MYC level HOIP_0004697 HOIP:HOIP_0004702 The process of removing one or more methyl groups from MYC gene promoter. MYC gene promoter demethylation HOIP_0004702 HOIP:HOIP_0004706 NDUFA12 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFA12 (NADH:ubiquinone oxidoreductase subunit A12) to be lower. NDUFA12 inactivation HOIP_0004706 HOIP:HOIP_0004707 NCBI-Human-GeneID:55967 NCBI-Mouse-GeneID:66414 NCBI-Rat-GeneID:299739 NDUFA12 (mol) HOIP_0004707 NCBI-Human-GeneID:55967 http://www.ncbi.nlm.nih.gov/gene/55967 NCBI-Mouse-GeneID:66414 http://www.ncbi.nlm.nih.gov/gene/66414 NCBI-Rat-GeneID:299739 http://www.ncbi.nlm.nih.gov/gene/299739 HOIP:HOIP_0004708 NDUFB6 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFB6 (NADH:ubiquinone oxidoreductase subunit B6) to be lower. NDUFB6 inactivation HOIP_0004708 HOIP:HOIP_0004709 NCBI-Human-GeneID:4712 NCBI-Mouse-GeneID:230075 NCBI-Rat-GeneID:297990 NDUFB6 (mol) HOIP_0004709 NCBI-Human-GeneID:4712 http://www.ncbi.nlm.nih.gov/gene/4712 NCBI-Mouse-GeneID:230075 http://www.ncbi.nlm.nih.gov/gene/230075 NCBI-Rat-GeneID:297990 http://www.ncbi.nlm.nih.gov/gene/297990 HOIP:HOIP_0004710 NDUFS2 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFS2 (NADH:ubiquinone oxidoreductase core subunit S2) to be lower. NDUFS2 inactivaiton HOIP_0004710 HOIP:HOIP_0004711 NCBI-Human-GeneID:4720 NCBI-Mouse-GeneID:226646 NCBI-Rat-GeneID:289218 NDUFS2 (mol) HOIP_0004711 NCBI-Human-GeneID:4720 http://www.ncbi.nlm.nih.gov/gene/4720 NCBI-Mouse-GeneID:226646 http://www.ncbi.nlm.nih.gov/gene/226646 NCBI-Rat-GeneID:289218 http://www.ncbi.nlm.nih.gov/gene/289218 HOIP:HOIP_0004712 NDUFV1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFV1 (NADH:ubiquinone oxidoreductase core subunit V1) to be lower. NDUFV1 inactivation HOIP_0004712 HOIP:HOIP_0004713 NCBI-Human-GeneID:4723 NCBI-Mouse-GeneID:17995 NCBI-Rat-GeneID:293655 NDUFV1 (mol) HOIP_0004713 NCBI-Human-GeneID:4723 http://www.ncbi.nlm.nih.gov/gene/4723 NCBI-Mouse-GeneID:17995 http://www.ncbi.nlm.nih.gov/gene/17995 NCBI-Rat-GeneID:293655 http://www.ncbi.nlm.nih.gov/gene/293655 HOIP:HOIP_0004714 NDUFV3 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFV3 (NADH:ubiquinone oxidoreductase core subunit V3) to be lower. NDUFV3 inactivation HOIP_0004714 HOIP:HOIP_0004715 NCBI-Human-GeneID:4731 NCBI-Mouse-GeneID:78330 NCBI-Rat-GeneID:64539 NDUFV3 (mol) HOIP_0004715 NCBI-Human-GeneID:4731 http://www.ncbi.nlm.nih.gov/gene/4731 NCBI-Mouse-GeneID:78330 http://www.ncbi.nlm.nih.gov/gene/78330 NCBI-Rat-GeneID:64539 http://www.ncbi.nlm.nih.gov/gene/64539 HOIP:HOIP_0004716 Increasing production quantity of NO is a subtype of increasing quantity: A process that changes the production amount of nitric oxide (NO) to be higher. Increasing production quantity of NO HOIP_0004716 HOIP:HOIP_0004717 Increasing production quantity of NO is a subtype of increasing quantity: A process that changes the production amount of nitric oxide (NO) to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 Increasing production quantity of NO [mitochondrial disorder (course)] HOIP_0004717 PMID:23299992 NAFLD has been associated with higher hepatic expression of the inducible nitric oxide (NO) synthase (iNOS), mainly as a consequence of tumor necrosis factor‐α (TNF‐α) overproduction by the Kupffer cells. NO can readily react with the superoxide anion, thus generating the RNS peroxynitrite, which has deleterious effects on mitochondrial function and genome. PMID:25339807 NO may affect mitochondrial respiratory chain function by reacting with cytochrome c oxidase, thus interrupting electron transfer to oxygen. HOIP:HOIP_0004718 Increasing production quantity of RNS is a subtype of increasing quantity: A process that changes the production amount of reactive nitrogen species (RNS) to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 increasing production quantity of RNS [mitochondrial disorder (course)] HOIP_0004718 PMID:23299992 NAFLD has been associated with higher hepatic expression of the inducible nitric oxide (NO) synthase (iNOS), mainly as a consequence of tumor necrosis factor‐α (TNF‐α) overproduction by the Kupffer cells. NO can readily react with the superoxide anion, thus generating the RNS peroxynitrite, which has deleterious effects on mitochondrial function and genome. HOIP:HOIP_0004719 NRF2 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NRF2 (nuclear factor 2) to be lower. NRF2 inactivation HOIP_0004719 HOIP:HOIP_0004720 NRF2 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NRF2 (nuclear factor 2) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 NRF2 inactivation [mitochondrial disorder (course)] HOIP_0004720 PMID:31623280 H2O2 produced by mitochondria induces antioxidant enzyme expression through AMPK-mediated activation of nuclear factor 2 (NRF2), and consistently, NRF2 knockout mice on a high-fat diet develop more severe NASH associated with decreased antioxidant response, reduced β-oxidation genes, and increased lipogenic genes. HOIP:HOIP_0004721 NCBI-Human-GeneID:4780 NCBI-Mouse-GeneID:18024 NCBI-Rat-GeneID:83619 PMID:31623280 NRF2 - inactive form (canonical) [mitochondrial disorder (course)] HOIP_0004721 NCBI-Human-GeneID:4780 http://www.ncbi.nlm.nih.gov/gene/4780 NCBI-Mouse-GeneID:18024 http://www.ncbi.nlm.nih.gov/gene/18024 NCBI-Rat-GeneID:83619 http://www.ncbi.nlm.nih.gov/gene/83619 PMID:31623280 H2O2 produced by mitochondria induces antioxidant enzyme expression through AMPK-mediated activation of nuclear factor 2 (NRF2), and consistently, NRF2 knockout mice on a high-fat diet develop more severe NASH associated with decreased antioxidant response, reduced β-oxidation genes, and increased lipogenic genes. HOIP:HOIP_0004722 Negative regulation of antioxidant enzyme activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of antioxidant enzyme activation. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:31623280 negative regulation of antioxidant enzyme activation [mitochondrial disorder (course)] HOIP_0004722 PMID:23299992 Reduced ROS detoxification could also favor oxidative stress. Indeed, several studies showed lower GSH levels in NAFLD, including within the mitochondria. Decreased expression and/or activity of antioxidant enzymes such as GPx and SODs could also occur, in particular at the mitochondrial level. PMID:31623280 H2O2 produced by mitochondria induces antioxidant enzyme expression through AMPK-mediated activation of nuclear factor 2 (NRF2), and consistently, NRF2 knockout mice on a high-fat diet develop more severe NASH associated with decreased antioxidant response, reduced β-oxidation genes, and increased lipogenic genes. HOIP:HOIP_0004723 Hypofunction of lipid biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient lipid biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 hypofunction of lipid biosynthesis [mitochondrial disorder (course)] HOIP_0004723 PMID:31623280 H2O2 produced by mitochondria induces antioxidant enzyme expression through AMPK-mediated activation of nuclear factor 2 (NRF2), and consistently, NRF2 knockout mice on a high-fat diet develop more severe NASH associated with decreased antioxidant response, reduced β-oxidation genes, and increased lipogenic genes. HOIP:HOIP_0004724 Notch signaling is a process that a signal is transmitted by Notch. Notch signaling HOIP_0004724 HOIP:HOIP_0004729 ORC1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the ORC1 (origin recognition complex subunit 1) to be lower. ORC1 inactivation HOIP_0004729 HOIP:HOIP_0004730 NCBI-Human-GeneID:4998 NCBI-Mouse-GeneID:18392 NCBI-Rat-GeneID:313479 ORC1 (mol) HOIP_0004730 NCBI-Human-GeneID:4998 http://www.ncbi.nlm.nih.gov/gene/4998 NCBI-Mouse-GeneID:18392 http://www.ncbi.nlm.nih.gov/gene/18392 NCBI-Rat-GeneID:313479 http://www.ncbi.nlm.nih.gov/gene/313479 HOIP:HOIP_0004733 NCBI-Human-GeneID:101154753 P21 associated ncRNA DNA damage activated PANDA HOIP_0004733 NCBI-Human-GeneID:101154753 https://www.ncbi.nlm.nih.gov/gene/101154753 HOIP:HOIP_0004734 Increasing PANDA level is a subtype of increasing quantity: A process that changes the amount of PANDA level to be higher. Increasing PANDA level HOIP_0004734 HOIP:HOIP_0004736 NCBI-Human-GeneID:101154753 PMID:28646235 P21 associated ncRNA DNA damage activated PANDA (human) [hepatocarcinogenesis] HOIP_0004736 NCBI-Human-GeneID:101154753 https://www.ncbi.nlm.nih.gov/gene/101154753 PMID:28646235 Over Expression of Long Non-Coding RNA PANDA Promotes Hepatocellular Carcinoma by Inhibiting Senescence Associated Inflammatory Factor IL8. Importantly, this aberrant function was attributed to its inhibitory action on cell senescence by suppressing senescence associated inflammatory chemokine IL8. HOIP:HOIP_0004737 PCK1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the PCK1 (phosphoenolpyruvate carboxykinase 1) to be lower. PCK1 inactivation HOIP_0004737 HOIP:HOIP_0004740 PCK1 activation is a subtype of molecular activation: A process that changes the activity of the PCK1 (phosphoenolpyruvate carboxykinase 1) to be higher. PCK1 activation HOIP_0004740 HOIP:HOIP_0004741 PCK1 activation is a subtype of molecular activation: A process that changes the activity of the PCK1 (phosphoenolpyruvate carboxykinase 1) to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:26571396 PMID:29335519 PCK1 activation [mitochondrial disorder (course)] HOIP_0004741 PMID:26571396 Mitochondrial metabolism mediates oxidative stress and inflammation in fatty liver. Second, loss of anaplerosis/cataplerosis via genetic knockdown of phosphoenolpyruvate carboxykinase 1 (Pck1) prevented fatty acid-induced rise in oxidative flux, oxidative stress, and inflammation. PMID:29335519 Collectively, these data suggest that enforced PCK1 expression triggers glucose-deprived liver cancer cell death by causing truncated gluconeogenesis, energy crisis, TCA cycle cataplerosis and high ROS levels. Supporting this notion, PCK1 expression in SK-Hep-1 dramatically reduced cellular ATP level by 4 folds in cells cultured in low glucose medium, but not in normal medium (Fig. 4c). HOIP:HOIP_0004742 Any process that stops, prevents, or reduces the frequency, rate or extent of gluconeogenesis. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29335519 negative regulation of gluconeogenesis [mitochondrial disorder (course)] HOIP_0004742 PMID:29335519 Collectively, these data suggest that enforced PCK1 expression triggers glucose-deprived liver cancer cell death by causing truncated gluconeogenesis, energy crisis, TCA cycle cataplerosis and high ROS levels. HOIP:HOIP_0004743 Increasing PCNA level is a subtype of increasing quantity: A process that changes the amount of PCNA level to be higher. Increasing PCNA level HOIP_0004743 HOIP:HOIP_0004744 NCBI-Human-GeneID:5111 NCBI-Mouse-GeneID:18538 NCBI-Rat-GeneID:25737 PCNA (mol) HOIP_0004744 NCBI-Human-GeneID:5111 http://www.ncbi.nlm.nih.gov/gene/5111 NCBI-Mouse-GeneID:18538 http://www.ncbi.nlm.nih.gov/gene/18538 NCBI-Rat-GeneID:25737 http://www.ncbi.nlm.nih.gov/gene/25737 HOIP:HOIP_0004747 PHB inactivation is a subtype of molecular inactivation: A process that changes the activity of the PHB (prohibitin) to be lower. PHB inactivation HOIP_0004747 HOIP:HOIP_0004748 NCBI-Human-GeneID:5245 NCBI-Mouse-GeneID:18673 NCBI-Rat-GeneID:25344 PHB (mol) HOIP_0004748 NCBI-Human-GeneID:5245 http://www.ncbi.nlm.nih.gov/gene/5245 NCBI-Mouse-GeneID:18673 http://www.ncbi.nlm.nih.gov/gene/18673 NCBI-Rat-GeneID:25344 http://www.ncbi.nlm.nih.gov/gene/25344 HOIP:HOIP_0004754 PIM3 activation is a subtype of molecular activation: A process that changes the activity of the PIM3 (Pim-3 proto-oncogene, serine/threonine kinase) to be higher. PIM3 activation HOIP_0004754 HOIP:HOIP_0004756 NCBI-Human-GeneID:415116 PMID:20101231 PIM3 (human) [hepatocarcinogenesis] HOIP_0004756 NCBI-Human-GeneID:415116 http://www.ncbi.nlm.nih.gov/gene/415116 PMID:20101231 These observations indicate that the DEN challenge enhanced liver damage in Pim-3 transgenic mice, compared with that observed for WT mice, despite increased hepatocyte proliferation. Lipid droplet accumulation was more evident in Pim-3 transgenic mice than in WT mice, until 6 months after DEN treatment (Figure 4a). Dysplastic cells were observed and lobules were distorted in livers of Pim-3 transgenic mice, but not of WT mice, 6 months after DEN treatment (Figure 5a). The enhanced hepatocarcinogenesis in Pim-3 transgenic mice may mirror the fact that neovascularization, an essential process for hepatocarcinogenesis, was augmented in Pim-3 transgenic mice compared with that observed for WT mice, as demonstrated by increases in CD31-positive areas in the liver (Figures 5f and g). Pim-3-transgenic mouse-derived hepatocytes exhibited accelerated cell cycle progression. HOIP:HOIP_0004760 PKC activation is a subtype of molecular activation: A process that changes the activity of the PKC ( protein kinase C) to be higher. PKC activation HOIP_0004760 HOIP:HOIP_0004761 PKC activation is a subtype of molecular activation: A process that changes the activity of the PKC ( protein kinase C) to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31649547 PKC activation [mitochondrial disorder (course)] HOIP_0004761 PMID:31649547 As a result, fatty acids especially diacylglycerol and ceramide may excessively accumulate in liver tissue. Previous report has shown that diacylglycerol can activate PKC to impair insulin signal pathway. Moreover, ceramide also activates PKC to suppress protein kinase AKT and further inhibits insulin signal pathway. HOIP:HOIP_0004762 PMAIP1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the PMAIP1 (phorbol-12-myristate-13-acetate-induced protein 1) to be lower. PMAIP1 inactivation HOIP_0004762 HOIP:HOIP_0004765 Increasing PPARA level is a subtype of increasing quantity: A process that changes the amount of PPARA level to be higher. Increasing PPARA level HOIP_0004765 HOIP:HOIP_0004768 Hypofunction of PPARGC1A gene expression is a subtype of hypofunction of transcription, DNA-templated: A process that performs a decreased or insufficient PPARGC1A gene expression. Hypofunction of PPARGC1A gene expression HOIP_0004768 HOIP:HOIP_0004769 NCBI-Human-GeneID:10891 NCBI-Mouse-GeneID:19017 NCBI-Rat-GeneID:83516 PMID:23299992 PMID:31623280 PGC-1(alpha) PPARGC1A (canonical) [mitochondrial disorder (course)] HOIP_0004769 NCBI-Human-GeneID:10891 http://www.ncbi.nlm.nih.gov/gene/10891 NCBI-Mouse-GeneID:19017 http://www.ncbi.nlm.nih.gov/gene/19017 NCBI-Rat-GeneID:83516 http://www.ncbi.nlm.nih.gov/gene/83516 PMID:23299992 Indeed, FoxO1 activation is able to reduce the content of different MRC polypeptides, possibly by decreasing heme synthesis and impairing PGC1α activity. Interestingly, oxidative stress and inflammation are able to reduce PGC1α expression. PMID:31623280 Decreased mitochondrial biogenesis is associated with a reduction of PGC-1α, transcription factor A, mitochondrial (TFAM), or PPARs in fatty livers. HOIP:HOIP_0004772 NCBI-Human-GeneID:5624 NCBI-Mouse-GeneID:19123 NCBI-Rat-GeneID:25268 PROC (mol) HOIP_0004772 NCBI-Human-GeneID:5624 http://www.ncbi.nlm.nih.gov/gene/5624 NCBI-Mouse-GeneID:19123 http://www.ncbi.nlm.nih.gov/gene/19123 NCBI-Rat-GeneID:25268 http://www.ncbi.nlm.nih.gov/gene/25268 HOIP:HOIP_0004775 The covalent transfer of a methyl group to PROC gene promoter. PROC gene promoter methylation HOIP_0004775 HOIP:HOIP_0004777 Increasing PROM1 level is a subtype of increasing quantity: A process that changes the amount of PROM1 level to be higher. Increasing PROM1 level HOIP_0004777 HOIP:HOIP_0004778 NCBI-Human-GeneID:8842 NCBI-Mouse-GeneID:19126 NCBI-Rat-GeneID:60357 CD133 PROM1 (mol) HOIP_0004778 NCBI-Human-GeneID:8842 http://www.ncbi.nlm.nih.gov/gene/8842 NCBI-Mouse-GeneID:19126 http://www.ncbi.nlm.nih.gov/gene/19126 NCBI-Rat-GeneID:60357 http://www.ncbi.nlm.nih.gov/gene/60357 HOIP:HOIP_0004781 Increasing PROX1 level is a subtype of increasing quantity: A process that changes the amount of PROX1 level to be higher. Increasing PROX1 level HOIP_0004781 HOIP:HOIP_0004782 NCBI-Human-GeneID:5629 NCBI-Mouse-GeneID:19130 NCBI-Rat-GeneID:305066 PROX1 (mol) HOIP_0004782 NCBI-Human-GeneID:5629 http://www.ncbi.nlm.nih.gov/gene/5629 NCBI-Mouse-GeneID:19130 http://www.ncbi.nlm.nih.gov/gene/19130 NCBI-Rat-GeneID:305066 http://www.ncbi.nlm.nih.gov/gene/305066 HOIP:HOIP_0004785 PTPRD inactivation is a subtype of molecular inactivation: A process that changes the activity of the PTPRD (protein tyrosine phosphatase receptor type D) to be lower. PTPRD inactivation HOIP_0004785 HOIP:HOIP_0004788 The covalent transfer of a methyl group to PTPRD gene promoter. PTPRD gene promoter methylation HOIP_0004788 HOIP:HOIP_0004790 Increasing PVT1 level is a subtype of increasing quantity: A process that changes the amount of PVT1 level to be higher. Increasing PVT1 level HOIP_0004790 HOIP:HOIP_0004795 hypofunction of S-adenosylmethionine biosynthetic process is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient S-adenosylmethionine biosynthetic process. hypofunction of S-adenosylmethionine biosynthetic process HOIP_0004795 HOIP:HOIP_0004796 hypofunction of S-adenosylmethionine biosynthetic process is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient S-adenosylmethionine biosynthetic process. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 hypofunction of S-adenosylmethionine biosynthetic process [mitochondrial disorder (course)] HOIP_0004796 PMID:25339807 Depletion of mitochondrial GSH levels could also be due to its reduced uptake by mitochondria as a result of enhanced levels of cholesterol within the inner mitochondrial membrane and the decrease in synthesis of S-adenosylmethionine, the major methyl donor in liver and precursor to GSH. HOIP:HOIP_0004797 Decreasing glutathione level is a subtype of decreasing quantity: A process that changes the amount of glutathione level to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 decreasing glutathione level [mitochondrial disorder (course)] HOIP_0004797 PMID:23299992 Reduced ROS detoxification could also favor oxidative stress. Indeed, several studies showed lower GSH levels in NAFLD, including within the mitochondria. Decreased expression and/or activity of antioxidant enzymes such as GPx and SODs could also occur, in particular at the mitochondrial level. Indeed, increased mitochondrial cholesterol during NAFLD could reduce mitochondrial transport of GSH, thus inducing lower mtGSH levels and oxidative stress (Fig. 4).18,50,261 PMID:25339807 Depletion of mitochondrial GSH levels could also be due to its reduced uptake by mitochondria as a result of enhanced levels of cholesterol within the inner mitochondrial membrane and the decrease in synthesis of S-adenosylmethionine, the major methyl donor in liver and precursor to GSH. HOIP:HOIP_0004798 SFRP1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the SFRP1 (secreted frizzled related protein 1) to be lower. SFRP1 inactivation HOIP_0004798 HOIP:HOIP_0004799 NCBI-Human-GeneID:6422 NCBI-Mouse-GeneID:20377 NCBI-Rat-GeneID:84402 secreted frizzled related protein 1 SFRP1 (mol) HOIP_0004799 NCBI-Human-GeneID:6422 http://www.ncbi.nlm.nih.gov/gene/6422 NCBI-Mouse-GeneID:20377 https://www.ncbi.nlm.nih.gov/gene/20377 NCBI-Rat-GeneID:84402 https://www.ncbi.nlm.nih.gov/gene/84402 HOIP:HOIP_0004802 Increasing SPTLC3 level is a subtype of increasing quantity: A process that changes the amount of SPTLC3 level to be higher. Increasing SPTLC3 level HOIP_0004802 HOIP:HOIP_0004805 A series of molecular signals mediated by SRC. SRC signal transduction pathway HOIP_0004805 HOIP:HOIP_0004806 A series of molecular signals mediated by STAT3 (signal transducer and activator of transcription 3). STAT3 signal transduction pathway HOIP_0004806 HOIP:HOIP_0004807 STAT3 signaling is a process that a signal is transmitted by the STAT3 (signal transducer and activator of transcription 3) . STAT3 signaling HOIP_0004807 HOIP:HOIP_0004810 Snail1 signaling is a process that a signal is transmitted by the Snail1 (snail family transcriptional repressor 1) . Snail1 signaling HOIP_0004810 HOIP:HOIP_0004811 A series of molecular signals mediated by Snail1 (snail family transcriptional repressor 1). Snail1 signal transduction pathway HOIP_0004811 HOIP:HOIP_0004813 A series of molecular signals mediated by TAZ (tafazzin). TAZ signal transduction pathway HOIP_0004813 HOIP:HOIP_0004814 TAZ signaling is a process that a signal is transmitted by TAZ. TAZ signaling HOIP_0004814 HOIP:HOIP_0004815 NCBI-Human-GeneID:6901 NCBI-Mouse-GeneID:66826 NCBI-Rat-GeneID:363521 TAZ (mol) HOIP_0004815 NCBI-Human-GeneID:6901 http://www.ncbi.nlm.nih.gov/gene/6901 NCBI-Mouse-GeneID:66826 http://www.ncbi.nlm.nih.gov/gene/66826 NCBI-Rat-GeneID:363521 http://www.ncbi.nlm.nih.gov/gene/363521 HOIP:HOIP_0004819 C16H8Cl4N2O2 C1=CC(=CC=C1OC2=C(C=C(C=N2)Cl)Cl)OC3=C(C=C(C=N3)Cl)Cl CAS:76150-91-9 PubChem CID:5382 TCPOBOP 1,4-bis[2-(3,5-dichloropyridyloxy)]benzene HOIP_0004819 HOIP:HOIP_0004820 Hypofunction of TFAM gene expression is a subtype of hypofunction of transcription, DNA-templated: A process that performs a decreased or insufficient TFAM gene expression. Hypofunction of TFAM gene expression HOIP_0004820 HOIP:HOIP_0004821 Hypofunction of TFAM gene expression is a subtype of hypofunction of transcription, DNA-templated: A process that performs a decreased or insufficient TFAM gene expression. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Hypofunction of TFAM gene expression [mitochondrial disorder (course)] HOIP_0004821 PMID:31623280 Decreased mitochondrial biogenesis is associated with a reduction of PGC-1α, transcription factor A, mitochondrial (TFAM), or PPARs in fatty livers. HOIP:HOIP_0004822 NCBI-Human-GeneID:7019 NCBI-Mouse-GeneID:21780 NCBI-Rat-GeneID:83474 PMID:31623280 TFAM (canonical) [mitochondrial disorder (course)] HOIP_0004822 NCBI-Human-GeneID:7019 http://www.ncbi.nlm.nih.gov/gene/7019 NCBI-Mouse-GeneID:21780 http://www.ncbi.nlm.nih.gov/gene/21780 NCBI-Rat-GeneID:83474 http://www.ncbi.nlm.nih.gov/gene/83474 PMID:31623280 Decreased mitochondrial biogenesis is associated with a reduction of PGC-1α, transcription factor A, mitochondrial (TFAM), or PPARs in fatty livers. HOIP:HOIP_0004823 A series of molecular signals mediated by TGF-alpha (transforming growth factor alpha). TGF-alpha signal transduction pathway HOIP_0004823 HOIP:HOIP_0004824 TGF-alpha signaling is a process that a signal is transmitted by TGF-alpha. TGF-alpha signaling HOIP_0004824 HOIP:HOIP_0004829 TLR4 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 4. TLR4 signaling HOIP_0004829 HOIP:HOIP_0004830 The rupture of cell membranes and the loss of cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Wikipedia:Cytolysis cytolysis [mitochondrial disorder (course)] HOIP_0004830 PMID:31623280 Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. HOIP:HOIP_0004831 NCBI-Human-GeneID:7099 NCBI-Mouse-GeneID:21898 NCBI-Rat-GeneID:29260 PMID:31623280 TLR4 (mol)＠ミトコンドリア障害 Toll-like receptor 4 TLR4 (canonical) [mitochondrial disorder (course)] HOIP_0004831 NCBI-Human-GeneID:7099 https://www.ncbi.nlm.nih.gov/gene/7099 NCBI-Mouse-GeneID:21898 https://www.ncbi.nlm.nih.gov/gene/21898 NCBI-Rat-GeneID:29260 https://www.ncbi.nlm.nih.gov/gene/29260 PMID:31623280 Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. HOIP:HOIP_0004832 TNF signaling is a process that a signal is transmitted by TNF. TNF signaling HOIP_0004832 HOIP:HOIP_0004833 TNF signaling is a process that a signal is transmitted by TNF. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 TNF signaling [mitochondrial disorder (course)] HOIP_0004833 PMID:31623280 Moreover, mitochondrial-free cholesterol sensitizes liver cells to TNFα- and Fas-mediated steatohepatitis and causes mitochondrial-reduced glutathione (mGSH) depletion, which is also reported in animal models and patients with NASH. Moreover, TNF-α and IL-6 promote iron accumulation, which further fuels oxidative stress-driven cell toxicity and can activate fibrogenesis and carcinogenesis in metabolic syndrome. HOIP:HOIP_0004838 A series of molecular signals mediated by TSLC (Tumor suppressor in lung cancer-1) proteins. TSLC signaling cascade TSLC signaling pathway TSLC signal transduction pathway HOIP_0004838 HOIP:HOIP_0004839 TSLC signaling is a process that a signal is transmitted by the TSLC (Tumor suppressor in lung cancer-1) . TSLC signaling HOIP_0004839 HOIP:HOIP_0004840 Any process that stops, prevents, or reduces the frequency, rate or extent of TSLC signaling, a series of reactions mediated by TSLC. negative regulation of TSLC signalling cascade negative regulation of TSLC signaling HOIP_0004840 HOIP:HOIP_0004846 A series of molecular signals mediated by twist1. Twist1 signal transduction pathway HOIP_0004846 HOIP:HOIP_0004848 Twist1 signaling is a process that a signal is transmitted by the cytokine Twist1. Twist1 signaling HOIP_0004848 HOIP:HOIP_0004850 PMID:29507645 trimeric UHRF1 repression complex HOIP_0004850 PMID:29507645 The complex comprises three subunits, namely DNA methyltransferase 1 (DNMT1), ubiquitin-specific-processing protease 7 (USP7), and E3 ubiquitin-like containing PHD and RING finger domain 1 (UHRF1). HOIP:HOIP_0004853 UHRF1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the UHRF1 (ubiquitin like with PHD and ring finger domains 1) to be lower. UHRF1 inactivation HOIP_0004853 HOIP:HOIP_0004856 Increasing VEGF level is a subtype of increasing quantity: A process that changes the amount of VEGF level to be higher. Increasing VEGF level HOIP_0004856 HOIP:HOIP_0004859 A series of molecular signals mediated by WNT (wingless/int-1). WNT signal transduction pathway HOIP_0004859 HOIP:HOIP_0004860 WNT signaling is a process that a signal is transmitted by WNT. WNT signaling HOIP_0004860 HOIP:HOIP_0004867 A series of molecular signals mediated by YAP (Yes associated protein). YAP signal transduction pathway HOIP_0004867 HOIP:HOIP_0004868 YAP signaling is a process that a signal is transmitted by YAP. YAP signaling HOIP_0004868 HOIP:HOIP_0004870 A series of molecular signals mediated by beta-catenin. beta-catenin signal transduction pathway HOIP_0004870 HOIP:HOIP_0004871 beta-catenin signaling is a process that a signal is transmitted by beta-catenin. beta-catenin signaling HOIP_0004871 HOIP:HOIP_0004875 c-Src signaling is a process that a signal is transmitted by c-Src. c-Src signaling HOIP_0004875 HOIP:HOIP_0004876 NCBI-Human-GeneID:6714 NCBI-Mouse-GeneID:20779 NCBI-Rat-GeneID:83805 PMID:31781608 c-Src p60-Src Src (canonical) [hepatocarcinogenesis] HOIP_0004876 NCBI-Human-GeneID:6714 https://www.ncbi.nlm.nih.gov/gene/6714 NCBI-Mouse-GeneID:20779 https://www.ncbi.nlm.nih.gov/gene/20779 NCBI-Rat-GeneID:83805 https://www.ncbi.nlm.nih.gov/gene/83805 PMID:31781608 In addition to the Wnt pathway, activated c-Src, STAT3, Akt, and Notch1 were also identified as mediators of EMT induced by HBV. HOIP:HOIP_0004877 Negative regulation of caspase-3 activation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of caspase-3 activation. negative regulation of caspase-3 activation HOIP_0004877 HOIP:HOIP_0004878 Negative regulation of activation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of activation. negative regulation of activation HOIP_0004878 HOIP:HOIP_0004880 The selective interaction of the cyclin A with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus. cytoplasmic sequestering of cyclin A HOIP_0004880 HOIP:HOIP_0004884 iNOS production is a subtype of protein production: A process that makes existent of iNOS ( inducible nitric oxide synthase) due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. inducible nitric oxide synthase production HOIP_0004884 HOIP:HOIP_0004885 NCBI-Human-GeneID:4843 NCBI-Mouse-GeneID:18126 NCBI-Rat-GeneID:24599 nitric oxide synthase 2 NOS2 (canonical) [mitochondrial disorder (course)] HOIP_0004885 NCBI-Human-GeneID:4843 http://www.ncbi.nlm.nih.gov/gene/4843 NCBI-Mouse-GeneID:18126 http://www.ncbi.nlm.nih.gov/gene/18126 NCBI-Rat-GeneID:24599 http://www.ncbi.nlm.nih.gov/gene/24599 HOIP:HOIP_0004888 mitochondria morphology changes is a subtype of changing shape: A process that changes the morphology of the mitochondria. mitochondria morphology change HOIP_0004888 HOIP:HOIP_0004890 Proto-oncogene mutation is a subtype of changing an operand: A process that changes the nucleotide sequence of Tumor suppressor gene randomly and permanently. proto-oncogene mutation HOIP_0004890 HOIP:HOIP_0004894 NCBI-Human-GeneID:3845 NCBI-Mouse-GeneID:16653 NCBI-Rat-GeneID:24525 PMID:21160980 K-Ras Ki-ras KRAS (canonical) [hepatocarcinogenesis] HOIP_0004894 NCBI-Human-GeneID:3845 https://www.ncbi.nlm.nih.gov/gene/3845 NCBI-Mouse-GeneID:16653 https://www.ncbi.nlm.nih.gov/gene/16653 NCBI-Rat-GeneID:24525 https://www.ncbi.nlm.nih.gov/gene/24525 PMID:21160980 In HCC, the tumor suppressor gene p53 codon 249 mutation is associated with AFB(1) exposure and mutations in the K-ras oncogene are related to vinyl chloride exposure. AFB1-induced HCC in Fischer 344 rats showed activating mutations in codon 12 of K-ras, but in human HCC, the incidence of point mutation of K-ras and N-ras oncogenes was low. Afterwards, in HCC in workers exposed to VC, a high prevalence of K-ras-2 mutation was reported. HOIP:HOIP_0004897 Any process that activates or increases the frequency, rate or extent of cancer stem cell division. positive regulation of cancer stem cell division HOIP_0004897 HOIP:HOIP_0004898 Cancer-stem like cell proliferation is a subtype of cell proliferation: A process of the multiplication or reproduction of cancer-stem like cells, resulting in the rapid expansion of a cancer-stem like cell population. cancer stem-like cell proliferation HOIP_0004898 HOIP:HOIP_0004900 Tumor suppressor inactivation is a subtype of molecular inactivation: A process that changes the activity of the tumor suppressor to be lower. tumor suppressor inactivation HOIP_0004900 HOIP:HOIP_0004902 Tumor suppressor gene mutation is a subtype of changing an operand: A process that changes the nucleotide sequence of Tumor suppressor gene randomly and permanently. Tumor suppressor gene mutation HOIP_0004902 HOIP:HOIP_0004903 Negative regulation of actin cytoskeleton organization is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of actin cytoskeleton organization. negative regulation of actin cytoskeleton organization HOIP_0004903 HOIP:HOIP_0004904 acetyl-CoA biosynthetic process is a subtype of generating: A process that synthesizes acetyl-CoA resulting in having output (s). acetyl-CoA biosynthetic process HOIP_0004904 HOIP:HOIP_0004905 Decreasing adiponectin level is a subtype of decreasing quantity: A process that changes the amount of adiponectin level to be lower. decreasing adiponectin level HOIP_0004905 HOIP:HOIP_0004906 Decreasing adiponectin level is a subtype of decreasing quantity: A process that changes the amount of adiponectin level to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 decreasing adiponectin level [mitochondrial disorder (course)] HOIP_0004906 PMID:23299992 Other mechanisms leading to impaired MRC activity could include higher levels of different lipid intermediates including free FAs, increased generation of lipid peroxidation products such as 4‐HNE, and reduced adiponectin action. HOIP:HOIP_0004920 Any process that activates or increases the frequency, rate or extent of arachidonic acid metabolic process. positive regulation of arachidonic acid metabolic process HOIP_0004920 HOIP:HOIP_0004921 Decreasing arachidonic acid level is a subtype of decreasing quantity: A process that changes the amount of arachidonic acid level to be lower. Decreasing arachidonic acid level HOIP_0004921 HOIP:HOIP_0004925 NLRP3 is a inflammasome component NCBI-Human-GeneID:114548 NCBI-Mouse-GeneID:216799 NCBI-Rat-GeneID:287362 PMID:31623280 NLRP3 (canonical)[mitochondrial disorder (course)]] HOIP_0004925 NCBI-Human-GeneID:114548 http://www.ncbi.nlm.nih.gov/gene/114548 NCBI-Mouse-GeneID:216799 http://www.ncbi.nlm.nih.gov/gene/216799 NCBI-Rat-GeneID:287362 http://www.ncbi.nlm.nih.gov/gene/287362 PMID:31623280 After binding to TLR9, mitochondrial DAMPs trigger numerous downstream pathways, including nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), the nucleotide binding oligomerization domain (NOD)-like receptor family, pyrin domain containing 3 (NLRP3), and interferon regulatory factor-dependent type 1 to promote inflammation. HOIP:HOIP_0004926 Hypofunction of oxysterol biosynthesis is a subtype of hypofunction of lipid biosynthesis: A process that performs a decreased or insufficient oxysterol biosynthesis. hypofunction of oxysterol biosynthesis HOIP_0004926 HOIP:HOIP_0004927 Hypofunction of oxysterol biosynthesis is a subtype of hypofunction of lipid biosynthesis: A process that performs a decreased or insufficient oxysterol biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. hypofunction of oxysterol biosynthesis [mitochondrial disorder (course)] HOIP_0004927 HOIP:HOIP_0004928 The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorders. PMID:27151080 autophagy [mitochondrial disorder (course)] HOIP_0004928 PMID:27151080 not reported in the liver. We found evidence of autophagy/mitophagy in dynamic equilibrium with the biogenesis of novel mitochondria, particularly in mutant C9ORF72 fibroblasts where an increase of mitochondrial DNA content and mass, and of PGC1-α protein was observed. The autophagic process is also partially activated in mC9ORF72 as evidenced by electron microscopy data and p62 protein down-regulation. HOIP:HOIP_0004931 cardiolipin peroxidation is a subtype of phospholipid oxidation: The degradation of cardiolipin caused by an oxidative attack from free radicals. cardiolipin peroxidation HOIP_0004931 HOIP:HOIP_0004932 phospholipid peroxidation is a subtype of lipid oxidation: The degradation of phospholipids caused by an oxidative attack from free radicals. phospholipid peroxidation HOIP_0004932 HOIP:HOIP_0004933 A process that stops, prevents, or reduces the frequency, rate or extent of phospholipid degradation. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). negative regulation of phospholipid degradation [phospholipidosis (latent)] HOIP_0004933 HOIP:HOIP_0004935 Increasing glucagon level is a subtype of increasing quantity: A process that changes the amount of glucagon level to be higher. Increasing glucagon level HOIP_0004935 HOIP:HOIP_0004936 Increasing glucagon level is a subtype of increasing quantity: A process that changes the amount of glucagon level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 Increasing glucagon level [mitochondrial disorder (course)] HOIP_0004936 PMID:23299992 A second mechanism is ROS generation due to CYP2E1 overexpression and reduced levels of mtGSH. Whereas CYP2E1 induction could be secondary to higher levels of glucagon, FAs and KBs, reduced mtGSH could result from higher mitochondrial levels of cholesterol. HOIP:HOIP_0004937 Glucose homeostasis imbalance is a subtype of chemical homeostasis imbalance: A process that becomes lacking a glucose homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 PMID:31649547 glucose homeostasis imbalance [mitochondrial disorder (course)] HOIP_0004937 PMID:31623280 Recent studies also show that MAMs are important for hepatic insulin signaling, nutrient sensing, and glucose homeostasis. Therefore, disruption of ER-mitochondria contact sites could exacerbate hepatic lipid accumulation and miscommunication between organelles appears to be related to the pathology of hepatic metabolic diseases. PMID:31649547 lipotoxicity and inflammation can interfere with insulin signaling pathway to cause hepatic insulin resistance; HOIP:HOIP_0004938 Increasing glucose level is a subtype of increasing quantity: A process that changes the amount of glucose level to be higher. increasing glucose level HOIP_0004938 HOIP:HOIP_0004939 Increasing glucose level is a subtype of increasing quantity: A process that changes the amount of glucose level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:31623280 increasing glucose level [mitochondrial disorder (course)] HOIP_0004939 PMID:23299992 Furthermore, high glucose levels promote ROS overproduction within hepatocytes, thus favoring oxidative stress and mitochondrial dysfunction. PMID:31623280 Consistent with this, high glucose induces mitochondrial fragmentation, ROS production, loss of mitochondrial membrane potential, and ATP depletion in several rodent and human cell models. HOIP:HOIP_0004940 Decreasing glucose level is a subtype of decreasing quantity: A process that changes the amount of glucose level to be lower. glucose depletion decreasing glucose level HOIP_0004940 HOIP:HOIP_0004941 Decreasing glucose level is a subtype of decreasing quantity: A process that changes the amount of glucose level to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:29335519 glucose depletion Decreasing glucose level [mitochondrial disorder (course)] HOIP_0004941 PMID:29335519 Collectively, these data suggest that enforced PCK1 expression triggers glucose-deprived liver cancer cell death by causing truncated gluconeogenesis, energy crisis, TCA cycle cataplerosis and high ROS levels. HOIP:HOIP_0004942 Hyperfunction of gluconeogenesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive gluconeogenesis. hyperfunction of gluconeogenesis HOIP_0004942 HOIP:HOIP_0004943 Decreasing glutathione level is a subtype of decreasing quantity: A process that changes the amount of glutathione level to be lower. decreasing glutathione level HOIP_0004943 HOIP:HOIP_0004944 Negative regulation of glutathione transport is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of glutathione into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Negative regulation of glutathione transport HOIP_0004944 HOIP:HOIP_0004945 Increasing ketone body level is a subtype of increasing quantity: A process that changes the amount of ketone body level to be higher. Increasing ketone body level HOIP_0004945 HOIP:HOIP_0004946 Increasing ketone body level is a subtype of increasing quantity: A process that changes the amount of ketone body level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 Increasing ketone body level [mitochondrial disorder (course)] HOIP_0004946 PMID:23299992 A second mechanism is ROS generation due to CYP2E1 overexpression and reduced levels of mtGSH. Whereas CYP2E1 induction could be secondary to higher levels of glucagon, FAs and KBs, reduced mtGSH could result from higher mitochondrial levels of cholesterol. HOIP:HOIP_0004947 Any process that results in genomic instability. genomic instability HOIP_0004947 HOIP:HOIP_0004954 Increasing cholesterol level is a subtype of increasing quantity: A process that changes the amount of cholesterol level to be higher. Increasing cholesterol level HOIP_0004954 HOIP:HOIP_0004955 Increasing cholesterol level is a subtype of increasing quantity: A process that changes the amount of cholesterol level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Increasing cholesterol level [mitochondrial disorder (course)] HOIP_0004955 PMID:31623280 Bellanti et al. showed through targeted lipidomic analysis that rats fed diets rich in cholesterol exhibited increased toxic hepatic triol, which induces apoptosis and impaired mitochondrial respiration in vitro. Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Moreover, mitochondrial-free cholesterol sensitizes liver cells to TNFα- and Fas-mediated steatohepatitis and causes mitochondrial-reduced glutathione (mGSH) depletion, which is also reported in animal models and patients with NASH. HOIP:HOIP_0004956 Increasing triol level is a subtype of increasing quantity: A process that changes the amount of triol level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Increasing triol level [mitochondrial disorder (course)] HOIP_0004956 PMID:31623280 Bellanti et al. showed through targeted lipidomic analysis that rats fed diets rich in cholesterol exhibited increased toxic hepatic triol, which induces apoptosis and impaired mitochondrial respiration in vitro. HOIP:HOIP_0004957 cisplatin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to cisplatin to be lower. cisplatin resistance HOIP_0004957 HOIP:HOIP_0004958 drug resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the drug to be lower. drug resistance HOIP_0004958 HOIP:HOIP_0004959 diacylglycerol accumulation is a subtype of accumulation of substances in a biological object: A process that keeps diacylglycerol in an organism, tissue, organelle, or cell. diacylglycerol acumulation HOIP_0004959 HOIP:HOIP_0004960 diacylglycerol accumulation is a subtype of accumulation of substances in a biological object: A process that keeps diacylglycerol in an organism, tissue, organelle, or cell. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 PMID:31649547 diacylglycerol accumulation [mitochondrial disorder (course)] HOIP_0004960 PMID:31623280 Saturated fats promote fatty liver and accumulation of lipotoxic byproducts including ceramides and diacylglycerols is associated with hepatic inflammation and mitochondrial ROS production resulting in liver cell death. PMID:31649547 As a result, fatty acids especially diacylglycerol and ceramide may excessively accumulate in liver tissue. Previous report has shown that diacylglycerol can activate PKC to impair insulin signal pathway. HOIP:HOIP_0004962 Negative regulation of sphingolipid metabolic process is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of sphingolipid metabolic process. Negative regulation of sphingolipid metabolic process HOIP_0004962 HOIP:HOIP_0004964 ceramide accumulation is a subtype of accumulation of substances in a biological object: A process that keeps ceramide in an organism, tissue, organelle, or cell. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 PMID:31649547 ceramide accumulation [mitochondrial disorder (course)] HOIP_0004964 PMID:31623280 Saturated fats promote fatty liver and accumulation of lipotoxic byproducts including ceramides and diacylglycerols is associated with hepatic inflammation and mitochondrial ROS production resulting in liver cell death. PMID:31649547 As a result, fatty acids especially diacylglycerol and ceramide may excessively accumulate in liver tissue. Moreover, ceramide also activates PKC to suppress protein kinase AKT and further inhibits insulin signal pathway. HOIP:HOIP_0004965 sorafenib resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to sorafenib to be lower. sorafenib resistance (process) HOIP_0004965 HOIP:HOIP_0004966 Telomerase reverse transcriptase gene mutation is a subtype of changing an operand: A process that changes the nucleotide sequence of Telomerase reverse transcriptase gene randomly and permanently. Telomerase reverse transcriptase gene mutation HOIP_0004966 HOIP:HOIP_0004968 Increasing triol level is a subtype of increasing quantity: A process that changes the amount of triol level to be higher. Increasing triol level HOIP_0004968 HOIP:HOIP_0004970 Panadiplon (U-78875) is an anxiolytic drug with a novel chemical structure that is not closely related to other drugs of this type. (by Wikipedia) C18H17N5O2 CAS:124423-84-3 Wikipedia:Panadiplon U-78875 panadiplon HOIP_0004970 HOIP:HOIP_0004972 Fialuridine, or 1-(2-deoxy-2-fluoro-1-D-arabinofuranosyl)-5-iodouracil (FIAU), is a nucleoside analogue that was investigated as a potential therapy for hepatitis B virus infection. (by Wikipedia) C9H10FIN2O5 OC[C@H]1O[C@H]([C@@H](F)[C@@H]1O)N1C=C(I)C(=O)NC1=O CAS:69123-98-4 DrugBank:DB15427 Wikipedia:Fialuridine 2'-fluoro-5-iodoarauracil FIAU fialuridine HOIP_0004972 HOIP:HOIP_0004973 Increasing fructose level is a subtype of increasing quantity: A process that changes the amount of fructose level to be higher. Increasing fructose level HOIP_0004973 HOIP:HOIP_0004974 Increasing fructose level is a subtype of increasing quantity: A process that changes the amount of fructose level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Increasing fructose level [mitochondrial disorder (course)] HOIP_0004974 PMID:31623280 In addition to its ability to promote de novo lipogenesis and block β-oxidation of fatty acids, fructose consumption seems to cause a drop in ATP and an elevation of uric acid, which can further induce mitochondrial oxidative stress. Moreover, a diet rich in fructose is associated with increased oxidative mtDNA lesions in rat liver coupled with reduced mitochondrial repair capacity and rats consuming a diet high in fat and rich in fructose have increased hepatocyte damage, inflammation, and lipid peroxidation coupled with impaired mitochondrial respiration and activity. HOIP:HOIP_0004975 Hypofunction of mitochondrial repair is a subtype of hypofunctioning: A process that performs a decreased or insufficient mitochondrial repair. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Hypofunction of mitochondrial repair [mitochondrial disorder (course)] HOIP_0004975 PMID:31623280 Moreover, a diet rich in fructose is associated with increased oxidative mtDNA lesions in rat liver coupled with reduced mitochondrial repair capacity and rats consuming a diet high in fat and rich in fructose have increased hepatocyte damage, inflammation, and lipid peroxidation coupled with impaired mitochondrial respiration and activity. HOIP:HOIP_0004976 Increasing uric acid level is a subtype of increasing quantity: A process that changes the amount of uric acid level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Increasing uric acid level [mitochondrial disorder (course)] HOIP_0004976 PMID:31623280 In addition to its ability to promote de novo lipogenesis and block β-oxidation of fatty acids, fructose consumption seems to cause a drop in ATP and an elevation of uric acid, which can further induce mitochondrial oxidative stress. HOIP:HOIP_0004977 Any process that activates or decreases the frequency, rate or extent of mitophagy. nagative regulation of mitophagy HOIP_0004977 HOIP:HOIP_0004978 The orderly movement of a macrophage from one site to another. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31649547 macrophage migration [mitochondrial disorder (course)] HOIP_0004978 PMID:31649547 Wu et al. (2019) have found that impaired mitophagy can accelerate macrophage infiltration in white adipose tissue in high-fat diet–fed mice with FUNDC1 knockout. They have also demonstrated that impaired mitophagy can promote macrophage infiltration to activate MAPK signal pathway and inflammatory response to impair mitochondrial quality control, subsequently causing insulin resistance and hepatic steatosis. HOIP:HOIP_0004979 PMID:25339807 malondialdehyde [mitochondrial disorder (course)] HOIP_0004979 PMID:25339807 These compounds may undergo fragmentation to produce several reactive intermediates, among them, malondialdehyde and the most reactive 4-hydroxy-trans-2-nonenal. These two by-products of lipid peroxidation have been shown to interact with and inactivate ETC components, including cytochrome c oxidase, by forming adducts with this enzyme[, contributing to triggering mitochondrial dysfunction in NASH. HOIP:HOIP_0004980 Disruption of ER-mitochondria contact sites is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of ER-mitochondria contact site. disruption of ER-mitochondria contact sites HOIP_0004980 HOIP:HOIP_0004981 Disruption of ER-mitochondria contact sites is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of ER-mitochondria contact site. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Disruption of ER-mitochondria contact sites [mitochondrial disorder (course)] HOIP_0004981 PMID:31623280 Therefore, disruption of ER-mitochondria contact sites could exacerbate hepatic lipid accumulation and miscommunication between organelles appears to be related to the pathology of hepatic metabolic diseases. HOIP:HOIP_0004982 Increasing mtDNA level is a subtype of decreasing quantity: A process that changes the amount of glycogen level to be higher. increasing mtDNA level HOIP_0004982 HOIP:HOIP_0004983 glutathione transport from cytoplasm into mitochondria is a subtype of glutathione transport: A process that exports the glutathione from cytoplasm into mitochondria. PMID:23299992 glutathione transport from cytoplasm into mitochondria HOIP_0004983 PMID:23299992 Indeed, increased mitochondrial cholesterol during NAFLD could reduce mitochondrial transport of GSH, thus inducing lower mtGSH levels and oxidative stress (Fig. 4). HOIP:HOIP_0004984 Negative regulation of glutathione transport into mitochondria is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of glutathione into mitochondria by means of some agent such as a transporter or pore. Negative regulation of glutathione transport into mitochondria HOIP_0004984 HOIP:HOIP_0004985 Negative regulation of glutathione transport into mitochondria is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of glutathione into mitochondria by means of some agent such as a transporter or pore. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 Negative regulation of glutathione transport into mitochondria [mitochondrial disorder (course)] HOIP_0004985 PMID:23299992 Indeed, increased mitochondrial cholesterol during NAFLD could reduce mitochondrial transport of GSH, thus inducing lower mtGSH levels and oxidative stress (Fig. 4). PMID:25339807 Depletion of mitochondrial GSH levels could also be due to its reduced uptake by mitochondria as a result of enhanced levels of cholesterol within the inner mitochondrial membrane and the decrease in synthesis of S-adenosylmethionine, the major methyl donor in liver and precursor to GSH. HOIP:HOIP_0004986 The directed movement of long-chain fatty acids into a mitochondria. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. long-chain fatty acid import into mitochondria HOIP_0004986 HOIP:HOIP_0004987 The directed movement of long-chain fatty acids into a mitochondria. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 long-chain fatty acid import into mitochondria [mitochondrial disorder (course)] HOIP_0004987 PMID:23299992 Whereas SCFAs and MCFAs freely enter mitochondria, the entry of LCFAs within these organelles requires different enzymes such as long‐chain acyl‐CoA synthetase (ACS), CPT1, and CPT2. For instance, LCFA‐mediated PPARα activation increases the expression of the mitochondrial enzymes CPT1 and medium‐chain acyl‐CoA dehydrogenase (MCAD). HOIP:HOIP_0004988 Hypofunction of mitochondrial repair is a subtype of hypofunctioning: A process that performs a decreased or insufficient mitochondrial repair. Hypofunction of mitochondrial repair HOIP_0004988 HOIP:HOIP_0004989 Increase in mitochondrial calcium level is a subtype of increase in calcium level: A process that changes the calcium ion concentration within a mitochondria to be higher. Increase in mitochondrial calcium level HOIP_0004989 HOIP:HOIP_0004990 Increase in mitochondrial calcium level is a subtype of increase in calcium level: A process that changes the calcium ion concentration within a mitochondria to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 Increase in mitochondrial calcium level [mitochondrial disorder (course)] HOIP_0004990 PMID:25339807 MPTP is defined as the sudden increase of mitochondrial inner membrane permeability to low molecular weight solutes (1.5 kDa) in response to many stimuli, including high levels of Ca2+ and oxidant stress. HOIP:HOIP_0004991 Mitochondrial cholesterol storage is a subtype of cholesterol storage: A process that keeps cholesterol in the mitochondria. mitochondrial cholesterol storage HOIP_0004991 HOIP:HOIP_0004992 Mitochondrial cholesterol storage is a subtype of cholesterol storage: A process that keeps cholesterol in the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 PMID:25339807 PMID:31623280 mitochondrial cholesterol storage [mitochondrial disorder (course)] HOIP_0004992 PMID:23299992 Indeed, increased mitochondrial cholesterol during NAFLD could reduce mitochondrial transport of GSH, thus inducing lower mtGSH levels and oxidative stress (Fig. 4). PMID:25339807 Depletion of mitochondrial GSH levels could also be due to its reduced uptake by mitochondria as a result of enhanced levels of cholesterol within the inner mitochondrial membrane and the decrease in synthesis of S-adenosylmethionine, the major methyl donor in liver and precursor to GSH. PMID:31623280 Bellanti et al. showed through targeted lipidomic analysis that rats fed diets rich in cholesterol exhibited increased toxic hepatic triol, which induces apoptosis and impaired mitochondrial respiration in vitro. Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. Moreover, mitochondrial-free cholesterol sensitizes liver cells to TNFα- and Fas-mediated steatohepatitis and causes mitochondrial-reduced glutathione (mGSH) depletion, which is also reported in animal models and patients with NASH. Thus, accumulating evidences suggest that cholesterol overload in mitochondria induces redox imbalances leading to oxidative stress and cell death associated with steatohepatitis. HOIP:HOIP_0004993 Negative regulation of mitochondrial respiratory chain complex I subunit phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex I subunit phosphorylation. Negative regulation of mitochondrial respiratory chain complex I subunit phosphorylation HOIP_0004993 HOIP:HOIP_0004994 Negative regulation of phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of phosphorylation. negative regulation of phosphorylation HOIP_0004994 HOIP:HOIP_0004995 mitochondrial respiratory chain complex I subunit phosphorylation HOIP_0004995 HOIP:HOIP_0004997 Dysregulation of mitochondrion organization is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of mitochondrion organization appropriately or cannot realize it at all. dysregulation of mitochondrion organization HOIP_0004997 HOIP:HOIP_0004998 mitochondrial membrane morphology changes is a subtype of mitochondria morphology changes: A process that changes the morphology of the mitochondrial membrane. mitochondrial membrane morphology changes HOIP_0004998 HOIP:HOIP_0004999 Increasing mitochondrial membrane potential is a subtype of increasing membrane potential: A process that changes the electrical potential of a mitochondrial membrane to be higher. Increasing mitochondrial membrane potential HOIP_0004999 HOIP:HOIP_0005000 Increasing membrane potential is a subtype of changing membrane potential: A process that changes the electrical potential across a membrane to be higher. Increasing membrane potential HOIP_0005000 HOIP:HOIP_0005001 Metalloprotease activation is a subtype of activating: A process that changes the activity of the metalloprotease to be higher. metalloprotease activation HOIP_0005001 HOIP:HOIP_0005004 Negative regulation of methionine metabolic process is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of methionine metabolic process. Negative regulation of methionine metabolic process HOIP_0005004 HOIP:HOIP_0005009 phospholipid peroxidation is a subtype of lipid oxidation: The degradation of phospholipids caused by an oxidative attack from free radicals. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 phospholipid peroxidation [mitochondrial disorder (course)] HOIP_0005009 PMID:25339807 Phospholipid peroxidation is considered an important contributing factor in mitochondrial dysfunction in several physiopathological conditions as well as during the aging process. In fact, phospholipid peroxidation alters the structural organization of the mitochondrial bilayer, perturbing membrane fluidity and permeability. HOIP:HOIP_0005011 Any process that results in a change in state of redox. redox change HOIP_0005011 HOIP:HOIP_0005012 Increasing leptin level is a subtype of increasing quantity: A process that changes the amount of leptin level to be higher. increasing leptin level HOIP_0005012 HOIP:HOIP_0005013 Increasing leptin level is a subtype of increasing quantity: A process that changes the amount of glucagon level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:23299992 increasing leptin level [mitochondrial disorder (course)] HOIP_0005013 PMID:23299992 Numerous studies showed increased expression of PPARα in fatty liver. Different cues such as FAs, leptin, and IL6 could activate PPARα and its target genes involved in mtFAO (CPT1, MCAD), peroxisomal FAO (acyl‐CoA oxidase), and VLDL production (microsomal triglyceride transfer protein). mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). HOIP:HOIP_0005015 Malfunctioning of centrosome duplication is a subtype of malfunctioning process: A process that cannot perform centrosome duplication appropriately or cannot realize it at all. malfunctioning of centrosome duplication HOIP_0005015 HOIP:HOIP_0005018 Dysregulation of immune balance is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of immune balance appropriately or cannot realize it at all. immune imbalance dysregulation of immune balance HOIP_0005018 HOIP:HOIP_0005020 The orderly movement of a regulatory T cell from one site to another. regulatory T cell migration HOIP_0005020 HOIP:HOIP_0005021 protooncogene activation is a subtype of activation: A process that changes the activity of the protooncogene to be higher. protooncogene activation HOIP_0005021 HOIP:HOIP_0005023 Increasing production amount of reactive aldehyde is a subtype of increasing quantity: A process that changes the production amount of reactive aldehyde to be higher. increasing production amount of reactive aldehyde HOIP_0005023 HOIP:HOIP_0005024 reactive aldehyde [mitochondrial disorder (course)] HOIP_0005024 HOIP:HOIP_0005025 A monounsaturated fatty aldehyde that is nonanal that has undergone dehydrogenation to introduce a double bond at any position in the aliphatic chain and in which a hydrogen at position 4 has been replaced by a hydroxy group. PMID:23299992 PMID:25339807 4-hydroxy-trans-2-nonenal 4-hydroxynonenal [mitochondrial disorder (course)] HOIP_0005025 PMID:23299992 Several MRC complexes including COX are sensitive to ROS and RNS. In addition, COX can be inhibited by low levels of NO and inactivated by 4‐hydroxynonenal (4‐HNE), a reactive aldehyde generated during lipid peroxidation. PMID:25339807 These compounds may undergo fragmentation to produce several reactive intermediates, among them, malondialdehyde and the most reactive 4-hydroxy-trans-2-nonenal. These two by-products of lipid peroxidation have been shown to interact with and inactivate ETC components, including cytochrome c oxidase, by forming adducts with this enzyme[, contributing to triggering mitochondrial dysfunction in NASH. HOIP:HOIP_0005027 Increasing uric acid level is a subtype of increasing quantity: A process that changes the amount of uric acid level to be higher. Increasing uric acid level HOIP_0005027 HOIP:HOIP_0005028 Hypofunction of immune response to tumor cell is a subtype of hypofunctioning: A process that performs a decreased or insufficient immune response to tumor cell. hypofunction of immune response to tumor cell HOIP_0005028 HOIP:HOIP_0005029 Negative regulation of antioxidant enzyme activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of antioxidant enzyme activation. negative regulation of antioxidant enzyme activation HOIP_0005029 HOIP:HOIP_0005030 Increasing damaged mitochondria is a subtype of increasing quantity: A process that changes the amount of damaged mitochondria to be higher. increasing damaged mitochondria HOIP_0005030 HOIP:HOIP_0005031 The process that results in the movement of inflammatory DAMPs from the mitochondria. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 release of inflammatory DAMPs [mitochondrial disorder (course)] HOIP_0005031 PMID:31623280 Prevention of autophagy further leads to accumulation of damaged mitochondria that can release inflammatory DAMPs and cytochrome C to promote cell death, and/or exacerbate endoplasmic reticulum (ER) stress. Reduced mitophagy results in the accumulation of severely damaged mitochondria, leading to cell necrosis releasing mitochondrial damage-associated molecular patterns (DAMPs) that can promote liver inflammation and NASH development. Mitochondrial DAMPs (MTDs) activate pattern recognition receptors (PRRs), such as Toll-like receptor (TLR)9. HOIP:HOIP_0005033 Malfunctioning of cytokinesis is a subtype of malfunctioning process: A process that cannot perform cytokinesis appropriately or cannot realize it at all. malfunctioning of cytokinesis HOIP_0005033 HOIP:HOIP_0005034 Increasing blood glucose level is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:26571396 hyperglycemia increasing blood glucose level [mitochondrial disorder (course)] HOIP_0005034 PMID:26571396 On the whole, the data indicate that increased flux through anaplerotic/cataplerotic pathways not only contributes to dysregulation of downstream nutrients (e.g., glycemia and lipidemia), but also triggers oxidative metabolism and altered antioxidant capacity that contribute to the development of oxidative stress, inflammation, and insulin resistance (Figure 8B and Supplemental Table 2). HOIP:HOIP_0005037 Hepatocyte regeneration is a subtype of changing material: The regrowth of lost or destroyed hepatocytes. hepatocyte regeneration HOIP_0005037 HOIP:HOIP_0005039 Increasing lipid concentration in blood is a subtype of increasing concentration: A process that changes the lipid concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:26571396 hyperlipidemia increasing lipid concentration [mitochondrial disorder (course)] HOIP_0005039 PMID:26571396 On the whole, the data indicate that increased flux through anaplerotic/cataplerotic pathways not only contributes to dysregulation of downstream nutrients (e.g., glycemia and lipidemia), but also triggers oxidative metabolism and altered antioxidant capacity that contribute to the development of oxidative stress, inflammation, and insulin resistance (Figure 8B and Supplemental Table 2). HOIP:HOIP_0005040 Tumor malignancy alteration is a subtype of changing quality of tumor: A process that changes the quality of the tumors to progress, invade surrounding tissues or metastasize. tumor malignancy alteration HOIP_0005040 HOIP:HOIP_0005041 A mebrane potential which is relatively high. increased membrane potential HOIP_0005041 HOIP:HOIP_0005042 Increasing cholesterol concentration in blood is a subtype of increasing lipid concentration in blood: A process that changes the cholesterol concentration in the blood to be higher. hypercholesterolemia Increasing cholesterol concentration in blood HOIP_0005042 HOIP:HOIP_0005043 Increasing lipid concentration in blood is a subtype of increasing concentration: A process that changes the lipid concentration in the blood to be higher. hyperlipidemia increasing lipid concentration HOIP_0005043 HOIP:HOIP_0005044 Increasing cholesterol concentration in blood is a subtype of increasing lipid concentration in blood: A process that changes the cholesterol concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 hypercholesterolemia Increasing cholesterol concentration in blood [mitochondrial disorder (course)] HOIP_0005044 PMID:31623280 More precisely, dietary-induced hypercholesterolemia causes oxidative stress, loss of mitochondrial membrane potential, reduction in ATP content, loss of mitochondrial cristae, and hepatic steatosis in mice. HOIP:HOIP_0005045 The movement of an endothelial progenitor cell (EPC) within or between different tissues and organs of the body. endothelial progenitor cell mobilization HOIP_0005045 HOIP:HOIP_0005046 A process that constructs blood vessels. angiogenesis vascularization HOIP_0005046 HOIP:HOIP_0005048 Enzyme production is a subtype of protein production: A process that makes existent of enzyme due to biosynthesis, secretion, or membrane trafficking, resulting in an increase in its levels. enzyme production HOIP_0005048 HOIP:HOIP_0005050 iron metabolic dysfunction is a subtype of Metabolic dysfunctioning: A process that performs an abnormal and incomplete energy metabolic function. iron metabolic dysfunction HOIP_0005050 HOIP:HOIP_0005052 Increasing iron uptake level is a subtype of increasing quantity: A process that changes the iron uptake level to be larger. Increasing iron uptake level HOIP_0005052 HOIP:HOIP_0005053 Hypofunction of heme biosynthesis is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient heme biosynthesis. hypofunction of heme biosynthesis HOIP_0005053 HOIP:HOIP_0005054 Increasing long-chain free fatty acid level is a subtype of increasing quantity: A process that changes the amount of long-chain free fatty acid level to be higher. Increasing long-chain free fatty acid level HOIP_0005054 HOIP:HOIP_0005055 Increasing long-chain free fatty acid level is a subtype of increasing quantity: A process that changes the amount of long-chain free fatty acid level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:25339807 Increasing long-chain free fatty acid level [mitochondrial disorder (course)] HOIP_0005055 PMID:25339807 Long-chain free fatty acids which accumulate in nonalcoholic fatty liver are considered the initial source of this ROS damaging cycle. These compounds have been shown to promote ROS production in mitochondria, although the mechanism(s) underlying this effect is still unclear. HOIP:HOIP_0005056 Increasing saturated fatty acid level is a subtype of increasing quantity: A process that changes the amount of saturated fatty acid level to be higher. increasing saturated fatty acid level HOIP_0005056 HOIP:HOIP_0005057 Increasing saturated fatty acid level is a subtype of increasing quantity: A process that changes the amount of saturated fatty acid level to be higher. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31623280 Increasing saturated fatty acid level [mitochondrial disorder (course)] HOIP_0005057 PMID:31623280 Saturated fats promote fatty liver and accumulation of lipotoxic byproducts including ceramides and diacylglycerols is associated with hepatic inflammation and mitochondrial ROS production resulting in liver cell death. Moreover, in vitro treatment of liver cells with saturated fatty acids (palmitic and stearic acids) reproduces mitochondrial dysfunction found in NASH, including decreasing cellular ATP content and mtDNA-encoded oxidative phosphorylation (OXPHOS) subunit expression, coupled with increased oxidative stress. HOIP:HOIP_0005058 saturated fatty acid [mitochondrial disorder (course)] HOIP_0005058 HOIP:HOIP_0005059 Hypofunction of phospholipid degradation is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient phospholipid degradation. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (latent). hypofunction of phospholipid degradation [Phospholipidosis(latent)] HOIP_0005059 HOIP:HOIP_0005061 Hypofunction of 17β-Estradiol metabolic process is a subtype of hypofunction of metabolism: A process that performs a decreased or insufficient 17β-Estradiol metabolic process. Hypofunction of 17β-Estradiol metabolic process HOIP_0005061 HOIP:HOIP_0005064 A series of molecular signals mediated by AGGF1 (angiogenic factor with G-patch and FHA domains 1). AGGF1 signal transduction pathway HOIP_0005064 HOIP:HOIP_0005065 AGGF1 signaling is a process that a signal is transmitted by AGGF1. AGGF1 signaling HOIP_0005065 HOIP:HOIP_0005066 NCBI-Human-GeneID:5562 NCBI-Mouse-GeneID:105787 NCBI-Rat-GeneID:65248 AMPK(canonical) [mitochondrial disorder (course)] HOIP_0005066 NCBI-Human-GeneID:5562 http://www.ncbi.nlm.nih.gov/gene/5562 NCBI-Mouse-GeneID:105787 http://www.ncbi.nlm.nih.gov/gene/105787 NCBI-Rat-GeneID:65248 http://www.ncbi.nlm.nih.gov/gene/65248 HOIP:HOIP_0005068 NCBI-Human-GeneID:8678 NCBI-Mouse-GeneID:56208 NCBI-Rat-GeneID:114558 BECN1 (mol) HOIP_0005068 NCBI-Human-GeneID:8678 http://www.ncbi.nlm.nih.gov/gene/8678 NCBI-Mouse-GeneID:56208 http://www.ncbi.nlm.nih.gov/gene/56208 NCBI-Rat-GeneID:114558 http://www.ncbi.nlm.nih.gov/gene/114558 HOIP:HOIP_0005069 NCBI-Human-GeneID:23705 NCBI-Mouse-GeneID:54725 NCBI-Rat-GeneID:363058 TSLC1 CADM1 (mol) HOIP_0005069 NCBI-Human-GeneID:23705 http://www.ncbi.nlm.nih.gov/gene/23705 NCBI-Mouse-GeneID:54725 http://www.ncbi.nlm.nih.gov/gene/54725 NCBI-Rat-GeneID:363058 http://www.ncbi.nlm.nih.gov/gene/363058 HOIP:HOIP_0005076 NCBI-Human-GeneID:1553 CYP2A13 (mol) HOIP_0005076 NCBI-Human-GeneID:1553 http://www.ncbi.nlm.nih.gov/gene/1553 HOIP:HOIP_0005077 NCBI-Human-GeneID:1548 CYP2A6 (mol) HOIP_0005077 NCBI-Human-GeneID:1548 http://www.ncbi.nlm.nih.gov/gene/1548 HOIP:HOIP_0005078 NCBI-Human-GeneID:1551 CYP3A7 (mol) HOIP_0005078 NCBI-Human-GeneID:1551 http://www.ncbi.nlm.nih.gov/gene/1551 HOIP:HOIP_0005079 NCBI-Human-GeneID:23136 NCBI-Mouse-GeneID:13823 NCBI-Rat-GeneID:116724 DAL-1 differentially expressed in adenocarcinoma of the lung 1 EPB41L3 (mol) HOIP_0005079 NCBI-Human-GeneID:23136 https://www.ncbi.nlm.nih.gov/gene/23136 NCBI-Mouse-GeneID:13823 http://www.ncbi.nlm.nih.gov/gene/13823 NCBI-Rat-GeneID:116724 http://www.ncbi.nlm.nih.gov/gene/116724 HOIP:HOIP_0005081 NCBI-Human-GeneID:8321 NCBI-Mouse-GeneID:14362 NCBI-Rat-GeneID:58868 FZD1 (mol) HOIP_0005081 NCBI-Human-GeneID:8321 http://www.ncbi.nlm.nih.gov/gene/8321 NCBI-Mouse-GeneID:14362 http://www.ncbi.nlm.nih.gov/gene/14362 NCBI-Rat-GeneID:58868 http://www.ncbi.nlm.nih.gov/gene/58868 HOIP:HOIP_0005082 NCBI-Human-GeneID:2535 NCBI-Mouse-GeneID:57265 NCBI-Rat-GeneID:64512 FZD2 (mol) HOIP_0005082 NCBI-Human-GeneID:2535 http://www.ncbi.nlm.nih.gov/gene/2535 NCBI-Mouse-GeneID:57265 http://www.ncbi.nlm.nih.gov/gene/57265 NCBI-Rat-GeneID:64512 http://www.ncbi.nlm.nih.gov/gene/64512 HOIP:HOIP_0005083 NCBI-Human-GeneID:7855 NCBI-Mouse-GeneID:14367 NCBI-Rat-GeneID:317674 FZD5 (mol) HOIP_0005083 NCBI-Human-GeneID:7855 http://www.ncbi.nlm.nih.gov/gene/7855 NCBI-Mouse-GeneID:14367 http://www.ncbi.nlm.nih.gov/gene/14367 NCBI-Rat-GeneID:317674 http://www.ncbi.nlm.nih.gov/gene/317674 HOIP:HOIP_0005084 NCBI-Human-GeneID:8323 NCBI-Mouse-GeneID:14368 NCBI-Rat-GeneID:282581 FZD6 (mol) HOIP_0005084 NCBI-Human-GeneID:8323 http://www.ncbi.nlm.nih.gov/gene/8323 NCBI-Mouse-GeneID:14368 http://www.ncbi.nlm.nih.gov/gene/14368 NCBI-Rat-GeneID:282581 http://www.ncbi.nlm.nih.gov/gene/282581 HOIP:HOIP_0005085 NCBI-Human-GeneID:8324 NCBI-Mouse-GeneID:14369 NCBI-Rat-GeneID:100360552 FZD7 (mol) HOIP_0005085 NCBI-Human-GeneID:8324 http://www.ncbi.nlm.nih.gov/gene/8324 NCBI-Mouse-GeneID:14369 http://www.ncbi.nlm.nih.gov/gene/14369 NCBI-Rat-GeneID:100360552 http://www.ncbi.nlm.nih.gov/gene/100360552 HOIP:HOIP_0005086 NCBI-Human-GeneID:8326 NCBI-Mouse-GeneID:14371 NCBI-Rat-GeneID:266608 FZD9 (mol) HOIP_0005086 NCBI-Human-GeneID:8326 http://www.ncbi.nlm.nih.gov/gene/8326 NCBI-Mouse-GeneID:14371 http://www.ncbi.nlm.nih.gov/gene/14371 NCBI-Rat-GeneID:266608 http://www.ncbi.nlm.nih.gov/gene/266608 HOIP:HOIP_0005087 NCBI-Human-GeneID:2697 NCBI-Mouse-GeneID:14609 NCBI-Rat-GeneID:24392 CX43 GJA1 (mol) HOIP_0005087 NCBI-Human-GeneID:2697 http://www.ncbi.nlm.nih.gov/gene/2697 NCBI-Mouse-GeneID:14609 http://www.ncbi.nlm.nih.gov/gene/14609 NCBI-Rat-GeneID:24392 http://www.ncbi.nlm.nih.gov/gene/24392 HOIP:HOIP_0005088 NCBI-Human-GeneID:2705 NCBI-Mouse-GeneID:14618 NCBI-Rat-GeneID:29584 CX32 GJB1 (mol) HOIP_0005088 NCBI-Human-GeneID:2705 http://www.ncbi.nlm.nih.gov/gene/2705 NCBI-Mouse-GeneID:14618 http://www.ncbi.nlm.nih.gov/gene/14618 NCBI-Rat-GeneID:29584 http://www.ncbi.nlm.nih.gov/gene/29584 HOIP:HOIP_0005090 NCBI-Human-GeneID:3091 NCBI-Mouse-GeneID:15251 NCBI-Rat-GeneID:29560 HIF1A(canonical) [mitochondrial disorder (course)] HOIP_0005090 NCBI-Human-GeneID:3091 http://www.ncbi.nlm.nih.gov/gene/3091 NCBI-Mouse-GeneID:15251 http://www.ncbi.nlm.nih.gov/gene/15251 NCBI-Rat-GeneID:29560 http://www.ncbi.nlm.nih.gov/gene/29560 HOIP:HOIP_0005092 NCBI-Human-GeneID:100124700 NCBI-Mouse-GeneID:100503872 HOTAIR (mol) HOIP_0005092 NCBI-Human-GeneID:100124700 http://www.ncbi.nlm.nih.gov/gene/100124700 NCBI-Mouse-GeneID:100503872 http://www.ncbi.nlm.nih.gov/gene/100503872 HOIP:HOIP_0005093 NCBI-Human-GeneID:4485 NCBI-Mouse-GeneID:15235 NCBI-Rat-GeneID:24566 MST1 (mol) HOIP_0005093 NCBI-Human-GeneID:4485 http://www.ncbi.nlm.nih.gov/gene/4485 NCBI-Mouse-GeneID:15235 http://www.ncbi.nlm.nih.gov/gene/15235 NCBI-Rat-GeneID:24566 http://www.ncbi.nlm.nih.gov/gene/24566 HOIP:HOIP_0005094 NCBI-Human-GeneID:6788 NCBI-Mouse-GeneID:56274 NCBI-Rat-GeneID:65189 MST2 STK3 (mol) HOIP_0005094 NCBI-Human-GeneID:6788 http://www.ncbi.nlm.nih.gov/gene/6788 NCBI-Mouse-GeneID:56274 http://www.ncbi.nlm.nih.gov/gene/56274 NCBI-Rat-GeneID:65189 http://www.ncbi.nlm.nih.gov/gene/65189 HOIP:HOIP_0005096 NCBI-Human-GeneID:3791 NCBI-Mouse-GeneID:16542 NCBI-Rat-GeneID:25589 VEGFR2 KDR (mol) HOIP_0005096 NCBI-Human-GeneID:3791 http://www.ncbi.nlm.nih.gov/gene/3791 NCBI-Mouse-GeneID:16542 http://www.ncbi.nlm.nih.gov/gene/16542 NCBI-Rat-GeneID:25589 http://www.ncbi.nlm.nih.gov/gene/25589 HOIP:HOIP_0005098 NCBI-Human-GeneID:4233 NCBI-Mouse-GeneID:17295 NCBI-Rat-GeneID:24553 HGFR MET (mol) HOIP_0005098 NCBI-Human-GeneID:4233 http://www.ncbi.nlm.nih.gov/gene/4233 NCBI-Mouse-GeneID:17295 http://www.ncbi.nlm.nih.gov/gene/17295 NCBI-Rat-GeneID:24553 http://www.ncbi.nlm.nih.gov/gene/24553 HOIP:HOIP_0005100 NCBI-Human-GeneID:4436 NCBI-Mouse-GeneID:17685 NCBI-Rat-GeneID:81709 MSH2 (mol) HOIP_0005100 NCBI-Human-GeneID:4436 http://www.ncbi.nlm.nih.gov/gene/4436 NCBI-Mouse-GeneID:17685 http://www.ncbi.nlm.nih.gov/gene/17685 NCBI-Rat-GeneID:81709 http://www.ncbi.nlm.nih.gov/gene/81709 HOIP:HOIP_0005102 NCBI-Human-GeneID:2956 NCBI-Mouse-GeneID:17688 NCBI-Rat-GeneID:100360342 MSH6 (mol) HOIP_0005102 NCBI-Human-GeneID:2956 http://www.ncbi.nlm.nih.gov/gene/2956 NCBI-Mouse-GeneID:17688 http://www.ncbi.nlm.nih.gov/gene/17688 NCBI-Rat-GeneID:100360342 http://www.ncbi.nlm.nih.gov/gene/100360342 HOIP:HOIP_0005103 NCBI-Human-GeneID:4507 NCBI-Mouse-GeneID:66902 NCBI-Rat-GeneID:298227 MTAP (mol) HOIP_0005103 NCBI-Human-GeneID:4507 https://www.ncbi.nlm.nih.gov/gene/4507 NCBI-Mouse-GeneID:66902 http://www.ncbi.nlm.nih.gov/gene/66902 NCBI-Rat-GeneID:298227 http://www.ncbi.nlm.nih.gov/gene/298227 HOIP:HOIP_0005104 NCBI-Human-GeneID:55967 NDUFA12 (human) [mitochondrial disorder (course)] HOIP_0005104 NCBI-Human-GeneID:55967 http://www.ncbi.nlm.nih.gov/gene/55967 HOIP:HOIP_0005105 NCBI-Human-GeneID:55967 PMID:24746669 NDUFA12 - inactive form (human)[mitochondrial disorder (course)] HOIP_0005105 NCBI-Human-GeneID:55967 http://www.ncbi.nlm.nih.gov/gene/55967 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005106 NDUFA12 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFA12 (NADH:ubiquinone oxidoreductase core subunit A12) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 NDUFA12 inactivation [mitochondrial disorder (course)] HOIP_0005106 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005107 NCBI-Human-GeneID:4712 NDUFB6 (human) [mitochondrial disorder (course)] HOIP_0005107 NCBI-Human-GeneID:4712 http://www.ncbi.nlm.nih.gov/gene/4712 HOIP:HOIP_0005108 NCBI-Human-GeneID:4712 PMID:24746669 NDUFB6 - inactive form (human)[mitochondrial disorder (course)] HOIP_0005108 NCBI-Human-GeneID:4712 http://www.ncbi.nlm.nih.gov/gene/4712 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005109 NDUFB6 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFB6 (NADH:ubiquinone oxidoreductase core subunit B6) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 NDUFB6 inactivation [mitochondrial disorder (course)] HOIP_0005109 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005110 NCBI-Human-GeneID:4720 NDUFS2 (human) [mitochondrial disorder (course)] HOIP_0005110 NCBI-Human-GeneID:4720 http://www.ncbi.nlm.nih.gov/gene/4720 HOIP:HOIP_0005111 NCBI-Human-GeneID:4720 PMID:24746669 NDUFS2 - inactive form (human)[mitochondrial disorder (course)] HOIP_0005111 NCBI-Human-GeneID:4720 http://www.ncbi.nlm.nih.gov/gene/4720 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005112 NDUFS2 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFS2 (NADH:ubiquinone oxidoreductase core subunit S2) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 NDUFS2 inactivation [mitochondrial disorder (course)] HOIP_0005112 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005113 NCBI-Human-GeneID:4723 NDUFV1 (human) [mitochondrial disorder (course)] HOIP_0005113 NCBI-Human-GeneID:4723 http://www.ncbi.nlm.nih.gov/gene/4723 HOIP:HOIP_0005114 NCBI-Human-GeneID:4723 PMID:24746669 NDUFV1 - inactive form (human)[mitochondrial disorder (course)] HOIP_0005114 NCBI-Human-GeneID:4723 http://www.ncbi.nlm.nih.gov/gene/4723 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005115 NDUFV1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFV1 (NADH:ubiquinone oxidoreductase core subunit V1) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 NDUFV1 inactivation [mitochondrial disorder (course)] HOIP_0005115 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005116 NCBI-Human-GeneID:4731 NDUFV3 (human) [mitochondrial disorder (course)] HOIP_0005116 NCBI-Human-GeneID:4731 http://www.ncbi.nlm.nih.gov/gene/4731 HOIP:HOIP_0005117 NCBI-Human-GeneID:4731 PMID:24746669 NDUFV3 - inactive form (human)[mitochondrial disorder (course)] HOIP_0005117 NCBI-Human-GeneID:4731 http://www.ncbi.nlm.nih.gov/gene/4731 PMID:24746669 not reported in the liver. These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). HOIP:HOIP_0005118 NDUFV3 inactivation is a subtype of molecular inactivation: A process that changes the activity of the NDUFV3 (NADH:ubiquinone oxidoreductase core subunit V3) to be lower. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:24746669 NDUFV3 inactovation [mitochondrial disorder (course)] HOIP_0005118 PMID:24746669 These results were repeated and confirmed by generating phosphorylation defective forms of these 5 CI subunits through substitutions of Serine/Threonine (S/T) residues with Alanine (A) on either Cdk1 optimal or minimal consensus motifs (T383 on NDUFV1, S105 on NDUFV3, S364 on NDUFS2, S55/S29/T5 on NDUFB6 and T142/T120 on NDUFA12). The mutation of Cdk1 consensus motifs severely diminished their phosphorylation (Figure 3F). not reported in the liver. HOIP:HOIP_0005119 NCBI-Human-GeneID:4843 NCBI-Mouse-GeneID:18126 NCBI-Rat-GeneID:24599 nitric oxide synthase 2 NOS2 (mol) HOIP_0005119 NCBI-Human-GeneID:4843 http://www.ncbi.nlm.nih.gov/gene/4843 NCBI-Mouse-GeneID:18126 http://www.ncbi.nlm.nih.gov/gene/18126 NCBI-Rat-GeneID:24599 http://www.ncbi.nlm.nih.gov/gene/24599 HOIP:HOIP_0005120 NCBI-Human-GeneID:4780 NCBI-Mouse-GeneID:18024 NCBI-Rat-GeneID:83619 NRF2(canonical) [mitochondrial disorder (course)] HOIP_0005120 NCBI-Human-GeneID:4780 http://www.ncbi.nlm.nih.gov/gene/4780 NCBI-Mouse-GeneID:18024 http://www.ncbi.nlm.nih.gov/gene/18024 NCBI-Rat-GeneID:83619 http://www.ncbi.nlm.nih.gov/gene/83619 HOIP:HOIP_0005125 NCBI-Human-GeneID:5465 NCBI-Mouse-GeneID:19013 NCBI-Rat-GeneID:25747 PMID:23299992 PPARA(canonical) [mitochondrial disorder (course)] HOIP_0005125 NCBI-Human-GeneID:5465 http://www.ncbi.nlm.nih.gov/gene/5465 NCBI-Mouse-GeneID:19013 http://www.ncbi.nlm.nih.gov/gene/19013 NCBI-Rat-GeneID:25747 http://www.ncbi.nlm.nih.gov/gene/25747 PMID:23299992 Numerous studies showed increased expression of PPARα in fatty liver. Different cues such as FAs, leptin, and IL6 could activate PPARα and its target genes involved in mtFAO (CPT1, MCAD), peroxisomal FAO (acyl‐CoA oxidase), and VLDL production (microsomal triglyceride transfer protein). mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). For instance, LCFA‐mediated PPARα activation increases the expression of the mitochondrial enzymes CPT1 and medium‐chain acyl‐CoA dehydrogenase (MCAD). HOIP:HOIP_0005127 NCBI-Human-GeneID:10891 NCBI-Mouse-GeneID:19017 NCBI-Rat-GeneID:83516 PPARGC1A (mol) HOIP_0005127 NCBI-Human-GeneID:10891 http://www.ncbi.nlm.nih.gov/gene/10891 NCBI-Mouse-GeneID:19017 http://www.ncbi.nlm.nih.gov/gene/19017 NCBI-Rat-GeneID:83516 http://www.ncbi.nlm.nih.gov/gene/83516 HOIP:HOIP_0005128 NCBI-Human-GeneID:10544 NCBI-Mouse-GeneID:19124 NCBI-Rat-GeneID:362248 PROCR (mol) HOIP_0005128 NCBI-Human-GeneID:10544 http://www.ncbi.nlm.nih.gov/gene/10544 NCBI-Mouse-GeneID:19124 http://www.ncbi.nlm.nih.gov/gene/19124 NCBI-Rat-GeneID:362248 http://www.ncbi.nlm.nih.gov/gene/362248 HOIP:HOIP_0005130 NCBI-Human-GeneID:5747 NCBI-Mouse-GeneID:14083 NCBI-Rat-GeneID:25614 FAK PTK2 (mol) HOIP_0005130 NCBI-Human-GeneID:5747 http://www.ncbi.nlm.nih.gov/gene/5747 NCBI-Mouse-GeneID:14083 http://www.ncbi.nlm.nih.gov/gene/14083 NCBI-Rat-GeneID:25614 http://www.ncbi.nlm.nih.gov/gene/25614 HOIP:HOIP_0005132 NCBI-Human-GeneID:6615 NCBI-Mouse-GeneID:20613 NCBI-Rat-GeneID:116490 Snail SNAI1 (mol) HOIP_0005132 NCBI-Human-GeneID:6615 http://www.ncbi.nlm.nih.gov/gene/6615 NCBI-Mouse-GeneID:20613 http://www.ncbi.nlm.nih.gov/gene/20613 NCBI-Rat-GeneID:116490 http://www.ncbi.nlm.nih.gov/gene/116490 HOIP:HOIP_0005134 NCBI-Human-GeneID:7019 NCBI-Mouse-GeneID:21780 NCBI-Rat-GeneID:83474 TFAM (mol) HOIP_0005134 NCBI-Human-GeneID:7019 http://www.ncbi.nlm.nih.gov/gene/7019 NCBI-Mouse-GeneID:21780 http://www.ncbi.nlm.nih.gov/gene/21780 NCBI-Rat-GeneID:83474 http://www.ncbi.nlm.nih.gov/gene/83474 HOIP:HOIP_0005135 NCBI-Human-GeneID:7039 NCBI-Mouse-GeneID:21802 NCBI-Rat-GeneID:24827 TGFA (mol) HOIP_0005135 NCBI-Human-GeneID:7039 http://www.ncbi.nlm.nih.gov/gene/7039 NCBI-Mouse-GeneID:21802 http://www.ncbi.nlm.nih.gov/gene/21802 NCBI-Rat-GeneID:24827 http://www.ncbi.nlm.nih.gov/gene/24827 HOIP:HOIP_0005136 A protein that is a translation product of the human USP7 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7874 NCBI-Mouse-GeneID:252870 NCBI-Rat-GeneID:360471 USP7 ubiquitin specific peptidase 7 ubiquitin carboxyl-terminal hydrolase 7 HOIP_0005136 NCBI-Human-GeneID:7874 http://www.ncbi.nlm.nih.gov/gene/7874 NCBI-Mouse-GeneID:252870 https://www.ncbi.nlm.nih.gov/gene/252870 NCBI-Rat-GeneID:360471 https://www.ncbi.nlm.nih.gov/gene/360471 HOIP:HOIP_0005137 NCBI-Human-GeneID:10413 NCBI-Mouse-GeneID:22601 NCBI-Rat-GeneID:363014 YAP YAP1 (mol) HOIP_0005137 NCBI-Human-GeneID:10413 http://www.ncbi.nlm.nih.gov/gene/10413 NCBI-Mouse-GeneID:22601 http://www.ncbi.nlm.nih.gov/gene/22601 NCBI-Rat-GeneID:363014 http://www.ncbi.nlm.nih.gov/gene/363014 HOIP:HOIP_0005139 The process that results in the movement of inflammatory DAMPs from the mitochondria. release of inflammatory DAMPs HOIP_0005139 HOIP:HOIP_0005140 From Drug Induced Liver Injury Rank (DILIrank) Dataset. DILIrank consists of 1,036 FDA-approved drugs that are divided into four classes according to their potential for causing drug-induced liver injury (DILI). Less-DILI-Concern HOIP_0005140 HOIP:HOIP_0005141 Tumor malignancy alteration is a subtype of changing quality: A process that changes the tumor malignancy. Changing quality of tumor is a subtype of changing quality: A process that changes the quailty of tumor cells. changing quality of tumor HOIP_0005141 HOIP:HOIP_0005142 From Drug Induced Liver Injury Rank (DILIrank) Dataset. DILIrank consists of 1,036 FDA-approved drugs that are divided into four classes according to their potential for causing drug-induced liver injury (DILI). No-DILI-Concern HOIP_0005142 HOIP:HOIP_0005143 Sphingomyelin homeostasis imbalance is a subtype of lipid homeostasis imbalance: A process that becomes lacking a phospholipid homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of Niemann Pick Disease Type A. central nervous system sphingomyelin homeostasis imbalance [course of Niemann–Pick disease type A] HOIP_0005143 HOIP:HOIP_0005144 indomethacin HOIP_0005144 HOIP:HOIP_0005145 rifampin HOIP_0005145 HOIP:HOIP_0005146 dactinomycin HOIP_0005146 HOIP:HOIP_0005147 methyldopa HOIP_0005147 HOIP:HOIP_0005148 propylthiouracil HOIP_0005148 HOIP:HOIP_0005149 isoniazid HOIP_0005149 HOIP:HOIP_0005150 niacin HOIP_0005150 HOIP:HOIP_0005151 cyclosporine HOIP_0005151 HOIP:HOIP_0005152 aminosalicylic acid HOIP_0005152 HOIP:HOIP_0005153 entecavir HOIP_0005153 HOIP:HOIP_0005154 nilotinib hydrochloride monohydrate HOIP_0005154 HOIP:HOIP_0005155 ticrynafen HOIP_0005155 HOIP:HOIP_0005157 dronedarone hydrochloride HOIP_0005157 HOIP:HOIP_0005158 divalproex sodium HOIP_0005158 HOIP:HOIP_0005161 triacetyldiphenolisatin HOIP_0005161 HOIP:HOIP_0005162 fiduxosin HOIP_0005162 HOIP:HOIP_0005163 pafuramidine HOIP_0005163 HOIP:HOIP_0005164 phenoxypropazine HOIP_0005164 HOIP:HOIP_0005165 azacitidine HOIP_0005165 HOIP:HOIP_0005166 cinchophen HOIP_0005166 HOIP:HOIP_0005167 exifone HOIP_0005167 HOIP:HOIP_0005168 fipexide HOIP_0005168 HOIP:HOIP_0005169 isocarboxazid HOIP_0005169 HOIP:HOIP_0005170 moxisylyte HOIP_0005170 HOIP:HOIP_0005171 nialamide HOIP_0005171 HOIP:HOIP_0005172 pentostatin HOIP_0005172 HOIP:HOIP_0005173 suloctidil HOIP_0005173 HOIP:HOIP_0005174 fenclozic acid HOIP_0005174 HOIP:HOIP_0005175 tetrabamate HOIP_0005175 HOIP:HOIP_0005176 xenazoic acid HOIP_0005176 HOIP:HOIP_0005177 falnidamol HOIP_0005177 HOIP:HOIP_0005178 mepazine HOIP_0005178 HOIP:HOIP_0005179 alaproclate HOIP_0005179 HOIP:HOIP_0005180 DrugBank:DB00056 gemtuzumab ozogamicin HOIP_0005180 HOIP:HOIP_0005182 DrugBank:DB00105 interferon alfa-2b HOIP_0005182 HOIP:HOIP_0005183 DrugBank:DB00060 interferon beta-1a HOIP_0005183 HOIP:HOIP_0005184 DrugBank:DB00069 interferon alfacon-1 HOIP_0005184 HOIP:HOIP_0005186 DrugBank:DB00022 peginterferon alfa-2b HOIP_0005186 HOIP:HOIP_0005187 DrugBank:DB00108 natalizumab HOIP_0005187 HOIP:HOIP_0005188 DrugBank:DB06268 sitaxsentan HOIP_0005188 HOIP:HOIP_0005189 The chemical reactions and pathways resulting in the formation of phospholipids, any lipid containing phosphoric acid as a mono- or diester. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis(latent). phospholipid biosynthetic process [Phospholipidosis(latent)] HOIP_0005189 HOIP:HOIP_0031002 The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli. This process can constitute the course of severe COVID-19. platelet activating factor biosynthetic process (very high) in severe COVID-19 HOIP_0031002 HOIP:HOIP_0031005 The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli. platelet activating factor biosynthetic process HOIP_0031005 HOIP:HOIP_0031006 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. This process can constitute the course of coronavirus infectious disease (homeostatic balance). Wikipedia:Coagulation blood clotting blood coagulation in coronavirus infectious disease (homeostatic balance) HOIP_0031006 HOIP:HOIP_0031007 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. Wikipedia:Coagulation blood clotting blood coagulationin COVID-19 (homeostatic balance) HOIP_0031007 HOIP:HOIP_0031008 A protein activation cascade that contributes to blood coagulation. blood coagulation pathway HOIP_0031008 HOIP:HOIP_0031009 Increasing D-dimer concentration is a subtype of increasing concentration: A process that changes the D-dimer concentration to be higher. increasing D-dimer concentration HOIP_0031009 HOIP:HOIP_0031010 The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli. This process can constitute the course of COVID-19. platelet activating factor biosynthetic process in COVID-19 HOIP_0031010 HOIP:HOIP_0031013 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. This process can constitute the course of COVID-19. PMID:32339221 PMID:32629875 PMID:33077917 Wikipedia:Coagulation blood clotting blood coagulation in COVID-19 HOIP_0031013 PMID:32339221 The initial coagulopathy of COVID-19 presents with prominent elevation of D-dimer and fibrin/fibrinogen-degradation products, whereas abnormalities in prothrombin time, partial thromboplastin time, and platelet counts are relatively uncommon in initial presentations. Coagulation test screening, including the measurement of D-dimer and fibrinogen levels, is suggested. PMID:32629875 Since soluble IL-6R is abnormally elevated in the plasma of COVID-19 patients, presumably secondary to cleavage from the cells surface by TACE/ADAM17 upon SARS-CoV-2 infection and the inflammatory response associated with COVID-19, IL-6 can activate most cells, including endothelial cells, which do not express endogenous IL-6R but can be activated by the complex of soluble IL-6R and IL-6. In COVID-19, adding to the blood clotting risk from increased IL-6, SARS-CoV-2 can infect, replicate and induce endothelial cell death, compromising the continuity of the luminal vascular surface; a perturbed endothelium can actively participate in pro-coagulant reactions. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0031026 A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is very low. Wikipedia:Fibrinolysis fibrinolysis (very low) in severe COVID-19 HOIP_0031026 HOIP:HOIP_0031030 Negative regulation of fibrinolysis is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of fibrinolysis. This process can constitute the course of severe COVID-19. negative regulation of fibrinolysisin severe COVID-19 HOIP_0031030 HOIP:HOIP_0031031 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This process can constitute the course of coronavirus infectious disease (homeostatic balance). apoptotic process in coronavirus infectious disease (homeostatic balance) HOIP_0031031 HOIP:HOIP_0031032 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This process can constitute the course of COVID-19 (homeostatic balance). apoptotic process in COVID-19 (homeostatic balance) HOIP_0031032 HOIP:HOIP_0031033 D-dimer is a fibrin degradation product, a small protein fragment in the blood after blood clot degradation by fibrinolysis. It contaims two D fragemts of the fibrin protein joined by a cross-link. D-dimer HOIP_0031033 HOIP:HOIP_0031034 An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). This process can constitute the course of coronavirus infectious disease (homeostatic balance). adaptive immune response in coronavirus infectious disease (homeostatic balance) HOIP_0031034 HOIP:HOIP_0031035 An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). This process can constitute the course of COVID-19 (homeostatic balance). adaptive immune response in COVID-19 (homeostatic balance) HOIP_0031035 HOIP:HOIP_0031036 A substance used as an indicator of the blood coagulation. blood coagulation marker HOIP_0031036 HOIP:HOIP_0031037 D-dimer is a fibrin degradation product, a small protein fragment in the blood after blood clot degradation by fibrinolysis. It contaims two D fragemts of the fibrin protein joined by a cross-link. D-dimer(human)in severe COVID-19 HOIP_0031037 HOIP:HOIP_0031038 Microthrombus formation is a subtype of thrombus formation: A process that construcs microthrombus. microthrombus formation HOIP_0031038 HOIP:HOIP_0031040 Microthrombus formation is a subtype of thrombus formation: A process that construcs microthrombus. This process can constitute the course of COVID-19. microthrombus formation in COVID-19 HOIP_0031040 HOIP:HOIP_0031042 The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration. entry receptor-mediated virion attachment to host cell in MERS HOIP_0031042 HOIP:HOIP_0031043 Interacting selectively and non-covalently with a receptor on the host cell surface host cell surface receptor binding in MERS HOIP_0031043 HOIP:HOIP_0031044 Interacting selectively and non-covalently with a virion, either by binding to components of the capsid or the viral envelope. virion binding with host cell surface receptor in MERS HOIP_0031044 HOIP:HOIP_0031046 Any compound that inhibits the viral genome replication viral genome replication inhibitor HOIP_0031046 HOIP:HOIP_0031048 Negative regulation of incretin hydrolysis is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of incretin hydrolysis. negative regulation of incretin hydrolysis HOIP_0031048 HOIP:HOIP_0031049 Negative regulation of incretin hydrolysis is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of incretin hydrolysis. negative regulation of incretin hydrolysis in MERS HOIP_0031049 HOIP:HOIP_0031050 incretin hydrolysis is a subtype of hydrolysis: A chemical reaction that uses water to break down a incretin incretin hydrolysis in MERS HOIP_0031050 HOIP:HOIP_0031054 A RNA polymerase inhibitor that interferes with the activity of RNA-directed RNA polymerase, a viral RNA polymerase enzyme. RNA dependent RNA polymerase inhibitor RdRp inhibitor RNA-directed RNA polymerase inhibitor HOIP_0031054 HOIP:HOIP_0031055 An EC 2.7.7.* (nucleotidyltransferase) inhibitor that interferes with the action of RNA polymerase (EC 2.7.7.6). EC 2.7.7.6 (RNA polymerase) inhibitor HOIP_0031055 HOIP:HOIP_0031058 Any process that decreases the rate, frequency or extent of viral protein maturation by peptide bond cleavage. negative regulation of viral protein processing HOIP_0031058 HOIP:HOIP_0031059 Any process that decreases the rate, frequency or extent of viral polyprotein maturation by peptide bond cleavage. negative regulation of viral polyprotein processing HOIP_0031059 HOIP:HOIP_0031060 The cleavage of a peptide bond or bonds within a viral polyprotein. viral polyprotein processing HOIP_0031060 HOIP:HOIP_0031061 Any process that decreases the rate, frequency or extent of viral polyprotein maturation by peptide bond cleavage. PMID:33077917 negative regulation of viral polyprotein processing in COVID-19 drug treatment HOIP_0031061 PMID:33077917 The combination of HIV protease inhibitors lopinavir/ritonavir has also been investigated for their ability to treat COVID-19. However, these drugs specifically inhibit the HIV aspartyl protease (retropepsin), an enzyme that is essential HIV virion maturation. Consistent with this high selectivity, a randomized, controlled, open-label trial reported no differences between treatment with lopinavir/ritonavir and standard care in time to clinical improvement. Given the lack of specific SARS-CoV-2 protease inhibitors, preclinical studies are underway to develop more effective antiviral treatments for COVID-19, including a specific inhibitor of the SARS-CoV-2 protease Mpro (also called 3CLpro),although it may be some time before these novel targeted drugs are available for use in humans. HOIP:HOIP_0031063 A process that performs a decreased or insufficient of the cleavage of a peptide bond or bonds within a viral polyprotein. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. hypofunction of viral polyprotein processing [COVID-19 with drug] viral polyprotein processing (very low) in COVID-19 drug treatment HOIP_0031063 HOIP:HOIP_0031064 Any process that decreases the rate, frequency or extent of viral polyprotein maturation by peptide bond cleavage. negative regulation of viral protein processing in COVID-19 drug treatment HOIP_0031064 HOIP:HOIP_0031065 Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. viral protein processing (very low) in COVID-19 drug treatment HOIP_0031065 HOIP:HOIP_0031066 Changing cell survival-cell death balance is a subtype of changing balance: A process that changes the steady state of cell number between cell death and cell survival within an organ or an organism. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis. changing cell survival-cell death balance [cell death (course)] HOIP_0031066 HOIP:HOIP_0031067 reduced oxygenation of body tissues resulting in the decreased pressure of this component of body gases; commonly due to hypoxemia This entity is a specific course-dependent process. This process can constitute the course of apoptosis. hypoxia (moderate)[apoptosis (course)] HOIP_0031067 HOIP:HOIP_0031068 reduced oxygenation of body tissues resulting in the decreased pressure of this component of body gases; commonly due to hypoxemia This entity is a specific course-dependent process. This process can constitute the course of necrosis. hypoxia (very high) [necrosis (course)] HOIP_0031068 HOIP:HOIP_0031069 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of apoptosis. increasing demand for response to oxidative stress(moderate) [apoptosis (course)] HOIP_0031069 HOIP:HOIP_0031070 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of necrosis. increasing demand for response to oxidative stress(very high) [necrosis (course)] HOIP_0031070 HOIP:HOIP_0031071 Drug-, radiation-induced, or spontaneous injuries to DNA that introduce deviations from its normal double-helical conformation. These changes include structural distortions that interfere with replication and transcription, as well as point mutations that disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. If the damage is minor, it can often be repaired (DNA repair); extensive damage can induce apoptosis. This entity is a specific course-dependent process. This process can constitute the course of cell death. DNA damage [cell death (course)] HOIP_0031071 HOIP:HOIP_0031073 Cellular damage is a subtype of damaging: A process that injuries the structure of the cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of anoikis. cellular damage [anoikis (course)] HOIP_0031073 HOIP:HOIP_0031074 Cellular damage is a subtype of damaging: A process that injuries the structure of the cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of cell death. cellular damage [cell death (course)] HOIP_0031074 HOIP:HOIP_0031075 Mcrovascular dysfunction is a subtype of organ malfunction: A process that does not perform microvascular function correctly or not functioning at all. microvascular dysfunction[Type2 diabetes] HOIP_0031075 HOIP:HOIP_0031076 Renal system malfunction is a subtype of malfunction: A process that does not perform renal system function correctly or not functioning at all. renal system malfunction HOIP_0031076 HOIP:HOIP_0031077 Renal system malfunction is a subtype of malfunction: A process that does not perform renal system function correctly or not functioning at all. renal system malfunction[type2 diabetes] HOIP_0031077 HOIP:HOIP_0031078 Anatomical system malfunction is a subtype of malfunctioning process: A process that cannot perform anatomical system function appropriately or cannot realize it at all. anatomical system malfunction HOIP_0031078 HOIP:HOIP_0031079 Narrowing of the renal artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the renal arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of Type 2 Diabetes. narrowing of the renal artery [type2 diabetes] HOIP_0031079 HOIP:HOIP_0031080 Nervous system malfunction is a subtype of malfunction: A process that does not perform nervous system system function correctly or not functioning at all. nervous system malfunction HOIP_0031080 HOIP:HOIP_0031081 Nervous system malfunction is a subtype of malfunction: A process that does not perform nervous system system function correctly or not functioning at all. nervous system malfunction[type2 diabetes] HOIP_0031081 HOIP:HOIP_0031082 Increasing blood glucose level is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of diabetes. hyperglycemia increasing blood glucose level (moderate)[Type2 diabetes] HOIP_0031082 HOIP:HOIP_0031083 Increasing blood glucose level is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of diabetes. hyperglycemia increasing blood glucose level(very high) [type 1 diabetes mellitus course] HOIP_0031083 HOIP:HOIP_0031084 A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. viral assembly virion organization virion assembly(very low) in COVID-19 drug treatment HOIP_0031084 HOIP:HOIP_0031085 Any process that decreases the rate, frequency or extent of negative stranded viral RNA transcription. PMID:32505227 PMID:32629875 negative regulation of negative stranded viral RNA transcription in COVID-19 drug treatment HOIP_0031085 PMID:32505227 Remdesivir inhibits RNA dependent RNA polymerase(RdRp) by binding to RNA strands and preventing additional nucleotides from being added, thereby terminating RNA transcription. Chen et al. conducted a multicenter, randomized priority trial on 240 patients with confirmed COVID-19 infection to test favipiravir or arbidol and favipiravir was suggested to significantly improve symptom relief. However, the interpretation of this study is limited by a short clinical recovery window of 7 days, only 100 of 236 patients with confirmed COVID-19, and the lack of a control group. PMID:32629875 In addition, the antiviral drug, remdesivir, which has received Emergency Use Authorization for the treatment of hospitalized patients with suspected or laboratory-confirmed, severe COVID-19 could also be beneficial to reduce replication and release of infectious particles (NCT04292730). HOIP:HOIP_0031086 Any process that decreases the rate, frequency or extent of negative stranded viral RNA transcription. negative regulation of negative stranded viral RNA transcription HOIP_0031086 HOIP:HOIP_0031087 Any molecular entity that contains carbon. organic molecular entity with pharmaological role HOIP_0031087 HOIP:HOIP_0031088 This course is categorized from the viewpoint of the findings of Ground-glass opacification on pulmonary HRCT. This entity is inferred from Description Logic. course based on ground glass HOIP_0031088 HOIP:HOIP_0031100 Symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. This process can constitute the course of COVID-19 (homeostatic balance). symbiotic balance between host and virus in COVID-19 (homeostatic balance) HOIP_0031100 HOIP:HOIP_0031101 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32142651 viral entry into host cell in COVID-19 (homeostatic balance) HOIP_0031101 PMID:32142651 Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases. HOIP:HOIP_0031103 A role combining with a virus component and mediating entry of the virus into the cell. virus receptor HOIP_0031103 HOIP:HOIP_0031104 Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. receptor mediated endocytosis by host of virus particle receptor mediated endocytosis of virus by host receptor mediated endocytosis of virus particle by host receptor-mediated endocytosis of virus by host viral receptor mediated endocytosis virus receptor-mediated endocytosis by host viral entry into host cell via receptor-mediated endocytosis viral entry into host cell via receptor-mediated endocytosis receptor-mediated endocytosis of virus by host cell in MERS HOIP_0031104 viral entry into host cell via receptor-mediated endocytosis GOC:bf GOC:jl HOIP:HOIP_0031105 Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. fusion of virus membrane with host endosomal membrane fusion of virus membrane with host endosome membrane in MERS HOIP_0031105 HOIP:HOIP_0031106 A protein that is encoded in the genome of middle east respiratory syndrome-related coronavirus. middle east respiratory syndrome-related coronavirus protein HOIP_0031106 HOIP:HOIP_0031107 A protein that is a translation product of the S gene in MERS-CoV. GenPept:YP_009047204.1 PMID:30413791 PMID:30712865 spike glycoprotein (MERS-CoV) HOIP_0031107 HOIP:HOIP_0031108 A spike glycoprotein, signal peptide removed form (MERS-CoV) that has been processed by proteolytic cleavage to yield the C-terminal portion. PMID:30413791 PMID:30712865 PMID:32142651 S2 (MERS-CoV) S2 (MERS-CoV)[MERS] spike protein S2 (MERS-CoV) HOIP_0031108 HOIP:HOIP_0031110 A spike glycoprotein, signal peptide removed form (MERS-CoV) that has been processed by proteolytic cleavage to yield the N-terminal portion. PMID:30413791 PMID:30712865 S1 (MERS-CoV) S1 (MERS-CoV)[MERS] spike protein S1 (MERS-CoV) HOIP_0031110 HOIP:HOIP_0031248 A process of fibosis leading to the interstitial lung disease that is characterized by destruction, scarring, and thickening of the interstitial lung tissues and progressive pulmonary function loss in a restrictive pattern, has_symptom progressive shortness of breath, fatigue, and chronic cough, possibly has_material_basis_in exposure to certain chemicals, autoimmune conditions, and radiation. PMID:32307653 pulmonary fibrosis process [pulmonary fibrosis(course)] HOIP_0031248 PMID:32307653 Moreover, resident lung progenitor/stem are extensively differentiated into myofibroblasts during pulmonary fibrosis, a complication observed in COVID-19 patients. In addition to direct viral invasion and loss of lung stem cells, stocks of these cells also can be affected during SARS-CoV-2 infection by extensive differentiation into myofibroblasts. These cell deposit extracellular matrix proteins and are the main cells presents in fibrotic diseases, including pulmonary fibrosis and fibrous stripes due to COVID-19. Recent evidence using lineage tracing showed that resident mesenchymal cells are the main sources of myofibroblasts in pulmonary fibrosis, rather than epithelial or bone marrow-derived cells. HOIP:HOIP_0031249 Pulmonary fibrosis dependent process is a subtype of disease course dependent process: A process that can constitute the course of pulmonary fibrosis. pulmonary fibrosis dependent process HOIP_0031249 HOIP:HOIP_0031250 Decreaing leucocyte is a subtype of decreasing number of cells: A process that becomes smaller in number of leucocytes. decreasing leucocyte HOIP_0031250 HOIP:HOIP_0031251 Decreasing lymphocytes is a subtype of decreasing leucocytes: A process that changes the amount of lymphocytes to be lower. decreasing lymphoyte HOIP_0031251 HOIP:HOIP_0031254 Lymphopenia dependent process is a subtype of disease course dependent process: A process that can constitute the course of lymphopenia. lymphopenia dependent process HOIP_0031254 HOIP:HOIP_0031255 Decreasing lymphocytes is a subtype of decreasing leucocytes: A process that changes the amount of lymphocytes to be lower. This entity is a specific course-dependent process. This process can constitute the course of lymphopenia. decreasing lymphocytes [lymphopenia] HOIP_0031255 HOIP:HOIP_0031259 Any process involved in the maintenance of a steady state of symbiosis between host and virus within an organ or an organism. symbiotic balance between host and virus HOIP_0031259 HOIP:HOIP_0031260 Any process involved in lacking a balance of of symbiosis between host and virus within an organ or an organism. symbiotic imbalance between host and virus HOIP_0031260 HOIP:HOIP_0031261 Fc gamma receptor signaling is a subtype of biological signaling: A process of molecular signaling of Fc-gamma receptor on the surface of a signal-receiving cell. Fc-gamma receptor signaling HOIP_0031261 HOIP:HOIP_0031268 Interacting selectively and non-covalently with a virion, either by binding to components of the capsid or the viral envelope. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. virion binding with host cell surface receptor (very low) in COVID-19 drug treatment HOIP_0031268 HOIP:HOIP_0031269 Interacting selectively and non-covalently with the surface of a host cell. host cell surface binding (very low) in COVID-19 drug treatment HOIP_0031269 HOIP:HOIP_0031271 angiotensin II hydrolysis is a subtype of hydrolysis: A chemical reaction that uses water to break down a angiotensin II ACE2 hydrolyzes Angiotensin II and produces Angiotensin-(1-7). angiotensin II hydrolysis in COVID-19 drug treatment HOIP_0031271 HOIP:HOIP_0031276 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32726803 viral replication complex formation (very low) in COVID-19 drug treatment HOIP_0031276 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. ISBN:0781718325 PMID:32726803 The SARS-CoV-2 genome shares high sequence identity with SARS-CoV7,8. Both viruses critically rely on the activity of viral proteases: the main protease (Mpro, also known as 3CLpro or non-structural protein 5 (nsp5)) and the papain-like protease (PLpro, the protease domain of nsp3) to generate a functional replicase complex and enable viral spread1,2. HOIP:HOIP_0031277 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32726803 viral replication complex formation and maintenance (very high) in severe COVID-19_2 HOIP_0031277 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. ISBN:0781718325 PMID:32726803 The SARS-CoV-2 genome shares high sequence identity with SARS-CoV7,8. Both viruses critically rely on the activity of viral proteases: the main protease (Mpro, also known as 3CLpro or non-structural protein 5 (nsp5)) and the papain-like protease (PLpro, the protease domain of nsp3) to generate a functional replicase complex and enable viral spread1,2. HOIP:HOIP_0031278 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces subgenomic negative stranded (-) mRNA . This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. subgenomic negative stranded viral mRNA biosynthetic process (very low) in COVID-19 drug treatment HOIP_0031278 HOIP:HOIP_0031283 A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. viral genome expression viral gene expression(very low) in COVID-19 drug treatment HOIP_0031283 HOIP:HOIP_0031284 A process by which viral mRNA is translated into viral protein for viral replication complex, using the host cellular machinery. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis translation for viral replication complex(very low) in COVID-19 drug treatment HOIP_0031284 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0031287 The metabolic process in which viral RNA replicase is formed, using the sequence of a viral RNA to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is low. viral RNA replicase translation(very low) in COVID-19 drug treatment HOIP_0031287 HOIP:HOIP_0031288 The process by which an incoming virus is disassembled in the host cell to release a replication-competent viral genome. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is low. viral uncoating uncoating of virus (very low) in COVID-19 drug treatment HOIP_0031288 HOIP:HOIP_0031292 The transport of a virus between adjacent cells in a multicellular organism. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32362314 PMID:32629875 VZ:1018 cell to cell spread of virus within host intercellular virus transport transport of virus in host, cell to cell (very low) in COVID-19 drug treatment HOIP_0031292 PMID:32362314 Finally, the addition of an arginine residue to the S1/S2 site of SARS-2-S jointly with alanine-to-lysine exchange strongly increased syncytium formation, indicating that viral variants with optimized S1/S2 sites might show augmented cell-cell spread and potentially altered pathogenicity. PMID:32629875 Epidemiologic evidence indicates that the virus is transmitted among close contacts mostly through the respiratory route, presumably directly through infected droplet secretions or indirectly via fomites (Figure 2). The proximity between the infected respiratory epithelium releasing the virus and endothelial cells may favor local transmission. HOIP:HOIP_0031296 The directed movement of a virus, or part of a virus, into, out of, or within a host cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. transport of virus (very low) in COVID-19 drug treatment HOIP_0031296 HOIP:HOIP_0031297 The assembly of a virus capsid from its protein subunits. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. viral capsid assembly(very low) in COVID-19 drug treatment HOIP_0031297 HOIP:HOIP_0031300 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32422178 PMID:32697943 PMID:32843733 PMID:33123165 cytokine storm in COVID-19 associated with ARDS HOIP_0031300 PMID:32422178 In some cases, abnormal immune mechanisms initiate and promote pulmonary fibrosis, possibly as a consequence of a cytokine storm. PMID:32697943 Cytokine storm also plays a critical role in lung injury of patients with severe COVID-19 (Shi et al., 2020). PMID:32843733 The damaged cells in the lungs elicit a strong innate immune response, which seems to be largely mediated by pro-inflammatory macrophages and granulocytes. This response is thought to be responsible for the cytokine release syndrome or ‘cytokine storm’ that is believed to contribute to ARDS. Levels of inflammatory cytokines such as IL-1, TNF and IL-6 can be high in the lungs of patients with COVID-19; therefore, blocking one or more of these cytokines could potentially benefit these individuals by reducing the severity of the cytokine storm and ARDS. PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. HOIP:HOIP_0031303 adaptive immune response An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. adaptive immune response (normal) in COVID-19 drug treatment HOIP_0031303 HOIP:HOIP_0031304 An immune response mediated through a body fluid. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. humoral immune response in COVID-19 drug treatment HOIP_0031304 HOIP:HOIP_0031305 An immune response mediated through cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. cellular immune response in COVID-19 drug treatment HOIP_0031305 HOIP:HOIP_0031306 Any process involved with the carrying out of an immune response by a B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. PMID:33123165 B cell mediated immunity in COVID-19 drug treatment HOIP_0031306 PMID:33123165 Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0031307 The change in morphology and behavior of a mature or immature B cell during an immune response, resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This process can constitute the course of COVID-19 drug treatment. B cell activation involved in adaptive immune response in COVID-19 drug treatment HOIP_0031307 HOIP:HOIP_0031308 The appearance of immunoglobulin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. antibody production immunoglobulin production (normal) in COVID-19 drug treatment HOIP_0031308 HOIP:HOIP_0031310 The inhibition of an antigen's biological effects by antibody binding to it. An example is neutralization of diphtheria toxin by preventing its entry into human cells via the binding of antibody specific for diphtheria toxin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. immunoglobulin-mediated neutralization in COVID-19 drug treatment HOIP_0031310 HOIP:HOIP_0031311 Narrowing of the renal artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the renal arteries to be smaller. narrowing of the renal artery HOIP_0031311 HOIP:HOIP_0031312 Narrowing of the brain artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the cerebral arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of brain infarction. Wikipedia:Cerebral_infarction brain artery narrowing [brain infarction course] HOIP_0031312 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0031313 Narrowing of the brain artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the cerebral arteries to be smaller. brain artery narrowing HOIP_0031313 HOIP:HOIP_0031315 Decreasing brain blood flow is a subtype of decreasing flow: A process that changes the amount of brain blood flow to be lower. decreasing brain blood flow HOIP_0031315 HOIP:HOIP_0031318 An arterial blood vessel that is part of a kidney kidney arterial blood vessel HOIP_0031318 HOIP:HOIP_0031320 An arterial blood vessel that is part of a brain brain arterial blood vessel HOIP_0031320 HOIP:HOIP_0031321 Decreasing brain blood flow is a subtype of decreasing flow: A process that changes the amount of brain blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of brain infarction. Wikipedia:Cerebral_infarction decreasing brain blood flow [brain infarction course] HOIP_0031321 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0031322 A type of brain cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of brain infaction. Wikipedia:Cerebral_infarction brain cell necrosis [brain infarction course] HOIP_0031322 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0031323 A type of brain cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. brain cell necrosis HOIP_0031323 HOIP:HOIP_0031327 Brain Ischemia is a changing process to lack enough to blood supply of brain. This entity is a specific course-dependent process. This process can constitute the course of brain infaction. brain ischemia [brain infarction course] HOIP_0031327 HOIP:HOIP_0031328 Brain blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform brain blood vessel function correctly or not functioning at all. PMID:32629875 brain blood vessel dysfunction HOIP_0031328 PMID:32629875 COVID-19, however, appears to include an evolving set of clinical manifestation not previously reported in SARS and MERS, including stroke and cardiomyopathies associated with coagulopathy and vasculopathy, which can cause sudden death and other serious morbidities. HOIP:HOIP_0031330 Brain Ischemia is a changing process to lack enough to blood supply of brain. brain ischemia HOIP_0031330 HOIP:HOIP_0036001 Any processes of signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. cytoplasmic pattern recognition receptor signaling in response to virus HOIP_0036001 HOIP:HOIP_0036002 Any constituent part of a virion, a complete fully infectious extracellular virus particle. [database_cross_reference: virion part HOIP_0036002 HOIP:HOIP_0036003 Ground-glass opacification is a non-specific sign and can be observed with many conditions including infection, chronic interstitial disease and acute alveolar disease. A descriptive term that is applied to computer tomography imaging and that refers to a hazy area of increased attenuation in the lung with preserved bronchial and vascular markings. PMID:32085846 Ground-glass opacification is a non-specific sign and can be observed with many conditions including infection, chronic interstitial disease and acute alveolar disease. Ground-glass opacification on pulmonary HRCT [Pulmonary Pathological findings] HOIP_0036003 HOIP:HOIP_0036005 Any process that stops, prevents, or reduces the frequency, rate, or extent of membrane fusion involved in viral entry into host cell. This process can constitute the course of COVID-19. PMID:32505227 negative regulation of membrane fusion involved in viral entry into host cell in COVID-19 HOIP_0036005 HOIP:HOIP_0036006 The totality of all processes through which COVID-19 infection with acute respiratory distress is realized. COVID-19 course associated with acute respiratory distress syndrome HOIP_0036006 HOIP:HOIP_0036007 Respirtory disfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete gas change of respiration system. respiratory dysfunction HOIP_0036007 HOIP:HOIP_0036008 Respirtory disfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete gas change of respiration system. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32412710 PMID:32697943 respiratory dysfunction in COVID-19 associated with ARDS HOIP_0036008 PMID:32412710 Dyspnea is the most common symptom of severe disease and is often accompanied by hypoxemia (Fig. 1). Progressive respiratory failure develops in many patients with severe Covid-19 soon after the onset of dyspnea and hypoxemia. These patients commonly meet the criteria for the acute respiratory distress syndrome (ARDS), which is defined as the acute onset of bilateral infiltrates, severe hypoxemia, and lung edema that is not fully explained by cardiac failure or fluid overload. PMID:32697943 These data may explain why uncontrolled diabetes may lead to compromised adaptive immune response and lung dysfunction in patients with severe COVID-19 symptoms. HOIP:HOIP_0036010 Abnormal presence of an eosinophilic hyaline (glass-like) material composed of fibrin, proteinaceous exudate and cellular debris, and lining or filling the alveoli, alveolar ducts and bronchioles; hyaline membranes block gas exchange and are usually found at autopsy in individuals that have died of respiratory distress syndrome. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). pulmonary hyaline membrane formationin COVID-19 associated with ARDS HOIP_0036010 HOIP:HOIP_0036011 Endothelial cell damage damage is a subtype of cellular damage: A process that injuries the structure of the endothelial cell as the direct or indirect result of a force. vascular endothelial cell damage HOIP_0036011 HOIP:HOIP_0036013 type I alveolar epithelial cell injury is a subtype of cellular damage: A process that injuries the structure of the type I alveolar epithelial cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). type I alveolar epithelial cell injury in COVID-19 associated with ARDS HOIP_0036013 HOIP:HOIP_0036014 Type I alveolar epithelial cell injury is a subtype of cellular damage: A process that injuries the structure of the type I alveolar epithelial cell. type I alveolar epithelial cell injury HOIP_0036014 HOIP:HOIP_0036015 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). leaking fluid to alveolar space in COVID-19 associated with ARDS HOIP_0036015 HOIP:HOIP_0036016 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. leaking fluid to alveolar space HOIP_0036016 HOIP:HOIP_0036017 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). leaking fluid to pulmonary interstitium in COVID-19 associated with ARDS HOIP_0036017 HOIP:HOIP_0036018 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. leaking fluid to pulmonary interstitium HOIP_0036018 HOIP:HOIP_0036019 The multiplication or reproduction of Type II alveolar epithelium cells, resulting in the rapid expansion of a cell population. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). Type II alveolar epithelium cell proliferation in COVID-19 associated with ARDS HOIP_0036019 HOIP:HOIP_0036020 The multiplication or reproduction of Type II alveolar epithelium cells, resulting in the rapid expansion of a cell population. This entity is a specific course-dependent process. This process can constitute the course of COVID 10 with ARDS. Type II alveolar epithelium cell proliferation HOIP_0036020 HOIP:HOIP_0036021 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). Yuki Yuki inflammatory cell infiltration to pulmonary interstitium (very high) in COVID-19 associated with ARDS HOIP_0036021 Yuki Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. HOIP:HOIP_0036022 Pulmonary interstitium edema is a subtype of accumulation of substances in a biological object: A process that keeps fluids in the pulmonary interstitium. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). pulmonary interstitium edema in COVID-19 associated with ARDS HOIP_0036022 HOIP:HOIP_0036023 Pulmonary interstitium edema is a subtype of pulmonary edema: A process that keeps fluids in the pulmonary interstitium. pulmonary interstitium edema HOIP_0036023 HOIP:HOIP_0036024 IRF7 activation is a subtype of molecular activation: A process that changes the activity of the IRF7 to be higher. IRF7 activation HOIP_0036024 HOIP:HOIP_0036025 Increasing lung weight is a subtype of increasing weight: A process that changes the weight of the lung to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). increasing lung weight in COVID-19 associated with ARDS HOIP_0036025 HOIP:HOIP_0036026 Increasing lung weight is a subtype of increasing weight: A process that changes the weight of the lung to be higher. increasing lung weight HOIP_0036026 HOIP:HOIP_0036028 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. hyperfunction of cytokine secretion cytokine storm HOIP_0036028 HOIP:HOIP_0036029 Viral entry-innate immune response balance is a subtype of maiintaining balance: A process that keeps a balance between the viral entry and the innate immune response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. viral entry-innate immune response balance in mild COVID-19 HOIP_0036029 HOIP:HOIP_0036030 Viral entry-innate immune response imbalance is a subtype of stress response imbalance: A process that lacks a balance between the viral entry and the innate immune response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. viral entry-innate immune response imbalance in moderate COVID-19 HOIP_0036030 HOIP:HOIP_0036034 Any process that stops, prevents, or reduces the frequency, rate, or extent of membrane fusion involved in viral entry into host cell. negative regulation of membrane fusion involved in viral entry into host cell HOIP_0036034 HOIP:HOIP_0036035 Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production. This process can constitute the course of COVID-19. PMID:32505227 PMID:33116300 negative regulation of type I interferon production in COVID-19 HOIP_0036035 PMID:33116300 For example, nsp1 is rapidly proteolytically released from pp1a and pp1ab and affects cellular translation in the cytoplasm to favour viral mRNAs over cellular mRNA, and thereby also decreases the expression of type I and III interferons and of other host proteins of the innate immune response. Although this activity is not predicted for any accessory protein of SARS-CoV or SARS-CoV-2, the ORF3b, ORF6 and N proteins of SARS-CoV have been shown to interfere at multiple levels of the cellular interferon signalling pathway, thereby efficiently inhibiting innate immune responses103. Interestingly, an initial report recently suggested a similar role of SARS-CoV-2 ORF3b as an effective interferon antagonist. HOIP:HOIP_0036036 Viral entry regulator role is a role played by any substance that regulates the process of viral entry to the host. viral entry regulator role HOIP_0036036 HOIP:HOIP_0036037 Viral entry regulator role is a role played by any substance that induces the process of viral entry to the host. viral entry inducer role HOIP_0036037 HOIP:HOIP_0036038 Viral entry regulator role is a role played by any substance that inhibits the process of viral entry to the host. viral entry inhibitor role HOIP_0036038 HOIP:HOIP_0036039 Viral entry regulator role is a role played by any substance that regulates the process of membrane fusion involved in viral entry into host cell. regulator role of host-viral membrane fusion HOIP_0036039 HOIP:HOIP_0036040 Viral entry regulator role is a role played by any substance that positively regulates the process of membrane fusion involved in viral entry into host cell. host-viral membrane fusion inducer role HOIP_0036040 HOIP:HOIP_0036041 Viral entry regulator role is a role played by any substance that positively regulates the process of membrane fusion involved in viral entry into host cell. host-viral membrane fusion inhibitor role HOIP_0036041 HOIP:HOIP_0036046 A transcription process that uses a viral DNA as a template. DNA-templated viral transcription HOIP_0036046 HOIP:HOIP_0036047 The metabolic process in which a protein is formed, using the sequence of a viral RNA to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome. viral RNA replicase translation HOIP_0036047 HOIP:HOIP_0036048 The metabolic process in which viral RNA replicase is formed, using the sequence of a viral RNA to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome. This process can constitute the course of COVID-19. viral RNA replicase translation in COVID-19 HOIP_0036048 HOIP:HOIP_0036049 The metabolic process in which viral RNA replicase is formed, using the sequence of a viral RNA to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome. This process can constitute the course of coronavirus infectious disease. viral RNA replicase translation in coronavirus infection HOIP_0036049 HOIP:HOIP_0036054 Coronavirus infectious course dependent chemical compound is a subtype of course dependent chemical entity. This entity (drug) can participate in the coronavirus infectious course. coronavirus infectious disease dependent chemical compound HOIP_0036054 HOIP:HOIP_0036055 A role played by the entity which that neutralizes the IL-6 by binding specifically to it. IL-6 antibody HOIP_0036055 HOIP:HOIP_0036057 Any process that decreases the rate, frequency or extent of the series of molecular events generated as a consequence of interleukin-6 binding to a cell surface receptor. This process can constitute the course of COVID-19 drug treatment. negative regulation of IL-6-mediated signaling pathway in COVID-19 drug treatment negative regulation of interleukin-6-mediated signaling in COVID-19 drug treatment HOIP_0036057 HOIP:HOIP_0036058 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. viral replication complex formation in coronavirus infection HOIP_0036058 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. ISBN:0781718325 HOIP:HOIP_0036059 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 viral replication complex formation in COVID-19 HOIP_0036059 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. ISBN:0781718325 PMID:32726803 The SARS-CoV-2 genome shares high sequence identity with SARS-CoV7,8. Both viruses critically rely on the activity of viral proteases: the main protease (Mpro, also known as 3CLpro or non-structural protein 5 (nsp5)) and the papain-like protease (PLpro, the protease domain of nsp3) to generate a functional replicase complex and enable viral spread1,2. HOIP:HOIP_0036060 A process by which viral mRNA is translated into viral protein for viral replication complex, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:26868298 viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis translation for viral replication complex in coronavirus infection HOIP_0036060 PMID:26868298 The large replicase polyprotein 1a (pp1a) and pp1ab, which are encoded by the 5'-terminal open reading frame 1a/b (ORF1a/b), are cleaved by two viral proteases, the papain-like protease (PLpro) and the 3C-like protease (3CLpro), to produce non-structural proteins (NSPs) such as RNA-dependent RNA polymerase (RdRp) and helicase, which are involved in the transcription and replication of the virus. viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0036061 The totality of all processes through which drug efficacy for COVID-19 infection is realized. COVID-19 drug treatment course HOIP_0036061 HOIP:HOIP_0036062 Any process that stops, prevents, or reduces the frequency, rate, or extent of cytokine storm. down regulation of cytokine storm negative regulation of cytokine storm HOIP_0036062 HOIP:HOIP_0036063 Any process that stops, prevents, or reduces the frequency, rate, or extent of cytokine storm. This process can constitute the course of COVID-19 drug treatment. down regulation of cytokine storm in COVID-19 drug treatment negative regulation of cytokine storm in COVID-19 drug treatment HOIP_0036063 HOIP:HOIP_0036064 The appearance of interleukin-6 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:31623280 PMID:32276453 PMID:32412710 PMID:32697943 interleukin-6 production (very low) in COVID-19 drug treatment HOIP_0036064 PMID:31623280 Once inside cells, the viral RNAs are detected by the pattern recognition receptors (PRRs) which trigger a downstream cascade of molecules leading to the activation of the transcription factor nuclear factor-κB (NF-κB) and interferon regulatory factor 3 (IRF3), with the subsequent production of type I interferons (IFN-α/β) and a series of pro-inflammatory cytokines [2,9] including interleukin (IL)-1β and IL-6. The development of an uncontrolled inflammatory response can thus lead to potentially life-threatening damage to lung tissue. PMID:32276453 mtFAO in liver could be favored by increased levels of hormones and other circulating factors such as leptin, FGF21, and interleukin 6 (IL6). PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. These organ failures may be associated with clinical and laboratory signs of inflammation, including high fevers, thrombocytopenia, hyperferritinemia, and elevations in C-reactive protein and interleukin-6. PMID:32697943 2-DG treatment also inhibited CoV-2-induced TNF-a, IL-6, and IFN a, b, and l expression in monocytes (Figure S3A). HOIP:HOIP_0036065 A process by which viral mRNA is translated into viral protein for viral replication complex, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis translation for viral replication complex in COVID-19 HOIP_0036065 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0036066 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces subgenomic negative stranded (-) mRNA . subgenomic negative stranded viral mRNA biosynthetic process HOIP_0036066 HOIP:HOIP_0036067 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces subgenomic negative stranded (-) mRNA. This process can constitute the course of coronavirus infectious disease. As well as the viral mRNAs and proteins, a virus needs to make copies of its genome for inclusion into the next generation of viruses. For viruses with single-strand genomes, this involeves the synthesis of an oppsite sense "antigenome" from which new gennomes are transcribed. As well as the viral mRNAs and proteins, a virus needs to make copies of its genome for inclusion into the next generation of viruses. For viruses with single-strand genomes, this involeves the synthesis of an oppsite sense "antigenome" from which new gennomes are transcribed. subgenomic negative stranded viral mRNA biosynthetic process in coronavirus infection HOIP_0036067 As well as the viral mRNAs and proteins, a virus needs to make copies of its genome for inclusion into the next generation of viruses. For viruses with single-strand genomes, this involeves the synthesis of an oppsite sense "antigenome" from which new gennomes are transcribed. ISBN:0815341504 HOIP:HOIP_0036068 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces subgenomic negative stranded (-) mRNA. This process can constitute the course of COVID-19. subgenomic negative stranded viral mRNA biosynthetic process in COVID-19 HOIP_0036068 HOIP:HOIP_0036069 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces the full-length negative stranded (-) mRNA for synthesis of new genomic RNAs and subgenomic negative strand templates. full length negative stranded viral mRNA biosynthetic process full length negative stranded viral mRNA biosynthetic process HOIP_0036069 HOIP:HOIP_0036070 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces the full-length negative stranded (-) mRNA for synthesis of new genomic RNAs and subgenomic negative strand templates. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33116300 full length negative stranded viral mRNA biosynthetic process full length negative stranded viral mRNA biosynthetic process in coronavirus infection HOIP_0036070 PMID:33116300 Viral genomic replication is initiated by the synthesis of full-length negative-sense genomic copies, which function as templates for the generation of new positive-sense genomic RNA. These newly synthesized genomes are used for translation to generate more nsps and replication and transcription complex (RTC)s or are packaged into new virions. HOIP:HOIP_0036072 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces the full-length negative stranded (-) mRNA for synthesis of new genomic RNAs and subgenomic negative strand templates. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. full length negative stranded viral mRNA biosynthetic process in COVID-19 full length negative stranded viral mRNA biosynthetic process in COVID-19 HOIP_0036072 HOIP:HOIP_0036073 A process by which viral mRNA is translated into viral protein for viral replication complex, using the host cellular machinery. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis translation for viral replication complex HOIP_0036073 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0036074 The assembly of a virus capsid from its protein subunits. This process can constitute the course of coronaviurs infectious disease. PMID:33116300 viral capsid assembly in coronavirus infection HOIP_0036074 PMID:33116300 Translated structural proteins translocate into endoplasmic reticulum (ER) membranes and transit through the ER-to-Golgi intermediate compartment (ERGIC), where interaction with N-encapsidated, newly produced genomic RNA results in budding into the lumen of secretory vesicular compartment. In general, coronavirus structural proteins assemble and assist in the budding of new virions at the endoplasmic reticulum (ER)-to-Golgi compartment that are suggested to exit the infected cell by exocytosis. However, recent evidence shows that betacoronaviruses, including MHV and SARS-CoV-2, rather egress infected cells via the lysosomal trafficking pathway. During this process, viral interference with lysosomal acidification, lysosomal enzyme activity and antigen presentation was demonstrated. HOIP:HOIP_0036075 The assembly of a virus capsid from its protein subunits. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. viral capsid assembly in COVID-19 HOIP_0036075 HOIP:HOIP_0036076 The directed movement of a virus, or part of a virus, into, out of, or within a host cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. transport of virus in coronavirus infection HOIP_0036076 HOIP:HOIP_0036077 The directed movement of a virus, or part of a virus, into, out of, or within a host cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. transport of virus in COVID-19 HOIP_0036077 HOIP:HOIP_0036081 Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral polyprotein 1a. This process can constitute the course of coronavirus infectious disease. PMID:26868298 viral polyprotein 1a processing in coronavirus infection HOIP_0036081 HOIP:HOIP_0036082 The cleavage of a peptide bond or bonds within a viral polyprotein 1ab. This process can constitute the course of coronavirus infectious disease. PMID:26868298 viral polyprotein1ab processing in coronavirus infection HOIP_0036082 HOIP:HOIP_0036083 A gene of an organism of SARS-CoV2 9606 gene of SARS-CoV2 HOIP_0036083 HOIP:HOIP_0036084 2697049 ORF1a polyprotein;ORF1ab polyprotein Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped, positive-sense, single-stranded RNA virus that causes coronavirus disease 2019 (COVID-19). Virus particles include the RNA genetic material and structural proteins needed for invasion of host cells. Once inside the cell the infecting RNA is used to encode structural proteins that make up virus particles, nonstructural proteins that direct virus assembly, transcription, replication and host control and accessory proteins whose function has not been determined.~ ORF1ab, the largest gene, contains overlapping open reading frames that encode polyproteins PP1ab and PP1a. The polyproteins are cleaved to yield 16 nonstructural proteins, NSP1-16. Production of the longer (PP1ab) or shorter protein (PP1a) depends on a -1 ribosomal frameshifting event. The proteins, based on similarity to other coronaviruses, include the papain-like proteinase protein (NSP3), 3C-like proteinase (NSP5), RNA-dependent RNA polymerase (NSP12, RdRp), helicase (NSP13, HEL), endoRNAse (NSP15), 2'-O-Ribose-Methyltransferase (NSP16) and other nonstructural proteins. SARS-CoV-2 nonstructural proteins are responsible for viral transcription, replication, proteolytic processing, suppression of host immune responses and suppression of host gene expression. The RNA-dependent RNA polymerase is a target of antiviral therapies. orf1ab HOIP_0036084 HOIP:HOIP_0036086 The cleavage of a peptide bond or bonds within a viral polyprotein. This process can constitute the course of COVID-19. PMID:33116300 non-structural proteins are procduced. viral polyprotein processing in COVID-19 HOIP_0036086 PMID:33116300 Following entry, the release and uncoating of the incoming genomic RNA subject it to the immediate translation of two large open reading frames, ORF1a and ORF1b. The resulting polyproteins pp1a and pp1ab are co-translationally and post-translationally processed into the individual non-structural proteins (nsps) that form the viral replication and transcription complex. PMID:33116300 The translation of ORF1a and ORF1b from the genomic RNA produces two polyproteins, pp1a and pp1ab, respectively. Sixteen non-structural proteins are co-translationally and post-translationally released from pp1a (nsp1–11) and pp1ab (nsp1–10, nsp12–16) upon proteolytic cleavage by two cysteine proteases that are located within nsp3 (papain-like protease; PLpro) and nsp5 (chymotrypsin-like protease)/3C-like protease (3CLpro). HOIP:HOIP_0036087 Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral polyprotein 1a. This process can constitute the course of COVID-19. viral polyprotein 1a processing in COVID-19 HOIP_0036087 HOIP:HOIP_0036088 The cleavage of a peptide bond or bonds within a viral polyprotein 1ab. This process can constitute the course of COVID-19. viral polyprotein1ab processing in COVID-19 HOIP_0036088 HOIP:HOIP_0036095 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This process can constitute the course of coronavirus infectious disease. antiviral innate immune response in coronavirus infection HOIP_0036095 HOIP:HOIP_0036096 The promotion of an immune response by natural killer cells through direct recognition of target cells or through the release of cytokines. This process can constitute the course of coronavirus infectious disease. NK cell mediated immunity natural killer cell mediated immunity in coronavirus infection HOIP_0036096 HOIP:HOIP_0036097 Antigen processing and presentation which is initiated by phagocytosis of antigen bound directly or indirectly to a cell surface toll-like receptor (TLR). antigen processing and presentation initiated by toll-like receptor mediated phagocytosis of antigen HOIP_0036097 HOIP:HOIP_0036098 Antigen processing and presentation which is initiated by phagocytosis of antigen bound directly or indirectly to a cell surface toll-like receptor (TLR). This process can constitute the course of COVID-19. antigen processing and presentation initiated by toll-like receptor mediated phagocytosis of antigen in COVID-19 HOIP_0036098 HOIP:HOIP_0036099 Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. RIG-I signaling pathway HOIP_0036099 HOIP:HOIP_0036100 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of COVID-19. PMID:32505227 RIG-I signaling in COVID-19 HOIP_0036100 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of pattern recognition receptors (PRRs) by viral single-stranded RNA(ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). HOIP:HOIP_0036101 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of COVID-19. PMID:32505227 MDA-5 signaling in COVID-19 HOIP_0036101 HOIP:HOIP_0036102 RIG-I signaling is a process that a signal is transmitted by the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. RIG-I signaling HOIP_0036102 HOIP:HOIP_0036103 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. MDA-5 signaling HOIP_0036103 HOIP:HOIP_0036104 IRF7 activation is a subtype of molecular activation: A process that changes the activity of the IRF7 to be higher. This process can constitute the course of coronavirus infectious disease. IRF7 activation in coronavirus infection HOIP_0036104 HOIP:HOIP_0036105 PKR signaling is a process that a signal is transmitted by the cytoplasmic pattern recognition receptor (PRR) PKR (also known as EIF2AK2) binding to viral RNA. PKR detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of COVID-19. PKR signaling in COVID-19 HOIP_0036105 HOIP:HOIP_0036106 TLR3 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 3. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. TLR3 signaling in COVID-19 HOIP_0036106 HOIP:HOIP_0036109 Antigen processing and presentation which is initiated by phagocytosis of antigen bound directly or indirectly to a cell surface toll-like receptor (TLR). This process can constitute the course of coronavirus infectious disease. antigen processing and presentation initiated by toll-like receptor mediated phagocytosis of antigen in coronavirus infection HOIP_0036109 HOIP:HOIP_0036112 Any process in which a virus stops, prevents, or reduces the activity of the host serine/threonine kinase TBK1. This process can constitute the course of COVID-19. PMID:32353859 PMID:32505227 suppression by virus of host TBK1 activity in COVID-19 HOIP_0036112 PMID:32353859 Several innate immune signalling proteins are targeted by SARS-CoV-2 viral proteins. The interferon pathway is targeted by NSP13 (TBK1 and TBKBP1), NSP15 (RNF41 (also known as NRDP1)) and ORF9b (TOMM70); and the NF-κB pathway is targeted by NSP13 (TLE1, TLE3 and TLE5) and ORF9c (NLRX1, F2RL1 and NDFIP2). Furthermore, two other E3 ubiquitin ligases that regulate antiviral innate immune signalling, TRIM59 and MIB1, are bound by ORF3a and NSP9, respectively PMID:32505227 SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3. HOIP:HOIP_0036117 The promotion of an immune response by natural killer cells through direct recognition of target cells or through the release of cytokines. This process can constitute the course of COVID-19. NK cell mediated immunity natural killer cell mediated immunity in COVID-19 HOIP_0036117 HOIP:HOIP_0036118 The change in morphology and behavior of a mature or immature natural killer T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific, leading to the initiation or perpetuation of an immune response. NK T cell activation involved in immune response HOIP_0036118 HOIP:HOIP_0036119 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. ISBN:0815341504 cellular response to type I interferon in coronavirus infection HOIP_0036119 ISBN:0815341504 ISBN:0815341504 Table 4.3 ISBN:0815341504 Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. PMID:33723416 In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. PMID:33153908 SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. PMID:32505227 TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. PMID:33153908 HOIP:HOIP_0036122 TLR3 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 3. TLR3 signaling HOIP_0036122 HOIP:HOIP_0036124 TLR3 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 3. This process can constitute the course of coronavirus infectious disease. TLR3 is a endosome TLR, which recognizes double strand RNA. TLR3 signaling in coronavirus infection HOIP_0036124 HOIP:HOIP_0036127 Viral entry-innate immune response imbalance is a subtype of stress response imbalance: A process that lacks a balance between the viral entry and the innate immune response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. viral entry-innate immune response imbalance in coronavirus infection HOIP_0036127 HOIP:HOIP_0036128 The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. natural killer cell activation in coronavirus infection HOIP_0036128 HOIP:HOIP_0036129 The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. natural killer cell activation in COVID-19 HOIP_0036129 HOIP:HOIP_0036132 IL-1beta processing is a subtype of protein processing: A process that IL-1beta maturation process achieved by the cleavage of pro IL-1beta. This process can constitute the course of severe COVID-19. IL-1beta processing in severe COVID-19 HOIP_0036132 HOIP:HOIP_0036135 Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activation of a host protein. suppression by virus of host molecular activation HOIP_0036135 HOIP:HOIP_0036136 Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. This is a mechanism by which the virus evades the host innate immune response. suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling HOIP_0036136 HOIP:HOIP_0036137 Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. suppression by virus of host type I interferon-mediated signaling HOIP_0036137 HOIP:HOIP_0036138 Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This process can constitute the course of coronavirus infectious disease. suppression by virus of host type I interferon-mediated signalingin coronavirus infection HOIP_0036138 HOIP:HOIP_0036139 Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This process can constitute the course of COVID-19. suppression by virus of host type I interferon-mediated signalingin COVID-19 HOIP_0036139 HOIP:HOIP_0036140 Type I interferon signaling is a subtype of biological signaling: A process transduced by the binding of a type I interferon to a receptor on the surface of a cell. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. reactome:R-HSA-909729.3 type I interferon signaling in coronavirus infection HOIP_0036140 HOIP:HOIP_0036145 IL6 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding of Interleukin 6. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. IL-6 signaling (very low) in COVID-19 drug treatment HOIP_0036145 HOIP:HOIP_0036146 Any process that decreases the rate, frequency or extent of the series of molecular events generated as a consequence of interleukin-6 binding to a cell surface receptor. negative regulation of IL-6-mediated signaling negative regulation of interleukin-6-mediated signaling HOIP_0036146 HOIP:HOIP_0036147 Any process that stops, prevents, or reduces the frequency, rate or extent of the cytokine mediated signaling pathway. negative regulation of cytokine-mediated signaling HOIP_0036147 HOIP:HOIP_0036149 Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm. This process can constitute the course of coronavirus infectious disease. viral penetration via host endosomal membrane disruption by virus viral penetration via perforation of host organellar membrane by virus viral penetration via permeabilization of host organellar membrane viral entry into host cell via permeabilization of host organelle membrane viral membrane-penetration protein permeabilization of host organelle membrane involved in viral entry into host cell in coronavirus infection HOIP_0036149 HOIP:HOIP_0036152 The inhibition of an antigen's biological effects by induction of immunogloblin G (IgG). immunoglobulin-mediated neutralization HOIP_0036152 HOIP:HOIP_0036155 IRF7 activation is a subtype of molecular activation: A process that changes the activity of the IRF7 to be higher. This process can constitute the course of COVID-19. IRF7 activation in COVID-19 HOIP_0036155 HOIP:HOIP_0036157 The appearance of immunoglobulin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of coronavirus infectious disease. antibody production immunoglobulin production in coronavirus infection HOIP_0036157 HOIP:HOIP_0036158 The appearance of immunoglobulin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. antibody production immunoglobulin production in COVID-19 HOIP_0036158 HOIP:HOIP_0036160 adaptive immune response An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). This process can constitute the course of COVID-19. adaptive immune response in COVID-19 HOIP_0036160 HOIP:HOIP_0036162 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. M1マクロファージは強力な抗菌エフェクター細胞である． reactive oxygen species biosynthetic process in coronavirus infection HOIP_0036162 HOIP:HOIP_0036163 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class I. This process can constitute the course of coronavirus infectious disease. positive regulation of MHC class I biosynthetic process in coronavirus infection HOIP_0036163 HOIP:HOIP_0036164 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class I. This process can constitute the course of COVID-19. positive regulation of MHC class I biosynthetic process in COVID-19 HOIP_0036164 HOIP:HOIP_0036166 The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. This process can constitute the course of coronavirus infectious disease. antigen processing and presentation of exogenous peptide antigen via MHC class I in coronavirus infection HOIP_0036166 HOIP:HOIP_0036167 The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. This process can constitute the course of COVID-19. antigen processing and presentation of exogenous peptide antigen via MHC class I in COVID-19 HOIP_0036167 HOIP:HOIP_0036168 Any apoptotic process in a cytotoxic T cell. This process can constitute the course of coronavirus infectious disease. cytotoxic T cell apoptotic process in coronavirus infection HOIP_0036168 HOIP:HOIP_0036169 Any apoptotic process in a cytotoxic T cell. This process can constitute the course of COVID-19. cytotoxic T cell apoptotic process in COVID-19 HOIP_0036169 HOIP:HOIP_0036170 Any apoptotic process in a natural killer cell, a lymphocyte that can spontaneously kill a variety of target cells without prior antigenic activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. natural killer cell apoptotic process in coronavirus infection HOIP_0036170 HOIP:HOIP_0036171 Any apoptotic process in a natural killer cell, a lymphocyte that can spontaneously kill a variety of target cells without prior antigenic activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. natural killer cell apoptotic process in COVID-19 HOIP_0036171 HOIP:HOIP_0036172 Removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue. removing infected cell HOIP_0036172 HOIP:HOIP_0036173 Removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. removing infected cell in coronavirus infection HOIP_0036173 HOIP:HOIP_0036174 Removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue. This process can constitute the course of COVID-19. removing infected cell in COVID-19 HOIP_0036174 HOIP:HOIP_0036175 NfkB signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by NF-kappaB. This process can constitute the course of coronavirus infectious disease. NfkB signalingin coronavirus infection HOIP_0036175 HOIP:HOIP_0036176 Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This process can constitute the course of coronavirus infectious disease. positive regulation of type I interferon production in coronavirus infection HOIP_0036176 HOIP:HOIP_0036177 type I interferon production The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:25301932 type I interferon production in coronavirus infection HOIP_0036177 HOIP:HOIP_0036178 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. interferon-alpha production in coronavirus infection HOIP_0036178 HOIP:HOIP_0036179 The appearance of interferon-beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. interferon-beta production in coronavirus infection HOIP_0036179 HOIP:HOIP_0036180 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of coronavirus infectious disease. PMID:32505227 MDA-5 signaling in coronavirus infection HOIP_0036180 HOIP:HOIP_0036181 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of coronavirus infectious disease. PMID:32505227 RIG-I signaling in coronavirus infection HOIP_0036181 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of pattern recognition receptors (PRRs) by viral single-stranded RNA(ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). HOIP:HOIP_0036182 PKR signaling is a process that a signal is transmitted by the cytoplasmic pattern recognition receptor (PRR) PKR (also known as EIF2AK2) binding to viral RNA. PKR detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of coronavirus infectious disease. PKR signaling in coronavirus infection HOIP_0036182 HOIP:HOIP_0036183 Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. A series of molecular signals passed on to downstream proteins within the cell via PKR (also known as EIF2AK3), an intracellular protein kinase that is activated by stress signals or upon binding to double-stranded RNA (dsRNA), followed by autophosphorylation. PKR plays a role in the antiviral response, phosphorylating proteins such as the translation initiation factor eIF2 to inhibit protein synthesis during viral infection. Begins with activation of PKR activity, and ends with regulation of a downstream cellular process, e.g. regulation of transcription or inhibition of translation. PKR signaling pathway HOIP_0036183 HOIP:HOIP_0036184 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This process can constitute the course of coronavirus infectious disease. apoptotic process in coronavirus infection HOIP_0036184 HOIP:HOIP_0036185 MAVS complex assembly is a subtype of protein complex assembly: A process that forms a complex consisting of MAVS. MAVS complex assembly HOIP_0036185 HOIP:HOIP_0036186 MAVS complex assembly is a subtype of protein complex assembly: A process that forms a complex consisting of MAVS. This process can constitute the course of coronavirus infectious disease. MAVS complex assembly in coronavirus infection HOIP_0036186 HOIP:HOIP_0036187 MAVS complex assembly is a subtype of protein complex assembly: A process that forms a complex consisting of MAVS. This process can constitute the course of COVID-19. MAVS complex assembly in COVID-19 HOIP_0036187 HOIP:HOIP_0036188 TBK1 activation is a subtype of molecular activation: A process that changes the activity of the TBK1 to be higher. This process can constitute the course of coronavirus infectious disease. TBK1 activation in coronavirus infection HOIP_0036188 HOIP:HOIP_0036189 TBK1 activation is a subtype of molecular activation: A process that changes the activity of the TBK1 to be higher. This process can constitute the course of COVID-19. TBK1 activation in COVID-19 HOIP_0036189 HOIP:HOIP_0036190 TBK1 activation is a subtype of molecular activation: A process that changes the activity of the TBK1 to be higher. TBK1 activation HOIP_0036190 HOIP:HOIP_0036191 IRF3 activation is a subtype of molecular activation: A process that changes the activity of the IRF3 to be higher. This process can constitute the course of coronavirus infectious disease. IRF3 activation in coronavirus infection HOIP_0036191 HOIP:HOIP_0036192 IRF3 activation is a subtype of molecular activation: A process that changes the activity of the IRF3 to be higher. This process can constitute the course of COVID-19. IRF3 activation in COVID-19 HOIP_0036192 HOIP:HOIP_0036193 IRF3 activation is a subtype of molecular activation: A process that changes the activity of the IRF3 to be higher. IRF3 activation HOIP_0036193 HOIP:HOIP_0036194 An inhibitor of TMPRSS2 TMPRSS2 inhibitor HOIP_0036194 HOIP:HOIP_0036198 An organism population persisting in a site it has colonized. colony HOIP_0036198 HOIP:HOIP_0036201 JAK signaling is a process that a signal is transmitted by the JAK (Janus kinase). This process can constitute the course of coronavirus infectious disease. JAK signaling in coronavirus infection HOIP_0036201 HOIP:HOIP_0036202 JAK signaling is a process that a signal is transmitted by the JAK (Janus kinase) . This process can constitute the course of COVID-19. JAK signaling in COVID-19 HOIP_0036202 HOIP:HOIP_0036203 STAT1 signaling is a process that a signal is transmitted by the STAT1 (signal transducer and activator of transcription 1) . STAT1 signaling HOIP_0036203 HOIP:HOIP_0036204 A series of molecular signals mediated by STAT3 (signal transducer and activator of transcription 3). STAT1 signal transduction pathway HOIP_0036204 HOIP:HOIP_0036205 STAT1 signaling is a process that a signal is transmitted by the STAT1 (signal transducer and activator of transcription 1). This process can constitute the course of coronavirus infectious disease. STAT1 signaling in coronavirus infection HOIP_0036205 HOIP:HOIP_0036206 STAT1 signaling is a process that a signal is transmitted by the STAT1 (signal transducer and activator of transcription 1). This process can constitute the course of COVID-19. STAT1 signaling in COVID-19 HOIP_0036206 HOIP:HOIP_0036209 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. cell death in coronavirus infection HOIP_0036209 HOIP:HOIP_0036213 IL6 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding of Interleukin 6. This process can constitute the course of coronavirus infectious disease. IL-6 signaling in coronavirus infection HOIP_0036213 HOIP:HOIP_0036215 Mitochondrial dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete mitochondrial function. This process can constitute the course of severe COVID-19. PMID:32697943 mitochondrial dysfunction (very high) in severe COVID-19 HOIP_0036215 PMID:32697943 Moreover, several components of respiratory electron chain com- plexes are downregulated in CoV-2-infected monocytes, such as NDUFV1 (complex I), SDHA (complex II), cytochrome c reductase COR1 and UQCRC2 (complex III), ATP5PF, ATP5F1A, ATP5PD, F-type ATPase a, and PPA2 (ATP synthase) (Figure S2D). In agreement with our proteomic data, the spare respiratory capacity was reduced in CoV-2-infected monocytes (Figure 3I). Reduced respiration in LPS-activated macrophages is known to increase mitochondrial ROS (mtROS) production (Mills et al., 2016). HOIP:HOIP_0036217 The process that results in the movement of mitochondriall DNA from the mitochondria. This process can constitute the course of severe COVID-19. release of DNA from mitochondria in severe COVID-19 HOIP_0036217 HOIP:HOIP_0036219 The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32325025 PMID:32697943 PMID:33123165 tumor necrosis factor production in COVID-19 HOIP_0036219 PMID:32325025 One of the major pathways for NF-κB activation after coronavirus infection is the MyD88 pathway through pattern recognition receptors (PRRs), leading to the induction of a variety of pro-inflammatory cytokines, including interleukin-6 (IL-6), tumor necrosis factor alpha (TNFα) and chemokines. The AngII-AT1R axis also activates NF-κB and disintegrin and metalloprotease 17 (ADAM17), which generates the mature form of epidermal growth factor receptor (EGFR) ligands and TNFα, two NF-κB stimulators (Eguchi et al., 2018). ADAM17 induction also processes the membrane form of IL-6Rα to the soluble form (sIL-6Rα), followed by the gp130-mediated activation of STAT3 via the sIL-6Rα-IL-6 complex in a variety of IL-6Rα-negative nonimmune cells including fibroblasts, endothelial cells, and epithelial cells (Murakami et al., 2019). STAT3 is required for full activation of the NF-κB pathway, and the main stimulator of STAT3 in vivo is IL-6, especially during inflammation, although there are nine other members of IL-6 family cytokines that can activate STAT3, at least in vitro (Murakami et al., 2019). Therefore, SARS-CoV-2 infection in the respiratory system can activate both NF-κB and STAT3, which in turn can activate the IL-6 amplifier (IL-6 Amp), a mechanism for the hyper-activation of NF-κB by STAT3, leading to multiple inflammatory and autoimmune diseases (Murakami et al., 2019). PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). PMID:33123165 For example, patients with severe COVID-19 had higher levels of IL-6, IL-2R, IL-10, and tumor necrosis factor alpha (TNF-alpha) than those with moderate disease, the former of which correlated with clinical severity and death. Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0036221 The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of coronavirus infectious disease. tumor necrosis factor production in coronavirus infection HOIP_0036221 HOIP:HOIP_0036222 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This process can constitute the course of COVID-19. PMID:32697943 apoptotic process in COVID-19 HOIP_0036222 PMID:32697943 CM-CoV-2 induced apoptosis of A549 cells (Figure 4D), which was prevented when CoV-2-infected monocytes were treated with a HIF-1a inhibitor (Figure 4D). HOIP:HOIP_0036223 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:32697943 cell death in COVID-19 HOIP_0036223 PMID:32629875 In COVID-19, adding to the blood clotting risk from increased IL-6, SARS-CoV-2 can infect, replicate and induce endothelial cell death, compromising the continuity of the luminal vascular surface; a perturbed endothelium can actively participate in pro-coagulant reactions. First, SARS-CoV-2 can cause endothelial cell death through lytic replication, as discussed in Section 4.1. PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS-CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. SARS-CoV-2-Induced Metabolic Reprogramming of Monocytes Directly Affects T Cell Response and Lung Epithelial Cell Death HOIP:HOIP_0036230 Increasing creatinine concentration is a subtype of increasing concentration: A process that changes the creatine kinase concentration to be higher. increasing creatine kinase concentration HOIP_0036230 HOIP:HOIP_0036233 The process in which an antigen-presenting cell expresses antigen (peptide or polysaccharide) on its cell surface in association with an MHC class II protein complex. This process can constitute the course of coronavirus infectious disease. The MHC-I pathway predominantly activates cytotoxic T lymphocytes, while the MHC-II pathway mainly activates helper T cells. Peptide-MHC-II complexes are recognozed by T cells with the CD4 surface marker protein (CD4+Tcells) via theit TCR-CD3 complex. The main type of T cell activation by this pathway is hepler T cells. Chapter 4.3 Viruses: Biology, Applications, and Control The MHC-I pathway predominantly activates cytotoxic T lymphocytes, while the MHC-II pathway mainly activates helper T cells. Peptide-MHC-II complexes are recognozed by T cells with the CD4 surface marker protein (CD4+Tcells) via theit TCR-CD3 complex. The main type of T cell activation by this pathway is hepler T cells. Chapter 4.3 Viruses: Biology, Applications, and Control antigen processing and presentation of exogenous peptide antigen via MHC class II in coronavirus infection HOIP_0036233 The MHC-I pathway predominantly activates cytotoxic T lymphocytes, while the MHC-II pathway mainly activates helper T cells. Peptide-MHC-II complexes are recognozed by T cells with the CD4 surface marker protein (CD4+Tcells) via theit TCR-CD3 complex. The main type of T cell activation by this pathway is hepler T cells. Chapter 4.3 Viruses: Biology, Applications, and Control ISBN:0815341504 HOIP:HOIP_0036236 The process in which an antigen-presenting cell expresses antigen (peptide or polysaccharide) on its cell surface in association with an MHC class II protein complex. This process can constitute the course of COVID-19. antigen processing and presentation of exogenous peptide antigen via MHC class II in COVID-19 HOIP_0036236 HOIP:HOIP_0036237 The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. neutrophil chemotaxis HOIP_0036237 HOIP:HOIP_0036239 A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation of inflammatory response or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. macrophage activation involved in inflammatory response in coronavirus infection HOIP_0036239 HOIP:HOIP_0036240 A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation of inflammatory response or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. macrophage activation involved in inflammatory response in COVID-19 HOIP_0036240 HOIP:HOIP_0036242 The appearance of interleukin-8 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of coronavirus infectious disease. macrophage CXCL8 production macrophage interleukin-8 production in coronavirus infection HOIP_0036242 HOIP:HOIP_0036243 The appearance of interleukin-8 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of COVID-19. macrophage CXCL8 production macrophage interleukin-8 production in COVID-19 HOIP_0036243 HOIP:HOIP_0036245 The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. This process can constitute the course of coronavirus infectious disease. neutrophil chemotaxisin coronavirus infection HOIP_0036245 HOIP:HOIP_0036246 The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. This process can constitute the course of COVID-19. PMID:33123165 Wikipedia:Inflammation neutrophil chemotaxisin COVID-19 HOIP_0036246 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0036252 The directed killing of a target cell by a neutrophil. This process can constitute the course of coronavirus infectious disease. neutrophil mediated cytotoxicity in coronavirus infection HOIP_0036252 HOIP:HOIP_0036253 The directed killing of a target cell by a neutrophil. This process can constitute the course of COVID-19. neutrophil mediated cytotoxicity in COVID-19 HOIP_0036253 HOIP:HOIP_0036255 The appearance of interleukin-6 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of coronavirus infectious disease. PMID:31623280 interleukin-6 production in coronavirus infection HOIP_0036255 PMID:31623280 Once inside cells, the viral RNAs are detected by the pattern recognition receptors (PRRs) which trigger a downstream cascade of molecules leading to the activation of the transcription factor nuclear factor-κB (NF-κB) and interferon regulatory factor 3 (IRF3), with the subsequent production of type I interferons (IFN-α/β) and a series of pro-inflammatory cytokines [2,9] including interleukin (IL)-1β and IL-6. The development of an uncontrolled inflammatory response can thus lead to potentially life-threatening damage to lung tissue. HOIP:HOIP_0036256 The appearance of any member of the interleukin-17 family of cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of coronavirus infectious disease. interleukin-17 production in coronavirus infection HOIP_0036256 HOIP:HOIP_0036257 The appearance of any member of the interleukin-17 family of cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of COVID-19. interleukin-17 production in COVID-19 HOIP_0036257 HOIP:HOIP_0036258 The appearance of any member of the interleukin-17 family of cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of severe COVID-19. interleukin-17 production in severe COVID-19 HOIP_0036258 HOIP:HOIP_0036259 The process in which a relatively unspecialized T cell acquires specialized features of a T-helper 2 (Th2) cell. A Th2 cell is a CD4-positive, alpha-beta T cell that has the phenotype GATA-3-positive and produces interleukin-4. T-helper 2 cell differentiation HOIP_0036259 HOIP:HOIP_0036261 Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm. This process can constitute the course of COVID-19. permeabilization of host organelle membrane involved in viral entry into host cell in COVID-19 HOIP_0036261 HOIP:HOIP_0036262 IL-17 signaling is a process that a signal is transmitted by the cytokine IL-17. IL-17 signaling HOIP_0036262 HOIP:HOIP_0036263 IL-17 signaling is a process that a signal is transmitted by the cytokine IL-17. This process can constitute the course of coronavirus infectious disease. IL-17 signaling in coronavirus infection HOIP_0036263 HOIP:HOIP_0036264 IL-17 signaling is a process that a signal is transmitted by the cytokine IL-17. This process can constitute the course of COVID-19. IL-17 signaling in COVID-19 HOIP_0036264 HOIP:HOIP_0036265 Any process that contributes to cytokine production by a T-helper 2 cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T-helper 2 cell cytokine production in coronavirus infection HOIP_0036265 HOIP:HOIP_0036266 Any process that contributes to cytokine production by a T-helper 2 cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. T-helper 2 cell cytokine production in COVID-19 HOIP_0036266 HOIP:HOIP_0036268 The process in which a relatively unspecialized T cell acquires specialized features of a T-helper 2 (Th2) cell. A Th2 cell is a CD4-positive, alpha-beta T cell that has the phenotype GATA-3-positive and produces interleukin-4. This process can constitute the course of coronavirus infectious disease. T-helper 2 cell differentiation in coronavirus infection HOIP_0036268 HOIP:HOIP_0036269 The process in which a relatively unspecialized T cell acquires specialized features of a T-helper 2 (Th2) cell. A Th2 cell is a CD4-positive, alpha-beta T cell that has the phenotype GATA-3-positive and produces interleukin-4. This process can constitute the course of COVID-19. T-helper 2 cell differentiation in COVID-19 HOIP_0036269 HOIP:HOIP_0036275 IL-17 signaling is a process that a signal is transmitted by the cytokine IL-17. This process can constitute the course of severe COVID-19. IL-17 signaling in severe COVID-19 HOIP_0036275 HOIP:HOIP_0036276 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 17 (Th17) cell. A Th17 cell is a CD4-positive, alpha-beta T cell with the phenotype RORgamma-t-positive that produces IL-17. This process can constitute the course of coronavirus infectious disease. T-helper 17 cell differentiation in coronavirus infection HOIP_0036276 HOIP:HOIP_0036281 Any process that contributes to cytokine production by a T-helper 1 cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T-helper 1 cell cytokine production in coronavirus infection HOIP_0036281 HOIP:HOIP_0036283 Any process that contributes to cytokine production by a T-helper 1 cell. This process can constitute the course of COVID-19. T-helper 1 cell cytokine production in COVID-19 HOIP_0036283 HOIP:HOIP_0036284 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 17 (Th17) cell. A Th17 cell is a CD4-positive, alpha-beta T cell with the phenotype RORgamma-t-positive that produces IL-17. This process can constitute the course of COVID-19. T-helper 17 cell differentiation in COVID-19 HOIP_0036284 HOIP:HOIP_0036285 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 17 (Th17) cell. A Th17 cell is a CD4-positive, alpha-beta T cell with the phenotype RORgamma-t-positive that produces IL-17. This process can constitute the course of severe COVID-19. T-helper 17 cell differentiation in severe COVID-19 HOIP_0036285 HOIP:HOIP_0036286 Any process that contributes to cytokine production by a T-helper 17 cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T-helper 17 cell cytokine production in coronavirus infection HOIP_0036286 HOIP:HOIP_0036287 Any process that contributes to cytokine production by a T-helper 17 cell. This process can constitute the course of COVID-19. T-helper 17 cell cytokine production in COVID-19 HOIP_0036287 HOIP:HOIP_0036288 Any process that contributes to cytokine production by a T-helper 17 cell. This process can constitute the course of severe COVID-19. T-helper 17 cell cytokine production in severe COVID-19 HOIP_0036288 HOIP:HOIP_0036289 Any process that contributes to cytokine production by a T-helper 17 cell. T-helper 17 cell cytokine production HOIP_0036289 HOIP:HOIP_0036291 TGF beta receptor signaling is a subtype of signaling that a signal is transmitted by the TGF beta receptor (transforming growth factor beta receptor) on the surface of a cell, starting with a ligand binding to a TGFR. This process can constitute the course of coronavirus infectious disease. TGF beta receptor signaling in coronavirus infection HOIP_0036291 HOIP:HOIP_0036293 TGF beta receptor signaling is a subtype of signaling that a signal is transmitted by the TGF beta receptor (transforming growth factor beta receptor) on the surface of a cell, starting with a ligand binding to a TGFR. This process can constitute the course of COVID-19. TGF beta receptor signaling in COVID-19 HOIP_0036293 HOIP:HOIP_0036294 TGF beta receptor signaling is a subtype of signaling that a signal is transmitted by the TGF beta receptor (transforming growth factor beta receptor) on the surface of a cell, starting with a ligand binding to a TGFR. This process can constitute the course of COVID-19. TGF beta receptor signaling in COVID-19 HOIP_0036294 HOIP:HOIP_0036295 Any immune responses of an organism against its own healthy cells and tissues. autoimmune response HOIP_0036295 HOIP:HOIP_0036296 Any immune responses of an organism against its own healthy cells and tissues. This process can constitute the course of coronavirus infectious disease. autoimmune response in coronavirus infection HOIP_0036296 HOIP:HOIP_0036297 Any immune responses of an organism against its own healthy cells and tissues. This process can constitute the course of COVID-19. autoimmune response in COVID-19 HOIP_0036297 HOIP:HOIP_0036298 Any immune responses of an organism against its own healthy cells and tissues. This process can constitute the course of severe COVID-19. autoimmune response in severe COVID-19 HOIP_0036298 HOIP:HOIP_0036301 Interacting selectively and non-covalently with a virion, either by binding to components of the capsid or the viral envelope. This process can constitute the course of coronavirus infectious disease. virion binding with host cell surface receptor in coronavirus infection HOIP_0036301 HOIP:HOIP_0036305 Negative regulation of angiotensin II hydrolysis is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of angiotensin II hydrolysis. ACE2 hydrolyzes Angiotensin II and produces Angiotensin-(1-7). negative regulation of Angiotensin II hydrolysis HOIP_0036305 HOIP:HOIP_0036306 angiotensin II hydrolysis is a subtype of hydrolysis: A chemical reaction that uses water to break down a angiotensin II ACE2 hydrolyzes Angiotensin II and produces Angiotensin-(1-7). Angiotensin II hydrolysis HOIP_0036306 HOIP:HOIP_0036310 The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration. This process can constitute the course of coronavirus infectious disease. viral attachment to host entry receptor entry receptor-mediated virion attachment to host cell in coronavirus infection HOIP_0036310 HOIP:HOIP_0036311 Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. This process can constitute the course of coronavirus infectious disease. PMID:32641482 PMID:32690910 PMID:33116300 receptor-mediated endocytosis of virus by host cell in coronavirus infection HOIP_0036311 PMID:32641482 The entry process begins by the binding of viral envelope spike proteins to their specific receptors on the plasma membrane, which triggers endocytosis to internalize the viruses into the endocytic vesicles. PMID:32690910 Alternatively, SARS- CoV-2 can also use an endosomal entry pathway, whereby the ACE2–virus complex is translocated to endosomes and S protein priming is performed by the endosomal cysteine proteases cathepsin B and cathepsin L, after which the virus is released from the endosome into the cytoplasm. PMID:33116300 Besides receptor binding, the proteolytic cleavage of coronavirus S proteins by host cell-derived proteases is essential to permit fusion24,25. SARS-CoV has been shown to use the cell-surface serine protease TMPRSS2 for priming and entry, although the endosomal cysteine proteases cathepsin B (CatB) and CatL can also assist in this process HOIP:HOIP_0036312 Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. This process can constitute the course of coronavirus infectious disease. PMID:32641482 fusion of virus membrane with host endosome membrane in coronavirus infection HOIP_0036312 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0036314 Increasing cellular membrane permeability is a subtype of increasing membrane permeabilization: A process that changes the permeability of the cellular membrane to be higher. increasing cellular membrane permeability HOIP_0036314 HOIP:HOIP_0036316 Interacting selectively and non-covalently with a receptor on the host cell surface. This process can constitute the course of coronavirus infectious disease. PMID:32641482 host cell surface receptor binding in coronavirus infection HOIP_0036316 PMID:32641482 The entry process begins by the binding of viral envelope spike proteins to their specific receptors on the plasma membrane, which triggers endocytosis to internalize the viruses into the endocytic vesicles. HOIP:HOIP_0036317 Interacting selectively and non-covalently with the surface of a host cell. This process can constitute the course of coronavirus infectious disease. host cell surface binding in coronavirus infection HOIP_0036317 HOIP:HOIP_0036318 Fusion of a viral membrane with the host cell membrane during viral entry. Results in release of the virion contents into the cytoplasm. This process can constitute the course of coronavirus infectious disease. fusion of virus membrane with host plasma membrane in coronavirus infection HOIP_0036318 HOIP:HOIP_0036319 Accumulation of abnormal proteins is a subtype of protein accumulation: A process that keeps Angiotensin II in a biological object. Angiotensin II accumulation HOIP_0036319 HOIP:HOIP_0036323 Interacting selectively and non-covalently with a virion, either by binding to components of the capsid or the viral envelope. This process can constitute the course of COVID-19. virion binding with host cell surface receptor in COVID-19 HOIP_0036323 HOIP:HOIP_0036326 Cleavage of viral spike protein is a subtype of proteolysis: A process in which ciral spike protein is cleaved. This process can constitute the course of coronavirus infectious disease. PMID:32641482 PMID:33116300 cleavage of viral spike protein in coronavirus infection HOIP_0036326 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. PMID:33116300 Coronavirus particles bind to cellular attachment factors and specific S interactions with the cellular receptors (such as angiotensin-converting enzyme 2 (ACE2)), together with host factors (such as the cell surface serine protease TMPRSS2), promote viral uptake and fusion at the cellular or endosomal membrane. SARS-CoV has been shown to use the cell-surface serine protease TMPRSS2 for priming and entry, although the endosomal cysteine proteases cathepsin B (CatB) and CatL can also assist in this proces. HOIP:HOIP_0036335 angiotensin signaling is a process that a signal is transmitted by angiotensin. angiotensin signaling HOIP_0036335 HOIP:HOIP_0036336 The series of molecular signals generated as a consequence of angiotensin II binding to an angiotensin receptor on the surface of the cell, and proceeding with the activated receptor transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity. Ends with regulation of a downstream cellular process, e.g. transcription. angiotensin-activated signaling pathway HOIP_0036336 HOIP:HOIP_0036345 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile. serine protease HOIP_0036345 HOIP:HOIP_0036346 Cleavage of viral spike protein is a subtype of proteolysis: A process in which ciral spike protein is cleaved. cleavage of viral spike protein HOIP_0036346 HOIP:HOIP_0036347 Cleavage of viral spike protein S2 is a subtype of proteolysis: A process in which viral spike protein s2 is cleaved. This process can constitute the course of coronavirus infectious disease. PMID:33116300 cleavage of viral spike S2 protein in coronavirus infection HOIP_0036347 PMID:33116300 Coronavirus S proteins are homotrimeric class I fusion glycoproteins that are divided into two functionally distinct parts (S1 and S2) (Fig. 2). The surface-exposed S1 contains the receptor-binding domain (RBD) that specifically engages the host cell receptor, thereby determining virus cell tropism and pathogenicity. The transmembrane S2 domain contains heptad repeat regions and the fusion peptide, which mediate the fusion of viral and cellular membranes upon extensive conformational rearrangements. HOIP:HOIP_0036348 Cleavage of viral spike protein is a subtype of proteolysis: A process in which viral spike protein is cleaved. This process can constitute the course of COVID-19. PMID:33116300 cleavage of viral spike S2 protein in COVID-19 HOIP_0036348 HOIP:HOIP_0036349 Cleavage of viral spike protein is a subtype of proteolysis: A process in which ciral spike protein is cleaved. This process can constitute the course of COVID-19. PMID:32142651 PMID:32221306 PMID:32361028 PMID:32362314 PMID:32404436 PMID:33123165 cleavage of viral spike S protein in COVID-19 HOIP_0036349 PMID:32142651 Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases. Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. PMID:32221306 While cathepsin B inhibitor treatment did not show any marked effect on virus entry, cathepsin L inhibition treatment decreased entry of SARS-CoV-2 S pseudovirions into 293/hACE2 by over 76% (Fig. 4a), suggesting that cathepsin L should be essential for priming of SARS-CoV-2 S protein in lysosome for entry into 293/hACE2 cells. PMID:32361028 SARS-Cov-2 entry into a cell is dependent upon binding of the viral spike (S) protein to cellular receptor and on cleavage of the spike protein by the host cell proteases such as Cathepsin L and Cathepsin B. PMID:32362314 Furin Cleaves the SARS-CoV-2 Spike Protein at the S1/ S2 Site, and Cleavage Is Required for Efficient Cell-Cell Fusion SARS-2-S expression triggered syncytium formation that was strongly increased by trypsin and TMPRSS2. PMID:32404436 Following receptor engagement, SARS-CoV-2 S is processed by a plasma membrane-associated type II transmembrane serine protease, TMPRSS2, prior to membrane fusion which is essential to release the viral contents into the host cell cytosol (3, 6). Here, we present evidence that SARS-CoV-2 infects human mature enterocytes from the apical surface and triggers epithelial cell fusion. TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion. PMID:33123165 Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0036354 A system consisting of renin, angiotensin-converting enzyme, and angiotensin II. Renin, an enzyme produced in the kidney, acts on angiotensinogen, an alpha-2 globulin produced by the liver, forming angiotensin I. The converting enzyme contained in the lung acts on angiotensin I in the plasma converting it to angiotensin II, the most powerful directly pressor substance known. It causes contraction of the arteriolar smooth muscle and has other indirect actions mediated through the adrenal cortex. renin-angiotensin system HOIP_0036354 HOIP:HOIP_0036376 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. viral colonization HOIP_0036376 HOIP:HOIP_0036377 Any compound that inhibits the biosynthesis of any sterol. cytokine biosynthesis inhibitor cytokine synthesis inhibitor HOIP_0036377 HOIP:HOIP_0036380 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. establishment of virus infection in coronavirus infection HOIP_0036380 HOIP:HOIP_0036381 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This process can constitute the course of COVID-19. establishment of virus infection in COVID-19 HOIP_0036381 HOIP:HOIP_0036386 Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the strain of coronavirus that causes coronavirus disease 2019 (COVID-19), the respiratory illness responsible for the COVID-19 pandemic. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the strain of coronavirus that causes coronavirus disease 2019 (COVID-19), the respiratory illness responsible for the COVID-19 pandemic. severe acute respiratory syndrome coronavirus 2 SARS-CoV-2 HOIP_0036386 Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the strain of coronavirus that causes coronavirus disease 2019 (COVID-19), the respiratory illness responsible for the COVID-19 pandemic. Wikipedia:Severe_acute_respiratory_syndrome_coronavirus HOIP:HOIP_0036387 Severe acute respiratory syndrome coronavirus (SARS-CoV or SARS-CoV-1) is a strain of virus that causes severe acute respiratory syndrome (SARS). Severe acute respiratory syndrome coronavirus (SARS-CoV or SARS-CoV-1) is a strain of virus that causes severe acute respiratory syndrome (SARS). https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus severe acute respiratory syndrome coronavirus SARS-CoV HOIP_0036387 Severe acute respiratory syndrome coronavirus (SARS-CoV or SARS-CoV-1) is a strain of virus that causes severe acute respiratory syndrome (SARS). Wikipedia:Severe_acute_respiratory_syndrome_coronavirus HOIP:HOIP_0036467 Changing symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. changing symbiotic balance between host and virus HOIP_0036467 HOIP:HOIP_0036469 COVID-19 infectious course (balance) is a subtype of coronavirus infectious course (balance). The totality of all processes to a homeostatic balance between functional supply by the immune system and functional demand by SARS-CoV2. COVID-19 infectious course (homeostasis balance) HOIP_0036469 HOIP:HOIP_0036477 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. decreasing number of virus HOIP_0036477 HOIP:HOIP_0036503 Negative regulation of virus transport is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of virus transport. negative regulation of virus transport HOIP_0036503 HOIP:HOIP_0036509 Coronavirus infectious course (balance) is a subtype of coronavirus infectious course. The totality of all processes to a homeostatic balance between functional supply by the immune system and functional demand by coronaviruses. corona virus infectious course (homeostasis balance) HOIP_0036509 HOIP:HOIP_0036518 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. This process can constitute the course of coronavirus infectious disease (homeostatic balance). decreasing number of virus in coronavirus infectious disease (homeostatic balance) HOIP_0036518 HOIP:HOIP_0037001 Coronavirus infectious course (homeostatic imbalance) is a subtype of coronavirus infectious course. The totality of all processes to a homeostatic imbalance between functional supply by the immune system and functional demand by coronaviruses. corona virus infectious course (homeostatic imbalance) HOIP_0037001 HOIP:HOIP_0037002 COVID-19 infectious course (homeostatic imbalance) is a subtype of coronavirus infectious course (homeostatic imbalance). The totality of all processes to a homeostatic imbalance between functional supply by the immune system and functional demand by SARS-CoV2. COVID-19 infectious course (homeostatic imbalance) HOIP_0037002 HOIP:HOIP_0037004 Coronavirus infectious disease dependent process is a subtype of the ｃおcourse-dependent process: A process that can constitute the coronavirus infectious disease course and its subclasses. coronavirus infectous disease dependent process HOIP_0037004 HOIP:HOIP_0037012 The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration. This process can constitute the course of COVID-19. PMID:33462185 viral attachment to host entry receptor entry receptor-mediated virion attachment to host cell in COVID-19 HOIP_0037012 PMID:33462185 The SARS-CoV-2 spike (S) glycoproteins facilitate the binding and subsequent fusion of this coronavirus with the host cell membrane. These are cleaved (during the host cell entry or the production of SARS-CoV-2 particles) into two components that remain non-covalently linked, namely S1 which constitutes the cell connecting head of this molecule and S2 which remains anchored to the viral membrane and facilitates its fusion. As such, S1 binds to angiotensin-converting enzyme 2 (ACE2) on the cell membrane, whilst S2 mediates the fusion between the viral and host cell membranes after proteolytic exposure of a S2 fusion peptide by transmembrane protease serine 2 (TMPRSS2) or other host cell proteases, such as furin, located within the host cell secretory pathway and endocytic compartments. Indeed, furin cleaves the SARS-CoV-2 S glycoprotein at the S1-S2 junction/boundary which consists of a sequence of basic amino acids. Notably, this furin-mediated cleavage of the polybasic S1-S2 junction exposes a carboxyl-terminal motif [RRAR, where R represents arginine (Arg): Arg-Arg-Ala-Arg], which conforms to the “C-end rule” (CendR) motif [R-XX-R, where R represents arginine (Arg) and can be substituted by lysine (Lys), whilst X can be any amino acid]. This CendR motif of S1 can bind to neuropilin-1 via its b1 domain (NRP1; a pleiotropic single-transmembrane co-receptor for class-3 semaphorins and vascular endothelial growth factors), which is shown to act as a host cell mediator that can increase the SARS-CoV-2 infectivity and contribute to its tissue/organ tropism. HOIP:HOIP_0037016 The replication of a viral RNA genome. viral RNA genome replication HOIP_0037016 HOIP:HOIP_0037021 Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. This process can constitute the course of COVID-19. PMID:32221306 PMID:32361028 PMID:33116300 receptor mediated endocytosis by host of virus particle in COVID-19 receptor mediated endocytosis of virus by host in COVID-19 receptor mediated endocytosis of virus particle by host in COVID-19 receptor-mediated endocytosis of virus by host in COVID-19 viral receptor mediated endocytosis in COVID-19 virus receptor-mediated endocytosis by host in COVID-19 viral entry into host cell via receptor-mediated endocytosis viral entry into host cell via receptor-mediated endocytosis viral entry into host cell via receptor-mediated endocytosis in COVID-19 receptor-mediated endocytosis of virus by host cell in COVID-19 HOIP_0037021 PMID:32221306 Here, using SARS-CoV-2 S protein pseudovirus system, we confirm that human angiotensin converting enzyme 2 (hACE2) is the receptor for SARS-CoV-2, find that SARS-CoV-2 enters 293/hACE2 cells mainly through endocytosis, that PIKfyve, TPC2, and cathepsin L are critical for entry, and that SARS-CoV-2 S protein is less stable than SARS-CoV S. Phosphoinositides play many essential roles in endocytosis. Among them, one is phosphatidylinositol-3,5-bisphosphate (PI(3,5)P2), which regulates early endosome to late endosome dynamics. Two pore channel subtype 2 (TPC2) and TRPML1 in lysosome are two major downstream effectors of PI(3,5)P2. We confirmed this in this study, and further showed that blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. PMID:32361028 Host protease dependence of SARS-CoV-2 entry is a critical step. SARS-CoV takes advantage of the endosomal cysteine proteases Cathepsin B and L (CTSL and CTSB). CTSL/B are crucial elements of lysosomal pathway and both enzymes are almost exclusively located in the lysosomes. PMID:33116300 Besides receptor binding, the proteolytic cleavage of coronavirus S proteins by host cell-derived proteases is essential to permit fusion24,25. SARS-CoV has been shown to use the cell-surface serine protease TMPRSS2 for priming and entry, although the endosomal cysteine proteases cathepsin B (CatB) and CatL can also assist in this process viral entry into host cell via receptor-mediated endocytosis GOC:bf GOC:jl HOIP:HOIP_0037024 Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. This process can constitute the course of COVID-19. fusion of virus membrane with host endosomal membrane fusion of virus membrane with host endosome membrane in COVID-19 HOIP_0037024 HOIP:HOIP_0037028 Fusion of a viral membrane with the host cell membrane during viral entry. Results in release of the virion contents into the cytoplasm. This process can constitute the course of COVID-19. PMID:32155444 PMID:32404436 PMID:32704094 PMID:33123165 fusion of virus membrane with host plasma membrane in COVID-19 HOIP_0037028 PMID:32155444 As a result, SARS-CoV-2 SB opening is expected to be necessary for interacting with ACE2 at the host cell surface and initiating the conformational changes leading to cleavage of the S2' site, membrane fusion and viral entry (Gui et al., 2017; Kirchdoerfer et al., 2018; Millet and Whittaker, 2014; Pallesen et al., 2017; Park et al., 2016; Song et al., 2018; Walls et al., 2019; Yuan et al., 2017). PMID:32404436 Following receptor engagement, SARS-CoV-2 S is processed by a plasma membrane-associated type II transmembrane serine protease, TMPRSS2, prior to membrane fusion which is essential to release the viral contents into the host cell cytosol (3, 6). Here, we present evidence that SARS-CoV-2 infects human mature enterocytes from the apical surface and triggers epithelial cell fusion. TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion. TMPRSS4 expression triggered S-mediated cell-cell fusion, although to a lesser extent than TMPRSS2 (Fig. 3E). PMID:32704094 Mechanistic studies revealed that LY6E inhibits CoV entry into cells by interfering with spike protein-mediated membrane fusion. LY6E reduced CoV S-mediated cell–cell fusion of HCoV-229E (Fig.2e,f), MERS-CoV (Fig.2e,f) and SARS-CoV-2 (Fig. 2g,h), as visualized by a reduction of GFP-positive syncytia, indicating that LY6E blocks the fusion of viral and cellular membranes. PMID:33123165 Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0037030 A viral genome replication process where the template genome is positive stranded, single stranded RNA ((+)ssRNA). Replication of the positive strand leads to dsRNA formation, which in turn is transcribed into positive single stranded RNA. This process can constitute the course of COVID-19. PMID:32629875 PMID:32697943 PMID:32726803 positive stranded viral RNA replication in COVID-19 HOIP_0037030 PMID:32629875 However, a study in twelve patients with COVID-19 reported significantly increased plasma levels of angiotensin II, which appeared to directly correlate with circulating SARS-CoV-2 RNA levels and degree of hypoxia. Since SARS-CoV-2 can infect the epithelial cells on the luminal side of the small intestine and the virus has been detected in stools and rectal swabs, gastrointestinal symptoms are potentially attributable to viral infection and replication in the intestine. Vascular pathology of COVID-19 is most prominent in the lungs (Section 5.2), which is not unexpected since in COVID-19 the respiratory epithelium is the site of primary SARS-CoV-2 replication with secondary destruction of the pulmonary parenchyma. PMID:32697943 Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. PMID:32726803 For SCoV2-PLpro, these interactions include PRKDC (associated with induction by type I interferons), heterogenous nuclear ribonucleoprotein K (HNRNPK; involved in host RNA splicing, a process essential for SARS-CoV-2 replication in cells) and galectin1, which can induce viral fusion with target cells during HIV infection (Fig. 4a). The SARS-CoV-2 genome shares high sequence identity with SARS-CoV7,8. Both viruses critically rely on the activity of viral proteases: the main protease (Mpro, also known as 3CLpro or non-structural protein 5 (nsp5)) and the papain-like protease (PLpro, the protease domain of nsp3) to generate a functional replicase complex and enable viral spread. HOIP:HOIP_0037031 A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. This process can constitute the course of COVID-19. viral genome expression viral gene expression in COVID-19 HOIP_0037031 HOIP:HOIP_0037032 A process by which viral mRNA is translated into viral protein, using the host cellular machinery. This process can constitute the course of COVID-19. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis viral translation in COVID-19 HOIP_0037032 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0037040 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This process can constitute the course of COVID-19. antiviral innate immune response in COVID-19 HOIP_0037040 HOIP:HOIP_0037043 Viral entry-innate immune response imbalance is a subtype of stress response imbalance: A process that lacks a balance between the viral entry and the innate immune response as biological defence response. viral entry-innate immune response imbalance HOIP_0037043 HOIP:HOIP_0037044 Viral entry-innate immune response imbalance is a subtype of stress response imbalance: A process that lacks a balance between the viral entry and the innate immune response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. viral entry-innate immune response imbalance in COVID-19 HOIP_0037044 HOIP:HOIP_0037048 coronavirus infectious disease dependent chemical entity is a subtype of disease course dependent chemical entity. This entity can participate in the course of coronavirus infectious disease . coronavirus infectious disease dependent chemical entity HOIP_0037048 HOIP:HOIP_0037049 Coronavirus infectious disease dependent molecule is a subtype of disease course dependent chemical entity. This entity can participate in the course of coronavirus infectious disease as a gene product. Gene profile: human coronavirus infectious disease dependent molecule (human) HOIP_0037049 HOIP:HOIP_0037052 Coronavirus infectious disease dependent molecule is a subtype of course dependent chemical entity. This entity can participate in the course of coronavirus infectious disease as a gene product. Gene profile:caonical that described in textbooks or articles. coronavirus infectious disease dependent molecule (canonical) HOIP_0037052 HOIP:HOIP_0037055 Coronavirus infectious disease dependent molecule is a subtype of disease course dependent chemical entity. This entity can participate in the course of coronavirus infectious disease as a gene product. Gene profile: virus coronavirus infectious disease dependent molecule (virus) HOIP_0037055 HOIP:HOIP_0037056 The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. This process can constitute the course of COVID-19. viral absorption virion attachment to host cell surface receptor in COVID-19 viral attachment to host cell in COVID-19 virion attachment to host cell in COVID-19 HOIP_0037056 HOIP:HOIP_0037060 Interacting selectively and non-covalently with the surface of a host cell. This process can constitute the course of COVID-19. host cell surface binding in COVID-19 HOIP_0037060 HOIP:HOIP_0037062 The process by which an incoming virus is disassembled in the host cell to release a replication-competent viral genome. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. viral uncoating uncoating of virus in COVID-19 HOIP_0037062 HOIP:HOIP_0037065 A viral genome replication process where the template genome is positive stranded, single stranded RNA ((+)ssRNA). Replication of the positive strand leads to dsRNA formation, which in turn is transcribed into positive single stranded RNA. This process can constitute the course of coronavirus infectious disease. PMID:32641482 positive stranded viral RNA replication in coronavirus infection HOIP_0037065 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0037066 A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. virion assembly in coronavirus infection HOIP_0037066 HOIP:HOIP_0037067 A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. viral assembly viral particle assembly virion assembly and maintenance virion organization virus assembly virus particle assembly virion assembly in COVID-19 HOIP_0037067 HOIP:HOIP_0037069 Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. This process can constitute the course of COVID-19. viral protein processing in COVID-19 HOIP_0037069 HOIP:HOIP_0037070 The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. This process can constitute the course of coronavirus infectious disease. viral absorption viral attachment to host cell virion attachment to host cell in coronavirus infection HOIP_0037070 HOIP:HOIP_0037071 The process by which an incoming virus is disassembled in the host cell to release a replication-competent viral genome. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:32641482 viral uncoating uncoating of virus in coronavirus infection HOIP_0037071 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0037072 A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. This process can constitute the course of coronavirus infectious disease. PMID:32641482 viral genome expression viral gene expression in coronavirus infection HOIP_0037072 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0037073 A process by which subgenomic negative stranded viral mRNA is translated into viral protein, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis subgenomic negative stranded viral mRNA viral translation in coronavirus infection HOIP_0037073 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0037074 The cleavage of a peptide bond or bonds within a viral protein. This process can constitute the course of coronavirus infectious disease. viral protein processing in coronavirus infection HOIP_0037074 HOIP:HOIP_0037076 TLR7 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 7 TLR7 signaling HOIP_0037076 HOIP:HOIP_0037078 TLR7 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 7. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. TLR7 signaling in COVID-19 HOIP_0037078 HOIP:HOIP_0037080 A role played by the entity which receives RNA and transmits operand(s). RNA sensor HOIP_0037080 HOIP:HOIP_0037081 A role played by the entity which receives viral RNA and transmits operand(s). single-strand RNA sensor HOIP_0037081 HOIP:HOIP_0037082 NfkB signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by NF-kappaB. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32325025 PMID:32505227 PMID:32726803 Wikipedia:NF-κB NfkB signaling in COVID-19 HOIP_0037082 PMID:32325025 SARS-CoV-2 itself activates NF-kB via pattern recognition receptors (PPRs), and the accumulated AngII induces inflammatory cytokines including TNFa and IL-6-soluble (s)IL-6R via disintegrin and metalloprotease 17 (ADAM17), followed by activation of the IL-6 amplifier (IL-6 AMP), which describes enhanced NF-kB activation machinery via the coactivation of NF-kB and transcription factor STAT3. PMID:32505227 Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. PMID:32726803 Here we perform biochemical, structural and functional characterization of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) PLpro (SCoV2-PLpro) and outline differences with SARS-CoV PLpro (SCoV-PLpro) in regulation of host interferon and NF-κB pathways. Moreover, phosphorylation of IRF3 and TBK1, markers for IFN pathway activation, and p65 phosphorylation, used to monitor NF-κB pathway activation, were increased in SARS-CoV-2-infected cells upon GRL-0617 treatment (Fig. 5f). Wikipedia:NF-κB NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) is a protein complex that controls transcription of DNA, cytokine production and cell survival. HOIP:HOIP_0037089 The appearance of interleukin-6 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 PMID:32629875 PMID:33123165 interleukin-6 production in COVID-19 HOIP_0037089 PMID:32629875 In COVID-19, adding to the blood clotting risk from increased IL-6, SARS-CoV-2 can infect, replicate and induce endothelial cell death, compromising the continuity of the luminal vascular surface; a perturbed endothelium can actively participate in pro-coagulant reactions. PMID:33123165 The resultant inflammatory response provides immediate antiviral immunity via activation of antiviral type 1 and 3 interferon (IFN) pathways leading to an upregulation of inflammatory cytokines such as interleukin 6 (IL-6) and IL-1β, further recruiting neutrophils, other innate immune cells and stimulating anti-SARS-CoV-2 adaptive memory T cells and B cells (Figure 2). HOIP:HOIP_0037090 The appearance of interferon-beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 interferon-beta production in COVID-19 HOIP_0037090 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0037091 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 interferon-alpha production in COVID-19 HOIP_0037091 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0037098 interferon-gamma production The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This process can constitute the course of COVID-19. interferon-gamma production in COVID-19 HOIP_0037098 HOIP:HOIP_0037108 Type I interferon signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by Type I interferon. Type I interferon signaling HOIP_0037108 HOIP:HOIP_0037110 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. response to type I interferon HOIP_0037110 HOIP:HOIP_0037112 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. cellular response to type I interferon in COVID-19 HOIP_0037112 HOIP:HOIP_0037113 Type I interferon signaling is a subtype of biological signaling: A process transduced by the binding of a type I interferon to a receptor on the surface of a cell. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 PMID:32726803 type I interferon signaling in COVID-19 HOIP_0037113 PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). PMID:32726803 For SCoV2-PLpro, these interactions include PRKDC (associated with induction by type I interferons), heterogenous nuclear ribonucleoprotein K (HNRNPK; involved in host RNA splicing, a process essential for SARS-CoV-2 replication in cells) and galectin1, which can induce viral fusion with target cells during HIV infection (Fig. 4a). Moreover, phosphorylation of IRF3 and TBK1, markers for IFN pathway activation, and p65 phosphorylation, used to monitor NF-κB pathway activation, were increased in SARS-CoV-2-infected cells upon GRL-0617 treatment (Fig. 5f). HOIP:HOIP_0037114 IL6 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding of Interleukin 6. This process can constitute the course of COVID-19. IL-6 signaling in COVID-19 HOIP_0037114 HOIP:HOIP_0037115 type I interferon production The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:25301932 type I interferon production in COVID-19 HOIP_0037115 HOIP:HOIP_0037117 Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This process can constitute the course of COVID-19. positive regulation of type I interferon production in COVID-19 HOIP_0037117 HOIP:HOIP_0037120 TLR7 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 7. This process can constitute the course of coronavirus infectious disease. TLR7/8 is a endosome TLR, which recognizes single strand RNA. TLR7 signaling in coronavirus infection HOIP_0037120 HOIP:HOIP_0038002 The totality of all processes through which MERS infection is realized. MERS infectious course HOIP_0038002 HOIP:HOIP_0038003 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. viral proliferation HOIP_0038003 HOIP:HOIP_0038004 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. This process can constitute the course of coronavirus infectious disease. コロナウイルス感染機序におけるウイルス増殖 viral proliferation in coronavirus infection HOIP_0038004 HOIP:HOIP_0038005 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. This process can constitute the course of COVID-19 (homeostatic balance). decreasing number of virus in COVID-19 (homeostatic balance) HOIP_0038005 HOIP:HOIP_0038006 Negative regulation of virus transport is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of virus transport. This process can constitute the course of coronavirus infectious disease (homeostatic balance). negative regulation of virus transport in coronavirus infectious disease (homeostatic balance) HOIP_0038006 HOIP:HOIP_0038007 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. viral proliferation [coronavirus infectious disease (imbalance)] HOIP_0038007 HOIP:HOIP_0038008 Negative regulation of virus transport is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of virus transport. This process can constitute the course of COVID-19 (homeostatic balance). negative regulation of virus transport in COVID-19 (homeostatic balance) HOIP_0038008 HOIP:HOIP_0038009 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. This process can constitute the course of coronavirus infectious disease (homeostatic balance). viral proliferation in coronavirus infectious disease (homeostatic balance) HOIP_0038009 HOIP:HOIP_0038010 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. This process can constitute the course of COVID-19 (homeostatic balance). viral proliferation in COVID-19 (homeostatic balance) HOIP_0038010 HOIP:HOIP_0038011 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This process can constitute the course of coronavirus infectious disease (homeostatic balance). viral entry into host cell in coronavirus infectious disease (homeostatic balance) HOIP_0038011 HOIP:HOIP_0038012 Viral entry-innate immune response balance is a subtype of maiintaining balance: A process that keeps a balance between the viral entry and the innate immune response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). viral entry-innate immune response balance in coronavirus infectious disease (homeostatic balance) HOIP_0038012 HOIP:HOIP_0038013 Viral entry-innate immune response balance is a subtype of maiintaining balance: A process that keeps a balance between the viral entry and the innate immune response as biological defence response. viral entry-innate immune response balance HOIP_0038013 HOIP:HOIP_0038014 Changing viral entry-innate immune response balance is a subtype of changing balance: A process that changes the state of viral entry-innate immune response balance within an host organ or an organism. changing viral entry-innate immune response balance HOIP_0038014 HOIP:HOIP_0038015 Viral entry-innate immune response balance is a subtype of maiintaining balance: A process that keeps a balance between the viral entry and the innate immune response as biological defence response. This process can constitute the course of COVID-19 (homeostatic balance). Viral entry-innate immune response balance in COVID-19 (homeostatic balance) HOIP_0038015 HOIP:HOIP_0038016 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This process can constitute the course of coronavirus infectious disease (homeostatic balance). antiviral innate immune response in coronavirus infectious disease (homeostatic balance) HOIP_0038016 HOIP:HOIP_0038017 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This process can constitute the course of COVID-19 (homeostatic balance). antiviral innate immune response in COVID-19 (homeostatic balance) HOIP_0038017 HOIP:HOIP_0038018 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This process can constitute the course of COVID-19 drug treatment. antiviral innate immune response in COVID-19 drug treatment HOIP_0038018 HOIP:HOIP_0038019 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32629875 PMID:33077917 inflammatory response (very low) in COVID-19 drug treatment HOIP_0038019 PMID:32629875 This is consistent with the observation that inflammatory signals induce the rapid release of ANG2 from endothelial cells, particularly in the presence of TNFα, and that ANG2 inhibitors can reduce vessel inflammation. PMID:33077917 A case report of a patient with COVID-19-associated ARDS and pneumonia showed that treatment with a C3 inhibitor was safe and associated with a favourable course, suggesting that C3 blockade may have broad anti-inflammatory potential owing to the upstream positioning of C3 in innate immune cascade signalling. HOIP:HOIP_0038022 The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is low. virion attachment to host cell (very low) in COVID-19 drug treatment HOIP_0038022 HOIP:HOIP_0038023 The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is low. entry receptor-mediated virion attachment to host cell (very low) in COVID-19 drug treatment HOIP_0038023 HOIP:HOIP_0038024 Changing symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. This process can constitute the course of coronavirus infectious disease. changing symbiotic balance between host and virus in coronavirus infection HOIP_0038024 HOIP:HOIP_0038025 A series of changing processes in an organism, from a balance to an imbalance between functional supply by the immune system and functional demand by coronaviruses. corona virus infectious course HOIP_0038025 HOIP:HOIP_0038026 Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. fusion of virus membrane with host endosome membrane (very low) in COVID-19 drug treatment HOIP_0038026 HOIP:HOIP_0038027 Any process that stops, prevents, or reduces the frequency, rate, or extent of endosomal membrane fusion involved in viral entry into host cell. This process can constitute the course of COVID-19 drug treatment. PMID:32505227 negative regulation of endosomal membrane fusion involved in viral entry into host cell in COVID-19 drug treatment HOIP_0038027 HOIP:HOIP_0038029 Any process that stops, prevents, or reduces the frequency, rate, or extent of membrane fusion involved in viral entry into host cell. negative regulation of endosomal membrane fusion involved in viral entry into host cell HOIP_0038029 HOIP:HOIP_0038030 Negative regulation of cleavage of viral spike protein is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of cleavage of viral spike protein. negative regulation of cleavage of viral spike protein HOIP_0038030 HOIP:HOIP_0038031 Negative regulation of cleavage of viral spike protein S2 is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of cleavage of viral spike protein S2. This process can constitute the course of COVID-19 drug treatment. negative regulation of cleavage of viral spike protein S2 in COVID-19 drug treatment HOIP_0038031 HOIP:HOIP_0038032 Hypofunction of cleavage of viral spike protein S2 is a subtype of hypofunctioning: A process that performs a decreased or insufficient cleavage of viral spike protein S2. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. cleavage of viral spike S2 protein (very low) in COVID-19 drug treatment HOIP_0038032 HOIP:HOIP_0038034 Interacting selectively and non-covalently with a receptor on the host cell surface. This process can constitute the course of COVID-19 drug treatment. host cell surface receptor binding(very low) in COVID-19 drug treatment HOIP_0038034 HOIP:HOIP_0038035 Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32221306 PMID:32361028 receptor-mediated endocytosis of virus by host cell (very low) in COVID-19 drug treatment HOIP_0038035 PMID:32221306 More than 98% reduction in transduction on 293/hACE2 cells by SARS-CoV-2 S pseudovirions was also shown when the cells were incubated with either NH4Cl or bafilomycin A (Fig. 3a), indicating that SARS-CoV-2 S pseudovirions enter 293/hACE2 cells mainly through endocytosis, despite that its spike proteins were cleaved. PMID:32361028 One of the top significant results shown to downregulate the expression of the CTSL gene is amantadine (10uM). Amantadine in addition to downregulating CTSL appears to further disrupt lysosomal pathway, hence, interfering with the capacity of the virus to replicate. HOIP:HOIP_0038036 Positive regulation of HIF1A gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of HIF1A gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of HIF1A gene expression (very high) in severe COVID-19 HOIP_0038036 PMID:32697943 When compared to healthy controls, BAL monocytes from severe COVID-19 patients had higher expression of HIF-1 target genes (Figure 3A). Blood monocytes from severe COVID-19 patients present high expression of HIF-1a in comparison to healthy donors (Figure 3C). We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). Altogether, these results highlight the metabolic alterations that take place in CoV-2-infected monocytes under high glucose conditions. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. HOIP:HOIP_0038037 This gene encodes a nuclear-localized E3 ubiquitin ligase. The encoded protein can promote tumor formation by targeting tumor suppressor proteins, such as p53, for proteasomal degradation. This gene is itself transcriptionally-regulated by p53. Overexpression or amplification of this locus is detected in a variety of different cancers. There is a pseudogene for this gene on chromosome 2. Alternative splicing results in a multitude of transcript variants, many of which may be expressed only in tumor cells. [provided by RefSeq, Jun 2013] NCBI-Human-GeneID:4193 NCBI-Mouse-GeneID:17246 NCBI-Rat-GeneID:314856 http://www.genecards.org/cgi-bin/carddisp.pl?gene=MDM2 MDM2(canonical)[glutathione depletion (course)] HOIP_0038037 NCBI-Human-GeneID:4193 http://www.ncbi.nlm.nih.gov/gene/4193 NCBI-Mouse-GeneID:17246 http://www.ncbi.nlm.nih.gov/gene/17246 NCBI-Rat-GeneID:314856 http://www.ncbi.nlm.nih.gov/gene/314856 HOIP:HOIP_0038038 Any biological process that results in permanent cessation of all vital functions of a cell in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32843733 PMID:33077917 cell death in lung (very high) in COVID-19 associated with ARDS HOIP_0038038 PMID:32843733 The damaged cells in the lungs elicit a strong innate immune response, which seems to be largely mediated by pro-inflammatory macrophages and granulocytes. PMID:33077917 A new study has also indicated that neutrophil activation and the formation of neutrophil extracellular traps (NETs) may have a prominent role in propagating the severe cytokine release observed in severe cases of COVID-19, representing a previously unrecognized, but powerful innate defence response that may exacerbate lung damage in affected patients. Infiltrating, activated neutrophils produce large amounts of histotoxic mediators, including reactive oxygen species, as well as NETs, which have been found in arterial microthrombi in the post-mortem lung specimens from four deceased patients with COVID-19. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0038041 A process by which viral mRNA is translated into viral protein, using the host cellular machinery. This process can constitute the course of severe COVID-19. viral protein anabolism in severe COVID-19 viral protein biosynthesis in severe COVID-19 viral protein biosynthetic process viral protein biosynthetic process viral protein biosynthetic process in severe COVID-19 viral protein formation in severe COVID-19 viral protein synthesis in severe COVID-19 viral translation in severe COVID-19 HOIP_0038041 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0038042 Thrombus formation in deep vein is a subtype of thrombus formation: A process that construcs thrombus in deep vein. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 thrombus formation in deep vein in COVID-19 associated with ARDS HOIP_0038042 PMID:32629875 Results of 12 consecutive complete autopsies of patients with COVID-19 concluded that massive pulmonary embolism was the cause of death in 4/12 cases and that VTE was present in 7/12 (58%) patients. An autopsy series showed the presence of deep venous thrombosis involving the lower extremities bilaterally in 56% (7/12) of cases, associated with massive pulmonary embolism in four of these cases, which was listed as the cause of death. Consistent with the presence of a coagulopathy, deep vein thrombosis appears more frequently than expected in hospitalized COVID-19 patients, even with anti-coagulant prophylaxis. A systematic search for pulmonary emboli in 26 COVID-19 patients on mechanical ventilation showed that they were detected in 23% (6/26) of patients, and venous thromboembolism (VTE) was detected in 69% (18/26). HOIP:HOIP_0038044 thrombus formation is a subtype of biological structure formation: A process that construcs thrombus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The thrombus formation level is very low. PMID:32412710 PMID:32629875 PMID:33077917 thrombus formation (very low) in COVID-19 drug treatment HOIP_0038044 PMID:32412710 The majority of patients with severe Covid-19 have lymphopenia, and some have thromboembolic complications as well as disorders of the central or peripheral nervous system. PMID:32629875 Also, among patients who died with COVID-19, 71% met the International Society on Thrombosis and Haemostasis criteria for disseminated intravascular coagulation (DIC), compared to only 0.6% of the survivors. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32629875 An autopsy series showed the presence of deep venous thrombosis involving the lower extremities bilaterally in 56% (7/12) of cases, associated with massive pulmonary embolism in four of these cases, which was listed as the cause of death. Post-mortem histopathologic analysis of lung tissue from 38 COVID-19 patients documented the presence of platelet-fibrin thrombi in lung arterioles of most (33/38) cases, congested capillaries (33/38) proximal to hemorrhagic alveoli often containing CD61+ megakaryocytes, and dense capillary foci presumably resulting from vessel intussusceptive sprouting (18/38). As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. Consistent with the presence of a coagulopathy, deep vein thrombosis appears more frequently than expected in hospitalized COVID-19 patients, even with anti-coagulant prophylaxis. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. The presence of thrombi involving the portal venules was observed in 15/22 autopsies, occasionally associated with thrombi in some hepatic arteries and arterioles. Thus, IL-6 can promote a pro-coagulant and pro-thrombotic vascular pathology, raising the possibility that an abnormally high level of IL-6 may contribute to the vascular phenotype in severe COVID-19. PMID:33077917 Although clinical insights into complement activation following SARS-CoV-2 infection are limited, the above findings indicate that unrestrained complement activation - mainly at the downstream terminal phases of the complement cascades - may contribute to endothelial cell injury, thrombosis and intravascular coagulation, ultimately leading to multi-systemic organ failure in patients with COVID-19. HOIP:HOIP_0038045 Inreasing urine protein concentration is a subtype of increasing concentration: A process that changes the protein concentration in the urine to be higher. inreasing urine protein concentration HOIP_0038045 HOIP:HOIP_0038046 Protrusion that develops in the cytoplasm of an oocyte. protrusion of oocyte cytoplasm HOIP_0038046 HOIP:HOIP_0038051 G5EF09 NCBI-GeneID:175446 TRP homologous cation channel protein trp-3 TRP3 (mol) HOIP_0038051 G5EF09 https://www.uniprot.org/uniprot/G5EF09 NCBI-GeneID:175446 https://www.ncbi.nlm.nih.gov/gene/175446 HOIP:HOIP_0038052 Brain microvascular dysfunction is a subtype of organ malfunction: A process that does not perform microvascular function correctly or not functioning at all in the brain. brain microvascular dysfunction HOIP_0038052 HOIP:HOIP_0038055 Member of a set of two cells that generate exclusively sperm and ovum. C.elegans germline precursor cell HOIP_0038055 HOIP:HOIP_0038056 C.elegans fertilization dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the hermaphrodite fertilization course in C. elegans. C.elegans fertilization dependent chemical entity HOIP_0038056 HOIP:HOIP_0038057 C.elegans fertilization dependent chemical compound dependent chemical compound is a subtype of course dependent chemical entity. This entity (drug) can participate in the hermaphrodite fertilization course in C. elegans. C.elegans fertilization dependent chemical compound HOIP_0038057 HOIP:HOIP_0038058 calcium(2+) HOIP_0038058 HOIP:HOIP_0038059 C.elegans fertilization dependent molecule (canonical) is a subtype of course dependent chemical entity. This entity can participate in participate in the hermaphrodite fertilization course in C. elegans as a gene product. Gene profile:caonical that described in textbooks or articles. C.elegans fertilization dependent molecule (canonical) HOIP_0038059 HOIP:HOIP_0038060 The directed movement of calcium ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans calcium ion transport [hermaphrodite fertilization course in C. elegans'] HOIP_0038060 HOIP:HOIP_0038061 The directed movement of calcium ion from endoplasmic reticulum to cytosol. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C. elegans release of sequestered calcium ion into cytosol by endoplasmic reticulum [hermaphrodite fertilization course in C. elegans'] HOIP_0038061 HOIP:HOIP_0038062 C.elegans fertilization dependent molecule (C.elegans) is a subtype of course dependent chemical entity. This entity can participate in participate in the hermaphrodite fertilization course in C. elegans as a gene product. Gene profile:C.elegans C.elegans fertilization dependent molecule (C.elegans) HOIP_0038062 HOIP:HOIP_0038064 hermaphrodite fertilization dependent process in C. elegans is a subtype of course dependent process: A process that can constitute the course of hermaphrodite fertilization in C.elegans. hermaphrodite fertilization process in C. elegans HOIP_0038064 HOIP:HOIP_0038065 Moving calcium channel to the inside of other cell is a subtype of moving A to the inside of B: A process that of the movement of calcium channel into the other cell. moving calcium channel to other cell HOIP_0038065 HOIP:HOIP_0038066 The totality of all processes through which hermaphrodite fertilization in C.elegans is realized. hermaphrodite fertilization course in C. elegans HOIP_0038066 HOIP:HOIP_0038067 inositol phosphate signaling is a subtype of biological signaling: Any processes of intracellular signals transduced by the inositol phosphate. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans inositol phosphate-mediated signaling [hermaphrodite fertilization course in C. elegans'] HOIP_0038067 HOIP:HOIP_0038068 Any intracellular signal transduction in which the signal is passed on within the cell via an inositol phosphate. Includes production of the inositol phosphate, and downstream effectors that further transmit the signal within the cell. Inositol phosphates are a group of mono- to poly-phosphorylated inositols, and include inositol monophosphate (IP), inositol trisphosphate (IP3), inositol pentakisphosphate (IP5) and inositol hexaphosphate (IP6). C.elegans inositol phosphate-mediated signaling pathway HOIP_0038068 HOIP:HOIP_0038069 C.elegans moving calcium channel from sperm into oocyte is a subtype of moving A to the inside of B: A process that of the movement of calcium channel from sperm into the oocyte. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. PMID:27069469 Figure.7 (F) Transfer of TRP-3::TagRFP-T signals from the sperm to the oocyte upon fusion. PMID:27069469 Figure.7 (F) Transfer of TRP-3::TagRFP-T signals from the sperm to the oocyte upon fusion. PMID:27069469 Movie S6. Transfer of TRP-3::TagRFP-T from the Sperm to the Oocyte during Fertilization, Related to Figure 7 PMID:27069469 Movie S6. Transfer of TRP-3::TagRFP-T from the Sperm to the Oocyte during Fertilization, Related to Figure 7 PMID:27068469 C.elegans moving calcium channel from sperm into oocyte [hermaphrodite fertilization course in C. elegans'] HOIP_0038069 PMID:27069469 Figure.7 (F) Transfer of TRP-3::TagRFP-T signals from the sperm to the oocyte upon fusion. PMID:27069469 Movie S6. Transfer of TRP-3::TagRFP-T from the Sperm to the Oocyte during Fertilization, Related to Figure 7 https://ars.els-cdn.com/content/image/1-s2.0-S2211124716302960-mmc8.mp4 HOIP:HOIP_0038071 Oocytes develop in close association with proximal gonadal sheath cells, smooth muscle-like cells that regulate meiotic maturation and contract to drive ovulation (McCarter et al., 1997; Hall et al., 1999; Miller et al., 2003). Meiotic maturation takes place in an assembly line fashion, such that the most proximal oocyte (often referred to as the –1 oocyte) matures, enters the spermatheca at ovulation, and is fertilized. In adult hermaphrodites, the cycle repeats every ~23 minutes (McCarter et al., 1999). This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. Oocytes develop in close association with proximal gonadal sheath cells, smooth muscle-like cells that regulate meiotic maturation and contract to drive ovulation (McCarter et al., 1997; Hall et al., 1999; Miller et al., 2003). Meiotic maturation takes place in an assembly line fashion, such that the most proximal oocyte (often referred to as the –1 oocyte) matures, enters the spermatheca at ovulation, and is fertilized. In adult hermaphrodites, the cycle repeats every ~23 minutes (McCarter et al., 1999). This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans fertilization [hermaphrodite fertilization course in C. elegans'] HOIP_0038071 Oocytes develop in close association with proximal gonadal sheath cells, smooth muscle-like cells that regulate meiotic maturation and contract to drive ovulation (McCarter et al., 1997; Hall et al., 1999; Miller et al., 2003). Meiotic maturation takes place in an assembly line fashion, such that the most proximal oocyte (often referred to as the –1 oocyte) matures, enters the spermatheca at ovulation, and is fertilized. In adult hermaphrodites, the cycle repeats every ~23 minutes (McCarter et al., 1999). This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. http://www.wormbook.org/chapters/www_controloocytematuration/controloocytematuration.html HOIP:HOIP_0038072 Actication of the transmembrane transfer of a calcium ion by a channel that opens when inositol 1,4,5-trisphosphate (IP3) has been bound by the channel complex or one of its constituent parts. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans inositol 1,4,5-trisphosphate-sensitive calcium-release channel activation [hermaphrodite fertilization course in C. elegans'] HOIP_0038072 HOIP:HOIP_0038073 The process in which the egg becomes metabolically active, initiates protein and DNA synthesis and undergoes structural changes. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans egg activation [hermaphrodite fertilization course in C. elegans'] HOIP_0038073 HOIP:HOIP_0038074 The binding and fusion of a sperm, with the plasma membrane of the oocyte as part of the process of double fertilization. fusion of sperm to egg plasma membrane HOIP_0038074 HOIP:HOIP_0038075 The binding and fusion of a sperm, with the plasma membrane of the oocyte as part of the process of fertilization. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans fusion of sperm to egg plasma membrane [hermaphrodite fertilization course in C. elegans'] HOIP_0038075 HOIP:HOIP_0038076 The membrane surrounding an oocyte. oocyte plasma membrane HOIP_0038076 HOIP:HOIP_0038077 The membrane surrounding an oocyte. C.elegans oocyte plasma membrane HOIP_0038077 HOIP:HOIP_0038078 The process that occurs after sperm attachment, fusion of the plasma membrane and enters into an oocyte. sperm entry into oocyte HOIP_0038078 HOIP:HOIP_0038079 The process that occurs after sperm attachment, fusion of the plasma membrane and enters into an oocyte. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans sperm entry into oocyte [hermaphrodite fertilization course in C. elegans'] HOIP_0038079 HOIP:HOIP_0038080 Increase in calcium level in sperm entry region of oocyte is a subtype of increase in calcium level: A process that changes the calcium ion concentration in an oocyte to be higher. This entity is a specific course-dependent process. This process can constitute the course of hermaphrodite fertilization course in C. elegans. C.elegans increase in calcium level in sperm entry region of oocyte [hermaphrodite fertilization course in C. elegans'] HOIP_0038080 HOIP:HOIP_0038081 The release of a mature oocyte. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans ovulation into spermatheca [hermaphrodite fertilization course in C. elegans'] HOIP_0038081 HOIP:HOIP_0038082 A tube or collection of tubes in an animal from the ovaries to the outside of the body. In all remaining vertebrates (i.e., coelacanths, lungfishes, amphibians, reptiles, birds, and mammals), the oviduct arises in ontogeny as a longitudinal, groovelike invagination of the coelomic epithelium on the lateral surface of the mesonephros C.elegans oviduct HOIP_0038082 HOIP:HOIP_0038083 The totality of all processes through which homeostatic imbalance of hermaphrodite fertilization in C.elegans is realized. hermaphrodite fertilization imbalance course in C. elegans HOIP_0038083 HOIP:HOIP_0038084 G5EF09 NCBI-GeneID:175446 WormBase:WBGene00004963 TRP homologous cation channel protein trp-3 SPE-41 [ Caenorhabditis elegans ] HOIP_0038084 G5EF09 https://www.uniprot.org/uniprot/G5EF09 NCBI-GeneID:175446 https://www.ncbi.nlm.nih.gov/gene/175446 HOIP:HOIP_0038085 The region of the sperm entry of an oocyte. sparm entry region HOIP_0038085 HOIP:HOIP_0038086 Increase in calcium level in wide region of oocyte is a subtype of increase in calcium level: A process that changes the calcium ion concentration in an oocyte to be higher. This entity is a specific course-dependent process. This process can constitute the course of hermaphrodite fertilization course in C. elegans. C.elegans increase in calcium level in wide region of oocyte [hermaphrodite fertilization course in C. elegans'] HOIP_0038086 HOIP:HOIP_0038087 Interacting selectively and non-covalently with inositol 1,4,5 trisphosphate. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans inositol 1,4,5 trisphosphate binding [hermaphrodite fertilization course in C. elegans'] HOIP_0038087 HOIP:HOIP_0038089 A CRID registry is a dataset of CRID records, each consisting of a CRID symbol and additional information which was recorded in the dataset through a assigning a centrally registered identifier process. centrally registered identifier registry HOIP_0038089 HOIP:HOIP_0038090 Protrusion that develops in the cytoplasm of an oocyte. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. PMID: 27068469 C.elegans protrusion of oocyte cytoplasm [hermaphrodite fertilization course in C. elegans'] HOIP_0038090 PMID: 27068469 PMID: 27068469 We observed that the tip of the oocyte suddenly protruded just after the oocyte entered the spermatheca (Figure 1C). HOIP:HOIP_0038092 Calcium transport gene mutation is a subtype of gene mutation: A process thatchanges the sequence of a cacium transport (calcium channel) gene. calcium transport gene mutation HOIP_0038092 HOIP:HOIP_0038093 NCBI-GeneID:173042 PMID:15282160 PMID:9546393 Uniprot:Q9TVY6 SPE-9 [ Caenorhabditis elegans ] HOIP_0038093 NCBI-GeneID:173042 https://www.ncbi.nlm.nih.gov/gene/173042 PMID:9546393 A common feature of proteins that include epidermal growth factor-like motifs is their involvement in extracellular functions such as adhesive and ligand-receptor interactions. Additionally, the overall structure of the predicted SPE-9 protein is similar to that of ligands for the Notch/LIN-12/GLP-1 family of transmembrane receptors. These results suggest that SPE-9 functions in the specialized cell-cell interactions required for fertilization. Uniprot:Q9TVY6 https://www.uniprot.org/uniprot/Q9TVY6 HOIP:HOIP_0038094 NCBI-GeneID:175446 PMID:15282160 PMID:9546393 Uniprot:Q9TVY6 SPE-9 (mol) HOIP_0038094 NCBI-GeneID:175446 https://www.ncbi.nlm.nih.gov/gene/173042 PMID:9546393 A common feature of proteins that include epidermal growth factor-like motifs is their involvement in extracellular functions such as adhesive and ligand-receptor interactions. Additionally, the overall structure of the predicted SPE-9 protein is similar to that of ligands for the Notch/LIN-12/GLP-1 family of transmembrane receptors. These results suggest that SPE-9 functions in the specialized cell-cell interactions required for fertilization. Uniprot:Q9TVY6 https://www.uniprot.org/uniprot/Q9TVY6 HOIP:HOIP_0038095 NCBI-GeneID:173042 PMID:15282160 PMID:9546393 Uniprot:Q9TVY6 Fertilization defective 9 Spermatogenesis defective 9 Sperm transmembrane protein 9 (Caenorhabditis elegans) HOIP_0038095 NCBI-GeneID:173042 https://www.ncbi.nlm.nih.gov/gene/173042 PMID:9546393 A common feature of proteins that include epidermal growth factor-like motifs is their involvement in extracellular functions such as adhesive and ligand-receptor interactions. Additionally, the overall structure of the predicted SPE-9 protein is similar to that of ligands for the Notch/LIN-12/GLP-1 family of transmembrane receptors. These results suggest that SPE-9 functions in the specialized cell-cell interactions required for fertilization. Uniprot:Q9TVY6 https://www.uniprot.org/uniprot/Q9TVY6 HOIP:HOIP_0038097 Uniprot: G5EF09 TRP homologous cation channel protein (Caenorhabditis elegans) TRP-3 channel protein TRP_2 domain-containing protein TRP homologous cation channel protein (Caenorhabditis elegans) HOIP_0038097 Uniprot: G5EF09 https://www.uniprot.org/uniprot/G5EF09 HOIP:HOIP_0038099 NCBI-GeneID:172179 Spermatocyte protein spe-11 (Caenorhabditis elegans) HOIP_0038099 NCBI-GeneID:172179 https://www.ncbi.nlm.nih.gov/gene/172179 HOIP:HOIP_0038100 NCBI-GeneID:172179 PMID:20971008 SPE-11 (mol) HOIP_0038100 NCBI-GeneID:172179 https://www.ncbi.nlm.nih.gov/gene/172179 HOIP:HOIP_0038101 membrane transport gene mutation is a subtype of gene mutation: A process that changes in membrane transport gene. membrane transport gene mutation HOIP_0038101 HOIP:HOIP_0038102 Membrane transport gene mutation is a subtype of gene mutation: A process that changes in transport gene. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans membrane transport gene mutation [hermaphrodite fertilization course in C. elegans'] HOIP_0038102 HOIP:HOIP_0038103 The process that occurs after sperm attachment, fusion of the plasma membrane and enters into an oocyte. The entry level is very low. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans sperm entry into oocyte (very low) [hermaphrodite fertilization course in C. elegans'] HOIP_0038103 HOIP:HOIP_0038105 Actication of the transmembrane transfer of a calcium ion by a channel that opens when inositol 1,4,5-trisphosphate (IP3) has been bound by the channel complex or one of its constituent parts. inositol 1,4,5-trisphosphate-sensitive calcium-release channel activation HOIP_0038105 HOIP:HOIP_0038106 Enables the facilitated diffusion of a calcium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism. http://purl.obolibrary.org/obo/GO_0005262 calcium channel activation HOIP_0038106 HOIP:HOIP_0039008 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. This process can constitute the course of coronavirus infectious disease. decreasing number of virus in coronavirus infection HOIP_0039008 HOIP:HOIP_0039011 Symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. This process can constitute the course of coronavirus infectious disease (homeostatic balance). symbiotic balance between host and virus in coronavirus infectious disease (homeostatic balance) HOIP_0039011 HOIP:HOIP_0039013 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. decreasing number of virus [coronavirus infectious disease(imbalance)] HOIP_0039013 HOIP:HOIP_0039014 Changing symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. This process can constitute the course of coronavirus infectious disease. symbiotic imbalance between host and virus [coronavirus infectious disease(imbalance)] HOIP_0039014 HOIP:HOIP_0039020 Any processes of signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of coronavirus infectious disease. PMID:32505227 cytoplasmic pattern recognition receptor signaling in response to virus in coronavirus infection HOIP_0039020 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of patternrecognition receptors (PRRs) by viral single-stranded RNA (ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). HOIP:HOIP_0039021 Any processes of signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of COVID-19. PMID:32505227 Wikipedia:Inflammation cytoplasmic cytoplasmic pattern recognition receptor signaling in response to virus in COVID-19 HOIP_0039021 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of patternrecognition receptors (PRRs) by viral single-stranded RNA (ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0039022 Dysregulation of metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of metabolism appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 dysregulation of metabolism (very high) in COVID-19 in liver HOIP_0039022 PMID:32651579 Hyperinflammation seen with cytokine storm and hypoxia-associated metabolic derangements are other potential mechanisms of liver damage. HOIP:HOIP_0039023 Virus recognition is a subtype of receiving: A process that recognizes viruses. virus recognition HOIP_0039023 HOIP:HOIP_0039024 Virus recognition is a subtype of receiving: A process that recognizes viruses. This entity is a specific course-dependent process. This process can constitute the course of coronaviurs infectious disease. virus recognition in coronavirus infection HOIP_0039024 HOIP:HOIP_0039027 Any processes of signals generated as a consequence of a cell surface pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species. cell surface pattern recognition receptor signaling HOIP_0039027 HOIP:HOIP_0039028 Any processes of molecular signals generated as a consequence of a pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species, or damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. pattern recognition receptor signaling in response to virus HOIP_0039028 HOIP:HOIP_0039029 TLR signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor. This process can constitute the course of coronavirus infectious disease. TLR signaling in coronavirus infection HOIP_0039029 HOIP:HOIP_0039030 TLR8 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 8 TLR8 signaling HOIP_0039030 HOIP:HOIP_0039031 Any processes of molecular signals generated as a consequence of a pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species, or damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. This process can constitute the course of coronavirus infectious disease. pattern recognition receptor signaling in response to virus in coronavirus infection HOIP_0039031 HOIP:HOIP_0039032 TLR8 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 8. This process can constitute the course of coronavirus infectious disease. TLR8 signaling in coronavirus infection HOIP_0039032 HOIP:HOIP_0039033 TLR8 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 8. This process can constitute the course of COVID-19. TLR8 signaling in COVID-19 HOIP_0039033 HOIP:HOIP_0039034 The destruction of infected cellin the early infectious stage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. innate immunity mediated infected cell damage [coronavirus infectious disease] early infected cell destruction in coronavirus infection HOIP_0039034 HOIP:HOIP_0039035 The destruction of infected cells in the early infectious stage. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. early infected cell destruction in COVID-19 HOIP_0039035 HOIP:HOIP_0039036 For ontology reasoning. possible cause of IL-6 signaling process HOIP_0039036 HOIP:HOIP_0039037 A process that cannot perform tissues function appropriately or cannot realize it at all. tissue dysfunction HOIP_0039037 HOIP:HOIP_0039038 Infected cell damage is a subtype of damaging: A process that injuries the structure of the infected cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. infected cell damagein coronavirus infection HOIP_0039038 HOIP:HOIP_0039039 Early removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue in the early infetious stage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. early removing infected cell in coronavirus infection HOIP_0039039 HOIP:HOIP_0039040 Early removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue in the early infetious stage. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. early removing infected cell in COVID-19 HOIP_0039040 HOIP:HOIP_0039041 Early removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue in the early infetious stage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. early removing infected cell in severe COVID-19 HOIP_0039041 HOIP:HOIP_0039042 Increasing C-reactive protein concentration in blood is a subtype of increasing concentration: A process that changes the C-reactive protein concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32412710 PMID:32651579 increasing blood CRP concentration (very high) in severe COVID-19 HOIP_0039042 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. These organ failures may be associated with clinical and laboratory signs of inflammation, including high fevers, thrombocytopenia, hyperferritinemia, and elevations in C-reactive protein and interleukin-6. PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0039043 A vesicle-mediated transport process that results in the engulfment of external particulate material by inflammatory macrophages and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. phagocytosis by inflammatory macrophage (very high)in severe COVID-19 HOIP_0039043 HOIP:HOIP_0039044 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. production of molecular mediator of immune response in coronavirus infection HOIP_0039044 HOIP:HOIP_0039045 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. production of molecular mediator of immune response in COVID-19 HOIP_0039045 HOIP:HOIP_0039046 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. production of molecular mediator of innate immune response in coronavirus infection HOIP_0039046 HOIP:HOIP_0039047 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. production of molecular mediator of innate immune response in COVID-19 HOIP_0039047 HOIP:HOIP_0039048 Removing infected cell in adaptive immunity is a subtype of removing infected cell: A process that takes a infected cell from an organism or tissue in the adaptive immune responses. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. removing infected cell in adaptive immunityin coronavirus infection HOIP_0039048 HOIP:HOIP_0039049 Removing infected cell in adaptive immunity is a subtype of removing infected cell: A process that takes a infected cell from an organism or tissue in the adaptive immune responses. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. removing infected cell in adaptive immunity in COVID-19 HOIP_0039049 HOIP:HOIP_0039050 Negative regulation of viral gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of viral gene expression. negative regulation of viral gene expression HOIP_0039050 HOIP:HOIP_0039051 Negative regulation of viral gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of viral gene expression. This process can constitute the course of coronavirus infectious disease. ISBN:0815341504 negative regulation of viral gene expression in coronavirus infection HOIP_0039051 ISBN:0815341504 Viruses: Biology, Applications, and Control Chapter 4, Innate immnune response and evasion, Table4-3 HOIP:HOIP_0039052 Negative regulation of viral gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of viral gene expression. This process can constitute the course of COVID-19. negative regulation of viral gene expression in COVID-19 HOIP_0039052 HOIP:HOIP_0039054 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 increasing oxidative stress (very high)in severe COVID-19 HOIP_0039054 PMID:32629875 Also, genetic and pharmacological studies in mice have shown that ACE2 regulates cardiac structure and function; decreased ACE2 in SARS-CoV-2-infected cardiomyocytes could disrupt these activities, particularly impairing cardiac remodeling and increasing oxidative stress in cardiomyocytes. PMID:32697943 We observed that oxidative stress-associated genes are enriched in BAL of severe COVID-19 patients (Figure 3A). (A) Single-cell RNA-seq data showing enrichment of HIF-1, glycolysis, and oxidative stress pathways in SARS-CoV-2 (CoV-2)-infected human monocytes. HOIP:HOIP_0039055 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. positive regulation of RNA catabolic process HOIP_0039055 HOIP:HOIP_0039056 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. This process can constitute the course of coronavirus infectious disease. positive regulation of viral RNA catabolic process in coronavirus infection HOIP_0039056 HOIP:HOIP_0039057 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. This process can constitute the course of COVID-19. positive regulation of viral RNA catabolic process in COVID-19 HOIP_0039057 HOIP:HOIP_0039058 Any process that stops, prevents, or reduces the frequency, rate or extent of viral translation. down regulation of viral translation down-regulation of viral translation negative regulation of viral translation HOIP_0039058 HOIP:HOIP_0039059 Any process that stops, prevents, or reduces the frequency, rate or extent of viral translation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Protein kinase-R is activated by double-stranded RNA (dsRNA) in cells by a viral infection. PKR is induced by interferon and phosphorylates the eukaryotic translation initiation factor eIF2α, which prevents viral translation and protein synthesis. negative regulation of viral translation in coronavirus infection HOIP_0039059 HOIP:HOIP_0039060 Any process that stops, prevents, or reduces the frequency, rate or extent of viral translation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. negative regulation of viral translation in COVID-19 HOIP_0039060 HOIP:HOIP_0039063 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 PMID:33188364 glycolysis glycolytic process (sustained) in COVID-19 in patient with diabetes HOIP_0039063 PMID:32697943 Elevated Glucose Levels Favor SARS-CoV-2 Infection and Monocyte Response through a HIF-1a/ Glycolysis-Dependent Axis. Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Monocytes and macrophages are the most enriched immune cell types in the lungs of COVID-19 patients and appear to have a central role in the pathogenicity of the disease.These cells adapt their metabolism upon infection and become highly glycolytic, which facilitates SARS-CoV-2 replication. The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes Glycolysis Is Necessary for SARS-CoV-2 Replication and Monocyte Response Taken together, our results indicate that CoV-2 replication in monocytes and CoV-2-induced monocyte response are sustained by a switch to aerobic glycolysis (the Warburg effect). We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). PMID:33188364 In human monocytes, elevated glucose levels directly increase SARS-CoV-2 replication, and glycolysis sustains SARS-CoV-2 replication via the production of mitochondrial reactive oxygen species and activation of hypoxia-inducible factor 1α. HOIP:HOIP_0039064 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication. This process can constitute the course of coronavirus infectious disease. negative regulation of viral genome replication in coronavirus infection HOIP_0039064 HOIP:HOIP_0039065 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. negative regulation of viral genome replication in COVID-19 HOIP_0039065 HOIP:HOIP_0039066 A protein that is a translation product of the human GSDMD gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:79792 NCBI-Mouse-GeneID:69146 NCBI-Rat-GeneID:315084 GSDMD gasdermin domain-containing protein 1 gasdermin-D HOIP_0039066 NCBI-Human-GeneID:79792 https://www.ncbi.nlm.nih.gov/gene/79792 NCBI-Mouse-GeneID:69146 https://www.ncbi.nlm.nih.gov/gene/69146 NCBI-Rat-GeneID:315084 https://www.ncbi.nlm.nih.gov/gene/315084 HOIP:HOIP_0039067 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell. This process can constitute the course of coronavirus infectious disease. negative regulation of viral entry into host cell in coronavirus infection HOIP_0039067 HOIP:HOIP_0039068 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell. This process can constitute the course of COVID-19. negative regulation of viral entry into host cell in COVID-19 HOIP_0039068 HOIP:HOIP_0039069 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of virion attachment to host cell. This process can constitute the course of coronavirus infectious disease. negative regulation of virion attachment to host cell in coronavirus infection HOIP_0039069 HOIP:HOIP_0039070 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of virion attachment to host cell negative regulation of virion attachment to host cell HOIP_0039070 HOIP:HOIP_0039071 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of virion attachment to host cell. This process can constitute the course of COVID-19. negative regulation of virion attachment to host cell in COVID-19 HOIP_0039071 HOIP:HOIP_0039073 Negative regulation of inflammatory response is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is very low. negative regulation of inflammatory response (very low) in severe COVID-19 HOIP_0039073 HOIP:HOIP_0039074 Any apoptotic process in a neutrophil, any of the immature or mature forms of a granular leukocyte that in its mature form has a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is very low. Wikipedia:Inflammation neutrophil apoptotic process (low) in severe COVID-19 HOIP_0039074 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0039075 Cellular damage is a subtype of damaging: A process that injuries the structure of the cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Cell damage (also known as cell injury) is a variety or changes of stress that a cell suffers due to external as well internal environmental changes. Among other causes, this can be due to physical, chemical, infectious, biological, nutritional or immunological factors. Cell damage can be reversible or irreversible. Depending on the extent of injury, the cellular response may be adaptive and where possible, homeostasis is restored. Cell death occurs when the severity of the injury exceeds the cell’s ability to repair itself. Cell death is relative to both the length of exposure to a harmful stimulus and the severity of the damage caused. Cell death may occur by necrosis or apoptosis. cell and tissue damage cell and tissue damage PMID:35615359 http://purl.jp/bio/4/id/200906069918862451 https://en.wikipedia.org/wiki/Cell_damage cellular damage (very high) in severe COVID-19 HOIP_0039075 cell and tissue damage http://purl.obolibrary.org/obo/MPATH_1 PMID:35615359 NETosis is likely initiated by both direct (through angiotensin-converting enzyme 2, serine protease, virus replication, and PAD-4 (157)) and indirect (through activated platelets and COVID-19-triggered cytokines and chemokines which stimulate NETosis (158)) mechanisms. This results in enhanced coagulation with decreases in lymphocyte counts, an abundance of inflammatory myeloid cells, endothelial cell damage, thrombus formation, and ensuing fibrosis, all of which is associated with a poor COVID-19 prognosis (97, 134, 141, 159). HOIP:HOIP_0039076 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:32629875 PMID:32697943 PMID:33123165 IL-1beta production in coronavirus infection HOIP_0039076 PMID:32629875 These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. PMID:32697943 Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). We observed that neutralization of IL-1b with anti-IL-1b (CM-aIL-1b) from UV-inactivated CM of CoV-2-infected monocytes restored T cell proliferation (Figures 4A and S4I). PMID:33123165 The resultant inflammatory response provides immediate antiviral immunity via activation of antiviral type 1 and 3 interferon (IFN) pathways leading to an upregulation of inflammatory cytokines such as interleukin 6 (IL-6) and IL-1β, further recruiting neutrophils, other innate immune cells and stimulating anti-SARS-CoV-2 adaptive memory T cells and B cells (Figure 2). HOIP:HOIP_0039077 The movement of a leukocyte in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. immune cell chemotaxis leucocyte chemotaxis inflammatory cell chemotaxis in coronavirus infection HOIP_0039077 HOIP:HOIP_0039078 A phase of elevated metabolic activity, during which oxygen consumption increases following a stimulus as part of an inflammatory response; this leads to the production, by an NADH dependent system, of hydrogen peroxide (H2O2), superoxide anions and hydroxyl radicals, resulting in an increase in their intracellular or extracellular levels. This process can constitute the course of coronavirus infectious disease. respiratory burst involved in inflammatory responsein coronavirus infection HOIP_0039078 HOIP:HOIP_0039079 A phase of elevated metabolic activity, during which oxygen consumption increases following a stimulus as part of an inflammatory response; this leads to the production, by an NADH dependent system, of hydrogen peroxide (H2O2), superoxide anions and hydroxyl radicals, resulting in an increase in their intracellular or extracellular levels. This process can constitute the course of COVID-19. respiratory burst involved in inflammatory response in COVID-19 HOIP_0039079 HOIP:HOIP_0039080 T cell exhaustion is a dysfunction of T cells, which changes in transcriptional profiles and sustained expression of inhibitory receptors and leads to progressive loss of function. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 PMID:33123165 T cell exhaustion (very high) in severe COVID-19 HOIP_0039080 PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. PMID:33123165 Severe COVID-19 patients exhibit immunological features associated with T cell anergy or exhaustion. For example, the lungs of severe COVID-19 patients contain high levels of CD8+ T cells expressing classic markers and genes of exhaustion, while patients who have recovered from moderate or severe COVID-19 seem to have robust memory T cell formation. HOIP:HOIP_0039081 Cell damage recognition is a subtype of receiving: A process that recognizes the damages of cells. cell damage recognition HOIP_0039081 HOIP:HOIP_0039082 CXCL10 signaling is a process that a signal is transmitted by CXCL10. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:34046036 CXCL10 signaling in moderate COVID-19 HOIP_0039082 PMID:34046036 CXCL10/IP10 is also secreted by many cells, including monocytes, endothelial cells, and fibroblasts, in response to IFN-gamma. Several clinical investigations involving autopsies have also provided evidence that thrombosis is an important consequence of hCoV diseases. These findings indicate that the thrombosis-related indicators (CXCL10/IP10, MCP-1) could be directly involved in different stages of hCoV infection and could be used as potential biomarkers to predict the risk of death in hCoV patients. HOIP:HOIP_0039083 Cell damage recognition is a subtype of receiving: A process that recognizes the damages of cells. This process can constitute the course of COVID-19. cell damage recognition in COVID-19 HOIP_0039083 HOIP:HOIP_0039084 Any process that activates or increases the frequency, rate or extent of thrombus formation. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32629875 PMID:32651579 PMID:33077917 positive regulation of thrombus formation in moderate COVID-19 HOIP_0039084 PMID:32629875 Second, to infect cells, SARS-CoV-2 binds to the cell surface ACE2 receptors, and in so doing compromises the vaso-protective functions of ACE2, an enzyme that attenuates the vasoconstrictive, pro-inflammatory, pro-apoptotic, pro-thrombotic and mitogenic effects of angiotensin II, as discussed in Section 4.2. PMID:32651579 Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. While patients with viral infections are at risk for MI in gen-eral, this risk may be exaggerated in patients with COVID-19, given reports of disproportionately increased hypercoagulability in affected people, which would lead to a possible increase in thrombotically mediated MI. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. HOIP:HOIP_0039088 The aggregation, arrangement and bonding together of a set of components by an organism to form a pore complex in a membrane of another organism. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. pore formation in membrane of other organismin coronavirus infection HOIP_0039088 HOIP:HOIP_0039089 TLR signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor. This process can constitute the course of COVID-19. TLR signaling in COVID-19 HOIP_0039089 HOIP:HOIP_0039090 The aggregation, arrangement and bonding together of a set of components by an organism to form a pore complex in a membrane of another organism. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. pore formation in membrane of other organismin COVID-19 HOIP_0039090 HOIP:HOIP_0039091 The aggregation, arrangement and bonding together of a set of components by an organism to form a pore complex in a membrane of another organism. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. pore formation in membrane of other organismin severe COVID-19 HOIP_0039091 HOIP:HOIP_0039092 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 apoptotic process (very high) in severe COVID-19 HOIP_0039092 PMID:32629875 In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). A comprehensive post-mortem analysis of multiple tissues (in 3 COVID-19 cases) described congestion and endotheliitis of small vessels with accumulation of mononuclear/lymphocytic cells around the capillary endothelium in the heart, small bowel, kidney, liver and lung; in one case, caspase 3-immunostaining revealed the presence of apoptotic bodies in endothelial cells lining the inner wall of inflamed blood vessels. PMID:32697943 CM-CoV-2 induced apoptosis of A549 cells (Figure 4D), which was prevented when CoV-2-infected monocytes were treated with a HIF-1a inhibitor (Figure 4D). This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. HOIP:HOIP_0039093 A process of molecular signals initiated by the cross-linking of an antigen receptor on a B or T cell. antigen receptor-mediated signaling HOIP_0039093 HOIP:HOIP_0039094 A series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell. B cell receptor signaling HOIP_0039094 HOIP:HOIP_0039095 A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell. T cell receptor signaling HOIP_0039095 HOIP:HOIP_0039096 A series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell. This process can constitute the course of coronavirus infectious disease. B cell receptor signaling in coronavirus infection HOIP_0039096 HOIP:HOIP_0039097 A process of molecular signals initiated by the cross-linking of an antigen receptor on a B or T cell. antigen receptor-mediated signaling in coronavirus infection HOIP_0039097 HOIP:HOIP_0039098 A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell. This process can constitute the course of coronavirus infectious disease. T cell receptor signaling in coronavirus infection HOIP_0039098 HOIP:HOIP_0039099 Any biological process that results in permanent cessation of all vital functions of an endothelial cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 endothelial cell necrosis in severe COVID-19 HOIP_0039099 PMID:32629875 In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. HOIP:HOIP_0039100 Virus recognition is a subtype of receiving: A process that recognizes viruses. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. virus recognition in COVID-19 HOIP_0039100 HOIP:HOIP_0039101 Endothelium malfunction is a subtype of organ malfunction: A process that does not perform endothelium function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Endothelium endothelium dysfunction in severe COVID-19 HOIP_0039101 Wikipedia:Endothelium The endothelium normally provides a surface on which blood does not clot, because it contains and expresses substances that prevent clotting, including heparan sulfate which acts as a cofactor for activating antithrombin, a protease that inactivates several factors in the coagulation cascade. HOIP:HOIP_0039102 Any processes of molecular signals generated as a consequence of a pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species, or damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. pattern recognition receptor signaling in response to virus in COVID-19 HOIP_0039102 HOIP:HOIP_0039103 Hypofunction of mitochondrial fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient fatty acid beta-oxidation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:34049969 hypofunction of mitochondrial fatty acid beta-oxidation in severe COVID-19 HOIP_0039103 PMID:34049969 We found that ex vivo T cells from acutely infected COVID-19 patients were highly activated and apoptotic and displayed more extensive mitochondrial metabolic dysfunction, especially cells in CD8+ T cell lineages, than those from convalescent COVID-19 patients or healthy controls, but slightly disturbed mitochondrial metabolic activity was observed in non-COVID-19 patients. Importantly, plasma IL-6 and C-reactive protein (CRP) levels positively correlated with mitochondrial mass and negatively correlated with fatty acid uptake in T cells from COVID-19 patients. HOIP:HOIP_0039104 A process of molecular signals initiated by the cross-linking of an antigen receptor on a B or T cell. This process can constitute the course of COVID-19. antigen receptor-mediated signaling in COVID-19 HOIP_0039104 HOIP:HOIP_0039105 A series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell. This process can constitute the course of COVID-19. B cell receptor signaling in COVID-19 HOIP_0039105 HOIP:HOIP_0039106 A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell. This process can constitute the course of COVID-19. T cell receptor signaling in COVID-19 HOIP_0039106 HOIP:HOIP_0039107 A vesicle-mediated transport process that results in the engulfment of external particulate material by neutrophils. Wikipedia:Phagocytosis phagocytosis by neutrophils HOIP_0039107 HOIP:HOIP_0039108 A vesicle-mediated transport process that results in the engulfment of external particulate material by monocytes. Wikipedia:Phagocytosis phagocytosis by monocytes HOIP_0039108 HOIP:HOIP_0039109 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. phagocytosis by macrophage HOIP_0039109 HOIP:HOIP_0039110 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. This process can constitute the course of coronavirus infectious disease. phagocytosis by macrophage in coronavirus infection HOIP_0039110 HOIP:HOIP_0039111 A vesicle-mediated transport process that results in the engulfment of external particulate material by monocytes. This process can constitute the course of coronavirus infectious disease. Wikipedia:Phagocytosis phagocytosis by monocyte in coronavirus infection HOIP_0039111 HOIP:HOIP_0039112 A vesicle-mediated transport process that results in the engulfment of external particulate material by neutrophils. This process can constitute the course of coronavirus infectious disease. phagocytosis by neutrophils in coronavirus infection HOIP_0039112 HOIP:HOIP_0039113 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. phagocytosis by dendritic cell HOIP_0039113 HOIP:HOIP_0039114 A vesicle-mediated transport process that results in the engulfment of external particulate material by dendritic cell. This process can constitute the course of coronavirus infectious disease. phagocytosis by dendritic cell in coronavirus infection HOIP_0039114 HOIP:HOIP_0039115 A vesicle-mediated transport process that results in the engulfment of external particulate material by dendritic cell. This process can constitute the course of COVID-19. phagocytosis by dendritic cell in COVID-19 HOIP_0039115 HOIP:HOIP_0039116 A vesicle-mediated transport process that results in the engulfment of external particulate material by monocytes. This process can constitute the course of COVID-19. Wikipedia:Phagocytosis phagocytosis by monocyte in COVID-19 HOIP_0039116 HOIP:HOIP_0039117 A vesicle-mediated transport process that results in the engulfment of external particulate material by neutrophils. This process can constitute the course of COVID-19. phagocytosis by neutrophils in COVID-19 HOIP_0039117 HOIP:HOIP_0039118 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. This process can constitute the course of COVID-19. phagocytosis by macrophagein COVID-19 HOIP_0039118 HOIP:HOIP_0039119 virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. decreasing virus sensitivity increasing anti-virus activity virus resistance HOIP_0039119 HOIP:HOIP_0039120 Increasing virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. decreasing virus sensitivity increasing virus resitance in COVID-19 HOIP_0039120 HOIP:HOIP_0039121 Increasing virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. decreasing virus sensitivity in coroavirus infection As protection against the virus, there are two ways: 1) antiviral action that suppresses the action of the virus itself (e.g., virus proliferation) 2) elimination of infected cells. TYPe-I IFN promotes not only antiviral action and also enables the latter by activation of NK cells. increasing virus resistance in coronavirus infection HOIP_0039121 HOIP:HOIP_0039122 Increasing virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. This process can constitute the course of coronavirus infectious disease (homeostatic balance). decreasing virus sensitivity in coronavirus infectious disease (homeostatic balance) increasing virus resistance in coronavirus infectious disease (homeostatic balance) HOIP_0039122 HOIP:HOIP_0039123 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of virion attachment to host cell. This process can constitute the course of coronavirus infectious disease (homeostatic balance). negative regulation of virion attachment to host cellin coronavirus infectious disease (homeostatic balance) HOIP_0039123 HOIP:HOIP_0039124 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of virion attachment to host cell. This process can constitute the course of COVID-19 (homeostatic balance). negative regulation of virion attachment to host cellin COVID-19 (homeostatic balance) HOIP_0039124 HOIP:HOIP_0039125 Increasing virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. This process can constitute the course of COVID-19 (homeostatic balance). decreasing virus sensitivity in COVID-19 (homeostatic balance) increasing virus resistance in COVID-19 (homeostatic balance) HOIP_0039125 HOIP:HOIP_0039126 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication. This process can constitute the course of coronavirus infectious disease (homeostatic balance). negative regulation of viral genome replication in coronavirus infectious disease (homeostatic balance) HOIP_0039126 HOIP:HOIP_0039127 Negative regulation of viral gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of viral gene expression. This process can constitute the course of coronavirus infectious disease (homeostatic balance). ISBN:0815341504 negative regulation of viral gene expression in coronavirus infectious disease (homeostatic balance) HOIP_0039127 ISBN:0815341504 Viruses: Biology, Applications, and Control Chapter 4, Innate immnune response and evasion, Table4-3 HOIP:HOIP_0039128 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. This process can constitute the course of coronavirus infectious disease (homeostatic balance). positive regulation of viral RNA catabolic process in coronavirus infectious disease (homeostatic balance) HOIP_0039128 HOIP:HOIP_0039129 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. This process can constitute the course of COVID-19 (homeostatic balance). positive regulation of viral RNA catabolic process in COVID-19 (homeostatic balance) HOIP_0039129 HOIP:HOIP_0039130 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication. This process can constitute the course of COVID-19 (homeostatic balance). negative regulation of viral gene expression in COVID-19 (homeostatic balance) HOIP_0039130 HOIP:HOIP_0039131 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell. This process can constitute the course of coronavirus infectious disease (homeostatic balance). negative regulation of viral entry into host cell in coronavirus infectious disease (homeostatic balance) HOIP_0039131 HOIP:HOIP_0039132 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell. This process can constitute the course of COVID-19 (homeostatic balance). negative regulation of viral entry into host cell in COVID-19 (homeostatic balance) HOIP_0039132 HOIP:HOIP_0039133 Any process that contributes to cytokine production by a natural killer cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. natural killer cell cytokine production in coronavirus infection HOIP_0039133 HOIP:HOIP_0039135 Neutrophil extracellular trap formation in lung is a subtype of biological structure formation: A process that construcs neutrophil extracellular trap in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 PMID:33214651 neutrophil extracellular trap formation in lung in COVID-19 associated with ARDS HOIP_0039135 PMID:33077917 A new study has also indicated that neutrophil activation and the formation of neutrophil extracellular traps (NETs) may have a prominent role in propagating the severe cytokine release observed in severe cases of COVID-19, representing a previously unrecognized, but powerful innate defence response that may exacerbate lung damage in affected patients. Infiltrating, activated neutrophils produce large amounts of histotoxic mediators, including reactive oxygen species, as well as NETs, which have been found in arterial microthrombi in the post-mortem lung specimens from four deceased patients with COVID-19. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. PMID:33214651 Neutrophil extracellular traps (NETs) have been shown to trigger thromboinflammation in patients with COVID-19, leading to vascular thrombosis and a high risk of death. HOIP:HOIP_0039137 Any process that activates or increases the frequency, rate or extent of blood coagulation in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 positive regulation of blood coagulation in lung (very high) in COVID-19 associated with ARDS HOIP_0039137 PMID:33077917 Mounting evidence suggests that loss of vessel barrier integrity and the development of a pro-coagulative endothelium contributes to the initiation and propagation of ARDS in COVID-19, by inducing endotheliitis and mediating inflammatory cell infiltration in the lungs. Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0039138 Any process that activates or increases the frequency, rate or extent of blood coagulation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 PMID:33188364 positive regulation of blood coagulation (very high) in COVID-19 in patient with diabetes HOIP_0039138 PMID:32687793 Obesity and diabetes are prothrombotic conditions that might contribute to worse prognosis in patients with COVID-19. Diabetes is associated with a prothrombotic state, with an imbalance between clotting factors and fibrinolysis and an increased risk of thromboembolic events. PMID:33188364 Patients with COVID-19 also exhibit elevation of other inflammatory markers, such as D-dimer, ferritin and IL-6, which might contribute to an increased risk of microvascular and macrovascular complications originating from low-grade vascular inflammation in patients with underlying diabetes mellitus. HOIP:HOIP_0039139 Any process that activates or increases the frequency, rate or extent of blood coagulation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32412710 positive regulation of blood coagulation (very high) in COVID-19 associated with ACS HOIP_0039139 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. HOIP:HOIP_0039140 Negative regulation of viral gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of viral gene expression. This process can constitute the course of COVID-19 (homeostatic balance). ISBN:0815341504 negative regulation of viral gene expression in COVID-19 (homeostatic balance) HOIP_0039140 ISBN:0815341504 Viruses: Biology, Applications, and Control Chapter 4, Innate immnune response and evasion, Table4-3 HOIP:HOIP_0039141 Removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue. This entity is a specific course-dependent process. This process This process can constitute the course of coronavirus infectious disease (homeostatic balance). removing infected cell in coronavirus infectious disease (homeostatic balance) HOIP_0039141 HOIP:HOIP_0039142 Early removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue in the early infetious stage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). early removing infected cell in coronavirus infectious disease (homeostatic balance) HOIP_0039142 HOIP:HOIP_0039143 Removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue. This process can constitute the course of COVID-19 (homeostatic balance). removing infected cell in COVID-19 (homeostatic balance) HOIP_0039143 HOIP:HOIP_0039144 thrombus formation is a subtype of biological structure formation: A process that construcs thrombus. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32412710 PMID:32629875 PMID:32651579 PMID:33077917 thrombus formation (high) in moderate COVID-19 HOIP_0039144 PMID:32412710 The majority of patients with severe Covid-19 have lymphopenia, and some have thromboembolic complications as well as disorders of the central or peripheral nervous system. PMID:32629875 An autopsy series showed the presence of deep venous thrombosis involving the lower extremities bilaterally in 56% (7/12) of cases, associated with massive pulmonary embolism in four of these cases, which was listed as the cause of death. Post-mortem histopathologic analysis of lung tissue from 38 COVID-19 patients documented the presence of platelet-fibrin thrombi in lung arterioles of most (33/38) cases, congested capillaries (33/38) proximal to hemorrhagic alveoli often containing CD61+ megakaryocytes, and dense capillary foci presumably resulting from vessel intussusceptive sprouting (18/38). As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. Consistent with the presence of a coagulopathy, deep vein thrombosis appears more frequently than expected in hospitalized COVID-19 patients, even with anti-coagulant prophylaxis. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. The presence of thrombi involving the portal venules was observed in 15/22 autopsies, occasionally associated with thrombi in some hepatic arteries and arterioles. Thus, IL-6 can promote a pro-coagulant and pro-thrombotic vascular pathology, raising the possibility that an abnormally high level of IL-6 may contribute to the vascular phenotype in severe COVID-19. Also, among patients who died with COVID-19, 71% met the International Society on Thrombosis and Haemostasis criteria for disseminated intravascular coagulation (DIC), compared to only 0.6% of the survivors. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32651579 There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. PMID:33077917 Although clinical insights into complement activation following SARS-CoV-2 infection are limited, the above findings indicate that unrestrained complement activation - mainly at the downstream terminal phases of the complement cascades - may contribute to endothelial cell injury, thrombosis and intravascular coagulation, ultimately leading to multi-systemic organ failure in patients with COVID-19. Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0039145 Early removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue in the early infetious stage. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). early removing infected cellin COVID-19 (homeostatic balance) HOIP_0039145 HOIP:HOIP_0039146 The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. This process can constitute the course of coronavirus infectious disease. antigen presentation in coronavirus infection HOIP_0039146 HOIP:HOIP_0039147 The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. This process can constitute the course of COVID-19. antigen presentationin COVID-19 HOIP_0039147 HOIP:HOIP_0039148 The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. This process can constitute the course of coronavirus infectious disease (homeostatic balance). antigen presentation in coronavirus infectious disease (homeostatic balance) HOIP_0039148 HOIP:HOIP_0039149 The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. This process can constitute the course of COVID-19 (homeostatic balance). antigen presentationin COVID-19 (homeostatic balance) HOIP_0039149 HOIP:HOIP_0039150 Any process that contributes to cytokine production by a natural killer cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. natural killer cell cytokine production in COVID-19 HOIP_0039150 HOIP:HOIP_0039151 Any process that contributes to cytokine production by a natural killer cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. natural killer cell cytokine production in severe COVID-19 HOIP_0039151 HOIP:HOIP_0039152 interferon-gamma production The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This process can constitute the course of coronavirus infectious disease. interferon-gamma production in coronavirus infection HOIP_0039152 HOIP:HOIP_0039153 An immune response which is associated with resistance to intracellular bacteria, fungi, and protozoa, and pathological conditions such as arthritis, and which is typically orchestrated by the production of particular cytokines by T-helper 1 cells, most notably interferon-gamma, IL-2, and lymphotoxin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. T-helper 1 type immune response in COVID-19 HOIP_0039153 HOIP:HOIP_0039154 The change in morphology and behavior of a T-helper 1 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 T-helper 1 cell activation in COVID-19 HOIP_0039154 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0039155 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 1 (Th1) cell. A Th1 cell is a CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive and produces interferon-gamma. This process can constitute the course of coronavirus infectious disease. T-helper 1 cell differentiation in coronavirus infection HOIP_0039155 HOIP:HOIP_0039156 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 1 (Th1) cell. A Th1 cell is a CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive and produces interferon-gamma. This process can constitute the course of COVID-19. T-helper 1 cell differentiation in COVID-19 HOIP_0039156 HOIP:HOIP_0039157 The change in morphology and behavior of a T-helper 1 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33123165 T-helper 1 cell activation in coronavirus infection HOIP_0039157 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0039158 An immune response which is associated with resistance to intracellular bacteria, fungi, and protozoa, and pathological conditions such as arthritis, and which is typically orchestrated by the production of particular cytokines by T-helper 1 cells, most notably interferon-gamma, IL-2, and lymphotoxin. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T-helper 1 type immune response in coronavirus infection HOIP_0039158 HOIP:HOIP_0039159 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. PMID:32221306 PMID:32641482 viral entry into host cell (moderate) in mild COVID-19 HOIP_0039159 PMID:32221306 As expected, apilimod treatment inhibited entry of SARS-CoV-2 S pseudovirions in a dose dependent manner (Fig. 3d). While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect (Supplementary Fig. 1), indicating that TPC2, not TRPML1, is important for SARS-CoV-2 entry. We confirmed this in this study, and further showed that blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. E64D treatment of 293/hACE2 cells reduced entry of SARS-CoV- 2 S pseudovirions by 92.5%, indicating that at least one of cathepsins or calpain might be required for SARS-CoV-2 entry (Fig. 4a). PMID:32641482 Moreover, we found that LY6E also efficiently restricted the entry mediated by the envelope spike proteins of other human coronaviruses, including the currently pandemic SARS-CoV-2. HOIP:HOIP_0039160 The innate immune system is one of the two main immunity strategies found in vertebrates (the other being the adaptive immune system). The innate immune system is an older evolutionary defense strategy, relatively speaking, and is the dominant immune system response found in plants, fungi, insects, and primitive multicellular organisms. The innate immune system is one of the two main immunity strategies found in vertebrates (the other being the adaptive immune system). The innate immune system is an older evolutionary defense strategy, relatively speaking, and is the dominant immune system response found in plants, fungi, insects, and primitive multicellular organisms. innnate immune system HOIP_0039160 The innate immune system is one of the two main immunity strategies found in vertebrates (the other being the adaptive immune system). The innate immune system is an older evolutionary defense strategy, relatively speaking, and is the dominant immune system response found in plants, fungi, insects, and primitive multicellular organisms. https://en.wikipedia.org/wiki/Innate_immune_system HOIP:HOIP_0039161 The totality of all processes to a homeostatic balance between functional supply by the immune system and functional demand by SARS-CoV2. The degree of clinical manifestation is mild. PMID:33723416 mild COVID-19 course HOIP_0039161 HOIP:HOIP_0039163 The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. PMID:32505227 PMID:33723416 early type I interferon production (moderate) in mild COVID-19 HOIP_0039163 PMID:33723416 When the type I interferon response to infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is early and robust, the viral load is quickly controlled, resulting in mild disease. This is followed by normal-level T cell and B cell responses. This may occur in young people or after low-dose viral exposure. https://www.ncbi.nlm.nih.gov/corecgi/tileshop/tileshop.fcgi?p=PMC3&id=76840&s=116&r=1&c=3 HOIP:HOIP_0039164 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. early cellular response to type I interferon (moderte) in mild COVID-19 HOIP_0039164 HOIP:HOIP_0039165 Type I interferon signaling is a subtype of biological signaling: A process transduced by the binding of a type I interferon to a receptor on the surface of a cell. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. early type I interferon signaling (moderate) in mild COVID-19 HOIP_0039165 HOIP:HOIP_0039166 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. negative regulation of viral genome replication (moderate) in mild COVID-19 HOIP_0039166 HOIP:HOIP_0039167 The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. natural killer cell activation (moderate) in mild COVID-19 HOIP_0039167 HOIP:HOIP_0039168 Any process that stops, prevents, or reduces the frequency, rate or extent of viral translation. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. negative regulation of viral translation (moderate) in mild COVID-19 HOIP_0039168 HOIP:HOIP_0039169 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class I. positive regulation of MHC class I biosynthetic process (moderate) in mild COVID-19 HOIP_0039169 HOIP:HOIP_0039170 Negative regulation of viral gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of viral gene expression. This process can constitute the course of mild COVID-19. negative regulation of viral gene expression (moderate) in mild COVID-19 HOIP_0039170 HOIP:HOIP_0039171 Increasing virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. This process can constitute the course of mild COVID-19. decreasing virus sensitivity in mild COVID-19 increasing virus resitance in mild COVID-19 HOIP_0039171 HOIP:HOIP_0039172 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. PMID:32629875 PMID:33077917 inflammatory response (moderate) in mild COVID-19 HOIP_0039172 PMID:32629875 This is consistent with the observation that inflammatory signals induce the rapid release of ANG2 from endothelial cells, particularly in the presence of TNFα, and that ANG2 inhibitors can reduce vessel inflammation. PMID:33077917 A case report of a patient with COVID-19-associated ARDS and pneumonia showed that treatment with a C3 inhibitor was safe and associated with a favourable course, suggesting that C3 blockade may have broad anti-inflammatory potential owing to the upstream positioning of C3 in innate immune cascade signalling. HOIP:HOIP_0039173 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. inflammatory cytokine production (moderate) in mild COVID-19 HOIP_0039173 HOIP:HOIP_0039174 The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33123165 neutrophil chemotaxis in lung (very high)in COVID-19 associated with ARDS HOIP_0039174 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039175 Inapparent COVID-19 infectious course is a subtype of coronavirus infectious course. The totality of all processes to a homeostatic imbalance between functional supply by the immune system and functional demand by COVID-19, but there are no symptoms. PMID:33723416 inapparent COVID-19 course HOIP_0039175 HOIP:HOIP_0039176 Viral entry-innate immune response imbalance is a subtype of stress response imbalance: A process that lacks a balance between the viral entry and the innate immune response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. Viral entry-innate immune response imbalance in inapparent COVID-19 HOIP_0039176 HOIP:HOIP_0039177 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. The functioning level is low. early cellular response to type I interferon (low) in inapparent COVID-19 HOIP_0039177 HOIP:HOIP_0039178 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. The functioning level is low. PMID:32629875 PMID:33077917 inflammatory response (very low) in inapparent COVID-19 HOIP_0039178 PMID:32629875 This is consistent with the observation that inflammatory signals induce the rapid release of ANG2 from endothelial cells, particularly in the presence of TNFα, and that ANG2 inhibitors can reduce vessel inflammation. PMID:33077917 A case report of a patient with COVID-19-associated ARDS and pneumonia showed that treatment with a C3 inhibitor was safe and associated with a favourable course, suggesting that C3 blockade may have broad anti-inflammatory potential owing to the upstream positioning of C3 in innate immune cascade signalling. HOIP:HOIP_0039179 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. The functioning level is low. inflammatory cytokine production (low) in inapparent COVID-19 HOIP_0039179 HOIP:HOIP_0039180 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. PMID:32843733 establishment of virus infection in inapparent COVID-19 HOIP_0039180 PMID:32843733 If the protective immune response is impaired, the virus is allowed to replicate and can cause widespread tissue damage. The lungs seem to be the main target, although other organs with high ACE2 expression, such as the intestine, heart, brain and kidney, might also be vulnerable. HOIP:HOIP_0039181 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. PMID:32221306 PMID:32641482 viral entry into host cell in inapparent COVID-19 SARS-CoV-2 entry to host cell in inapparent COVID-19 HOIP_0039181 PMID:32221306 As expected, apilimod treatment inhibited entry of SARS-CoV-2 S pseudovirions in a dose dependent manner (Fig. 3d). While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect (Supplementary Fig. 1), indicating that TPC2, not TRPML1, is important for SARS-CoV-2 entry. We confirmed this in this study, and further showed that blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. E64D treatment of 293/hACE2 cells reduced entry of SARS-CoV- 2 S pseudovirions by 92.5%, indicating that at least one of cathepsins or calpain might be required for SARS-CoV-2 entry (Fig. 4a). PMID:32641482 Moreover, we found that LY6E also efficiently restricted the entry mediated by the envelope spike proteins of other human coronaviruses, including the currently pandemic SARS-CoV-2. HOIP:HOIP_0039182 Organ malfunction is a subtype of malfunctioning process: A process that cannot perform organ(s) function appropriately or cannot realize it at all. This process can constitute the course of severe COVID-19. organ malfunction in severe COVID-19 HOIP_0039182 HOIP:HOIP_0039183 In the imbalance model, the basic units are as follows: 1) a functioning process (supply) for defense and maintaining homeostasis; 2) a functional demand process (demand) as demand activity; 3) balance/imbalance between demand activity and defense processes; and 4) outcome from organelles, cells, or tissues to the organ exhibiting abnormal manifestations. This entity is a compound state that includes step 1 to 4, and the defense performance level is very higher (VH) than usual which leads to imbalance and abnormal manifestations. imbalance VH< (demand action) HOIP_0039183 HOIP:HOIP_0039184 The migration of a leukocyte from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 inflammatory cell extravasation [COVOD-19 with ARDS] HOIP_0039184 PMID:33077917 C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma - pathological events that are all observed in severe cases of COVID-19. HOIP:HOIP_0039186 Any process that activates or increases the frequency, rate or extent of immune cell activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. positive regulation of immune cell activation in coronavirus infection HOIP_0039186 HOIP:HOIP_0039187 Any process that activates or increases the frequency, rate or extent of immune cell activation. This process can constitute the course of COVID-19. positive regulation of immune cell activation in COVID-19 HOIP_0039187 HOIP:HOIP_0039188 Any process that activates or increases the frequency, rate or extent of immune cell activation. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). positive regulation of immune cell activation in COVID-19 associated with ARDS HOIP_0039188 HOIP:HOIP_0039189 Any process that contributes to cytokine production by a natural killer cell. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. natural killer cell cytokine production in mild COVID-19 HOIP_0039189 HOIP:HOIP_0039190 Any process that contributes to inflammatory cytokine production by a natural killer cell. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. inflammatory cytokine production by natural killer cell (high) in moderate COVID-19 HOIP_0039190 HOIP:HOIP_0039191 The totality of all processes through which COVID-19 infection is realized. The degree of clinical manifestation is moderate. PMID:33723416 moderate COVID-19 course HOIP_0039191 HOIP:HOIP_0039192 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32221306 PMID:32641482 viral entry into host cell in moderate COVID-19 SARS-CoV-2 entry to host cell in moderate COVID-19 HOIP_0039192 PMID:32221306 As expected, apilimod treatment inhibited entry of SARS-CoV-2 S pseudovirions in a dose dependent manner (Fig. 3d). While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect (Supplementary Fig. 1), indicating that TPC2, not TRPML1, is important for SARS-CoV-2 entry. We confirmed this in this study, and further showed that blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. E64D treatment of 293/hACE2 cells reduced entry of SARS-CoV- 2 S pseudovirions by 92.5%, indicating that at least one of cathepsins or calpain might be required for SARS-CoV-2 entry (Fig. 4a). PMID:32641482 Moreover, we found that LY6E also efficiently restricted the entry mediated by the envelope spike proteins of other human coronaviruses, including the currently pandemic SARS-CoV-2. HOIP:HOIP_0039193 The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of COVID-19(moderate). PMID:32505227 PMID:33723416 type I interferon production (high) in moderate COVID-19 HOIP_0039193 HOIP:HOIP_0039194 Type I interferon signaling is a subtype of biological signaling: A process transduced by the binding of a type I interferon to a receptor on the surface of a cell. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. early type I interferon signaling (high) in moderate COVID-19 HOIP_0039194 HOIP:HOIP_0039195 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. cellular response to type I interferon (high) in moderate COVID-19 HOIP_0039195 HOIP:HOIP_0039196 The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. natural killer cell activation (high) in moderate COVID-19 HOIP_0039196 HOIP:HOIP_0039197 Increasing virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. decreasing virus sensitivity in moderate COVID-19 increasing virus resitance (high) in moderate COVID-19 HOIP_0039197 HOIP:HOIP_0039198 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. negative regulation of viral genome replication (high) in moderate COVID-19 HOIP_0039198 HOIP:HOIP_0039199 Negative regulation of viral gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of viral gene expression. negative regulation of viral gene expression (high) in moderate COVID-19 HOIP_0039199 HOIP:HOIP_0039200 Any process that stops, prevents, or reduces the frequency, rate or extent of viral translation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. negative regulation of viral translation (high) in moderate COVID-19 HOIP_0039200 HOIP:HOIP_0039201 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class I. positive regulation of MHC class I biosynthetic process (high) in moderate COVID-19 HOIP_0039201 HOIP:HOIP_0039202 The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. This process can constitute the course of moderate COVID-19. antigen processing and presentation of exogenous peptide antigen via MHC class I (high) in moderate COVID-19 HOIP_0039202 HOIP:HOIP_0039203 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19(moderate). PMID:32629875 PMID:33077917 inflammatory response (high) in moderate COVID-19 HOIP_0039203 PMID:32629875 This is consistent with the observation that inflammatory signals induce the rapid release of ANG2 from endothelial cells, particularly in the presence of TNFα, and that ANG2 inhibitors can reduce vessel inflammation. PMID:33077917 A case report of a patient with COVID-19-associated ARDS and pneumonia showed that treatment with a C3 inhibitor was safe and associated with a favourable course, suggesting that C3 blockade may have broad anti-inflammatory potential owing to the upstream positioning of C3 in innate immune cascade signalling. HOIP:HOIP_0039204 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. inflammatory cytokine production (high) in moderate COVID-19 HOIP_0039204 HOIP:HOIP_0039205 The totality of all processes through which COVID-19 infection is realized from inapparent to manifest severe symptoms. PMID:33723416 COVID-19 course (inapparent to apparent) HOIP_0039205 HOIP:HOIP_0039206 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation inflammatory response (very high) in apparent COVID-19 HOIP_0039206 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. The inflammatory response must be actively terminated when no longer needed to prevent unnecessary "bystander" damage to tissues.[10] Failure to do so results in chronic inflammation, and cellular destruction. HOIP:HOIP_0039207 Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production. This process can constitute the course of severe COVID-19. PMID:32505227 negative regulation of type I interferon production in severe COVID-19 HOIP_0039207 HOIP:HOIP_0039208 Expression of cell adhesion molecule expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature cell adhesion molecule gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. cell adhesion molecule expression in coronavirus infection HOIP_0039208 HOIP:HOIP_0039209 A molecular signal induced by NK cells which triggers the apoptotic death of a cell. natural killer cell mediated apoptotic signaling HOIP_0039209 HOIP:HOIP_0039210 Hyperfunction of lipid oxidation is a subtype of hyperfunction of lipid oxidation: A process that performs an excessive lipid oxidation. This entity is a specific course-dependent process. This process can constitute the course of diabetic ketoacidosis. hyperfunction of lipid oxidation [diabetic ketoacidosis course] HOIP_0039210 HOIP:HOIP_0039211 Hyperfunction of uptaking fatty acid into liver is a a process that performs an excesssive uptaking of fatty acids into the iver. This entity is a specific course-dependent process. This process can constitute the course of Lipidosis. hyperfunction of uptaking fatty acid into liver [diabetic ketoacidosis course] HOIP_0039211 HOIP:HOIP_0039212 Increasing free fatty acid concentration in blood is a subtype of increasing lipid concentration in blood: A process that changes the free fatty acid concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of diabetic ketoacidosis. increasing free fatty acid concentration in blood [diabetic ketoacidosis course] HOIP_0039212 HOIP:HOIP_0039213 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required. This entity is a specific course-dependent process. This process can constitute the course of diabetic ketoacidosis. insulin deficiency [diabetic ketoacidosis course] HOIP_0039213 HOIP:HOIP_0039214 Increasing osmotic pressure is a subtype of increasing pressure: A process that changes the osmotic pressure of the object to be higher. ncreasing osmotic pressure [diabetic ketoacidosis course] HOIP_0039214 HOIP:HOIP_0039215 A molecular signal induced by NK cells which triggers the apoptotic death of a cell. This process can constitute the course of coronavirus infectious disease. natural killer cell-mediated apoptotic process of infected cells in coronavirus infection HOIP_0039215 HOIP:HOIP_0039216 Dehydration is a subtype of decreasing concentration: A process that changes the concentration of the body fulids to be lower. dehydration (process) HOIP_0039216 HOIP:HOIP_0039217 Dehydration is a subtype of decreasing concentration: A process that changes the concentration of the body fulids to be lower. This entity is a specific course-dependent process. This process can constitute the course of diabetic ketoacidosis. dehydration (process) [diabetic ketoacidosis course] HOIP_0039217 HOIP:HOIP_0039218 A molecular signal induced by NK cells which triggers the apoptotic death of a cell. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. natural killer cell-mediated apoptotic process of infected cells (high) in moderate COVID-19 HOIP_0039218 HOIP:HOIP_0039219 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32843733 establishment of virus infection in moderate COVID-19 HOIP_0039219 PMID:32843733 If the protective immune response is impaired, the virus is allowed to replicate and can cause widespread tissue damage. The lungs seem to be the main target, although other organs with high ACE2 expression, such as the intestine, heart, brain and kidney, might also be vulnerable. HOIP:HOIP_0039220 A molecular signal induced by NK cells which triggers the apoptotic death of a cell. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. natural killer cell-mediated apoptotic process of infected cells (moderate) in mild COVID-19 HOIP_0039220 HOIP:HOIP_0039221 Any process involved directly in viral genome replication, including viral nucleotide metabolism. This entity is a specific course-dependent process. This process can constitute the course of coronaviurs infectious disease. PMID:32641482 viral genome replication in coronavirus infection HOIP_0039221 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0039222 The totality of all processes through which COVID-19 infection is realized. The degree of clinical manifestation is severe. PMID:33723416 severe COVID-19 course HOIP_0039222 HOIP:HOIP_0039223 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation inflammatory response (very high) in severe COVID-19 HOIP_0039223 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. The inflammatory response must be actively terminated when no longer needed to prevent unnecessary "bystander" damage to tissues.[10] Failure to do so results in chronic inflammation, and cellular destruction. HOIP:HOIP_0039224 Tissue damage is a subtype of damaging: A process that injuries the structure of the tissue as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 tissue damage (very high) in severe COVID-19 HOIP_0039224 PMID:32629875 As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. HOIP:HOIP_0039225 Inflammasome activation is a subtype of activating: A process that changes the activity of the inflammasome to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33153908 PMID:33231615 WikiPathways:WP4876 Wikipedia:Inflammasome inflammasome activation (very high) in severe COVID-19 HOIP_0039225 PMID:33153908 In the case of SARS-CoV-2, the specific ligands are also unknown, but infection with the virus can induce NLRP3 inflammasome activation, caspase-1 cleavage, and the release of IL-1β and IL-18 in PBMCs isolated from patients with COVID-19. Wikipedia:Inflammasome Inflammasome activation is initiated by different kinds of cytosolic pattern recognition receptors (PRRs) that respond to either microbe-derived pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) generated by the host cell. Traditionally, inflammasomes have mainly been studied in professional immune cells of the innate immune system, such as macrophages. More recent studies, however, indicate high levels of inflammasome component expression in epithelial barrier tissues, where they have been shown to represent an important first line of defense. As part of the innate immune system, inflammasomes play an important role in the induction of inflammatory cascades and coordination of host defenses, both via the activation and secretion of pro-inflammatory cytokines and the induction of a specialized form of immune-stimulatory programmed cell death termed pyroptosis. HOIP:HOIP_0039226 A caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID: 33153908 Wikipedia:Inflammasome Wikipedia:Pyroptosis pyroptosis (very high)in severe COVID-19 HOIP_0039226 Wikipedia:Inflammasome As part of the innate immune system, inflammasomes play an important role in the induction of inflammatory cascades and coordination of host defenses, both via the activation and secretion of pro-inflammatory cytokines and the induction of a specialized form of immune-stimulatory programmed cell death termed pyroptosis. Wikipedia:Pyroptosis Pyroptosis is a highly inflammatory form of lytic programmed cell death that occurs most frequently upon infection with intracellular pathogens and is likely to form part of the antimicrobial response. Pyroptosis can take place in immune cells and is also reported to occur in keratinocytes and some epithelial cells. Formation of pores causes cell membrane rupture and release of cytokines, as well as various damage-associated molecular pattern (DAMP) molecules such as HMGB-1, ATP and DNA, out of the cell. These molecules recruit more immune cells and further perpetuate the inflammatory cascade in the tissue. HOIP:HOIP_0039227 Cell damage recognition is a subtype of receiving: A process that recognizes the damages of cells. This process can constitute the course of severe COVID-19. cell damage recognition in severe COVID-19 HOIP_0039227 HOIP:HOIP_0039228 Interaction between host pattern recognition receptor and any DAMPs (damage-associated molecular patterns). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation binding of pattern recognition receptor to DAMPs in severe COVID-19 HOIP_0039228 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0039229 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 cell death (very high) in severe COVID-19 HOIP_0039229 PMID:32629875 In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Finally, we demonstrate that CoV-2-infected monocytes promote T cell dysfunction and lung epithelial cell death. This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. Finally, we demonstrate that CoV-2-infected monocytes promote T cell dysfunction and lung epithelial cell death. These data may explain why uncontrolled diabetes may lead to compromised adaptive immune response and lung dysfunction in patients with severe COVID-19 symptoms. HOIP:HOIP_0039230 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 inflammatory cell infiltration (very high)in severe COVID-19 HOIP_0039230 PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0039231 The movement of a leukocyte in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. immune cell chemotaxis leucocyte chemotaxis inflammatory cell chemotaxis (very high)in severe COVID-19 HOIP_0039231 HOIP:HOIP_0039232 The movement of a monocyte in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 monocyte chemotaxis (very high) in severe COVID-19 HOIP_0039232 PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell. HOIP:HOIP_0039233 The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 neutrophil chemotaxis (severe) in severe COVID-19 HOIP_0039233 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039234 The migration of a leukocyte from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 inflammatory cell extravasation (very high) [COVOD-19(severe)]2 HOIP_0039234 PMID:33077917 C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma - pathological events that are all observed in severe cases of COVID-19. HOIP:HOIP_0039235 The migration of a monocyte from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 monocyte extravasation (very high) in severe COVID-19 HOIP_0039235 PMID:32629875 Monocyte/macrophage-lineage cells, a major cell source of many pro-inflammatory cytokines, are numerically increased and phenotypically activated in many tissues of patients with severe COVID-19. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039236 The migration of a neutrophil from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 neutrophil extravasation (very high) in severe COVID-19 HOIP_0039236 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0039237 Any process that activates or increases the frequency, rate or extent of blood coagulation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32412710 PMID:32629875 PMID:33077917 positive regulation of blood coagulation (very high) in severe COVID-19 HOIP_0039237 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. PMID:32629875 In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). In a group of 22 consecutive COVID-19 patients admitted to the ICU, increased fibrinogen and D-dimer plasma levels, shorter clotting time and other coagulation abnormalities were significantly more frequent compared to healthy controls. Recently, new clinical syndromes associated with coagulopathy and vasculopathy have emerged as a cause of sudden death and other serious clinical manifestations in younger patients infected with SARS-CoV-2 infection. COVID-19, however, appears to include an evolving set of clinical manifestation not previously reported in SARS and MERS, including stroke and cardiomyopathies associated with coagulopathy and vasculopathy, which can cause sudden death and other serious morbidities. Patients with COVID-19 typically display hemostatic abnormalities consistent with the presence of a severe coagulopathy that predisposes to thrombotic events and is directly correlated with disease severity. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0039238 The synthesis or release of any molecular mediator of the inflammatory response following an inflammatory stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation synthesis or release of inflammatory mediator (very high) in severe COVID-19 HOIP_0039238 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. HOIP:HOIP_0039239 Increasing vascular permeabilization is a subtype of changing permeability: A process that changes the permeability of the vascular to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 increasing vascular permeabilization (very high) in severe COVID-19 HOIP_0039239 PMID:33077917 C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma - pathological events that are all observed in severe cases of COVID-19. Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. Mechanistically, disruption of the endothelial barrier by SARS-CoV-2 spike protein is mediated by changes in the surface expression of intracellular adhesion molecule-1 (ICAM1), vascular cell adhesion protein-1 (VCAM1) and the tight junction scaffold protein zonula occludens-1 (ZO-1), as reported by a preprint study. HOIP:HOIP_0039240 Leaking fluid from blood vessel is a subtype of leaking: A process that leaks fluid out from the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. leaking fluid from blood vessel (very high) in severe COVID-19 HOIP_0039240 HOIP:HOIP_0039241 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 PMID:33077917 PMID:33188364 Inflammatory cytokine production (very high) in severe COVID-19 HOIP_0039241 PMID:32629875 The systemic increase of pro-inflammatory cytokines in many patients with severe COVID-19 is likely another major contributor to the vascular pathology in COVID-19 (Section 4.3). Monocyte/macrophage-lineage cells, a major cell source of many pro-inflammatory cytokines, are numerically increased and phenotypically activated in many tissues of patients with severe COVID-19. PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Elevated glucose levels directly induce viral replication and proinflammatory cytokine expression. PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. PMID:33188364 Changes in insulin needs are seemingly associated with the levels of inflammatory cytokines. In individuals with obesity, pro-inflammatory cytokines with a T helper type 1 cell signature are known to increase insulin resistance; however, the role of such cytokines in COVID-19 is unclear. HOIP:HOIP_0039242 Organ damage is a subtype of damaging: A process that injuries the structure of the organ as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 organ damage in severe COVID-19 HOIP_0039242 PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. HOIP:HOIP_0039243 Multi-organ dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete multi-organ function. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32651579 multi-organ dysfunction in severe COVID-19 HOIP_0039243 PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. PMID:32651579 Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. HOIP:HOIP_0039244 Neutrophil extracellular trap formation is a subtype of biological structure formation: A process that construcs neutrophil extracellular trap. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 PMID:33214651 neutrophil extracellular trap formation in severe COVID-19 HOIP_0039244 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. PMID:33214651 Neutrophil extracellular traps (NETs) have been shown to trigger thromboinflammation in patients with COVID-19, leading to vascular thrombosis and a high risk of death. HOIP:HOIP_0039245 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a natural killer cell. This process can constitute the course of coronavirus infectious disease. natural killer cell degranulation in coronavirus infection HOIP_0039245 HOIP:HOIP_0039246 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a natural killer cell. This process can constitute the course of mild COVID-19. natural killer cell degranulation (moderate) in mild COVID-19 HOIP_0039246 HOIP:HOIP_0039247 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a natural killer cell. This process can constitute the course of moderate COVID-19. natural killer cell degranulation (moderate) in moderate COVID-19 HOIP_0039247 HOIP:HOIP_0039248 Leaking content from cell is a subtype of leaking: A process that leaks contents from the cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. leaking content from cell in severe COVID-19 HOIP_0039248 HOIP:HOIP_0039249 The complement system is a set of plasma proteins that act together to attack extracellular forms of pathogens. Complement activation can occur spontaneously on certain pathogens or by antibody binding to the pathogen. The complement system is a set of plasma proteins that act together to attack extracellular forms of pathogens. Complement activation can occur spontaneously on certain pathogens or by antibody binding to the pathogen. complement HOIP_0039249 The complement system is a set of plasma proteins that act together to attack extracellular forms of pathogens. Complement activation can occur spontaneously on certain pathogens or by antibody binding to the pathogen. https://www.ncbi.nlm.nih.gov/books/NBK10759/def-item/A2720/ HOIP:HOIP_0039250 A set or series of molecular interactions of the steps of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. complement cascade HOIP_0039250 HOIP:HOIP_0039251 A leukocyte granule-associated proteinase that is a translation product of the granzyme gene or a 1:1 ortholog thereof. Granzyme HOIP_0039251 HOIP:HOIP_0039252 Increasing ALT concentration in blood is a subtype of increasing concentration: A process that changes the alanine aminotransferase (ALT) concentration to be higher. This process can constitute the course of severe COVID-19. PMID:32687793 http://purl.bioontology.org/ontology/MEDDRA/10001845 increasing blood GPT concentration increasing blood ALT concentration in severe COVID-19 HOIP_0039252 PMID:32687793 In a Chinese retrospective study, patients with diabetes had more severe pneumonia, higher concentrations of lactate dehydrogenase, α-hydroxybutyrate dehydrogenase, alanine aminotransferase, and γ-glutamyl transferase, and fewer lymphocytes with a higher neutrophil count. HOIP:HOIP_0039253 Increasing AST concentration in blood is a subtype of increasing concentration: A process that changes the aspartate amino transferase (AST) concentration to be higher. This process can constitute the course of severe COVID-19. PMID:33520337 http://purl.bioontology.org/ontology/MEDDRA/10003544 inreasing blood GOT concentration increasing blood AST concentration (very high) in severe COVID-19 HOIP_0039253 HOIP:HOIP_0039254 A tissue-resident macrophage located in the alveolus of lung. alveolar macrophage HOIP_0039254 HOIP:HOIP_0039255 A T cell that expresses a gamma-delta T cell receptor complex. gamma-delta T cell HOIP_0039255 HOIP:HOIP_0039256 The directed killing of a target cell by a neutrophil. This process can constitute the course of severe COVID-19. PMID:28792873 neutrophil mediated cytotoxicity (very high) in severe COVID-19 HOIP_0039256 HOIP:HOIP_0039257 The appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 PMID:33123165 chemokine production (very high) in severe COVID-19 HOIP_0039257 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0039258 Chemokine signaling is a process that a signal is transmitted by the chemokine. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 PMID:33123165 chemokine signaling (very high) in severe COVID-19 HOIP_0039258 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0039259 The appearance of interleukin-8 due to biosynthesis or secretion by inflammatory macrophages following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of severe COVID-19. PMID:32505227 inflammatory macrophage CXCL8 production inflammatory macrophage interleukin-8 production in severe COVID-19 HOIP_0039259 PMID:32505227 Similarly, SARS-CoV-2 NSP9 and NSP10 might induce IL-6 and IL-8 production, potentially by inhibition of NKRF, an endogenous NF-kB repressor (Li et al., 2020a). HOIP:HOIP_0039260 The release of any leukotriene following a stimulus as part of an inflammatory response. leukotriene secretion involved in inflammatory response HOIP_0039260 HOIP:HOIP_0039261 CXCL8 signaling is a process that a signal is transmitted by CXCL8. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. CXCL8 signaling (very high) in severe COVID-19 HOIP_0039261 HOIP:HOIP_0039262 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32651579 PMID:32697943 PMID:32843733 PMID:33123165 cytokine storm in severe COVID-19 HOIP_0039262 PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. PMID:32651579 Dysregulated immune response and cytokine-release syndrome, due to overactivation of innate immunity in the setting of T cell lymphodepletion, characterize the presentations of severe COVID-19. Hyperinflammation seen with cytokine storm and hypoxia-associated metabolic derangements are other potential mechanisms of liver damage. PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). The cytokine storm is thought to be associated with lymphopenia in COVID-19 patients (Zheng et al., 2020). PMID:32843733 The idea that the cytokine storm is mediated by leukocytes other than T or B cells is supported by observations of lymphocytopenia and sometimes atrophy of the lymphatic tissues, such as lymph nodes and spleen, in patients with severe COVID-19. PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. HOIP:HOIP_0039263 A change in morphology and behavior of an inflammatory cell resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. inflammatory cell activation (very high) in severe COVID-19 HOIP_0039263 HOIP:HOIP_0039264 The directed killing of a target cell by an inflammatory cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32887954 inflammtory cell mediated cytotoxicity (very high)in severe COVID-19 HOIP_0039264 PMID:32887954 Furthermore, patients with symptomatic COVID-19 are reported to produce IgG anti-bodies with reduced fucosylation levels, which in turn promotes their interaction with activating FcgammaRIIIa. Fc-mediated effector functions: immune functions that are mediated through the interaction of the constant Fc region of antibodies with innate immune molecules, complement proteins and specialized Fc receptors expressed by innate immune cells. The resulting functions include complement-dependent cytotoxicity and antibody-dependent cellular phagocytosis or cell-mediated cytotoxicity. HOIP:HOIP_0039265 The directed killing of a target cell by a macrophage. macrophage mediated cytotoxicity HOIP_0039265 HOIP:HOIP_0039266 The directed killing of a target cell by a macrophage. This process can constitute the course of severe COVID-19. inflammatory macrophage mediated cytotoxicity (very high) in severe COVID-19 HOIP_0039266 HOIP:HOIP_0039267 Inflammatory cytokine signaling is a process that a signal is transmitted by the inflammatory cytokine. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 PMID:33077917 inflammatory cytokine signaling in severe COVID-19 HOIP_0039267 PMID:32629875 The systemic increase of pro-inflammatory cytokines in many patients with severe COVID-19 is likely another major contributor to the vascular pathology in COVID-19 (Section 4.3). PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0039268 A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. PMID:32629875 macrophage activation involved in inflammatory response (vey high) in severe COVID-19 HOIP_0039268 TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. https://www.ncbi.nlm.nih.gov/books/NBK27153/ PMID:32629875 Monocyte/macrophage-lineage cells, a major cell source of many pro-inflammatory cytokines, are numerically increased and phenotypically activated in many tissues of patients with severe COVID-19. HOIP:HOIP_0039269 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. This process can constitute the course of severe COVID-19. phagocytosis by inflammatory macrophage in severe COVID-19 HOIP_0039269 HOIP:HOIP_0039270 The process in which a relatively unspecialized myeloid precursor cell acquires the specialized features of a monocyte. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 monocyte differentiation (very high)in severe COVID-19 HOIP_0039270 PMID:32629875 GM-CSF, often abnormally elevated in plasma of severe COVID-19 patients, likely is a main contributor to this pathology, as GM-CSF promotes hematopoietic stem/progenitor cell differentiation into monocytes in the bone marrow, their release into the circulation and their activation. HOIP:HOIP_0039271 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32307653 PMID:32697943 PMID:33123165 macrophage cell differentiation inflammatory macrophage differentiation (very high) in severe COVID-19 HOIP_0039271 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. ISBN:0781735149 PMID:32307653 Some regions of reactive epithelial hyperplasia had also abundant alveolar macrophages. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32697943 Upon infection, there is an accumulation of immune cells in the lungs, especially macrophages and monocytes. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039272 The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 neutrophil activation involved in inflammatory response (very high) in severe COVID-19 HOIP_0039272 PMID:33077917 Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0039273 A vesicle-mediated transport process that results in the engulfment of external particulate material by neutrophils. This process can constitute the course of severe COVID-19. phagocytosis by neutrophils in severe COVID-19 HOIP_0039273 HOIP:HOIP_0039274 Neutrophil phagocytosis insufficiency is a subtype of insufficient functioning: A process that lacks enough to perform the function of neutrophil phagocytosis. neutrophil phagocytosis insufficiency HOIP_0039274 HOIP:HOIP_0039275 Neutrophil phagocytosis insufficiency is a subtype of insufficient functioning: A process that lacks enough to perform the function of neutrophil phagocytosis. This process can constitute the course of severe COVID-19. neutrophil phagocytosis insufficiency in severe COVID-19 HOIP_0039275 HOIP:HOIP_0039276 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32339221 PMID:32629875 PMID:33077917 Wikipedia:Coagulation blood clotting blood coagulation (very high) in severe COVID-19 HOIP_0039276 PMID:32339221 The initial coagulopathy of COVID-19 presents with prominent elevation of D-dimer and fibrin/fibrinogen-degradation products, whereas abnormalities in prothrombin time, partial thromboplastin time, and platelet counts are relatively uncommon in initial presentations. Coagulation test screening, including the measurement of D-dimer and fibrinogen levels, is suggested. PMID:32629875 In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). PMID:33077917 Although clinical insights into complement activation following SARS-CoV-2 infection are limited, the above findings indicate that unrestrained complement activation - mainly at the downstream terminal phases of the complement cascades - may contribute to endothelial cell injury, thrombosis and intravascular coagulation, ultimately leading to multi-systemic organ failure in patients with COVID-19. Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0039277 Increasing D-dimer concentration is a subtype of increasing concentration: A process that changes the D-dimer concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32407672 PMID:32629875 PMID:32651579 increasing D-dimer concentration (very high) in severe COVID-19 HOIP_0039277 PMID:32407672 The most typical finding in patients with COVID-19 and coagulopathy is an increased D-dimer concentration, a relatively modest decrease in platelet count, and a prolongation of the prothrombin time. PMID:32629875 In a cohort of 183 patients with COVID-19, the 21 patients who died (11.5%) differed from those who did not in having increased levels of D-dimer (a fibrin protein fragment; ~3.5-fold) and other fibrin degradation products (~1.9-fold). In a group of 22 consecutive COVID-19 patients admitted to the ICU, increased fibrinogen and D-dimer plasma levels, shorter clotting time and other coagulation abnormalities were significantly more frequent compared to healthy controls. The most common imaging and laboratory findings included abnormal chest CT scans (71 % ground-glass opacity and 30% consolidation), lymphopenia (48%), increased lactate dehydrogenase (42%), D-Dimer elevation (43%), and indicators of inflammation, including C-reactive protein and erythrocyte sedimentation rate. PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. Elevated levels of D-dimer at admission (reported in up to 46% of hospitalized patients) and a longitudinal increase during hospitalization have been linked with worse mortality in COVID-19. HOIP:HOIP_0039278 Any process that activates or increases the frequency, rate or extent of thrombus formation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32651579 PMID:33077917 positive regulation of thrombus formation (very high) in severe COVID-19 HOIP_0039278 PMID:32629875 Second, to infect cells, SARS-CoV-2 binds to the cell surface ACE2 receptors, and in so doing compromises the vaso-protective functions of ACE2, an enzyme that attenuates the vasoconstrictive, pro-inflammatory, pro-apoptotic, pro-thrombotic and mitogenic effects of angiotensin II, as discussed in Section 4.2. PMID:32651579 Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. While patients with viral infections are at risk for MI in gen-eral, this risk may be exaggerated in patients with COVID-19, given reports of disproportionately increased hypercoagulability in affected people, which would lead to a possible increase in thrombotically mediated MI. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. HOIP:HOIP_0039279 Microthrombus formation is a subtype of thrombus formation: A process that construcs microthrombus. This process can constitute the course of severe COVID-19. PMID:28792873 PMID:32629875 PMID:32651579 PMID:33077917 microthrombus formation in severe COVID-19 HOIP_0039279 PMID:32629875 Another autopsy series on 67 COVID-19 cases described the presence of vascular microthrombi in multiple organs, particularly in the lungs (in 23/25 cases) where it was associated with capillary sprouting and capillary inflammation, and in the brain (in 6/20 cases) where it was associated with evidence of patchy acute infarcts. The pulmonary capillary vessels of COVID-19 tissues contained microthrombi and evidence of intravascular (intussusceptive) neovascularization, which were more frequent than observed in the influenza cases PMID:32651579 Autopsy studies of patients who died due to COVID-19 have shown high rates of microvascular and macrovascular thromboses, especially in the pulmonary circulation. Microthrombi and microangiopathic pathology, associated with foci of hemorrhage, were also noted on autopsies of ten African-American patients with severe COVID-19 from New Orleans, Louisiana, USA100. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0039280 The extension of new blood vessels from existing vessels into avascular tissues, this process includes the specialization of endothelial cells into leading tip and stalk cells, proliferation and migration of the endothelial cells and cell adhesion resulting in angiogenic sprout fusion or lumen formation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 sprouting angiogenesis in severe COVID-19 HOIP_0039280 PMID:32629875 Another autopsy series on 67 COVID-19 cases described the presence of vascular microthrombi in multiple organs, particularly in the lungs (in 23/25 cases) where it was associated with capillary sprouting and capillary inflammation, and in the brain (in 6/20 cases) where it was associated with evidence of patchy acute infarcts. As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. In addition, by promoting VEGF-A secretion from various cell types, IL-6 induces vascular hyper-permeability and sprouting angiogenesis. HOIP:HOIP_0039281 Microvascular dysfunction is a subtype of organ malfunction: A process that does not perform microvascular function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. microvascular dysfunction in severe COVID-19 HOIP_0039281 HOIP:HOIP_0039282 thrombus formation is a subtype of biological structure formation: A process that construcs thrombus. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32412710 PMID:32629875 PMID:32651579 PMID:33077917 thrombus formation (severe) in severe COVID-19 HOIP_0039282 PMID:32412710 The majority of patients with severe Covid-19 have lymphopenia, and some have thromboembolic complications as well as disorders of the central or peripheral nervous system. PMID:32629875 An autopsy series showed the presence of deep venous thrombosis involving the lower extremities bilaterally in 56% (7/12) of cases, associated with massive pulmonary embolism in four of these cases, which was listed as the cause of death. Post-mortem histopathologic analysis of lung tissue from 38 COVID-19 patients documented the presence of platelet-fibrin thrombi in lung arterioles of most (33/38) cases, congested capillaries (33/38) proximal to hemorrhagic alveoli often containing CD61+ megakaryocytes, and dense capillary foci presumably resulting from vessel intussusceptive sprouting (18/38). As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. Consistent with the presence of a coagulopathy, deep vein thrombosis appears more frequently than expected in hospitalized COVID-19 patients, even with anti-coagulant prophylaxis. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. The presence of thrombi involving the portal venules was observed in 15/22 autopsies, occasionally associated with thrombi in some hepatic arteries and arterioles. Thus, IL-6 can promote a pro-coagulant and pro-thrombotic vascular pathology, raising the possibility that an abnormally high level of IL-6 may contribute to the vascular phenotype in severe COVID-19. Also, among patients who died with COVID-19, 71% met the International Society on Thrombosis and Haemostasis criteria for disseminated intravascular coagulation (DIC), compared to only 0.6% of the survivors. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32651579 There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. PMID:33077917 Although clinical insights into complement activation following SARS-CoV-2 infection are limited, the above findings indicate that unrestrained complement activation - mainly at the downstream terminal phases of the complement cascades - may contribute to endothelial cell injury, thrombosis and intravascular coagulation, ultimately leading to multi-systemic organ failure in patients with COVID-19. Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0039283 Narrowing of the artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the arteries to be smaller. artery narrowing HOIP_0039283 HOIP:HOIP_0039284 Narrowing of the artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. artery narrowing in severe COVID-19 HOIP_0039284 HOIP:HOIP_0039285 Decreasing blood flow is a subtype of decreasing flow: A process that changes the blood flow to be smaller. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. decreasing blood flow in severe COVID-19 HOIP_0039285 HOIP:HOIP_0039286 Ischemia is a changing process to lack enough to blood supply. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. ischemia in severe COVID-19 HOIP_0039286 HOIP:HOIP_0039287 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. necrosis in severe COVID-19 HOIP_0039287 HOIP:HOIP_0039288 In response to several stimuli, neutrophils and eosinophils can release the so-called neutrophil extracellular traps (NETs), that is, microbicidal structures composed of nuclear chromatin, histones and granular antimicrobial proteins. Netotic cells exhibit massive vacuolization of the cytoplasm, rapid chromatin decondensation and breakdown of both the nuclear and granular membranes, which is required for proper NET formation. Netosis is insensitive to caspase inhibitors and necrostatin-1, further demonstrating that it constitutes a cell death subroutine distinct from apoptosis and regulated necrosis. Netosis might be defined as a cell death subroutine that is: (i) restricted to granulocytic cells; (ii) insensitive to (and perhaps dependent on)163 caspase inhibition; (iii) insensitive to necrostatin; (iv) dependent on NAPDH oxidase-mediated superoxide generation; and (v) dependent on (components of) the autophagic machinery https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:28792873 PMID:33077917 PMID:33214651 PMID:33214719 netosis in severe COVID-19 HOIP_0039288 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. PMID:33214651 Neutrophil extracellular traps (NETs) have been shown to trigger thromboinflammation in patients with COVID-19, leading to vascular thrombosis and a high risk of death. PMID:33214719 Neutrophils entrapped inside inflamed pulmonary vessels can produce neutrophil extracellular traps (NETs) in a process termed ‘NETosis’, and these are thought to capture viral particles and thereby restrict viral dissemination. However, NETosis can also aggravate damage to the pulmonary endothelia and epithelia in severe influenza-induced pneumonia. NETs also activate the extrinsic and intrinsic coagulation pathway. HOIP:HOIP_0039289 Vascular endothelial cell damage damage is a subtype of cellular damage: A process that injuries the structure of the vascular endothelial cell. This process can constitute the course of severe COVID-19. PMID:33077917 vascular endothelial cell damage in severe COVID-19 HOIP_0039289 PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0039290 The regulated release of histamine by a cell as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. WikiPedia:Anaphylatoxin Wikipedia:Inflammation histamine secretion involved in inflammatory response (very high) in severe COVID-19 HOIP_0039290 WikiPedia:Anaphylatoxin The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Redness and heat are due to increased blood flow at body core temperature to the inflamed site; swelling is caused by accumulation of fluid; pain is due to the release of chemicals such as bradykinin and histamine that stimulate nerve endings. Histamine: Stored in preformed granules, histamine is released in response to a number of stimuli. It causes arteriole dilation, increased venous permeability, and a wide variety of organ-specific effects. HOIP:HOIP_0039291 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 PMID:32843733 antiviral innate immune response (very high) in severe COVID-19 HOIP_0039291 PMID:32651579 Dysregulated immune response and cytokine-release syndrome, due to overactivation of innate immunity in the setting of T cell lymphodepletion, characterize the presentations of severe COVID-19. PMID:32843733 The damaged cells in the lungs elicit a strong innate immune response, which seems to be largely mediated by pro-inflammatory macrophages and granulocytes. This response is thought to be responsible for the cytokine release syndrome or ‘cytokine storm’ that is believed to contribute to ARDS. HOIP:HOIP_0039293 Increasing vascular lumen area is a subtype of increasing area: A process that changes the area of the vascular lumen area to be larger. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation Vasodilation 血管拡張 increasing vascular lumen area in severe COVID-19 HOIP_0039293 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039294 Increasing blood flow is a subtype of increaseing flow: A process that changes the amount of blood flow to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation increasing blood flow in severe COVID-19 HOIP_0039294 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039295 Increasing temperature is a subtype of changing temperature: A process that increases the temperature of the object. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation heat increasing temperature (severe)in severe COVID-19 HOIP_0039295 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039296 Edema is a subtype of accumulation of fluids: A process that keeps an excessive fluid in cells or intercellular tissues. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. HP:0000969 PMID:32629875 edema (process) in severe COVID-19 HOIP_0039296 HP:0000969 Edema may be related to one or more of the following factors: 1) increased capillary hydrostatic pressure, 2) decreased osmotic pressure of plasma, 3) decreased tissue tension and lymphatic drainage, 4) increased osmotic pressure of tissue fluids, and 5) increased capillary permeability. PMID:32629875 As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. A post-mortem imaging study involving 19 patients who had died of COVID-19 disease showed subcortical bleeds in 2/19 cases and edematous changes in the cortex/subcortical regions in 1/19 cases. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. HOIP:HOIP_0039297 A phase of elevated metabolic activity, during which oxygen consumption increases following a stimulus as part of an inflammatory response; this leads to the production, by an NADH dependent system, of hydrogen peroxide (H2O2), superoxide anions and hydroxyl radicals, resulting in an increase in their intracellular or extracellular levels. This process can constitute the course of severe COVID-19. respiratory burst involved in inflammatory response in severe COVID-19 HOIP_0039297 HOIP:HOIP_0039300 Way is manner or method of doing or happening. way HOIP_0039300 HOIP:HOIP_0039301 A decrease in the diameter of blood vessels, especially arteries, due to constriction of smooth muscle cells that line the vessels, and usually causing an increase in blood pressure. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32694793 vasoconstriction in severe COVID-19 HOIP_0039301 PMID:32694793 Angiotensin II, the active RAS metabolite and a potent vasoconstrictor that increases peripheral vascular resistance, also causes insulin resistance and regulates sodium absorption in the kidneys. HOIP:HOIP_0039302 The appearance of delayed immunoglobulin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32350462 PMID:33391280 delayed immunoglobulin production in severe COVID-19 HOIP_0039302 PMID:32350462 Within 19 days after symptom onset, 100% of patients tested positive for antiviral immunoglobulin-G (IgG). Seroconversion for IgG and IgM occurred simultaneously or sequentially. PMID:33391280 Our data show that high frequency of NK cells and early and transient increase of specific IgA, IgM and, to a lower extent, IgG are associated with asymptomatic SARS-CoV-2 infection. By contrast, monocyte expansion and high and persistent levels of IgA and IgG, produced relatively late in the course of the infection, characterize severe disease. HOIP:HOIP_0039303 The regulated release of a prostaglandin that contributes to the immune response. Prostaglandins are a group of biologically active metabolites which contain a cyclopentane ring. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation prostaglandin secretion involved in inflammatory response in severe COVID-19 HOIP_0039303 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0039304 High fever is a subtype of increaseing body temperature: A process that increases the temperature of the body. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 Wikipedia:Inflammation high fever in severe COVID-19 HOIP_0039304 PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0039305 Any process that results in a change in state or activity of a cell as a result of a stimulus of pain sensation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation response to pain sensation stimulus in severe COVID-19 HOIP_0039305 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039307 A change in morphology and behavior of an inflammatory cell resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. inflammatory cell activation in coronavirus infection HOIP_0039307 HOIP:HOIP_0039308 The release of any leukotriene following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation leukotriene secretion involved in inflammatory response (very high) in severe COVID-19 HOIP_0039308 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. leukotriene B4: Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0039309 The release of bradykinin following a stimulus as part of an inflammatory response. bradykinin secretion involved in inflammatory response HOIP_0039309 HOIP:HOIP_0039310 The release of bradykinin following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation bradykinin secretion involved in inflammatory response (very high) in severe COVID-19 HOIP_0039310 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Bradykinin: A vasoactive protein that is able to induce vasodilation, increase vascular permeability, cause smooth muscle contraction, and induce pain. HOIP:HOIP_0039311 A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. WikiPedia:Anaphylatoxin smooth muscle contraction (very high) in severe COVID-19 HOIP_0039311 WikiPedia:Anaphylatoxin The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. HOIP:HOIP_0039312 The directed killing of a target cell by an inflammatory cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. inflammtory cell mediated cytotoxicity in coronavirus infection HOIP_0039312 HOIP:HOIP_0039313 A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Coagulation platelet activation (very high) in severe COVID-19 HOIP_0039313 Wikipedia:Coagulation When the endothelium is damaged, the normally isolated, underlying collagen is exposed to circulating platelets, which bind directly to collagen with collagen-specific glycoprotein Ia/IIa surface receptors. This adhesion is strengthened further by von Willebrand factor (vWF), which is released from the endothelium and from platelets; vWF forms additional links between the platelets' glycoprotein Ib/IX/V and A1 domain. Binding of collagen to glycoprotein VI triggers a signaling cascade that results in activation of platelet integrins Activated platelets release the contents of stored granules into the blood plasma. The main role of the tissue factor pathway is to generate a "thrombin burst", a process by which thrombin, the most important constituent of the coagulation cascade in terms of its feedback activation roles, is released very rapidly. HOIP:HOIP_0039314 The regulated exocytosis of secretory granules containing preformed mediators such as histamine and serotonin by a platelet. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. platelet degranulation (very high) in severe COVID-19 HOIP_0039314 HOIP:HOIP_0039315 The adhesion of one platelet to one or more other platelets via adhesion molecules. This process can constitute the course of severe COVID-19. PMID:32629875 platelet aggregation (very high) in severe COVID-19 HOIP_0039315 PMID:32629875 Similarly, thrombi/platelet aggregates were visualized microscopically in capillaries, arterioles and medium sized arteries of most COVID-19 lungs (21/23). HOIP:HOIP_0039316 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33077917 additional inflammatory cytokine production (very high) in severe COVID-19 HOIP_0039316 PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. PMID:33077917 Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0039317 The chemical reactions and pathways resulting in the formation of platelet activating factor, 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine, where alkyl = hexadecyl or octadecyl. Platelet activating factor is an inflammatory mediator released from a variety of cells in response to various stimuli. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. platelet activating factor production involved in inflammatory response (very high) [COVID-198severe)]2 HOIP_0039317 HOIP:HOIP_0039318 A dendritic cell type of distinct morphology, localization, and surface marker expression (CD123-positive) from other dendritic cell types and associated with early stage immune responses, particularly the release of physiologically abundant amounts of type I interferons in response to infection. interferon-producing cell IPC pDC plasmacytoid dendritic cell HOIP_0039318 HOIP:HOIP_0039319 The change in morphology and behavior of a monocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 monocyte activation involved in inflammatory response (very high) in severe COVID-19 HOIP_0039319 PMID:32629875 Monocyte/macrophage-lineage cells, a major cell source of many pro-inflammatory cytokines, are numerically increased and phenotypically activated in many tissues of patients with severe COVID-19. PMID:32697943 Glycolysis Is Necessary for SARS-CoV-2 Replication and Monocyte Response Taken together, our results indicate that CoV-2 replication in monocytes and CoV-2-induced monocyte response are sustained by a switch to aerobic glycolysis (the Warburg effect). HOIP:HOIP_0039320 Any process that activates or increases the frequency, rate, or extent of interferon-alpha production. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is very low. positive regulation of interferon-alpha production in the early stage (low) in severe COVID-19 HOIP_0039320 HOIP:HOIP_0039321 type I interferon production The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families in the early stage of the infection. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:25301932 early type I interferon production (low) in severe COVID-19 HOIP_0039321 HOIP:HOIP_0039322 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels in the early stage of the infection. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. PMID:32697943 early interferon-alpha production (low) in severe COVID-19 HOIP_0039322 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Moreover, increased glucose levels further augmented TNF-a, IL-6, and IFN a, b, and l expression (Figure S1A). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0039323 The appearance of interferon-beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels in the early stage of the infection. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. PMID:32697943 early interferon-beta production (severe) [COVID-19 (low)]2 HOIP_0039323 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0039324 Type I interferon signaling is a subtype of biological signaling: A process transduced by the binding of a type I interferon to a receptor on the surface of a cell. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. early type I interferon signaling (low) in severe COVID-19 HOIP_0039324 HOIP:HOIP_0039325 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. early cellular response to type I interferon (low) in severe COVID-19 HOIP_0039325 In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. PMID:33153908 SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. PMID:32505227 HOIP:HOIP_0039326 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 PMID:33077917 PMID:33188364 PMID:33318364 reactive oxygen species biosynthetic process (very high) in severe COVID-19 HOIP_0039326 PMID:32697943 Reactive oxygen species (ROS) are strong inducers of HIF-1a (Mills et al., 2016). We observed that CoV-2-infected monocytes have increased mtROS production as measured by mitoSOX (Figure 3J). These data indicate that RET is an important source of mtROS in CoV-2-infected monocytes. SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. PMID:33188364 ROS production and viral activation of the renin–angiotensin–aldosterone system (RAAS), (via increased angiotensin II expression) cause insulin resistance, hyperglycaemia and vascular endothelial damage, all of which contribute to cardiovascular events, thromboembolism and disseminated intravascular coagulation (DIC). Through increasing oxidative stress, IL-6 can damage proteins, lipids and DNA, and impair the body’s structure and function, and we propose that this effect might lead to rapid progression of COVID-19 in patients with diabetes mellitus (fig. 1). PMID:33318364 In human monocytes, elevated glucose levels directly increase SARS-CoV-2 replication, and glycolysis sustains SARS-CoV-2 replication via the production of mitochondrial reactive oxygen species and activation of hypoxia-inducible factor 1α. HOIP:HOIP_0039327 The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:34049969 T cell activation (very high) in severe COVID-19 HOIP_0039327 PMID:34049969 We found that ex vivo T cells from acutely infected COVID-19 patients were highly activated and apoptotic and displayed more extensive mitochondrial metabolic dysfunction, especially cells in CD8+ T cell lineages, than those from convalescent COVID-19 patients or healthy controls, but slightly disturbed mitochondrial metabolic activity was observed in non-COVID-19 patients. Importantly, plasma IL-6 and C-reactive protein (CRP) levels positively correlated with mitochondrial mass and negatively correlated with fatty acid uptake in T cells from COVID-19 patients. HOIP:HOIP_0039328 A change in morphology and behavior of an additional macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. ISBN:0815345518 PMID:32629875 additional macrophage activation involved in inflammatory response (vey high) in severe COVID-19 HOIP_0039328 ISBN:9780815345510 Janeway's Immunobiology, 9th ed. PMID:33879239 TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. https://www.ncbi.nlm.nih.gov/books/NBK27153/ PMID:32629875 Monocyte/macrophage-lineage cells, a major cell source of many pro-inflammatory cytokines, are numerically increased and phenotypically activated in many tissues of patients with severe COVID-19. HOIP:HOIP_0039329 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. This process can constitute the course of severe COVID-19. phagocytosis by inflammatory macrophage (very high) in severe COVID-19 HOIP_0039329 HOIP:HOIP_0039330 A role played by the entity which changes the activity of the operand(s). actovator role HOIP_0039330 HOIP:HOIP_0039331 A role played by the entity that regulates the activity of tumor cells. regulator of tumor cell activity role HOIP_0039331 HOIP:HOIP_0039332 A role played by the entity that activates the activity of macrophages. macrophage activator role HOIP_0039332 HOIP:HOIP_0039333 Any process that activates or increases the frequency, rate or extent of monocyte production. positive regulation of monocyte production HOIP_0039333 HOIP:HOIP_0039334 Any process that activates or increases the frequency, rate or extent of monocyte production. This process can constitute the course of severe COVID-19. Th1 cells recruit macrophages by two mechanisms. First, they make IL-3 and GM-CSF, which stimulates the production of new monocytes in the bone marrow. Second, TNF-a and lymphotoxin secreted by Th1 Cells at the sites of infection change the syrface of endotherial cells so that monocytes adhere to them. Th1 cells recruit macrophages by two mechanisms. First, they make IL-3 and GM-CSF, which stimulates the production of new monocytes in the bone marrow. Second, TNF-a and lymphotoxin secreted by Th1 Cells at the sites of infection change the syrface of endotherial cells so that monocytes adhere to them. positive regulation of monocyte production HOIP_0039334 Th1 cells recruit macrophages by two mechanisms. First, they make IL-3 and GM-CSF, which stimulates the production of new monocytes in the bone marrow. Second, TNF-a and lymphotoxin secreted by Th1 Cells at the sites of infection change the syrface of endotherial cells so that monocytes adhere to them. ISBN10:0815345518 HOIP:HOIP_0039335 Loss of vessel barrier integrity is a subtype of loss of function (process): A process that results in no longer having a loss of vessel barrier integrity function or the process that gradually loses it. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 loss of vessel barrier integrity in severe COVID-19 HOIP_0039335 PMID:33077917 Mounting evidence suggests that loss of vessel barrier integrity and the development of a pro-coagulative endothelium contributes to the initiation and propagation of ARDS in COVID-19, by inducing endotheliitis and mediating inflammatory cell infiltration in the lungs. Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0039336 The appearance of GM-CSF (granulocyte macrophage colony-stimulating factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 granulocyte macrophage colony-stimulating factor production GM-CSF production (very high) in severe COVID-19 HOIP_0039336 PMID:32629875 These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. GM-CSF, often abnormally elevated in plasma of severe COVID-19 patients, likely is a main contributor to this pathology, as GM-CSF promotes hematopoietic stem/progenitor cell differentiation into monocytes in the bone marrow, their release into the circulation and their activation. HOIP:HOIP_0039337 A process that emits blood. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33077917 PMID:33214651 hemorrhage bleeding in severe COVID-19 HOIP_0039337 PMID:32629875 As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. Also, among patients who died with COVID-19, 71% met the International Society on Thrombosis and Haemostasis criteria for disseminated intravascular coagulation (DIC), compared to only 0.6% of the survivors. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. PMID:33214651 Coronavirus disease 2019 (COVID-19) through either direct actions on platelets and the endothelium or indirect effects through inflammation and coagulopathy can lead to increased thrombus formation and to emboli and haemorrhage. HOIP:HOIP_0039338 Negative regulation of response to anticoagulant is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of response to anticoagulant. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 negative regulation of blood anticoagulantion in severe COVID-19 HOIP_0039338 PMID:33077917 Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. HOIP:HOIP_0039341 Any process that contributes to cytokine production by a T-helper 1 cell. This process can constitute the course of severe COVID-19. Th1 cells recruit macrophages by two mechanisms. First, they make IL-3 and GM-CSF, which stimulates the production of new monocytes in the bone marrow. Second, TNF-a and lymphotoxin secreted by Th1 Cells at the sites of infection change the syrface of endotherial cells so that monocytes adhere to them. Th1 cells recruit macrophages by two mechanisms. First, they make IL-3 and GM-CSF, which stimulates the production of new monocytes in the bone marrow. Second, TNF-a and lymphotoxin secreted by Th1 Cells at the sites of infection change the syrface of endotherial cells so that monocytes adhere to them. T-helper 1 cell cytokine production in severe COVID-19 HOIP_0039341 Th1 cells recruit macrophages by two mechanisms. First, they make IL-3 and GM-CSF, which stimulates the production of new monocytes in the bone marrow. Second, TNF-a and lymphotoxin secreted by Th1 Cells at the sites of infection change the syrface of endotherial cells so that monocytes adhere to them. ISBN10: 0815345518 HOIP:HOIP_0039342 A role played by the entity that activates the activity of macrophages. macrophage chemotaxis activator role HOIP_0039342 HOIP:HOIP_0039343 Negative regulation of response to anticoagulant is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of response to anticoagulant. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 Wikipedia:Endothelium negative regulation of blood anticoagulantion in COVID-19 HOIP_0039343 PMID:33077917 Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. Wikipedia:Endothelium Blood clotting (thrombosis and fibrinolysis). The endothelium normally provides a surface on which blood does not clot, because it contains and expresses substances that prevent clotting, including heparan sulfate which acts as a cofactor for activating antithrombin, a protease that inactivates several factors in the coagulation cascade. HOIP:HOIP_0039344 Negative regulation of response to anticoagulant is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of response to anticoagulant. negative regulation of blood anticoagulantion HOIP_0039344 HOIP:HOIP_0039345 An agent that inhibits the production and release of interferons. interferon inhibitor HOIP_0039345 HOIP:HOIP_0039346 Negative regulation of early INFB1 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFNB1 gene expression in the eraly stage of the infection. PMID:32726803 negative regulation of early INFB1 expression (very high) in severe COVID-19 HOIP_0039346 PMID:32726803 Expression of SCoV2-PLpro more effectively decreased the activation of the IFNB1 promoter compared with SCoV-PLpro following poly(I:C) treatment. HOIP:HOIP_0039347 The regulated release of inflammatory mediators from tissue-resident immune cells. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation release of inflammatory mediator from tissue-resident immune cells (very high) in severe COVID-19 HOIP_0039347 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039348 The migration of an inflamamtory cell from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation inflamamtory cell extravasation in coronavirus infection HOIP_0039348 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039349 The migration of an inflamamtory cell from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation inflamamtory cell extravasation in COVID-19 HOIP_0039349 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039350 Receiving pathogen signal in antigen receptor-mediated signalng pathway is a subtype of receiving signal: A process that recognizes antigen and changes into a signal in a antigen receptor-mediated signaling pathway. receiving viral signal in antigen receptor-mediated signalng pathway HOIP_0039350 HOIP:HOIP_0039351 Receiving pathogen signal in antigen receptor-mediated signalng pathway is a subtype of receiving signal: A process that recognizes antigen and changes into a signal in a antigen receptor-mediated signaling pathway. This process can constitute the course of COVID-19. receiving viral signal in antigen receptor-mediated signalng pathway in COVID-19 HOIP_0039351 HOIP:HOIP_0039352 Receiving pathogen signal in antigen receptor-mediated signalng pathway is a subtype of receiving signal: A process that recognizes antigen and changes into a signal in a antigen receptor-mediated signaling pathway. This process can constitute the course of coronavirus infectious disease. receiving viral signal in antigen receptor-mediated signalng pathway in coronavirus infection HOIP_0039352 HOIP:HOIP_0039353 Receiving pathogen signal in pattern recognition receptor signaling pathway is a subtype of receiving signal: A process that recognizes the pathogen-associated molecular pattern (PAMPs) and changes into a signal in a pattern recognition receptor signaling pathway. receiving pathogen signal in pattern recognition receptor signaling pathway HOIP_0039353 HOIP:HOIP_0039354 Receiving signal in pattern recognition receptor signaling pathway is a subtype of receiving signal: A process that recognizes the pathogen-associated molecular pattern (PAMPs) and changes into a signal in a pattern recognition receptor signaling pathway. This process can constitute the course of coronavirus infectious disease. receiving viral signal in pattern recognition signaling pathway in coronavirus infection HOIP_0039354 HOIP:HOIP_0039355 Receiving signal in pattern recognition receptor signaling pathway is a subtype of receiving signal: A process that recognizes the pathogen-associated molecular pattern (PAMPs) and changes into a signal in a pattern recognition receptor signaling pathway. This process can constitute the course of COVID-19. receiving viral signal in pattern recognition signaling pathway in COVID-19 HOIP_0039355 HOIP:HOIP_0039356 Biochemical degradation manner is a subtype of manner: A manner that biochemically decomposes a single chemical entity into multiple elements biochemical degradation manner HOIP_0039356 HOIP:HOIP_0039357 Any process that stops, prevents, or reduces the frequency, rate or extent of blood coagulation. negative regulation of blood coagulation HOIP_0039357 HOIP:HOIP_0039358 Negative regulation of response to anticoagulant is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of response to anticoagulant. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). negative regulation of blood anticoagulantion in COVID-19 associated with ARDS HOIP_0039358 HOIP:HOIP_0039359 Negative regulation of nitric oxide synthase activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of nitric oxide synthase activation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection Negative regulation of nitric oxide synthase activation in severe COVID-19 HOIP_0039359 Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection PMID:33077917 HOIP:HOIP_0039360 Reduced oxygenation of body tissues resulting in the decreased pressure of this component of body gases; commonly due to hypoxemia This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32651579 hypoxia (very high) in severe COVID-19 HOIP_0039360 PMID:32629875 However, a study in twelve patients with COVID-19 reported significantly increased plasma levels of angiotensin II, which appeared to directly correlate with circulating SARS-CoV-2 RNA levels and degree of hypoxia. As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. PMID:32651579 Hyperinflammation seen with cytokine storm and hypoxia-associated metabolic derangements are other potential mechanisms of liver damage. HOIP:HOIP_0039361 Dysregulation of metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of metabolism appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 malfunctioning of metabolism in severe COVID-19 HOIP_0039361 PMID:32651579 Hyperinflammation seen with cytokine storm and hypoxia-associated metabolic derangements are other potential mechanisms of liver damage. HOIP:HOIP_0039362 Liver damage is a subtype of damaging: A process that injuries the structure of the liver as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 liver damage in COVID-19 in liver HOIP_0039362 PMID:32651579 Hyperinflammation seen with cytokine storm and hypoxia-associated metabolic derangements are other potential mechanisms of liver damage. Other histopathologic changes in the liver included hepatic steatosis, portal fibrosis, lymphocytic infiltrates and ductular proliferation, lobular cholestasis, and acute liver-cell necrosis, together with central-vein thrombosis. HOIP:HOIP_0039363 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral entry into host cell (very high) in severe COVID-19 SARS-CoV-2 entry to host cell (very high) in severe COVID-19 HOIP_0039363 HOIP:HOIP_0039364 Viral entry-innate immune response imbalance is a subtype of stress response imbalance: A process that lacks a balance between the viral entry and the innate immune response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral entry-innate immune response imbalance in severe COVID-19 HOIP_0039364 HOIP:HOIP_0039365 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32843733 establishment of virus infection (very high) in severe COVID-19 HOIP_0039365 PMID:32843733 If the protective immune response is impaired, the virus is allowed to replicate and can cause widespread tissue damage. The lungs seem to be the main target, although other organs with high ACE2 expression, such as the intestine, heart, brain and kidney, might also be vulnerable. HOIP:HOIP_0039366 Fusion binding manner is a subtype of manner: A manner of a union by or as if by fusion. fusion binding manner HOIP_0039366 HOIP:HOIP_0039367 Binding manner is a subtype of manner: A manner of a union. binding manner HOIP_0039367 HOIP:HOIP_0039368 Any process that stops, prevents or reduces the frequency, rate or extent of cytokine production involved in inflammatory response. This process can constitute the course of COVID-19 drug treatment. PMID:33992179 https://clinicaltrials.gov/ct2/show/NCT04342663/ negative regulation of cytokine production involved in inflammatory response in COVID-19 drug treatment HOIP_0039368 PMID:33992179 Among all SSRI drugs, fluoxetine show a promising drug against COVID-19 by reducing the secretion of pro-inflammatory chemokine/cytokines (such as IL-6, TNF-α, CCL-2) and modulating immune system responsiveness to infection. HOIP:HOIP_0039369 A viral transcription process that produces the npositive stranded (+) mRNA for a new generation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33116300 Viral genomic replication is initiated by the synthesis of full-length negative-sense genomic copies, which function as templates for the generation of new positive-sense genomic RNA. positive stranded viral mRNA biosynthetic process Coronavirus is a single (+) strand RNA virus. Single (+)-strand RNA viruses initially use the (+)-strand genome to the (-) strand as a template to generate next-generation +-strand mRNA. next generation of positive stranded viral mRNA replication in coronavirus infection HOIP_0039369 PMID:33116300 Viral genomic replication is initiated by the synthesis of full-length negative-sense genomic copies, which function as templates for the generation of new positive-sense genomic RNA. HOIP:HOIP_0039370 The transport of a virus between adjacent cells in a multicellular organism. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:32362314 PMID:32629875 VZ:1018 cell to cell spread of virus within host intercellular virus transport transport of virus in host (cell to cell) HOIP_0039370 PMID:32362314 Finally, the addition of an arginine residue to the S1/S2 site of SARS-2-S jointly with alanine-to-lysine exchange strongly increased syncytium formation, indicating that viral variants with optimized S1/S2 sites might show augmented cell-cell spread and potentially altered pathogenicity. PMID:32629875 Epidemiologic evidence indicates that the virus is transmitted among close contacts mostly through the respiratory route, presumably directly through infected droplet secretions or indirectly via fomites (Figure 2). The proximity between the infected respiratory epithelium releasing the virus and endothelial cells may favor local transmission. HOIP:HOIP_0039371 Ligand-receptor binding manner is a subtype of binding manner: A manner of a union by holding between a receptor and a chemical entity, typically a small molecule or peptide, which binds the receptor and regulates its effector function. ligand-receptor binding manner HOIP_0039371 HOIP:HOIP_0039372 Positive regulation of an adaptive immune response mediated via cytokine production by helper T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. helper T cell enhancement of adaptive immune respons in COVID-19 HOIP_0039372 HOIP:HOIP_0039373 The cleavage of a peptide bond or bonds within a viral polyprotein. PMID:26868298 viral polyprotein processing [coronavirus infectious disease]2 HOIP_0039373 PMID:26868298 The large replicase polyprotein 1a (pp1a) and pp1ab, which are encoded by the 5'-terminal open reading frame 1a/b (ORF1a/b), are cleaved by two viral proteases, the papain-like protease (PLpro) and the 3C-like protease (3CLpro), to produce non-structural proteins (NSPs) such as RNA-dependent RNA polymerase (RdRp) and helicase, which are involved in the transcription and replication of the virus. HOIP:HOIP_0039374 The process in which a relatively unspecialized thymocyte acquires specialized features of a T-helper cell. This process can constitute the course of COVID-19. Helper T cells exist in two broad classes. T cells (Th1) are associated with the cell-killing and inflammatory responses of the immune system, including an important role of the activation of macrophages. Th2 cells activate B cells and the general serological (antibody) response. T-helper cell differentiation in COVID-19 HOIP_0039374 HOIP:HOIP_0039375 A protein that is a translation product of the S gene in Betacoronavirus. S glycoprotein (Betacoronavirus) surface glycoprotein (Betacoronavirus) S protein (Betacoronavirus) spike glycoprotein (Betacoronacirus) HOIP_0039375 HOIP:HOIP_0039377 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This process can constitute the course of coronavirus infectious disease. viral entry into host cell via vesicle-transport in coronavirus infection HOIP_0039377 HOIP:HOIP_0039378 Vesicle-mediated transport manner is a subtype of transporting manner: A manner of a transport by holding an entity in a vesicle. vesicle-mediated transport manner HOIP_0039378 HOIP:HOIP_0039379 Transport manner is a subtype of manner: A manner of transferring from one region to another. transport manner HOIP_0039379 HOIP:HOIP_0039380 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This process can constitute the course of coronavirus infectious disease. direct viral entry into host cell via cell surface membrane fusion in coronavirus infection HOIP_0039380 HOIP:HOIP_0039383 Viral protein production is a subtype of protein production: A process that produces a virus protein as an output. viral protein production HOIP_0039383 HOIP:HOIP_0039387 Viral protein production is a subtype of protein production: A process that produces a virus protein as an output. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious course. viral protein production in coronavirus infection HOIP_0039387 HOIP:HOIP_0039388 Viral protein production is a subtype of protein production: A process that produces a virus protein as an output. This entity is a specific course-dependent process. This process can constitute the course of COVId-19. viral protein production in COVID-19 HOIP_0039388 HOIP:HOIP_0039389 Viral protein production is a subtype of protein production: A process that produces a virus protein as an output. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral protein production (very high) in severe COVID-19 HOIP_0039389 HOIP:HOIP_0039390 Viral structural protein production is a subtype of protein production: A process that produces a virus structural protein as an output. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious course. PMID:33116300 viral structural protein production in coronavirus infection HOIP_0039390 PMID:33116300 The coronavirus virion consists of structural proteins, namely spike (S), envelope (E), membrane (M), nucleocapsid (N) and, for some betacoronaviruses, haemagglutinin-esterase (not shown). The positive-sense, single-stranded RNA genome (+ssRNA) is encapsidated by N, whereas M and E ensure its incorporation in the viral particle during the assembly process. S trimers protrude from the host-derived viral envelope and provide specificity for cellular entry receptors. HOIP:HOIP_0039391 Viral structural protein production is a subtype of protein production: A process that produces a virus structural protein as an output. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. viral structural protein production in COVID-19 HOIP_0039391 HOIP:HOIP_0039392 Viral structural protein production is a subtype of protein production: A process that produces a virus structural protein as an output. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral structural protein production in severe COVID-19 HOIP_0039392 HOIP:HOIP_0039393 A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral assembly viral particle assembly virion assembly and maintenance virion organization virus assembly virus particle assembly virion assembly (very high) in severe COVID-19 HOIP_0039393 HOIP:HOIP_0039395 A role of receptor protein that is localized to the plasma membrane. cell surface receptor role HOIP_0039395 HOIP:HOIP_0039396 The appearance of IgA antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32398307 PMID:33077917 IgA antibody production in severe COVID-19 HOIP_0039396 PMID:32398307 Considering the roles of mucosal and systemic IgA in COVID-19, inducing IgA production (using lactoferrin to activate canonical TGF-β signalling or retinoic acid to enhance lactoferrin-induced IgA responses) has been proposed as a novel therapy for severe COVID-19. However, as highlighted by our study, enhanced IgA responses observed in severe COVID-19 might confer damaging effects in severe COVID-19. As a result, we hypothesise that severe COVID-19 might be at least in part an IgA-mediated disease (related to IgA deposition and vasculitis), which helps to explain common organ injuries in COVID-19, e.g. acute pulmonary embolism, kidney injury, etc. PMID:33077917 Relative levels of IgA and IgG have also been demonstrated to be markedly higher in severely ill patients with COVID-19 than in patients with milder disease, suggesting that IgA may have synergistic effects with IgG in promoting antibody-dependent cellular cytotoxicity and COVID-19 exacerbation. These researchers also proposed that COVID-19 might be at least in part an IgA-mediated disease, possibly inducing a vasculitis phenotype via classical pathway-mediated cytotoxicity. HOIP:HOIP_0039397 The external part of the cell wall and/or plasma membrane. cell surface HOIP_0039397 HOIP:HOIP_0039398 Changing viral spike S protein S2 domain structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein S2 domain. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33123165 changing viral spike S2 protein conformation changing viral spike S2 protein structure in coronavirus infection HOIP_0039398 PMID:33123165 The virus receptor, angiotensin-converting enzyme 2 (ACE2), expressed on the surface of multiple human cells is engaged via the receptor binding domain (RBD), which is part of the S1 subunit of the S glycoprotein. Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039400 Changing viral spike S protein S2 domain structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein S2 domain. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33123165 changing viral spike S2 protein conformation changing viral spike S2 protein structure 2 in coronavirus infection HOIP_0039400 PMID:33123165 The virus receptor, angiotensin-converting enzyme 2 (ACE2), expressed on the surface of multiple human cells is engaged via the receptor binding domain (RBD), which is part of the S1 subunit of the S glycoprotein. Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039401 Cleavage of viral spike protein S is a subtype of proteolysis: A process in which viral spike protein S is cleaved. This process can constitute the course of coronavirus infectious disease. PMID:32641482 PMID:33116300 cleavage of viral spike S protein 2 in coronavirus infection HOIP_0039401 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. PMID:33116300 Coronavirus particles bind to cellular attachment factors and specific S interactions with the cellular receptors (such as angiotensin-converting enzyme 2 (ACE2)), together with host factors (such as the cell surface serine protease TMPRSS2), promote viral uptake and fusion at the cellular or endosomal membrane. SARS-CoV has been shown to use the cell-surface serine protease TMPRSS2 for priming and entry, although the endosomal cysteine proteases cathepsin B (CatB) and CatL can also assist in this proces. HOIP:HOIP_0039402 Cleavage of viral spike protein S is a subtype of proteolysis: A process in which viral spike protein S is cleaved. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32142651 cleavage of viral spike S protein (very low) 2 in COVID-19 drug treatment HOIP_0039402 PMID:32142651 Ammonium chloride treatment strongly inhibited SARS-2-S- and SARS-S-driven entry into TMPRSS2 293T cells (Figure S3 A), suggesting CatB/L dependence. Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. Indeed, camostat mesylate significantly reduced MERS-S-, SARS-S-, and SARS-2-S- but not VSV-G-driven entry into the lung cell line Calu-3 (Figure 4C) and exerted no unwanted cytotoxic effects (Figure S3 C). HOIP:HOIP_0039403 Cleavage of viral spike protein S is a subtype of proteolysis: A process in which viral spike protein S is cleaved. This process can constitute the course of COVID-19. PMID:32142651 PMID:32221306 PMID:32361028 PMID:32362314 PMID:32404436 PMID:33123165 cleavage of viral spike S protein 2 in COVID-19 HOIP_0039403 PMID:32142651 Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases. Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. PMID:32221306 While cathepsin B inhibitor treatment did not show any marked effect on virus entry, cathepsin L inhibition treatment decreased entry of SARS-CoV-2 S pseudovirions into 293/hACE2 by over 76% (Fig. 4a), suggesting that cathepsin L should be essential for priming of SARS-CoV-2 S protein in lysosome for entry into 293/hACE2 cells. PMID:32361028 SARS-Cov-2 entry into a cell is dependent upon binding of the viral spike (S) protein to cellular receptor and on cleavage of the spike protein by the host cell proteases such as Cathepsin L and Cathepsin B. PMID:32362314 Furin Cleaves the SARS-CoV-2 Spike Protein at the S1/ S2 Site, and Cleavage Is Required for Efficient Cell-Cell Fusion SARS-2-S expression triggered syncytium formation that was strongly increased by trypsin and TMPRSS2. PMID:32404436 Following receptor engagement, SARS-CoV-2 S is processed by a plasma membrane-associated type II transmembrane serine protease, TMPRSS2, prior to membrane fusion which is essential to release the viral contents into the host cell cytosol (3, 6). Here, we present evidence that SARS-CoV-2 infects human mature enterocytes from the apical surface and triggers epithelial cell fusion. TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion. PMID:33123165 Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039404 Changing viral spike S protein S2 domain structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein S2 domain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 changing viral spike S2 protein conformation changing viral spike S2 protein structure 2 in COVID-19 HOIP_0039404 PMID:33123165 The virus receptor, angiotensin-converting enzyme 2 (ACE2), expressed on the surface of multiple human cells is engaged via the receptor binding domain (RBD), which is part of the S1 subunit of the S glycoprotein. Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039406 Fusion peptide insert into host cell memnrane is a subtype of moving A to the inside of B: A process that of the fusion peptide insertion into the host cell membrane. Activated s2 protein inserts the fusion peptide into the target host cell membrane, which causes S2 structural change and membrane fusion. fusion peptide insert into host cell memnrane HOIP_0039406 HOIP:HOIP_0039407 Fusion peptide insert into host cell memnrane is a subtype of moving A to the inside of B: A process that of the fusion peptide insertion into the host cell membrane. This process can constitute the course of coronavirus infectious disease. Activated s2 protein inserts the fusion peptide into the target host cell membrane, which causes S2 structural change and membrane fusion. fusion peptide insert into host cell memnrane in coronavirus infection HOIP_0039407 HOIP:HOIP_0039408 A spike glycoprotein, signal peptide that has been processed by proteolytic cleavage to yield the C-terminal portion. S2 (Betacoronavirus) spike protein S2 (Betacoronavirus) HOIP_0039408 HOIP:HOIP_0039410 Fusion peptide insert into host cell memnrane is a subtype of moving A to the inside of B: A process that of the fusion peptide insertion into the host cell membrane. This process can constitute the course of COVID-19. Activated s2 protein inserts the fusion peptide into the target host cell membrane, which causes S2 structural change and membrane fusion. fusion peptide insert into host cell memnrane in COVID-19 HOIP_0039410 HOIP:HOIP_0039411 The directed killing of adjacent infected cells by a neutrophil. This process can constitute the course of severe COVID-19. PMID:28792873 neutrophil mediated cytotoxicity to adjacent infected cells in severe COVID-19 HOIP_0039411 HOIP:HOIP_0039412 Inflammation-anti-inflammation imbalance is a subtype of imbalance: A process that lacks a balance between the inflammatory response and the anti-inflammatory response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. inflammation-anti-inflammation imbalance in COVID-19 HOIP_0039412 HOIP:HOIP_0039413 Changing viral inflammation-anti-inflammation balance is a subtype of changing balance: A process that changes the state of inflammation-anti-inflammation balance within an host organ or an organism. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. changing viral inflammation-anti-inflammation balance in coronavirus infection HOIP_0039413 HOIP:HOIP_0039414 Changing viral inflammation-anti-inflammation balance is a subtype of changing balance: A process that changes the state of inflammation-anti-inflammation balance within an host organ or an organism. changing viral inflammation-anti-inflammation balance HOIP_0039414 HOIP:HOIP_0039415 The directed killing of adjacent infected cells by a neutrophil. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:28792873 neutrophil mediated cytotoxicity to adjacent infected cells in COVID-19 associated with ARDS HOIP_0039415 HOIP:HOIP_0039416 The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. This process can constitute the course of coronavirus infectious disease. apoptotic cell removal apoptotic cell clearance in coronavirus infection HOIP_0039416 The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. PMID:14685684 HOIP:HOIP_0039417 The appearance of IgG antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 delayed type IgG antibody production in severe COVID-19 HOIP_0039417 PMID:33077917 Relative levels of IgA and IgG have also been demonstrated to be markedly higher in severely ill patients with COVID-19 than in patients with milder disease, suggesting that IgA may have synergistic effects with IgG in promoting antibody-dependent cellular cytotoxicity and COVID-19 exacerbation. HOIP:HOIP_0039418 An delayed type immune response mediated by immunoglobulins, whether cell-bound or in solution. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 delayed immunoglobulin mediated immune response in severe COVID-19 HOIP_0039418 PMID:33077917 Relative levels of IgA and IgG have also been demonstrated to be markedly higher in severely ill patients with COVID-19 than in patients with milder disease, suggesting that IgA may have synergistic effects with IgG in promoting antibody-dependent cellular cytotoxicity and COVID-19 exacerbation. HOIP:HOIP_0039419 Cytolysis of target cells by natural killer cells, eosinophils, neutrophils, monocytes, or macrophages following engagement of antibodies bound to the target cells by Fc receptors on the effector cells. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 antibody-dependent cellular cytotoxicity (very high) in severe COVID-19 HOIP_0039419 PMID:33077917 Relative levels of IgA and IgG have also been demonstrated to be markedly higher in severely ill patients with COVID-19 than in patients with milder disease, suggesting that IgA may have synergistic effects with IgG in promoting antibody-dependent cellular cytotoxicity and COVID-19 exacerbation. HOIP:HOIP_0039420 adaptive immune response An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). This process can constitute the course of severe COVID-19. adaptive immune response in severe COVID-19 HOIP_0039420 HOIP:HOIP_0039421 The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 T cell mediated cytotoxicity (very high) in severe COVID-19 HOIP_0039421 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039422 The change in morphology and behavior of a T helper 2 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33123165 T-helper 2 cell activation in coronavirus infection HOIP_0039422 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0039423 The change in morphology and behavior of a mature or immature B cell during an immune response, resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. B cell activation involved in adaptive immune response in coronavirus infection HOIP_0039423 HOIP:HOIP_0039424 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class II. positive regulation of MHC class II biosynthetic process HOIP_0039424 HOIP:HOIP_0039425 The process in which a relatively unspecialized T cell acquires specialized features of a cytotoxic T cell. This process can constitute the course of coronavirus infectious disease. cytotoxic T cell differentiation in coronavirus infection HOIP_0039425 HOIP:HOIP_0039426 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class II. This process can constitute the course of coronavirus infectious disease. positive regulation of MHC class II biosynthetic process in coronavirus infection HOIP_0039426 HOIP:HOIP_0039427 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class II. This process can constitute the course of COVID-19. positive regulation of MHC class II biosynthetic process in COVID-19 HOIP_0039427 HOIP:HOIP_0039428 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class II. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. positive regulation of MHC class II biosynthetic process in mild COVID-19 HOIP_0039428 HOIP:HOIP_0039429 Any process that contributes to cytokine production by a T-helper 2 cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). T-helper 2 cell cytokine production in COVID-19 (homeostatic balance) HOIP_0039429 HOIP:HOIP_0039430 The process in which a macrophage expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. This process can constitute the course of coronavirus infectious disease. macrophage antigen presentationin coronavirus infection HOIP_0039430 HOIP:HOIP_0039431 The change in morphology and behavior of a mature or immature cytotoxic T cell resulting from exposure to an antigen for which its T cell receptor is specific bound to an MHC molecule on an antigen presenting cell, leading to the initiation or perpetuation of an immune response. This process can constitute the course of coronavirus infectious disease. Cytotoxic T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell in coronavirus infection HOIP_0039431 HOIP:HOIP_0039432 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a cytotoxic T cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33123165 cytotoxic T cell degranulation in coronavirus infection HOIP_0039432 PMID:33123165 Processing and presentation of SARS-CoV-2 epitopes by antigen presenting cells (APCs) via human leukocyte antigen (HLA) class I leads to activation of naïve CD8+ T cells which differentiate into cytolytic effectors (cytotoxic T lymphocytes [CTL]) that kill virus-infected cells. HOIP:HOIP_0039433 The process in which a relatively unspecialized thymocyte acquires specialized features of a T-helper cell. This process can constitute the course of coronavirus infectious disease. Helper T cells exist in two broad classes. T cells (Th1) are associated with the cell-killing and inflammatory responses of the immune system, including an important role of the activation of macrophages. Th2 cells activate B cells and the general serological (antibody) response. T-helper cell differentiation in coronavirus infection HOIP_0039433 HOIP:HOIP_0039434 Any process involved with the carrying out of an immune response by a B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:33123165 B cell mediated immunity in COVID-19 vaccination HOIP_0039434 PMID:33123165 Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0039435 The appearance of immunoglobulin due to biosynthesis or secretion following a cellular stimulus during an immune response, resulting in an increase in its intracellular or extracellular levels. immunoglobulin production involved in immunoglobulin-mediated immune response HOIP_0039435 HOIP:HOIP_0039436 The inhibition of an antigen's biological effects by antibody binding to it. An example is neutralization of diphtheria toxin by preventing its entry into human cells via the binding of antibody specific for diphtheria toxin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. immunoglobulin-mediated neutralization in COVID-19 HOIP_0039436 HOIP:HOIP_0039437 The inhibition of an antigen's biological effects by antibody binding to it. An example is neutralization of diphtheria toxin by preventing its entry into human cells via the binding of antibody specific for diphtheria toxin. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. immunoglobulin-mediated neutralization in coronavirus infection HOIP_0039437 HOIP:HOIP_0039438 The change in morphology and behavior of a mature or immature B cell during an immune response, resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. B cell activation involved in adaptive immune response in COVID-19 HOIP_0039438 HOIP:HOIP_0039439 The change in morphology and behavior of a T helper 2 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 T-helper 2 cell activation in COVID-19 HOIP_0039439 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0039440 T cell mediated removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue by T cell in the adaptive immune response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T cell mediated removing infected cell in coronavirus infection HOIP_0039440 HOIP:HOIP_0039441 Any process that stops, prevents, or reduces the frequency, rate or extent of the viral action. negative regulation of viral action HOIP_0039441 HOIP:HOIP_0039442 Any process that stops, prevents, or reduces the frequency, rate or extent of the viral action. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. negative regulation of viral action in coronavirus infection HOIP_0039442 HOIP:HOIP_0039443 Any process that stops, prevents, or reduces the frequency, rate or extent of the viral action. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. negative regulation of viral action in COVID-19 HOIP_0039443 HOIP:HOIP_0039444 Any process that stops, prevents, or reduces the frequency, rate or extent of the viral action. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is very low. negative regulation of viral action (very low) in severe COVID-19 HOIP_0039444 HOIP:HOIP_0039445 Any process involved with the carrying out of an immune response by a B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 B cell mediated immunity in COVID-19 HOIP_0039445 PMID:33123165 Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0039446 Any process involved with the carrying out of an immune response by a B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33123165 B cell mediated immunity in coronavirus infection HOIP_0039446 PMID:33123165 Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0039447 Any process that contributes to cytokine production by a T cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T cell cytokine production in coronavirus infection HOIP_0039447 HOIP:HOIP_0039448 Any process that contributes to cytokine production by a T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. T cell cytokine production in COVID-19 HOIP_0039448 HOIP:HOIP_0039449 The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T cell activation in coronavirus infection HOIP_0039449 HOIP:HOIP_0039450 The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. T cell activation in COVID-19 HOIP_0039450 HOIP:HOIP_0039451 The change in morphology and behavior of a cytotoxic T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. cytotoxic T cell degranulation in coronavirus infection HOIP_0039451 HOIP:HOIP_0039452 The change in morphology and behavior of a cytotoxic T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. cytotoxic T cell activation HOIP_0039452 HOIP:HOIP_0039453 The change in morphology and behavior of a cytotoxic T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19.. cytotoxic T cell activation in COVID-19 HOIP_0039453 HOIP:HOIP_0039454 Accumulation of abnormal proteins is a subtype of protein accumulation: A process that keeps Angiotensin II in a biological object. This process can constitute the course of severe COVID-19. PMID:32264791 PMID:32629875 Angiotensin II accumulation (very high) in severe COVID-19 HOIP_0039454 PMID:32264791 Ang II levels also further increases ADAM17 activity. ADAM17 correspondingly also cleaves its primary substrate releasing soluble TNF-α (tumor necrosis factor-α) into the extracellular region where it has auto- and paracrine functionality. TNF-α activation of its tumor necrosis factor receptor (TNFR) represents a third pathway elevating ADAM17 activity. TNF-α along with systemic cytokines released due to SARS-CoV-2 infection and in conjunction with comorbidities such as diabetes mellitus and hypertension can lead to a cytokine storm. TMPRSS2 indicates transmembrane protease serine 2. PMID:32264791 Ang II levels elevate with increased activity of angiotensin 1 receptors (AT1R) at the cost of ACE2/ Ang 1–7 driven pathways leading to adverse fibrosis, hypertrophy, increased reactive oxygen species (ROS), vasoconstriction, and gut dysbiosis. PMID:32629875 However, a study in twelve patients with COVID-19 reported significantly increased plasma levels of angiotensin II, which appeared to directly correlate with circulating SARS-CoV-2 RNA levels and degree of hypoxia. HOIP:HOIP_0039455 An immune response directed against a previously encountered antigen, being quicker and quantitatively better compared with the primary response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. adaptive immune memory response in coronavirus infection HOIP_0039455 HOIP:HOIP_0039456 An immune response directed against a previously encountered antigen, being quicker and quantitatively better compared with the primary response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. adaptive immune memory response in COVID-19 HOIP_0039456 HOIP:HOIP_0039457 A memory B cell is a mature B cell that is long-lived, readily activated upon re-encounter of its antigenic determinant, and has been selected for expression of higher affinity immunoglobulin. This cell type has the phenotype CD19-positive, CD20-positive, MHC Class II-positive, and CD138-negative. memory B cell HOIP_0039457 HOIP:HOIP_0039458 Any process that activates or increases the frequency, rate or extent of platelet aggregation. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules. This process can constitute the course of severe COVID-19. positive regulation of platelet aggregation (very high) in severe COVID-19 HOIP_0039458 HOIP:HOIP_0039462 A role played by an entity that regulates an immune memory. immune memory regulator role HOIP_0039462 HOIP:HOIP_0039463 A role played by the entity which regulates the process of infmammatory response. regulator of inflammatory response HOIP_0039463 HOIP:HOIP_0039465 An immune response mediated through cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. cellular immune response in COVID-19 HOIP_0039465 HOIP:HOIP_0039466 An immune response mediated through cells. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. cellular immune response in coronavirus infection HOIP_0039466 HOIP:HOIP_0039467 An immune response mediated through a body fluid. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. humoral immune response in COVID-19 HOIP_0039467 HOIP:HOIP_0039468 An immune response mediated through a body fluid. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. humoral immune response in coronavirus infection HOIP_0039468 HOIP:HOIP_0039469 Interaction between host pattern recognition receptor and any PAMPs (pathogen-associated molecular patterns). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. binding of pattern recognition receptor to PAMPs in severe COVID-19 HOIP_0039469 HOIP:HOIP_0039470 An immune response which is associated with resistance to extracellular organisms such as helminths and pathological conditions such as allergy, which is orchestrated by the production of particular cytokines, most notably IL-4, IL-5, IL-10, and IL-13, by any of a variety of cell types including T-helper 2 cells, eosinophils, basophils, mast cells, and nuocytes, resulting in enhanced production of certain antibody isotypes and other effects. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T-helper 2 type immune response in coronavirus infection HOIP_0039470 HOIP:HOIP_0039471 adaptive immune response An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). This process can constitute the course of coronavirus infectious disease. adaptive immune response in coronavirus infection HOIP_0039471 HOIP:HOIP_0039472 An immune response which is associated with resistance to extracellular organisms such as helminths and pathological conditions such as allergy, which is orchestrated by the production of particular cytokines, most notably IL-4, IL-5, IL-10, and IL-13, by any of a variety of cell types including T-helper 2 cells, eosinophils, basophils, mast cells, and nuocytes, resulting in enhanced production of certain antibody isotypes and other effects. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. T-helper 2 type immune response in COVID-19 HOIP_0039472 HOIP:HOIP_0039473 Positive regulation of an adaptive immune response mediated via cytokine production by helper T cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. helper T cell enhancement of adaptive immune respons in coronavirus infection HOIP_0039473 HOIP:HOIP_0039474 Any process that stops, prevents, or reduces the frequency, rate or extent of T-helper 2 cell activation. negative regulation of T-helper 2 cell activation HOIP_0039474 HOIP:HOIP_0039475 Any process that stops, prevents, or reduces the frequency, rate or extent of T-helper 2 cell activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Cytokines from one type of CD4 T cell inhibit the activation of the other. Thus, IL-10, a product of TH2 cells, can inhibit the development of TH1 cells by acting on the antigen-presenting cell, whereas IFN-γ, a product of TH1 cells, can prevent the activation of TH2 cells Cytokines from one type of CD4 T cell inhibit the activation of the other. Thus, IL-10, a product of TH2 cells, can inhibit the development of TH1 cells by acting on the antigen-presenting cell, whereas IFN-γ, a product of TH1 cells, can prevent the activation of TH2 cells negative regulation of type II interferon production in coronavirus infection HOIP_0039475 Cytokines from one type of CD4 T cell inhibit the activation of the other. Thus, IL-10, a product of TH2 cells, can inhibit the development of TH1 cells by acting on the antigen-presenting cell, whereas IFN-γ, a product of TH1 cells, can prevent the activation of TH2 cells https://www.ncbi.nlm.nih.gov/books/NBK27125/ HOIP:HOIP_0039476 Any process that stops, prevents, or reduces the frequency, rate or extent of T-helper 2 cell activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. This process can constitute the course of COVID-19. negative regulation of type II interferon production in COVID-19 HOIP_0039476 HOIP:HOIP_0039477 Any process that stops, prevents, or reduces the frequency, rate or extent of T-helper 1 cell activation. negative regulation of T-helper 1 cell activation HOIP_0039477 HOIP:HOIP_0039478 Any process that stops, prevents, or reduces the frequency, rate or extent of T-helper 1 cell activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Cytokines from one type of CD4 T cell inhibit the activation of the other. Thus, IL-10, a product of TH2 cells, can inhibit the development of TH1 cells by acting on the antigen-presenting cell, whereas IFN-γ, a product of TH1 cells, can prevent the activation of TH2 cells Cytokines from one type of CD4 T cell inhibit the activation of the other. Thus, IL-10, a product of TH2 cells, can inhibit the development of TH1 cells by acting on the antigen-presenting cell, whereas IFN-γ, a product of TH1 cells, can prevent the activation of TH2 cells negative regulation of T-helper 1 cell activation in coronavirus infection HOIP_0039478 Cytokines from one type of CD4 T cell inhibit the activation of the other. Thus, IL-10, a product of TH2 cells, can inhibit the development of TH1 cells by acting on the antigen-presenting cell, whereas IFN-γ, a product of TH1 cells, can prevent the activation of TH2 cells https://www.ncbi.nlm.nih.gov/books/NBK27125/ HOIP:HOIP_0039479 Any process that stops, prevents, or reduces the frequency, rate or extent of T-helper 1 cell activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. negative regulation of T-helper 1 cell activation in COVID-19 HOIP_0039479 HOIP:HOIP_0039480 The process in which a relatively unspecialized T cell acquires specialized features of a cytotoxic T cell. This process can constitute the course of COVID-19. cytotoxic T cell differentiation in COVID-19 HOIP_0039480 HOIP:HOIP_0039481 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. This process can constitute the course of coronavirus infectious disease. phagocytosis by inflammatory macrophage in coronavirus infection HOIP_0039481 HOIP:HOIP_0039482 The directed killing of a target cell by a macrophage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. inflammatory macrophage mediated cytotoxicity in coronavirus infection HOIP_0039482 HOIP:HOIP_0039483 Any process that activates or increases the frequency, rate or extent of cytotoxic T cell activation. positive regulation of cytotoxic T cell activation HOIP_0039483 HOIP:HOIP_0039484 Any process that activates or increases the frequency, rate or extent of cytotoxic T cell activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. positive regulation of cytotoxic T cell activation in coronavirus infection HOIP_0039484 HOIP:HOIP_0039485 Any process that activates or increases the frequency, rate or extent of cytotoxic T cell activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. positive regulation of cytotoxic T cell activation in COVID-19 HOIP_0039485 HOIP:HOIP_0039486 Cell killing caused by the membrane attack complex formed following complement activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. There are three pathways of complement activation: the classical pathway, which is triggered by antibody or by direct binding of complement component C1q to the pathogen surface; the MB-lectin pathway, which is triggered by mannan-binding lectin, a normal serum constituent that binds some encapsulated bacteria; and the alternative pathway, which is triggered directly on pathogen surfaces. All of these pathways generate a crucial enzymatic activity that, in turn, generates the effector molecules of complement. The three main consequences of complement activation are opsonization of pathogens, the recruitment of inflammatory cells, and direct killing of pathogens. Janeway's Immunobiology PMID:33077917 https://www.ncbi.nlm.nih.gov/books/NBK27100/ complement-dependent cytotoxicity in coronavirus infection HOIP_0039486 PMID:33077917 C3b also forms C5 convertase, which induces release of the potent anaphylatoxin C5a, as well as the fragment C5b that is responsible for the formation of the membrane attack complex C5b–9 on target cells — the terminal event of complement activation. HOIP:HOIP_0039487 The process in which a microorganism (or other particulate material) is rendered more susceptible to phagocytosis by coating with an opsonin, a blood serum protein such as a complement component or antibody. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. opsonization in coronavirus infection HOIP_0039487 HOIP:HOIP_0039488 Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33077917 complement activation in coronavirus infection HOIP_0039488 PMID:33077917 Insights into the pathogenic mechanisms underlying SARS-CoV-2 infection and COVID-19 progression are emerging and highlight the critical role of the immunological hyper-response — characterized by widespread endothelial damage, complement-induced blood clotting and systemic microangiopathy — in disease exacerbation. HOIP:HOIP_0039489 The regulated release of anaphylatoxin from a cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. release of anaphylatoxin in coronavirus infection HOIP_0039489 HOIP:HOIP_0039490 The rupture of cell membranes and the loss of cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. cytolysis in coronavirus infection HOIP_0039490 HOIP:HOIP_0039491 The rupture of cell membranes and the loss of cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. cytolysis in COVID-19 HOIP_0039491 HOIP:HOIP_0039492 The activation of the membrane attack complex components of the complement cascade which can result in death of a target cell through cytolysis. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33077917 activation of membrane attack complex in coronavirus infection HOIP_0039492 PMID:33077917 C3b also forms C5 convertase, which induces release of the potent anaphylatoxin C5a, as well as the fragment C5b that is responsible for the formation of the membrane attack complex C5b–9 on target cells — the terminal event of complement activation. HOIP:HOIP_0039493 A vesicle-mediated transport process that results in the engulfment of external particulate material by inflammatory macrophages and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. phagocytosis by inflammatory macrophagein coronavirus infection HOIP_0039493 HOIP:HOIP_0039494 A vesicle-mediated transport process that results in the engulfment of external particulate material by inflammatory macrophages and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. phagocytosis by inflammatory macrophagein COVID-19 HOIP_0039494 HOIP:HOIP_0039495 Any process that activates or increases the frequency, rate or extent of blood coagulation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. positive regulation of blood coagulation in coronavirus infection HOIP_0039495 HOIP:HOIP_0039496 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:32339221 PMID:32629875 PMID:33077917 Wikipedia:Coagulation blood clotting blood coagulationin coronavirus infection HOIP_0039496 PMID:32339221 The initial coagulopathy of COVID-19 presents with prominent elevation of D-dimer and fibrin/fibrinogen-degradation products, whereas abnormalities in prothrombin time, partial thromboplastin time, and platelet counts are relatively uncommon in initial presentations. Coagulation test screening, including the measurement of D-dimer and fibrinogen levels, is suggested. PMID:32629875 Since soluble IL-6R is abnormally elevated in the plasma of COVID-19 patients, presumably secondary to cleavage from the cells surface by TACE/ADAM17 upon SARS-CoV-2 infection and the inflammatory response associated with COVID-19, IL-6 can activate most cells, including endothelial cells, which do not express endogenous IL-6R but can be activated by the complex of soluble IL-6R and IL-6. In COVID-19, adding to the blood clotting risk from increased IL-6, SARS-CoV-2 can infect, replicate and induce endothelial cell death, compromising the continuity of the luminal vascular surface; a perturbed endothelium can actively participate in pro-coagulant reactions. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0039497 The adhesion of one platelet to one or more other platelets via adhesion molecules. This process can constitute the course of coronavirus infectious disease. platelet aggregation in coronavirus infection HOIP_0039497 HOIP:HOIP_0039498 A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug. This process can constitute the course of coronavirus infectious disease. platelet activation in coronavirus infection HOIP_0039498 HOIP:HOIP_0039499 Positive regulation of cell adhesion molecule expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of cell adhesion molecule expression. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Shortly after P-selectin gets to the cell surface,mRNA encoding E-selectin is synthesized, and within 2 hours, the endothelial cells are expressing mainly E-selectin. Sulfated sialyl-Lewisx is present on the surface of neutrophils, and interactions with P-selectin and E-selectin are important for neutrophil rolling on the endothelium. Janeway's Immunobiology 9th Edition Chapter 3 Shortly after P-selectin gets to the cell surface,mRNA encoding E-selectin is synthesized, and within 2 hours, the endothelial cells are expressing mainly E-selectin. Sulfated sialyl-Lewisx is present on the surface of neutrophils, and interactions with P-selectin and E-selectin are important for neutrophil rolling on the endothelium. Janeway's Immunobiology 9th Edition Chapter 3 positive regulation of cell adhesion molecule expression in coronavirus infection HOIP_0039499 ISBN-10: 0815345518 Shortly after P-selectin gets to the cell surface,mRNA encoding E-selectin is synthesized, and within 2 hours, the endothelial cells are expressing mainly E-selectin. Sulfated sialyl-Lewisx is present on the surface of neutrophils, and interactions with P-selectin and E-selectin are important for neutrophil rolling on the endothelium. Janeway's Immunobiology 9th Edition Chapter 3 ISBN:0815345518 HOIP:HOIP_0039500 Any process that activates or increases the frequency, rate or extent of cell adhesion. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Janeway's Immunobiology 9th Edition Chapter 3 PMID:33077917 positive regulation of cell adhesion in coronavirus infection HOIP_0039500 Janeway's Immunobiology 9th Edition Chapter 3 PMID:33077917 Mechanistically, disruption of the endothelial barrier by SARS-CoV-2 spike protein is mediated by changes in the surface expression of intracellular adhesion molecule-1 (ICAM1), vascular cell adhesion protein-1 (VCAM1) and the tight junction scaffold protein zonula occludens-1 (ZO-1), as reported by a preprint study. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0039501 Any process that activates or increases the frequency, rate or extent of thrombus formation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. positive regulation of thrombus formation in coronavirus infection HOIP_0039501 HOIP:HOIP_0039502 Perforation manner is a subtype of manner: A manner of making a hole to penetrate a surface. perforation manner HOIP_0039502 HOIP:HOIP_0039503 A developmental process, independent of morphogenetic (shape) change, that is required for a platelet to attain its fully functional state. A platelet is a non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 platelet maturation (very high) in severe COVID-19 HOIP_0039503 PMID:32629875 Acting on hepatocytes, IL-6 promotes the synthesis of fibrinogen, tissue factor and Factor VII. It also stimulates platelet production in the bone marrow. Thus, IL-6 can promote a pro-coagulant and pro-thrombotic vascular pathology, raising the possibility that an abnormally high level of IL-6 may contribute to the vascular phenotype in severe COVID-19. HOIP:HOIP_0039504 Any process that activates or increases the frequency, rate or extent of cell adhesion. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 positive regulation of cell adhesion (very high) in severe COVID-19 HOIP_0039504 PMID:33077917 Mechanistically, disruption of the endothelial barrier by SARS-CoV-2 spike protein is mediated by changes in the surface expression of intracellular adhesion molecule-1 (ICAM1), vascular cell adhesion protein-1 (VCAM1) and the tight junction scaffold protein zonula occludens-1 (ZO-1), as reported by a preprint study. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0039506 Decreasing NO level is a subtype of decreasing quantity: A process that changes the amount of NO (nitric oxide) level to be lower. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection Decreasing NO level in severe COVID-19 HOIP_0039506 Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection PMID:33077917 HOIP:HOIP_0039507 Hypofunction of vasodilation is a subtype of hypofunctioning: A process that performs a decreased or insufficient vasodilation. hypofunction of vasodilation HOIP_0039507 HOIP:HOIP_0039508 Hypofunction of vasodilatione is a subtype of hypofunctioning: A process that performs a decreased or insufficient vasodilation. hypofunction of vasodilation in severe COVID-19 HOIP_0039508 HOIP:HOIP_0039509 Increasing blood pressure is a subtype of increasing pressure: A process that changes the blood pressure to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. increasing vascular pressure increasing blood pressure in severe COVID-19 HOIP_0039509 HOIP:HOIP_0039510 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces subgenomic negative stranded (-) mRNA. This process can constitute the course of severe COVID-19. subgenomic negative stranded viral mRNA biosynthetic process(very high) in severe COVID-19 HOIP_0039510 HOIP:HOIP_0039511 A process by which subgenomic negative stranded viral mRNA is translated into viral protein, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis subgenomic negative stranded viral mRNA viral translation in COVID-19 HOIP_0039511 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0039512 A process by which subgenomic negative stranded viral mRNA is translated into viral protein, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis subgenomic negative stranded viral mRNA viral translation (very high) in severe COVID-19 HOIP_0039512 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0039513 Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. This process can constitute the course of severe COVID-19. viral protein processing (very high) in severe COVID-19 HOIP_0039513 HOIP:HOIP_0039514 The assembly of a virus capsid from its protein subunits. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral capsid assembly (very high) in severe COVID-19 HOIP_0039514 HOIP:HOIP_0039515 The directed movement of a virus, or part of a virus, into, out of, or within a host cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. transport of virus (very high) in severe COVID-19 HOIP_0039515 HOIP:HOIP_0039516 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces the full-length negative stranded (-) mRNA for synthesis of new genomic RNAs and subgenomic negative strand templates. This process can constitute the course of severe COVID-19. PMID:32726803 full length negative stranded viral mRNA biosynthetic process full length negative stranded viral mRNA biosynthetic process (very high) in severe COVID-19 HOIP_0039516 PMID:32726803 This suggests that inhibition of SCoV2-PLpro by GRL-0617 impedes viral replication, thereby attenuating the ongoing viral RNA synthesis. HOIP:HOIP_0039517 A viral transcription process that produces the npositive stranded (+) mRNA for a new generation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33116300 Viral genomic replication is initiated by the synthesis of full-length negative-sense genomic copies, which function as templates for the generation of new positive-sense genomic RNA. positive stranded viral mRNA biosynthetic process Coronavirus is a single (+) strand RNA virus. Single (+)-strand RNA viruses initially use the (+)-strand genome to the (-) strand as a template to generate next-generation +-strand mRNA. next generation of positive stranded viral mRNA replication in COVID-19 HOIP_0039517 PMID:33116300 Viral genomic replication is initiated by the synthesis of full-length negative-sense genomic copies, which function as templates for the generation of new positive-sense genomic RNA. HOIP:HOIP_0039518 The rupture of cell membranes and the loss of cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. cytolysis (very high) in severe COVID-19 HOIP_0039518 HOIP:HOIP_0039519 A viral transcription process that produces the npositive stranded (+) mRNA for a new generation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33116300 Viral genomic replication is initiated by the synthesis of full-length negative-sense genomic copies, which function as templates for the generation of new positive-sense genomic RNA. positive stranded viral mRNA biosynthetic process Coronavirus is a single (+) strand RNA virus. Single (+)-strand RNA viruses initially use the (+)-strand genome to the (-) strand as a template to generate next-generation +-strand mRNA. next generation of positive stranded viral mRNA replication (very high) in severe COVID-19 HOIP_0039519 PMID:33116300 Viral genomic replication is initiated by the synthesis of full-length negative-sense genomic copies, which function as templates for the generation of new positive-sense genomic RNA. HOIP:HOIP_0039520 The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 Previous HoIP ID: HOIP_0039520 SARS-CoV-2 shedding (very high) in severe COVID-19 HOIP_0039520 PMID:33077917 Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0039521 The transport of a virus between adjacent cells in a multicellular organism. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32362314 PMID:32629875 cell to cell spread of virus within host intercellular virus transport transport of virus in host (cell to cell) (very high) in severe COVID-19 HOIP_0039521 PMID:32362314 Finally, the addition of an arginine residue to the S1/S2 site of SARS-2-S jointly with alanine-to-lysine exchange strongly increased syncytium formation, indicating that viral variants with optimized S1/S2 sites might show augmented cell-cell spread and potentially altered pathogenicity. PMID:32629875 Epidemiologic evidence indicates that the virus is transmitted among close contacts mostly through the respiratory route, presumably directly through infected droplet secretions or indirectly via fomites (Figure 2). The proximity between the infected respiratory epithelium releasing the virus and endothelial cells may favor local transmission. HOIP:HOIP_0039522 Any process involved directly in viral genome replication, including viral nucleotide metabolism. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32641482 viral genome replication in COVID-19 HOIP_0039522 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0039523 Any process involved directly in viral genome replication, including viral nucleotide metabolism. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32641482 viral genome replication (very high) in severe COVID-19 HOIP_0039523 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0039524 A viral genome replication process where the template genome is positive stranded, single stranded RNA ((+)ssRNA). Replication of the positive strand leads to dsRNA formation, which in turn is transcribed into positive single stranded RNA. This process can constitute the course of severe COVID-19. PMID:32697943 positive stranded viral RNA replication (very high) in severe COVID-19 HOIP_0039524 PMID:32697943 Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Elevated glucose levels directly induce viral replication and proinflammatory cytokine expression. HOIP:HOIP_0039525 A process by which viral mRNA is translated into viral protein for viral replication complex, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis translation for viral replication complex (very high) in severe COVID-19 HOIP_0039525 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0039526 The metabolic process in which viral RNA replicase is formed, using the sequence of a viral RNA to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome. This process can constitute the course of severe COVID-19. viral RNA replicase translation (very high) in severe COVID-19 HOIP_0039526 HOIP:HOIP_0039527 The cleavage of a peptide bond or bonds within a viral polyprotein. This process can constitute the course of severe COVID-19. viral polyprotein processing (very high) in severe COVID-19 HOIP_0039527 HOIP:HOIP_0039528 A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. This process can constitute the course of severe COVID-19. viral genome expression viral gene expression (very high) in severe COVID-19 HOIP_0039528 HOIP:HOIP_0039529 The process by which an incoming virus is disassembled in the host cell to release a replication-competent viral genome. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral uncoating uncoating of virus (very high) in severe COVID-19 HOIP_0039529 HOIP:HOIP_0039530 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This process can constitute the course of COVID-19. viral entry into host cell via vesicle-transport in COVID-19 HOIP_0039530 HOIP:HOIP_0039531 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This process can constitute the course of severe COVID-19. viral entry into host cell via vesicle-transport (very high) in severe COVID-19 HOIP_0039531 HOIP:HOIP_0039532 Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. This process can constitute the course of severe COVID-19. PMID:32221306 PMID:32361028 PMID:33116300 receptor mediated endocytosis by host of virus particle receptor mediated endocytosis of virus by host receptor mediated endocytosis of virus particle by host receptor-mediated endocytosis of virus by host viral receptor mediated endocytosis virus receptor-mediated endocytosis by host viral entry into host cell via receptor-mediated endocytosis viral entry into host cell via receptor-mediated endocytosis receptor-mediated endocytosis of virus by host cell (very high) in severe COVID-19 HOIP_0039532 PMID:32221306 Here, using SARS-CoV-2 S protein pseudovirus system, we confirm that human angiotensin converting enzyme 2 (hACE2) is the receptor for SARS-CoV-2, find that SARS-CoV-2 enters 293/hACE2 cells mainly through endocytosis, that PIKfyve, TPC2, and cathepsin L are critical for entry, and that SARS-CoV-2 S protein is less stable than SARS-CoV S. Phosphoinositides play many essential roles in endocytosis. Among them, one is phosphatidylinositol-3,5-bisphosphate (PI(3,5)P2), which regulates early endosome to late endosome dynamics. Two pore channel subtype 2 (TPC2) and TRPML1 in lysosome are two major downstream effectors of PI(3,5)P2. We confirmed this in this study, and further showed that blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. PMID:32361028 Host protease dependence of SARS-CoV-2 entry is a critical step. SARS-CoV takes advantage of the endosomal cysteine proteases Cathepsin B and L (CTSL and CTSB). CTSL/B are crucial elements of lysosomal pathway and both enzymes are almost exclusively located in the lysosomes. PMID:33116300 Besides receptor binding, the proteolytic cleavage of coronavirus S proteins by host cell-derived proteases is essential to permit fusion24,25. SARS-CoV has been shown to use the cell-surface serine protease TMPRSS2 for priming and entry, although the endosomal cysteine proteases cathepsin B (CatB) and CatL can also assist in this process viral entry into host cell via receptor-mediated endocytosis GOC:bf GOC:jl HOIP:HOIP_0039533 Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. This process can constitute the course of severe COVID-19. fusion of virus membrane with host endosomal membrane fusion of virus membrane with host endosome membrane (very high)in severe COVID-19 HOIP_0039533 HOIP:HOIP_0039534 Changing viral spike S protein S2 domain structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein S2 domain. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 changing viral spike S2 protein conformation changing viral spike S2 protein structure 2 (very high) in severe COVID-19 HOIP_0039534 PMID:33123165 The virus receptor, angiotensin-converting enzyme 2 (ACE2), expressed on the surface of multiple human cells is engaged via the receptor binding domain (RBD), which is part of the S1 subunit of the S glycoprotein. Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039535 Cleavage of viral spike protein is a subtype of proteolysis: A process in which viral spike protein is cleaved. This process can constitute the course of severe COVID-19. PMID:33116300 cleavage of viral spike S2 protein (very high) in severe COVID-19 HOIP_0039535 HOIP:HOIP_0039536 Cleavage of viral spike protein S is a subtype of proteolysis: A process in which viral spike protein S is cleaved. This process can constitute the course of severe COVID-19. PMID:32142651 PMID:32221306 PMID:32361028 PMID:32362314 PMID:32404436 PMID:33123165 cleavage of viral spike S protein 2 (very high) in severe COVID-19 HOIP_0039536 PMID:32142651 Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases. Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. PMID:32221306 While cathepsin B inhibitor treatment did not show any marked effect on virus entry, cathepsin L inhibition treatment decreased entry of SARS-CoV-2 S pseudovirions into 293/hACE2 by over 76% (Fig. 4a), suggesting that cathepsin L should be essential for priming of SARS-CoV-2 S protein in lysosome for entry into 293/hACE2 cells. PMID:32361028 SARS-Cov-2 entry into a cell is dependent upon binding of the viral spike (S) protein to cellular receptor and on cleavage of the spike protein by the host cell proteases such as Cathepsin L and Cathepsin B. PMID:32362314 Furin Cleaves the SARS-CoV-2 Spike Protein at the S1/ S2 Site, and Cleavage Is Required for Efficient Cell-Cell Fusion SARS-2-S expression triggered syncytium formation that was strongly increased by trypsin and TMPRSS2. PMID:32404436 Following receptor engagement, SARS-CoV-2 S is processed by a plasma membrane-associated type II transmembrane serine protease, TMPRSS2, prior to membrane fusion which is essential to release the viral contents into the host cell cytosol (3, 6). Here, we present evidence that SARS-CoV-2 infects human mature enterocytes from the apical surface and triggers epithelial cell fusion. TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion. PMID:33123165 Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039537 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This process can constitute the course of COVID-19. direct viral entry into host cell via cell surface membrane fusion in COVID-19 HOIP_0039537 HOIP:HOIP_0039538 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This process can constitute the course of severe COVID-19. direct viral entry into host cell via cell surface membrane fusion (very high) in severe COVID-19 HOIP_0039538 HOIP:HOIP_0039539 Fusion of a viral membrane with the host cell membrane during viral entry. Results in release of the virion contents into the cytoplasm. This process can constitute the course of severe COVID-19. PMID:32155444 PMID:32404436 PMID:32704094 PMID:33123165 fusion of virus membrane with host plasma membrane (very high) in severe COVID-19 HOIP_0039539 PMID:32155444 As a result, SARS-CoV-2 SB opening is expected to be necessary for interacting with ACE2 at the host cell surface and initiating the conformational changes leading to cleavage of the S2' site, membrane fusion and viral entry (Gui et al., 2017; Kirchdoerfer et al., 2018; Millet and Whittaker, 2014; Pallesen et al., 2017; Park et al., 2016; Song et al., 2018; Walls et al., 2019; Yuan et al., 2017). PMID:32404436 Following receptor engagement, SARS-CoV-2 S is processed by a plasma membrane-associated type II transmembrane serine protease, TMPRSS2, prior to membrane fusion which is essential to release the viral contents into the host cell cytosol (3, 6). Here, we present evidence that SARS-CoV-2 infects human mature enterocytes from the apical surface and triggers epithelial cell fusion. TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion. TMPRSS4 expression triggered S-mediated cell-cell fusion, although to a lesser extent than TMPRSS2 (Fig. 3E). PMID:32704094 Mechanistic studies revealed that LY6E inhibits CoV entry into cells by interfering with spike protein-mediated membrane fusion. LY6E reduced CoV S-mediated cell–cell fusion of HCoV-229E (Fig.2e,f), MERS-CoV (Fig.2e,f) and SARS-CoV-2 (Fig. 2g,h), as visualized by a reduction of GFP-positive syncytia, indicating that LY6E blocks the fusion of viral and cellular membranes. PMID:33123165 Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039540 Negative regulation of IFN-responsive gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFN-responsive gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32726803 negative regulation of early IFN-responsive gene expression in severe COVID-19 HOIP_0039540 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0039541 Cleavage of viral spike protein is a subtype of proteolysis: A process in which ciral spike protein is cleaved. This process can constitute the course of severe COVID-19. PMID:32142651 PMID:32221306 PMID:32361028 PMID:32362314 PMID:32404436 PMID:33123165 cleavage of viral spike S protein (very high) in severe COVID-19 HOIP_0039541 PMID:32142651 Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases. Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. PMID:32221306 While cathepsin B inhibitor treatment did not show any marked effect on virus entry, cathepsin L inhibition treatment decreased entry of SARS-CoV-2 S pseudovirions into 293/hACE2 by over 76% (Fig. 4a), suggesting that cathepsin L should be essential for priming of SARS-CoV-2 S protein in lysosome for entry into 293/hACE2 cells. PMID:32361028 SARS-Cov-2 entry into a cell is dependent upon binding of the viral spike (S) protein to cellular receptor and on cleavage of the spike protein by the host cell proteases such as Cathepsin L and Cathepsin B. PMID:32362314 Furin Cleaves the SARS-CoV-2 Spike Protein at the S1/ S2 Site, and Cleavage Is Required for Efficient Cell-Cell Fusion SARS-2-S expression triggered syncytium formation that was strongly increased by trypsin and TMPRSS2. PMID:32404436 Following receptor engagement, SARS-CoV-2 S is processed by a plasma membrane-associated type II transmembrane serine protease, TMPRSS2, prior to membrane fusion which is essential to release the viral contents into the host cell cytosol (3, 6). Here, we present evidence that SARS-CoV-2 infects human mature enterocytes from the apical surface and triggers epithelial cell fusion. TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion. PMID:33123165 Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039542 Changing viral spike S protein S2 domain structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein S2 domain. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 changing viral spike S2 protein conformation changing viral spike S2 protein structure (very high) in severe COVID-19 HOIP_0039542 PMID:33123165 The virus receptor, angiotensin-converting enzyme 2 (ACE2), expressed on the surface of multiple human cells is engaged via the receptor binding domain (RBD), which is part of the S1 subunit of the S glycoprotein. Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0039543 Fusion peptide insert into host cell memnrane is a subtype of moving A to the inside of B: A process that of the fusion peptide insertion into the host cell membrane. This process can constitute the course of severe COVID-19. Activated s2 protein inserts the fusion peptide into the target host cell membrane, which causes S2 structural change and membrane fusion. fusion peptide insert into host cell memnrane (very high) in severe COVID-19 HOIP_0039543 HOIP:HOIP_0039544 Interacting selectively and non-covalently with the surface of a host cell. This process can constitute the course of severe COVID-19. host cell surface binding (very high) in severe COVID-19 HOIP_0039544 HOIP:HOIP_0039545 Any process that results in induction of metabolic reprogramming. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Metabolic Reprogramming (very high) in severe COVID-19 HOIP_0039545 PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. SARS-CoV-2-Induced Metabolic Reprogramming of Monocytes Directly Affects T Cell Response and Lung Epithelial Cell Death Proteomic analysis performed in CoV-2-infected monocytes confirmed alterations on oxidative metabolism with an overall downregulation of proteins involved in the TCA cycle (Figure S2D). Moreover, several components of respiratory electron chain com- plexes are downregulated in CoV-2-infected monocytes, such as NDUFV1 (complex I), SDHA (complex II), cytochrome c reductase COR1 and UQCRC2 (complex III), ATP5PF, ATP5F1A, ATP5PD, F-type ATPase a, and PPA2 (ATP synthase) (Figure S2D). These data indicate that RET is an important source of mtROS in CoV-2-infected monocytes. Altogether, these results highlight the metabolic alterations that take place in CoV-2-infected monocytes under high glucose conditions. HOIP:HOIP_0039546 The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. This process can constitute the course of severe COVID-19. viral absorption virion attachment to host cell surface receptor viral attachment to host cell virion attachment to host cell (very high) in severe COVID-19 HOIP_0039546 HOIP:HOIP_0039547 The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration. This process can constitute the course of severe COVID-19. viral attachment to host entry receptor entry receptor-mediated virion attachment to host cell (very high) in severe COVID-19 HOIP_0039547 HOIP:HOIP_0039548 Interacting selectively and non-covalently with a receptor on the host cell surface. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 SARS-CoV-2 S binding to human ACE2 (very high) in severe COVID-19 HOIP_0039548 PMID:32629875 Angiotensin converting enzyme 2 (ACE2), the receptor for SARS-CoV-2 and other coronaviruses, is a transmembrane protein expressed by lung alveolar epithelial cells, enterocytes, and vascular endothelial cells, whose physiologic role is to induce the maturation of angiotensin I to generate angiotensin 1-7, a peptide hormone that controls vasoconstriction and blood pressure. A consequence of SARS-CoV-2 infection is that ACE2 function is disrupted and this disruption contributes to the pathogenesis to COVID-19. ACE2 belongs to the family of angiotensin-converting enzymes, which are essential regulators of blood pressure, cardiac function, and fluid balance. There is also some evidence that SARS-CoV-2 can infect endothelial cells in patients with severe cases of COVID-19. This is consistent with immunohistochemical detection of the viral nucleocapsid antigen in the epithelium of the stomach, duodenum, and rectum of a COVID-19 patient where ACE2 protein was also detected. HOIP:HOIP_0039549 Interacting selectively and non-covalently with a virion, either by binding to components of the capsid or the viral envelope. This process can constitute the course of severe COVID-19. virion binding with host cell surface receptor (very high) in severe COVID-19 HOIP_0039549 HOIP:HOIP_0039550 Negative regulation of ACE2 activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 activation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33077917 negative regulation of ACE2 activation (very high) in severe COVID-19 HOIP_0039550 PMID:32629875 Angiotensin converting enzyme 2 (ACE2), the receptor for SARS-CoV-2 and other coronaviruses, is a transmembrane protein expressed by lung alveolar epithelial cells, enterocytes, and vascular endothelial cells, whose physiologic role is to induce the maturation of angiotensin I to generate angiotensin 1-7, a peptide hormone that controls vasoconstriction and blood pressure. A consequence of SARS-CoV-2 infection is that ACE2 function is disrupted and this disruption contributes to the pathogenesis to COVID-19. ACE2 belongs to the family of angiotensin-converting enzymes, which are essential regulators of blood pressure, cardiac function, and fluid balance. In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). PMID:33077917 Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. After binding by SARS-CoV-2, ACE2 is internalized, and the lack of ACE2 on endothelial cells favours the progression of inflammatory and thrombotic processes triggered by local angiotensin II (Ang II) hyperactivity. Inhibition of ACE2 by binding of SARS-CoV-2 reduces the ACE2-mediated conversion of Ang II to Ang 1–7, the vasoactive ligand of the MAS receptor. The reduction of MAS receptor activation induces a pro-inflammatory phenotype through increased activation of type 1 angiotensin receptors (AT1R). Additionally, the reduction in levels of ACE2 limits the degradation of des-Arg9 bradykinin (DABK) into inactive peptides, ultimately leading to increased pro- thrombotic signalling via the activation of bradykinin receptors (BKRs). HOIP:HOIP_0039551 Negative regulation of angiotensin II hydrolysis is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of angiotensin II hydrolysis. This process can constitute the course of severe COVID-19. ACE2 hydrolyzes Angiotensin II and produces Angiotensin-(1-7). negative regulation of Angiotensin II hydrolysis (very high)in severe COVID-19 HOIP_0039551 HOIP:HOIP_0039552 Expression of ACE2 is a subtype of gene expression: The process in which a gene sequence is converted into a mature ACE2 gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32687793 PMID:32694793 PMID:32697943 expression of ACE2 (very high) in severe COVID-19 HOIP_0039552 PMID:32687793 The virus binds to ACE2 receptors, which, among other locations, are expressed in pancreatic tissue and β-cells in particular. PMID:32694793 In people with T2D, ACE2 expression is elevated in multiple target tissues of SARS-CoV-2, and this elevation has been proposed to be an adaptive mechanism that protects the body against diabetes-associated physiological dysfunction. This increased expression may enhance SARS-CoV-2’s entry and subsequent replication, as well as its spread within the body in individuals with T2D. PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0039553 angiotensin signaling is a process that a signal is transmitted by angiotensin. This process can constitute the course of severe COVID-19. PMID:32407672 PMID:32694793 PMID:33188364 angiotensin signaling (very high) in severe COVID-19 HOIP_0039553 PMID:32694793 The prevalence of hypertension, cardiovascular disease, nephropathy and retinopathy in people with diabetes has implicated the renin–angiotensin system (RAS) in the pathogenesis of these disorders. Angiotensin II, the active RAS metabolite and a potent vasoconstrictor that increases peripheral vascular resistance, also causes insulin resistance and regulates sodium absorption in the kidneys. PMID:33188364 ROS production and viral activation of the renin–angiotensin–aldosterone system (RAAS), (via increased angiotensin II expression) cause insulin resistance, hyperglycaemia and vascular endothelial damage, all of which contribute to cardiovascular events, thromboembolism and disseminated intravascular coagulation (DIC). HOIP:HOIP_0039554 TNF signaling is a subtype of biological signaling: Any processes of intracellular signals transduced by Tumor necrosis factor (TNF). This process can constitute the course of severe COVID-19. PMID:28792873 PMID:32264791 PMID:32407672 TNF signaling (very high) in severe COVID-19 HOIP_0039554 PMID:28792873 PMID:28792873 Tumor necrosis factor (TNF)–mediated expression of tissue factor promotes platelet aggregation and microthrombus formation, as well as intraalveolar coagulation and hyaline­membrane formation PMID:32264791 Ang II increases ADAM17 activity. ADAM17 cleaves its primary substrate releasing soluble TNF-α. TNF-α along with systemic cytokines released due to SARS-CoV-2 infection and in conjunction with comorbidities such as diabetes mellitus and hypertension can lead to a cytokine storm. PMID:32407672 Severe COVID-19 is also associated with increased concentrations of proinflammatory cytokines, such as tumour necrosis factor-α (TNF-α) and interleukins (IL), including IL-1 and IL-6.7 IL-6 can induce tissue factor expression on mononuclear cells, which subsequently initiates coagulation activation and thrombin generation. TNF-α and IL-1 are the main mediators driving a suppression of endogenous anticoagulant pathways. HOIP:HOIP_0039555 A process that changes the magnitude of the inflammation to be larger. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. expanding inflammation in severe COVID-19 HOIP_0039555 HOIP:HOIP_0039556 IL6 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding of Interleukin 6. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32407672 IL-6 signaling (very high) in severe COVID-19 HOIP_0039556 PMID:32407672 Severe COVID-19 is also associated with increased concentrations of proinflammatory cytokines, such as tumour necrosis factor-α (TNF-α) and interleukins (IL), including IL-1 and IL-6.7 IL-6 can induce tissue factor expression on mononuclear cells, which subsequently initiates coagulation activation and thrombin generation. TNF-α and IL-1 are the main mediators driving a suppression of endogenous anticoagulant pathways. HOIP:HOIP_0039557 TF production is a subtype of protein production: A process that makes existent of a TF (Tissue Factor) protein due to biosynthesis or secretion resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33077917 tissue factor production (very high) in severe COVID-19 HOIP_0039557 PMID:32629875 Acting on hepatocytes, IL-6 promotes the synthesis of fibrinogen, tissue factor and Factor VII. It also stimulates platelet production in the bone marrow. In addition, by promoting VEGF-A secretion from various cell types, IL-6 induces vascular hyper-permeability and sprouting angiogenesis. PMID:33077917 The recruited platelets release VEGF, which amplifies the expression of TF by endothelial cells, further stimulating the coagulation cascade. The expression of tissue factor (TF) by activated monocytes stimulates the coagulation cascade and the subsequent generation of thrombin; these processes are ineffectually counterbalanced by tissue factor pathway inhibitor (TFPI), which is present in plasma and platelets, and produced mainly by endothelial cells. HOIP:HOIP_0039558 Any process that activates or increases the frequency, rate or extent of the inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. positive regulation of inflammatory response (very high) in severe COVID-19 HOIP_0039558 HOIP:HOIP_0039559 Negative regulation of insulin receptor signaling pathway is a subtype of negative regulation of signaling: Any process that stops, prevents, or reduces the frequency, rate or extent of insulin receptor signaling. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33188364 Negative regulation of insulin receptor signaling in severe COVID-19 HOIP_0039559 PMID:33188364 Changes in insulin needs are seemingly associated with the levels of inflammatory cytokines. In individuals with obesity, pro-inflammatory cytokines with a T helper type 1 cell signature are known to increase insulin resistance; however, the role of such cytokines in COVID-19 is unclear. Thus, during SARS-CoV-2 infection, the ensuing anti-viral immune and inflammatory responses can change insulin sensitivity, potentially aggravating impairments of glucose metabolism (fig. 1). HOIP:HOIP_0039560 Renin-angiotensin activation is a subtype of activating: A process that changes the activity of the renin-angiotensin system, which regulates blood pressure and fluid balance, to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33188364 renin-angiotensin activation in severe COVID-19 HOIP_0039560 PMID:33188364 ROS production and viral activation of the renin–angiotensin–aldosterone system (RAAS), (via increased angiotensin II expression) cause insulin resistance, hyperglycaemia and vascular endothelial damage, all of which contribute to cardiovascular events, thromboembolism and disseminated intravascular coagulation (DIC). HOIP:HOIP_0039561 Positive regulation of ACE2 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of ACE2 gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of ACE2 gene expression (very ihgh) in severe COVID-19 HOIP_0039561 PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0039562 Increasing peripheral vascular resistance is a subtype of increasing pressure: A process that changes the peripheral vascular resistance to be higher. increasing peripheral vascular resistance HOIP_0039562 HOIP:HOIP_0039563 Increasing peripheral vascular resistance is a subtype of increasing pressure: A process that changes the peripheral vascular resistance to be higher. This process can constitute the course of severe COVID-19. PMID:32694793 increasing peripheral vascular resistance in severe COVID-19 HOIP_0039563 PMID:32694793 Angiotensin II, the active RAS metabolite and a potent vasoconstrictor that increases peripheral vascular resistance, also causes insulin resistance and regulates sodium absorption in the kidneys. HOIP:HOIP_0039564 Any apoptotic process in a T cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:34049969 T cell apoptotic process (very high) in severe COVID-19 HOIP_0039564 PMID:34049969 We found that ex vivo T cells from acutely infected COVID-19 patients were highly activated and apoptotic and displayed more extensive mitochondrial metabolic dysfunction, especially cells in CD8+ T cell lineages, than those from convalescent COVID-19 patients or healthy controls, but slightly disturbed mitochondrial metabolic activity was observed in non-COVID-19 patients. Importantly, plasma IL-6 and C-reactive protein (CRP) levels positively correlated with mitochondrial mass and negatively correlated with fatty acid uptake in T cells from COVID-19 patients. HOIP:HOIP_0039565 Increasing blood glucose level is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 PMID:32694793 PMID:32697943 hyperglycemia increasing blood glucose level in severe COVID-19 HOIP_0039565 PMID:32651579 Moreover, patients hospitalized with COVID-19 have exhibited a range of abnormalities of glucose metabolism, including worsened hyperglycemia, euglycemic ketosis, and classic diabetic ketoacidosis. In addition, ACE2 expression has been reported in the endocrine pancreas, albeit inconsistently. This raises the possibility that direct binding of SARS-CoV-2 to ACE2 on beta-cells might contribute to insulin deficiency and hyperglycemia, as has been shown previously for infection with SARS-CoV. PMID:32694793 Glycaemic control is likely to be necessary to regulate the host inflammatory response, to limit tissue susceptibility to inflammatory damage signals and to sustain physiological function during the severe and critical stages of infection. PMID:32697943 Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Moreover, increased glucose levels further augmented TNF-a, IL-6, and IFN a, b, and l expression (Figure S1A). This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. Elevated glucose levels directly induce viral replication and proinflammatory cytokine expression. HOIP:HOIP_0039566 Changing symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. This process can constitute the course of COVID-19. symbiotic imbalance between host and virus in COVID-19 HOIP_0039566 HOIP:HOIP_0039567 Changing symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. This process can constitute the course of severe COVID-19. symbiotic imbalance between host and virus in severe COVID-19 HOIP_0039567 HOIP:HOIP_0039568 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. viral proliferation (very high) in severe COVID-19 HOIP_0039568 HOIP:HOIP_0039569 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. This process can constitute the course of COVID-19. decreasing number of virus in COVID-19 HOIP_0039569 HOIP:HOIP_0039570 Infected cell damage is a subtype of damaging: A process that injuries the structure of the infected cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. infected cell damage in COVID-19 HOIP_0039570 HOIP:HOIP_0039571 Infected cell damage is a subtype of damaging: A process that injuries the structure of the infected cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. infected cell damage (very high) in severe COVID-19 HOIP_0039571 HOIP:HOIP_0039572 The destruction of infected cells in the early infectious stage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. early infected cell destruction (very high) in severe COVID-19 HOIP_0039572 HOIP:HOIP_0039573 Any series of signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of severe COVID-19. PMID:32505227 Wikipedia:Inflammation cytoplasmic pattern recognition receptor signaling in response to virus in severe COVID-19 HOIP_0039573 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of patternrecognition receptors (PRRs) by viral single-stranded RNA (ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0039574 Any processes of molecular signals generated as a consequence of a pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species, or damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. This process can constitute the course of severe COVID-19. pattern recognition receptor signaling in response to virus in severe COVID-19 HOIP_0039574 HOIP:HOIP_0039575 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. production of molecular mediator of innate immune response in severe COVID-19 HOIP_0039575 HOIP:HOIP_0039576 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. decreasing number of virus in severe COVID-19 HOIP_0039576 HOIP:HOIP_0039577 Positive regulation of IFN alpha gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IFN alpha gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of IFN alpha gene expression in severe COVID-19 HOIP_0039577 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0039578 Endothelium damage is a subtype of damaging: A process that injuries the structure of the endothelium as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33077917 Wikipedia:Coagulation endothelium damage (very high) in severe COVID-19 HOIP_0039578 PMID:32629875 A comprehensive post-mortem analysis of multiple tissues (in 3 COVID-19 cases) described congestion and endotheliitis of small vessels with accumulation of mononuclear/lymphocytic cells around the capillary endothelium in the heart, small bowel, kidney, liver and lung; in one case, caspase 3-immunostaining revealed the presence of apoptotic bodies in endothelial cells lining the inner wall of inflamed blood vessels. As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. When present at abnormally high levels, IL-6 in conjunction with soluble IL-6R compromises endothelial cells and the vasculature in experimental conditions (Section 4.3), and IL-6 peak levels mark disease severity in COVID-19. PMID:33077917 Although clinical insights into complement activation following SARS-CoV-2 infection are limited, the above findings indicate that unrestrained complement activation - mainly at the downstream terminal phases of the complement cascades - may contribute to endothelial cell injury, thrombosis and intravascular coagulation, ultimately leading to multi-systemic organ failure in patients with COVID-19. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. Wikipedia:Coagulation When the endothelium is damaged, the normally isolated, underlying collagen is exposed to circulating platelets, which bind directly to collagen with collagen-specific glycoprotein Ia/IIa surface receptors. This adhesion is strengthened further by von Willebrand factor (vWF), which is released from the endothelium and from platelets; vWF forms additional links between the platelets' glycoprotein Ib/IX/V and A1 domain. Binding of collagen to glycoprotein VI triggers a signaling cascade that results in activation of platelet integrins HOIP:HOIP_0039579 Receiving signal in pattern recognition receptor signaling pathway is a subtype of receiving signal: A process that recognizes the pathogen-associated molecular pattern (PAMPs) and changes into a signal in a pattern recognition receptor signaling pathway. This process can constitute the course of severe COVID-19. receiving viral signal in pattern recognition signaling pathway in severe COVID-19 HOIP_0039579 HOIP:HOIP_0039580 The selective elimination of senescent neutrophils from the body by autoregulatory mechanisms. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. Wikipedia:Inflammation neutrophil clearance (low) in severe COVID-19 HOIP_0039580 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0039581 Tissue regeneration is a subtype of changing material: The regrowth of lost or destroyed tissues. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. tissue regeneration (very high) in severe COVID-19 HOIP_0039581 HOIP:HOIP_0039582 The appearance of anti-inflammatory cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. Wikipedia:Inflammation anti-inflammatory cytokine production (low) in severe COVID-19 HOIP_0039582 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0039583 TNF signaling is a process that a signal is transmitted by TNF. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:28792873 PMID:32264791 PMID:32407672 TNF signaling (very high) in COVID-19 associated with ARDS HOIP_0039583 PMID:28792873 Tumor necrosis factor (TNF)–mediated expression of tissue factor promotes platelet aggregation and microthrombus formation, as well as intraalveolar coagulation and hyaline­membrane formation PMID:32264791 Ang II increases ADAM17 activity. ADAM17 cleaves its primary substrate releasing soluble TNF-α. TNF-α along with systemic cytokines released due to SARS-CoV-2 infection and in conjunction with comorbidities such as diabetes mellitus and hypertension can lead to a cytokine storm. PMID:32407672 Severe COVID-19 is also associated with increased concentrations of proinflammatory cytokines, such as tumour necrosis factor-α (TNF-α) and interleukins (IL), including IL-1 and IL-6.7 IL-6 can induce tissue factor expression on mononuclear cells, which subsequently initiates coagulation activation and thrombin generation. TNF-α and IL-1 are the main mediators driving a suppression of endogenous anticoagulant pathways. HOIP:HOIP_0039584 Any process that activates or increases the frequency, rate or extent of positive stranded viral RNA replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32697943 positive regulation of positive stranded viral RNA replication (very high) in COVID-19 in patient with diabetes HOIP_0039584 PMID:32697943 Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Elevated glucose levels directly induce viral replication and proinflammatory cytokine expression. HOIP:HOIP_0039585 Vascular dysfunction is a subtype of organ malfunction: A process that does not perform vascular function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. vascular dysfunction in severe COVID-19 HOIP_0039585 HOIP:HOIP_0039586 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32651579 insulin depletion insulin deficiency in COVID-19 in patient with diabetes HOIP_0039586 PMID:32651579 Factors related to SARS-CoV-2 include substantially elevated cytokine levels, which may lead to impairments in pancreatic beta-cell function and apoptosis and, consequently, decreased insulin production and ketosis. In addition, ACE2 expression has been reported in the endocrine pancreas, albeit inconsistently. This raises the possibility that direct binding of SARS-CoV-2 to ACE2 on beta-cells might contribute to insulin deficiency and hyperglycemia, as has been shown previously for infection with SARS-CoV179. HOIP:HOIP_0039587 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32651579 insulin depletion insulin deficiency (very high) in COVID-19 in patient with diabetes HOIP_0039587 PMID:32651579 Factors related to SARS-CoV-2 include substantially elevated cytokine levels, which may lead to impairments in pancreatic beta-cell function and apoptosis and, consequently, decreased insulin production and ketosis. In addition, ACE2 expression has been reported in the endocrine pancreas, albeit inconsistently. This raises the possibility that direct binding of SARS-CoV-2 to ACE2 on beta-cells might contribute to insulin deficiency and hyperglycemia, as has been shown previously for infection with SARS-CoV179. HOIP:HOIP_0039588 Expression of ACE2 is a subtype of gene expression: The process in which a gene sequence is converted into a mature ACE2 gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 with diabetes. PMID:32687793 PMID:32694793 PMID:32697943 expression of ACE2 in type B pancreatic cell (very high) in COVID-19 in patient with diabetes HOIP_0039588 PMID:32687793 The virus binds to ACE2 receptors, which, among other locations, are expressed in pancreatic tissue and β-cells in particular. PMID:32694793 In people with T2D, ACE2 expression is elevated in multiple target tissues of SARS-CoV-2, and this elevation has been proposed to be an adaptive mechanism that protects the body against diabetes-associated physiological dysfunction. This increased expression may enhance SARS-CoV-2’s entry and subsequent replication, as well as its spread within the body in individuals with T2D. PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0039589 Decreasing lymphocytes is a subtype of decreasing leucocytes: A process that changes the amount of lymphocytes to be lower. This process can constitute the course of severe COVID-19. PMID:32843733 decreasing lymphocytes in severe COVID-19 HOIP_0039589 PMID:32843733 The idea that the cytokine storm is mediated by leukocytes other than T or B cells is supported by observations of lymphocytopenia and sometimes atrophy of the lymphatic tissues, such as lymph nodes and spleen, in patients with severe COVID-19. HOIP:HOIP_0039591 STAT3 signaling is a process that a signal is transmitted by the STAT3 (signal transducer and activator of transcription 3) .This process can constitute the course of severe COVID-19. STAT3 signaling in severe COVID-19 HOIP_0039591 HOIP:HOIP_0039593 An inhibitor of a natural killer (NK) cell activation. NK cell inhibitor role HOIP_0039593 HOIP:HOIP_0039594 The totality of all processes through which COVID-19 infection in liver is realized. COVID-19 course in liver HOIP_0039594 HOIP:HOIP_0039595 NfkB signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by NF-kappaB. This entity is a specific course-dependent process.This process can constitute the course of severe COVID-19. PMID:32325025 PMID:32505227 PMID:32726803 NfkB signaling in severe COVID-19 HOIP_0039595 PMID:32325025 SARS-CoV-2 itself activates NF-kB via pattern recognition receptors (PPRs), and the accumulated AngII induces inflammatory cytokines including TNFa and IL-6-soluble (s)IL-6R via disintegrin and metalloprotease 17 (ADAM17), followed by activation of the IL-6 amplifier (IL-6 AMP), which describes enhanced NF-kB activation machinery via the coactivation of NF-kB and transcription factor STAT3. PMID:32505227 Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. SARS-CoV-2 NSP9 and NSP10 might induce IL-6 and IL-8 production, potentially by inhibition of NKRF, an endogenous NF-kB repressor. PMID:32726803 Here we perform biochemical, structural and functional characterization of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) PLpro (SCoV2-PLpro) and outline differences with SARS-CoV PLpro (SCoV-PLpro) in regulation of host interferon and NF-κB pathways. Moreover, phosphorylation of IRF3 and TBK1, markers for IFN pathway activation, and p65 phosphorylation, used to monitor NF-κB pathway activation, were increased in SARS-CoV-2-infected cells upon GRL-0617 treatment (Fig. 5f). HOIP:HOIP_0039596 Vascular endothelial cell damage damage is a subtype of cellular damage: A process that injuries the structure of the vascular endothelial cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 Wikipedia:"Blood sugar level" vascular endothelial cell damage in lung (very high) in COVID-19 associated with ARDS HOIP_0039596 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. Wikipedia:"Blood sugar level" A persistent elevation in blood glucose leads to glucose toxicity, which contributes to cell dysfunction and the pathology grouped together as complications of diabetes. HOIP:HOIP_0039597 Tube damage is a subtype of damaging: A process that injures the structure of the tube as the direct or indirect result of an external force. tube damage HOIP_0039597 HOIP:HOIP_0039598 Respiratory system blood vessel smooth muscle damage is a subtype of damaging: A process that injuries the structure of the respiratory system blood vessel smooth muscle as the direct or indirect result of an external force. respiratory blood vessel smooth muscle damage HOIP_0039598 HOIP:HOIP_0039599 A molecular signal induced by NK cells which triggers the apoptotic death of a cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. natural killer cell-mediated apoptotic process of infected cells in COVID-19 HOIP_0039599 HOIP:HOIP_0039600 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a natural killer cell. This process can constitute the course of COVID-19. natural killer cell degranulation in COVID-19 HOIP_0039600 HOIP:HOIP_0039601 A molecular signal induced by NK cells which triggers the apoptotic death of a cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. natural killer cell-mediated apoptotic process of infected cells in severe COVID-19 HOIP_0039601 HOIP:HOIP_0039602 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a natural killer cell. natural killer cell degranulation in severe COVID-19 HOIP_0039602 HOIP:HOIP_0039603 The directed killing of a target cell by a macrophage. This process can constitute the course of COVID-19. inflammatory macrophage mediated cytotoxicity in COVID-19 HOIP_0039603 HOIP:HOIP_0039604 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. This process can constitute the course of COVID-19. phagocytosis by inflammatory macrophage in COVID-19 HOIP_0039604 HOIP:HOIP_0039605 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a cytotoxic T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 cytotoxic T cell degranulation in COVID-19 HOIP_0039605 PMID:33123165 Processing and presentation of SARS-CoV-2 epitopes by antigen presenting cells (APCs) via human leukocyte antigen (HLA) class I leads to activation of naïve CD8+ T cells which differentiate into cytolytic effectors (cytotoxic T lymphocytes [CTL]) that kill virus-infected cells. HOIP:HOIP_0039606 Inflammation-anti-inflammation imbalance is a subtype of imbalance: A process that lacks a balance between the inflammatory response and the anti-inflammatory response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. inflammation-anti-inflammation imbalance in severe COVID-19 HOIP_0039606 HOIP:HOIP_0039607 The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. This process can constitute the course of COVID-19. apoptotic cell removal apoptotic cell clearance in COVID-19 HOIP_0039607 The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. PMID:14685684 HOIP:HOIP_0039608 The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. apoptotic cell removal apoptotic cell clearance (low) in severe COVID-19 HOIP_0039608 The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The functioning level is low. PMID:14685684 HOIP:HOIP_0039612 Negative regulation of TBK1 activation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of TBK1 activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 negative regulation of TBK1 activation in COVID-19 HOIP_0039612 PMID:32726803 Decreases in phosphorylation of TBK1 and IRF3, and nuclear translocation of IRF3 were detected upon expression of SCoV-PLpro or SCoV2-PLpro (Extended Data Fig. 5d, e). TBK1 phosphorylation also activates the NF-κB pathway, causing upregulation of inflammatory signalling30. HOIP:HOIP_0039613 Negative regulation of TBK1 activation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of TBK1 activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 negative regulation of TBK1 activation HOIP_0039613 PMID:32726803 Decreases in phosphorylation of TBK1 and IRF3, and nuclear translocation of IRF3 were detected upon expression of SCoV-PLpro or SCoV2-PLpro (Extended Data Fig. 5d, e). TBK1 phosphorylation also activates the NF-κB pathway, causing upregulation of inflammatory signalling30. HOIP:HOIP_0039614 The process in which IL-6R alpha is released from the cell surface. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 Release of IL6-R alpha from cell surface in severe COVID-19 HOIP_0039614 PMID:32629875 Since soluble IL-6R is abnormally elevated in the plasma of COVID-19 patients, presumably secondary to cleavage from the cells surface by TACE/ADAM17 upon SARS-CoV-2 infection and the inflammatory response associated with COVID-19, IL-6 can activate most cells, including endothelial cells, which do not express endogenous IL-6R but can be activated by the complex of soluble IL-6R and IL-6. HOIP:HOIP_0039615 Hypofunction of cleavage of viral spike protein is a subtype of hypofunction of decomposing: A process that performs a decreased or insufficient cleavage of viral spike protein. hypofunction of cleavage of viral spike protein HOIP_0039615 HOIP:HOIP_0039617 A role played by the entity which stops, prevents, or reduces the frequency, rate or extent of a host translation. negative regulator role of host translation HOIP_0039617 HOIP:HOIP_0039618 Pulmonary hyaline membrane fibrosis is a subtype of fibrosis: A process that replaces pulmonary hyaline membranes to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 PMID:32422178 An interstitial lung disease that is characterized by destruction, scarring, and thickening of the interstitial lung tissues and progressive pulmonary function loss in a restrictive pattern, has_symptom progressive shortness of breath, fatigue, and chronic cough, possibly has_material_basis_in exposure to certain chemicals, autoimmune conditions, and radiation. pulmonary hyaline membrane fibrosis in COVID-19 associated with ARDS HOIP_0039618 PMID:32307653 Moreover, resident lung progenitor/stem are extensively differentiated into myofibroblasts during pulmonary fibrosis, a complication observed in COVID-19 patients. In addition to direct viral invasion and loss of lung stem cells, stocks of these cells also can be affected during SARS-CoV-2 infection by extensive differentiation into myofibroblasts. These cell deposit extracellular matrix proteins and are the main cells presents in fibrotic diseases, including pulmonary fibrosis and fibrous stripes due to COVID-19. Recent evidence using lineage tracing showed that resident mesenchymal cells are the main sources of myofibroblasts in pulmonary fibrosis, rather than epithelial or bone marrow-derived cells. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32422178 Although many patients who develop ARDS survive the acute phase of the illness, a substantial proportion die as a result of progressive pulmonary fibrosis. Importantly, in an autopsy study of 159 patients with ARDS, fibrosis was noted in three (4%) of 82 patients with a disease duration of less than 1 week, 13 (24%) of 54 patients with a disease duration of between weeks 1 and 3, and 14 (61%) of 23 patients with a disease duration of greater than 3 weeks, suggesting that to be effective, any potential antifibrotic intervention should be considered within the first week of ARDS onset. A substantial proportion of patients who develop ARDS will experience residual long-term impairment of lung function and CT evidence of pulmonary fibrosis, with anterior reticulation the dominant abnormality in as many as 85% of survivors. Multiple aberrant host pathways interconnect to result in pulmonary fibrosis in a subset of individuals who develop ARDS. Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. Canonical profibrotic pathways regulated by TGF-beta are important, and there is evidence that vascular dysfunction is a key component of the switch from ARDS to fibrosis, with VEGF and cytokines such as IL-6 and TNFalpha implicated. In fatal cases of COVID-19, pulmonary fibrosis is generally present at autopsy, with anecdotal reports of severe fibrotic organising pneumonia. In some cases, abnormal immune mechanisms initiate and promote pulmonary fibrosis, possibly as a consequence of a cytokine storm. HOIP:HOIP_0039619 Any process in which a virus prevents or reduces the frequency, rate or extent of translation of host mRNA. This process can constitute the course of COVID-19. PMID:33116300 suppression by virus of host translation in COVID-19 HOIP_0039619 PMID:33116300 Proteolytic release of nsp1 is known to occur rapidly, which enables nsp1 to target the host cell translation machinery. HOIP:HOIP_0039620 Pulmonary hyaline membrane fibrosis is a subtype of fibrosis: A process that replaces pulmonary hyaline membranes to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 PMID:32422178 An interstitial lung disease that is characterized by destruction, scarring, and thickening of the interstitial lung tissues and progressive pulmonary function loss in a restrictive pattern, has_symptom progressive shortness of breath, fatigue, and chronic cough, possibly has_material_basis_in exposure to certain chemicals, autoimmune conditions, and radiation. pulmonary hyaline membrane fibrosis HOIP_0039620 PMID:32307653 Moreover, resident lung progenitor/stem are extensively differentiated into myofibroblasts during pulmonary fibrosis, a complication observed in COVID-19 patients. In addition to direct viral invasion and loss of lung stem cells, stocks of these cells also can be affected during SARS-CoV-2 infection by extensive differentiation into myofibroblasts. These cell deposit extracellular matrix proteins and are the main cells presents in fibrotic diseases, including pulmonary fibrosis and fibrous stripes due to COVID-19. Recent evidence using lineage tracing showed that resident mesenchymal cells are the main sources of myofibroblasts in pulmonary fibrosis, rather than epithelial or bone marrow-derived cells. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32422178 Although many patients who develop ARDS survive the acute phase of the illness, a substantial proportion die as a result of progressive pulmonary fibrosis. Importantly, in an autopsy study of 159 patients with ARDS, fibrosis was noted in three (4%) of 82 patients with a disease duration of less than 1 week, 13 (24%) of 54 patients with a disease duration of between weeks 1 and 3, and 14 (61%) of 23 patients with a disease duration of greater than 3 weeks, suggesting that to be effective, any potential antifibrotic intervention should be considered within the first week of ARDS onset. A substantial proportion of patients who develop ARDS will experience residual long-term impairment of lung function and CT evidence of pulmonary fibrosis, with anterior reticulation the dominant abnormality in as many as 85% of survivors. Multiple aberrant host pathways interconnect to result in pulmonary fibrosis in a subset of individuals who develop ARDS. Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. Canonical profibrotic pathways regulated by TGF-beta are important, and there is evidence that vascular dysfunction is a key component of the switch from ARDS to fibrosis, with VEGF and cytokines such as IL-6 and TNFalpha implicated. In fatal cases of COVID-19, pulmonary fibrosis is generally present at autopsy, with anecdotal reports of severe fibrotic organising pneumonia. In some cases, abnormal immune mechanisms initiate and promote pulmonary fibrosis, possibly as a consequence of a cytokine storm. HOIP:HOIP_0039621 Any process that activates or increases the frequency, rate or extent of viral genome replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. positive regulation of viral genome replication in COVID-19 HOIP_0039621 HOIP:HOIP_0039622 A protein that is a translation product of the ORF3b gene in SARS-CoV-2. UniProtKB:P59633 ORF3b (SARS2) protein 3b (SARS-CoV-2) HOIP_0039622 HOIP:HOIP_0039624 Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon production. This process can constitute the course of COVID-19. PMID:32505227 PMID:33116300 negative regulation of type III interferon production in COVID-19 HOIP_0039624 PMID:33116300 For example, nsp1 is rapidly proteolytically released from pp1a and pp1ab and affects cellular translation in the cytoplasm to favour viral mRNAs over cellular mRNA, and thereby also decreases the expression of type I and III interferons and of other host proteins of the innate immune response. Although this activity is not predicted for any accessory protein of SARS-CoV or SARS-CoV-2, the ORF3b, ORF6 and N proteins of SARS-CoV have been shown to interfere at multiple levels of the cellular interferon signalling pathway, thereby efficiently inhibiting innate immune responses103. Interestingly, an initial report recently suggested a similar role of SARS-CoV-2 ORF3b as an effective interferon antagonist. HOIP:HOIP_0039625 Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon production. PMID:32505227 PMID:33116300 negative regulation of type III interferon production HOIP_0039625 PMID:33116300 For example, nsp1 is rapidly proteolytically released from pp1a and pp1ab and affects cellular translation in the cytoplasm to favour viral mRNAs over cellular mRNA, and thereby also decreases the expression of type I and III interferons and of other host proteins of the innate immune response. Although this activity is not predicted for any accessory protein of SARS-CoV or SARS-CoV-2, the ORF3b, ORF6 and N proteins of SARS-CoV have been shown to interfere at multiple levels of the cellular interferon signalling pathway, thereby efficiently inhibiting innate immune responses103. Interestingly, an initial report recently suggested a similar role of SARS-CoV-2 ORF3b as an effective interferon antagonist. HOIP:HOIP_0039626 The process in which a relatively unspecialized cell acquires specialized features of a myoblast. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into striated muscle fibers. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). myoblast differentiation in COVID-19 associated with ARDS HOIP_0039626 HOIP:HOIP_0039627 A process that performs a decreased or insufficient of the cleavage of a peptide bond or bonds within a viral polyprotein. The production of non-structural proteins are very low. hypofunction of viral polyprotein processing HOIP_0039627 HOIP:HOIP_0039628 Extracellular matrix excess deposition is a subtype of accumulation of substances in a biological object: A process that puts extracellular matrix down in an organism, tissue, organelle, or cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:28792873 extracellular matrix excess deposition in COVID-19 associated with ARDS HOIP_0039628 HOIP:HOIP_0039629 Chronic inflammatory response is a subtype of the inflammatory response: A process of chronic defensive reactions (by vertebrate tissues) to infection or injury. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. chronic inflammatory response in COVID-19 in patient with diabetes HOIP_0039629 HOIP:HOIP_0039630 An inhibitor of protease of viral polyprotein, an enzyme required for production of viral proteins, viral replicase, and so on. viral polyprotein protease inhibitor HOIP_0039630 HOIP:HOIP_0039631 Any process that decreases the rate, frequency or extent of the series of molecular events generated as a consequence of chemokine CXCL8 signaling. PMID:34031531 negative regulation of CXCL8-mediated signaling in COVID-19 drug treatment HOIP_0039631 PMID:34031531 Our data suggest that a timely modulation of PTX3 by siltuximab represents a local effect of IL-6 inhibition in reducing inflammation in the lung bronchoalveolar lavage fluid [7, 8]. Moreover, modulation of IL-8 levels by siltuximab suggests an inhibition of systemic inflammation, which may prevent IL-8–mediated recruitment and activation of neutrophil. HOIP:HOIP_0039632 Any process that decreases the rate, frequency or extent of the series of molecular events generated as a consequence of chemokine CXCL8 signaling. negative regulation of CXCL8-mediated signaling HOIP_0039632 HOIP:HOIP_0039633 CXCL8 signaling is a process that a signal is transmitted by CXCL8. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. CXCL8 signaling (very low) in COVID-19 drug treatment HOIP_0039633 HOIP:HOIP_0039634 Hypofunction of the directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:34031531 neutrophil chemotaxis (very low) in COVID-19 drug treatment HOIP_0039634 PMID:34031531 Our data suggest that a timely modulation of PTX3 by siltuximab represents a local effect of IL-6 inhibition in reducing inflammation in the lung bronchoalveolar lavage fluid. Moreover, modulation of IL-8 levels by siltuximab suggests an inhibition of systemic inflammation, which may prevent IL-8–mediated recruitment and activation of neutrophils. HOIP:HOIP_0039635 An inhibitor of a neutrophil activation. neutrophil inhibitor role HOIP_0039635 HOIP:HOIP_0039636 Negative regulation of loss of vessel barrier integrity in lung is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of a loss of vessel barrier integrity function. This process can constitute the course of COVID-19 drug treatment. negative regulation of loss of vessel barrier integrity in COVID-19 drug treatment HOIP_0039636 HOIP:HOIP_0039637 Negative regulation of loss of vessel barrier integrity in lung is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of a loss of vessel barrier integrity function. negative regulation of loss of vessel barrier integrity in lung HOIP_0039637 HOIP:HOIP_0039638 Leaking fluid to pulmonary interstitium (very low) is a subtype of leaking: A process that leaks fruids to the pulmonary interstitium . This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. leaking fluid to pulmonary interstitium (very low) in COVID-19 drug treatment HOIP_0039638 HOIP:HOIP_0039639 The appearance of IgA antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. PMID:32887954 PMID:32967006 IgA antibody production (very low) in COVID-19 vaccination HOIP_0039639 PMID:32887954 Protective IgG antibodies induced by parenteral vaccination readily appear at the respiratory mucosa, this being the primary mechanism by which intramuscular injection of measles or influenza vaccine offers protection in humans. However, this route of vaccination is unable to effectively induce mucosal IgA antibodies or TRM cells in the lungs. PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. Vaccines that are administered intramuscularly or intradermally induce mainly IgG, and no secretory IgA. HOIP:HOIP_0039640 Negative regulation of inflammatory response is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. Resolution of inflammation 炎症の解消 negative regulation of inflammatory response in COVID-19 drug treatment HOIP_0039640 HOIP:HOIP_0039641 The appearance of IgG antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32967006 IgG antibody production in COVID-19 vaccination HOIP_0039641 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. HOIP:HOIP_0039642 A manner of pathogen treatment in vaccine is a subtype of a manner. A manner treats pathogens in vaccines. manner of treating pathogen in vaccine HOIP_0039642 HOIP:HOIP_0039643 Any process that activates or increases the frequency, rate, or extent of an adaptive immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:33053279 PMID:33340022 up-regulation of adaptive immune response positive regulation of T-helper 1 type immune response in COVID-19 vaccination HOIP_0039643 PMID:33340022 PMID:33053279 PMID:33340022 PMID:33340022 PMID:33340022 PMID:33340022 PMID:33340022 PMID:33340022 PMID:33340022 PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. PMID:33340022 An ideal COVID-19 vaccine target would be expected to induce high titres of nAbs, reduce non-nAb production to minimize ADE potential, elicit robust TH1 cell-biased responses but low TH2 cell-biased responses to lower the ERD potential, maintain long-lasting immunological memory, and provide cross-protection between CoVs. HOIP:HOIP_0039644 An mRNA–lipid nanoparticle vaccine which express a SARS-CoV-2 RBD-trimer stabilized by the foldon trimerization domain. PMID:33340022 https://clinicaltrials.gov/ct2/show/NCT04537949 https://go.drugbank.com/drugs/DB16442 BNT162b3 vaccine HOIP_0039644 PMID:33340022 LNP-mRNA RBD-trimer (trimerized by addition of T4 fibritin foldon domain) BioNTech, with Fosun Pharma and Pfizer, Germany Induction of RBD-specific IgG and nAbs in humans, with nAb titres higher than convalescent plasma; induction of high TH1 cell responses but low TH2 cell responses in humans HOIP:HOIP_0039645 The inhibition of biological effects of S1 protein by induction of immunoglobulin G (IgG). IgG-mediated neutralization of S1 protein HOIP_0039645 HOIP:HOIP_0039646 The inhibition of biological effects of S1 protein by induction of immunoglobulin G (IgG). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32887954 IgG-mediated neutralization of S1 protein in COVID-19 vaccination HOIP_0039646 PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. HOIP:HOIP_0039647 The inhibition of biological effects of S protein by by two proline substitution (S-2P) of S protein and induction of immunoglobulin G (IgG). PMID:33340022 IgG-mediated neutralization of spike protein by two proline substitution (S-2P) HOIP_0039647 PMID:33340022 The pre-fusion S protein is generally metastable during in vitro preparations and prone to transform into its post-fusion conformation. Mutation of two residues (K986 and V987) to proline stabilizes S protein (S-2P) and prevents the pre-fusion to post-fusion structural change. HOIP:HOIP_0039648 The inhibition of biological effects of S protein by by two proline substitution (S-2P) of S protein and induction of immunoglobulin G (IgG). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32663912 PMID:32887954 PMID:33340022 S2P: two proline substitutions (2P) in the spike (S) protein IgG-mediated neutralization of spike protein by two proline substitution (S-2P) in COVID-19 vaccination HOIP_0039648 PMID:32663912 The mRNA-1273 vaccine was immunogenic, inducing robust binding antibody responses to both full-length S-2P and receptor-binding domain in all participants after the first vaccination in a time- and dose-dependent fashion. Commensurately high neutralizing antibody responses were also elicited in a dose-dependent fashion. PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. PMID:33340022 The pre-fusion S protein is generally metastable during in vitro preparations and prone to transform into its post-fusion conformation. Mutation of two residues (K986 and V987) to proline stabilizes S protein (S-2P) and prevents the pre-fusion to post-fusion structural change. HOIP:HOIP_0039649 The inhibition of biological effects of S1 protein, especially inhibition of the receptor-binding domain (RBD) by induction of immunoglobulin G (IgG). immunoglobulin-mediated neutralization of S1 protein RBD IgG-mediated neutralization of S1 protein receptor-binding domain HOIP_0039649 HOIP:HOIP_0039650 The inhibition of biological effects of S1 protein, especially inhibition of the receptor-binding domain (RBD) by induction of immunoglobulin G (IgG). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32663912 PMID:32702298 PMID:32702299 PMID:32887954 PMID:32998157 PMID:33123165 PMID:33270381 https://doi.org/10.1038/s41586-020-2639-4 https://doi.org/10.1101/2020.07.17.20140533 immunoglobulin-mediated neutralization of S1 protein RBD immunoglobulin-mediated neutralization of S1 protein receptor-binding domain in COVID-19 vaccination HOIP_0039650 PMID:32663912 The mRNA-1273 vaccine was immunogenic, inducing robust binding antibody responses to both full-length S-2P and receptor-binding domain in all participants after the first vaccination in a time- and dose-dependent fashion. Commensurately high neutralizing antibody responses were also elicited in a dose-dependent fashion. PMID:32702298 We did a phase 1/2, single-blind, randomised controlled trial in five trial sites in the UK of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein compared with a meningococcal conjugate vaccine (MenACWY) as control. Similar increases in serum antibody levels to both the spike protein and the receptor binding domain by day 28 and after a booster dose were observed when measured by MIA (appendix p 16). PMID:32702299 RBD-specific ELISA antibody responses induced by the Ad5-vectored COVID-19 vaccine were detected from day 14 onwards, with GMTs of 94·5 (95% CI 80·5–110·8) and 85·1 (66·0–109·7) in the 1×1011 and 5×1010 viral particles dose groups, respectively (figure 2). Both vaccine doses induced significant neutralising antibody responses to live SARS-CoV-2, with GMTs of 19·5 (95% CI 16·8–22·7) and 18·3 (14·4–23·3) in participants in the 1 × 1011 and 5 × 1010 viral particles dose groups, respectively, at day 28 post vaccination (figure 2). PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. PMID:32998157 Two doses of 1–50 micro g of BNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those seen in serum from a cohort of individuals who had recovered from COVID-19. PMID:33123165 All participants developed RBD Abs by ELISA and SARS-CoV-2-specific nAbs by neutralization assay after 2 doses in the upper range of those who have recovered from COVID-19 (convalescent serum).(mRNA-1273) An interim report from the Phase 1/2 dose-ranging study of 2 doses of BioNTech’s mRNA S protein vaccine candidate BNT162 administered to adults aged 18–55 years elicited RBD- binding IgG and SARS-CoV-2 nAbs in the order of 1.8–2.8- fold that of convalescent human plasma. PMID:33270381 At the 100-micro g dose, mRNA-1273 produced high levels of binding and neutralizing antibodies that declined slightly over time, as expected, but they remained elevated in all participants 3 months after the booster vaccination. https://doi.org/10.1038/s41586-020-2639-4 RBD-binding IgG concentrations and SARS-CoV-2 neutralizing titres in sera increased with dose level and after a second dose. https://doi.org/10.1101/2020.07.17.20140533 Recently, we reported safety, tolerability and antibody response data from an ongoing placebo-controlled, observer-blinded phase 1/2 COVID-19 vaccine trial with BNT162b1, a lipid nanoparticle (LNP) formulated nucleoside-modified messenger RNA encoding the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Two doses of 1 to 50 μg of nBNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those in a COVID-19 convalescent human serum panel (HCS). HOIP:HOIP_0039651 Any apoptotic process in a cytotoxic T cell. This process can constitute the course of COVID-19 vaccination. cytotoxic T cell apoptotic process in COVID-19 vaccination HOIP_0039651 HOIP:HOIP_0039652 Attenuated manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of a microbe that can replicate slowly and provoke a strong immune response yet does not normally make healthy people sick. Attenuated manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of a microbe that can replicate slowly and provoke a strong immune response yet does not normally make healthy people sick. atennuated manner HOIP_0039652 Attenuated manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of a microbe that can replicate slowly and provoke a strong immune response yet does not normally make healthy people sick. ISBN:0367076322 HOIP:HOIP_0039653 Subunit manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner manufactured from purified component parts of a microbe, such as virus capsomers. Subunit manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner manufactured from purified component parts of a microbe, such as virus capsomers. subunit manner HOIP_0039653 Subunit manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner manufactured from purified component parts of a microbe, such as virus capsomers. Molecular and cellular biology of viruses ISBN:0367076322 HOIP:HOIP_0039654 Entry vaccine into the cells of a host organism. entry of vaccine into host cell HOIP_0039654 HOIP:HOIP_0039655 A process of administering substance in vivo that involves in adding a vaccine into a host (e.g., human) in vivo with the intent to invoke a protective or therapeutic adaptive immune response. This process can constitute the course of COVID-19 vaccination. vaccination in COVID-19 vaccination HOIP_0039655 HOIP:HOIP_0039656 Inactivated manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of chemically or physically treated microbes that cannot replicate. Inactivated manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of chemically or physically treated microbes that cannot replicate. inactivated manner HOIP_0039656 Inactivated manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of chemically or physically treated microbes that cannot replicate. ISBN:0367076322 HOIP:HOIP_0039657 DNA -basedmanner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of DNA encoding protein sununits of a microbe. DNA -basedmanner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of DNA encoding protein sununits of a microbe. DNA-based manner HOIP_0039657 DNA -basedmanner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of DNA encoding protein sununits of a microbe. ISBN:0367076322 HOIP:HOIP_0039658 mRNA-based manner is a subtype of manner of treating pathogen in vaccine: A vaccine treatment manner composed of RNA of a microbe. PMID:32887954 mRNA-based manner HOIP_0039658 PMID:32887954 The antigen-encoding mRNA complexed with a carrier such as lipid nanoparticles can be efficiently delivered in vivo into the cytoplasm of host cells for protein translation and post-translational modifications, which is an advantage over recombinant protein subunit vaccines. mRNA vaccines are non-infectious and are synthesized by in vitro transcription, free of microbial molecules. These beneficial features differentiate mRNA vaccines from live attenuated viral vaccines, inactivated viral vaccines, subunit vaccines and recombinant viral-vectored vaccines in terms of safety, efficacy and issues of antivector immunity, enabling their rapid and inexpensive production and repeated vaccination HOIP:HOIP_0039659 Entry vaccine into the cells of a host organism. This process can constitute the course of COVID-19 vaccination. entry of vaccine into host cell in COVID-19 vaccination HOIP_0039659 HOIP:HOIP_0039660 A process by which viral mRNA in vaccine is translated into viral protein, using the host cellular machinery. vaccine derived viral protein biosynthetic process vaccine derived viral mRNA translation HOIP_0039660 HOIP:HOIP_0039661 The process that results in the movement of mRNA from the viral vaccine into the cytosol. release of mRNA from viral vaccine HOIP_0039661 HOIP:HOIP_0039662 The process that results in the movement of mRNA from the viral vaccine into the cytosol. This process can constitute the course of COVID-19 vaccination. release of mRNA from viral vaccine in COVID-19 vaccination HOIP_0039662 HOIP:HOIP_0039663 A process by which viral mRNA in vaccine is translated into viral protein, using the host cellular machinery. This process can constitute the course of COVID-19 vaccination. vaccine derived viral protein biosynthetic process vaccine derived viral mRNA translation in COVID-19 vaccination HOIP_0039663 HOIP:HOIP_0039664 A vaccine treatment manner that are built on either a replication deficient viral backbone or an attenuated replication component that is bioengeneered to express angitens derived from the target patohgen. A vaccine treatment manner that are built on either a replication deficient viral backbone or an attenuated replication component that is bioengeneered to express angitens derived from the target patohgen. recombinant virus vector manner HOIP_0039664 A vaccine treatment manner that are built on either a replication deficient viral backbone or an attenuated replication component that is bioengeneered to express angitens derived from the target patohgen. PMID:32887954 HOIP:HOIP_0039665 A vaccine treatment mannere based on multiple virus-derived proteins that are assembled to mimic the organization and conformation of authentic native viruses but that lack the viral genome. A vaccine treatment mannere based on multiple virus-derived proteins that are assembled to mimic the organization and conformation of authentic native viruses but that lack the viral genome. virus-like particle vaccine manner HOIP_0039665 A vaccine treatment mannere based on multiple virus-derived proteins that are assembled to mimic the organization and conformation of authentic native viruses but that lack the viral genome. PMID:32887954 HOIP:HOIP_0039666 A nanosized spherical or capsule-shaped structure consisting of lipids. A nanosized spherical or capsule-shaped structure. LNP lipid nanoparticle HOIP_0039666 HOIP:HOIP_0039667 CCL3 signaling is a process that a signal is transmitted by CCL3. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32629875 PMID:33123165 CCL3 signaling in moderate COVID-19 HOIP_0039667 PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0039668 Entry of mRNA vaccine into the cells of a host organism. This process can constitute the course of COVID-19 vaccination. entry of mRNA vaccine into host cell in COVID-19 vaccination HOIP_0039668 HOIP:HOIP_0039669 Entry of recombinant viral-vetored type vaccine into the cells of a host organism. This process can constitute the course of COVID-19 vaccination. entry of recombinant viral-vetored type vaccine into host cell in COVID-19 vaccination HOIP_0039669 HOIP:HOIP_0039670 Entry of DNA vaccine into the cells of a host organism. This process can constitute the course of COVID-19 vaccination. entry of DNA vaccine into host cell in COVID-19 vaccination HOIP_0039670 HOIP:HOIP_0039671 Entry of inactivated vaccine into the cells of a host organism. This process can constitute the course of COVID-19 vaccination. entry of inactivated vaccine into host cell in COVID-19 vaccination HOIP_0039671 HOIP:HOIP_0039672 Fusion of a lipid nanoparticle (LNP) with the host cell membrane during mRN Avaccine entry. Results in release of the mRNA into the cytoplasm. membrane and LNP fusion involved in mRNA vaccine into host cell HOIP_0039672 HOIP:HOIP_0039673 Fusion of a lipid nanoparticle (LNP) with the host cell membrane during mRN Avaccine entry. Results in release of the mRNA into the cytoplasm. This process can constitute the course of COVID-19 vaccination. PMID:29326426 membrane and LNP fusion involved in mRNA vaccine into host cell in COVID-19 vaccination HOIP_0039673 PMID:29326426 Lipid nanoparticles (LNPs) have become one of the most appealing and commonly used mRNA delivery tools. LNPs often consist of four components: an ionizable cationic lipid, which promotes self-assembly into virus-sized (~100nm) particles and allows endosomal release of mRNA to the cytoplasm HOIP:HOIP_0039674 Vaccine derived viral spike protein production is a subtype of protein production: A process that produces a virus spike protein as an output from a mRNA vaccine. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. vaccine derived viral spike protein production in COVID-19 vaccination HOIP_0039674 HOIP:HOIP_0039675 The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. This process can constitute the course of COVID-19 vaccination. DC can present viral antigens via MHC Class I (cross-presentation) . antigen processing and presentation of exogenous peptide antigen via MHC class I in COVID-19 vaccination HOIP_0039675 HOIP:HOIP_0039676 The change in morphology and behavior of a mature or immature cytotoxic T cell resulting from exposure to an antigen for which its T cell receptor is specific bound to an MHC class I molecule on an antigen presenting cell, leading to the initiation or perpetuation of an immune response. This process can constitute the course of COVID-19 vaccination. Cytotoxic T cell activation via T cell receptor contact with antigen bound to MHC I molecule on antigen presenting cell in COVID-19 vaccination HOIP_0039676 HOIP:HOIP_0039677 The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. T cell mediated cytotoxicity of infected cell in COVID-19 vaccination HOIP_0039677 HOIP:HOIP_0039678 A vesicle-mediated transport process that results in the engulfment of external particulate material by dendritic cell. This process can constitute the course of COVID-19 vaccination. phagocytosis by dendritic cell in COVID-19 vaccination HOIP_0039678 HOIP:HOIP_0039679 The process in which an antigen-presenting cell expresses antigen (peptide or polysaccharide) on its cell surface in association with an MHC class II protein complex. This process can constitute the course of COVID-19 vaccination. antigen processing and presentation of exogenous peptide antigen via MHC class II in COVID-19 vaccination HOIP_0039679 HOIP:HOIP_0039680 Any process that activates or increases the frequency, rate or extent of cytotoxic T cell activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. positive regulation of cytotoxic T cell activation in COVID-19 vaccination HOIP_0039680 HOIP:HOIP_0039681 The synthesis of mRNA on a template of DNA of vaccine. vaccine deriived DNA-templated transcription HOIP_0039681 HOIP:HOIP_0039682 The synthesis of mRNA on a template of DNA of vaccine. This process can constitute the course of COVID-19 vaccination. vaccine deriived vDNA-templated transcription in COVID-19 vaccination HOIP_0039682 HOIP:HOIP_0039683 TLR7 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 7. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:33674759 TLR7 signaling in COVID-19 vaccination HOIP_0039683 PMID:33674759 RNA sensors such as Toll-like receptor 7 (TLR7) and MDA5 are triggered by the mRNA vaccines, and TLR9 is the major double-stranded DNA sensor for the AdV vaccine. The resultant activated DCs present antigen and co-stimulatory molecules to S protein-specific naive T cells, which become activated and differentiated into effector cells to form cytotoxic T lymphocytes or helper T cells. T follicular helper (TFH) cells help S protein-specific B cells to differentiate into antibody-secreting plasma cells and promote the production of high affinity anti-S protein antibodies. Following vaccination, S protein-specific memory T cells and B cells develop and circulate along with high affinity SARS-CoV-2 antibodies, which together help prevent subsequent infection with SARS-CoV-2. TCR, T cell receptor. HOIP:HOIP_0039684 The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. type I interferon production in COVID-19 vaccination HOIP_0039684 HOIP:HOIP_0039685 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. early cellular response to type I interferon in COVID-19 vaccination HOIP_0039685 HOIP:HOIP_0039686 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class I. This process can constitute the course of COVID-19 vaccination. positive regulation of MHC class I biosynthetic process in COVID-19 vaccination HOIP_0039686 HOIP:HOIP_0039687 TLR9 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 9. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:33674759 TLR9 signaling in COVID-19 vaccination HOIP_0039687 PMID:33674759 RNA sensors such as Toll-like receptor 7 (TLR7) and MDA5 are triggered by the mRNA vaccines, and TLR9 is the major double-stranded DNA sensor for the AdV vaccine. The resultant activated DCs present antigen and co-stimulatory molecules to S protein-specific naive T cells, which become activated and differentiated into effector cells to form cytotoxic T lymphocytes or helper T cells. T follicular helper (TFH) cells help S protein-specific B cells to differentiate into antibody-secreting plasma cells and promote the production of high affinity anti-S protein antibodies. Following vaccination, S protein-specific memory T cells and B cells develop and circulate along with high affinity SARS-CoV-2 antibodies, which together help prevent subsequent infection with SARS-CoV-2. TCR, T cell receptor. HOIP:HOIP_0039688 Septic shock refers to sepsis accompanied by hypotension that cannot be corrected by the infusion of fluids. Septic shock refers to sepsis accompanied by hypotension that cannot be corrected by the infusion of fluids. septic shock (process) HOIP_0039688 Septic shock refers to sepsis accompanied by hypotension that cannot be corrected by the infusion of fluids. Harrison's Principles of Internal Medicine HOIP:HOIP_0039689 Any process that activates or increases the frequency, rate, or extent of B cell mediated immunity. This process can constitute the course of COVID-19 vaccination. positive regulation of B cell mediated immunity in COVID-19 vaccination HOIP_0039689 HOIP:HOIP_0039690 The change in morphology and behavior of a cytotoxic T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. cytotoxic T cell activation in COVID-19 vaccination HOIP_0039690 HOIP:HOIP_0039691 An immune response directed against a previously encountered antigen, being quicker and quantitatively better compared with the primary response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). adaptive immune memory response in coronavirus infectious disease (homeostatic balance) HOIP_0039691 HOIP:HOIP_0039692 An immune response directed against a previously encountered antigen, being quicker and quantitatively better compared with the primary response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). adaptive immune memory response in COVID-19 (homeostatic balance) HOIP_0039692 HOIP:HOIP_0039693 An immune response directed against a previously encountered antigen, being quicker and quantitatively better compared with the primary response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance).This process can constitute the course of COVID-19 vaccination. adaptive immune memory response in COVID-19 vaccination HOIP_0039693 HOIP:HOIP_0039694 Any process involved directly in viral genome replication, including viral nucleotide metabolism. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is low. PMID:32641482 viral genome replication (very low) in COVID-19 vaccination HOIP_0039694 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0039695 An immune response which is associated with resistance to extracellular organisms such as helminths and pathological conditions such as allergy, which is orchestrated by the production of particular cytokines, most notably IL-4, IL-5, IL-10, and IL-13, by any of a variety of cell types including T-helper 2 cells, eosinophils, basophils, mast cells, and nuocytes, resulting in enhanced production of certain antibody isotypes and other effects. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). T-helper 2 type immune response in COVID-19 (homeostatic balance) HOIP_0039695 HOIP:HOIP_0039696 The process in which a relatively unspecialized T cell acquires specialized features of a T-helper 2 (Th2) cell. A Th2 cell is a CD4-positive, alpha-beta T cell that has the phenotype GATA-3-positive and produces interleukin-4. This process can constitute the course of COVID-19 (homeostatic balance). T-helper 2 cell differentiation in COVID-19 (homeostatic balance) HOIP_0039696 HOIP:HOIP_0039697 Positive regulation of an adaptive immune response mediated via cytokine production by helper T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). helper T cell enhancement of adaptive immune respons in COVID-19 (homeostatic balance) HOIP_0039697 HOIP:HOIP_0039698 The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). T cell mediated cytotoxicity of infected cell in COVID-19 (homeostatic balance) HOIP_0039698 HOIP:HOIP_0039699 The change in morphology and behavior of a cytotoxic T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). cytotoxic T cell activation in COVID-19 (homeostatic balance) HOIP_0039699 HOIP:HOIP_0039700 Any apoptotic process in a cytotoxic T cell. This process can constitute the course of COVID-19 (homeostatic balance). cytotoxic T cell apoptotic process in COVID-19 (homeostatic balance) HOIP_0039700 HOIP:HOIP_0039701 The change in morphology and behavior of a mature or immature cytotoxic T cell resulting from exposure to an antigen for which its T cell receptor is specific bound to an MHC class I molecule on an antigen presenting cell, leading to the initiation or perpetuation of an immune response. This process can constitute the course of COVID-19 (homeostatic balance). Cytotoxic T cell activation via T cell receptor contact with antigen bound to MHC I molecule on antigen presenting cell in COVID-19 (homeostatic balance) HOIP_0039701 HOIP:HOIP_0039702 Any process that activates or increases the frequency, rate or extent of cytotoxic T cell activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). positive regulation of cytotoxic T cell activation in COVID-19 (homeostatic balance) HOIP_0039702 HOIP:HOIP_0039703 The process in which a relatively unspecialized T cell acquires specialized features of a mature T follicular helper cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 T follicular helper cell differentiation in COVID-19 ith vaccination HOIP_0039703 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0039704 The switching of activated B cells from IgM biosynthesis to biosynthesis of an IgG isotype, accomplished through a recombination process involving an intrachromosomal deletion between switch regions that reside 5' of the IgM and one of the IgG constant region gene segments in the immunoglobulin heavy chain locus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:33123165 isotype switching to IgG isotypes in COVID-19 vaccination HOIP_0039704 PMID:33123165 Importantly, class-switched IgG memory B cells to S and RBD have been demonstrated in COVID-19 patients confirming the generation of B cell memory which can provide a rapid recall response on subsequent SARS-CoV- 2 exposure. HOIP:HOIP_0039705 The change in morphology and behavior of a mature or immature B cell during an immune response, resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. B cell activation involved in immune response in COVID-19 vaccination HOIP_0039705 HOIP:HOIP_0039706 The change in morphology and behavior of a T follicular helper cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. T follicular helper cell activation HOIP_0039706 HOIP:HOIP_0039707 The change in morphology and behavior of a T follicular helper cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This process can constitute the course of COVID-19 vaccination. PMID:33674759 T follicular helper cell activation in COVID-19 vaccination HOIP_0039707 PMID:33674759 CD4+ T follicular helper (TFH) cells, which promote B cell differentiation into antibody-secreting plasma cells. Both the mRNA and AdV vaccines require two doses spaced 3–4 weeks apart to promote optimal protection and have been associated with mild to moderate side effects, including injection site pain, transient fever and chills, which can be augmented with the second dose. This secondary enhancement of the inflammatory response can derive from short-term changes to innate cells like macrophages through a phenomenon called ‘trained immunity’, and/or from activation of memory T cells and B cells generated from the initial injection. HOIP:HOIP_0039708 Septic shock refers to sepsis accompanied by hypotension that cannot be corrected by the infusion of fluids. Septic shock refers to sepsis accompanied by hypotension that cannot be corrected by the infusion of fluids. Septic shock refers to sepsis accompanied by hypotension that cannot be corrected by the infusion of fluids. This process can constitute the course of severe COVID-19. septic shock (process) in severe COVID-19 HOIP_0039708 Septic shock refers to sepsis accompanied by hypotension that cannot be corrected by the infusion of fluids. Harrison's Principles of Internal Medicine HOIP:HOIP_0039709 Any process that activates or increases the frequency, rate or extent of B cell activation. This process can constitute the course of COVID-19 vaccination. positive regulation of B cell activation in COVID-19 vaccination HOIP_0039709 HOIP:HOIP_0039710 Hypofunction of viral capsid assembly is a subtype of hypofunction of assembling: A process that performs a decreased or insufficient viral capsid assembly. hypofunction of viral capsid assembly HOIP_0039710 HOIP:HOIP_0039711 Decreasing blood pressure is a subtype of decreasing pressure: A process that changes the blood pressure to be lower. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. decreasing vascular pressure decreasing blood pressure in severe COVID-19 HOIP_0039711 HOIP:HOIP_0039712 Any process that activates or increases the frequency, rate or extent of isotype switching to IgG isotypes. This process can constitute the course of COVID-19 vaccination. positive regulation of isotype switching to IgG isotypes in COVID-19 vaccination HOIP_0039712 HOIP:HOIP_0039713 Hypofunction of interferon-beta production is a subtype of hypofunction of type I interferon production: A process that performs a decreased or insufficient interferon-beta production. hypofunction of interferon-beta production HOIP_0039713 HOIP:HOIP_0039714 Hypofunction of IL-1 beta production is a subtype of hypofunction of cytokine biosynthesis: A process that performs a decreased or insufficient IL-1 beta production. hypofunction of IL-1 beta production HOIP_0039714 HOIP:HOIP_0039715 Cough (process) is an explosive expulsion of air from the lungs. cough (process) HOIP_0039715 HOIP:HOIP_0039716 Hypofunction of interferon-alpha production is a subtype of hypofunction of type I interferon production: A process that performs a decreased or insufficient interferon-alpha production. hypofunction of interferon-alpha production HOIP_0039716 HOIP:HOIP_0039717 Hypofunction of transport of virus in host (cell to cell) is a subtype of hypofunction of transport of virus: A process that performs a decreased or insufficient transport of virus in host (cell to cell). hypofunction of transport of virus in host (cell to cell) HOIP_0039717 HOIP:HOIP_0039718 Hypofunction of positive stranded viral RNA replication is a subtype of hypofunction of viral genome replication: A process that performs a decreased or insufficient positive stranded viral RNA replication. hypofunction of positive stranded viral RNA replication HOIP_0039718 HOIP:HOIP_0039719 COVID-19 protein subunit vaccine HOIP_0039719 HOIP:HOIP_0039720 Any apoptotic process in a natural killer cell, a lymphocyte that can spontaneously kill a variety of target cells without prior antigenic activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). natural killer cell apoptotic process in coronavirus infectious disease (homeostatic balance) HOIP_0039720 HOIP:HOIP_0039721 Any apoptotic process in a natural killer cell, a lymphocyte that can spontaneously kill a variety of target cells without prior antigenic activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). natural killer cell apoptotic process in COVID-19 (homeostatic balance) HOIP_0039721 HOIP:HOIP_0039722 Any apoptotic process in a natural killer cell, a lymphocyte that can spontaneously kill a variety of target cells without prior antigenic activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. natural killer cell apoptotic process in COVID-19 vaccination HOIP_0039722 HOIP:HOIP_0039723 Early removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue in the early infetious stage. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. early removing infected cell in COVID-19 vaccination HOIP_0039723 HOIP:HOIP_0039724 The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. This process can constitute the course of COVID-19 (homeostatic balance). antigen processing and presentation of exogenous peptide antigen via MHC class I in COVID-19 (homeostatic balance) HOIP_0039724 HOIP:HOIP_0039725 The process in which an antigen-presenting cell expresses antigen (peptide or polysaccharide) on its cell surface in association with an MHC class II protein complex. This process can constitute the course of COVID-19 (homeostatic balance). antigen processing and presentation of exogenous peptide antigen via MHC class II in COVID-19 (homeostatic balance) HOIP_0039725 HOIP:HOIP_0039726 The process in which a relatively unspecialized thymocyte acquires specialized features of a T-helper cell. This process can constitute the course of COVID-19 (homeostatic balance). Helper T cells exist in two broad classes. T cells (Th1) are associated with the cell-killing and inflammatory responses of the immune system, including an important role of the activation of macrophages. Th2 cells activate B cells and the general serological (antibody) response. T-helper cell differentiation in COVID-19 (homeostatic balance) HOIP_0039726 HOIP:HOIP_0039727 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 1 (Th1) cell. A Th1 cell is a CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive and produces interferon-gamma. This process can constitute the course of COVID-19 (homeostatic balance). T-helper 1 cell differentiation in COVID-19 (homeostatic balance) HOIP_0039727 HOIP:HOIP_0039728 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 1 (Th1) cell. A Th1 cell is a CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive and produces interferon-gamma. This process can constitute the course of COVID-19 vaccination. T-helper 1 cell differentiation in COVID-19 vaccination HOIP_0039728 HOIP:HOIP_0039729 The process in which a relatively unspecialized thymocyte acquires specialized features of a T-helper cell. This process can constitute the course of COVID-19 vaccination. Helper T cells exist in two broad classes. T cells (Th1) are associated with the cell-killing and inflammatory responses of the immune system, including an important role of the activation of macrophages. Th2 cells activate B cells and the general serological (antibody) response. T-helper cell differentiation in COVID-19 vaccination HOIP_0039729 HOIP:HOIP_0039730 Removing infected cell in adaptive immunity is a subtype of removing infected cell: A process that takes a infected cell from an organism or tissue in the adaptive immune responses. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). removing infected cell in adaptive immunity in COVID-19 (homeostatic balance) HOIP_0039730 HOIP:HOIP_0039731 Removing infected cell in adaptive immunity is a subtype of removing infected cell: A process that takes a infected cell from an organism or tissue in the adaptive immune responses. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. removing infected cell in adaptive immunity in COVID-19 vaccination HOIP_0039731 HOIP:HOIP_0039732 Positive regulation of an adaptive immune response mediated via cytokine production by helper T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. helper T cell enhancement of adaptive immune response in COVID-19 vaccination HOIP_0039732 HOIP:HOIP_0039733 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell. This process can constitute the course of COVID-19 vaccination. negative regulation of viral entry into host cell in COVID-19 vaccination HOIP_0039733 HOIP:HOIP_0039734 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This process can constitute the course of COVID-19 vaccination. antiviral innate immune response in COVID-19 vaccination HOIP_0039734 HOIP:HOIP_0039735 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This process can constitute the course of COVID-19 vaccination. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. inflammatory response (high) in COVID-19 vaccination HOIP_0039735 HOIP:HOIP_0039736 The synthesis or release of any molecular mediator of the inflammatory response following an inflammatory stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation synthesis or release of inflammatory mediator in COVID-19 vaccination HOIP_0039736 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039737 The regulated release of histamine by a cell as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation histamine secretion involved in inflammatory response in COVID-19 vaccination HOIP_0039737 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Redness and heat are due to increased blood flow at body core temperature to the inflamed site; swelling is caused by accumulation of fluid; pain is due to the release of chemicals such as bradykinin and histamine that stimulate nerve endings. Histamine: Stored in preformed granules, histamine is released in response to a number of stimuli. It causes arteriole dilation, increased venous permeability, and a wide variety of organ-specific effects. HOIP:HOIP_0039738 Any process that results in a change in state or activity of a cell as a result of a stimulus of pain sensation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation response to pain sensation stimulus in COVID-19 vaccination HOIP_0039738 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039739 Increasing vascular permeabilization is a subtype of changing permeability: A process that changes the permeability of the vascular to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:33077917 Wikipedia:Inflammation increasing vascular permeabilization in COVID-19 vaccination HOIP_0039739 PMID:33077917 Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039740 Leaking fluid from blood vessel is a subtype of leaking: A process that leaks fluid out from the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. leaking fluid from blood vessel in COVID-19 vaccination HOIP_0039740 HOIP:HOIP_0039741 Increasing vascular lumen area is a subtype of increasing area: A process that changes the area of the vascular lumen area to be larger. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation Vasodilation 血管拡張 increasing vascular lumen area in COVID-19 vaccination HOIP_0039741 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039742 Increasing blood flow is a subtype of increaseing flow: A process that changes the amount of blood flow to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation increasing blood flow in COVID-19 vaccination HOIP_0039742 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039743 Increasing temperature is a subtype of changing temperature: A process that increases the temperature of the object. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation heat increasing temperature in COVID-19 vaccination HOIP_0039743 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039744 A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. smooth muscle contraction in COVID-19 vaccination HOIP_0039744 HOIP:HOIP_0039745 The regulated release of a prostaglandin that contributes to the immune response. Prostaglandins are a group of biologically active metabolites which contain a cyclopentane ring. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation prostaglandin secretion involved in inflammatory response in COVID-19 vaccination HOIP_0039745 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0039746 Any process that activates or increases the frequency, rate, or extent of fever generation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation positive regulation of fever generation in COVID-19 vaccination HOIP_0039746 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0039747 Increasing body temperature is a subtype of increaseing temperature: A process that increases the temperature of the body. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation increasing body temperature in COVID-19 vaccination HOIP_0039747 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0039748 The release of bradykinin following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation bradykinin secretion involved in inflammatory response in COVID-19 vaccination HOIP_0039748 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Bradykinin: A vasoactive protein that is able to induce vasodilation, increase vascular permeability, cause smooth muscle contraction, and induce pain. HOIP:HOIP_0039749 The release of any leukotriene following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. Wikipedia:Inflammation leukotriene secretion involved in inflammatory response in COVID-19 vaccination HOIP_0039749 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. leukotriene B4: Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0039750 Cytolysis of target cells by natural killer cells, eosinophils, neutrophils, monocytes, or macrophages following engagement of antibodies bound to the target cells by Fc receptors on the effector cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32887954 antibody-dependent cellular cytotoxicity in COVID-19 vaccination HOIP_0039750 PMID:32887954 Furthermore, patients with symptomatic COVID-19 are reported to produce IgG anti-bodies with reduced fucosylation levels, which in turn promotes their interaction with activating FcgammaRIIIa. Fc-mediated effector functions: immune functions that are mediated through the interaction of the constant Fc region of antibodies with innate immune molecules, complement proteins and specialized Fc receptors expressed by innate immune cells. The resulting functions include complement-dependent cytotoxicity and antibody-dependent cellular phagocytosis or cell-mediated cytotoxicity. HOIP:HOIP_0039751 Hypofunction of viral RNA replicase translation is a subtype of viral translation: A process that performs a decreased or insufficient viral RNA replicase translation. hypofunction of viral RNA replicase translation HOIP_0039751 HOIP:HOIP_0039752 Hypofunction of interleukin-6 production is a subtype of hypofunction of cytokine biosynthesis: A process that performs a decreased or insufficient interleukin-6 production. hypofunction of interleukin-6 production HOIP_0039752 HOIP:HOIP_0039753 Hypofunctioning is a subtype of fusion of virus membrane with host plasma membrane: A process that performs a decreased or insufficient fusion of virus membrane with host plasma membrane. hypofunction of fusion of virus membrane with host plasma membrane HOIP_0039753 HOIP:HOIP_0039754 Hypofunction of viral transcription is a subtype of hypofunctioning : A process that performs a decreased or insufficient viral transcription. hypofunction of viral transcription HOIP_0039754 HOIP:HOIP_0039755 Hypofunction of receptor-mediated endocytosis of virus by host cell is a subtype of hypofunction of transport of virus: A process that performs a decreased or insufficient receptor-mediated endocytosis of virus by host cell. hypofunction of receptor-mediated endocytosis of virus by host cell HOIP_0039755 HOIP:HOIP_0039756 Hypofunction of virion binding is a subtype of hypofunction of assembling: A process that performs a decreased or insufficient virion binding. hypofunction of virion binding HOIP_0039756 HOIP:HOIP_0039757 A process that performs a decreased or insufficient membrane fusion involved in viral entry into host cell. hypofunction of membrane fusion involved in viral entry into host cell HOIP_0039757 HOIP:HOIP_0039758 Hypofunction of production of molecular mediator of immune response is a subtype of hypofunction of transcription, DNA-templated: A process that performs a decreased or insufficient production of molecular mediator of immune response. hypofunction of production of molecular mediator of immune response HOIP_0039758 HOIP:HOIP_0039759 The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. This process can constitute the course of COVID-19 vaccination. antigen presentation in COVID-19 vaccination HOIP_0039759 HOIP:HOIP_0039760 Any process that activates or increases the frequency, rate or extent of B cell activation. This process can constitute the course of COVID-19 (homeostatic balance). positive regulation of B cell activation in COVID-19 (homeostatic balance) HOIP_0039760 HOIP:HOIP_0039761 An enzyme inhibitor that interferes with the activity of CYP3A4 involved in catalysis of organic substances. https://go.drugbank.com/categories/DBCAT002647 CYP3A4 inhibitor HOIP_0039761 HOIP:HOIP_0039763 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This entity is a specific course-dependent process. This process can constitute the course of apparent COVID-19. PMID:32843733 establishment of virus infection in apparent COVID-19 HOIP_0039763 PMID:32843733 If the protective immune response is impaired, the virus is allowed to replicate and can cause widespread tissue damage. The lungs seem to be the main target, although other organs with high ACE2 expression, such as the intestine, heart, brain and kidney, might also be vulnerable. HOIP:HOIP_0039764 A process that changes the magnitude of the virus proliferation to be larger. proliferative expansion of virus HOIP_0039764 HOIP:HOIP_0039765 A process that changes the magnitude of the virus proliferation to be larger. proliferative expansion of virus in apparent COVID-19 HOIP_0039765 HOIP:HOIP_0039767 Hypofunction of subgenomic negative stranded viral mRNA biosynthesis is a subtype of hypofunction of viral transcription : A process that performs a decreased or insufficient subgenomic negative stranded viral mRNA biosynthesis. hypofunction of subgenomic negative stranded viral mRNA biosynthesis HOIP_0039767 HOIP:HOIP_0039768 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen antiviral innate immune response [coronavirus infectious disease (infectious stage)] HOIP_0039768 HOIP:HOIP_0039769 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. decreasing number of virus [coronavirus infectious disease (infectious stage)] HOIP_0039769 HOIP:HOIP_0039770 Hypofunction of entry receptor-mediated virion attachment to host cell is a subtype of hypofunction of virion attachment to host cell: A process that performs a decreased or insufficient entry receptor-mediated virion attachment to host cell. hypofunction of entry receptor-mediated virion attachment to host cell HOIP_0039770 HOIP:HOIP_0039771 Removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. removing infected cell [coronavurus infectious diesase (infectious stage)] HOIP_0039771 HOIP:HOIP_0039772 Early removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue in the early infetious stage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. early removing infected cell [coronavirus infectious disease (infectious stage)] HOIP_0039772 HOIP:HOIP_0039773 A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. phagocytosis [coronavirus infectious disease (infectious stage)] HOIP_0039773 HOIP:HOIP_0039774 The destruction of infected cellin the early infectious stage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. innate immunity mediated infected cell damage [coronavirus infectious disease] early infected cell destruction [coronavirus infectious disease (infectious stage)] HOIP_0039774 HOIP:HOIP_0039775 Infected cell damage is a subtype of damaging: A process that injuries the structure of the infected cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. infected cell damage[coronavirus infectious disease (infectious stage)] HOIP_0039775 HOIP:HOIP_0039776 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. ISBN:0815341504 cellular response to type I interferon [coronavirus infectious disease (infectious stage)] HOIP_0039776 ISBN:0815341504 ISBN:0815341504 Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. PMID:33723416 In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. PMID:33153908 SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. PMID:32505227 TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. PMID:33153908 HOIP:HOIP_0039777 Hypofunction of full length negative stranded viral mRNA biosynthetic process is a subtype of hypofunction of viral transcription: A process that performs a decreased or insufficient full length negative stranded viral mRNA biosynthetic process. hypofunction of full length negative stranded viral mRNA biosynthetic process HOIP_0039777 HOIP:HOIP_0039778 A process that performs a decreased or insufficient fusion of virus membrane with host endosome membrane. hypofunction of fusion of virus membrane with host endosome membrane HOIP_0039778 HOIP:HOIP_0039779 Hypofunction of moving A to the inside of B is a subtype of hypofunctioning: A process that performs a decreased or insufficient moving A to the inside of B. hypofunction of moving A to the inside of B HOIP_0039779 HOIP:HOIP_0039780 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class I. This process can constitute the course of coronavirus infectious disease (homeostatic balance). positive regulation of MHC class I biosynthetic process in coronavirus infectious disease (homeostatic balance) HOIP_0039780 HOIP:HOIP_0039781 The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. This process can constitute the course of coronavirus infectious disease (homeostatic balance). antigen processing and presentation of exogenous peptide antigen via MHC class I in coronavirus infectious disease (homeostatic balance) HOIP_0039781 HOIP:HOIP_0039782 The change in morphology and behavior of a mature or immature cytotoxic T cell resulting from exposure to an antigen for which its T cell receptor is specific bound to an MHC molecule on an antigen presenting cell, leading to the initiation or perpetuation of an immune response. This process can constitute the course of coronavirus infectious disease (homeostatic balance). Cytotoxic T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell in coronavirus infectious disease (homeostatic balance) HOIP_0039782 HOIP:HOIP_0039783 The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). T cell mediated cytotoxicity in coronavirus infectious disease (homeostatic balance) HOIP_0039783 HOIP:HOIP_0039784 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a cytotoxic T cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). cytotoxic T cell degranulation in coronavirus infectious disease (homeostatic balance) HOIP_0039784 HOIP:HOIP_0039785 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). cell death in coronavirus infectious disease (homeostatic balance) HOIP_0039785 HOIP:HOIP_0039786 Any apoptotic process in a cytotoxic T cell. This process can constitute the course of coronavirus infectious disease (homeostatic balance). cytotoxic T cell apoptotic process in coronavirus infectious disease (homeostatic balance) HOIP_0039786 HOIP:HOIP_0039787 Any process involved in the carrying out of an immune response by a T cell. This entity is a specific course-dependent process. This process canThis process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33123165 T cell mediated immunity in coronavirus infectious disease (homeostatic balance) HOIP_0039787 PMID:33123165 Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0039788 The process in which a relatively unspecialized T cell acquires specialized features of a cytotoxic T cell. This process can constitute the course of coronavirus infectious disease (homeostatic balance). cytotoxic T cell differentiation in coronavirus infectious disease (homeostatic balance) HOIP_0039788 HOIP:HOIP_0039789 The change in morphology and behavior of a cytotoxic T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). cytotoxic T cell degranulation in coronavirus infectious disease (homeostatic balance) HOIP_0039789 HOIP:HOIP_0039790 Removing infected cell in adaptive immunity is a subtype of removing infected cell: A process that takes a infected cell from an organism or tissue in the adaptive immune responses. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). removing infected cell in adaptive immunityin coronavirus infectious disease (homeostatic balance) HOIP_0039790 HOIP:HOIP_0039791 The change in morphology and behavior of a mature or immature B cell during an immune response, resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). B cell activation involved in adaptive immune response in coronavirus infectious disease (homeostatic balance) HOIP_0039791 HOIP:HOIP_0039792 The switching of activated B cells from IgM biosynthesis to biosynthesis of an IgG isotype, accomplished through a recombination process involving an intrachromosomal deletion between switch regions that reside 5' of the IgM and one of the IgG constant region gene segments in the immunoglobulin heavy chain locus. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33123165 isotype switching to IgG isotypes in coronavirus infectious disease (homeostatic balance) HOIP_0039792 PMID:33123165 Importantly, class-switched IgG memory B cells to S and RBD have been demonstrated in COVID-19 patients confirming the generation of B cell memory which can provide a rapid recall response on subsequent SARS-CoV- 2 exposure. HOIP:HOIP_0039793 The appearance of IgG antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:32967006 IgG antibody production in coronavirus infectious disease (homeostatic balance) HOIP_0039793 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. HOIP:HOIP_0039794 Any process involved with the carrying out of an immune response by a B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33123165 B cell mediated immunity in coronavirus infectious disease (homeostatic balance) HOIP_0039794 PMID:33123165 Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0039795 Any process involved with the carrying out of an immune response by a memory B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33270381 memory B cell mediated immunity in coronavirus infectious disease (homeostatic balance) HOIP_0039795 PMID:33270381 Natural infection produces variable antibody longevity and may induce robust memory B-cell responses despite low plasma neutralizing activity. HOIP:HOIP_0039796 The process in which a B cell acquires the specialized features of a memory B cell. Memory B cells are cells that can respond rapidly to antigen re-exposure by production of high-affinity antibody. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33123165 memory B cell differentiation in coronavirus infectious disease (homeostatic balance) HOIP_0039796 PMID:33123165 Importantly, class-switched IgG memory B cells to S and RBD have been demonstrated in COVID-19 patients confirming the generation of B cell memory which can provide a rapid recall response on subsequent SARS-CoV- 2 exposure. HOIP:HOIP_0039797 The inhibition of an antigen's biological effects by antibody binding to it. An example is neutralization of diphtheria toxin by preventing its entry into human cells via the binding of antibody specific for diphtheria toxin. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). immunoglobulin-mediated neutralization in coronavirus infectious disease (homeostatic balance) HOIP_0039797 HOIP:HOIP_0039798 The appearance of immunoglobulin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of coronavirus infectious disease (homeostatic balance). immunoglobulin production in coronavirus infectious disease (homeostatic balance) HOIP_0039798 HOIP:HOIP_0039799 The appearance of IgM antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. IgM antibody production HOIP_0039799 HOIP:HOIP_0039800 The appearance of IgG antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:32967006 IgM antibody production in coronavirus infectious disease (homeostatic balance) HOIP_0039800 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. HOIP:HOIP_0039801 The appearance of IgG antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:32967006 IgA antibody production in coronavirus infectious disease (homeostatic balance) HOIP_0039801 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. HOIP:HOIP_0039802 An immune response mediated through a body fluid. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). humoral immune response in coronavirus infectious disease (homeostatic balance) HOIP_0039802 HOIP:HOIP_0039803 An immune response mediated through cells. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). cellular immune response in coronavirus infectious disease (homeostatic balance) HOIP_0039803 HOIP:HOIP_0039804 Positive regulation of an adaptive immune response mediated via cytokine production by helper T cell. This entity is a specific course-dependent process. This process can constituThis process can constitute the course of coronavirus infectious disease (homeostatic balance). helper T cell enhancement of adaptive immune respons in coronavirus infectious disease (homeostatic balance) HOIP_0039804 HOIP:HOIP_0039805 An immune response which is associated with resistance to intracellular bacteria, fungi, and protozoa, and pathological conditions such as arthritis, and which is typically orchestrated by the production of particular cytokines by T-helper 1 cells, most notably interferon-gamma, IL-2, and lymphotoxin. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). T-helper 1 type immune response in coronavirus infectious disease (homeostatic balance) HOIP_0039805 HOIP:HOIP_0039806 Any process that contributes to cytokine production by a T-helper 1 cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). T-helper 1 cell cytokine production in coronavirus infectious disease (homeostatic balance) HOIP_0039806 HOIP:HOIP_0039807 Any process that activates or increases the frequency, rate or extent of cytotoxic T cell activation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). positive regulation of cytotoxic T cell activation in coronavirus infectious disease (homeostatic balance) HOIP_0039807 HOIP:HOIP_0039808 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 1 (Th1) cell. A Th1 cell is a CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive and produces interferon-gamma. This process can constitute the course of coronavirus infectious disease (homeostatic balance). T-helper 1 cell differentiation in coronavirus infectious disease (homeostatic balance) HOIP_0039808 HOIP:HOIP_0039809 The process in which an antigen-presenting cell expresses antigen (peptide or polysaccharide) on its cell surface in association with an MHC class II protein complex. This process can constitute the course of coronavirus infectious disease (homeostatic balance). antigen processing and presentation of exogenous peptide antigen via MHC class II in coronavirus infectious disease (homeostatic balance) HOIP_0039809 HOIP:HOIP_0039810 The process in which a relatively unspecialized T cell acquires specialized features of a T-helper 2 (Th2) cell. A Th2 cell is a CD4-positive, alpha-beta T cell that has the phenotype GATA-3-positive and produces interleukin-4. This process can constitute the course of coronavirus infectious disease (homeostatic balance). T-helper 2 cell differentiation in coronavirus infectious disease (homeostatic balance) HOIP_0039810 HOIP:HOIP_0039811 The process in which a relatively unspecialized thymocyte acquires specialized features of a T-helper cell. This process can constitute the course of coronavirus infectious disease (homeostatic balance). Helper T cells exist in two broad classes. T cells (Th1) are associated with the cell-killing and inflammatory responses of the immune system, including an important role of the activation of macrophages. Th2 cells activate B cells and the general serological (antibody) response. T-helper cell differentiation in coronavirus infectious disease (homeostatic balance) HOIP_0039811 HOIP:HOIP_0039812 The change in morphology and behavior of a T-helper 1 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33123165 T-helper 1 cell activation in coronavirus infectious disease (homeostatic balance) HOIP_0039812 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0039813 The change in morphology and behavior of a T helper 2 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33123165 T-helper 2 cell activation in coronavirus infectious disease (homeostatic balance) HOIP_0039813 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0039814 Any process that contributes to cytokine production by a T-helper 2 cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). T-helper 2 cell cytokine production in coronavirus infectious disease (homeostatic balance) HOIP_0039814 HOIP:HOIP_0039815 An immune response which is associated with resistance to extracellular organisms such as helminths and pathological conditions such as allergy, which is orchestrated by the production of particular cytokines, most notably IL-4, IL-5, IL-10, and IL-13, by any of a variety of cell types including T-helper 2 cells, eosinophils, basophils, mast cells, and nuocytes, resulting in enhanced production of certain antibody isotypes and other effects. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). T-helper 2 type immune response in coronavirus infectious disease (homeostatic balance) HOIP_0039815 HOIP:HOIP_0039816 Any process that activates or increases the frequency, rate or extent of B cell activation. This process can constitute the course of coronavirus infectious disease (homeostatic balance). positive regulation of B cell activation in coronavirus infectious disease (homeostatic balance) HOIP_0039816 HOIP:HOIP_0039817 An immune response mediated by immunoglobulins, whether cell-bound or in solution. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:32967006 immunoglobulin mediated immune response in coronavirus infectious disease (homeostatic balance) HOIP_0039817 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. HOIP:HOIP_0039818 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class I. This process can constitute the course of COVID-19 (homeostatic balance). positive regulation of MHC class I biosynthetic process in COVID-19 (homeostatic balance) HOIP_0039818 HOIP:HOIP_0039819 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. ISBN:0815341504 cellular response to type I interferon in coronavirus infectious disease (homeostatic balance) HOIP_0039819 ISBN:0815341504 ISBN:0815341504 Table 4.3 Although interferons are highly potent at blocking SARS-CoV-2 replication, SARS-CoV-2 has an arsenal of evasion mechanisms to block the induction of endogenous interferons and interferon receptor signalling. This reduced early interferon response can lead to imbalanced host immune responses and to an inability to clear the virus. Ultimately, this leads to the prolonged increased levels of interferons and interferon-stimulated genes that have been observed in severe COVID-19 in many studies although not in others. Furthermore, an increased level of IFNα is a biomarker for mortality. These results suggest pathological roles of delayed and prolonged type I and type III interferon responses in COVID-19. PMID:33723416 In general, type I IFN production is thought to restrict SARS-CoV, MERS-CoV, SARS-CoV-2, and MHV infection in human and murine models. Indeed, mice deficient in key mediators of type I IFN production (Tlr7 -/-, Myd88 -/-, or Mda5 -/- mice) show more severe disease following MERS-CoV or MHV infection compared with WT mice; this increased disease severity may be due to the reduced type I IFN production and elevated concentrations of proinflammatory cytokines. During infection with SARS-CoV MA15, rapid viral replication in WT mice delays type I IFN signaling but orchestrates a robust proinflammatory cytokine response, including the induction of TNF and IL-6, which promotes lung immunopathology with diminished survival. PMID:33153908 SARS-CoV-1 studies have demonstrated that delayed IFN-I signaling and inflammatory monocytes-macrophages promote lung cytokine and chemokine levels, vascular leakage, and impaired antigen-specific T cell responses, culminating in lethal disease (Channappanavar et al., 2016). The role played by prominent IFN-producing pDCs in SARS-CoV-2 control or pathogenesis warrants investigation, as they have been shown to be critical in murine CoV (MHV) control. PMID:32505227 TLR- and RLR-mediated signaling lead to the secretion of type I interferons (IFNs), which stimulate the expression of IFN-stimulated genes (ISGs) by infected and neighboring cells, inducing an antiviral state. PMID:33153908 HOIP:HOIP_0039820 type I interferon production The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:25301932 type I interferon production in coronavirus infectious disease (homeostatic balance) HOIP_0039820 HOIP:HOIP_0039821 Type I interferon signaling is a subtype of biological signaling: A process transduced by the binding of a type I interferon to a receptor on the surface of a cell. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). reactome:R-HSA-909729.3 type I interferon signaling in coronavirus infectious disease (homeostatic balance) HOIP_0039821 HOIP:HOIP_0039822 TLR7 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 7. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33674759 TLR7 signaling in coronavirus infectious disease (homeostatic balance) HOIP_0039822 PMID:33674759 Endosomal Toll-like receptors (TLR7) bind to ssRNA in the endosome, while components of the inflammasome such as MDA5, RIG-I, NOD2 and PKR bind to ssRNA and dsRNA in the cytosol, resulting in cellular activation, and production of type I interferon and multiple inflammatory mediators. HOIP:HOIP_0039823 IRF7 activation is a subtype of molecular activation: A process that changes the activity of the IRF7 to be higher. This process can constitute the course of coronavirus infectious disease (homeostatic balance). IRF7 activation in coronavirus infectious disease (homeostatic balance) HOIP_0039823 HOIP:HOIP_0039824 TLR signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor. This process can constitute the course of coronavirus infectious disease (homeostatic balance). TLR signaling in coronavirus infectious disease (homeostatic balance) HOIP_0039824 HOIP:HOIP_0039825 TLR3 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 3. PMID:33674759 TLR3 signaling in coronavirus infectious disease (homeostatic balance) HOIP_0039825 PMID:33674759 Endosomal Toll-like receptors (TLR3 and TLR7) bind to ssRNA in the endosome, while components of the inflammasome such as MDA5, RIG-I, NOD2 and PKR bind to ssRNA and dsRNA in the cytosol, resulting in cellular activation, and production of type I interferon and multiple inflammatory mediators. HOIP:HOIP_0039826 IRF3 activation is a subtype of molecular activation: A process that changes the activity of the IRF3 to be higher. This process can constitute the course of coronavirus infectious disease (homeostatic balance). IRF3 activation in coronavirus infectious disease (homeostatic balance) HOIP_0039826 HOIP:HOIP_0039827 TBK1 activation is a subtype of molecular activation: A process that changes the activity of the TBK1 to be higher. This process can constitute the course of coronavirus infectious disease (homeostatic balance). TBK1 activation in coronavirus infectious disease (homeostatic balance) HOIP_0039827 HOIP:HOIP_0039828 MAVS complex assembly is a subtype of protein complex assembly: A process that forms a complex consisting of MAVS. This process can constitute the course of coronavirus infectious disease (homeostatic balance). MAVS complex assembly in coronavirus infectious disease (homeostatic balance) HOIP_0039828 HOIP:HOIP_0039829 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:32505227 RIG-I signaling in coronavirus infectious disease (homeostatic balance) HOIP_0039829 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of pattern recognition receptors (PRRs) by viral single-stranded RNA(ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). HOIP:HOIP_0039830 Any processes of signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:32505227 cytoplasmic pattern recognition receptor signaling in response to virus in coronavirus infectious disease (homeostatic balance) HOIP_0039830 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of patternrecognition receptors (PRRs) by viral single-stranded RNA (ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). HOIP:HOIP_0039831 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:32505227 MDA-5 signaling in coronavirus infectious disease (homeostatic balance) HOIP_0039831 HOIP:HOIP_0039832 TLR8 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 8. This process can constitute the course of coronavirus infectious disease (homeostatic balance). TLR8 signaling in coronavirus infectious disease (homeostatic balance) HOIP_0039832 HOIP:HOIP_0039833 Any processes of molecular signals generated as a consequence of a pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species, or damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. This process can constitute the course of coronavirus infectious disease (homeostatic balance). pattern recognition receptor signaling in response to virus in coronavirus infectious disease (homeostatic balance) HOIP_0039833 HOIP:HOIP_0039834 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). production of molecular mediator of immune response in coronavirus infectious disease (homeostatic balance) HOIP_0039834 HOIP:HOIP_0039835 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). production of molecular mediator of innate immune response in coronavirus infectious disease (homeostatic balance) HOIP_0039835 HOIP:HOIP_0039836 Infected cell damage is a subtype of damaging: A process that injuries the structure of the infected cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). infected cell damagein coronavirus infectious disease (homeostatic balance) HOIP_0039836 HOIP:HOIP_0039837 The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). PMID:33123165 natural killer cell mediated cytotoxicity in coronavirus infectious disease (homeostatic balance) HOIP_0039837 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039838 The promotion of an immune response by natural killer cells through direct recognition of target cells or through the release of cytokines. This process can constitute the course of coronavirus infectious disease (homeostatic balance). NK cell mediated immunity natural killer cell mediated immunity in coronavirus infectious disease (homeostatic balance) HOIP_0039838 HOIP:HOIP_0039839 The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). natural killer cell activation in coronavirus infectious disease (homeostatic balance) HOIP_0039839 HOIP:HOIP_0039840 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a natural killer cell. This process can constitute the course of coronavirus infectious disease (homeostatic balance). natural killer cell degranulation in coronavirus infectious disease (homeostatic balance) HOIP_0039840 HOIP:HOIP_0039841 A molecular signal induced by NK cells which triggers the apoptotic death of a cell. This process can constitute the course of coronavirus infectious disease (homeostatic balance). natural killer cell-mediated apoptotic process of infected cells in coronavirus infectious disease (homeostatic balance) HOIP_0039841 HOIP:HOIP_0039842 Any process that contributes to cytokine production by a natural killer cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). natural killer cell cytokine production in coronavirus infectious disease (homeostatic balance) HOIP_0039842 HOIP:HOIP_0039843 interferon-gamma production The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This process can constitute the course of coronavirus infectious disease (homeostatic balance). interferon-gamma production in coronavirus infectious disease (homeostatic balance) HOIP_0039843 HOIP:HOIP_0039844 The destruction of infected cellin the early infectious stage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). early infected cell destruction in coronavirus infectious disease (homeostatic balance) HOIP_0039844 HOIP:HOIP_0039845 The directed killing of a target cell by a neutrophil. This process can constitute the course of coronavirus infectious disease (homeostatic balance). neutrophil mediated cytotoxicity in coronavirus infectious disease (homeostatic balance) HOIP_0039845 HOIP:HOIP_0039846 The controlled release of lysosomal enzymes by a cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). Wikipedia:Inflammation secretion of lysosomal enzymes involved in inflammatory response in coronavirus infectious disease (homeostatic balance) HOIP_0039846 Wikipedia:Inflammation leukotriene B4: 'Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0039847 Receiving signal in pattern recognition receptor signaling pathway is a subtype of receiving signal: A process that recognizes the pathogen-associated molecular pattern (PAMPs) and changes into a signal in a pattern recognition receptor signaling pathway. This process can constitute the course of coronavirus infectious disease (homeostatic balance). receiving viral signal in pattern recognition signaling pathway in coronavirus infectious disease (homeostatic balance) HOIP_0039847 HOIP:HOIP_0039848 Interaction between host pattern recognition receptor and any PAMPs (pathogen-associated molecular patterns). This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). Wikipedia:Inflammation binding of pattern recognition receptor to PAMPs in coronavirus infectious disease (homeostatic balance) HOIP_0039848 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0039849 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). production of molecular mediator of immune response in COVID-19 (homeostatic balance) HOIP_0039849 HOIP:HOIP_0039850 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). production of molecular mediator of innate immune response in COVID-19 (homeostatic balance) HOIP_0039850 HOIP:HOIP_0039851 The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). type I interferon production in COVID-19 (homeostatic balance) HOIP_0039851 HOIP:HOIP_0039852 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. This entity is a specific course-dependent process.This process can constitute the course of COVID-19 (homeostatic balance). cellular response to type I interferon in COVID-19 (homeostatic balance) HOIP_0039852 HOIP:HOIP_0039853 Any process that stops, prevents, or reduces the frequency, rate or extent of viral translation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease (homeostatic balance). negative regulation of viral translation in coronavirus infectious disease (homeostatic balance) HOIP_0039853 HOIP:HOIP_0039854 Any process that stops, prevents, or reduces the frequency, rate or extent of viral translation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). negative regulation of viral translation in COVID-19 (homeostatic balance) HOIP_0039854 HOIP:HOIP_0039855 Any processes of molecular signals generated as a consequence of a pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species, or damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. This process can constitute the course of COVID-19 (homeostatic balance). pattern recognition receptor signaling in response to virus in COVID-19 (homeostatic balance) HOIP_0039855 HOIP:HOIP_0039856 TLR signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor. This process can constitute the course of COVID-19 (homeostatic balance). TLR signaling in COVID-19 (homeostatic balance) HOIP_0039856 HOIP:HOIP_0039857 TLR7 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 7. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33674759 TLR7 signaling in COVID-19 (homeostatic balance) HOIP_0039857 PMID:33674759 RNA sensors such as Toll-like receptor 7 (TLR7) and MDA5 are triggered by the mRNA vaccines, and TLR9 is the major double-stranded DNA sensor for the AdV vaccine. The resultant activated DCs present antigen and co-stimulatory molecules to S protein-specific naive T cells, which become activated and differentiated into effector cells to form cytotoxic T lymphocytes or helper T cells. T follicular helper (TFH) cells help S protein-specific B cells to differentiate into antibody-secreting plasma cells and promote the production of high affinity anti-S protein antibodies. Following vaccination, S protein-specific memory T cells and B cells develop and circulate along with high affinity SARS-CoV-2 antibodies, which together help prevent subsequent infection with SARS-CoV-2. TCR, T cell receptor. HOIP:HOIP_0039858 IRF7 activation is a subtype of molecular activation: A process that changes the activity of the IRF7 to be higher. This process can constitute the course of COVID-19 (homeostatic balance). IRF7 activation in COVID-19 (homeostatic balance) HOIP_0039858 HOIP:HOIP_0039859 TLR8 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 8. This process can constitute the course of COVID-19 (homeostatic balance). TLR8 signaling in COVID-19 (homeostatic balance) HOIP_0039859 HOIP:HOIP_0039860 TLR3 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 3. This process can constitute the course of COVID-19 (homeostatic balance). TLR3 signaling in COVID-19 (homeostatic balance) HOIP_0039860 HOIP:HOIP_0039861 TBK1 activation is a subtype of molecular activation: A process that changes the activity of the TBK1 to be higher. This process can constitute the course of COVID-19 (homeostatic balance). TBK1 activation in COVID-19 (homeostatic balance) HOIP_0039861 HOIP:HOIP_0039862 IRF3 activation is a subtype of molecular activation: A process that changes the activity of the IRF3 to be higher. This process can constitute the course of COVID-19 (homeostatic balance). IRF3 activation in COVID-19 (homeostatic balance) HOIP_0039862 HOIP:HOIP_0039863 Receiving signal in pattern recognition receptor signaling pathway is a subtype of receiving signal: A process that recognizes the pathogen-associated molecular pattern (PAMPs) and changes into a signal in a pattern recognition receptor signaling pathway. This process can constitute the course of COVID-19 (homeostatic balance). receiving viral signal in pattern recognition signaling pathway in COVID-19 (homeostatic balance) HOIP_0039863 HOIP:HOIP_0039864 Interaction between host pattern recognition receptor and any PAMPs (pathogen-associated molecular patterns). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). Wikipedia:Inflammation binding of pattern recognition receptor to PAMPs in COVID-19 (homeostatic balance) HOIP_0039864 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0039865 Any processes of signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32505227 Wikipedia:Inflammation cytoplasmic cytoplasmic pattern recognition receptor signaling in response to virus in COVID-19 (homeostatic balance) HOIP_0039865 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of patternrecognition receptors (PRRs) by viral single-stranded RNA (ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0039866 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32505227 MDA-5 signaling in COVID-19 (homeostatic balance) HOIP_0039866 HOIP:HOIP_0039867 Any processes of signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32505227 RIG-I signaling in COVID-19 (homeostatic balance) HOIP_0039867 PMID:32505227 In the case of RNA viruses such as SARS-CoV-2, these pathways are initiated through the engagement of pattern recognition receptors (PRRs) by viral single-stranded RNA(ssRNA) and double-stranded RNA (dsRNA) via cytosolic RIG-I like receptors (RLRs) and extracellular and endosomal Toll-like receptors (TLRs). HOIP:HOIP_0039868 The destruction of infected cells in the early infectious stage. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). early infected cell destruction in COVID-19 (homeostatic balance) HOIP_0039868 HOIP:HOIP_0039869 The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 natural killer cell mediated cytotoxicity in COVID-19 (homeostatic balance) HOIP_0039869 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039870 The promotion of an immune response by natural killer cells through direct recognition of target cells or through the release of cytokines. This process can constitute the course of COVID-19 (homeostatic balance). NK cell mediated immunity natural killer cell mediated immunity in COVID-19 (homeostatic balance) HOIP_0039870 HOIP:HOIP_0039871 Any process that contributes to cytokine production by a natural killer cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). natural killer cell cytokine production in COVID-19 (homeostatic balance) HOIP_0039871 HOIP:HOIP_0039872 The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). natural killer cell activation in COVID-19 (homeostatic balance) HOIP_0039872 HOIP:HOIP_0039873 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a natural killer cell. This process can constitute the course of COVID-19 (homeostatic balance). natural killer cell degranulation in COVID-19 (homeostatic balance) HOIP_0039873 HOIP:HOIP_0039874 A molecular signal induced by NK cells which triggers the apoptotic death of a cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). natural killer cell-mediated apoptotic process of infected cells in COVID-19 (homeostatic balance) HOIP_0039874 HOIP:HOIP_0039875 MAVS complex assembly is a subtype of protein complex assembly: A process that forms a complex consisting of MAVS. This process can constitute the course of COVID-19 (homeostatic balance). MAVS complex assembly in COVID-19 (homeostatic balance) HOIP_0039875 HOIP:HOIP_0039876 Type I interferon signaling is a subtype of biological signaling: A process transduced by the binding of a type I interferon to a receptor on the surface of a cell. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. early type I interferon signaling in COVID-19 (homeostatic balance) HOIP_0039876 HOIP:HOIP_0039877 The synthesis or release of any molecular mediator of the inflammatory response following an inflammatory stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation synthesis or release of inflammatory mediator in mild COVID-19 HOIP_0039877 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039878 The regulated release of histamine by a cell as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation histamine secretion involved in inflammatory response in mild COVID-19 HOIP_0039878 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Redness and heat are due to increased blood flow at body core temperature to the inflamed site; swelling is caused by accumulation of fluid; pain is due to the release of chemicals such as bradykinin and histamine that stimulate nerve endings. Histamine: Stored in preformed granules, histamine is released in response to a number of stimuli. It causes arteriole dilation, increased venous permeability, and a wide variety of organ-specific effects. HOIP:HOIP_0039879 Hypofunction of sperm entry into oocytel is a subtype of hypofunction of moving A to the inside of B: A process that performs a decreased or insufficient sperm entry into oocyte . hypofunction of sperm entry into oocyte HOIP_0039879 HOIP:HOIP_0039880 A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. smooth muscle contraction in mild COVID-19 HOIP_0039880 HOIP:HOIP_0039881 Any process that results in a change in state or activity of a cell as a result of a stimulus of pain sensation. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation response to pain sensation stimulus in mild COVID-19 HOIP_0039881 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039882 Increasing vascular lumen area is a subtype of increasing area: A process that changes the area of the vascular lumen area to be larger. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation Vasodilation 血管拡張 increasing vascular lumen area in mild COVID-19 HOIP_0039882 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039883 Increasing blood flow is a subtype of increaseing flow: A process that changes the amount of blood flow to be higher. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation increasing blood flow in mild COVID-19 HOIP_0039883 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039884 Increasing temperature is a subtype of changing temperature: A process that increases the temperature of the object. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation heat increasing temperature in mild COVID-19 HOIP_0039884 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039885 Increasing vascular permeabilization is a subtype of changing permeability: A process that changes the permeability of the vascular to be higher. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. PMID:33077917 Wikipedia:Inflammation increasing vascular permeabilization in mild COVID-19 HOIP_0039885 PMID:33077917 Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039886 Leaking fluid from blood vessel is a subtype of leaking: A process that leaks fluid out from the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. leaking fluid from blood vessel in COVID-19 (homeostatic balance) HOIP_0039886 HOIP:HOIP_0039887 The release of bradykinin following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation bradykinin secretion involved in inflammatory response in mild COVID-19 HOIP_0039887 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Bradykinin: A vasoactive protein that is able to induce vasodilation, increase vascular permeability, cause smooth muscle contraction, and induce pain. HOIP:HOIP_0039888 The regulated release of a prostaglandin that contributes to the immune response. Prostaglandins are a group of biologically active metabolites which contain a cyclopentane ring. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation prostaglandin secretion involved in inflammatory response in mild COVID-19 HOIP_0039888 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0039889 Any process that activates or increases the frequency, rate, or extent of fever generation. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation positive regulation of fever generation in mild COVID-19 HOIP_0039889 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0039890 Increasing body temperature is a subtype of increaseing temperature: A process that increases the temperature of the body. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation increasing body temperature in mild COVID-19 HOIP_0039890 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0039891 The release of any leukotriene following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. Wikipedia:Inflammation leukotriene secretion involved in inflammatory response in mild COVID-19 HOIP_0039891 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. leukotriene B4: Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0039892 Hypofunction of IgA antibody production is a subtype of hypofunction of protein synthesis: A process that performs a decreased or insufficient IgA antibody production. hypofunction of IgA antibody production HOIP_0039892 HOIP:HOIP_0039893 The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This process can constitute the course of mild COVID-19. PMID:32697943 PMID:32702298 PMID:32702299 PMID:32998157 PMID:33053279 PMID:33123165 https://doi.org/10.1101/2020.07.17.20140533 interferon-gamma production in mild COVID-19 HOIP_0039893 PMID:32697943 Similarly, CM-CoV-2 decreased IFN-g production by CD4 T cells, and this was reversed in CM-BAY87 and CM-MitoQ and appeared to be reversed in CM-aIL-1b (Figures 4B and S4J). PMID:32702298 We did a phase 1/2, single-blind, randomised controlled trial in five trial sites in the UK of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein compared with a meningococcal conjugate vaccine (MenACWY) as control. Interferon-gamma ELISpot responses against SARS-CoV-2 spike peptides peaked at 856 spot-forming cells per million peripheral blood mononuclear cells (IQR 493–1802; n=43) at day 14, declining to 424 (221–799; n=43) by day 56 after vaccination (figure 6). PMID:32702299 Ad5-vectored COVID-19 vaccine induced significant SARS-CoV-2 spike glycoprotein-specific IFNgamma-ELISpot responses in 227 (90%, 95% CI 85–93) of 253 participants receiving the 1×1011 viral particles dose, and 113 (88%, 81–92) of 129 partici- pants receiving the 5 × 1010 viral particles dose at day 28 (figure 3). PMID:32998157 Interferon-gamma was produced by a large fraction of RBD-specific CD8+ and CD4+ T cells. The robust RBD-specific antibody, T cell and favourable cytokine responses induced by the BNT162b1 mRNA vaccine suggest that it has the potential to protect against COVID-19 through multiple beneficial mechanisms. RBD-specific CD4+ T cells secreted IFNgamma, IL-2, or both, but in most individuals they did not secrete IL-4 (Fig. 4 a–c, Extended Data Table 6). Similarly, fractions of RBD-specific CD8+ T cells secreted IFNgamma+ and IL-2. PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. PMID:33123165 Intracellular staining confirmed production of IFN-γ, tumor necrosis factor (TNF) and interleukin-2 (IL-2) by both CD4+ and CD8+ T cells following Ad5-nCoV immunization, with more cytokine detected in CD4+ T cells as compared to CD8+ T cells. T cell responses measured in 16 participants showed that NVX-CoV2373/Matrix-M1 induces antigen-specific polyfunctional CD4+ T cell responses (IFN-γ, IL-2, and TNF- α) in response to spike protein stimulation; there was a strong bias toward this Th1 phenotype. Both vaccine (Ad5-nCoV, ChAdOx1 nCoV-19) constructs elicited T cell responses which peaked at 14 days post-immunization, as determined by interferon- gamma (IFN-γ) enzyme linked immunospot (ELISpot) assay. T cell responses measured by intracellular staining for Th1 (TNF, IL-2, IFN-γ) and Th2 (IL-4, IL-13) cytokines following stimulation with an S protein peptide pool showed a Th1 cytokine bias and low-level CD8 T cell responses. (mRNA-1273) https://doi.org/10.1101/2020.07.17.20140533 Interferon (IFN)gamma was produced by a high fraction of RBD-specific CD8+ and CD4+ T cells. RBD-specific CD4+ T cells secreted IFNgamma, IL-2, or both, but did not secrete IL-4 (Figure 4a-c). Similarly, fractions of RBD-specific CD8+ T cells secreted IFNgamma and IL-2. IFNgamma is a key cytokine for several antiviral responses. It acts in synergy with type I interferons to inhibit replication of SARS-CoV-2. HOIP:HOIP_0039894 Hypofunction of negative regulation of viral action is is a subtype of hypofunctioning of controlling: A process that performs a decreased or insufficient negative regulation of viral action. hypofunction of negative regulation of viral action HOIP_0039894 HOIP:HOIP_0039895 The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of mild COVID-19. PMID:33123165 natural killer cell mediated cytotoxicity in mild COVID-19 HOIP_0039895 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039896 Any biological process that results in permanent cessation of all vital functions of an infected cell. This process can constitute the course of mild COVID-19. infected cell death in mild COVID-19 HOIP_0039896 HOIP:HOIP_0039897 Viral entry-innate immune response balance is a subtype of maiintaining balance: A process that keeps a balance between the viral entry and the innate immune response as biological defence response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. viral entry-innate immune response balance in COVID-19 vaccination HOIP_0039897 HOIP:HOIP_0039898 Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon signaling pathway. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. PMID:32726803 PMID:33188364 negative regulation of type I interferon signaling pathway in the early stage in inapparent COVID-19 HOIP_0039898 PMID:32726803 Having demonstrated a role for expression of SCoV2-PLpro and SCoV-PLpro in attenuating host antiviral IFN pathways, we anticipated that inhibition by GRL-0617 would reverse this process. Moreover, phosphorylation of IRF3 and TBK1, markers for IFN pathway activation, and p65 phosphorylation, used to monitor NF-κB pathway activation, were increased in SARS-CoV-2-infected cells upon GRL-0617 treatment (Fig. 5f). Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). Consistent with these observations, a recent study has shown that SARS-CoV-2 infection in animal models and in human patients with COVID-19 is correlated with low IFN type I and type III responses. PMID:33188364 In addition, an integrated analysis showed that patients with severe COVID-19 have a highly impaired interferon type I response with low IFNα activity in the blood, indicating high blood viral load, and an impaired inflammatory response. HOIP:HOIP_0039899 Negative regulation of IFN-responsive gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFN-responsive gene expression. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. PMID:32726803 negative regulation of early IFN-responsive gene expression in inapparent COVID-19 HOIP_0039899 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0039900 A change in morphology and behavior of an inflammatory cell resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. inflammatory cell activation (very high) in moderate COVID-19 HOIP_0039900 HOIP:HOIP_0039901 The directed killing of a target cell by an inflammatory cell. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32887954 inflammtory cell mediated cytotoxicity (high) in moderate COVID-19 HOIP_0039901 PMID:32887954 Furthermore, patients with symptomatic COVID-19 are reported to produce IgG anti-bodies with reduced fucosylation levels, which in turn promotes their interaction with activating FcgammaRIIIa. Fc-mediated effector functions: immune functions that are mediated through the interaction of the constant Fc region of antibodies with innate immune molecules, complement proteins and specialized Fc receptors expressed by innate immune cells. The resulting functions include complement-dependent cytotoxicity and antibody-dependent cellular phagocytosis or cell-mediated cytotoxicity. HOIP:HOIP_0039902 The directed killing of a target cell by a neutrophil. This process can constitute the course of moderate COVID-19. PMID:28792873 neutrophil mediated cytotoxicity (high) in moderate COVID-19 HOIP_0039902 HOIP:HOIP_0039903 The controlled release of lysosomal enzymes by a cell. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. Wikipedia:Inflammation secretion of lysosomal enzymes involved in inflammatory response (high) in moderate COVID-19 HOIP_0039903 Wikipedia:Inflammation leukotriene B4: 'Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0039904 The directed killing of adjacent infected cells by a neutrophil. This process can constitute the course of moderate COVID-19. PMID:28792873 neutrophil mediated cytotoxicity to adjacent infected cells in moderate COVID-19 HOIP_0039904 HOIP:HOIP_0039905 A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. PMID:32629875 macrophage activation involved in inflammatory response (high) in moderate COVID-19 HOIP_0039905 TH1 cells activate macrophages to become highly microbicidal. Activated macrophages increase their expression of CD40 and of TNF receptors, and secrete TNF-α. This autocrine stimulus synergizes with IFN-γ secreted by TH1 cells to increase the antimicrobial action of the macrophage, in particular by inducing the production of nitric oxide (NO) and oxygen radicals (O2•). The macrophage also upregulates its B7 molecules in response to binding to CD40 ligand on the T cell, and increases its expression of MHC class II molecules, thus allowing further activation of resting CD4 T cells. https://www.ncbi.nlm.nih.gov/books/NBK27153/ PMID:32629875 Monocyte/macrophage-lineage cells, a major cell source of many pro-inflammatory cytokines, are numerically increased and phenotypically activated in many tissues of patients with severe COVID-19. HOIP:HOIP_0039906 A vesicle-mediated transport process that results in the engulfment of external particulate material by macrophages. This process can constitute the course of moderate COVID-19. phagocytosis by inflammatory macrophage in moderate COVID-19 HOIP_0039906 HOIP:HOIP_0039907 The appearance of interleukin-8 due to biosynthesis or secretion by inflammatory macrophages following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of moderate COVID-19. inflammatory macrophage CXCL8 production inflammatory macrophage interleukin-8 production in moderate COVID-19 HOIP_0039907 HOIP:HOIP_0039908 CXCL8 signaling is a process that a signal is transmitted by CXCL8. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. CXCL8 signaling (high) in moderate COVID-19 HOIP_0039908 HOIP:HOIP_0039909 The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33123165 neutrophil chemotaxis (high) in moderate COVID-19 HOIP_0039909 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039910 The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33077917 neutrophil activation involved in inflammatory response (high) in moderate COVID-19 HOIP_0039910 PMID:33077917 Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0039911 A vesicle-mediated transport process that results in the engulfment of external particulate material by neutrophils. This process can constitute the course of moderate COVID-19. phagocytosis by neutrophils in moderate COVID-19 HOIP_0039911 HOIP:HOIP_0039912 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. necrosis in moderate COVID-19 HOIP_0039912 HOIP:HOIP_0039913 Any biological process that results in permanent cessation of all vital functions of a cell. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32629875 PMID:32697943 cell death (high) in moderate COVID-19 HOIP_0039913 PMID:32629875 In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Finally, we demonstrate that CoV-2-infected monocytes promote T cell dysfunction and lung epithelial cell death. This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. Finally, we demonstrate that CoV-2-infected monocytes promote T cell dysfunction and lung epithelial cell death. These data may explain why uncontrolled diabetes may lead to compromised adaptive immune response and lung dysfunction in patients with severe COVID-19 symptoms. HOIP:HOIP_0039914 Tissue damage is a subtype of damaging: A process that injuries the structure of the tissue as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32629875 PMID:33123165 tissue damage (high) in moderate COVID-19 HOIP_0039914 PMID:32629875 As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. HOIP:HOIP_0039915 The directed killing of a target cell by a macrophage. This process can constitute the course of moderate COVID-19. inflammatory macrophage mediated cytotoxicity (high) in moderate COVID-19 HOIP_0039915 HOIP:HOIP_0039916 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32651579 PMID:32843733 antiviral innate immune response (high) in moderate COVID-19 HOIP_0039916 PMID:32651579 Dysregulated immune response and cytokine-release syndrome, due to overactivation of innate immunity in the setting of T cell lymphodepletion, characterize the presentations of severe COVID-19. PMID:32843733 The damaged cells in the lungs elicit a strong innate immune response, which seems to be largely mediated by pro-inflammatory macrophages and granulocytes. This response is thought to be responsible for the cytokine release syndrome or ‘cytokine storm’ that is believed to contribute to ARDS. HOIP:HOIP_0039917 The destruction of infected cells in the early infectious stage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. innate immunity mediated infected cell damage (very high) [COVID-19(severe)] early infected cell destruction (high) in moderate COVID-19 HOIP_0039917 HOIP:HOIP_0039918 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of moderate COVID-19. PMID:33123165 inflammatory cell infiltration (high) in moderate COVID-19 HOIP_0039918 PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0039919 The movement of a leukocyte in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. immune cell chemotaxis leucocyte chemotaxis inflammatory cell chemotaxis (high) in moderate COVID-19 HOIP_0039919 HOIP:HOIP_0039920 The directed movement of a natural killer cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33123165 natural killer cell chemotaxis (high) in moderate COVID-19 HOIP_0039920 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0039921 The movement of a monocyte in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32697943 monocyte chemotaxis (high) in moderate COVID-19 HOIP_0039921 PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell. HOIP:HOIP_0039922 The change in morphology and behavior of a monocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32629875 PMID:32697943 monocyte activation involved in inflammatory response (high) in moderate COVID-19 HOIP_0039922 PMID:32629875 Monocyte/macrophage-lineage cells, a major cell source of many pro-inflammatory cytokines, are numerically increased and phenotypically activated in many tissues of patients with severe COVID-19. PMID:32697943 Glycolysis Is Necessary for SARS-CoV-2 Replication and Monocyte Response Taken together, our results indicate that CoV-2 replication in monocytes and CoV-2-induced monocyte response are sustained by a switch to aerobic glycolysis (the Warburg effect). HOIP:HOIP_0039923 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32307653 PMID:32697943 PMID:33123165 macrophage cell differentiation inflammatory macrophage differentiation (high) in moderate COVID-19 HOIP_0039923 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. ISBN:0781735149 PMID:32307653 Some regions of reactive epithelial hyperplasia had also abundant alveolar macrophages. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32697943 Upon infection, there is an accumulation of immune cells in the lungs, especially macrophages and monocytes. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039924 The synthesis or release of any molecular mediator of the inflammatory response following an inflammatory stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation synthesis or release of inflammatory mediator (high) in moderate COVID-19 HOIP_0039924 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. HOIP:HOIP_0039925 The appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33077917 PMID:33123165 chemokine production (high) in moderate COVID-19 HOIP_0039925 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0039926 Chemokine signaling is a process that a signal is transmitted by the chemokine. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33077917 PMID:33123165 chemokine signaling (high) in moderate COVID-19 HOIP_0039926 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0039927 The regulated release of inflammatory mediators from tissue-resident immune cells. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. Wikipedia:Inflammation release of inflammatory mediator from tissue-resident immune cells (high) in moderate COVID-19 HOIP_0039927 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0039928 The migration of a leukocyte from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33077917 inflammatory cell extravasation (high) in moderate COVOD-19 HOIP_0039928 PMID:33077917 C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma - pathological events that are all observed in severe cases of COVID-19. HOIP:HOIP_0039929 The migration of a monocyte from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32629875 PMID:33123165 monocyte extravasation (high) in moderate COVID-19 HOIP_0039929 PMID:32629875 Monocyte/macrophage-lineage cells, a major cell source of many pro-inflammatory cytokines, are numerically increased and phenotypically activated in many tissues of patients with severe COVID-19. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039930 The migration of a neutrophil from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33077917 neutrophil extravasation (high) in moderate COVID-19 HOIP_0039930 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0039931 Infected cell damage is a subtype of damaging: A process that injuries the structure of the infected cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. infected cell damage (high) in moderate COVID-19 HOIP_0039931 HOIP:HOIP_0039932 Hypofunction of host cell receptor surface binding is a subtype of hypofunction of host cell surface binding: A process that performs a decreased or insufficient host cell surface receptor binding. hypofunction of host cell surface receptor binding HOIP_0039932 HOIP:HOIP_0039933 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. production of molecular mediator of innate immune response in moderate COVID-19 HOIP_0039933 HOIP:HOIP_0039934 Inflammatory cytokine signaling is a process that a signal is transmitted by the inflammatory cytokine. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32629875 PMID:32697943 PMID:33077917 inflammatory cytokine signaling [COVID-19 (moderate] HOIP_0039934 PMID:32629875 The systemic increase of pro-inflammatory cytokines in many patients with severe COVID-19 is likely another major contributor to the vascular pathology in COVID-19 (Section 4.3). PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0039935 Any process involved directly in viral genome replication, including viral nucleotide metabolism. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32641482 viral genome replication in moderate COVID-19 HOIP_0039935 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0039936 A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. viral assembly viral particle assembly virion assembly and maintenance virion organization virus assembly virus particle assembly virion assembly in moderate COVID-19 HOIP_0039936 HOIP:HOIP_0039937 The assembly of a virus capsid from its protein subunits. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. viral capsid assembly in moderate COVID-19 HOIP_0039937 HOIP:HOIP_0039938 The directed movement of a virus, or part of a virus, into, out of, or within a host cell. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. transport of virus in moderate COVID-19 HOIP_0039938 HOIP:HOIP_0039939 The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33077917 viral release from host cell [COVID-19 (moderate)] ウイルス排出 SARS-CoV-2 shedding in COVID-19 (moderate) HOIP_0039939 PMID:33077917 Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0039940 The transport of a virus between adjacent cells in a multicellular organism. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32362314 PMID:32629875 transport of virus in host (cell to cell) in moderate COVID-19 HOIP_0039940 PMID:32362314 Finally, the addition of an arginine residue to the S1/S2 site of SARS-2-S jointly with alanine-to-lysine exchange strongly increased syncytium formation, indicating that viral variants with optimized S1/S2 sites might show augmented cell-cell spread and potentially altered pathogenicity. PMID:32629875 Epidemiologic evidence indicates that the virus is transmitted among close contacts mostly through the respiratory route, presumably directly through infected droplet secretions or indirectly via fomites (Figure 2). The proximity between the infected respiratory epithelium releasing the virus and endothelial cells may favor local transmission. HOIP:HOIP_0039941 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. viral proliferation in moderate COVID-19 HOIP_0039941 HOIP:HOIP_0039942 The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. This process can constitute the course of moderate COVID-19. virion attachment to host cell in moderate COVID-19 HOIP_0039942 HOIP:HOIP_0039943 Viral protein production is a subtype of protein production: A process that produces a virus protein as an output. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. viral protein production in moderate COVID-19 HOIP_0039943 HOIP:HOIP_0039944 Changing symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. symbiotic imbalance between host and virus in moderate COVID-19 HOIP_0039944 HOIP:HOIP_0039945 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. decreasing number of virus in moderate COVID-19 HOIP_0039945 HOIP:HOIP_0039946 adaptive immune response An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). adaptive immune response in moderate COVID-19 HOIP_0039946 HOIP:HOIP_0039947 The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33123165 T cell mediated cytotoxicity (high) in moderate COVID-19 HOIP_0039947 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039948 T cell exhaustion is a dysfunction of T cells, which changes in transcriptional profiles and sustained expression of inhibitory receptors and leads to progressive loss of function,. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33077917 PMID:33123165 T cell exhaustion in moderate COVID-19 HOIP_0039948 PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. PMID:33123165 Severe COVID-19 patients exhibit immunological features associated with T cell anergy or exhaustion. For example, the lungs of severe COVID-19 patients contain high levels of CD8+ T cells expressing classic markers and genes of exhaustion, while patients who have recovered from moderate or severe COVID-19 seem to have robust memory T cell formation. HOIP:HOIP_0039949 The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:33123165 natural killer cell mediated cytotoxicity (very high) in moderate COVID-19 HOIP_0039949 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0039950 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of virion attachment to host cell negative regulation of virion attachment to host cell (high) in moderate COVID-19 HOIP_0039950 HOIP:HOIP_0039951 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell. negative regulation of viral entry into host cell in moderate COVID-19 HOIP_0039951 HOIP:HOIP_0039952 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. positive regulation of viral RNA catabolic process in moderate COVID-19 HOIP_0039952 HOIP:HOIP_0039953 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32697943 interferon-alpha production in moderate COVID-19 HOIP_0039953 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Moreover, increased glucose levels further augmented TNF-a, IL-6, and IFN a, b, and l expression (Figure S1A). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0039954 The appearance of interferon-beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. PMID:32697943 interferon-beta production in moderate COVID-19 HOIP_0039954 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0039955 Hypofunction of type I interferon signaling is a subtype of hypofunction of signaling: A process that performs a decreased or insufficient type I interferon signaling . hypofunction of type I interferon signaling HOIP_0039955 HOIP:HOIP_0039956 Any process that activates or increases the frequency, rate or extent of the inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. positive regulation of inflammatory response (high) in moderate COVID-19 HOIP_0039956 HOIP:HOIP_0039957 angiotensin signaling is a process that a signal is transmitted by angiotensin. PMID:32407672 PMID:32694793 PMID:33188364 angiotensin signaling (high) in moderate COVID-19 HOIP_0039957 PMID:32694793 The prevalence of hypertension, cardiovascular disease, nephropathy and retinopathy in people with diabetes has implicated the renin–angiotensin system (RAS) in the pathogenesis of these disorders. Angiotensin II, the active RAS metabolite and a potent vasoconstrictor that increases peripheral vascular resistance, also causes insulin resistance and regulates sodium absorption in the kidneys. PMID:33188364 ROS production and viral activation of the renin–angiotensin–aldosterone system (RAAS), (via increased angiotensin II expression) cause insulin resistance, hyperglycaemia and vascular endothelial damage, all of which contribute to cardiovascular events, thromboembolism and disseminated intravascular coagulation (DIC). HOIP:HOIP_0039958 Accumulation of abnormal proteins is a subtype of protein accumulation: A process that keeps Angiotensin II in a biological object. This process can constitute the course of moderate COVID-19. PMID:32264791 PMID:32629875 Angiotensin II accumulation (high) in moderate COVID-19 HOIP_0039958 PMID:32264791 Ang II levels also further increases ADAM17 activity. ADAM17 correspondingly also cleaves its primary substrate releasing soluble TNF-α (tumor necrosis factor-α) into the extracellular region where it has auto- and paracrine functionality. TNF-α activation of its tumor necrosis factor receptor (TNFR) represents a third pathway elevating ADAM17 activity. TNF-α along with systemic cytokines released due to SARS-CoV-2 infection and in conjunction with comorbidities such as diabetes mellitus and hypertension can lead to a cytokine storm. TMPRSS2 indicates transmembrane protease serine 2. PMID:32264791 Ang II levels elevate with increased activity of angiotensin 1 receptors (AT1R) at the cost of ACE2/ Ang 1–7 driven pathways leading to adverse fibrosis, hypertrophy, increased reactive oxygen species (ROS), vasoconstriction, and gut dysbiosis. PMID:32629875 However, a study in twelve patients with COVID-19 reported significantly increased plasma levels of angiotensin II, which appeared to directly correlate with circulating SARS-CoV-2 RNA levels and degree of hypoxia. HOIP:HOIP_0039959 Chronic inflammatory response is a subtype of the inflammatory response: A process of chronic defensive reactions (by vertebrate tissues) to infection or injury. This entity is a specific course-dependent process. This process can constitute the course of moderate COVID-19. chronic inflammatory response in moderate COVID-19 HOIP_0039959 HOIP:HOIP_0039960 Hyperfunction of immune response is a subtype of hyperfunctioning: A process that performs an excessive immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (apparent). hyperfunction of immune response in apparent COVID-19 HOIP_0039960 HOIP:HOIP_0039961 Any process involved directly in viral genome replication, including viral nucleotide metabolism. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. PMID:32641482 viral genome replication in inapparent COVID-19 HOIP_0039961 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0039962 A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. virion assembly in inapparent COVID-19 HOIP_0039962 HOIP:HOIP_0039963 The assembly of a virus capsid from its protein subunits. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. viral capsid assembly in inapparent COVID-19 HOIP_0039963 HOIP:HOIP_0039964 The directed movement of a virus, or part of a virus, into, out of, or within a host cell. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. transport of virus in inapparent COVID-19 HOIP_0039964 HOIP:HOIP_0039965 The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. PMID:33077917 viral release from host cell in inapparent COVID-19 ウイルス排出 Previous HoIP ID: HOIP_0039965 SARS-CoV-2 shedding in inapparent COVID-19 HOIP_0039965 PMID:33077917 Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0039966 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. viral proliferation in inapparent COVID-19 HOIP_0039966 HOIP:HOIP_0039967 Viral protein production is a subtype of protein production: A process that produces a virus protein as an output. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. viral protein production in inapparent COVID-19 HOIP_0039967 HOIP:HOIP_0039968 The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. This process can constitute the course of inapparent COVID-19. viral absorption virion attachment to host cell surface receptor viral attachment to host cell virion attachment to host cell in inapparent COVID-19 HOIP_0039968 HOIP:HOIP_0039969 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. This process can constitute the course of inapparent COVID-19. decreasing number of virus in inapparent COVID-19 HOIP_0039969 HOIP:HOIP_0039970 Changing symbiotic balance between host and virus balance is a subtype of changing balance: A process that changes the steady state of symbiosis between host and virus within an organ or an organism. This process can constitute the course of inapparent COVID-19. symbiotic imbalance between host and virus in inapparent COVID-19 HOIP_0039970 HOIP:HOIP_0039971 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19. The functioning level is low. This process can constitute the course of inapparent COVID-19. PMID:32651579 PMID:32843733 antiviral innate immune response (low) in inapparent COVID-19 HOIP_0039971 PMID:32651579 Dysregulated immune response and cytokine-release syndrome, due to overactivation of innate immunity in the setting of T cell lymphodepletion, characterize the presentations of severe COVID-19. PMID:32843733 The damaged cells in the lungs elicit a strong innate immune response, which seems to be largely mediated by pro-inflammatory macrophages and granulocytes. This response is thought to be responsible for the cytokine release syndrome or ‘cytokine storm’ that is believed to contribute to ARDS. HOIP:HOIP_0039972 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of inapparent COVID-19 production of molecular mediator of innate immune response in inapparent COVID-19 HOIP_0039972 HOIP:HOIP_0039973 Increasing virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. This process can constitute the course of inapparent COVID-19. decreasing virus resitance in inapparent COVID-19 HOIP_0039973 HOIP:HOIP_0039974 Increasing virus resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the viruses to be lower. decreasing virus sensitivity decreasing virus resitance HOIP_0039974 HOIP:HOIP_0039975 Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production. This process can constitute the course of inapparent COVID-19. PMID:32505227 PMID:33116300 negative regulation of type I interferon production in inapparent COVID-19 HOIP_0039975 PMID:33116300 For example, nsp1 is rapidly proteolytically released from pp1a and pp1ab and affects cellular translation in the cytoplasm to favour viral mRNAs over cellular mRNA, and thereby also decreases the expression of type I and III interferons and of other host proteins of the innate immune response. Although this activity is not predicted for any accessory protein of SARS-CoV or SARS-CoV-2, the ORF3b, ORF6 and N proteins of SARS-CoV have been shown to interfere at multiple levels of the cellular interferon signalling pathway, thereby efficiently inhibiting innate immune responses103. Interestingly, an initial report recently suggested a similar role of SARS-CoV-2 ORF3b as an effective interferon antagonist. HOIP:HOIP_0039977 Hypofunction of negative regulation of inflammatory response is is a subtype of hypofunctioning of controlling: A process that performs a decreased or insufficient negative regulation of inflammatory response. hypofunction of negative regulation of inflammatory response HOIP_0039977 HOIP:HOIP_0039978 Hypofunction of phagocytosis is a subtype of hypofunctioning: A process that performs a decreased or insufficient phagocytosis. hypofunction of phagocytosis HOIP_0039978 HOIP:HOIP_0039979 Hypofunction of apoptotic cell clearance is a subtype of hypofunction of phagocytosis: A process that performs a decreased or insufficient apoptotic cell clearance. hypofunction of apoptotic cell clearance HOIP_0039979 HOIP:HOIP_0039981 Hypofunction of cytokine production is a subtype of hypofunction of protein biosynthesis: A process that performs a decreased or insufficient cytokine production. hypofunction of cytokine production HOIP_0039981 HOIP:HOIP_0039982 Hypofunction of tumor necrosis factor production is a subtype of hypofunction of cytokine biosynthesis: A process that performs a decreased or insufficient tumor necrosis factor production. hypofunction of tumor necrosis factor production HOIP_0039982 HOIP:HOIP_0039983 Hypofunction of neutrophil chemotaxis is a subtype of hypofunctioning: A process that performs a decreased or insufficient neutrophil chemotaxis. hypofunction of neutrophil chemotaxis HOIP_0039983 HOIP:HOIP_0039984 Hypofunction of expression of ACE2 is a subtype of hypofunction of transcription, DNA-templated: A process that performs a decreased or insufficient ACE2 expression. hypofunction of expression of ACE2 HOIP_0039984 HOIP:HOIP_0039985 Hypofunction of is inflammatory response a subtype of hypofunctioning: A process that performs a decreased or insufficient inflammatory response by the immune system . hypofunction of inflammatory response HOIP_0039985 HOIP:HOIP_0039986 Hypofunction of hypofunction of neutrophil apoptosis is a subtype of hypofunctioning: A process that performs a decreased or insufficient hypofunction of neutrophil apoptosis . hypofunction of neutrophil apoptosis HOIP_0039986 HOIP:HOIP_0039987 Hypofunction of thrombus formation is a process that performs a decreased thrombus formation. hypofunction of thrombus formation HOIP_0039987 HOIP:HOIP_0039988 Hypofunction of viral translation is a subtype of hypofunctioning: A process that performs a decreased or insufficient viral translation . hypofunction of viral translation HOIP_0039988 HOIP:HOIP_0039989 Hypofunction of virion assembly is a subtype of hypofunction of assembling: A process that performs a decreased or insufficient virion assembly. hypofunction of virion assembly HOIP_0039989 HOIP:HOIP_0039990 Hypofunction of assembling is a subtype of hypofunctioning: A process that performs a decreased or insufficient assembling . hypofunction of assembling HOIP_0039990 HOIP:HOIP_0039991 Hypofunction of IL-6 signaling is a subtype of hypofunction of signaling: A process that performs a decreased or insufficient IL-6 signaling . hypofunction of IL-6 signaling HOIP_0039991 HOIP:HOIP_0039992 Hypofunction of signaling is a subtype of hypofunction of transport: A process that performs a decreased or insufficient signaling . hypofunction of signaling HOIP_0039992 HOIP:HOIP_0039993 Hypofunction of uncoating of virus is a subtype of hypofunctioning: A process that performs a decreased or insufficient uncoating of virus . hypofunction of uncoating of virus HOIP_0039993 HOIP:HOIP_0039994 Hypofunction of transport of virus is a subtype of hypofunction of transport: A process that performs a decreased or insufficient transport of virus . hypofunction of transport of virus HOIP_0039994 HOIP:HOIP_0039995 Hypofunction of fibrinolysis is a subtype of hypofunctioning: A process that performs a decreased or insufficient fibrinolysis. hypofunction of fibrinolysis HOIP_0039995 HOIP:HOIP_0039996 Hypofunction of viral genome replication is a subtype of hypofunctioning: A process that performs a decreased or insufficient viral genome replication. hypofunction of viral genome replication HOIP_0039996 HOIP:HOIP_0039997 Hypofunction of viral release from host cell is a subtype of hypofunction of moving A to the outside of B: A process that performs a decreased or insufficient viral release from host cell. hypofunction of viral release from host cell HOIP_0039997 HOIP:HOIP_0039998 Hypofunction of CXCL8 signaling is a subtype of hypofunction of signaling: A process that performs a decreased or insufficient CXCL8 signaling . hypofunction of CXCL8 signaling HOIP_0039998 HOIP:HOIP_0040005 Negative regulation of cleavage of viral spike protein S is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of cleavage of viral spike protein S. This process can constitute the course of COVID-19 drug treatment. PMID:32142651 PMID:32362314 negative regulation of cleavage of viral spike S protein in COVID-19 drug treatment HOIP_0040005 PMID:32142651 In order to determine whether SARS-CoV-2 can use CatB/L for cell entry, we initially employed ammonium chloride, which elevates endosomal pH and thereby blocks CatB/L activity. Ammonium chloride treatment strongly inhibited SARS-2-S- and SARS-S-driven entry into TMPRSS2 293T cells (Figure S3 A), suggesting CatB/L dependence. Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. PMID:32362314 Decanoyl-RVKR-CMK inhibited processing of MERS-S, which is known to depend on furin (Gierer et al., 2015; Millet and Whittaker, 2014), in a concentration- dependent manner and had no effect on SARS-S expression (Figure 2C), as expected. Processing of SARS-2-S was also inhibited, indicating that furin cleaves SARS-2-S at the S1/S2 site. HOIP:HOIP_0040007 Cleavage of viral spike protein is a subtype of proteolysis: A process in which ciral spike protein is cleaved. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32142651 cleavage of viral spike S protein (very low) in COVID-19 drug treatment HOIP_0040007 PMID:32142651 Ammonium chloride treatment strongly inhibited SARS-2-S- and SARS-S-driven entry into TMPRSS2 293T cells (Figure S3 A), suggesting CatB/L dependence. Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. Indeed, camostat mesylate significantly reduced MERS-S-, SARS-S-, and SARS-2-S- but not VSV-G-driven entry into the lung cell line Calu-3 (Figure 4C) and exerted no unwanted cytotoxic effects (Figure S3 C). HOIP:HOIP_0040010 Negative regulation of receptor-mediated endocytosis of virus by host cell is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of receptor-mediated endocytosis of virus by host cell. This process can constitute the course of COVID-19 drug treatment. PMID:32221306 PMID:32361028 PMID:33516131 PMID:32221306 PMID:32221306 negative regulation of receptor-mediated endocytosis of virus by host cell in COVID-19 drug treatment HOIP_0040010 PMID:32221306 HEK 293/hACE2 cells were treated with lysosomotropic agents, ammonia chloride and bafilomycin A, and their effect on virus entry was evaluated. More than 98% reduction in transduction on 293/hACE2 cells by SARS-CoV-2 S pseudovirions was also shown when the cells were incubated with either NH4Cl or bafilomycin A (Fig. 3a), indicating that SARS-CoV-2 S pseudovirions enter 293/hACE2 cells mainly through endocytosis, despite that its spike proteins were cleaved. PMID:32361028 "One of the top significant results shown to downregulate the expression of the CTSL gene is amantadine (10uM). Amantadine in addition to downregulating CTSL appears to further disrupt lysosomal pathway, hence, interfering with the capacity of the virus to replicate." PMID:33516131 Cleaved spike glycoproteins are then able to interact with a specific intracellular receptor such as NPC1 (Ebola virus) or lamp1 (Lassa virus), which leads to spike glycoprotein-mediated fusion between the viral envelope and the endo-lysosomal membrane, and lysosome ion channels (TPCs and TRPML2) help trigger the fusion process. TPCs and TRPMLs are potential Ca2+ release channels in lysosomes. TPC2 has also been shown to be required for release of the SARS-CoV-2 genome into target cells, although the specific role of TPC2 in virus escape into the cytoplasm is not completely clear. PMID:32221306 As expected, apilimod treatment inhibited entry of SARS-CoV-2 S pseudovirions in a dose dependent manner (Fig. 3d). While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect. Blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. E64D treatment of 293/hACE2 cells reduced entry of SARS-CoV- 2 S pseudovirions by 92.5%, indicating that at least one of cathepsins or calpain might be required for SARS-CoV-2 entry (Fig. 4a). HOIP:HOIP_0040011 Negative regulation of receptor-mediated endocytosis of virus by host cell is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of receptor-mediated endocytosis of virus by host cell. negative regulation of receptor-mediated endocytosis of virus by host cell HOIP_0040011 HOIP:HOIP_0040019 WEB: http://www.ncbi.nlm.nih.gov/gene phosphoinositide kinase, FYVE-type zinc finger containing 200576 2q34 20140408 9606 2 protein-coding Official from a nomenclature committee phosphoinositide kinase, FYVE-type zinc finger containing Ensembl:ENSG00000115020 HGNC:23785 HPRD:17852 MIM:609414 Vega:OTTHUMG00000132945 PIKFYVE HOIP_0040019 HOIP:HOIP_0040023 Pulmonary fibrosis is a subtype of fibrosis: A process that replaces pulmonary tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. pulmonary fibrosis HOIP_0040023 HOIP:HOIP_0040025 The transport of a virus between adjacent cells in a multicellular organism. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32362314 PMID:32629875 cell to cell spread of virus within host intercellular virus transport transport of virus in host (cell to cell) in COVID-19 HOIP_0040025 PMID:32362314 Finally, the addition of an arginine residue to the S1/S2 site of SARS-2-S jointly with alanine-to-lysine exchange strongly increased syncytium formation, indicating that viral variants with optimized S1/S2 sites might show augmented cell-cell spread and potentially altered pathogenicity. PMID:32629875 Epidemiologic evidence indicates that the virus is transmitted among close contacts mostly through the respiratory route, presumably directly through infected droplet secretions or indirectly via fomites (Figure 2). The proximity between the infected respiratory epithelium releasing the virus and endothelial cells may favor local transmission. HOIP:HOIP_0040026 Negative regulation of host cell surface receptor binding is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of host cell surface receptor binding. This process can constitute the course of COVID-19 drug treatment. PMID:32307653 PMID:32629875 negative regulation of host cell surface receptor binding in COVID-19 drug treatment HOIP_0040026 PMID:32307653 The most interesting finding of this study was that all patients treated with hydroxychloroquine and azithromycin had negative PCR results in nasopharyngeal samples, i.e., 100% of patients treated with both drugs were virologically cured compared to 57.1% of subjects treated with hydroxychloroquine only, and 12.5% of untreated individuals. Studies suggest beneficial effects of azithromycin in reducing viral load of hospitalized patients, possibly interfering with ligand/CD147 receptor interactions; however, its possible effects on SARS-CoV-2 invasion has not yet been evaluated. PMID:32629875 Recombinant human ACE2, the cell entry receptor of SARS-CoV-2, has been shown to competitively neutralize SARS-CoV-2 infection of cells, including endothelial cells in vitro. HOIP:HOIP_0040031 Negative regulation of host cell surface receptor binding is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of host cell surface receptor binding. negative regulation of host cell surface receptor binding HOIP_0040031 HOIP:HOIP_0040034 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32221306 PMID:32641482 viral entry into host cell (very low) in COVID-19 drug treatment HOIP_0040034 PMID:32221306 As expected, apilimod treatment inhibited entry of SARS-CoV-2 S pseudovirions in a dose dependent manner (Fig. 3d). While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect (Supplementary Fig. 1), indicating that TPC2, not TRPML1, is important for SARS-CoV-2 entry. We confirmed this in this study, and further showed that blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. E64D treatment of 293/hACE2 cells reduced entry of SARS-CoV- 2 S pseudovirions by 92.5%, indicating that at least one of cathepsins or calpain might be required for SARS-CoV-2 entry (Fig. 4a). PMID:32641482 Moreover, we found that LY6E also efficiently restricted the entry mediated by the envelope spike proteins of other human coronaviruses, including the currently pandemic SARS-CoV-2. HOIP:HOIP_0040036 Changing viral spike S protein structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein. This process can constitute the course of COVID-19. PMID:32075877 PMID:32155444 changing viral spike S protein conformation changing viral spike S protein structure in COVID-19 HOIP_0040036 PMID:32075877 The S protein is a trimeric class I fusion protein that exists in a metastable prefusion conformation that undergoes a substantial structural rearrangement to fuse the viral membrane with the host cell membrane. This process is triggered when the S1 subunit binds to a host cell receptor. Receptor binding destabilizes the prefusion trimer, resulting in shedding of the S1 subunit and transition of the S2 subunit to a stable postfusion conformation. PMID:32155444 As a result, SARS-CoV-2 SB opening is expected to be necessary for interacting with ACE2 at the host cell surface and initiating the conformational changes leading to cleavage of the S2' site, membrane fusion and viral entry (Gui et al., 2017; Kirchdoerfer et al., 2018; Millet and Whittaker, 2014; Pallesen et al., 2017; Park et al., 2016; Song et al., 2018; Walls et al., 2019; Yuan et al., 2017). HOIP:HOIP_0040038 Changing viral spike S protein structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein. changing viral spike S protein conformation changing viral spike S protein structure HOIP_0040038 HOIP:HOIP_0040039 Negative regulation of viral entry into host cell is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral entry into host cell. This process can constitute the course of COVID-19 drug treatment. PMID:32221306 PMID:32641482 negative regulation of viral entry into host cell in COVID-19 drug treatment HOIP_0040039 PMID:32221306 As expected, apilimod treatment inhibited entry of SARS-CoV-2 S pseudovirions in a dose dependent manner (Fig. 3d). While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect (Supplementary Fig. 1), indicating that TPC2, not TRPML1, is important for SARS-CoV-2 entry. We confirmed this in this study, and further showed that blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. E64D treatment of 293/hACE2 cells reduced entry of SARS-CoV- 2 S pseudovirions by 92.5%, indicating that at least one of cathepsins or calpain might be required for SARS-CoV-2 entry (Fig. 4a). PMID:32641482 LY6E Restricts Entry of Human Coronaviruses, Including Currently Pandemic SARS-CoV-2 HOIP:HOIP_0040040 Negative regulation of host cell surface receptor binding is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of host cell surface receptor binding. negative regulation of viral entry into host cell HOIP_0040040 HOIP:HOIP_0040041 Changing viral spike S protein structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein. This process can constitute the course of coronavirus infectious disease. PMID:32641482 changing viral spike S protein conformation changing viral spike S protein structure in coronavirus infection HOIP_0040041 PMID:32641482 The cleavage of viral envelope spike proteins by endocytic proteases and/or endosomal acidification triggers the conformational change of spike proteins to induce the fusion of viral envelope with the endocytic membrane, and thus release nucleocapsids into the cytoplasm to initiate viral protein synthesis and RNA replication. HOIP:HOIP_0040042 Negative regulation of virus membrane fusion with host plasma membrane is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of virus membrane fusion with host plasma membrane. This process can constitute the course of COVID-19 drug treatment. PMID:32704094 PMID:32887954 negative regulation of virus membrane fusion with host plasma membrane in COVID-19 drug treatment HOIP_0040042 PMID:32704094 Mechanistic studies revealed that LY6E inhibits CoV entry into cells by interfering with spike protein-mediated membrane fusion. LY6E reduced CoV S-mediated cell–cell fusion of HCoV-229E (Fig.2e,f), MERS-CoV (Fig.2e,f) and SARS-CoV-2 (Fig. 2g,h), as visualized by a reduction of GFP-positive syncytia, indicating that LY6E blocks the fusion of viral and cellular membranes. PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. HOIP:HOIP_0040043 Negative regulation of virus membrane fusion with host plasma membrane is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of virus membrane fusion with host plasma membrane. negative regulation of virus membrane fusion with host plasma membrane HOIP_0040043 HOIP:HOIP_0040044 Fusion of a viral membrane with the host cell membrane during viral entry. Results in release of the virion contents into the cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32704094 fusion of virus membrane with host plasma membrane (very low) in COVID-19 drug treatment HOIP_0040044 PMID:32704094 LY6E reduced CoV S-mediated cell–cell fusion of HCoV-229E (Fig.2e,f), MERS-CoV(Fig.2e,f) and SARS-CoV-2 (Fig. 2g,h), as visualized by a reduction of GFP-positive syncytia, indicating that LY6E blocks the fusion of viral and cellular membranes. HOIP:HOIP_0040046 Any process that stops, prevents, or reduces the frequency, rate or extent of glycolysis. This process can constitute the course of COVID-19. negative regulation of glycolytic process in COVID-19 HOIP_0040046 HOIP:HOIP_0040047 Any process that activates or increases the frequency, rate or extent of glycolytic process. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 PMID:33188364 positive regulation of glycolysis positive regulation of glycolytic process in severe COVID-19 HOIP_0040047 PMID:32697943 Monocytes and macrophages are the most enriched immune cell types in the lungs of COVID-19 patients and appear to have a central role in the pathogenicity of the disease.These cells adapt their metabolism upon infection and become highly glycolytic, which facilitates SARS-CoV-2 replication. The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes Taken together, our results indicate that CoV-2 replication in monocytes and CoV-2-induced monocyte response are sustained by a switch to aerobic glycolysis (the Warburg effect). We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). PMID:33188364 In human monocytes, elevated glucose levels directly increase SARS-CoV-2 replication, and glycolysis sustains SARS-CoV-2 replication via the production of mitochondrial reactive oxygen species and activation of hypoxia-inducible factor 1α. HOIP:HOIP_0040048 Pulmonary fibrosis is a subtype of fibrosis: A process that replaces pulmonary tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 PMID:32422178 An interstitial lung disease that is characterized by destruction, scarring, and thickening of the interstitial lung tissues and progressive pulmonary function loss in a restrictive pattern, has_symptom progressive shortness of breath, fatigue, and chronic cough, possibly has_material_basis_in exposure to certain chemicals, autoimmune conditions, and radiation. pulmonary fibrosis in COVID-19 associated with ARDS HOIP_0040048 PMID:32307653 Moreover, resident lung progenitor/stem are extensively differentiated into myofibroblasts during pulmonary fibrosis, a complication observed in COVID-19 patients. In addition to direct viral invasion and loss of lung stem cells, stocks of these cells also can be affected during SARS-CoV-2 infection by extensive differentiation into myofibroblasts. These cell deposit extracellular matrix proteins and are the main cells presents in fibrotic diseases, including pulmonary fibrosis and fibrous stripes due to COVID-19. Recent evidence using lineage tracing showed that resident mesenchymal cells are the main sources of myofibroblasts in pulmonary fibrosis, rather than epithelial or bone marrow-derived cells. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32422178 Although many patients who develop ARDS survive the acute phase of the illness, a substantial proportion die as a result of progressive pulmonary fibrosis. Importantly, in an autopsy study of 159 patients with ARDS, fibrosis was noted in three (4%) of 82 patients with a disease duration of less than 1 week, 13 (24%) of 54 patients with a disease duration of between weeks 1 and 3, and 14 (61%) of 23 patients with a disease duration of greater than 3 weeks, suggesting that to be effective, any potential antifibrotic intervention should be considered within the first week of ARDS onset. A substantial proportion of patients who develop ARDS will experience residual long-term impairment of lung function and CT evidence of pulmonary fibrosis, with anterior reticulation the dominant abnormality in as many as 85% of survivors. Multiple aberrant host pathways interconnect to result in pulmonary fibrosis in a subset of individuals who develop ARDS. Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. Canonical profibrotic pathways regulated by TGF-beta are important, and there is evidence that vascular dysfunction is a key component of the switch from ARDS to fibrosis, with VEGF and cytokines such as IL-6 and TNFalpha implicated. In fatal cases of COVID-19, pulmonary fibrosis is generally present at autopsy, with anecdotal reports of severe fibrotic organising pneumonia. In some cases, abnormal immune mechanisms initiate and promote pulmonary fibrosis, possibly as a consequence of a cytokine storm. HOIP:HOIP_0040049 NCBI-Human-GeneID:682 NCBI-Mouse-GeneID:12215 NCBI-Rat-GeneID:25246 CD147 basigin BSG (mol) HOIP_0040049 NCBI-Human-GeneID:682 https://www.ncbi.nlm.nih.gov/gene/682 NCBI-Mouse-GeneID:12215 https://www.ncbi.nlm.nih.gov/gene/12215 NCBI-Rat-GeneID:25246 https://www.ncbi.nlm.nih.gov/gene/25246 HOIP:HOIP_0040050 Cell malfunction is a subtype of malfunctioning process: A process that cannot perform cell(s) function appropriately or cannot realize it at all. cell malfunction HOIP_0040050 HOIP:HOIP_0040052 T cell malfunction is a subtype of malfunctioning process: A process that cannot perform T cell(s) function appropriately or cannot realize it at all. T cell dysfunction T cell malfunction HOIP_0040052 HOIP:HOIP_0040053 T cell malfunction is a subtype of malfunctioning process: A process that cannot perform T cell(s) function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 T cell dysfunction T cell malfunction in severe COVID-19 HOIP_0040053 PMID:32697943 Diabetic people with uncontrolled blood glucose levels have a greater risk to develop severe COVID-19 disease. Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. These results provide evidence to explain why elevated glucose levels during CoV-2 infection may lead to T cell dysfunction and lymphopenia. HOIP:HOIP_0040054 Any process that activates or increases the frequency, rate or extent of positive stranded viral RNA replication. positive regulation of positive stranded viral RNA replication HOIP_0040054 HOIP:HOIP_0040055 Any process that activates or increases the frequency, rate or extent of positive stranded viral RNA replication. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of positive stranded viral RNA replication in severe COVID-19 HOIP_0040055 PMID:32697943 Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Elevated glucose levels directly induce viral replication and proinflammatory cytokine expression. HOIP:HOIP_0040058 HIF1A stabilization is a subtype of keeping activation: A process that maintains the activation of HIF1A. HIF1A stabilization HOIP_0040058 HOIP:HOIP_0040059 HIF1A stabilization is a subtype of keeping activation: A process that maintaing the activation of HIF1A. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 HIF1A stabilization (very high) in severe COVID-19 HOIP_0040059 PMID:32697943 In contrast, stabilization of HIF-1a increased the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l in CoV-2-infected monocytes (Figures 3G, 3H, and S4E). Our findings demonstrated that HIF-1a is necessary for the induction of glycolysis and the consequent proinflammatory state of CoV-2-infected monocytes. It is known that succinate accumulation drives HIF-1a stabilization (Tannahill et al., 2013). We used cell-permeable diethyl succinate and observed that succinate boosted CoV-2 viral load (Figure S4F). The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes CM-CoV-2 induced apoptosis of A549 cells (Figure 4D), which was prevented when CoV-2-infected monocytes were treated with a HIF-1a inhibitor (Figure 4D). This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. Altogether, these results highlight the metabolic alterations that take place in CoV-2-infected monocytes under high glucose conditions. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. HOIP:HOIP_0040061 Negative regulation of T cell mediated immunity is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the T cell mediated immunity. Negative regulation of T cell mediated immunity HOIP_0040061 HOIP:HOIP_0040062 Negative regulation of T cell mediated immunity is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the T cell mediated immunity. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 PMID:33077917 PMID:33123165 negative regulation of T cell mediated immunity (very high) in severe COVID-19 HOIP_0040062 PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Exacerbated proinflammatory stimuli can negatively affect T cell response (de Marcken et al., 2019). We found that CM-CoV-2 impaired CD4 and CD8 T cell proliferation (Figures 4A and S4I), whereas CM-BAY87 or CM-MitoQ restored T cell proliferation to the same extent as CM-Mock (Figures 4A and S4I). These results provide evidence to explain why elevated glucose levels during CoV-2 infection may lead to T cell dysfunction and lymphopenia. PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). PMID:33123165 This model could account for poorer outcomes in the elderly who have diminished T cell repertoires and better outcomes in children who have a diverse and abundant naïve T cell pool. HOIP:HOIP_0040063 The migration of a monocyte from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32307653 PMID:32697943 PMID:33123165 monocyte extravasation in COVID-19 HOIP_0040063 PMID:32307653 Some regions of reactive epithelial hyperplasia had also abundant alveolar macrophages. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32697943 Upon infection, there is an accumulation of immune cells in the lungs, especially macrophages and monocytes (Merad and Martin, 2020). These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0040065 The appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 PMID:32887954 PMID:33077917 PMID:33123165 chemokine production in COVID-19 HOIP_0040065 PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). PMID:32887954 Cytokine profiles from patients infected with SARS-CoV-2 resemble those in macrophage activation syndrome and are characterized by high levels of inflammatory cytokines and chemokines. PMID:33077917 Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0040066 Expression of ACE2 is a subtype of gene expression: The process in which a gene sequence is converted into a mature ACE2 gene product or products (proteins or RNA). Expression of ACE2 HOIP_0040066 HOIP:HOIP_0040067 Expression of ACE2 is a subtype of gene expression: The process in which a gene sequence is converted into a mature ACE2 gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:32697943 PMID:33077917 PMID:33188364 Expression of ACE2in COVID-19 HOIP_0040067 PMID:32629875 However, cardiomyocytes are potential targets of SARS-CoV-2 infection as they express ACE2. PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). PMID:33077917 SARS-CoV-2 has also been found in proximal tubular cells, which exhibit high levels of ACE2 in the apical brush border. Tubule epithelial cells and podocytes exhibit high levels of ACE2 and TMPRSS2, suggesting that they are potential SARS-CoV-2 targets. PMID:33188364 This finding and the localization of ACE2 expression in the endocrine pancreas together suggest that coronaviruses might specifically damages islets, potentially leading to hyperglycaemia. HOIP:HOIP_0040068 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:32697943 PMID:33123165 IL-1beta production in COVID-19 HOIP_0040068 PMID:32629875 These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. PMID:32697943 Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). We observed that neutralization of IL-1b with anti-IL-1b (CM-aIL-1b) from UV-inactivated CM of CoV-2-infected monocytes restored T cell proliferation (Figures 4A and S4I). PMID:33123165 The resultant inflammatory response provides immediate antiviral immunity via activation of antiviral type 1 and 3 interferon (IFN) pathways leading to an upregulation of inflammatory cytokines such as interleukin 6 (IL-6) and IL-1β, further recruiting neutrophils, other innate immune cells and stimulating anti-SARS-CoV-2 adaptive memory T cells and B cells (Figure 2). HOIP:HOIP_0040070 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 delayed interferon-alpha production in severe COVID-19 HOIP_0040070 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Moreover, increased glucose levels further augmented TNF-a, IL-6, and IFN a, b, and l expression (Figure S1A). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0040071 The appearance of interferon-beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 delayed interferon-beta production (severe) in severe COVID-19 HOIP_0040071 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0040072 HIF1A stabilization is a subtype of keeping activation: A process that maintains the activation of HIF1A. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 HIF1A stabilizationin COVID-19 HOIP_0040072 PMID:32697943 In contrast, stabilization of HIF-1a increased the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l in CoV-2-infected monocytes (Figures 3G, 3H, and S4E). Our findings demonstrated that HIF-1a is necessary for the induction of glycolysis and the consequent proinflammatory state of CoV-2-infected monocytes. It is known that succinate accumulation drives HIF-1a stabilization (Tannahill et al., 2013). We used cell-permeable diethyl succinate and observed that succinate boosted CoV-2 viral load (Figure S4F). The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. HOIP:HOIP_0040074 The change in morphology and behavior of a monocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 monocyte activation involved in inflammatory response in COVID-19 HOIP_0040074 PMID:32697943 Glycolysis Is Necessary for SARS-CoV-2 Replication and Monocyte Response Taken together, our results indicate that CoV-2 replication in monocytes and CoV-2-induced monocyte response are sustained by a switch to aerobic glycolysis (the Warburg effect). HOIP:HOIP_0040075 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 PMID:33188364 glycolysis glycolytic process in COVID-19 HOIP_0040075 PMID:32697943 Monocytes and macrophages are the most enriched immune cell types in the lungs of COVID-19 patients and appear to have a central role in the pathogenicity of the disease.These cells adapt their metabolism upon infection and become highly glycolytic, which facilitates SARS-CoV-2 replication. The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes Glycolysis Is Necessary for SARS-CoV-2 Replication and Monocyte Response Taken together, our results indicate that CoV-2 replication in monocytes and CoV-2-induced monocyte response are sustained by a switch to aerobic glycolysis (the Warburg effect). We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). PMID:33188364 In human monocytes, elevated glucose levels directly increase SARS-CoV-2 replication, and glycolysis sustains SARS-CoV-2 replication via the production of mitochondrial reactive oxygen species and activation of hypoxia-inducible factor 1α. HOIP:HOIP_0040076 Negative regulation of PFKFB3 activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of PFKFB3 activation. negative regulation of PFKFB3 activation HOIP_0040076 HOIP:HOIP_0040078 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of positive stranded viral RNA replication. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 PMID:32726803 PMID:32756549 Negative regulation of positive stranded viral RNA replication in COVID-19 drug treatment HOIP_0040078 PMID:32697943 We used 2-DG to inhibit glucose flux and oligomycin to inhibit ATP synthase (Figure 2A). Treatment with 2-DG completely blocked viral replication in CoV-2-infected monocytes, as well as the CoV-2-induced increase of ACE2 and IL-1b expression (Figures 2B–2D). To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). Finally, to evaluate the importance of aerobic glycolysis for CoV-2 infection, we blocked lactate dehydrogenase A (LDH-A) activity with oxamate. This also completely abrogated viral replication and reduced ACE2 and IL-1b expression in CoV-2-infected cells (Figures 2K and S3F). In contrast, dimethyl malonate, which has been shown to inhibit succinate oxidation through its action on succinate dehydrogenase (SDH) (Mills et al., 2016), partially decreased CoV-2 replication in monocytes (Figure S4G). Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). CoV-2-infected monocytes treated with rotenone have reduced viral replication (Figure 3O). PMID:32726803 Notably, inhibition of SCoV2-PLpro with GRL-0617 impairs the virus-induced cytopathogenic effect, maintains the antiviral interferon pathway and reduces viral replication in infected cells. In addition, GRL-0617 treatment reduced active viral replication (SARS-CoV-2 subgenomic RNA4-encoding E gene), as measured by genetic monitoring of the intracellular production of viral RNA (Fig. 5c). Consequently, a decrease in the release of viral particles from infected cells into the supernatant was also observed upon GRL-0617 treatment (Fig. 5d, Extended Data Fig. 7a). This suggests that inhibition of SCoV2-PLpro by GRL-0617 impedes viral replication, thereby attenuating the ongoing viral RNA synthesis. PMID:32756549 Here we have shown that 1 μg of mRNA-1273 is sufficient to induce robust pseudovirus-neutralizing activity and CD8 T cell responses, balanced TH1–TH2 antibody isotype responses, and protection from viral replication for more than three months following a prime–boost regimen similar to the one being tested in humans. HOIP:HOIP_0040079 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of positive stranded viral RNA replication. Negative regulation of positive stranded viral RNA replication HOIP_0040079 HOIP:HOIP_0040080 A viral genome replication process where the template genome is positive stranded, single stranded RNA ((+)ssRNA). Replication of the positive strand leads to dsRNA formation, which in turn is transcribed into positive single stranded RNA. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is low. PMID:32697943 positive stranded viral RNA replicationvery (low) in COVID-19 drug treatment HOIP_0040080 PMID:32697943 We used 2-DG to inhibit glucose flux and oligomycin to inhibit ATP synthase (Figure 2A). In contrast, oligo- mycin treatment led to an increase in the viral load, ACE2 and IL- 1b expression, and TNF-a, IL-6, a, b, and l IFN expression in monocytes (Figures 2E–2G and S3B). To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). HOIP:HOIP_0040081 Expression of ACE2 is a subtype of gene expression: The process in which a gene sequence is converted into a mature ACE2 gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32697943 Expression of ACE2(very low) in COVID-19 drug treatment HOIP_0040081 PMID:32697943 We used 2-DG to inhibit glucose flux and oligomycin to inhibit ATP synthase (Figure 2A). Treatment with 2-DG completely blocked viral replication in CoV-2-infected monocytes, as well as the CoV-2-induced increase of ACE2 and IL-1b expression (Figures 2B–2D). To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). Finally, to evaluate the importance of aerobic glycolysis for CoV-2 infection, we blocked lactate dehydrogenase A (LDH-A) activity with oxamate. This also completely abrogated viral replication and reduced ACE2 and IL-1b expression in CoV-2-infected cells (Figures 2K and S3F). HOIP:HOIP_0040082 Negative regulation of ACE2 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 gene expression. negative regulation of ACE2 expression HOIP_0040082 HOIP:HOIP_0040083 Negative regulation of ACE2 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 gene expression. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 negative regulation of ACE2 expression in COVID-19 drug treatment HOIP_0040083 PMID:32697943 We used 2-DG to inhibit glucose flux and oligomycin to inhibit ATP synthase (Figure 2A). Treatment with 2-DG completely blocked viral replication in CoV-2-infected monocytes, as well as the CoV-2-induced increase of ACE2 and IL-1b expression (Figures 2B–2D). To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). Finally, to evaluate the importance of aerobic glycolysis for CoV-2 infection, we blocked lactate dehydrogenase A (LDH-A) activity with oxamate. This also completely abrogated viral replication and reduced ACE2 and IL-1b expression in CoV-2-infected cells (Figures 2K and S3F). BAY87 decreased HIF-1a levels and completely abrogated CoV-2 replication (Figures 3E and 3F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). HOIP:HOIP_0040084 The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32697943 tumor necrosis factor production (very low) in COVID-19 drug treatment HOIP_0040084 PMID:32697943 2-DG treatment also inhibited CoV-2-induced TNF-a, IL-6, and IFN a, b, and l expression in monocytes (Figure S3A). HOIP:HOIP_0040085 Negative regulation of TNF gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of TNF gene expression. negative regulation of TNF expression HOIP_0040085 HOIP:HOIP_0040086 Negative regulation of TNF gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of TNF gene expression. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 negative regulation of TNF expression in COVID-19 drug treatment HOIP_0040086 PMID:32697943 2-DG treatment also inhibited CoV-2-induced TNF-a, IL-6, and IFN a, b, and l expression in monocytes (Figure S3A). BAY87 decreased HIF-1a levels and completely abrogated CoV-2 replication (Figures 3E and 3F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). These antioxidants also prevented the upregulation of TNF-a; IL-6; IFN a, b, and l; and HIF-1a target genes (Figure S4H). HOIP:HOIP_0040087 Negative regulation of IL6 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IL6 gene expression. negative regulation of IL6 expression HOIP_0040087 HOIP:HOIP_0040088 Negative regulation of IL-6 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IL-6 gene expression. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 negative regulation of IL-6 expression in COVID-19 drug treatment HOIP_0040088 PMID:32697943 2-DG treatment also inhibited CoV-2-induced TNF-a, IL-6, and IFN a, b, and l expression in monocytes (Figure S3A). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). These antioxidants also prevented the upregulation of TNF-a; IL-6; IFN a, b, and l; and HIF-1a target genes (Figure S4H). HOIP:HOIP_0040089 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32697943 interferon-alpha production (very low) in COVID-19 drug treatment HOIP_0040089 PMID:32697943 2-DG treatment also inhibited CoV-2-induced TNF-a, IL-6, and IFN a, b, and l expression in monocytes (Figure S3A). HOIP:HOIP_0040090 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 interferon-beta production in COVID-19 drug treatment HOIP_0040090 PMID:32697943 2-DG treatment also inhibited CoV-2-induced TNF-a, IL-6, and IFN a, b, and l expression in monocytes (Figure S3A). HOIP:HOIP_0040091 Negative regulation of INIFN alpha gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFN alpha gene expression. negative regulation of IFN alpha expression HOIP_0040091 HOIP:HOIP_0040092 Negative regulation of INFA gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFNA gene expression. PMID:32697943 Negative regulation of IFN alpha gene expression in COVID-19 drug treatment HOIP_0040092 PMID:32697943 2-DG treatment also inhibited CoV-2-induced TNF-a, IL-6, and IFN a, b, and l expression in monocytes (Figure S3A). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). These antioxidants also prevented the upregulation of TNF-a; IL-6; IFN a, b, and l; and HIF-1a target genes (Figure S4H). HOIP:HOIP_0040093 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32697943 IL-1beta production (very low) in COVID-19 drug treatment HOIP_0040093 PMID:32697943 We used 2-DG to inhibit glucose flux and oligomycin to inhibit ATP synthase (Fig- ure 2A). Treatment with 2-DG completely blocked viral replication in CoV-2-infected monocytes, as well as the CoV-2-induced increase of ACE2 and IL-1b expression (Figures 2B–2D). To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). Finally, to evaluate the importance of aerobic glycolysis for CoV-2 infection, we blocked lactate dehydrogenase A (LDH-A) activity with oxamate. This also completely abrogated viral replication and reduced ACE2 and IL-1b expression in CoV-2-infected cells (Figures 2K and S3F). HOIP:HOIP_0040094 Negative regulation of INFB1 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFNB1 gene expression. negative regulation of INFB1 expression HOIP_0040094 HOIP:HOIP_0040095 Negative regulation of INFB1 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFNB1 gene expression. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 negative regulation of INFB1 expression in COVID-19 drug treatment HOIP_0040095 PMID:32697943 2-DG treatment also inhibited CoV-2-induced TNF-a, IL-6, and IFN a, b, and l expression in monocytes (Figure S3A). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). These antioxidants also prevented the upregulation of TNF-a; IL-6; IFN a, b, and l; and HIF-1a target genes (Figure S4H). HOIP:HOIP_0040096 Negative regulation of IL1B gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IL1B gene expression. negative regulation of IL1B expression HOIP_0040096 HOIP:HOIP_0040097 Negative regulation of IL1B gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IL1B gene expression. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 negative regulation of IL1B expression in COVID-19 drug treatment HOIP_0040097 PMID:32697943 We used 2-DG to inhibit glucose flux and oligomycin to inhibit ATP synthase (Figure 2A). Treatment with 2-DG completely blocked viral replication in CoV-2-infected monocytes, as well as the CoV-2-induced increase of ACE2 and IL-1b expression (Figures 2B–2D). To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). Finally, to evaluate the importance of aerobic glycolysis for CoV-2 infection, we blocked lactate dehydrogenase A (LDH-A) activity with oxamate. This also completely abrogated viral replication and reduced ACE2 and IL-1b expression in CoV-2-infected cells (Figures 2K and S3F). BAY87 decreased HIF-1a levels and completely abrogated CoV-2 replication (Figures 3E and 3F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). HOIP:HOIP_0040100 Negative regulation of PFKFB3 activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of PFKFB3 activation. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 Negative regulation of PFKFB3 activation in COVID-19 drug treatment HOIP_0040100 PMID:32697943 To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). HOIP:HOIP_0040101 Any process that stops, prevents, or reduces the frequency, rate or extent of glycolysis. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 negative regulation of glycolytic process in COVID-19 drug treatment HOIP_0040101 PMID:32697943 To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho-fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). HOIP:HOIP_0040103 Expression of SLC2A1 is a subtype of gene expression: The process in which a gene sequence is converted into a mature SLC2A1 gene product or products (proteins or RNA). Expression of SLC2A1 HOIP_0040103 HOIP:HOIP_0040105 Negative regulation of LDHA activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of LDHA activation. negative regulation of LDHA activation HOIP_0040105 HOIP:HOIP_0040106 Negative regulation of LDHA activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of LDHA activation. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 Negative regulation of LDHA activation in COVID-19 drug treatment HOIP_0040106 PMID:32697943 Finally, to evaluate the importance of aerobic glycolysis for CoV-2 infection, we blocked lactate dehydrogenase A (LDH-A) activity with oxamate. This also completely abrogated viral replication and reduced ACE2 and IL-1b expression in CoV-2-infected cells (Figures 2K and S3F). HOIP:HOIP_0040109 HIF1A activation is a subtype of molecular activation: A process that changes the activity of the HIF1A (hypoxia inducible factor 1 subunit alpha) to be higher. This entity is a specific course-dependent process. This procThis process can constitute the course of severe COVID-19. PMID:32651579 PMID:32697943 HIF1A activation in severe COVID-19 HOIP_0040109 PMID:32651579 Hypoxia-mediated hyperviscosity and upregulation of the HIF-1 (hypoxia-inducible factor 1) signaling pathway subsequent to acute lung injury may also contribute to the prothrombotic state. PMID:32697943 Our proteomic analysis further supports that CoV-2-infected monocytes have increased HIF-1a function given that HIF-1a targets are enriched among the upregulated proteins (Figure 3B). HIF-1a is a strong inducer of glycolysis and IL-1b transcription (Tannahill et al., 2013). HOIP:HOIP_0040110 Positive regulation of HIF1A gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of HIF1A gene expression. positive regulation of HIF1A gene expression HOIP_0040110 HOIP:HOIP_0040111 Positive regulation of HIF1A gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of HIF1A gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of HIF1A gene expression in COVID-19 HOIP_0040111 PMID:32697943 Blood monocytes from severe COVID-19 patients present high expression of HIF-1a in comparison to healthy donors (Figure 3C). We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. HOIP:HOIP_0040113 The removal of one or more electrons from succinate, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. succinate oxidation HOIP_0040113 HOIP:HOIP_0040116 The removal of one or more electrons from succinate, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 succinate oxidation in COVID-19 HOIP_0040116 PMID:32697943 In contrast, dimethyl malonate, which has been shown to inhibit succinate oxidation through its action on succinate dehydrogenase (SDH) (Mills et al., 2016), partially decreased CoV-2 replication in monocytes (Figure S4G). Thus, succinate oxidation is important for CoV-2 replication. HOIP:HOIP_0040118 Positive regulation of PFKFB3 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of PFKFB3 gene expression. positive regulation of PFKFB3 gene expression HOIP_0040118 HOIP:HOIP_0040119 Positive regulation of PFKFB3 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of PFKFB3 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of PFKFB3 gene expression in COVID-19 HOIP_0040119 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040120 Positive regulation of LDHA gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of LDHA gene expression. positive regulation of LDHA gene expression HOIP_0040120 HOIP:HOIP_0040121 Positive regulation of LDHA gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of LDHA gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of LDHA gene expression in COVID-19 HOIP_0040121 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040124 Positive regulation of PKM gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of PKM gene expression. positive regulation of PKM gene expression HOIP_0040124 HOIP:HOIP_0040125 Positive regulation of PKM gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of PKM gene expression. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of PKM gene expression in COVID-19 HOIP_0040125 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycoytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040126 C26H26F3N7O2 CC1=CC(=NN1CC2=CC(=NC=C2)N3CCN(CC3)C4CC4)C5=NC(=NO5)C6=CC=C(C=C6)OC(F)(F)F PMID:32697943 PubChem:67377767 http://ctdbase.org/detail.go?type=chem&acc=C000591541 1-Cyclopropyl-4-[4-[[5-methyl-3-[3-[4-(trifluoromethoxy)phenyl]-1,2,4-oxadiazol-5-yl]-1H-pyrazol-1-yl]methyl]-2-pyridinyl]-piperazine BAY 87-2243 HOIP_0040126 PMID:32697943 BAY87 decreased HIF-1a levels and completely abrogated CoV-2 replication (Figures 3E and 3F). CM-CoV-2 induced apoptosis of A549 cells (Figure 4D), which was prevented when CoV-2-infected monocytes were treated with a HIF-1a inhibitor (Figure 4D). HOIP:HOIP_0040128 Negative regulation of HIF1A activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of HIF1A activation. Negative regulation of HIF1A activation HOIP_0040128 HOIP:HOIP_0040129 Negative regulation of HIF1A activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of HIF1A activation. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 Negative regulation of HIF1A activation in COVID-19 drug treatment HOIP_0040129 PMID:32697943 BAY87 decreased HIF-1a levels and completely abrogated CoV-2 replication (Fig- ures 3E and 3F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0040130 Positive regulation of ACE2 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of ACE2 gene expression. positive regulation of ACE2 gene expression HOIP_0040130 HOIP:HOIP_0040132 Positive regulation of IL1B gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IL1B gene expression. Positive regulation of IL1B gene expression HOIP_0040132 HOIP:HOIP_0040134 Negative regulation of succinate oxidation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of succinate oxidation. Negative regulation of succinate oxidation HOIP_0040134 HOIP:HOIP_0040135 Negative regulation of succinate oxidation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of succinate oxidation. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 Negative regulation of succinate oxidation in COVID-19 drug treatment HOIP_0040135 PMID:32697943 In contrast, dimethyl malonate, which has been shown to inhibit succinate oxidation through its action on succinate dehydrogenase (SDH) (Mills et al., 2016), partially decreased CoV-2 replication in monocytes (Figure S4G). HOIP:HOIP_0040137 Positive regulation of IL1B gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IL1B gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of IL1B gene expression in COVID-19 HOIP_0040137 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). We observed that neutralization of IL-1b with anti-IL-1b (CM-aIL-1b) from UV-inactivated CM of CoV-2-infected monocytes restored T cell proliferation (Figures 4A and S4I). HOIP:HOIP_0040138 Positive regulation of TNFΑ gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of TNFΑ gene expression. positive regulation of TNFΑ gene expression HOIP_0040138 HOIP:HOIP_0040139 Positive regulation of TNFΑ gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of TNFΑ gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of TNFΑ gene expression (very high)in severe COVID-19 HOIP_0040139 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0040140 Positive regulation of IL-6 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IL-6 gene expression. positive regulation of IL-6 gene expression HOIP_0040140 HOIP:HOIP_0040141 Positive regulation of IL-6 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IL-6 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of IL-6 gene expression in COVID-19 HOIP_0040141 PMID:32697943 Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0040142 Positive regulation of IFN alpha gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IFN alpha gene expression. positive regulation of IFN alpha gene expression HOIP_0040142 HOIP:HOIP_0040143 Positive regulation of IFN alpha gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IFN alpha gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of IFN alpha gene expression in COVID-19 HOIP_0040143 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0040144 Hyperfunction of IFNB1 gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive IFNB1 gene expression. positive regulation of IFNB1 gene expression HOIP_0040144 HOIP:HOIP_0040145 Positive regulation of IFNB1 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IFNB1gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of IFNB1 gene expression in COVID-19 HOIP_0040145 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0040146 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 reactive oxygen species biosynthetic process in COVID-19 HOIP_0040146 PMID:32697943 Reactive oxygen species (ROS) are strong inducers of HIF-1a (Mills et al., 2016). We observed that CoV-2-infected monocytes have increased mtROS production as measured by mitoSOX (Figure 3J). These data indicate that RET is an important source of mtROS in CoV-2-infected monocytes. SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes HOIP:HOIP_0040147 Oxidation-antioxidtion inbalance is a subtype of imbalance: A process that lacks a balance between oxidation and anti-oxidation that inhibits oxidation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 oxidation-antioxidtion inbalance in COVID-19 HOIP_0040147 PMID:32697943 Proteomic analysis performed in CoV-2-infected monocytes confirmed alterations on oxidative metabolism with an overall downregulation of proteins involved in the TCA cycle (Figure S2D). HOIP:HOIP_0040148 Malfunctioning of TCA cycle is a subtype of malfunctioning of metabolism: A process that cannot perform a tricarboxylic acid cycle appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 Malfunctioning of TCA cycle in COVID-19 HOIP_0040148 PMID:32697943 Proteomic analysis performed in CoV-2-infected monocytes confirmed alterations on oxidative metabolism with an overall downregulation of proteins involved in the TCA cycle (Figure S2D). In agreement with our proteomic data, the spare respiratory capacity was reduced in CoV-2-infected monocytes (Figure 3I). Reduced respiration in LPS-activated macrophages is known to increase mitochondrial ROS (mtROS) production (Mills et al., 2016). HOIP:HOIP_0040149 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex assembly. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 Negative regulation of respiratory complex proteins synthesis in COVID-19 HOIP_0040149 PMID:32697943 Moreover, several components of respiratory electron chain complexes are downregulated in CoV-2-infected monocytes, such as NDUFV1 (complex I), SDHA (complex II), cytochrome c reductase COR1 and UQCRC2 (complex III), ATP5PF, ATP5F1A, ATP5PD, F-type ATPase a, and PPA2 (ATP synthase) (Figure S2D). In agreement with our proteomic data, the spare respiratory capacity was reduced in CoV-2-infected monocytes (Figure 3I). HOIP:HOIP_0040150 C37H46O4P+ CC1=C(C(=C(C(=C1O)OC)OC)O)CCCCCCCCCC[P+](C2=CC=CC=C2)(C3=CC=CC=C3)C4=CC=CC=C4 CAS:747398-82-9 PMID:32697943 PubChem:9917765 Mitoquinol cation mitoquinol HOIP_0040150 PMID:32697943 Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). These antioxidants also prevented the upregulation of TNF-a; IL-6; IFN a, b, and l; and HIF-1a target genes (Figure S4H). HOIP:HOIP_0040154 Negative regulation of HIF1A stabilization is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of HIF1A stabilization. Negative regulation of HIF1A stabilization HOIP_0040154 HOIP:HOIP_0040155 Negative regulation of HIF1A stabilization is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of HIF1A stabilization. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 Negative regulation of HIF1A stabilization in COVID-19 drug treatment HOIP_0040155 PMID:32697943 Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). HOIP:HOIP_0040156 Expression of SLC2A1 is a subtype of gene expression: The process in which a gene sequence is converted into a mature SLC2A1 gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Expression of SLC2A1 (very high) in severe COVID-19 HOIP_0040156 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycoytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040158 The movement of electrons from ubiquinol, which are transferred back to respiratory complex I, reducing NAD+ to NADH. PMID: 28701960 RET Reverse electron flow reverse electron transport HOIP_0040158 PMID: 28701960 The best example of site-specific ROS signaling is reverse electron transport (RET). RET is produced when electrons from ubiquinol are transferred back to respiratory complex I, reducing NAD+ to NADH. This process generates a significant amount of ROS. HOIP:HOIP_0040159 The movement of electrons from ubiquinol, which are transferred back to respiratory complex I, reducing NAD+ to NADH. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 RET in COVID-19 Reverse electron flow in COVID-19 reverse electron transport in COVID-19 HOIP_0040159 PMID:32697943 Succinate is known to drive reverse electron transport (RET) (Chouchani et al., 2014; Mills et al., 2016). These data indicate that RET is an important source of mtROS in CoV-2-infected monocytes. HOIP:HOIP_0040160 Any process that results in induction of metabolic reprogramming. Metabolic Reprogramming HOIP_0040160 HOIP:HOIP_0040161 Any process that results in induction of metabolic reprogramming. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 Metabolic Reprogramming in COVID-19 HOIP_0040161 PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. SARS-CoV-2-Induced Metabolic Reprogramming of Monocytes Directly Affects T Cell Response and Lung Epithelial Cell Death Proteomic analysis performed in CoV-2-infected monocytes confirmed alterations on oxidative metabolism with an overall downregulation of proteins involved in the TCA cycle (Figure S2D). Moreover, several components of respiratory electron chain com- plexes are downregulated in CoV-2-infected monocytes, such as NDUFV1 (complex I), SDHA (complex II), cytochrome c reductase COR1 and UQCRC2 (complex III), ATP5PF, ATP5F1A, ATP5PD, F-type ATPase a, and PPA2 (ATP synthase) (Figure S2D). These data indicate that RET is an important source of mtROS in CoV-2-infected monocytes. HOIP:HOIP_0040162 Expression of HIF1A is a subtype of gene expression: The process in which a gene sequence is converted into a mature HIF1A gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 Expression of HIF1A in COVID-19 HOIP_0040162 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. HOIP:HOIP_0040163 The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 T cell activation involved in immune response in COVID-19 HOIP_0040163 PMID:32697943 SARS-CoV-2-Induced Metabolic Reprogramming of Monocytes Directly Affects T Cell Response and Lung Epithelial Cell Death HOIP:HOIP_0040164 Negative regulation of T cell mediated immunity is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the T cell mediated immunity. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 PMID:32887954 Negative regulation of T cell mediated immunity in COVID-19 HOIP_0040164 PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. PMID:32887954 The 2–12-day incubation or presymptomatic period of SARS-CoV-2 infection is associated not only with virus-mediated innate immune suppression but also with delayed activation of T cells, particularly CD8+ T cells, as is the case for SARS and MERS. HOIP:HOIP_0040165 Expression of HIF1A is a subtype of gene expression: The process in which a gene sequence is converted into a mature HIF1A gene product or products (proteins or RNA). Expression of HIF1A HOIP_0040165 HOIP:HOIP_0040166 The expansion of a T cell population by cell division. Follows T cell activation. The expansion of a T cell population by cell division. Follows T cell activation. The expansion of a T cell population by cell division. Follows T cell activation. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 https://doi.org/10.1101/2020.07.17.20140533 T cell proliferation in COVID-19 drug treatment HOIP_0040166 The expansion of a T cell population by cell division. Follows T cell activation. GO:0042098 PMID:32697943 We found that CM-CoV-2 impaired CD4 and CD8 T cell proliferation (Figures 4A and S4I), whereas CM-BAY87 or CM-MitoQ restored T cell proliferation to the same extent as CM-Mock (Figures 4A and S4I). We observed that neutralization of IL-1b with anti-IL-1b (CM-aIL-1b) from UV-inactivated CM of CoV-2-infected monocytes restored T cell proliferation (Figures 4A and S4I). https://doi.org/10.1101/2020.07.17.20140533 Most participants had TH1 skewed T cell immune responses with RBD-specific CD8+ and CD4+ T cell expansion. HOIP:HOIP_0040167 Negative regulation of cell proliferation is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the cell proliferation. Negative regulation of cell proliferation HOIP_0040167 HOIP:HOIP_0040168 Negative regulation of T cell proliferation is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the T cell proliferation. Negative regulation of T cell proliferation HOIP_0040168 HOIP:HOIP_0040169 Negative regulation of T cell proliferation is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the T cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 negative regulation of T cell proliferation in COVID-19 HOIP_0040169 PMID:32697943 We found that CM-CoV-2 impaired CD4 and CD8 T cell proliferation (Figures 4A and S4I), whereas CM-BAY87 or CM-MitoQ restored T cell proliferation to the same extent as CM-Mock (Figures 4A and S4I). HOIP:HOIP_0040170 Negative regulation of INFG gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFNG gene expression. negative regulation of INFG expression HOIP_0040170 HOIP:HOIP_0040171 Negative regulation of INFG gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFNG gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 negative regulation of INFG expression in COVID-19 HOIP_0040171 PMID:32697943 Similarly, CM-CoV-2 decreased IFN-g production by CD4 T cells, and this was reversed in CM-BAY87 and CM-MitoQ and appeared to be reversed in CM-aIL-1b (Figures 4B and S4J). HOIP:HOIP_0040172 interferon-gamma production The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 interferon-gamma production in COVID-19 drug treatment HOIP_0040172 PMID:32697943 Similarly, CM-CoV-2 decreased IFN-g production by CD4 T cells, and this was reversed in CM-BAY87 and CM-MitoQ and appeared to be reversed in CM-aIL-1b (Figures 4B and S4J). HOIP:HOIP_0040173 A role played by the entity which that neutralizes the IL-1b by binding specifically to it. IL-1b antibody HOIP_0040173 HOIP:HOIP_0040174 anti-IL-1b (clone MAB601) HOIP_0040174 HOIP:HOIP_0040176 Expression of HIF1A is a subtype of gene expression: The process in which a gene sequence is converted into a mature HIF1A gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Expression of HIF1A (very high) in severe COVID-19 HOIP_0040176 PMID:32697943 When compared to healthy controls, BAL monocytes from severe COVID-19 patients had higher expression of HIF-1 target genes (Figure 3A). Blood monocytes from severe COVID-19 patients present high expression of HIF-1a in comparison to healthy donors (Figure 3C). We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). Altogether, these results highlight the metabolic alterations that take place in CoV-2-infected monocytes under high glucose conditions. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. HOIP:HOIP_0040177 Expression of LDHA is a subtype of gene expression: The process in which a gene sequence is converted into a mature LDHA gene product or products (proteins or RNA). Expression of LDHA HOIP_0040177 HOIP:HOIP_0040180 Expression of LDHA is a subtype of gene expression: The process in which a gene sequence is converted into a mature LDHA gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Expression of LDHA (severe)in severe COVID-19 HOIP_0040180 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040181 Expression of PFKFB3 is a subtype of gene expression: The process in which a gene sequence is converted into a mature PFKFB3 gene product or products (proteins or RNA). Expression of PFKFB3 HOIP_0040181 HOIP:HOIP_0040183 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 negative regulation of apoptotic process in COVID-19 drug treatment HOIP_0040183 PMID:32697943 CM-CoV-2 induced apoptosis of A549 cells (Figure 4D), which was prevented when CoV-2-infected monocytes were treated with a HIF-1a inhibitor (Figure 4D). HOIP:HOIP_0040184 Expression of PFKFB3 is a subtype of gene expression: The process in which a gene sequence is converted into a mature PFKFB3 gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Expression of PFKFB3 (very high) in severe COVID-19 HOIP_0040184 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040185 Expression of PKM is a subtype of gene expression: The process in which a gene sequence is converted into a mature PKM gene product or products (proteins or RNA). Expression of PKM HOIP_0040185 HOIP:HOIP_0040187 Expression of PKM is a subtype of gene expression: The process in which a gene sequence is converted into a mature PKM gene product or products (proteins or RNA). This entity is a specific course-dependent process.This process can constitute the course of severe COVID-19. PMID:32697943 Expression of PKM (very high) in severe COVID-19 HOIP_0040187 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040188 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 PMID:33188364 glycolysis glycolytic process in severe COVID-19 HOIP_0040188 PMID:32697943 Elevated Glucose Levels Favor SARS-CoV-2 Infection and Monocyte Response through a HIF-1a/ Glycolysis-Dependent Axis. Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Monocytes and macrophages are the most enriched immune cell types in the lungs of COVID-19 patients and appear to have a central role in the pathogenicity of the disease.These cells adapt their metabolism upon infection and become highly glycolytic, which facilitates SARS-CoV-2 replication. The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes Glycolysis Is Necessary for SARS-CoV-2 Replication and Monocyte Response Taken together, our results indicate that CoV-2 replication in monocytes and CoV-2-induced monocyte response are sustained by a switch to aerobic glycolysis (the Warburg effect). We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). PMID:33188364 In human monocytes, elevated glucose levels directly increase SARS-CoV-2 replication, and glycolysis sustains SARS-CoV-2 replication via the production of mitochondrial reactive oxygen species and activation of hypoxia-inducible factor 1α. HOIP:HOIP_0040193 Negative regulation of T cell proliferation is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the T cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 PMID:33077917 Negative regulation of T cell proliferation (very high) in severe COVID-19 HOIP_0040193 PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Exacerbated proinflammatory stimuli can negatively affect T cell response (de Marcken et al., 2019). We found that CM-CoV-2 impaired CD4 and CD8 T cell proliferation (Figures 4A and S4I), whereas CM-BAY87 or CM-MitoQ restored T cell proliferation to the same extent as CM-Mock (Figures 4A and S4I). These results provide evidence to explain why elevated glucose levels during CoV-2 infection may lead to T cell dysfunction and lymphopenia. PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. HOIP:HOIP_0040196 A protein that is a translation product of the human ISG15 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:9636 NCBI-Mouse-GeneID:100038882 NCBI-Rat-GeneID:298693 IP17 ISG15 interferon-induced 15 kDa protein interferon-induced 17 kDa protein ubiquitin-like protein ISG15 HOIP_0040196 NCBI-Human-GeneID:9636 http://www.ncbi.nlm.nih.gov/gene/9636 NCBI-Mouse-GeneID:100038882 http://www.ncbi.nlm.nih.gov/gene/100038882 NCBI-Rat-GeneID:298693 http://www.ncbi.nlm.nih.gov/gene/298693 HOIP:HOIP_0040197 Negative regulation of protein modification by small protein conjugation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of protein modification by small protein conjugation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of ISG15 modification by small protein conjugation in COVID-19 HOIP_0040197 PMID:32726803 Together, these results indicate that SCoV2-PLpro preferentially cleaves ISG15 from substrates over ubiquitin chains and Nedd8 in vitro, whereas SCoV-PLpro targets ubiquitin chains and, to a lesser extent, ISG15 and Nedd8 (Fig. 1d). HOIP:HOIP_0040198 Negative regulation of glucose metabolic process is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of glucose metabolic process. Negative regulation of glucose metabolic process HOIP_0040198 HOIP:HOIP_0040199 Negative regulation of glucose metabolic process is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of glucose metabolic process. This process can constitute the course of COVID-19 drug treatment. PMID:32697943 Negative regulation of glucose metabolic process in COVID-19 drug treatment HOIP_0040199 PMID:32697943 We used 2-DG to inhibit glucose flux and oligomycin to inhibit ATP synthase (Fig- ure 2A). Treatment with 2-DG completely blocked viral replication in CoV-2-infected monocytes, as well as the CoV-2-induced increase of ACE2 and IL-1b expression (Figures 2B–2D). HOIP:HOIP_0040200 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32697943 glycolysis glycolytic process (very low) in COVID-19 drug treatment HOIP_0040200 PMID:32697943 To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho-fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). HOIP:HOIP_0040202 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 increasing demand for response to oxidative stress in COVID-19 HOIP_0040202 PMID:32697943 We observed that oxidative stress-associated genes are enriched in BAL of severe COVID-19 patients (Figure 3A). (A) Single-cell RNA-seq data showing enrichment of HIF-1, glycolysis, and oxidative stress pathways in SARS-CoV-2 (CoV-2)-infected human monocytes. HOIP:HOIP_0040204 Malfunctioning of TCA cycle is a subtype of malfunctioning of metabolism: A process that cannot perform a tricarboxylic acid cycle appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Malfunctioning of TCA cycle (very high) in severe COVID-19 HOIP_0040204 PMID:32697943 Proteomic analysis performed in CoV-2-infected monocytes confirmed alterations on oxidative metabolism with an overall downregulation of proteins involved in the TCA cycle (Figure S2D). In agreement with our proteomic data, the spare respiratory capacity was reduced in CoV-2-infected monocytes (Figure 3I). Reduced respiration in LPS-activated macrophages is known to increase mitochondrial ROS (mtROS) production (Mills et al., 2016). HOIP:HOIP_0040205 Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon signaling pathway. Negative regulation of type I interferon signaling pathway HOIP_0040205 HOIP:HOIP_0040206 Any process that stops, prevents, or reduces the frequency, rate or extent of mitochondrial respiratory chain complex assembly. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Negative regulation of respiratory complex proteins synthesis (very high) in severe COVID-19 HOIP_0040206 PMID:32697943 Moreover, several components of respiratory electron chain complexes are downregulated in CoV-2-infected monocytes, such as NDUFV1 (complex I), SDHA (complex II), cytochrome c reductase COR1 and UQCRC2 (complex III), ATP5PF, ATP5F1A, ATP5PD, F-type ATPase a, and PPA2 (ATP synthase) (Figure S2D). In agreement with our proteomic data, the spare respiratory capacity was reduced in CoV-2-infected monocytes (Figure 3I). HOIP:HOIP_0040208 Reverse electron transport is a suntype of transport. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Reverse electron flow reverse electron transport (very high) in severe COVID-19 HOIP_0040208 PMID:32697943 Succinate is known to drive reverse electron transport (RET) (Chouchani et al., 2014; Mills et al., 2016). These data indicate that RET is an important source of mtROS in CoV-2-infected monocytes. These data may explain why uncontrolled diabetes may lead to compromised adaptive immune response and lung dysfunction in patients with severe COVID-19 symptoms. HOIP:HOIP_0040212 Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon signaling pathway. This process can constitute the course of COVID-19. PMID:32726803 PMID:33123165 Negative regulation of type I interferon signaling pathway in COVID-19 HOIP_0040212 PMID:32726803 Here we perform biochemical, structural and functional characterization of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) PLpro (SCoV2-PLpro) and outline differences with SARS-CoV PLpro (SCoV-PLpro) in regulation of host interferon and NF-κB pathways. Furthermore, upon infection, SCoV2-PLpro contributes to the cleavage of ISG15 from interferon responsive factor 3 (IRF3) and attenuates type I interferon responses. Having demonstrated a role for expression of SCoV2-PLpro and SCoV-PLpro in attenuating host antiviral IFN pathways, we anticipated that inhibition by GRL-0617 would reverse this process. Moreover, phosphorylation of IRF3 and TBK1, markers for IFN pathway activation, and p65 phosphorylation, used to monitor NF-κB pathway activation, were increased in SARS-CoV-2-infected cells upon GRL-0617 treatment (Fig. 5f). Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). Consistent with these observations, a recent study has shown that SARS-CoV-2 infection in animal models and in human patients with COVID-19 is correlated with low IFN type I and type III responses. PMID:33123165 Emerging data suggest that the innate response to SARS-CoV-2 is aberrant. For example, the early type I and III interferon responses are relatively suppressed by SARS-CoV-2, an immune evasion strategy employed by the virus, leading to early failure to control the virus. HOIP:HOIP_0040213 Type I interferon signaling is a subtype of biological signaling: A process transduced by the binding of a type I interferon to a receptor on the surface of a cell. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This process can constitute the course of COVID-19 drug treatment. PMID:32726803 type I interferon signaling in COVID-19 drug treatment HOIP_0040213 PMID:32726803 Notably, inhibition of SCoV2-PLpro with GRL-0617 impairs the virus-induced cytopathogenic effect, maintains the antiviral interferon pathway and reduces viral replication in infected cells. Indeed, GRL-0617 treatment of SARS-CoV-2-infected cells led to a marked increase in IRF3 ISGylation (Fig. 5e), which has previously been shown to regulate antiviral immune response. However, we found that GRL-0617 was consistently more effective in restoring ISGylation and phosphorylation level of IRF3 and expression of IFN-responsive genes upon infection with SARS-CoV-2 compared with SARS-CoV (Fig. 5e–g). Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0040214 Negative regulation of SCoV2-PLpro activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of SCoV2-PLpro activation. Negative regulation of SCoV2-PLpro activation HOIP_0040214 HOIP:HOIP_0040215 Negative regulation of viral enzyme activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of viral enzyme activation. negative regulation of viral enzyme activation HOIP_0040215 HOIP:HOIP_0040216 Negative regulation of SCoV2-PLpro activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of SCoV2-PLpro activation. This process can constitute the course of COVID-19 drug treatment. PMID:32726803 Negative regulation of SCoV2-PLpro activation in COVID-19 drug treatment HOIP_0040216 PMID:32726803 Notably, inhibition of SCoV2-PLpro with GRL-0617 impairs the virus-induced cytopathogenic effect, maintains the antiviral interferon pathway and reduces viral replication in infected cells. HOIP:HOIP_0040221 Positive regulation of ACE2 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of ACE2 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32413319 PMID:32697943 positive regulation of ACE2 gene expression in COVID-19 HOIP_0040221 PMID:32413319 We directly tested whether IFN-a induces ACE2 in primary human upper airway epithelial cells in greater detail. Only IFN-a2 and IFN-g led to upregulation of ACE2 over the time period tested, and compared with all other cytokines, IFN-a2 lead to greater and more significant upregulation over all doses tested (Fig- ure S3D,Wilcoxon test: IFN-a2 FDR-adjusted p = 4.1E-07; IFN-g p = 9.3E-03,Figures S3E and S3F, all statistical tests compared with 0 ng/mL dose). PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0040227 Interaction between any viral protein (or viral protein complex) and any host protein (or host protein complex). Viral protein-host protein interactions Viral-host PPI viral protein-host protein binding HOIP_0040227 HOIP:HOIP_0040228 Interaction between any viral protein (or viral protein complex) and any host protein (or host protein complex). This process can constitute the course of COVID-19. PMID:32726803 Viral protein-host protein interactions Viral-host PPI viral protein-host protein binding in COVID-19 HOIP_0040228 PMID:32726803 Moreover, these closely related PLpro enzymes associate with distinct and specific sets of host proteins (Fig. 4a). For SCoV2-PLpro, these interactions include PRKDC (associated with induction by type I interferons), heterogenous nuclear ribonucleoprotein K (HNRNPK; involved in host RNA splicing, a process essential for SARS-CoV-2 replication in cells) and galectin1, which can induce viral fusion with target cells during HIV infection (Fig. 4a). HOIP:HOIP_0040229 NCBI-Human-GeneID:3190 NCBI-Mouse-GeneID:15387 NCBI-Rat-GeneID:117282 heterogeneous nuclear ribonucleoprotein K HOIP_0040229 NCBI-Human-GeneID:3190 http://www.ncbi.nlm.nih.gov/gene/3190 NCBI-Mouse-GeneID:15387 http://www.ncbi.nlm.nih.gov/gene/15387 NCBI-Rat-GeneID:117282 http://www.ncbi.nlm.nih.gov/gene/117282 HOIP:HOIP_0040230 NCBI-Human-GeneID:55803 NCBI-Mouse-GeneID:216991 NCBI-Rat-GeneID:56826 ADAP2 (mol) HOIP_0040230 NCBI-Human-GeneID:55803 http://www.ncbi.nlm.nih.gov/gene/55803 NCBI-Mouse-GeneID:216991 http://www.ncbi.nlm.nih.gov/gene/216991 NCBI-Rat-GeneID:56826 http://www.ncbi.nlm.nih.gov/gene/56826 HOIP:HOIP_0040232 A protein that is a translation product of the human PRKDC gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:5591 NCBI-Mouse-GeneID:19090 NCBI-Rat-GeneID:360748 DNA-PK catalytic subunit DNPK1 PRKDC DNA-dependent protein kinase catalytic subunit HOIP_0040232 NCBI-Human-GeneID:5591 http://www.ncbi.nlm.nih.gov/gene/5591 NCBI-Mouse-GeneID:19090 http://www.ncbi.nlm.nih.gov/gene/19090 NCBI-Rat-GeneID:360748 http://www.ncbi.nlm.nih.gov/gene/360748 HOIP:HOIP_0040233 Negative regulation of ISG15 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of ISG15 gene expression. Negative regulation of ISG15 gene expression HOIP_0040233 HOIP:HOIP_0040235 Expression of PRKDC is a subtype of gene expression: The process in which a gene sequence is converted into a mature PRKDC gene product or products (proteins or RNA). Expression of PRKDC HOIP_0040235 HOIP:HOIP_0040237 host RNA splicing is a subtype of removing: The process of removing sections of the host RNA transcript to remove sequences. host RNA splicing HOIP_0040237 HOIP:HOIP_0040239 Negative regulation of protein modification by small protein conjugation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of protein modification by small protein conjugation. Negative regulation of protein modification by small protein conjugation HOIP_0040239 HOIP:HOIP_0040240 Negative regulation of IRF3 modification by small protein conjugation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IRF3 modification by small protein conjugation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of IRF3 modification by small protein conjugation in COVID-19 HOIP_0040240 PMID:32726803 Consistently, expression of SCoV2-PLpro and SCoV-PLpro in mammalian cells decreased ISGylation of cellular proteins following IFN-α stimulation (Extended Data Fig. 5c), including ISGylation of interferon regulatory factor 3 (IRF3), a critical component in the type 1 interferon pathway. Both SCoV2-PLpro and SCoV-PLpro reduced IRF3 ISGylation, with SCoV2-PLpro having a more potent effect (Fig. 4d). HOIP:HOIP_0040241 A process by which Plpro gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. This process can constitute the course of COVID-19. PMID:32726803 Plpro gene expression in COVID-19 HOIP_0040241 PMID:32726803 Consistently, expression of SCoV2-PLpro and SCoV-PLpro in mammalian cells decreased ISGylation of cellular proteins following IFN-α stimulation (Extended Data Fig. 5c), including ISGylation of interferon regulatory factor 3 (IRF3), a critical component in the type 1 interferon pathway. Decreases in phosphorylation of TBK1 and IRF3, and nuclear translocation of IRF3 were detected upon expression of SCoV-PLpro or SCoV2-PLpro (Extended Data Fig. 5d, e). Expression of SCoV2-PLpro more effectively decreased the activation of the IFNB1 promoter compared with SCoV-PLpro following poly(I:C) treatment. HOIP:HOIP_0040242 Negative regulation of ISG15 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of ISG15 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of ISG15 gene expression in COVID-19 HOIP_0040242 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0040243 Negative regulation of protein phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of protein phosphorylation. Negative regulation of protein phosphorylation HOIP_0040243 HOIP:HOIP_0040244 Negative regulation of TBK1 phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of TBK1 phosphorylation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of TBK1 phosphorylation in COVID-19 HOIP_0040244 PMID:32726803 Decreases in phosphorylation of TBK1 and IRF3, and nuclear translocation of IRF3 were detected upon expression of SCoV-PLpro or SCoV2-PLpro (Extended Data Fig. 5d, e). TBK1 phosphorylation also activates the NF-κB pathway, causing upregulation of inflammatory signalling30. HOIP:HOIP_0040245 Negative regulation of OAS1 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of OAS1 gene expression. Negative regulation of OAS1 gene expression HOIP_0040245 HOIP:HOIP_0040246 Negative regulation of nuclear transport is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substance into, out of or within a nucleus by means of some agent such as a transporter or pore. Negative regulation of nuclear transport HOIP_0040246 HOIP:HOIP_0040247 Negative regulation of nuclear transport is a subtype of negative regulation of transport: Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substance into, out of or within a nucleus by means of some agent such as a transporter or pore. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of nuclear transport in COVID-19 HOIP_0040247 PMID:32726803 Decreases in phosphorylation of TBK1 and IRF3, and nuclear translocation of IRF3 were detected upon expression of SCoV-PLpro or SCoV2-PLpro (Extended Data Fig. 5d, e). HOIP:HOIP_0040248 Negative regulation of OAS1 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of OAS1 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of OAS1 gene expression in COVID-19 HOIP_0040248 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0040249 Negative regulation of INFB1 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFNB1 gene expression. This process can constitute the course of COVID-19. PMID:32726803 negative regulation of INFB1 expression in COVID-19 HOIP_0040249 PMID:32726803 Expression of SCoV2-PLpro more effectively decreased the activation of the IFNB1 promoter compared with SCoV-PLpro following poly(I:C) treatment. HOIP:HOIP_0040250 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. The functioning level is low. PMID:32726803 interferon-beta production (very low) in COVID-19 HOIP_0040250 PMID:32726803 Expression of SCoV2-PLpro more effectively decreased the activation of the IFNB1 promoter compared with SCoV-PLpro following poly(I:C) treatment. HOIP:HOIP_0040251 The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32629875 PMID:32726803 ウイルス排出 viral release from host cell (very low) in COVID-19 drug treatment HOIP_0040251 PMID:32629875 In addition, the antiviral drug, remdesivir, which has received Emergency Use Authorization for the treatment of hospitalized patients with suspected or laboratory-confirmed, severe COVID-19 could also be beneficial to reduce replication and release of infectious particles (NCT04292730). PMID:32726803 In addition, GRL-0617 treatment reduced active viral replication (SARS-CoV-2 subgenomic RNA4-encoding E gene), as measured by genetic monitoring of the intracellular production of viral RNA (Fig. 5c). Consequently, a decrease in the release of viral particles from infected cells into the supernatant was also observed upon GRL-0617 treatment (Fig. 5d, Extended Data Fig. 7a). HOIP:HOIP_0040252 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces the full-length negative stranded (-) mRNA for synthesis of new genomic RNAs and subgenomic negative strand templates. This process can constitute the course of COVID-19 drug treatment. PMID:32726803 full length negative stranded viral mRNA biosynthetic process full length negative stranded viral mRNA biosynthetic process (very low) in COVID-19 drug treatment HOIP_0040252 PMID:32726803 This suggests that inhibition of SCoV2-PLpro by GRL-0617 impedes viral replication, thereby attenuating the ongoing viral RNA synthesis. HOIP:HOIP_0040253 Negative regulation of IRF3 phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IRF3 phosphorylation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of IRF3 phosphorylation in COVID-19 HOIP_0040253 PMID:32726803 Decreases in phosphorylation of TBK1 and IRF3, and nuclear translocation of IRF3 were detected upon expression of SCoV-PLpro or SCoV2-PLpro (Extended Data Fig. 5d, e). HOIP:HOIP_0040254 Any process that stops, prevents, or reduces the frequency, rate, or extent of NfkB signaling. Negative regulation of NfkB signaling HOIP_0040254 HOIP:HOIP_0040255 Any process that stops, prevents, or reduces the frequency, rate, or extent of NfkB signaling. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of NfkB signaling in COVID-19 HOIP_0040255 PMID:32726803 Decreases in phosphorylation of TBK1 and IRF3, and nuclear translocation of IRF3 were detected upon expression of SCoV-PLpro or SCoV2-PLpro (Extended Data Fig. 5d, e). TBK1 phosphorylation also activates the NF-κB pathway, causing upregulation of inflammatory signalling30. HOIP:HOIP_0040256 Negative regulation of inflammatory response is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Wikipedia:Inflammation negative regulation of inflammatory response in COVID-19 HOIP_0040256 PMID:32726803 Decreases in phosphorylation of TBK1 and IRF3, and nuclear translocation of IRF3 were detected upon expression of SCoV-PLpro or SCoV2-PLpro (Extended Data Fig. 5d, e). TBK1 phosphorylation also activates the NF-κB pathway, causing upregulation of inflammatory signalling. Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0040257 Negative regulation of EIF2AK2 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of EIF2AK2 gene expression. Negative regulation of EIF2AK2 gene expression HOIP_0040257 HOIP:HOIP_0040258 Negative regulation of EIF2AK2 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of EIF2AK2 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of EIF2AK2 gene expression in COVID-19 HOIP_0040258 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0040259 Negative regulation of MX1 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of MX1 gene expression. Negative regulation of MX1 gene expression HOIP_0040259 HOIP:HOIP_0040260 Negative regulation of MX1 gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of MX1 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of MX1 gene expression in COVID-19 HOIP_0040260 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0040261 Type III interferon signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by Type III interferon. Type III interferon signaling HOIP_0040261 HOIP:HOIP_0040262 Positive regulation of TNFΑ gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of TNFΑ gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 Positive regulation of TNFΑ gene expressionin COVID-19 HOIP_0040262 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0040263 A series of molecular signals initiated by the binding of a type III interferon to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. Type III interferons include the interferon-lamda gene families. type III interferon-activated signaling pathway type III interferon-mediated signalling pathway type III interferon signaling pathway HOIP_0040263 HOIP:HOIP_0040264 Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon signaling pathway. Negative regulation of type III interferon signaling pathway HOIP_0040264 HOIP:HOIP_0040265 Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon signaling pathway. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 PMID:33123165 Negative regulation of type III interferon signaling pathway in COVID-19 HOIP_0040265 PMID:32726803 Consistent with these observations, a recent study has shown that SARS-CoV-2 infection in animal models and in human patients with COVID-19 is correlated with low IFN type I and type III responses. PMID:33123165 Emerging data suggest that the innate response to SARS-CoV-2 is aberrant. For example, the early type I and III interferon responses are relatively suppressed by SARS-CoV-2, an immune evasion strategy employed by the virus, leading to early failure to control the virus. HOIP:HOIP_0040266 Negative regulation of IRF3 phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IRF3 phosphorylation. Negative regulation of IRF3 phosphorylation HOIP_0040266 HOIP:HOIP_0040267 IRF3 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into IRF3. IRF3 phosphorylation HOIP_0040267 HOIP:HOIP_0040268 Negative regulation of TBK1 phosphorylation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of TBK1 phosphorylation. Negative regulation of TBK1 phosphorylation HOIP_0040268 HOIP:HOIP_0040269 TBK1 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into TBK1. TBK1 phosphorylation HOIP_0040269 HOIP:HOIP_0040270 Negative regulation of IRF3 modification by small protein conjugation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IRF3 modification by small protein conjugation. Negative regulation of IRF3 modification by small protein conjugation HOIP_0040270 HOIP:HOIP_0040271 A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to IRF3. IRF3 modification by small protein conjugation HOIP_0040271 HOIP:HOIP_0040274 Positive regulation of PKM gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of PKM gene expression. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of PKM gene expression (very high) in severe COVID-19 HOIP_0040274 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycoytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040276 Positive regulation of PFKFB3 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of PFKFB3 gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of PFKFB3 gene expression (very high) in severe COVID-19 HOIP_0040276 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040278 Positive regulation of LDHA gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of LDHA gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of LDHA gene expression (very high) in severe COVID-19 HOIP_0040278 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycolytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040279 Positive regulation of IL1B gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IL1B gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of IL1B gene expression (severe)in severe COVID-19 HOIP_0040279 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). We observed that neutralization of IL-1b with anti-IL-1b (CM-aIL-1b) from UV-inactivated CM of CoV-2-infected monocytes restored T cell proliferation (Figures 4A and S4I). HOIP:HOIP_0040280 Positive regulation of IL-6 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IL-6 gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of IL-6 gene expression (very high) in severe COVID-19 HOIP_0040280 PMID:32697943 Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0040283 Positive regulation of SLC2A1 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of SLC2A1 gene expression. Positive regulation of SLC2A1 gene expression HOIP_0040283 HOIP:HOIP_0040284 Positive regulation of SLC2A1 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of SLC2A1 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 Positive regulation of SLC2A1 gene expression in COVID-19 HOIP_0040284 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycoytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040285 Positive regulation of SLC2A1 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of SLC2A1 gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 Positive regulation of SLC2A1 gene expression (severe)in severe COVID-19 HOIP_0040285 PMID:32697943 We observed that HIF-1a protein levels and its transcriptional activity measured by the target genes GLUT-1, PFKFB3, PKM2, and LDH-A, which are involved in the glucose transport and glycoytic pathway, were increased in CoV-2-infected monocytes (Figures 3D and S4A). HOIP:HOIP_0040286 Positive regulation of IFNB1 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IFNB1gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 positive regulation of IFNB1 gene expression (severe)in severe COVID-19 HOIP_0040286 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0040287 Any process that activates or increases the frequency, rate or extent of glycolytic process. positive regulation of glycolytic process HOIP_0040287 HOIP:HOIP_0040290 Negative regulation of CTSL gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of CTSL gene expression. Negative regulation of CTSL gene expression HOIP_0040290 HOIP:HOIP_0040292 Expression of CTSL is a subtype of gene expression: The process in which a gene sequence is converted into a mature CTSL gene product or products (proteins or RNA). Expression of CTSL HOIP_0040292 HOIP:HOIP_0040293 Expression of CTSL is a subtype of gene expression: The process in which a gene sequence is converted into a mature CTSL gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Expression of CTSL in COVID-19 HOIP_0040293 HOIP:HOIP_0040295 Negative regulation of IRF3 phosphorylation inhibition is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IRF3 phosphorylation inhibition. This process can constitute the course of COVID-19 drug treatment. PMID:32726803 Negative regulation of IRF3 phosphorylation inhibition in COVID-19 drug treatment HOIP_0040295 PMID:32726803 However, we found that GRL-0617 was consistently more effective in restoring ISGylation and phosphorylation level of IRF3 and expression of IFN-responsive genes upon infection with SARS-CoV-2 compared with SARS-CoV (Fig. 5e–g). These findings provide evidence that inhibition of SCoV2-PLpro, in addition to blocking viral RNA synthesis, can also increase antiviral signalling via TBK1 and IRF3 (Extended Data Fig. 7c). HOIP:HOIP_0040296 Negative regulation of IRF3 phosphorylation inhibition is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IRF3 phosphorylation inhibition. Negative regulation of IRF3 phosphorylation inhibition HOIP_0040296 HOIP:HOIP_0040297 Negative regulation of TBK1 phosphorylation inhibition is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of TBK1 phosphorylation inhibition. Negative regulation of TBK1 phosphorylation inhibition HOIP_0040297 HOIP:HOIP_0040298 Negative regulation of TBK1 phosphorylation inhibition is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of TBK1 phosphorylation inhibition.　This process can constitute the course of COVID-19 drug treatment. PMID:32726803 Negative regulation of TBK1 phosphorylation inhibition in COVID-19 drug treatment HOIP_0040298 PMID:32726803 Moreover, phosphorylation of IRF3 and TBK1, markers for IFN pathway activation, and p65 phosphorylation, used to monitor NF-κB pathway activation, were increased in SARS-CoV-2-infected cells upon GRL-0617 treatment (Fig. 5f). TBK1 phosphorylation also activates the NF-κB pathway, causing upregulation of inflammatory signalling. These findings provide evidence that inhibition of SCoV2-PLpro, in addition to blocking viral RNA synthesis, can also increase antiviral signalling via TBK1 and IRF3 (Extended Data Fig. 7c). HOIP:HOIP_0040299 Negative regulation of IRF3 modification by small protein conjugation inhibition is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IRF3 modification by small protein conjugation inhibition. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 Negative regulation of IRF3 modification by small protein conjugation inhibition in COVID-19 drug treatment HOIP_0040299 PMID:32726803 Indeed, GRL-0617 treatment of SARS-CoV-2-infected cells led to a marked increase in IRF3 ISGylation (Fig. 5e), which has previously been shown to regulate antiviral immune response. However, we found that GRL-0617 was consistently more effective in restoring ISGylation and phosphorylation level of IRF3 and expression of IFN-responsive genes upon infection with SARS-CoV-2 compared with SARS-CoV (Fig. 5e–g). Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). Notably, inhibition of SCoV2-PLpro with GRL-0617 impairs the virus-induced cytopathogenic effect, maintains the antiviral interferon pathway and reduces viral replication in infected cells. These findings provide evidence that inhibition of SCoV2-PLpro, in addition to blocking viral RNA synthesis, can also increase antiviral signalling via TBK1 and IRF3 (Extended Data Fig. 7c). HOIP:HOIP_0040300 Negative regulation of IRF3 modification by small protein conjugation inhibition is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IRF3 modification by small protein conjugation inhibition. Negative regulation of IRF3 modification by small protein conjugation inhibition HOIP_0040300 HOIP:HOIP_0040301 NfkB signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by NF-kappaB. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. PMID:32726803 NfkB signaling(very low) in COVID-19 drug treatment HOIP_0040301 PMID:32726803 Moreover, phosphorylation of IRF3 and TBK1, markers for IFN pathway activation, and p65 phosphorylation, used to monitor NF-κB pathway activation, were increased in SARS-CoV-2-infected cells upon GRL-0617 treatment (Fig. 5f). TBK1 phosphorylation also activates the NF-κB pathway, causing upregulation of inflammatory signalling. HOIP:HOIP_0040303 Negative regulation of IFN-responsive gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFN-responsive gene expression. Negative regulation of IFN-responsive gene expression HOIP_0040303 HOIP:HOIP_0040304 Negative regulation of IFN-responsive gene expression is a subtype of negative regulation of gene expression: A process that stops, prevents, or reduces the frequency, rate or extent of IFN-responsive gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32726803 negative regulation of IFN-responsive gene expression in COVID-19 HOIP_0040304 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0040305 Negative regulation of IFN-responsive gene expression inhibition is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IFN-responsive gene expression inhibition. Negative regulation of IFN-responsive gene expression inhibition HOIP_0040305 HOIP:HOIP_0040306 Negative regulation of IFN-responsive gene expression inhibition is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of IFN-responsive gene expression inhibition. PMID:32726803 Negative regulation of IFN-responsive gene expression inhibition in COVID-19 drug treatment HOIP_0040306 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). HOIP:HOIP_0040312 The inhibition of an antigen's biological effects by antibody binding to it. An example is neutralization of diphtheria toxin by preventing its entry into human cells via the binding of antibody specific for diphtheria toxin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32887954 immunoglobulin-mediated neutralization in COVID-19 vaccination HOIP_0040312 PMID:32887954 Protective IgG antibodies induced by parenteral vaccination readily appear at the respiratory mucosa, this being the primary mechanism by which intramuscular injection of measles or influenza vaccine offers protection in humans. However, this route of vaccination is unable to effectively induce mucosal IgA antibodies or TRM cells in the lungs HOIP:HOIP_0040313 Any process that contributes to cytokine production by a T-helper 1 cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32663912 PMID:33123165 https://doi.org/10.1101/2020.07.17.20140533 T-helper 1 cell cytokine production in COVID-19 vaccination HOIP_0040313 PMID:32663912 The 25-micro g and 100-micro g doses elicited CD4 T-cell responses (Figs. S9 and S10) that on stimulation by S-specific peptide pools were strongly biased toward expression of Th1 cytokines (tumor necrosis factor alpha > interleukin 2 > interferon gamma), with minimal type 2 helper T-cell (Th2) cytokine expression (interleukin 4 and interleukin 13). PMID:33123165 T cell responses measured by intracellular staining for Th1 (TNF, IL-2, IFN-γ) and Th2 (IL-4, IL-13) cytokines following stimulation with an S protein peptide pool showed a Th1 cytokine bias and low-level CD8 T cell responses. (mRNA-1273) https://doi.org/10.1101/2020.07.17.20140533 Most participants had TH1 skewed T cell immune responses with RBD-specific CD8+ and CD4+ T cell expansion. Interferon (IFN)γ was produced by a high fraction of RBD-specific CD8+ and CD4+ T cells. In summary, these findings indicate that BNT162b1 induces functional and proinflammatory CD4+/CD8+ T cell responses in almost all participants, with TH1 polarisation of the helper response. The detection of IFNgamma, IL-2 and IL-12p70 but not IL-4 indicates a favorable TH1 profile and the absence of a potentially deleterious TH2 immune response. HOIP:HOIP_0040314 The appearance of interleukin-2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32998157 PMID:33053279 PMID:33123165 https://doi.org/10.1101/2020.07.17.20140533 interleukin-2 production in COVID-19 vaccination HOIP_0040314 PMID:32998157 RBD-specific CD4+ T cells secreted IFNgamma, IL-2, or both, but in most individuals they did not secrete IL-4 (Fig. 4 a–c, Extended Data Table 6). Similarly, fractions of RBD-specific CD8+ T cells secreted IFNgamma+ and IL-2. PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. PMID:33123165 Intracellular staining confirmed production of IFN-γ, tumor necrosis factor (TNF) and interleukin-2 (IL-2) by both CD4+ and CD8+ T cells following Ad5-nCoV immunization, with more cytokine detected in CD4+ T cells as compared to CD8+ T cells. T cell responses measured in 16 participants showed that NVX-CoV2373/Matrix-M1 induces antigen-specific polyfunctional CD4+ T cell responses (IFN-γ, IL-2, and TNF- α) in response to spike protein stimulation; there was a strong bias toward this Th1 phenotype. T cell responses measured by intracellular staining for Th1 (TNF, IL-2, IFN-γ) and Th2 (IL-4, IL-13) cytokines following stimulation with an S protein peptide pool showed a Th1 cytokine bias and low-level CD8 T cell responses. (mRNA-1273) https://doi.org/10.1101/2020.07.17.20140533 RBD-specific CD4+ T cells secreted IFNgamma, IL-2, or both, but did not secrete IL-4 (Figure 4a-c). Similarly, fractions of RBD-specific CD8+ T cells secreted IFNγ+ and IL-2. The detection of IFNgamma, IL-2 and IL-12p70 but not IL-4 indicates a favorable TH1 profile and the absence of a potentially deleterious TH2 immune response. HOIP:HOIP_0040316 The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32663912 PMID:32998157 PMID:33123165 tumor necrosis factor production in COVID-19 vaccination HOIP_0040316 PMID:32663912 The 25-micro g and 100-micro g doses elicited CD4 T-cell responses (Figs. S9 and S10) that on stimulation by S-specific peptide pools were strongly biased toward expression of Th1 cytokines (tumor necrosis factor alpha > interleukin 2 > interferon gamma), with minimal type 2 helper T-cell (Th2) cytokine expression (interleukin 4 and interleukin 13). PMID:32998157 The supernatants of PBMCs from five vaccinated participants were stimulated ex vivo with overlapping RBD peptides and produced the proinflammatory cytokines TNF, IL-1beta and IL-12p70, but neither IL-4 nor IL-5 (Fig. 4d). PMID:33123165 Intracellular staining confirmed production of IFN-γ, tumor necrosis factor (TNF) and interleukin-2 (IL-2) by both CD4+ and CD8+ T cells following Ad5-nCoV immunization, with more cytokine detected in CD4+ T cells as compared to CD8+ T cells. T cell responses measured in 16 participants showed that NVX-CoV2373/Matrix-M1 induces antigen-specific polyfunctional CD4+ T cell responses (IFN-γ, IL-2, and TNF- α) in response to spike protein stimulation; there was a strong bias toward this Th1 phenotype. T cell responses measured by intracellular staining for Th1 (TNF, IL-2, IFN-γ) and Th2 (IL-4, IL-13) cytokines following stimulation with an S protein peptide pool showed a Th1 cytokine bias and low-level CD8 T cell responses. (mRNA-1273) HOIP:HOIP_0040317 Changing viral spike S protein S2 domain structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein S2 domain. changing viral spike S2 protein conformation changing viral spike S2 protein structure HOIP_0040317 HOIP:HOIP_0040318 Changing viral spike S protein S2 domain structure is a subtype of changing protein structure: A process that changes the stucture of the viral spike S protein S2 domain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 changing viral spike S2 protein conformation changing viral spike S2 protein structure in COVID-19 HOIP_0040318 PMID:33123165 The virus receptor, angiotensin-converting enzyme 2 (ACE2), expressed on the surface of multiple human cells is engaged via the receptor binding domain (RBD), which is part of the S1 subunit of the S glycoprotein. Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. HOIP:HOIP_0040320 Tissue damage is a subtype of damaging: A process that injuries the structure of the tissue as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Tissue damage in COVID-19 HOIP_0040320 HOIP:HOIP_0040323 The appearance of interleukin-10 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 interleukin-10 production in COVID-19 HOIP_0040323 PMID:33123165 For example, patients with severe COVID-19 had higher levels of IL-6, IL-2R, IL-10, and tumor necrosis factor alpha (TNF-alpha) than those with moderate disease, the former of which correlated with clinical severity and death. Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040324 The appearance of interleukin-10 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 interleukin-10 production (very high) in severe COVID-19 HOIP_0040324 PMID:32629875 A retrospective study of 21 patients identified significant elevations of plasma IL-6, IL-10, TNFα and IL-2 receptor in severe (n = 11) compared to moderate (n = 10) cases of COVID-19, whereas IL-1β and IL-8 levels were not significantly different. Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. PMID:33123165 For example, patients with severe COVID-19 had higher levels of IL-6, IL-2R, IL-10, and tumor necrosis factor alpha (TNF-alpha) than those with moderate disease, the former of which correlated with clinical severity and death. Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. Furthermore, IL-10 is an immunosuppressive cytokine suggesting dysregulated immune homeostasis rather than pure inflammation. HOIP:HOIP_0040325 IL-2R production is a subtype of protein production: A process that makes existent of a IL-2R protein due to biosynthesis or secretion resulting in an increase in its levels. IL-2R production HOIP_0040325 HOIP:HOIP_0040326 IL-2R production is a subtype of protein production: A process that makes existent of a IL-2R protein due to biosynthesis or secretion resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 IL-2R production in COVID-19 HOIP_0040326 PMID:33123165 For example, patients with severe COVID-19 had higher levels of IL-6, IL-2R, IL-10, and tumor necrosis factor alpha (TNF-alpha) than those with moderate disease, the former of which correlated with clinical severity and death. HOIP:HOIP_0040327 IL-2R production is a subtype of protein production: A process that makes existent of a IL-2R protein due to biosynthesis or secretion resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 IL-2R production (severe)in severe COVID-19 HOIP_0040327 PMID:32629875 A retrospective study of 21 patients identified significant elevations of plasma IL-6, IL-10, TNFα and IL-2 receptor in severe (n = 11) compared to moderate (n = 10) cases of COVID-19, whereas IL-1β and IL-8 levels were not significantly different. PMID:33123165 For example, patients with severe COVID-19 had higher levels of IL-6, IL-2R, IL-10, and tumor necrosis factor alpha (TNF-alpha) than those with moderate disease, the former of which correlated with clinical severity and death. HOIP:HOIP_0040328 The appearance of a cytokine receptor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. cytokine receptor production HOIP_0040328 HOIP:HOIP_0040329 The appearance of interleukin-2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 interleukin-2 production in COVID-19 HOIP_0040329 PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040330 The appearance of interleukin-2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process.This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 interleukin-2 production (very high) in severe COVID-19 HOIP_0040330 PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040332 an mRNA–lipid nanoparticle vaccine encoding the S protein RBD. PMID:32887954 PMID:32967006 PMID:32998157 PMID:33123165 PMID:33340022 https://clinicaltrials.gov/ct2/show/NCT04368728 BNT162 BNT162b1 vaccine HOIP_0040332 PMID:32887954 Table 2 Preclinical data: Published data from mouse model showing strong antibody and T cell responses, Clinical data: Submitted report indicating safety, high neutralizing antibody titres and TH1 cell-type CD4+ and CD8+ T cell responses Pfizer and BioNTech are also assessing an mRNA–lipid nanoparticle vaccine encoding the S protein RBD (known as BNT162b1) in humans, who developed robust S protein-specific antibody and CD4+ and CD8+ T cell responses following two repeated parenteral injections. PMID:32967006 In an additional study, Pfizer recently reported a direct comparison between BNT162b1 and BNT162b2 (NCT04368728). Whereas antibody titres between the two candidates were comparable, BNT162b2 showed a more favourable safety profile. PMID:32998157 BNT162b1 encodes the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein, a key target of neutralising antibodies. Recently, we reported safety, tolerability and antibody response data from an ongoing placebo-controlled, observer-blinded phase 1/2 COVID-19 vaccine trial with BNT162b1, a lipid nanoparticle (LNP) formulated nucleoside-modified messenger RNA encoding the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Here we present antibody and T cell responses after BNT162b1 vaccination from a second, non-randomized open-label phase 1/2 trial in healthy adults, 18-55 years of age. Two doses of 1 to 50 μg of nBNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those in a COVID-19 convalescent human serum panel (HCS). Most participants had TH1 skewed T cell immune responses with RBD-specific CD8+ and CD4+ T cell expansion. Interferon (IFN)gamma was produced by a high fraction of RBD-specific CD8+ and CD4+ T cells. PMID:33123165 An interim report from the Phase 1/2 dose-ranging study of 2 doses of BioNTech’s mRNA S protein vaccine candidate BNT162 administered to adults aged 18–55 years elicited RBD-binding IgG and SARS-CoV-2 nAbs in the order of 1.8–2.8- fold that of convalescent human plasma. This vaccine encodes trimerized RBD which is modified by adding a “foldon” trimerization domain to increase immunogenicity. PMID:33340022 S-2P LNP-mRNA Full-length S with two proline substitutions (K986P and V987P) BioNTech, with Fosun Pharma and Pfizer, Germany Induction of S1-specific IgG and nAbs in humans, with nAb titres higher than convalescent plasma HOIP:HOIP_0040333 an Inactivated SARS-CoV-2 vaccine encoding multiple viral antigens PMID:32778225 PMID:32887954 PMID:33123165 BBIP-CorV BBIBP-CorV vaccine HOIP_0040333 PMID:32887954 Table 2 Preclinical data: Published data from rodents, rabbits and NHP models showing neutralizing antibodies and protection, Clinical data: Interim information released to indicate safety and high antibody conversion rates in vaccinees PMID:33123165 The Beijing inactivated vaccine candidate (BBIP-CorV) has published pre-clinical data confirming induction of high levels of nAbs in several animal models and protection against intra-tracheal SARS-CoV-2 challenge in rhesus macaques after 2 doses of vaccine. HOIP:HOIP_0040339 a protein subunit vaccine encoding S protein PMID:32887954 MVC-COV1901 vaccine HOIP_0040339 PMID:32887954 Table 2 Preclinical data: Information released indicating induction of neutralizing antibodies and T cells HOIP:HOIP_0040340 Negative regulation of viral spike S protein structure change is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral spike S protein structure change. Negative regulation of viral spike S protein structure change HOIP_0040340 HOIP:HOIP_0040342 Negative regulation of innate immune response is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of innate immune response. Negative regulation of innate immune response HOIP_0040342 HOIP:HOIP_0040344 The appearance of interleukin-7 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 interleukin-7 production in COVID-19 HOIP_0040344 PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040345 Cytolysis of target cells by natural killer cells, eosinophils, neutrophils, monocytes, or macrophages following engagement of antibodies bound to the target cells by Fc receptors on the effector cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32887954 antibody-dependent cellular cytotoxicity in COVID-19 HOIP_0040345 PMID:32887954 Furthermore, patients with symptomatic COVID-19 are reported to produce IgG anti-bodies with reduced fucosylation levels, which in turn promotes their interaction with activating FcgammaRIIIa. Fc-mediated effector functions: immune functions that are mediated through the interaction of the constant Fc region of antibodies with innate immune molecules, complement proteins and specialized Fc receptors expressed by innate immune cells. The resulting functions include complement-dependent cytotoxicity and antibody-dependent cellular phagocytosis or cell-mediated cytotoxicity. HOIP:HOIP_0040346 The appearance of interleukin-7 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 interleukin-7 production (very high) in severe COVID-19 HOIP_0040346 PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040347 A signaling of Fc-gamma receptor on the surface of a signal-receiving cell, initiated by the binding of the Fc portion of immunoglobulin G (IgG) to Fc-gamma receptor with regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32887954 Fc-gamma receptor signaling in COVID-19 HOIP_0040347 PMID:32887954 Furthermore, patients with symptomatic COVID-19 are reported to produce IgG anti-bodies with reduced fucosylation levels, which in turn promotes their interaction with activating FcgammaRIIIa. Fc-mediated effector functions: immune functions that are mediated through the interaction of the constant Fc region of antibodies with innate immune molecules, complement proteins and specialized Fc receptors expressed by innate immune cells. The resulting functions include complement-dependent cytotoxicity and antibody-dependent cellular phagocytosis or cell-mediated cytotoxicity. HOIP:HOIP_0040348 The appearance of IgG antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. IgG antibody production HOIP_0040348 HOIP:HOIP_0040352 Cell killing caused by the membrane attack complex formed following complement activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. There are three pathways of complement activation: the classical pathway, which is triggered by antibody or by direct binding of complement component C1q to the pathogen surface; the MB-lectin pathway, which is triggered by mannan-binding lectin, a normal serum constituent that binds some encapsulated bacteria; and the alternative pathway, which is triggered directly on pathogen surfaces. All of these pathways generate a crucial enzymatic activity that, in turn, generates the effector molecules of complement. The three main consequences of complement activation are opsonization of pathogens, the recruitment of inflammatory cells, and direct killing of pathogens. Janeway's Immunobiology PMID:32887954 PMID:33077917 complement-dependent cytotoxicity in COVID-19 HOIP_0040352 PMID:32887954 Furthermore, patients with symptomatic COVID-19 are reported to produce IgG anti-bodies with reduced fucosylation levels, which in turn promotes their interaction with activating FcgammaRIIIa. Fc-mediated effector functions: immune functions that are mediated through the interaction of the constant Fc region of antibodies with innate immune molecules, complement proteins and specialized Fc receptors expressed by innate immune cells. The resulting functions include complement-dependent cytotoxicity and antibody-dependent cellular phagocytosis or cell-mediated cytotoxicity. PMID:33077917 C3b also forms C5 convertase, which induces release of the potent anaphylatoxin C5a, as well as the fragment C5b that is responsible for the formation of the membrane attack complex C5b–9 on target cells — the terminal event of complement activation. HOIP:HOIP_0040353 The appearance of G-CSF (granulocyte colony-stimulating factor) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 granulocyte colony-stimulating factor production G-CSF production in COVID-19 HOIP_0040353 PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040354 The directed killing of a target cell by an inflammatory cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32887954 inflammtory cell mediated cytotoxicity in COVID-19 HOIP_0040354 PMID:32887954 Furthermore, patients with symptomatic COVID-19 are reported to produce IgG anti-bodies with reduced fucosylation levels, which in turn promotes their interaction with activating FcgammaRIIIa. Fc-mediated effector functions: immune functions that are mediated through the interaction of the constant Fc region of antibodies with innate immune molecules, complement proteins and specialized Fc receptors expressed by innate immune cells. The resulting functions include complement-dependent cytotoxicity and antibody-dependent cellular phagocytosis or cell-mediated cytotoxicity. HOIP:HOIP_0040355 An Fc-gamma receptor signaling pathway that contributes to the endocytic engulfment of external particulate material by phagocytes. Fc-gamma receptor signaling pathway involved in phagocytosis HOIP_0040355 HOIP:HOIP_0040357 The inhibition of biological effects of S protein by induction of immunoglobulin. immunoglobulin-mediated neutralization of S protein HOIP_0040357 HOIP:HOIP_0040358 The inhibition of biological effects of S protein by induction of immunoglobulin G (IgG). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32663912 PMID:32702298 PMID:32702299 PMID:32756549 PMID:32887954 PMID:32967006 PMID:33053279 PMID:33123165 https://doi.org/10.1101/2020.07.17.20140533 immunoglobulin-mediated neutralization of S protein in COVID-19 vaccination HOIP_0040358 PMID:32663912 The mRNA-1273 vaccine was immunogenic, inducing robust binding antibody responses to both full-length S-2P and receptor-binding domain in all participants after the first vaccination in a time- and dose-dependent fashion. Commensurately high neutralizing antibody responses were also elicited in a dose-dependent fashion. PMID:32702298 We did a phase 1/2, single-blind, randomised controlled trial in five trial sites in the UK of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein compared with a meningococcal conjugate vaccine (MenACWY) as control. Anti-spike IgG responses rose by day 28 (median 157 ELISA units [EU], 96–317; n=127), and were boosted following a second dose (639 EU, 360–792; n=10). Neutralising antibody responses against SARS-CoV-2 were detected in 32 (91%) of 35 participants after a single dose when measured in MNA80 and in 35 (100%) participants when measured in PRNT50. In the ChAdOx1 nCoV-19 group, antibodies against SARS-CoV-2 spike protein peaked by day 28 (median 157 ELISA units [EU], IQR 96–317; n=127) and remained elevated to day 56 (119 EU, 70–203; n=43) in participants who received only one dose, and increased to a median of 639 EU (360–792) at day 56 in the ten participants who received a booster dose (figure 3). Similar increases in serum antibody levels to both the spike protein and the receptor binding domain by day 28 and after a booster dose were observed when measured by MIA (appendix p 16). PMID:32702299 Both vaccine doses induced significant neutralising antibody responses to live SARS-CoV-2, with GMTs of 19·5 (95% CI 16·8–22·7) and 18·3 (14·4–23·3) in participants in the 1 × 1011 and 5 × 1010 viral particles dose groups, respectively, at day 28 post vaccination (figure 2). PMID:32756549 Structural studies have led to the development of mutations that stabilize Betacoronavirus spike proteins in the prefusion state, improving their expression and increasing immunogenicity. This principle has been applied to design mRNA-1273, an mRNA vaccine that encodes a SARS-CoV-2 spike protein that is stabilized in the prefusion conformation. Here we have shown that 1 μg of mRNA-1273 is sufficient to induce robust pseudovirus-neutralizing activity and CD8 T cell responses, balanced TH1–TH2 antibody isotype responses, and protection from viral replication for more than three months following a prime–boost regimen similar to the one being tested in humans. PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. PMID:32967006 More informative, PRNT80 values with authentic SARS-CoV-2 reached 1:339.7 and 1:654.3 in the 25 micro g and 100 micro g groups (data for the 250 micro g group was not provided), which is within the range seen in convalescent samples from patients who have recovered from COVID-19. (mRNA-1273) PMID:33053279 Antigen-binding IgG and virus-neutralizing responses to vaccination with 10 μg to 30 μg of BNT162b1 or BNT162b2 were boosted by the second dose in both the younger adults and the older adults. PMID:33123165 A strong correlation was observed between nAb titers and anti-spike IgG to S protein with the adjuvanted, but not the unadjuvanted, vaccine. (NVX-CoV2373 vaccine) Neutralization titers were comparable to those observed in convalescent plasma from people who had recovered from COVID-19. (ChAdOx1 nCoV-19) https://doi.org/10.1101/2020.07.17.20140533 Two doses of 1 to 50 μg of nBNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those in a COVID-19 convalescent human serum panel (HCS). HOIP:HOIP_0040359 Any process involved in the carrying out of an immune response by a T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32663912 PMID:32702298 PMID:32702299 PMID:32756549 PMID:32887954 PMID:33123165 https://doi.org/10.1101/2020.07.17.20140533 T cell response T cell mediated immunity in COVID-19 vaccination HOIP_0040359 PMID:32663912 The 25-micro g and 100-micro g doses elicited CD4 T-cell responses (Figs. S9 and S10) that on stimulation by S-specific peptide pools were strongly biased toward expression of Th1 cytokines (tumor necrosis factor alpha > interleukin 2 > interferon gamma), with minimal type 2 helper T-cell (Th2) cytokine expression (interleukin 4 and interleukin 13). PMID:32702298 In the ChAdOx1 nCoV-19 group, spike-specific T-cell responses peaked on day 14 (median 856 spot-forming cells per million peripheral blood mononuclear cells, IQR 493–1802; n=43). Importantly, there are accumulating data to suggest T-cell responses play an important role in COVID-19 mitigation; individuals who were exposed but asymptomatic developed a robust memory T-cell response without symptomatic disease in the absence of a measurable humoral response. Adenovirus-vectored vaccines are known to induce strong cellular immunity and ChAdOx1 nCoV-19 vaccination resulted in marked increases in SARS-CoV-2 spike-specific effector T-cell responses as early as day 7, peaking at day 14 and maintained up to day 56 as expected with adenoviral vectors. PMID:32702299 Significant increases of post-vaccination T-cell responses in terms of spot-forming cells were observed both in participants with high and low pre-existing neutralising antibody at day 28. PMID:32756549 Here we have shown that 1 μg of mRNA-1273 is sufficient to induce robust pseudovirus-neutralizing activity and CD8 T cell responses, balanced TH1–TH2 antibody isotype responses, and protection from viral replication for more than three months following a prime–boost regimen similar to the one being tested in humans. PMID:32887954 In the ChAdOx1 nCoV-19 group, spike-specific T-cell responses peaked on day 14 (median 856 spot-forming cells per million peripheral blood mononuclear cells, IQR 493–1802; n=43). PMID:33123165 Both vaccine (Ad5-nCoV, ChAdOx1 nCoV-19) constructs elicited T cell responses which peaked at 14 days post-immunization, as determined by interferon- gamma (IFN-γ) enzyme linked immunospot (ELISpot) assay. T cell responses measured in 16 participants showed that NVX-CoV2373/Matrix-M1 induces antigen-specific polyfunctional CD4+ T cell responses (IFN-γ, IL-2, and TNF- α) in response to spike protein stimulation; there was a strong bias toward this Th1 phenotype. T cell responses measured by intracellular staining for Th1 (TNF, IL-2, IFN-γ) and Th2 (IL-4, IL-13) cytokines following stimulation with an S protein peptide pool showed a Th1 cytokine bias and low-level CD8 T cell responses. (mRNA-1273) https://doi.org/10.1101/2020.07.17.20140533 Here we present antibody and T cell responses after BNT162b1 vaccination from a second, non-randomized open-label phase 1/2 trial in healthy adults, 18-55 years of age. Two doses of 1 to 50 μg of nBNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those in a COVID-19 convalescent human serum panel (HCS). In summary, these findings indicate that BNT162b1 induces functional and proinflammatory CD4+/CD8+ T cell responses in almost all participants, with TH1 polarisation of the helper response. HOIP:HOIP_0040360 An inhibitor of S protein (Spike protein), a protein involved in virus entry. S protein inhibitor HOIP_0040360 HOIP:HOIP_0040361 The appearance of G-CSF (granulocyte colony-stimulating factor) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 granulocyte colony-stimulating factor production G-CSF production (very high) in severe COVID-19 HOIP_0040361 PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040362 An immune response mediated through a body fluid. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32702298 PMID:33053279 PMID:33270381 humoral immune response in COVID-19 vaccination HOIP_0040362 PMID:32702298 Immunisation with ChAdOx1 nCoV-19 results in rapid induction of both humoral and cellular immune responses against SARS-CoV-2, with increased responses after a second dose. PMID:33053279 This ability to elicit both humoral and cell-mediated antiviral mechanisms makes BNT162b1 a promising vaccine candidate. PMID:33270381 Although correlates of protection against SARS-CoV-2 infection in humans are not yet established, these results show that despite a slight expected decline in titers of binding and neutralizing antibodies, mRNA-1273 has the potential to provide durable humoral immunity. HOIP:HOIP_0040363 An immune response mediated through cells. cellular immune response HOIP_0040363 HOIP:HOIP_0040364 An immune response mediated through cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32702298 PMID:32967006 PMID:33053279 cellular immune response in COVID-19 vaccination HOIP_0040364 PMID:32702298 Immunisation with ChAdOx1 nCoV-19 results in rapid induction of both humoral and cellular immune responses against SARS-CoV-2, with increased responses after a second dose. PMID:32967006 Cellular immunity peaked at day 14, with 856 SFU per 106 cells, and decreased to 424 SFU by day 56. (ChAdOx1 nCoV-19) PMID:33053279 This ability to elicit both humoral and cell-mediated antiviral mechanisms makes BNT162b1 a promising vaccine candidate. HOIP:HOIP_0040365 homeostasis between T-helper 1 (Th1) and T-helper 2 (Th2) activity. Th1 cells drive the type-1 pathway ("cellular immunity") to fight viruses and other intracellular pathogens, eliminate cancerous cells, and stimulate delayed-type hypersensitivity (DTH) skin reactions. Th2 cells drive the type-2 pathway ("humoral immunity") and up-regulate antibody production to fight extracellular organisms. (PMID: 12946237) balanced Th1/Th2 immune response HOIP_0040365 HOIP:HOIP_0040367 The appearance of immunoglobulin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32663912 PMID:32702298 PMID:32702299 PMID:32756549 PMID:32887954 PMID:32967006 PMID:32998157 PMID:33053279 PMID:33123165 PMID:33270381 https://doi.org/10.1038/s41586-020-2639-4 https://doi.org/10.1101/2020.07.17.20140533 antibody production immunoglobulin production in COVID-19 vaccination HOIP_0040367 PMID:32663912 Binding antibody IgG geometric mean titers (GMTs) to S-2P increased rapidly after the first vaccination, with seroconversion in all participants by day 15 (Table 2 and Fig. 2A). PMID:32702298 Anti-spike IgG responses rose by day 28 (median 157 ELISA units [EU], 96–317; n=127), and were boosted following a second dose (639 EU, 360–792; n=10). Neutralising antibody responses against SARS-CoV-2 were detected in 32 (91%) of 35 participants after a single dose when measured in MNA80 and in 35 (100%) participants when measured in PRNT50. Immunisation with ChAdOx1 nCoV-19 results in rapid induction of both humoral and cellular immune responses against SARS-CoV-2, with increased responses after a second dose. In the ChAdOx1 nCoV-19 group, antibodies against SARS-CoV-2 spike protein peaked by day 28 (median 157 ELISA units [EU], IQR 96–317; n=127) and remained elevated to day 56 (119 EU, 70–203; n=43) in participants who received only one dose, and increased to a median of 639 EU (360–792) at day 56 in the ten participants who received a booster dose (figure 3). Similar increases in serum antibody levels to both the spike protein and the receptor binding domain by day 28 and after a booster dose were observed when measured by MIA (appendix p 16). PMID:32702299 Both vaccine doses induced significant neutralising antibody responses to live SARS-CoV-2, with GMTs of 19·5 (95% CI 16·8–22·7) and 18·3 (14·4–23·3) in participants in the 1 × 1011 and 5 × 1010 viral particles dose groups, respectively, at day 28 post vaccination (figure 2). PMID:32756549 Structural studies have led to the development of mutations that stabilize Betacoronavirus spike proteins in the prefusion state, improving their expression and increasing immunogenicity. This principle has been applied to design mRNA-1273, an mRNA vaccine that encodes a SARS-CoV-2 spike protein that is stabilized in the prefusion conformation. Here we have shown that 1 μg of mRNA-1273 is sufficient to induce robust pseudovirus-neutralizing activity and CD8 T cell responses, balanced TH1–TH2 antibody isotype responses, and protection from viral replication for more than three months following a prime–boost regimen similar to the one being tested in humans. PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. PMID:32967006 Whereas antibody titres between the two candidates were comparable, BNT162b2 showed a more favourable safety profile. (BNT162b1 and BNT162b2) PMID:32998157 Two doses of 1–50 micro g of BNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those seen in serum from a cohort of individuals who had recovered from COVID-19. The robust RBD-specific antibody, T cell and favourable cytokine responses induced by the BNT162b1 mRNA vaccine suggest that it has the potential to protect against COVID-19 through multiple beneficial mechanisms. PMID:33053279 Antigen-binding IgG and virus-neutralizing responses to vaccination with 10 μg to 30 μg of BNT162b1 or BNT162b2 were boosted by the second dose in both the younger adults and the older adults. Both vaccines elicited generally lower antigen-binding IgG and virus-neutralizing responses in participants 65 to 85 years of age than in those 18 to 55 years of age. PMID:33123165 The Wuhan vaccine has been shown to be safe and immunogenic in a randomized, double-blind, placebo- controlled phase 1/2 trial, which recently reported interim results. Reasonable geometric mean anti-SARS-CoV-2 nAb titers (206–316) in 50% plaque reduction neutralization assays were induced at 14 days post- immunization All participants developed RBD Abs by ELISA and SARS-CoV-2-specific nAbs by neutralization assay after 2 doses in the upper range of those who have recovered from COVID-19 (convalescent serum). (mRNA-1273) An interim report from the Phase 1/2 dose-ranging study of 2 doses of BioNTech’s mRNA S protein vaccine candidate BNT162 administered to adults aged 18–55 years elicited RBD- binding IgG and SARS-CoV-2 nAbs in the order of 1.8–2.8- fold that of convalescent human plasma. PMID:33270381 At the 100-micro g dose, mRNA-1273 produced high levels of binding and neutralizing antibodies that declined slightly over time, as expected, but they remained elevated in all participants 3 months after the booster vaccination. https://doi.org/10.1038/s41586-020-2639-4 RBD-binding IgG concentrations and SARS-CoV-2 neutralizing titres in sera increased with dose level and after a second dose. https://doi.org/10.1101/2020.07.17.20140533 Two doses of 1 to 50 μg of nBNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those in a COVID-19 convalescent human serum panel (HCS). HOIP:HOIP_0040372 The appearance of chemokine (C-C motif) ligand 3 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 CCL3 production MIP-1alpha production Macrophage Inframmatory Protein-1 alpha production chemokine (C-C motif) ligand 3 production in COVID-19 HOIP_0040372 PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040373 The appearance of chemokine (C-C motif) ligand 3 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 CCL3 production MIP-1alpha production Macrophage Inframmatory Protein-1 alpha production chemokine (C-C motif) ligand 3 production (very high) in severe COVID-19 HOIP_0040373 PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040375 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of COVID-19. PMID:33123165 inflammatory cell infiltration in COVID-19 HOIP_0040375 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0040379 The totality of all processes to homeostatic balance between functional supply by the immune system and functional demand by SARS-CoV2 due to vaccination. COVID-19 vaccination course HOIP_0040379 HOIP:HOIP_0040380 The directed movement of a natural killer cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 natural killer cell chemotaxis in COVID-19 HOIP_0040380 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0040381 The directed movement of a natural killer cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 natural killer cell chemotaxis (very high) in severe COVID-19 HOIP_0040381 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0040382 Any process that stops, prevents, or reduces the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 Negative regulation of immune response in severe COVID-19 HOIP_0040382 PMID:33123165 Severe disease is associated with profound lymphopaenia lending support to the theory that the disease also causes immunosuppression, although lymphocyte trafficking to the site of infection may also be responsible. HOIP:HOIP_0040383 The movement of a T cell within or between different tissues and organs of the body. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 T cell migration in COVID-19 HOIP_0040383 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0040384 The movement of a T cell within or between different tissues and organs of the body. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 T cell migration in severe COVID-19 HOIP_0040384 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0040386 Any process that stops, prevents, or reduces the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 Negative regulation of immune response in COVID-19 HOIP_0040386 PMID:33123165 Severe disease is associated with profound lymphopaenia lending support to the theory that the disease also causes immunosuppression, although lymphocyte trafficking to the site of infection may also be responsible. HOIP:HOIP_0040387 Decreasing number of T cell repertoires is a subtype of decreasing number of objects: A process that becomes smaller in number of T cell repertoires. decreasing number of T cell repertoires HOIP_0040387 HOIP:HOIP_0040388 Any process contributing to anergy in T cells, a state of functional inactivation which is part of T cell tolerance induction. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 T細胞免疫不応答 T cell anergy in severe COVID-19 HOIP_0040388 PMID:33123165 Severe COVID-19 patients exhibit immunological features associated with T cell anergy or exhaustion. HOIP:HOIP_0040389 T cell exhaustion is a dysfunction of T cells, which changes in transcriptional profiles and sustained expression of inhibitory receptors and leads to progressive loss of function. PMID:31822213 T cell exhaustion HOIP_0040389 PMID:31822213 In chronic infections or cancer, CD8+T cells are constantly exposed to antigens and inflammatory signals. Such excessive and constitutive signals lead to the deterioration of T cell function, called ‘exhaustion’. HOIP:HOIP_0040391 Decreasing number of T cell repertoires is a subtype of decreasing number of objects: A process that becomes smaller in number of T cell repertoires. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 decreasing number of T cell repertoires in severe COVID-19 HOIP_0040391 PMID:33123165 This model could account for poorer outcomes in the elderly who have diminished T cell repertoires and better outcomes in children who have a diverse and abundant naïve T cell pool. HOIP:HOIP_0040392 Negative regulation of host cell surface receptor binding is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of host cell surface receptor binding. This process can constitute the course of COVID-19 vaccination. PMID:32702298 PMID:32702299 PMID:32887954 Negative regulation of host cell surface receptor binding in COVID-19 vaccination HOIP_0040392 PMID:32702298 We did a phase 1/2, single-blind, randomised controlled trial in five trial sites in the UK of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein compared with a meningococcal conjugate vaccine (MenACWY) as control. Similar increases in serum antibody levels to both the spike protein and the receptor binding domain by day 28 and after a booster dose were observed when measured by MIA (appendix p 16). PMID:32702299 RBD-specific ELISA antibody responses induced by the Ad5-vectored COVID-19 vaccine were detected from day 14 onwards, with GMTs of 94·5 (95% CI 80·5–110·8) and 85·1 (66·0–109·7) in the 1×1011 and 5×1010 viral particles dose groups, respectively (figure 2). PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. HOIP:HOIP_0040393 Interacting selectively and non-covalently with a receptor on the host cell surface. This process can constitute the course of COVID-19 vaccination. PMID:32702298 PMID:32702299 PMID:32887954 host cell surface receptor binding(very low) in COVID-19 vaccination HOIP_0040393 PMID:32702298 We did a phase 1/2, single-blind, randomised controlled trial in five trial sites in the UK of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein compared with a meningococcal conjugate vaccine (MenACWY) as control. Similar increases in serum antibody levels to both the spike protein and the receptor binding domain by day 28 and after a booster dose were observed when measured by MIA (appendix p 16). PMID:32702299 RBD-specific ELISA antibody responses induced by the Ad5-vectored COVID-19 vaccine were detected from day 14 onwards, with GMTs of 94·5 (95% CI 80·5–110·8) and 85·1 (66·0–109·7) in the 1×1011 and 5×1010 viral particles dose groups, respectively (figure 2). PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. HOIP:HOIP_0040394 Negative regulation of viral spike S protein structure change is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral spike S protein structure change. This process can constitute the course of COVID-19 vaccination. PMID:32756549 PMID:32887954 Negative regulation of viral spike S protein structure change in COVID-19 vaccination HOIP_0040394 PMID:32756549 Structural studies have led to the development of mutations that stabilize Betacoronavirus spike proteins in the prefusion state, improving their expression and increasing immunogenicity. This principle has been applied to design mRNA-1273, an mRNA vaccine that encodes a SARS-CoV-2 spike protein that is stabilized in the prefusion conformation. Here we have shown that 1 μg of mRNA-1273 is sufficient to induce robust pseudovirus-neutralizing activity and CD8 T cell responses, balanced TH1–TH2 antibody isotype responses, and protection from viral replication for more than three months following a prime–boost regimen similar to the one being tested in humans. PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. HOIP:HOIP_0040395 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of positive stranded viral RNA replication. This process can constitute the course of COVID-19 vaccination. PMID:32756549 Negative regulation of positive stranded viral RNA replication in COVID-19 vaccination HOIP_0040395 PMID:32756549 Here we have shown that 1 μg of mRNA-1273 is sufficient to induce robust pseudovirus-neutralizing activity and CD8 T cell responses, balanced TH1–TH2 antibody isotype responses, and protection from viral replication for more than three months following a prime–boost regimen similar to the one being tested in humans. HOIP:HOIP_0040396 A viral genome replication process where the template genome is positive stranded, single stranded RNA ((+)ssRNA). Replication of the positive strand leads to dsRNA formation, which in turn is transcribed into positive single stranded RNA. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. PMID:32756549 positive stranded viral RNA replicationvery (very low) in COVID-19 vaccination HOIP_0040396 PMID:32756549 Here we have shown that 1 μg of mRNA-1273 is sufficient to induce robust pseudovirus-neutralizing activity and CD8 T cell responses, balanced TH1–TH2 antibody isotype responses, and protection from viral replication for more than three months following a prime–boost regimen similar to the one being tested in humans. HOIP:HOIP_0040397 Negative regulation of virus membrane fusion with host plasma membrane is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of virus membrane fusion with host plasma membrane. This process can constitute the course of COVID-19 vaccination. PMID:32887954 negative regulation of virus membrane fusion with host plasma membrane in COVID-19 vaccination HOIP_0040397 PMID:32887954 The major target of neutralizing antibodies to coronaviruses is the S protein, which is composed of S1 and S2 domains. S1 is membrane distal and contains the RBD that binds to the cellular receptor ACE2. S2 is membrane proximal and has a role in membrane fusion. Antibodies that bind to the S1 RBD block its interaction with ACE2, whereas those that bind to other regions of S1 and S2 can inhibit conformational change of the S protein and block membrane fusion, respectively. HOIP:HOIP_0040398 The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This process can constitute the course of COVID-19 vaccination. PMID:32697943 PMID:32702298 PMID:32702299 PMID:32998157 PMID:33053279 PMID:33123165 https://doi.org/10.1101/2020.07.17.20140533 interferon-gamma production in COVID-19 vaccination HOIP_0040398 PMID:32697943 Similarly, CM-CoV-2 decreased IFN-g production by CD4 T cells, and this was reversed in CM-BAY87 and CM-MitoQ and appeared to be reversed in CM-aIL-1b (Figures 4B and S4J). PMID:32702298 We did a phase 1/2, single-blind, randomised controlled trial in five trial sites in the UK of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein compared with a meningococcal conjugate vaccine (MenACWY) as control. Interferon-gamma ELISpot responses against SARS-CoV-2 spike peptides peaked at 856 spot-forming cells per million peripheral blood mononuclear cells (IQR 493–1802; n=43) at day 14, declining to 424 (221–799; n=43) by day 56 after vaccination (figure 6). PMID:32702299 Ad5-vectored COVID-19 vaccine induced significant SARS-CoV-2 spike glycoprotein-specific IFNgamma-ELISpot responses in 227 (90%, 95% CI 85–93) of 253 participants receiving the 1×1011 viral particles dose, and 113 (88%, 81–92) of 129 partici- pants receiving the 5 × 1010 viral particles dose at day 28 (figure 3). PMID:32998157 Interferon-gamma was produced by a large fraction of RBD-specific CD8+ and CD4+ T cells. The robust RBD-specific antibody, T cell and favourable cytokine responses induced by the BNT162b1 mRNA vaccine suggest that it has the potential to protect against COVID-19 through multiple beneficial mechanisms. RBD-specific CD4+ T cells secreted IFNgamma, IL-2, or both, but in most individuals they did not secrete IL-4 (Fig. 4 a–c, Extended Data Table 6). Similarly, fractions of RBD-specific CD8+ T cells secreted IFNgamma+ and IL-2. PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. PMID:33123165 Intracellular staining confirmed production of IFN-γ, tumor necrosis factor (TNF) and interleukin-2 (IL-2) by both CD4+ and CD8+ T cells following Ad5-nCoV immunization, with more cytokine detected in CD4+ T cells as compared to CD8+ T cells. T cell responses measured in 16 participants showed that NVX-CoV2373/Matrix-M1 induces antigen-specific polyfunctional CD4+ T cell responses (IFN-γ, IL-2, and TNF- α) in response to spike protein stimulation; there was a strong bias toward this Th1 phenotype. Both vaccine (Ad5-nCoV, ChAdOx1 nCoV-19) constructs elicited T cell responses which peaked at 14 days post-immunization, as determined by interferon- gamma (IFN-γ) enzyme linked immunospot (ELISpot) assay. T cell responses measured by intracellular staining for Th1 (TNF, IL-2, IFN-γ) and Th2 (IL-4, IL-13) cytokines following stimulation with an S protein peptide pool showed a Th1 cytokine bias and low-level CD8 T cell responses. (mRNA-1273) https://doi.org/10.1101/2020.07.17.20140533 Interferon (IFN)gamma was produced by a high fraction of RBD-specific CD8+ and CD4+ T cells. RBD-specific CD4+ T cells secreted IFNgamma, IL-2, or both, but did not secrete IL-4 (Figure 4a-c). Similarly, fractions of RBD-specific CD8+ T cells secreted IFNgamma and IL-2. IFNgamma is a key cytokine for several antiviral responses. It acts in synergy with type I interferons to inhibit replication of SARS-CoV-2. HOIP:HOIP_0040399 Fusion of a viral membrane with the host cell membrane during viral entry. Results in release of the virion contents into the cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. fusion of virus membrane with host plasma membrane (very low) in COVID-19 vaccination HOIP_0040399 HOIP:HOIP_0040400 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. viral entry into host cell (very low) in COVID-19 vaccination HOIP_0040400 HOIP:HOIP_0040401 The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32702298 PMID:32702299 interferon-gamma production in COVID-19 (homeostatic balance) HOIP_0040401 PMID:32702298 We did a phase 1/2, single-blind, randomised controlled trial in five trial sites in the UK of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein compared with a meningococcal conjugate vaccine (MenACWY) as control. Interferon-gamma ELISpot responses against SARS-CoV-2 spike peptides peaked at 856 spot-forming cells per million peripheral blood mononuclear cells (IQR 493–1802; n=43) at day 14, declining to 424 (221–799; n=43) by day 56 after vaccination (figure 6). PMID:32702299 Ad5-vectored COVID-19 vaccine induced significant SARS-CoV-2 spike glycoprotein-specific IFNgamma-ELISpot responses in 227 (90%, 95% CI 85–93) of 253 participants receiving the 1×1011 viral particles dose, and 113 (88%, 81–92) of 129 partici- pants receiving the 5 × 1010 viral particles dose at day 28 (figure 3). HOIP:HOIP_0040402 The inhibition of an antigen's biological effects by antibody binding to it. An example is neutralization of diphtheria toxin by preventing its entry into human cells via the binding of antibody specific for diphtheria toxin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). immunoglobulin-mediated neutralization in COVID-19 (homeostatic balance) HOIP_0040402 HOIP:HOIP_0040403 The appearance of immunoglobulin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 antibody production immunoglobulin production in COVID-19 (homeostatic balance) HOIP_0040403 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). Antibodies (Abs) produced by activated B cells play a key role in anti-viral immunity via several mechanisms including viral neutralization, antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP), and antibody-dependent complement activation (ADCA) (Figure3). HOIP:HOIP_0040405 Any process that contributes to cytokine production by a T-helper 1 cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). T-helper 1 cell cytokine production in COVID-19 (homeostatic balance) HOIP_0040405 HOIP:HOIP_0040406 The appearance of interleukin-2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). interleukin-2 production in COVID-19 (homeostatic balance) HOIP_0040406 HOIP:HOIP_0040407 The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). tumor necrosis factor production in COVID-19 (homeostatic balance) HOIP_0040407 HOIP:HOIP_0040408 Any process involved in the carrying out of an immune response by a T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 T cell response T cell mediated immunity in COVID-19 (homeostatic balance) HOIP_0040408 PMID:33123165 Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0040409 An immune response mediated through a body fluid. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). humoral immune response in COVID-19 (homeostatic balance) HOIP_0040409 HOIP:HOIP_0040410 An immune response mediated through cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). cellular immune response in COVID-19 (homeostatic balance) HOIP_0040410 HOIP:HOIP_0040414 The change in morphology and behavior of a mature or immature B cell during an immune response, resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). B cell activation involved in immune response in COVID-19 (homeostatic balance) HOIP_0040414 HOIP:HOIP_0040416 The switching of activated B cells from IgM biosynthesis to biosynthesis of an IgG isotype, accomplished through a recombination process involving an intrachromosomal deletion between switch regions that reside 5' of the IgM and one of the IgG constant region gene segments in the immunoglobulin heavy chain locus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 isotype switching to IgG isotypes in COVID-19 (homeostatic balance) HOIP_0040416 PMID:33123165 Importantly, class-switched IgG memory B cells to S and RBD have been demonstrated in COVID-19 patients confirming the generation of B cell memory which can provide a rapid recall response on subsequent SARS-CoV- 2 exposure. HOIP:HOIP_0040417 The process in which a relatively unspecialized T cell acquires specialized features of a mature T follicular helper cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 T follicular helper cell differentiation in COVID-19 (homeostatic balance) HOIP_0040417 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0040418 The process in which a B cell acquires the specialized features of a memory B cell. Memory B cells are cells that can respond rapidly to antigen re-exposure by production of high-affinity antibody. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 memory B cell differentiation in COVID-19 (homeostatic balance) HOIP_0040418 PMID:33123165 Importantly, class-switched IgG memory B cells to S and RBD have been demonstrated in COVID-19 patients confirming the generation of B cell memory which can provide a rapid recall response on subsequent SARS-CoV- 2 exposure. HOIP:HOIP_0040419 Antigen processing and presentation which is initiated by phagocytosis of antigen bound directly or indirectly to a cell surface toll-like receptor (TLR). This process can constitute the course of COVID-19 (homeostatic balance). Processing and presentation of SARS-CoV-2 epitopes by antigen presenting cells (APCs) via human leukocyte antigen (HLA) class I leads to activation of naïve CD8+ T cells which differentiate into cytolytic effectors (cytotoxic T lymphocytes [CTL]) that kill virus-infected cells. antigen processing and presentation initiated by toll-like receptor mediated phagocytosis of antigen in COVID-19 (homeostatic balance) HOIP_0040419 HOIP:HOIP_0040422 The change in morphology and behavior of a CD8-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 CD8-positive, alpha-beta T cell activation in COVID-19 (homeostatic balance) HOIP_0040422 PMID:33123165 Processing and presentation of SARS-CoV-2 epitopes by antigen presenting cells (APCs) via human leukocyte antigen (HLA) class I leads to activation of naïve CD8+ T cells which differentiate into cytolytic effectors (cytotoxic T lymphocytes [CTL]) that kill virus-infected cells. Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus- specific antibody production (Figure 3). HOIP:HOIP_0040424 The process in which a relatively unspecialized T cell acquires specialized features of a cytotoxic T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33053279 PMID:33123165 cytotoxic T cell differentiation in COVID-19 (homeostatic balance) HOIP_0040424 PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. PMID:33123165 Processing and presentation of SARS-CoV-2 epitopes by antigen presenting cells (APCs) via human leukocyte antigen (HLA) class I leads to activation of naïve CD8+ T cells which differentiate into cytolytic effectors (cytotoxic T lymphocytes [CTL]) that kill virus-infected cells. Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0040426 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a cytotoxic T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 cytotoxic T cell degranulation in COVID-19 (homeostatic balance) HOIP_0040426 PMID:33123165 Processing and presentation of SARS-CoV-2 epitopes by antigen presenting cells (APCs) via human leukocyte antigen (HLA) class I leads to activation of naïve CD8+ T cells which differentiate into cytolytic effectors (cytotoxic T lymphocytes [CTL]) that kill virus-infected cells. HOIP:HOIP_0040427 The change in morphology and behavior of a CD4-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 CD4-positive, alpha-beta T cell activation in COVID-19 (homeostatic balance) HOIP_0040427 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0040428 an mRNA–lipid nanoparticle vaccine encoding a membrane-anchored SARS-CoV-2 full-length spike, stabilized in the prefusion conformation. PMID:32967006 PMID:33053279 BNT162b2 vaccine HOIP_0040428 PMID:32967006 In an additional study, Pfizer recently reported a direct comparison between BNT162b1 and BNT162b2 (NCT04368728). Whereas antibody titres between the two candidates were comparable, BNT162b2 showed a more favourable safety profile. BNT126b2 was selected to move forward and is now in a phase III trial in healthy adults and older age groups (NCT04368728). PMID:33053279 Inanongoing, placebo-controlled, observer-blinded, dose-escalation, phase1 trial conducted in the United States, we randomly assigned healthy adults 18 to 55 years of age and those 65 to 85 years of age to receive either placebo or one of two lipid nanoparticle–formulated, nucleoside-modified RNA vaccine candidates: BNT162b1, which encodes a secreted trimerized SARS-CoV-2 receptor–binding domain; or BNT162b2, which encodes a membrane-anchored SARS-CoV-2 full- length spike, stabilized in the prefusion conformation. BNT162b2 was associated with a lower incidence and severity of systemic reactions than BNT162b1, particularly in older adults. In both younger and older adults, the two vaccine candidates elicited similar dose-dependent SARS-CoV-2–neutralizing geometric mean titers, which were similar to or higher than the geometric mean titer of a panel of SARS-CoV-2 convalescent serum samples. The safety and immunogenicity data from this U.S. phase 1 trial of two vaccine candidates in younger and older adults, added to earlier interim safety and im- munogenicity data regarding BNT162b1 in younger adults from trials in Germany and the United States, support the selection of BNT162b2 for advancement to a pivotal phase 2–3 safety and efficacy evaluation. (Funded by BioNTech and Pfizer; ClinicalTrials.gov number, NCT04368728.) HOIP:HOIP_0040429 The change in morphology and behavior of a T helper 2 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 T-helper 2 cell activation in COVID-19 (homeostatic balance) HOIP_0040429 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0040430 The change in morphology and behavior of a T-helper 1 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 T-helper 1 cell activation in COVID-19 (homeostatic balance) HOIP_0040430 PMID:33123165 Activation of T helper 1 (Th1) CD4+ T cells via viral peptides presented on HLA class II alleles further enhances the CD8+ T cell response, while HLA class II-restricted follicular helper (TFH) and Th2 cells enhance virus-specific antibody production (Figure 3). HOIP:HOIP_0040431 Any biological process that results in permanent cessation of all vital functions of a cell. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 cell death in COVID-19 (homeostatic balance) HOIP_0040431 PMID:33123165 Processing and presentation of SARS-CoV-2 epitopes by antigen presenting cells (APCs) via human leukocyte antigen (HLA) class I leads to activation of naïve CD8+ T cells which differentiate into cytolytic effectors (cytotoxic T lymphocytes [CTL]) that kill virus-infected cells. HOIP:HOIP_0040433 Any process involved with the carrying out of an immune response by a B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33123165 B cell mediated immunity in COVID-19 (homeostatic balance) HOIP_0040433 PMID:33123165 Effective viral clearance therefore requires a combination of CD8+ CTL and CD4+ T cell mediated enhancement of B cell and CD8+ T cell responses. HOIP:HOIP_0040436 The change in morphology and behavior of a T-helper 1 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32998157 PMID:33123165 T-helper 1 cell activation in COVID-19 vaccination HOIP_0040436 PMID:32998157 Most participants had T helper type 1 (TH1)-skewed T cell immune responses with RBD-specific CD8+ and CD4+ T cell expansion. The robust RBD-specific antibody, T cell and favourable cytokine responses induced by the BNT162b1 mRNA vaccine suggest that it has the potential to protect against COVID-19 through multiple beneficial mechanisms. In summary, these findings indicate that BNT162b1 induces functional and proinflammatory CD4+ and CD8+ T cell responses in almost all participants, with TH1 polarization of the helper response. PMID:33123165 This (EPV-Cov19) uses synthetic peptides chemically linked to the 4-amino acid Ii-Key to ensure robust immune activation of Th1 and Th2 CD4+ T cells in particular, which in turn facilitate antibody production. T cell responses measured in 16 participants showed that NVX-CoV2373/Matrix-M1 induces antigen-specific polyfunctional CD4+ T cell responses (IFN-γ, IL-2, and TNF- α) in response to spike protein stimulation; there was a strong bias toward this Th1 phenotype. T cell responses measured by intracellular staining for Th1 (TNF, IL-2, IFN-γ) and Th2 (IL-4, IL-13) cytokines following stimulation with an S protein peptide pool showed a Th1 cytokine bias and low-level CD8 T cell responses. (mRNA-1273) HOIP:HOIP_0040437 The change in morphology and behavior of a T helper 2 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. T-helper 2 cell activation in COVID-19 vaccination HOIP_0040437 HOIP:HOIP_0040439 Decreasing number of virus is a subtype of decreasing number of objects: A process that becomes smaller in number of viruses. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. decreasing number of virus in COVID-19 drug treatment HOIP_0040439 HOIP:HOIP_0040440 An immune response which is associated with resistance to intracellular bacteria, fungi, and protozoa, and pathological conditions such as arthritis, and which is typically orchestrated by the production of particular cytokines by T-helper 1 cells, most notably interferon-gamma, IL-2, and lymphotoxin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32967006 PMID:33053279 PMID:33270381 T-helper 1 type immune response in COVID-19 vaccination HOIP_0040440 PMID:32967006 CD4+ responses were evaluated 7 days post-boost, and both adjuvanted groups showed a robust, TH1-polarized response. (NVX-CoV2373) PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. PMID:33270381 Although the memory cellular response to mRNA-1273 is not yet defined, this vaccine elicited primary CD4 type 1 helper T responses 43 days after the first vaccination, and studies of vaccine-induced B cells are ongoing. HOIP:HOIP_0040441 An immune response which is associated with resistance to intracellular bacteria, fungi, and protozoa, and pathological conditions such as arthritis, and which is typically orchestrated by the production of particular cytokines by T-helper 1 cells, most notably interferon-gamma, IL-2, and lymphotoxin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). T-helper 1 type immune response in COVID-19 (homeostatic balance) HOIP_0040441 HOIP:HOIP_0040443 The process in which a relatively unspecialized T cell acquires specialized features of a cytotoxic T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:33053279 cytotoxic T cell differentiation in COVID-19 vaccination HOIP_0040443 PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. HOIP:HOIP_0040444 Any process that activates or increases the frequency, rate or extent of the inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32307653 PMID:32629875 positive regulation of inflammatory response in COVID-19 HOIP_0040444 PMID:32307653 Some regions of reactive epithelial hyperplasia had also abundant alveolar macrophages. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32629875 Also, as a consequence of SARS-CoV-2 receptor binding and entry into any cells, cell surface ACE2 is reduced in association with increased angiotensin II, which confers a pro-inflammatory, pro-coagulant and pro-apoptotic phenotype to endothelial cells. HOIP:HOIP_0040445 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a cytotoxic T cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:33053279 cytotoxic T cell degranulation in COVID-19 vaccination HOIP_0040445 PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. HOIP:HOIP_0040446 Decreaing stem cell is a subtype of decreasing number of cells: A process that becomes smaller in number of stem cell. decreasing stem cell HOIP_0040446 HOIP:HOIP_0040447 Decreaing stem cell is a subtype of decreasing number of cells: A process that becomes smaller in number of stem cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 decreasing stem cell in COVID-19 associated with ARDS HOIP_0040447 PMID:32307653 Moreover, resident lung progenitor/stem are extensively differentiated into myofibroblasts during pulmonary fibrosis, a complication observed in COVID-19 patients. This process, and the possible direct viral invasion of progenitor/stem cells via CD147 or ACE2, could result in the decline of these cellular stocks and failing lung repair. In addition to direct viral invasion and loss of lung stem cells, stocks of these cells also can be affected during SARS- CoV-2 infection by extensive differentiation into myofibroblasts. Since both early-phase and severe COVID-19 stages show strong involvement of inflammatory components and possibly loss of resident stem cell stocks, a considerable amount of research activities are engaged in investigating the role of cellular therapy using immune response-suppressing MSCs for COVID-19 therapy. HOIP:HOIP_0040448 Any process that stops, prevents, or reduces the frequency, rate or extent of tissue regeneration. negative regulation of tissue regeneration HOIP_0040448 HOIP:HOIP_0040449 Any process that stops, prevents, or reduces the frequency, rate or extent of tissue regeneration. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 negative regulation of tissue regeneration in COVID-19 associated with ARDS HOIP_0040449 PMID:32307653 Moreover, resident lung progenitor/stem are extensively differentiated into myofibroblasts during pulmonary fibrosis, a complication observed in COVID-19 patients. This process, and the possible direct viral invasion of progenitor/stem cells via CD147 or ACE2, could result in the decline of these cellular stocks and failing lung repair. HOIP:HOIP_0040450 The change in morphology and behavior of a CD4-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32998157 CD4-positive, alpha-beta T cell activation in COVID-19 vaccination HOIP_0040450 PMID:32998157 Two doses of 1–50 micro g of BNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those seen in serum from a cohort of individuals who had recovered from COVID-19. Although the magnitude of the response varied between individuals, participants with the strongest CD4+ T cell responses to RBD had more than tenfold the memory responses observed in the same participants when stimulated with cytomegalovirus (CMV), Epstein Barr virus (EBV), influenza virus and tetanus toxoid-derived immuno-dominant peptide panels (Fig. 3a–c). In summary, these findings indicate that BNT162b1 induces functional and proinflammatory CD4+ and CD8+ T cell responses in almost all participants, with TH1 polarization of the helper response. HOIP:HOIP_0040451 The change in morphology and behavior of a CD8-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32998157 CD8-positive, alpha-beta T cell activation in COVID-19 vaccination HOIP_0040451 PMID:32998157 Two doses of 1–50 micro g of BNT162b1 elicited robust CD4+ and CD8+ T cell responses and strong antibody responses, with RBD-binding IgG concentrations clearly above those seen in serum from a cohort of individuals who had recovered from COVID-19. Among participants who showed any vaccine-induced CD8+ T cell response (32/42 participants receiving the prime-boost dosing, 76.2%), the majority mounted strong responses (Fig. 3a) that were comparable with memory responses against CMV, EBV and influenza virus in the same participants (Fig. 3b, c). In summary, these findings indicate that BNT162b1 induces functional and proinflammatory CD4+ and CD8+ T cell responses in almost all participants, with TH1 polarization of the helper response. HOIP:HOIP_0040452 Any biological process that results in permanent cessation of all vital functions of an infected cell. This process can constitute the course of COVID-19 vaccination. PMID:33053279 infected cell death in COVID-19 vaccination HOIP_0040452 PMID:33053279 BNT162b1 also elicited CD4+ type 1 helper T (Th1) cell responses and strong interferon-gamma–producing and interleukin-2–producing CD8+ cytotoxic T-cell responses. HOIP:HOIP_0040454 The expansion of a CD8-positive, alpha-beta T cell population by cell division. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). CD8-positive, alpha-beta T cell proliferation in COVID-19 (homeostatic balance) HOIP_0040454 HOIP:HOIP_0040455 The expansion of a CD8-positive, alpha-beta T cell population by cell division. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32998157 CD8-positive, alpha-beta T cell proliferation in COVID-19 vaccination HOIP_0040455 PMID:32998157 Most participants had T helper type 1 (TH1)-skewed T cell immune responses with RBD-specific CD8+ and CD4+ T cell expansion. The robust RBD-specific antibody, T cell and favourable cytokine responses induced by the BNT162b1 mRNA vaccine suggest that it has the potential to protect against COVID-19 through multiple beneficial mechanisms. HOIP:HOIP_0040456 The expansion of a CD4-positive, alpha-beta T cell population by cell division. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). CD4-positive, alpha-beta T cell proliferation in COVID-19 (homeostatic balance) HOIP_0040456 HOIP:HOIP_0040457 The expansion of a CD4-positive, alpha-beta T cell population by cell division. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32998157 CD4-positive, alpha-beta T cell proliferation in COVID-19 vaccination HOIP_0040457 PMID:32998157 Most participants had T helper type 1 (TH1)-skewed T cell immune responses with RBD-specific CD8+ and CD4+ T cell expansion. The robust RBD-specific antibody, T cell and favourable cytokine responses induced by the BNT162b1 mRNA vaccine suggest that it has the potential to protect against COVID-19 through multiple beneficial mechanisms. HOIP:HOIP_0040458 Any process involved with the carrying out of an immune response by a memory B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. memory B cell mediated immunity HOIP_0040458 HOIP:HOIP_0040459 Any process involved with the carrying out of an immune response by a memory B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:33270381 memory B cell mediated immunity in COVID-19 (homeostatic balance) HOIP_0040459 PMID:33270381 Natural infection produces variable antibody longevity and may induce robust memory B-cell responses despite low plasma neutralizing activity. HOIP:HOIP_0040460 An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). This process can constitute the course of COVID-19 vaccination. PMID:32998157 adaptive immune response in COVID-19 vaccination HOIP_0040460 PMID:32998157 Although the magnitude of the response varied between individuals, participants with the strongest CD4+ T cell responses to RBD had more than tenfold the memory responses observed in the same participants when stimulated with cytomegalovirus (CMV), Epstein Barr virus (EBV), influenza virus and tetanus toxoid-derived immuno-dominant peptide panels (Fig. 3a–c). Among participants who showed any vaccine-induced CD8+ T cell response (32/42 participants receiving the prime-boost dosing, 76.2%), the majority mounted strong responses (Fig. 3a) that were comparable with memory responses against CMV, EBV and influenza virus in the same participants (Fig. 3b, c). HOIP:HOIP_0040462 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of COVID-19 (homeostatic balance). IL-1beta production in COVID-19 (homeostatic balance) HOIP_0040462 HOIP:HOIP_0040463 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of COVID-19 vaccination. PMID:32998157 IL-1beta production in COVID-19 vaccination HOIP_0040463 PMID:32998157 The supernatants of PBMCs from five vaccinated participants were stimulated ex vivo with overlapping RBD peptides and produced the proinflammatory cytokines TNF, IL-1beta and IL-12p70, but neither IL-4 nor IL-5 (Fig. 4d). HOIP:HOIP_0040464 The appearance of interleukin-12p70 (a heterodimer composed of p40 and p35 subunits) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interleukin-12p70 production HOIP_0040464 HOIP:HOIP_0040465 The appearance of interleukin-12p70 (a heterodimer composed of p40 and p35 subunits) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of COVID-19 (homeostatic balance). interleukin-12p70 production in COVID-19 (homeostatic balance) HOIP_0040465 HOIP:HOIP_0040466 The appearance of interleukin-12p70 (a heterodimer composed of p40 and p35 subunits) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of COVID-19 vaccination. PMID:32998157 https://doi.org/10.1101/2020.07.17.20140533 interleukin-12p70 production in COVID-19 vaccination HOIP_0040466 PMID:32998157 The supernatants of PBMCs from five vaccinated participants were stimulated ex vivo with overlapping RBD peptides and produced the proinflammatory cytokines TNF, IL-1beta and IL-12p70, but neither IL-4 nor IL-5 (Fig. 4d). https://doi.org/10.1101/2020.07.17.20140533 The detection of IFNgamma, IL-2 and IL-12p70 but not IL-4 indicates a favorable TH1 profile and the absence of a potentially deleterious TH2 immune response. HOIP:HOIP_0040467 The synthesis and release of immunoglobulin in the mucosal tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32967006 immunoglobulin production in mucosal tissue in COVID-19 (homeostatic balance) HOIP_0040467 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). HOIP:HOIP_0040468 The appearance of IgA antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. IgA antibody production HOIP_0040468 HOIP:HOIP_0040469 The appearance of IgA antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32967006 IgA antibody production in COVID-19 (homeostatic balance) HOIP_0040469 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. HOIP:HOIP_0040470 The appearance of IgG antibody due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32967006 IgG antibody production in COVID-19 (homeostatic balance) HOIP_0040470 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. HOIP:HOIP_0040471 Decreasing oxygen concentration in blood is a subtype of decreasing concentration: A process that changes the concentration of the oxygen in the blood to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32412710 decreasing oxygen concentration in blood in COVID-19 associated with ARDS HOIP_0040471 PMID:32412710 Dyspnea is the most common symptom of severe disease and is often accompanied by hypoxemia (Fig. 1). Progressive respiratory failure develops in many patients with severe Covid-19 soon after the onset of dyspnea and hypoxemia. These patients commonly meet the criteria for the acute respiratory distress syndrome (ARDS), which is defined as the acute onset of bilateral infiltrates, severe hypoxemia, and lung edema that is not fully explained by cardiac failure or fluid overload. HOIP:HOIP_0040472 An immune response mediated by immunoglobulins, whether cell-bound or in solution. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 (homeostatic balance). PMID:32967006 immunoglobulin mediated immune response in COVID-19 (homeostatic balance) HOIP_0040472 PMID:32967006 Neutralizing antibodies have now also been implicated as a correlate of protection in humans after studies of an outbreak on a fishing vessel; however, it is important to note that natural infection induces both mucosal antibody responses (secretory immunoglobulin A (IgA)) and systemic antibody responses (IgG). The upper respiratory tract is thought to be mainly protected by secretory IgA, whereas the lower respiratory tract is thought to be mainly protected by IgG. HOIP:HOIP_0040474 thrombus formation is a subtype of biological structure formation: A process that construcs thrombus. thrombus formation HOIP_0040474 HOIP:HOIP_0040477 Liver malfunction is a subtype of organ malfunction: A process that does not perform liver function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32412710 liver malfunction in COVID-19 in liver HOIP_0040477 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. HOIP:HOIP_0040478 kidney malfunction is a subtype of organ malfunction: A process that does not perform kidney function correctly or not functioning at all. renal malfunction kidney injury renal failure kidney malfunction HOIP_0040478 HOIP:HOIP_0040482 Dysregulation of heartbeats is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of heartbeats appropriately or cannot realize it at all. cardiac arrhythmias dysregulation of heartbeats HOIP_0040482 HOIP:HOIP_0040484 https://en.wikipedia.org/wiki/Rhabdomyolysis rhabdomyolysis HOIP_0040484 https://en.wikipedia.org/wiki/Rhabdomyolysis Rhabdomyolysis is a condition in which damaged skeletal muscle breaks down rapidly. Some of the muscle breakdown products, such as the protein myoglobin, are harmful to the kidneys and may lead to kidney failure. HOIP:HOIP_0040485 Rhabdomyolysis is a condition in which damaged skeletal muscle breaks down rapidly. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32412710 rhabdomyolysis in severe COVID-19 HOIP_0040485 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. HOIP:HOIP_0040490 Decrease in platelet count is a subtype of decreasing number of objects: A process that becomes smaller in platelet count. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32412710 PMID:32651579 thrombocytopenia decrease in platelet count in severe COVID-19 HOIP_0040490 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. These organ failures may be associated with clinical and laboratory signs of inflammation, including high fevers, thrombocytopenia, hyperferritinemia, and elevations in C-reactive protein and interleukin-6. PMID:32651579 Thrombocytopenia, although often mild (in 5–36% of admissions), is associated with worse patient outcomes. HOIP:HOIP_0040491 Increasing ferritin concentration in blood is a subtype of increasing concentration: A process that changes the ferritin concentration in the blood to be higher. hyperferritinemia increasing ferritin concentration in blood HOIP_0040491 HOIP:HOIP_0040492 Increasing ferritin concentration in blood is a subtype of increasing concentration: A process that changes the ferritin concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32412710 PMID:32651579 hyperferritinemia increasing ferritin concentration in blood (very high) in severe COVID-19 HOIP_0040492 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. These organ failures may be associated with clinical and laboratory signs of inflammation, including high fevers, thrombocytopenia, hyperferritinemia, and elevations in C-reactive protein and interleukin-6. PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0040494 Increasing C-reactive protein concentration in blood is a subtype of increasing concentration: A process that changes the C-reactive protein concentration in the blood to be higher. increasing C-reactive protein concentration in blood HOIP_0040494 HOIP:HOIP_0040495 Vascular dysfunction is a subtype of organ malfunction: A process that does not perform vascular function correctly or not functioning at all. vasculopathy vascular dysfunction HOIP_0040495 HOIP:HOIP_0040498 Merging of the virion membrane and a host membrane (host plasma membrane or host organelle membrane) that is involved in the uptake of a virus into a host cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. membrane fusion involved in viral entry into host cell (very low) in COVID-19 vaccination HOIP_0040498 HOIP:HOIP_0040499 Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. receptor-mediated endocytosis of virus by host cell (very low) in COVID-19 vaccination HOIP_0040499 HOIP:HOIP_0040504 Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. fusion of virus membrane with host endosome membrane (very low) in COVID-19 vaccination HOIP_0040504 HOIP:HOIP_0040505 The cleavage of a peptide bond or bonds within a viral polyprotein. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. non-structural proteins are procduced. viral polyprotein processing (very low) in COVID-19 vaccination HOIP_0040505 HOIP:HOIP_0040506 cardiomyopathy dependent process is a subtype of disease course dependent process: A process that can constitute the course of cardiomyopathy. cardiomyopathy dependent process HOIP_0040506 HOIP:HOIP_0040507 The totality of all processes through which a given cardiomyopathy instance is realized. cardiomyopathy course HOIP_0040507 HOIP:HOIP_0040511 Negative regulation of ACE2 activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 activation. Negative regulation of ACE2 activation HOIP_0040511 HOIP:HOIP_0040512 Negative regulation of ACE2 activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:33077917 Negative regulation of ACE2 activation in COVID-19 HOIP_0040512 PMID:32629875 Angiotensin converting enzyme 2 (ACE2), the receptor for SARS-CoV-2 and other coronaviruses, is a transmembrane protein expressed by lung alveolar epithelial cells, enterocytes, and vascular endothelial cells, whose physiologic role is to induce the maturation of angiotensin I to generate angiotensin 1-7, a peptide hormone that controls vasoconstriction and blood pressure. A consequence of SARS-CoV-2 infection is that ACE2 function is disrupted and this disruption contributes to the pathogenesis to COVID-19. ACE2 belongs to the family of angiotensin-converting enzymes, which are essential regulators of blood pressure, cardiac function, and fluid balance. Also, as a consequence of SARS-CoV-2 receptor binding and entry into any cells, cell surface ACE2 is reduced in association with increased angiotensin II, which confers a pro-inflammatory, pro-coagulant and pro-apoptotic phenotype to endothelial cells. Second, to infect cells, SARS-CoV-2 binds to the cell surface ACE2 receptors, and in so doing compromises the vaso-protective functions of ACE2, an enzyme that attenuates the vasoconstrictive, pro-inflammatory, pro-apoptotic, pro-thrombotic and mitogenic effects of angiotensin II, as discussed in Section 4.2. PMID:33077917 Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. After binding by SARS-CoV-2, ACE2 is internalized, and the lack of ACE2 on endothelial cells favours the progression of inflammatory and thrombotic processes triggered by local angiotensin II (Ang II) hyperactivity. Inhibition of ACE2 by binding of SARS-CoV-2 reduces the ACE2-mediated conversion of Ang II to Ang 1–7, the vasoactive ligand of the MAS receptor. The reduction of MAS receptor activation induces a pro-inflammatory phenotype through increased activation of type 1 angiotensin receptors (AT1R). Additionally, the reduction in levels of ACE2 limits the degradation of des-Arg9 bradykinin (DABK) into inactive peptides, ultimately leading to increased pro-thrombotic signalling via the activation of bradykinin receptors (BKRs). ACE2 internalization following SARS-CoV-2 infection could induce an imbalance in the renin–angiotensin–aldosterone system, with increased Ang II signalling leading to pro-inflammatory and profibrotic processes in the kidney. HOIP:HOIP_0040521 Dysregulation of fluid balance is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of fluid balance appropriately or cannot realize it at all. Dysregulation of fluid balance HOIP_0040521 HOIP:HOIP_0040526 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. viral replication complex formation (very low) in COVID-19 vaccination HOIP_0040526 The process of organizing and assembling viral replication proteins in preparation for viral replication. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. ISBN:0781718325 HOIP:HOIP_0040527 A process by which viral mRNA is translated into viral protein for viral replication complex, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is low. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis translation for viral replication complex (very low) in COVID-19 vaccination HOIP_0040527 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0040528 A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. viral genome expression viral gene expression (very low) in COVID-19 vaccination HOIP_0040528 HOIP:HOIP_0040530 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces subgenomic negative stranded (-) mRNA . This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. subgenomic negative stranded viral mRNA biosynthetic process (very low) in COVID-19 vaccination HOIP_0040530 HOIP:HOIP_0040531 The cleavage of a peptide bond or bonds within a viral protein. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. viral protein processing (very low) in COVID-19 vaccination HOIP_0040531 HOIP:HOIP_0040534 Any process that activates or increases the frequency, rate or extent of apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 positive regulation of apoptotic process in COVID-19 HOIP_0040534 PMID:32629875 Also, as a consequence of SARS-CoV-2 receptor binding and entry into any cells, cell surface ACE2 is reduced in association with increased angiotensin II, which confers a pro-inflammatory, pro-coagulant and pro-apoptotic phenotype to endothelial cells. HOIP:HOIP_0040535 Any process that activates or increases the frequency, rate or extent of apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 positive regulation of apoptotic process in severe COVID-19 HOIP_0040535 PMID:32629875 In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). HOIP:HOIP_0040537 thrombosis dependent process is a subtype of disease course dependent process: A process that can constitute the course of thrombosis. thrombosis dependent process HOIP_0040537 HOIP:HOIP_0040539 thrombus formation is a subtype of biological structure formation: A process that construcs thrombus. This entity is a specific course-dependent process. This process can constitute the course of thrombosis. thrombus formation [thrombosis(course)] HOIP_0040539 HOIP:HOIP_0040540 A viral transcription process that uses positive stranded (+) single stranded (ss) RNA as a template and produces the full-length negative stranded (-) mRNA for synthesis of new genomic RNAs and subgenomic negative strand templates. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. full length negative stranded viral mRNA biosynthetic process full length negative stranded viral mRNA biosynthetic process (very low) in COVID-19 vaccination HOIP_0040540 HOIP:HOIP_0040541 A process by which viral mRNA is translated into viral protein, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. The functioning level is very low. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis viral translation (very low) in COVID-19 vaccination HOIP_0040541 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0040542 pulmonary embolism dependent process is a subtype of disease course dependent process: A process that can constitute the course of pulmonary embolism. pulmonary embolism dependent process HOIP_0040542 HOIP:HOIP_0040543 embolus formation is a subtype of biological structure formation: A process that construcs embolus. embolus formation HOIP_0040543 HOIP:HOIP_0040544 Embolus formation in lung is a subtype of embolus formation: A process that construcs embolus in lung. This entity is a specific course-dependent process. This process can constitute the course of pulmonary embolism. embolus formation in lung [pulmonary embolism course] HOIP_0040544 HOIP:HOIP_0040545 embolus formation in lung is a subtype of embolus formation: A process that construcs embolus in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 PMID:32651579 embolus formation in lung in COVID-19 associated with ARDS HOIP_0040545 PMID:32629875 An autopsy series showed the presence of deep venous thrombosis involving the lower extremities bilaterally in 56% (7/12) of cases, associated with massive pulmonary embolism in four of these cases, which was listed as the cause of death. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. A systematic search for pulmonary emboli in 26 COVID-19 patients on mechanical ventilation showed that they were detected in 23% (6/26) of patients, and venous thromboembolism (VTE) was detected in 69% (18/26). Results of 12 consecutive complete autopsies of patients with COVID-19 concluded that massive pulmonary embolism was the cause of death in 4/12 cases and that VTE was present in 7/12 (58%) patients. PMID:32651579 Isolated right ventricular failure with and without confirmed pulmonary embolism has also been reported. Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. HOIP:HOIP_0040546 The totality of all processes through which a given pulmonary embolism instance is realized. pulmonary embolism course HOIP_0040546 HOIP:HOIP_0040549 Capillary congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the capillary. capillary congestion HOIP_0040549 HOIP:HOIP_0040551 Capillary congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the capillary. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 capillary congestion in severe COVID-19 HOIP_0040551 PMID:32629875 Post-mortem histopathologic analysis of lung tissue from 38 COVID-19 patients documented the presence of platelet-fibrin thrombi in lung arterioles of most (33/38) cases, congested capillaries (33/38) proximal to hemorrhagic alveoli often containing CD61+ megakaryocytes, and dense capillary foci presumably resulting from vessel intussusceptive sprouting (18/38). A comprehensive post-mortem analysis of multiple tissues (in 3 COVID-19 cases) described congestion and endotheliitis of small vessels with accumulation of mononuclear/lymphocytic cells around the capillary endothelium in the heart, small bowel, kidney, liver and lung; in one case, caspase 3-immunostaining revealed the presence of apoptotic bodies in endothelial cells lining the inner wall of inflamed blood vessels. As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. HOIP:HOIP_0040553 The movement of megakaryocytes within or between different tissues and organs of the body. megakaryocyte migration megakaryocyte trafficking megakaryocyte migration HOIP_0040553 HOIP:HOIP_0040557 Intussusceptive angiogenesis is a subtype of biological structure formation: A process that constructs an alternate blood vessels. Intussusceptive angiogenesis also known as splitting angiogenesis, is a type of angiogenesis, the process whereby a new blood vessel is created. (https://en.wikipedia.org/wiki/Intussusceptive_angiogenesis) This process can constitute the course of severe COVID-19. PMID:32629875 Intussusceptive angiogenesis in severe COVID-19 HOIP_0040557 PMID:32629875 Post-mortem histopathologic analysis of lung tissue from 38 COVID-19 patients documented the presence of platelet-fibrin thrombi in lung arterioles of most (33/38) cases, congested capillaries (33/38) proximal to hemorrhagic alveoli often containing CD61+ megakaryocytes, and dense capillary foci presumably resulting from vessel intussusceptive sprouting (18/38). As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. HOIP:HOIP_0040558 Increasing density is a subtype of changing density: A process that increases the density of the object. increasing density HOIP_0040558 HOIP:HOIP_0040559 Increasing density is a subtype of changing density: A process that increases the density of the object. increasing density of capillary HOIP_0040559 HOIP:HOIP_0040560 Increasing density is a subtype of changing density: A process that increases the density of the object. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 increasing density of capillary in severe COVID-19 HOIP_0040560 PMID:32629875 Post-mortem histopathologic analysis of lung tissue from 38 COVID-19 patients documented the presence of platelet-fibrin thrombi in lung arterioles of most (33/38) cases, congested capillaries (33/38) proximal to hemorrhagic alveoli often containing CD61+ megakaryocytes, and dense capillary foci presumably resulting from vessel intussusceptive sprouting (18/38). HOIP:HOIP_0040561 Endothelium damage is a subtype of damaging: A process that injuries the structure of the endothelium as the direct or indirect result of an external force. endotheliitis endothelium damage HOIP_0040561 HOIP:HOIP_0040563 The movement of a lymphocyt within or between different tissues and organs of the body. lymphocyte migration HOIP_0040563 HOIP:HOIP_0040564 The movement of a lymphocyt within or between different tissues and organs of the body. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 lymphocyte migration in severe COVID-19 HOIP_0040564 PMID:32629875 A comprehensive post-mortem analysis of multiple tissues (in 3 COVID-19 cases) described congestion and endotheliitis of small vessels with accumulation of mononuclear/lymphocytic cells around the capillary endothelium in the heart, small bowel, kidney, liver and lung; in one case, caspase 3-immunostaining revealed the presence of apoptotic bodies in endothelial cells lining the inner wall of inflamed blood vessels. Immune dysfunction is not known to play a role in typical COVID-19, except for the severe lymphopenia in severe cases of COVID-19, which may relate to tissue recruitment of lymphocyte and redistribution away from blood, and perhaps a low or delayed type I interferon response. HOIP:HOIP_0040565 Brain infarction dependent process is a subtype of disease course dependent process: A process that can constitute the course of brain infarction. brain infarction dependent process HOIP_0040565 HOIP:HOIP_0040566 The totality of all processes through which a given brain infarction instance is realized. brain infarction course HOIP_0040566 HOIP:HOIP_0040571 Fibrosis is a subtype of changing material: A process that replaces tissues to fibrous connective tissues/ This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 http://purl.obolibrary.org/obo/MPATH_181 fibrosis in severe COVID-19 HOIP_0040571 PMID:32629875 As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. HOIP:HOIP_0040573 The appearance of chemokine (C-C motif) ligand 10 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32422178 PMID:32629875 PMID:34046036 IP-10 production chemokine (C-C motif) ligand 10 production (very high) in severe COVID-19 HOIP_0040573 PMID:32422178 Indeed, circulating IFN-gamma and CXCL10 concentrations are raised in patients with severe COVID-19. PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. PMID:34046036 CXCL10/IP10 is also secreted by many cells, including monocytes, endothelial cells, and fibroblasts, in response to IFN-gamma. Several clinical investigations involving autopsies have also provided evidence that thrombosis is an important consequence of hCoV diseases. These findings indicate that the thrombosis-related indicators (CXCL10/IP10, MCP-1) could be directly involved in different stages of hCoV infection and could be used as potential biomarkers to predict the risk of death in hCoV patients. HOIP:HOIP_0040575 The appearance of GM-CSF (granulocyte macrophage colony-stimulating factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 granulocyte macrophage colony-stimulating factor production GM-CSF production in COVID-19 HOIP_0040575 PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0040577 Organ damage is a subtype of damaging: A process that injures the structure of the organ as the direct or indirect result of an external force. organ damage HOIP_0040577 HOIP:HOIP_0040579 Increasing fibrinogen concentration is a subtype of increasing concentration: A process that changes the fibrinogen concentration to be higher. increasing fibrinogen concentration HOIP_0040579 HOIP:HOIP_0040580 Increasing fibrinogen concentration is a subtype of increasing concentration: A process that changes the fibrinogen concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32651579 increasing fibrinogen concentration (very high) in severe COVID-19 HOIP_0040580 PMID:32629875 In a group of 22 consecutive COVID-19 patients admitted to the ICU, increased fibrinogen and D-dimer plasma levels, shorter clotting time and other coagulation abnormalities were significantly more frequent compared to healthy controls. Acting on hepatocytes, IL-6 promotes the synthesis of fibrinogen, tissue factor and Factor VII. PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0040583 Narrowing of the mesenteric artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the mesenteric arteries to be smaller. mesenteric artery narrowing HOIP_0040583 HOIP:HOIP_0040584 disseminated intravascular coagulation dependent process is a subtype of disease course dependent process: A process that can constitute the course of disseminated intravascular coagulation. disseminated intravascular coagulation dependent process HOIP_0040584 HOIP:HOIP_0040585 Hepatic blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform hepatic blood vessel function correctly or not functioning at all. PMID:32629875 hepatic blood vessel dysfunction HOIP_0040585 PMID:32629875 Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. HOIP:HOIP_0040586 thrombus formation is a subtype of biological structure formation: A process that construcs thrombus. This entity is a specific course-dependent process. This process can constitute the course of disseminated intravascular coagulation. thrombus formation (severe) [disseminated intravascular coagulation course] HOIP_0040586 HOIP:HOIP_0040587 Decrease in platelet count is a subtype of decreasing number of objects: A process that becomes smaller in platelet count. This entity is a specific course-dependent process. This process can constitute the course of disseminated intravascular coagulation. thrombocytopenia decrease in platelet count [disseminated intravascular coagulation course] HOIP_0040587 HOIP:HOIP_0040588 Narrowing of the mesenteric artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the mesenteric arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 mesenteric artery narrowing in severe COVID-19 HOIP_0040588 PMID:32629875 Surgical resection specimens from four patients with COVID-19 with severe abdominal symptoms showed macroscopic evidence of bowel infarction or ischemia. Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. HOIP:HOIP_0040589 Decreasing coagulation factor level is a subtype of decreasing quantity: A process that changes the amount of coagulation factor level to be lower. Decreasing coagulation factor level HOIP_0040589 HOIP:HOIP_0040590 Decreasing coagulation factor level is a subtype of decreasing quantity: A process that changes the amount of coagulation factor level to be lower. This entity is a specific course-dependent process. This process can constitute the course of disseminated intravascular coagulation. Decreasing coagulation factor level [disseminated intravascular coagulation course] HOIP_0040590 HOIP:HOIP_0040591 Tubular damage is a subtype of organ damaging: A process that injuries the structure of the tubular as the direct or indirect result of an external force. tubular injury tubular damage HOIP_0040591 HOIP:HOIP_0040592 Decreasing coagulation factor level is a subtype of decreasing quantity: A process that changes the amount of coagulation factor level to be lower. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Decreasing coagulation factor level in severe COVID-19 HOIP_0040592 HOIP:HOIP_0040593 A process that emits blood. This entity is a specific course-dependent process. This process can constitute the course of disseminated intravascular coagulation. hemorrhage bleeding [disseminated intravascular coagulation course] HOIP_0040593 HOIP:HOIP_0040594 The totality of all processes through which a given disseminated intravascular coagulation instance is realized. disseminated intravascular coagulation course HOIP_0040594 HOIP:HOIP_0040595 Increasing soluble IL-6R alpha level is a subtype of increasing quantity: A process that changes the amount of soluble IL-6R alpha level to be higher. Increasing soluble IL-6R alpha level HOIP_0040595 HOIP:HOIP_0040596 Increasing soluble IL-6R alpha level is a subtype of increasing quantity: A process that changes the amount of soluble IL-6R alpha level to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 Increasing soluble IL-6R alpha level in severe COVID-19 HOIP_0040596 PMID:32629875 Since soluble IL-6R is abnormally elevated in the plasma of COVID-19 patients, presumably secondary to cleavage from the cells surface by TACE/ADAM17 upon SARS-CoV-2 infection and the inflammatory response associated with COVID-19 [29], IL-6 can activate most cells, including endothelial cells, which do not express endogenous IL-6R but can be activated by the complex of soluble IL-6R and IL-6. HOIP:HOIP_0040597 The process in which IL-6R alpha is released from the cell surface. Release of IL6-R alpha from cell surface HOIP_0040597 HOIP:HOIP_0040600 The change in morphology and behavior of a endothelial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. endothelial cell activation HOIP_0040600 HOIP:HOIP_0040601 The change in morphology and behavior of a endothelial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:33077917 endothelial cell activation in COVID-19 HOIP_0040601 PMID:32629875 Since soluble IL-6R is abnormally elevated in the plasma of COVID-19 patients, presumably secondary to cleavage from the cells surface by TACE/ADAM17 upon SARS-CoV-2 infection and the inflammatory response associated with COVID-19, IL-6 can activate most cells, including endothelial cells, which do not express endogenous IL-6R but can be activated by the complex of soluble IL-6R and IL-6. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0040602 Any process that activates or increases the frequency, rate or extent of blood coagulation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 positive regulation of blood coagulation in COVID-19 HOIP_0040602 PMID:32629875 In COVID-19, adding to the blood clotting risk from increased IL-6, SARS-CoV-2 can infect, replicate and induce endothelial cell death, compromising the continuity of the luminal vascular surface; a perturbed endothelium can actively participate in pro-coagulant reactions. Also, as a consequence of SARS-CoV-2 receptor binding and entry into any cells, cell surface ACE2 is reduced in association with increased angiotensin II, which confers a pro-inflammatory, pro-coagulant and pro-apoptotic phenotype to endothelial cells. HOIP:HOIP_0040604 Decreasing bowel blood flow is a subtype of decreasing flow: A process that changes the amount of bowel blood flow to be lower. decreasing bowel blood flow HOIP_0040604 HOIP:HOIP_0040605 Any process that stops, prevents, or reduces the frequency, rate or extent of angiotensin signaling, a series of reactions mediated by angiotensin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 negative regulation of angiotensin signaling in COVID-19 HOIP_0040605 PMID:32629875 Also, as a consequence of SARS-CoV-2 receptor binding and entry into any cells, cell surface ACE2 is reduced in association with increased angiotensin II, which confers a pro-inflammatory, pro-coagulant and pro-apoptotic phenotype to endothelial cells. Second, to infect cells, SARS-CoV-2 binds to the cell surface ACE2 receptors, and in so doing compromises the vaso-protective functions of ACE2, an enzyme that attenuates the vasoconstrictive, pro-inflammatory, pro-apoptotic, pro-thrombotic and mitogenic effects of angiotensin II, as discussed in Section 4.2. HOIP:HOIP_0040606 Decreasing bowel blood flow is a subtype of decreasing flow: A process that changes the amount of bowel blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 decreasing bowel blood flow in severe COVID-19 HOIP_0040606 PMID:32629875 Surgical resection specimens from four patients with COVID-19 with severe abdominal symptoms showed macroscopic evidence of bowel infarction or ischemia. Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. HOIP:HOIP_0040607 Bowel ischemia is a changing process to lack enough to blood supply of bowel. bowel ischemia HOIP_0040607 HOIP:HOIP_0040608 Bowel ischemia is a changing process to lack enough to blood supply of Bowel. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 bowel ischemia in severe COVID-19 HOIP_0040608 PMID:32629875 Table 1. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. Surgical resection specimens from four patients with COVID-19 with severe abdominal symptoms showed macroscopic evidence of bowel infarction or ischemia. Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. HOIP:HOIP_0040609 A type of hepatic cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. hepatic cell necrosis HOIP_0040609 HOIP:HOIP_0040610 A type of hepatic cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This process can constitute the course of COVID-19 in the liver. PMID:32629875 PMID:32651579 hepatic cell necrosis in COVID-19 in liver HOIP_0040610 PMID:32629875 Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. PMID:32651579 Other histopathologic changes in the liver included hepatic steatosis, portal fibrosis, lymphocytic infiltrates and ductular proliferation, lobular cholestasis, and acute liver-cell necrosis, together with central-vein thrombosis. HOIP:HOIP_0040611 A type of bowel cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. bowel cell necrosis HOIP_0040611 HOIP:HOIP_0040612 transient ischemic attack dependent process is a subtype of disease course dependent process: A process that can constitute the course of transient ischemic attack. transient ischemic attack dependent process HOIP_0040612 HOIP:HOIP_0040613 The totality of all processes through which a given transient ischemic attack instance is realized. transient ischemic attack course HOIP_0040613 HOIP:HOIP_0040614 Narrowing of the brain artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the cerebral arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of transient ischemic attack. brain artery narrowing [transient ischemic attack course] HOIP_0040614 HOIP:HOIP_0040615 Decreasing brain blood flow is a subtype of decreasing flow: A process that changes the amount of brain blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of transient ischemic attack. decreasing brain blood flow [transient ischemic attack course] HOIP_0040615 HOIP:HOIP_0040616 Brain Ischemia is a changing process to lack enough to blood supply of brain. This entity is a specific course-dependent process. This process can constitute the course of brain infaction. brain ischemia [transient ischemic attack course] HOIP_0040616 HOIP:HOIP_0040617 A type of bowel cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 bowel cell necrosis in severe COVID-19 HOIP_0040617 PMID:32629875 Surgical resection specimens from four patients with COVID-19 with severe abdominal symptoms showed macroscopic evidence of bowel infarction or ischemia. Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. HOIP:HOIP_0040618 Hepatic blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform hepatic blood vessel function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32629875 hepatic blood vessel dysfunction in COVID-19 in liver HOIP_0040618 PMID:32629875 Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. HOIP:HOIP_0040619 Narrowing of the mesenteric artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the mesenteric arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of bowel infarction. mesenteric artery narrowing [bowel infarction course] HOIP_0040619 HOIP:HOIP_0040620 Increasing portal vein lumen area is a subtype of increasing area: A process that changes the area of the portal vein lumen area to be larger. portal vessel dilation increasing portal vein lumen area HOIP_0040620 HOIP:HOIP_0040621 Increasing portal vein lumen area is a subtype of increasing area: A process that changes the area of the portal vein lumen area to be larger. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32629875 portal vessel dilation in COVID-19 in liver increasing portal vein lumen area in COVID-19 in liver HOIP_0040621 PMID:32629875 Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. HOIP:HOIP_0040622 Hepatic fibrosis is a subtype of fibrosis: A process that replaces liver tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32629875 hepatic fibrosis in COVID-19 in liver HOIP_0040622 PMID:32629875 Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. HOIP:HOIP_0040623 Decreasing bowel blood flow is a subtype of decreasing flow: A process that changes the amount of bowel blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of bowel infarction. decreasing bowel blood flow [bowel infarction course] HOIP_0040623 HOIP:HOIP_0040624 Anoxic brain damage is a subtype of brain damage: A process that injuries the structure of the brain as the direct or indirect result of anoxia. anoxic brain injury anoxic brain damage HOIP_0040624 HOIP:HOIP_0040625 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of neural tissue. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 viral entry into host cell in neural tissue in COVID-19 in nervous system SARS-CoV-2 entry to host cell in COVID-19 in nervous system HOIP_0040625 PMID:32651579 Direct viral invasion of neural parenchyma is a possibility; SARS-CoV-2 may access the central nervous system via the nasal mucosa, lamina cribrosa, and olfactory bulb or via retrograde axonal transport. HOIP:HOIP_0040626 Nervous system malfunction is a subtype of malfunction: A process that does not perform nervous system system function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32412710 PMID:32651579 nervous system system malfunction in COVID-19 in nervous system HOIP_0040626 PMID:32412710 The majority of patients with severe Covid-19 have lymphopenia, and some have thromboembolic complications as well as disorders of the central or peripheral nervous system. PMID:32651579 A number of non-specific mild neurological symptoms are notable in hospitalized patients with COVID-19, including headache (8–42%), dizziness (12%), myalgia and/or fatigue (11–44%), anorexia (40%), anosmia (5%), and ageusia (5%), although the epidemiology may be different in milder outpatient presentations. Direct viral invasion of neural parenchyma is a possibility; SARS-CoV-2 may access the central nervous system via the nasal mucosa, lamina cribrosa, and olfactory bulb or via retrograde axonal transport. HOIP:HOIP_0040627 Bowel ischemia is a changing process to lack enough to blood supply of Bowel. This entity is a specific course-dependent process. This process can constitute the course of bowel infarction. bowel ischemia [bowel infarction course] HOIP_0040627 HOIP:HOIP_0040628 Edema in brain is a subtype of edema: A process that keeps an excessive fluid in cells or intercellular tissues of brain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32629875 edema (process) in brain in COVID-19 in nervous system HOIP_0040628 PMID:32629875 Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. A post-mortem imaging study involving 19 patients who had died of COVID-19 disease showed subcortical bleeds in 2/19 cases and edematous changes in the cortex/subcortical regions in 1/19 cases. HOIP:HOIP_0040629 A type of bowel cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. bowel cell necrosis [bowel infarction course] HOIP_0040629 HOIP:HOIP_0040630 bowel infarction dependent process is a subtype of disease course dependent process: A process that can constitute the course of bowel infarction. bowel infarction dependent process HOIP_0040630 HOIP:HOIP_0040631 The totality of all processes through which a given bowel infarction instance is realized. bowel infarction course HOIP_0040631 HOIP:HOIP_0040633 Bowel blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform bowel blood vessel function correctly or not functioning at all. bowel blood vessel dysfunction HOIP_0040633 HOIP:HOIP_0040634 Bowel blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform bowel blood vessel function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 bowel blood vessel dysfunction in severe COVID-19 HOIP_0040634 PMID:32629875 Several studies have described the presence of abdominal symptoms, such as nausea, vomiting and diarrhea in a variable proportion (5–50%) of patients who also had respiratory symptoms of COVID-19. In a multicenter study of 318 patients with confirmed COVID-19, 61% of patients reported at least one gastrointestinal symptom on presentation, most commonly anorexia (35%), diarrhea (34%) and nausea (26%). The vascular pathology was considered causative of the bowel ischemia, raising the broader possibility that gastrointestinal symptoms in COVID-19 may have a vascular pathogenesis. HOIP:HOIP_0040635 Bowel infarction or gangrenous bowel represents an irreversible injury to the intestine resulting from insufficient blood flow. (https://en.wikipedia.org/wiki/Bowel_infarction) bowel infarction HOIP_0040635 HOIP:HOIP_0040636 The movement of a mononuclear cell within or between different tissues and organs of the body. mononuclear cell migration HOIP_0040636 HOIP:HOIP_0040637 The totality of all processes through which COVID-19 infection accompanied by myocarditis is realized. COVID-19 course associated with myocarditis HOIP_0040637 HOIP:HOIP_0040638 Microthrombus formation in brain is a subtype of microthrombus formation: A process that construcs microthrombus. Microthrombus formation in brain HOIP_0040638 HOIP:HOIP_0040639 Increasing troponin concentration is a subtype of increasing concentration: A process that changes the troponin concentration to be higher. Increasing troponin concentration HOIP_0040639 HOIP:HOIP_0040640 Interacting selectively and non-covalently with a receptor on the host cell surface of myocardium. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 PMID:32651579 SARS-CoV-2 S binding to human ACE2 (very high) in COVID-19 associated with myocarditis HOIP_0040640 PMID:32629875 Also, genetic and pharmacological studies in mice have shown that ACE2 regulates cardiac structure and function; decreased ACE2 in SARS-CoV-2-infected cardiomyocytes could disrupt these activities, particularly impairing cardiac remodeling and increasing oxidative stress in cardiomyocytes. PMID:32651579 ACE2 has high expression in cardiovascular tissue, including cardiac myocytes, fibroblasts, endothelial cells, and smooth-muscle cells in support of a possible mechanism of direct viral injury. HOIP:HOIP_0040641 bowel infarction dependent process is a subtype of disease course dependent process: A process that can constitute the course of bowel infarction. pulmonary infarction dependent process HOIP_0040641 HOIP:HOIP_0040642 Cardiac muscle cells are striated muscle cells that are responsible for heart contraction. In mammals, the contractile fiber resembles those of skeletal muscle but are only one third as large in diameter, are richer in sarcoplasm, and contain centrally located instead of peripheral nuclei. cardiomyocyte cardiac muscle cell HOIP_0040642 HOIP:HOIP_0040644 Negative regulation of ACE2 activation in cardiomyocytes is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 activation in cardiomyocytes. Negative regulation of ACE2 activation in cardiomyocytes HOIP_0040644 HOIP:HOIP_0040645 Negative regulation of ACE2 activation in cardiomyocytes is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 activation in cardiomyocytes. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 negative regulation of ACE2 activation in cardiomyocytes in COVID-19 associated with myocarditis HOIP_0040645 PMID:32629875 Also, genetic and pharmacological studies in mice have shown that ACE2 regulates cardiac structure and function; decreased ACE2 in SARS-CoV-2-infected cardiomyocytes could disrupt these activities, particularly impairing cardiac remodeling and increasing oxidative stress in cardiomyocytes. HOIP:HOIP_0040646 Negative regulation of cell function is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the cell function. negative regulation of cellular function HOIP_0040646 HOIP:HOIP_0040647 Negative regulation of cardiomyocyte function is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the cardiomyocyte function. negative regulation of cardiomyocyte function HOIP_0040647 HOIP:HOIP_0040649 The directed movement of a virus, or part of a virus into kidney. transport of virus into kidney HOIP_0040649 HOIP:HOIP_0040650 A process that emits blood in brain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32629875 Wikipedia:Intracranial hemorrhage hemorrhage in brain bleeding in brain in COVID-19 in nervous system HOIP_0040650 PMID:32629875 A post-mortem imaging study involving 19 patients who had died of COVID-19 disease showed subcortical bleeds in 2/19 cases and edematous changes in the cortex/subcortical regions in 1/19 cases. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. Wikipedia:Intracranial hemorrhage Intracranial hemorrhage is a serious medical emergency because the buildup of blood within the skull can lead to increases in intracranial pressure, which can crush delicate brain tissue or limit its blood supply. HOIP:HOIP_0040651 A type of pulmonary cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. pulmonary cell necrosis HOIP_0040651 HOIP:HOIP_0040652 a severe condition related to Kawasaki disease (KD) Kawasaki disease shock syndrome HOIP_0040652 HOIP:HOIP_0040653 A type of pulmonary cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of pulmonary infarction. pulmonary cell necrosis [pulmonary infarction (course)] HOIP_0040653 HOIP:HOIP_0040654 Pulmonary ischemia is a changing process to lack enough to blood supply of lung. pulmonary ischemia HOIP_0040654 HOIP:HOIP_0040656 Pulmonary ischemia is a changing process to lack enough to blood supply of lung. This entity is a specific course-dependent process. This process can constitute the course of pulmonary infarction. pulmonary ischemia [pulmonary infarction (course)] HOIP_0040656 HOIP:HOIP_0040657 Pulmonary ischemia is a changing process to lack enough to blood supply of lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 pulmonary ischemia in COVID-19 associated with ARDS HOIP_0040657 PMID:32629875 Another report on 11 randomly selected COVID-19 autopsies described macroscopic pulmonary thrombi in all cases with associated pulmonary infarcts in 9/11 autopsies. HOIP:HOIP_0040658 A type of pulmonary cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 pulmonary cell necrosis in COVID-19 associated with ARDS HOIP_0040658 PMID:32629875 Another report on 11 randomly selected COVID-19 autopsies described macroscopic pulmonary thrombi in all cases with associated pulmonary infarcts in 9/11 autopsies. HOIP:HOIP_0040659 Narrowing of the pulmonary artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the pulmonary arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of pulmonary infarction. pulmonary artery narrowing [pulmonary infarction (course)] HOIP_0040659 HOIP:HOIP_0040660 Thrombus formation in lung is a subtype of thrombus formation: A process that construcs thrombus in lung. thrombus formation in lung HOIP_0040660 HOIP:HOIP_0040661 Narrowing of the pulmonary artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the pulmonary arteries to be smaller. pulmonary artery narrowing HOIP_0040661 HOIP:HOIP_0040662 Narrowing of the pulmonary artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the pulmonary arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 PMID:32651579 pulmonary artery narrowing in COVID-19 associated with ARDS HOIP_0040662 PMID:32629875 Another report on 11 randomly selected COVID-19 autopsies described macroscopic pulmonary thrombi in all cases with associated pulmonary infarcts in 9/11 autopsies. PMID:32651579 Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. HOIP:HOIP_0040663 Decreasing pulmonary blood flow is a subtype of decreasing flow: A process that changes the amount of pulmonary blood flow to be lower. decreasing pulmonary blood flow HOIP_0040663 HOIP:HOIP_0040664 Decreasing pulmonary blood flow is a subtype of decreasing flow: A process that changes the amount of pulmonary blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of pulmonary infarction. decreasing pulmonary blood flow [pulmonary infarction (course)] HOIP_0040664 HOIP:HOIP_0040665 Decreasing pulmonary blood flow is a subtype of decreasing flow: A process that changes the amount of pulmonary blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 decreasing pulmonary blood flow in COVID-19 associated with ARDS HOIP_0040665 PMID:32629875 Another report on 11 randomly selected COVID-19 autopsies described macroscopic pulmonary thrombi in all cases with associated pulmonary infarcts in 9/11 autopsies. HOIP:HOIP_0040666 Embolus formation in lung is a subtype of embolus formation: A process that construcs embolus in lung. embolus formation in lung HOIP_0040666 HOIP:HOIP_0040667 Detaching of blood clot is a subtype of detaching: A process of a blood clot detaching from the area of the blood stream where it coagulated and grew to obstruct the vessel. detaching of blood clot HOIP_0040667 HOIP:HOIP_0040668 Thrombus formation in deep vein is a subtype of thrombus formation: A process that construcs thrombus in deep vein. thrombus formation in deep vein HOIP_0040668 HOIP:HOIP_0040669 Thrombus formation in deep vein is a subtype of thrombus formation: A process that construcs thrombus in deep vein. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 thrombus formation in deep vein in severe COVID-19 HOIP_0040669 PMID:32629875 An autopsy series showed the presence of deep venous thrombosis involving the lower extremities bilaterally in 56% (7/12) of cases, associated with massive pulmonary embolism in four of these cases, which was listed as the cause of death. Results of 12 consecutive complete autopsies of patients with COVID-19 concluded that massive pulmonary embolism was the cause of death in 4/12 cases and that VTE was present in 7/12 (58%) patients. Consistent with the presence of a coagulopathy, deep vein thrombosis appears more frequently than expected in hospitalized COVID-19 patients, even with anti-coagulant prophylaxis. HOIP:HOIP_0040670 Increasing lactate dehydrogenase concentration is a subtype of increasing concentration: A process that changes the lactate dehydrogenase concentration to be higher. increasing lactate dehydrogenase concentration HOIP_0040670 HOIP:HOIP_0040671 lactate dehydrogenase HOIP_0040671 HOIP:HOIP_0040672 Increasing lactate dehydrogenase concentration is a subtype of increasing concentration: A process that changes the lactate dehydrogenase concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32651579 increasing lactate dehydrogenase concentration (very high) in severe COVID-19 HOIP_0040672 PMID:32629875 The most common imaging and laboratory findings included abnormal chest CT scans (71 % ground-glass opacity and 30% consolidation), lymphopenia (48%), increased lactate dehydrogenase (42%), D-Dimer elevation (43%), and indicators of inflammation, including C-reactive protein and erythrocyte sedimentation rate. PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0040673 Thrombus formation in portal and sinusoidal vessels is a subtype of thrombus formation: A process that construcs thrombus in portal and sinusoidal vessels. thrombus formation in portal and sinusoidal vessels HOIP_0040673 HOIP:HOIP_0040674 Thrombus formation in portal and sinusoidal vessels is a subtype of thrombus formation: A process that construcs thrombus in portal and sinusoidal vessels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32629875 thrombus formation in portal and sinusoidal vessels in COVID-19 in liver HOIP_0040674 PMID:32629875 Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. HOIP:HOIP_0040675 A process that emits blood in lung. hemorrhage in lung bleeding in lung HOIP_0040675 HOIP:HOIP_0040676 A process that emits blood in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 PMID:33077917 hemorrhage in lung bleeding in lung in COVID-19 associated with ARDS HOIP_0040676 PMID:32629875 Post-mortem histopathologic analysis of lung tissue from 38 COVID-19 patients documented the presence of platelet-fibrin thrombi in lung arterioles of most (33/38) cases, congested capillaries (33/38) proximal to hemorrhagic alveoli often containing CD61+ megakaryocytes, and dense capillary foci presumably resulting from vessel intussusceptive sprouting (18/38). Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0040677 A process that emits blood in liver. hemorrhage in liver bleeding in liver HOIP_0040677 HOIP:HOIP_0040678 A process that emits blood in liver. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 hemorrhage in liver bleeding in liver in COVID-19 in liver HOIP_0040678 PMID:32629875 Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. HOIP:HOIP_0040679 A process that emits blood in brain. hemorrhage in brain bleeding in brain HOIP_0040679 HOIP:HOIP_0040680 Microthrombus formation in brain is a subtype of microthrombus formation: A process that construcs microthrombus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 Microthrombus formation in brain in COVID-19 associated with cerebral infarction HOIP_0040680 PMID:32629875 In addition, 6/20 cases showed widespread microthrombi associated with evidence of patchy ischemic infarcts. Diffuse microthrombi in the brain may underlie cognitive problems, headaches, and other symptoms in patients with COVID-19 even after the apparent resolution of the disease. HOIP:HOIP_0040681 A troponin T, cardiac muscle that is encoded in the genome of human. Troponin, or the troponin complex, is a complex of three regulatory proteins (troponin C, troponin I, and troponin T) that are integral to muscle contraction[2] in skeletal muscle and cardiac muscle, but not smooth muscle. (https://en.wikipedia.org/wiki/Troponin) PMID:32629875 UniProtKB:P45379 cardiac muscle troponin T (human) hTNNT2 troponin T, cardiac muscle (human) HOIP_0040681 PMID:32629875 Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. HOIP:HOIP_0040682 A fibrinogen complex that is composed of two trimers of human fibrinogen alpha, fibrinogen beta, and fibrinogen gamma subunits. PMID:32629875 hFG fibrinogen complex (human) HOIP_0040682 PMID:32629875 In a group of 22 consecutive COVID-19 patients admitted to the ICU, increased fibrinogen and D-dimer plasma levels, shorter clotting time and other coagulation abnormalities were significantly more frequent compared to healthy controls. HOIP:HOIP_0040683 Brain edema dependent process is a subtype of disease course dependent process: A process that can constitute the course of brain edema. brain edema dependent process HOIP_0040683 HOIP:HOIP_0040685 Edema in brain is a subtype of edema: A process that keeps an excessive fluid in cells or intercellular tissues of brain. edema (process) in brain HOIP_0040685 HOIP:HOIP_0040686 Anoxic brain damage is a subtype of brain damage: A process that injuries the structure of the brain as the direct or indirect result of anoxia. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. Wikipedia:Cerebral_infarction anoxic brain injury anoxic brain damage [brain infarction course] HOIP_0040686 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0040689 A protein complex that binds iron and acts as a major iron storage system. Intracellular and extracellular ferritin complexes have different ratios of two types of ferritin monomer, the L (light) chain and H (heavy) chain. ferritin complex HOIP_0040689 HOIP:HOIP_0040691 A role played by the entity that shows an expression change according to the degree of cardiac damage. Cardiac biomarker role HOIP_0040691 HOIP:HOIP_0040692 Negative regulation of thrombus formation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of thrombus formation. Negative regulation of thrombus formation HOIP_0040692 HOIP:HOIP_0040693 Negative regulation of thrombus formation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of thrombus formation.　This process can constitute the course of COVID-19 drug treatment. negative regulation of thrombus formation in COVID-19 drug treatment HOIP_0040693 HOIP:HOIP_0040694 A role played by the entity which that neutralizes the IL-6R by binding specifically to it. IL-6R antibody HOIP_0040694 HOIP:HOIP_0040695 The killing by a virus of a cell by means of the rupture of cell membranes and the loss of cytoplasm. The killing by a virus of a cell by means of the rupture of cell membranes and the loss of cytoplasm. The killing by a virus of a cell by means of the rupture of cell membranes and the loss of cytoplasm. This process can constitute the course of COVID-19. https://github.com/geneontology/go-ontology/issues/18852 GO:0019077 GO:0046756 PMID:32629875 VZ:1077 lytic viral release viral exit from host cell by cytolysis viral release by cell lysis viral release by host cell lysis cytolysis by virus of host cell lytic viral life cycle viral release from host cell by cytolysis in COVID-19 HOIP_0040695 The killing by a virus of a cell by means of the rupture of cell membranes and the loss of cytoplasm. GOC:jl PMID:26728778 PMID:32629875 First, SARS-CoV-2 can cause endothelial cell death through lytic replication, as discussed in Section 4.1. VZ:1077 Cell lysis HOIP:HOIP_0040696 Any process that activates or increases the frequency, rate or extent of thrombus formation. positive regulation of thrombus formation HOIP_0040696 HOIP:HOIP_0040697 Any process that activates or increases the frequency, rate or extent of thrombus formation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:33077917 positive regulation of thrombus formation in COVID-19 HOIP_0040697 PMID:32629875 Second, to infect cells, SARS-CoV-2 binds to the cell surface ACE2 receptors, and in so doing compromises the vaso-protective functions of ACE2, an enzyme that attenuates the vasoconstrictive, pro-inflammatory, pro-apoptotic, pro-thrombotic and mitogenic effects of angiotensin II, as discussed in Section 4.2. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0040698 thrombus formation is a subtype of biological structure formation: A process that construcs thrombus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:33077917 thrombus formation in COVID-19 HOIP_0040698 PMID:32629875 Second, to infect cells, SARS-CoV-2 binds to the cell surface ACE2 receptors, and in so doing compromises the vaso-protective functions of ACE2, an enzyme that attenuates the vasoconstrictive, pro-inflammatory, pro-apoptotic, pro-thrombotic and mitogenic effects of angiotensin II, as discussed in Section 4.2. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0040704 A recombinant, soluble glycosylated form of human angiotensin converting enzyme 2 (rhACE2) with antihypertensive and potential antineoplastic activities. Recombinant human angiotensin converting enzyme 2 APN01 may normalize ACE2 levels, cleaving angiotensin II to create angiotensin-(1-7) and restoring the function of the renin-angiotensin system (RAS). ACE2, a homolog of ACE1, appears to function as a negative regulator of the RAS system by converting angiotensin II to angiotensin-(1-7), a peptide with actions that counteract the cardiovascular actions of angiotensin II. In addition, angiotensin-(1-7) may inhibit cyclooxygenase 2 (COX-2) and the production of proinflammatory prostaglandins and may activate the angiotensin-(1-7) G protein-coupled receptor Mas, resulting in diminished tumor cell proliferation. ACE2 levels may be reduced in malignancy and diabetes and in liver, cardiovascular and lung diseases. (https://www.ebi.ac.uk/ols/ontologies/ncit/terms?iri=http%3A%2F%2Fpurl.obolibrary.org%2Fobo%2FNCIT_C85447) PMID:32629875 Recombinant Human Angiotensin Converting Enzyme 2 APN01 HOIP_0040704 PMID:32629875 Consistent with these results, recombinant human ACE2 protected primary human endothelial cells from death induced by angiotensin II, and stimulation of endogenous ACE2 in human coronary arterial endothelial cells inhibited NF-kB signaling and reduced TNFα activity. Table 2. Investigational treatments with potential impact on vascular manifestations of COVID-19. Recombinant human ACE2, the cell entry receptor of SARS-CoV-2, has been shown to competitively neutralize SARS-CoV-2 infection of cells, including endothelial cells in vitro. Currently, recombinant human ACE2 is being tested in initial trials (Table 2). HOIP:HOIP_0040706 Increasing VEGF level is a subtype of increasing quantity: A process that changes the amount of VEGF level to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33077917 Increasing VEGF level (very high) in severe COVID-19 HOIP_0040706 PMID:32629875 In addition, by promoting VEGF-A secretion from various cell types, IL-6 induces vascular hyper-permeability and sprouting angiogenesis. Thus, IL-6 can promote a pro-coagulant and pro-thrombotic vascular pathology, raising the possibility that an abnormally high level of IL-6 may contribute to the vascular phenotype in severe COVID-19. PMID:33077917 The recruited platelets release VEGF, which amplifies the expression of TF by endothelial cells, further stimulating the coagulation cascade. HOIP:HOIP_0040707 Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon signaling pathway. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33188364 negative regulation of type I interferon signaling pathway in the early stage (very high) in severe COVID-19 HOIP_0040707 PMID:33188364 In addition, an integrated analysis showed that patients with severe COVID-19 have a highly impaired interferon type I response with low IFNα activity in the blood, indicating high blood viral load, and an impaired inflammatory response. HOIP:HOIP_0040709 Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. PMID:32629875 negative regulation of cell death in COVID-19 drug treatment HOIP_0040709 PMID:32629875 Consistent with these results, recombinant human ACE2 protected primary human endothelial cells from death induced by angiotensin II, and stimulation of endogenous ACE2 in human coronary arterial endothelial cells inhibited NF-kB signaling and reduced TNFα activity. HOIP:HOIP_0040714 A role played by the entity which that neutralizes the TNF-alpha by binding specifically to it. TNF-alpha antibody HOIP_0040714 HOIP:HOIP_0040716 An inhibitor of IL-1 (interleukin 1), cytokines that plays a central role in the regulation of immune and inflammatory responses to infections or sterile insults. IL-1 inhibitor HOIP_0040716 HOIP:HOIP_0040718 A humanized monoclonal antibody directed against the pro-inflammatory cytokine interleukin-6 (IL-6), with potential immunomodulating and anti-inflammatory activities. Upon administration, olokizumab targets, binds to and blocks the activity of IL-6, which may inhibit the binding of IL-6 to its receptor interleukin-6 receptor (IL-6R). This may inhibit the IL-6/IL-6R-mediated signal transduction pathway and the associated inflammatory response. (https://www.ebi.ac.uk/ols/ontologies/ncit/terms?iri=http%3A%2F%2Fpurl.obolibrary.org%2Fobo%2FNCIT_C172654) CAS:1007223-17-7 Olokizumab HOIP_0040718 HOIP:HOIP_0040724 Reduced oxygenation of body tissues resulting in the decreased pressure of this component of body gases; commonly due to hypoxemia This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 PMID:33214651 hypoxia (very high) in COVID-19 associated with ARDS HOIP_0040724 PMID:33077917 Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection. PMID:33214651 Thrombocytopenia in some patients with COVID-19 might be due to decreased platelet production in the lungs caused by ARDS and hypoxia during coronavirus infections. HOIP:HOIP_0040725 Tissue damage in lung is a subtype of tissue damage: A process that injuries the structure of the tissue in lung as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33123165 Tissue damage in lung (severe)in COVID-19 associated with ARDS HOIP_0040725 PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. HOIP:HOIP_0040729 A pulmonary infiltrate is a substance denser than air, such as pus, blood, or protein, which lingers within the parenchyma of the lungs. Pulmonary infiltrates are associated with pneumonia, and tuberculosis. (https://en.wikipedia.org/wiki/Pulmonary_infiltrate) This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32412710 pulmonary infiltrates in COVID-19 associated with ARDS HOIP_0040729 PMID:32412710 Progressive respiratory failure develops in many patients with severe Covid-19 soon after the onset of dyspnea and hypoxemia. These patients commonly meet the criteria for the acute respiratory distress syndrome (ARDS), which is defined as the acute onset of bilateral infiltrates, severe hypoxemia, and lung edema that is not fully explained by cardiac failure or fluid overload. HOIP:HOIP_0040732 A role played by the entity which that neutralizes the VEGF by binding specifically to it. VEGF antibody HOIP_0040732 HOIP:HOIP_0040734 A humanized monoclonal antibody directed against the Angiopoietin-2 (Ang2). Zansecimab LY3127804 HOIP_0040734 HOIP:HOIP_0040735 A role played by the entity which that neutralizes the Ang2 (angiopoietin-2) by binding specifically to it. Ang2 antibody HOIP_0040735 HOIP:HOIP_0040737 Increasing angiopoietin-2 concentration in blood is a subtype of increasing concentration: A process that changes the angiopoietin-2 concentration in the blood to be higher. increasing angiopoietin-2 concentration in blood HOIP_0040737 HOIP:HOIP_0040741 Increasing angiopoietin-2 concentration in blood is a subtype of increasing concentration: A process that changes the angiopoietin-2 concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 increasing angiopoietin-2 concentration in blood (very high) in severe COVID-19 HOIP_0040741 PMID:32629875 The rationale for this approach is that circulating levels of angiopoietin-2 (ANG2) are abnormally elevated in severe COVID-19 patients. This is consistent with the observation that inflammatory signals induce the rapid release of ANG2 from endothelial cells, particularly in the presence of TNFα, and that ANG2 inhibitors can reduce vessel inflammation. HOIP:HOIP_0040742 Dysregulation of matrix metallopeptidase secretion is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of matrix metallopeptidase secretion process appropriately or cannot realize it at all. dysregulation of matrix metalloproteinase secretion HOIP_0040742 HOIP:HOIP_0040743 Dysregulation of matrix metallopeptidase secretion is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of matrix metallopeptidase secretion process appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32422178 dysregulation of matrix metalloproteinase secretion in COVID-19 associated with ARDS HOIP_0040743 PMID:32422178 Multiple aberrant host pathways interconnect to result in pulmonary fibrosis in a subset of individuals who develop ARDS. Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. HOIP:HOIP_0040744 The expansion of a neutrophile population by cell division. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32843733 neutrophile proliferation (very high) in COVID-19 associated with ARDS HOIP_0040744 PMID:32843733 In line with observations in lethal cases of SARS and MERS, patients infected with SARS-CoV-2 show increased numbers of neutrophils and macrophages in their airways and blood. HOIP:HOIP_0040747 Negative regulation of platelet maturation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of platelet maturation. negative regulation of platelet maturation HOIP_0040747 HOIP:HOIP_0040748 Negative regulation of platelet maturation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of platelet maturation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33214651 negative regulation of platelet maturation in COVID-19 associated with ARDS HOIP_0040748 PMID:33214651 Thrombocytopenia in some patients with COVID-19 might be due to decreased platelet production in the lungs caused by ARDS and hypoxia during coronavirus infections. HOIP:HOIP_0040749 Decrease in platelet count is a subtype of decreasing number of objects: A process that becomes smaller in platelet count. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33214651 thrombocytopenia decrease in platelet count in COVID-19 associated with ARDS HOIP_0040749 PMID:33214651 Thrombocytopenia in some patients with COVID-19 might be due to decreased platelet production in the lungs caused by ARDS and hypoxia during coronavirus infections. HOIP:HOIP_0040751 Inflammatory response in lung is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammation in lung inflammatory response in lung HOIP_0040751 HOIP:HOIP_0040752 Endothelium damage in lung is a subtype of endothelium damage: A process that injuries the structure of the endothelium in lung as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 with ARDS. PMID:32422178 PMID:32629875 PMID:32651579 PMID:33077917 Wikipedia:Endothelium-derived_relaxing_factor endothelium damage in lung in COVID-19 associated with ARDS HOIP_0040752 PMID:32422178 Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. PMID:32629875 A comprehensive post-mortem analysis of multiple tissues (in 3 COVID-19 cases) described congestion and endotheliitis of small vessels with accumulation of mononuclear/lymphocytic cells around the capillary endothelium in the heart, small bowel, kidney, liver and lung; in one case, caspase 3-immunostaining revealed the presence of apoptotic bodies in endothelial cells lining the inner wall of inflamed blood vessels. PMID:32651579 Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. Wikipedia:Endothelium-derived_relaxing_factor Endothelium produces NO which then diffuses to the vascular smooth muscle tissue, although there seems to be evidence that vasodilation may also be of neuronal origin, rather than endothelial. NO is produced by the enzyme nitric oxide synthase and it relaxes smooth muscle tissue by promoting the synthesis of cGMP. HOIP:HOIP_0040755 Pulmonary blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform pulmonary blood vessel function correctly or not functioning at all. pulmonary blood vessel dysfunction HOIP_0040755 HOIP:HOIP_0040756 Pulmonary blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform pulmonary blood vessel function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32422178 pulmonary blood vessel dysfunction in COVID-19 associated with ARDS HOIP_0040756 PMID:32422178 Canonical profibrotic pathways regulated by TGF-beta are important, and there is evidence that vascular dysfunction is a key component of the switch from ARDS to fibrosis, with VEGF and cytokines such as IL-6 and TNFalpha implicated. Subsequent studies have found that exogenously administered as well as endogenously produced interferon might induce pulmonary vasculopathy, and this finding is important given that pulmonary vascular disease could play an important role in severe COVID-19 disease. HOIP:HOIP_0040757 interferon-gamma production The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32422178 interferon-gamma production (severe)in severe COVID-19 HOIP_0040757 PMID:32422178 Indeed, circulating IFN-gamma and CXCL10 concentrations are raised in patients with severe COVID-19. HOIP:HOIP_0040758 JNK signaling is a process that a signal is transmitted by the JNK (a stress-activated protein kinase (SAPK) ). This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32422178 Wikipedia:c-Jun_N-terminal_kinases JNK signaling in COVID-19 HOIP_0040758 PMID:32422178 Furthermore, JNK family inhibition impairs synthesis of H5N1 viral RNA, and SARS-CoV-2 has been shown to stimulate pro-inflammatory pathways via JNK signalling pathways. Wikipedia:c-Jun_N-terminal_kinases Inflammatory signals, changes in levels of reactive oxygen species, ultraviolet radiation, protein synthesis inhibitors, and a variety of stress stimuli can activate JNK. JNK1 is involved in apoptosis, neurodegeneration, cell differentiation and proliferation, inflammatory conditions and cytokine production mediated by AP-1 (activation protein 1) such as RANTES, IL-8 and GM-CSF. HOIP:HOIP_0040759 The extension of new blood vessels from existing vessels into avascular tissues, this process includes the specialization of endothelial cells into leading tip and stalk cells, proliferation and migration of the endothelial cells and cell adhesion resulting in angiogenic sprout fusion or lumen formation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 sprouting angiogenesis in COVID-19 associated with ARDS HOIP_0040759 PMID:32629875 Another autopsy series on 67 COVID-19 cases described the presence of vascular microthrombi in multiple organs, particularly in the lungs (in 23/25 cases) where it was associated with capillary sprouting and capillary inflammation, and in the brain (in 6/20 cases) where it was associated with evidence of patchy acute infarcts. As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. The pulmonary capillary vessels of COVID-19 tissues contained microthrombi and evidence of intravascular (intussusceptive) neovascularization, which were more frequent than observed in the influenza cases. In addition, by promoting VEGF-A secretion from various cell types, IL-6 induces vascular hyper-permeability and sprouting angiogenesis. HOIP:HOIP_0040760 Loss of vessel barrier integrity is a subtype of loss of function (process): A process that results in no longer having a loss of vessel barrier integrity function or the process that gradually loses it. loss of vessel barrier integrity HOIP_0040760 HOIP:HOIP_0040762 Loss of vessel barrier integrity in lung is a subtype of loss of function (process): A process that results in no longer having a loss of vessel barrier integrity function or the process in lung that gradually loses it. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 loss of vessel barrier integrity in lung in COVID-19 associated with ARDS HOIP_0040762 PMID:33077917 Mounting evidence suggests that loss of vessel barrier integrity and the development of a pro-coagulative endothelium contributes to the initiation and propagation of ARDS in COVID-19, by inducing endotheliitis and mediating inflammatory cell infiltration in the lungs. Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0040763 Detaching of blood clot is a subtype of detaching: A process of a blood clot detaching from the area of the blood stream where it coagulated and grew to obstruct the vessel. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 detaching of blood clot in COVID-19 associated with ARDS HOIP_0040763 PMID:32629875 An autopsy series showed the presence of deep venous thrombosis involving the lower extremities bilaterally in 56% (7/12) of cases, associated with massive pulmonary embolism in four of these cases, which was listed as the cause of death. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. A systematic search for pulmonary emboli in 26 COVID-19 patients on mechanical ventilation showed that they were detected in 23% (6/26) of patients, and venous thromboembolism (VTE) was detected in 69% (18/26). Results of 12 consecutive complete autopsies of patients with COVID-19 concluded that massive pulmonary embolism was the cause of death in 4/12 cases and that VTE was present in 7/12 (58%) patients. HOIP:HOIP_0040764 TF production is a subtype of protein production: A process that makes existent of a TF (Tissue Factor) protein due to biosynthesis or secretion resulting in an increase in its levels. TF production HOIP_0040764 HOIP:HOIP_0040766 The adhesion of one platelet to one or more other platelets via adhesion molecules. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 platelet aggregation (very high) in COVID-19 associated with ARDS HOIP_0040766 PMID:32629875 Similarly, thrombi/platelet aggregates were visualized microscopically in capillaries, arterioles and medium sized arteries of most COVID-19 lungs (21/23). HOIP:HOIP_0040767 TF production is a subtype of protein production: A process that makes existent of a TF (Tissue Factor) protein due to biosynthesis or secretion resulting in an increase in its levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 tissue factor production in COVID-19 HOIP_0040767 PMID:33077917 The recruited platelets release VEGF, which amplifies the expression of TF by endothelial cells, further stimulating the coagulation cascade. The expression of tissue factor (TF) by activated monocytes stimulates the coagulation cascade and the subsequent generation of thrombin; these processes are ineffectually counterbalanced by tissue factor pathway inhibitor (TFPI), which is present in plasma and platelets, and produced mainly by endothelial cells. HOIP:HOIP_0040768 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot in lung; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 blood coagulation in lung (very high)in COVID-19 associated with ARDS HOIP_0040768 PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0040769 Endothelium malfunction in lung is a subtype of endothelium malfunction: A process that does not perform endothelium function in lung correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). Wikipedia:Endothelium endothelium dysfunction in lung in COVID-19 associated with ARDS HOIP_0040769 Wikipedia:Endothelium The endothelium normally provides a surface on which blood does not clot, because it contains and expresses substances that prevent clotting, including heparan sulfate which acts as a cofactor for activating antithrombin, a protease that inactivates several factors in the coagulation cascade. HOIP:HOIP_0040770 Inflammatory cell infiltration into lung is a subtype of inflammatory cell infiltration: A process that moves the outside inflammatory cell to the inside of lung in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 PMID:33123165 inflammatory cell infiltration into lung (very high) in COVID-19 associated with ARDS HOIP_0040770 PMID:33077917 Mounting evidence suggests that loss of vessel barrier integrity and the development of a pro-coagulative endothelium contributes to the initiation and propagation of ARDS in COVID-19, by inducing endotheliitis and mediating inflammatory cell infiltration in the lungs. PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. HOIP:HOIP_0040771 Negative regulation of nitric oxide synthase activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of nitric oxide synthase activation. Negative regulation of nitric oxide synthase activation HOIP_0040771 HOIP:HOIP_0040772 Negative regulation of nitric oxide synthase activation is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of nitric oxide synthase activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 Wikipedia:Endothelium-derived_relaxing_factor Negative regulation of nitric oxide synthase activation in COVID-19 associated with ARDS HOIP_0040772 PMID:33077917 Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection. Wikipedia:Endothelium-derived_relaxing_factor Endothelium produces NO which then diffuses to the vascular smooth muscle tissue, although there seems to be evidence that vasodilation may also be of neuronal origin, rather than endothelial. NO is produced by the enzyme nitric oxide synthase and it relaxes smooth muscle tissue by promoting the synthesis of cGMP. HOIP:HOIP_0040773 Decreasing NO level is a subtype of decreasing quantity: A process that changes the amount of NO (nitric oxide) level to be lower. Decreasing NO level HOIP_0040773 HOIP:HOIP_0040774 Decreasing NO level is a subtype of decreasing quantity: A process that changes the amount of NO (nitric oxide) level to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 Decreasing NO level in COVID-19 associated with ARDS HOIP_0040774 PMID:33077917 Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection. HOIP:HOIP_0040775 Increasing VEGF level is a subtype of increasing quantity: A process that changes the amount of VEGF level to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 Increasing VEGF level (very high) in COVID-19 associated with ARDS HOIP_0040775 PMID:33077917 Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection. The recruited platelets release VEGF, which amplifies the expression of TF by endothelial cells, further stimulating the coagulation cascade. HOIP:HOIP_0040778 Negative regulation of complement activation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of complement activation. Negative regulation of complement activation HOIP_0040778 HOIP:HOIP_0040779 Negative regulation of complement activation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of complement activation. PMID:33077917 Negative regulation of complement activation in COVID-19 drug treatment HOIP_0040779 PMID:33077917 A case report of a patient with COVID-19-associated ARDS and pneumonia showed that treatment with a C3 inhibitor was safe and associated with a favourable course, suggesting that C3 blockade may have broad anti-inflammatory potential owing to the upstream positioning of C3 in innate immune cascade signalling. HOIP:HOIP_0040780 Positive regulation of complement component gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of complement component gene expression. positive regulation of complement component gene expression HOIP_0040780 HOIP:HOIP_0040781 Positive regulation of complement component gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of complement component gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 positive regulation of complement component gene expression in COVID-19 associated with ARDS HOIP_0040781 PMID:33077917 In line with these findings, immunohistochemistry analyses in post-mortem lung tissue from SARS-CoV-2-infected patients revealed high expression of the complement components MBL, C4, C3 and C5b–9, in alveolar epithelial cells and pneumocytes, as well as in inflammatory cells, as reported by a preprint study. HOIP:HOIP_0040784 Detaching of blood clot is a subtype of detaching: A process of a blood clot detaching from the area of the blood stream where it coagulated and grew to obstruct the vessel. This entity is a specific course-dependent process. This process can constitute the course of pulmonary embolism. detaching of blood clot [pulmonary embolism course] HOIP_0040784 HOIP:HOIP_0040785 Moving blood clot is a subtype of moving. A process that change the location of the blood clot. . moving blood clot HOIP_0040785 HOIP:HOIP_0040786 Lung damage is a subtype of damaging: A process that injuries the structure of the lung as the direct or indirect result of an external force. lung damage HOIP_0040786 HOIP:HOIP_0040787 Lung damage is a subtype of damaging: A process that injuries the structure of the lung as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 lung damage in COVID-19 associated with ARDS HOIP_0040787 PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. A new study has also indicated that neutrophil activation and the formation of neutrophil extracellular traps (NETs) may have a prominent role in propagating the severe cytokine release observed in severe cases of COVID-19, representing a previously unrecognized, but powerful innate defence response that may exacerbate lung damage in affected patients. HOIP:HOIP_0040791 The expansion of a macrophage population by cell division. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32843733 tissue-resident macrophage proliferation in severe COVID-19 HOIP_0040791 PMID:32843733 In line with observations in lethal cases of SARS and MERS, patients infected with SARS-CoV-2 show increased numbers of neutrophils and macrophages in their airways and blood. HOIP:HOIP_0040793 Kidney Ischemia is a changing process to lack enough to blood supply of kidney. kidney Ischemia HOIP_0040793 HOIP:HOIP_0040794 Protein leakage into urine is a subtype of leaking: A process that leaks the protein leakage into urine from the kidney filters. protein leakage into urine HOIP_0040794 HOIP:HOIP_0040795 Blood leakage into urine is a subtype of leaking: A process that leaks the blood (or red blood cells) leakage into urine. blood leakage into urine HOIP_0040795 HOIP:HOIP_0040796 Thrombus formation in brain is a subtype of thrombus formation: A process that construcs thrombus in brain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 PMID:32651579 cerebral thrombus formation in COVID-19 associated with cerebral infarction HOIP_0040796 PMID:32629875 Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32651579 Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. HOIP:HOIP_0040797 Kidney damage is a subtype of damaging: A process that injuries the structure of the kidney as the direct or indirect result of an external force. kidney damage HOIP_0040797 HOIP:HOIP_0040798 Glomerular damage is a subtype of organ damaging: A process that injuries the structure of the glomerular as the direct or indirect result of an external force. glomerular impairment glomerular damage HOIP_0040798 HOIP:HOIP_0040802 Narrowing of the brain artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the cerebral arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 PMID:32651579 brain artery narrowing in COVID-19 associated with cerebral infarction HOIP_0040802 PMID:32629875 Another autopsy series on 67 COVID-19 cases described the presence of vascular microthrombi in multiple organs, particularly in the lungs (in 23/25 cases) where it was associated with capillary sprouting and capillary inflammation, and in the brain (in 6/20 cases) where it was associated with evidence of patchy acute infarcts. In a retrospective single-center study in Brescia, Italy, among neurological patients admitted in March, those diagnosed with COVID-19 (56 patients) were significantly more likely to have been admitted for stroke and transient ischemic attack (TIA) than those without the diagnosis of COVID-19 (117 patients), perhaps in part because the COVID-19 patients were older. PMID:32651579 There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. HOIP:HOIP_0040803 Kidney damage is a subtype of damaging: A process that injuries the structure of the kidney as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. kidney injury kidney damage in COVID-19 in renal system HOIP_0040803 HOIP:HOIP_0040804 Glomerular filtration malfunction is a subtype of malfunction: A process that does not perform glomerular filtration function correctly or not functioning at all. glomerular filtration malfunction HOIP_0040804 HOIP:HOIP_0040807 A glomerular visceral epithelial cell is a specialized kidney epithelial cell that contains "feet" that interdigitate with the "feet" of other glomerular epithelial cells. podocyte glomerular visceral epithelial cell HOIP_0040807 HOIP:HOIP_0040808 Glomerular visceral epithelial cell injury is a subtype of cellular damage: A process that injuries the structure of the glomerular visceral epithelial cell. glomerular visceral epithelial cell injury HOIP_0040808 HOIP:HOIP_0040809 Brain microvascular dysfunction is a subtype of organ malfunction: A process that does not perform microvascular function correctly or not functioning at all in the brain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. bain microvascular dysfunction in COVID-19 in nervous system HOIP_0040809 HOIP:HOIP_0040811 A type of brain cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 brain cell necrosis in COVID-19 associated with cerebral infarction HOIP_0040811 PMID:32629875 Oxley et al. reported on a small case series of five 33 to 50-year-old patients who presented with ischemic stroke during a two-week period (from March 23 to April 7, 2020) in a single center in New York City, and who were subsequently diagnosed with SARS-CoV-2 infection. In addition, 6/20 cases showed widespread microthrombi associated with evidence of patchy ischemic infarcts. Furthermore, histological examination of 20 brains from COVID-19 autopsies revealed the presence of anoxic brain injury in two patients with the clinical diagnosis of stroke. HOIP:HOIP_0040812 Inreasing urine albumin concentration is a subtype of increasing concentration: A process that changes the albumin concentration in the urine to be higher. inreasing urine albumin concentration HOIP_0040812 HOIP:HOIP_0040813 Brain Ischemia is a changing process to lack enough to blood supply of brain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 brain ischemia in COVID-19 associated with cerebral infarction HOIP_0040813 PMID:32629875 Oxley et al. reported on a small case series of five 33 to 50-year-old patients who presented with ischemic stroke during a two-week period (from March 23 to April 7, 2020) in a single center in New York City, and who were subsequently diagnosed with SARS-CoV-2 infection. In a retrospective single-center study in Brescia, Italy, among neurological patients admitted in March, those diagnosed with COVID-19 (56 patients) were significantly more likely to have been admitted for stroke and transient ischemic attack (TIA) than those without the diagnosis of COVID-19 (117 patients), perhaps in part because the COVID-19 patients were older. HOIP:HOIP_0040815 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of myocardium. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32651579 viral entry into host cell in myocardium in COVID-19 associated with myocarditis SARS-CoV-2 entry to host cell in COVID-19 associated with myocarditis HOIP_0040815 PMID:32651579 ACE2 has high expression in cardiovascular tissue, including cardiac myocytes, fibroblasts, endothelial cells, and smooth-muscle cells in support of a possible mechanism of direct viral injury. Myocarditis is a presumed etiology of cardiac dysfunction, and the development of myocarditis may relate to viral load. While isolation of the virus from myocardial tissue has been reported in a few autopsy studies, other pathological reports have described inflammatory infiltrates without myocardial evidence of SARS-CoV-2. HOIP:HOIP_0040816 Any biological process that results in permanent cessation of all vital functions of an endothelial cell in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 PMID:32697943 PMID:33077917 endothelial necrosis in lung in COVID-19 associated with ARDS HOIP_0040816 PMID:32629875 In addition to laboratory evidence that SARS-CoV-2 infects endothelial cells and that loss of endothelial ACE2 as a consequence of coronavirus infection confers a pro-inflammatory, pro-coagulant, and pro-apoptotic phenotype to endothelial cells, there is now emerging evidence of vascular pathology in most patients with severe COVID-19 (Figure 1). Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32697943 HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Finally, we demonstrate that CoV-2-infected monocytes promote T cell dysfunction and lung epithelial cell death. This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. Finally, we demonstrate that CoV-2-infected monocytes promote T cell dysfunction and lung epithelial cell death. These data may explain why uncontrolled diabetes may lead to compromised adaptive immune response and lung dysfunction in patients with severe COVID-19 symptoms. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0040817 Hardening of glomeruli in kidney is a subtype of changing hardness: A process that changes the hardness of the glomeruli in the kidney to become hard due to the replacement of normal glomeruli to scar tissue. hardening of glomeruli in kidney HOIP_0040817 HOIP:HOIP_0040818 Glomerulosclerosis dependent process is a subtype of course dependent process: A process that can constitute the course of glomerulosclerosis. glomerulosclerosis dependent process HOIP_0040818 HOIP:HOIP_0040820 Hardening of glomeruli in kidney is a subtype of changing hardness: A process that changes the hardness of the glomeruli in the kidney to become hard due to the replacement of normal glomeruli to scar tissue. This entity is a specific course-dependent process. This process can constitute the course of glomerulosclerosis. hardening of glomeruli in kidney [glomerulosclerosis] HOIP_0040820 HOIP:HOIP_0040821 Decreasing brain blood flow is a subtype of decreasing flow: A process that changes the amount of brain blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 decreasing brain blood flow in COVID-19 associated with cerebral infarction HOIP_0040821 PMID:32629875 In a retrospective single-center study in Brescia, Italy, among neurological patients admitted in March, those diagnosed with COVID-19 (56 patients) were significantly more likely to have been admitted for stroke and transient ischemic attack (TIA) than those without the diagnosis of COVID-19 (117 patients), perhaps in part because the COVID-19 patients were older. HOIP:HOIP_0040822 Glomerular capillary homeostasis imbalance is a subtype of homeostasis imbalance: A process that becomes lacking a glomerular capillary homeostastasis balance. glomerular capillary homeostasis imbalance HOIP_0040822 HOIP:HOIP_0040823 Brain vasculature damage is a subtype of damaging: A process that injures the structure of the brain vasculature as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32629875 PMID:32651579 brain vasculature damage in COVID-19 in nervous system HOIP_0040823 PMID:32629875 Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32651579 Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. HOIP:HOIP_0040824 Thrombus formation in kidney is a subtype of thrombus formation: A process that construcs thrombus in kidney. thrombus formation in kidney HOIP_0040824 HOIP:HOIP_0040825 Brain blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform brain blood vessel function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32629875 brain blood vessel disorder in COVID-19 in nervous system HOIP_0040825 PMID:32629875 COVID-19, however, appears to include an evolving set of clinical manifestation not previously reported in SARS and MERS, including stroke and cardiomyopathies associated with coagulopathy and vasculopathy, which can cause sudden death and other serious morbidities. In a subsequent prospective series over the following month involving a group of New York City Hospitals, the age range of ten SARS-CoV-2-infected patients presenting with stroke had broadened to include patients 27 to 75 years old. In addition, a retrospective analysis on 214 patients hospitalized with COVID-19 in Wuhan found that acute cerebrovascular disease was present in one of 126 patients with non-severe COVID-19 and in five of 88 patients with severe COVID-19. HOIP:HOIP_0040827 The expansion of a macrophage population by cell division. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32843733 macrophage proliferation in COVID-19 associated with ARDS HOIP_0040827 PMID:32843733 In line with observations in lethal cases of SARS and MERS, patients infected with SARS-CoV-2 show increased numbers of neutrophils and macrophages in their airways and blood. HOIP:HOIP_0040828 Microthrombus formation in brain is a subtype of microthrombus formation: A process that construcs microthrombus. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. Wikipedia:Cerebral_infarction Microthrombus formation in brain [brain infarction course] HOIP_0040828 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0040829 Albumin leakage into urine is a subtype of leaking: A process that leaks the albumin leakage into urine from the kidney filters. albumin leakage into urine HOIP_0040829 HOIP:HOIP_0040830 Anoxic brain damage is a subtype of brain damage: A process that injuries the structure of the brain as the direct or indirect result of anoxia. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 anoxic brain injury anoxic brain damage in COVID-19 associated with cerebral infarction HOIP_0040830 PMID:32629875 Furthermore, histological examination of 20 brains from COVID-19 autopsies revealed the presence of anoxic brain injury in two patients with the clinical diagnosis of stroke. HOIP:HOIP_0040831 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 establishment of virus infection in COVID-19 in patient with diabetes HOIP_0040831 PMID:32694793 In people with T2D, ACE2 expression is elevated in multiple target tissues of SARS-CoV-2, and this elevation has been proposed to be an adaptive mechanism that protects the body against diabetes-associated physiological dysfunction. This increased expression may enhance SARS-CoV-2’s entry and subsequent replication, as well as its spread within the body in individuals with T2D. HOIP:HOIP_0040832 Family of globular proteins, the most common of which are the serum albumins. All the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. This process can constitute the course of COVID-19. albumin type (human) in COVID-19 HOIP_0040832 HOIP:HOIP_0040833 Increasing vascular permeabilization is a subtype of changing permeability: A process that changes the permeability of the vascular to be higher. Wikipedia:Inflammation increasing vascular permeabilization HOIP_0040833 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0040834 Proximal convoluted tubule brush border damage is a subtype of organ damaging: A process that injuries the structure of the proximal convoluted tubule brush border as the direct or indirect result of an external force. renal brush border damage proximal convoluted tubule brush border damage HOIP_0040834 HOIP:HOIP_0040835 Heart damage is a subtype of damaging: A process that injuries the structure of the heart as the direct or indirect result of an external force. cardiac damage cardiac injury heart damage HOIP_0040835 HOIP:HOIP_0040836 Vacuolar degeneration is a subtype of changing material: A process that degenerates vacuole. vacuolar degeneration HOIP_0040836 HOIP:HOIP_0040837 Edema in white matter of occipital lobe is a subtype of edema: A process that keeps an excessive fluid in cells or intercellular tissues of white matter of occipital lobe. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 edema (process) in white matter of occipital lobe in COVID-19 in nervous system HOIP_0040837 PMID:32651579 In addition, meningoencephalitis, hemorrhagic posterior reversible encephalopathy syndrome, and acute necrotizing encephalopathy, including the brainstem and basal ganglia, have been described in case reports. HOIP:HOIP_0040838 Increasing vascular permeabilization is a subtype of changing permeability: A process that changes the permeability of the vascular to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 Wikipedia:Inflammation increasing vascular permeabilization in COVID-19 HOIP_0040838 PMID:33077917 Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0040839 A type of nephron tubule epithelial cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. nephron tubule epithelial cell necrosis HOIP_0040839 HOIP:HOIP_0040840 Myocardial damage is a subtype of damaging: A process that injuries the structure of the myocardial muscle as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32629875 PMID:32651579 myocardial damage in COVID-19 associated with ACS HOIP_0040840 PMID:32629875 Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. PMID:32651579 Systemic inflammatory response syndrome (cytokine storm) is another putative mechanism of myocardial injury. HOIP:HOIP_0040841 Inflammatory response in meninx is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 inflammatory response in meninx (very high) in COVID-19 in nervous system HOIP_0040841 PMID:32651579 In addition, meningoencephalitis, hemorrhagic posterior reversible encephalopathy syndrome, and acute necrotizing encephalopathy, including the brainstem and basal ganglia, have been described in case reports. HOIP:HOIP_0040842 Myelin sheath damage is a subtype of damaging: A process that injuries the structure of the myelin sheath as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 myelin sheath damage in COVID-19 in nervous system HOIP_0040842 PMID:32651579 Acute inflammatory demyelinating polyneuropathy (Guillain-Barré syndrome) has also been reported in some patients. HOIP:HOIP_0040843 Myocardium malfunction is a subtype of malfunctioning process: A process that cannot perform signaling [biological] appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32629875 PMID:32651579 Myocardium malfunction in COVID-19 associated with ACS HOIP_0040843 PMID:32629875 COVID-19, however, appears to include an evolving set of clinical manifestation not previously reported in SARS and MERS, including stroke and cardiomyopathies associated with coagulopathy and vasculopathy, which can cause sudden death and other serious morbidities. However, cardiovascular disease is prevalent in patients with COVID-19; 7% of all patients and 22 % of severe cases experienced myocardial injury. Cases of cardiomyopathy have been reported in patients with COVID-19, raising the possibility that myocarditis-related cardiac events may be increased in COVID-19. Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. In one study, atrial arrhythmias were commonly detected in patients with severe COVID-19. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Biventricular cardiomyopathy has been reported in 7–33% of critically ill patients with COVID-19. HOIP:HOIP_0040844 The directed movement of a virus, or part of a virus into central nervous system. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 transport of virus into central nervous system (very high) in COVID-19 in nervous system HOIP_0040844 PMID:32651579 Direct viral invasion of neural parenchyma is a possibility; SARS-CoV-2 may access the central nervous system via the nasal mucosa, lamina cribrosa, and olfactory bulb or via retrograde axonal transport. HOIP:HOIP_0040845 The directed movement of a virus, or part of a virus into central nervous system via retrograde axonal transport. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 transport of virus into central nervous system via retrograde axonal transpor (very high) in COVID-19 in nervous system HOIP_0040845 PMID:32651579 Direct viral invasion of neural parenchyma is a possibility; SARS-CoV-2 may access the central nervous system via the nasal mucosa, lamina cribrosa, and olfactory bulb or via retrograde axonal transport. HOIP:HOIP_0040847 Blood brain barrier damage is a subtype of damaging: A process that injuries the structure of the blood brain barrier as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 Wikipedia:Posterior_reversible_encephalopathy_syndrome blood brain barrier damage in COVID-19 in nervous system HOIP_0040847 PMID:32651579 Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. Wikipedia:Posterior_reversible_encephalopathy_syndrome While the precise mechanism is PRES is not fully understood, it is considered to be related to a problem with the blood vessels of the brain. There are several theories as to why these blood vessels may become inappropriately permeable and allow the surrounding brain tissue to become swollen. The excessive pressure damages the endothelial layer and the blood-brain barrier, leading to swelling (edema). There appears to be a role of cytokines in causing endothelial dysfunction. HOIP:HOIP_0040848 Increasing troponin concentration is a subtype of increasing concentration: A process that changes the troponin concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of myocarditis. Increasing troponin concentration [myocarditis course] HOIP_0040848 HOIP:HOIP_0040849 Cell killing caused by the membrane attack complex formed following complement activation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 complement-dependent cytotoxicity (very high) in severe COVID-19 HOIP_0040849 PMID:33077917 C3b also forms C5 convertase, which induces release of the potent anaphylatoxin C5a, as well as the fragment C5b that is responsible for the formation of the membrane attack complex C5b–9 on target cells — the terminal event of complement activation. HOIP:HOIP_0040851 Cell killing in kidney caused by the membrane attack complex formed following complement activation. complement-dependent cytotoxicity in kidney HOIP_0040851 HOIP:HOIP_0040852 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 cytokine storm in COVID-19 in nervous system HOIP_0040852 PMID:32651579 Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. HOIP:HOIP_0040853 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of kidney. The process ends when the viral nucleic acid is released into the host cell cytoplasm. viral entry into host cell in kidney HOIP_0040853 HOIP:HOIP_0040854 Interacting selectively and non-covalently with a receptor on the host cell surface of myocardium. host cell surface receptor binding in myocardium HOIP_0040854 HOIP:HOIP_0040856 Endothelium inflammatory response in lung is a subtype of inflammatory response in endothelium: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 PMID:32651579 PMID:33077917 PMID:32422178 PMID:32422178 endothelium inflammatory response in lung in COVID-19 associated with ARDS HOIP_0040856 PMID:32629875 Another autopsy series on 67 COVID-19 cases described the presence of vascular microthrombi in multiple organs, particularly in the lungs (in 23/25 cases) where it was associated with capillary sprouting and capillary inflammation, and in the brain (in 6/20 cases) where it was associated with evidence of patchy acute infarcts. As expected from vascular pathology that includes inflammation, congestion, thrombosis, hemorrhage and endothelial cell death, the surrounding hypoxic tissues had evidence of interstitial edema, damage, destruction, inflammation, fibrosis and vascular regeneration. Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. PMID:32651579 Infection-mediated endothelial injury (characterized by elevated levels of von Willebrand factor) and endothelialitis (marked by the presence of activated neutrophils and macrophages), found in multiple vascular beds (including the lungs, kidney, heart, small intestine, and liver) in patients with COVID-19, can trigger excessive thrombin production, inhibit fibrinolysis, and activate complement pathways, initiating thromboinflammation and ultimately leading to microthrombi deposition and microvascular dysfunction. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. PMID:32422178 Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. HOIP:HOIP_0040858 The totality of all processes through which COVID-19 infection with cerebral infarction is realized. COVID-19 course associated with cerebral infarction HOIP_0040858 HOIP:HOIP_0040859 Systemic inflammatory response is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. Systemic inflammatory response HOIP_0040859 HOIP:HOIP_0040860 Malfunctioning of cognitive function is a subtype of malfunctioning process: A process that cannot perform cognitive function appropriately or cannot realize it at all. malfunctioning of cognitive function HOIP_0040860 HOIP:HOIP_0040861 Malfunctioning of cognitive function is a subtype of malfunctioning process: A process that cannot perform cognitive function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 malfunctioning of cognitive function in COVID-19 associated with cerebral infarction HOIP_0040861 PMID:32629875 Diffuse microthrombi in the brain may underlie cognitive problems, headaches, and other symptoms in patients with COVID-19 even after the apparent resolution of the disease. HOIP:HOIP_0040862 Inreasing blood protein concentration is a subtype of increasing concentration: A process that changes the blood concentration in the urine to be higher. inreasing urine blood concentration HOIP_0040862 HOIP:HOIP_0040863 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32651579 cytokine storm in COVID-19 associated with cerebral infarction HOIP_0040863 PMID:32651579 Other neurological manifestations support, at least, the neurovirulence of COVID-19, perhaps reflecting the proinflammatory and prothrombotic cascade in the wake of cytokine storm as it affects brain vasculature and the blood–brain barrier, especially in the setting of toxic-metabolic sequelae of multi-organ dysfunction often seen in COVID-19-associated critical illness. HOIP:HOIP_0040864 Systemic inflammatory response is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 PMID:33077917 Systemic inflammatory response in COVID-19 in renal system HOIP_0040864 PMID:32416769 The cause of kidney involvement in COVID-19 is likely to be multifactorial, with cardiovascular comorbidity and predisposing factors (eg, sepsis, hypovolaemia, and nephrotoxins) as important contributors. PMID:33077917 Several non-specific mechanisms may contribute to the development of AKI in the setting of COVID-19, including haemodynamic alterations, cardiac dysfunction, hypovolaemia due to poor oral intake or high-grade fever, use of nephrotoxic drugs and nosocomial sepsis. HOIP:HOIP_0040865 Renal cell damage is a subtype of cellular damage: A process that injuries the structure of the renal cell as the direct or indirect result of an external force. renal cell injury renal cell damage HOIP_0040865 HOIP:HOIP_0040866 Glomerular capillary homeostasis imbalance is a subtype of homeostasis imbalance: A process that becomes lacking a glomerular capillary homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 glomerular capillary homeostasis imbalance in COVID-19 in renal system HOIP_0040866 PMID:33077917 Infection of endothelial cells alters glomerular capillary haemostasis and induces the formation of fibrin thrombi. HOIP:HOIP_0040867 Any process that activates or increases the frequency, rate or extent of the inflammatory response in kidney. positive regulation of inflammatory response in kidney HOIP_0040867 HOIP:HOIP_0040868 Dysregulation of heartbeats is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of heartbeats appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of myocarditis. cardiac arrhythmias dysregulation of heartbeats [myocarditis course] HOIP_0040868 HOIP:HOIP_0040870 Brain damage is a subtype of Organ damage: A process that injuries the structure of the brain as the direct or indirect result of an external force. brain damage HOIP_0040870 HOIP:HOIP_0040871 Inflammatory response in kidney is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammation in kidney inflammatory response in kidney HOIP_0040871 HOIP:HOIP_0040873 Brain damage is a subtype of Organ damage: A process that injuries the structure of the brain as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in nervous system. brain damage in COVID-19 in nervous system HOIP_0040873 HOIP:HOIP_0040874 Renal fibrosis is a subtype of fibrosis: A process that replaces renal tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. renal fibrosis process HOIP_0040874 HOIP:HOIP_0040875 Any process that activates or increases the frequency, rate or extent of the inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 PMID:32651579 positive regulation of inflammatory response (very high) in COVID-19 associated with myocarditis HOIP_0040875 PMID:32629875 Consistent with cardiomyopathy, COVID-19 autopsy reports revealed the presence of a few mononuclear cell infiltrates in the myocardium, presumably recruited from the circulation through inflamed capillaries, but no obvious histological changes in the heart tissue. PMID:32651579 Myocarditis is a presumed etiology of cardiac dysfunction, and the development of myocarditis may relate to viral load. HOIP:HOIP_0040876 Brain damage is a subtype of Organ damage: A process that injuries the structure of the brain as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. brain damage in COVID-19 associated with cerebral infarction HOIP_0040876 HOIP:HOIP_0040877 Positive regulation of cell adhesion molecule expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of cell adhesion molecule expression. positive regulation of cell adhesion molecule expression HOIP_0040877 HOIP:HOIP_0040878 Renal fibrosis dependent process is a subtype of disease course dependent process: A process that can constitute the course of renal fibrosis. renal fibrosis dependent process HOIP_0040878 HOIP:HOIP_0040880 Renal fibrosis process is a subtype of fibrosis: A process that replaces renal tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of renal fibrosis. renal fibrosis [renal fibrosis (course)] HOIP_0040880 HOIP:HOIP_0040883 Positive regulation of cell adhesion molecule expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of cell adhesion molecule expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 positive regulation of cell adhesion molecule expression (very high) in severe COVID-19 HOIP_0040883 PMID:33077917 C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma - pathological events that are all observed in severe cases of COVID-19. Mechanistically, disruption of the endothelial barrier by SARS-CoV-2 spike protein is mediated by changes in the surface expression of intracellular adhesion molecule-1 (ICAM1), vascular cell adhesion protein-1 (VCAM1) and the tight junction scaffold protein zonula occludens-1 (ZO-1), as reported by a preprint study. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0040885 Any biological process that results in permanent cessation of all vital functions of an endothelial cell. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. endothelial cell death [endotheliitis course] HOIP_0040885 HOIP:HOIP_0040886 Endothelium damage is a subtype of damaging: A process that injuries the structure of the endothelium as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. endotheliitis endothelium damage [endotheliitis course] HOIP_0040886 HOIP:HOIP_0040887 Positive regulation of cell adhesion molecule expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of cell adhesion molecule expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 positive regulation of cell adhesion molecule expression (very high) in COVID-19 associated with ARDS HOIP_0040887 PMID:33077917 C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma - pathological events that are all observed in severe cases of COVID-19. HOIP:HOIP_0040888 Increasing vascular permeabilization in lung is a subtype of increasing vascular permeabilization : A process that changes the permeability of the vascular to be higher in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 increasing vascular permeabilization in lung (very high) in COVID-19 associated with ARDS HOIP_0040888 PMID:33077917 C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma - pathological events that are all observed in severe cases of COVID-19. Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. HOIP:HOIP_0040891 Pancreatic damage is a subtype of damaging: A process that injuries the structure of the pancreas as the direct or indirect result of an external force. pancreatic damage HOIP_0040891 HOIP:HOIP_0040892 The change in morphology and behavior of a endothelial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33077917 endothelial cell activation (very high) in severe COVID-19 HOIP_0040892 PMID:32629875 Since soluble IL-6R is abnormally elevated in the plasma of COVID-19 patients, presumably secondary to cleavage from the cells surface by TACE/ADAM17 upon SARS-CoV-2 infection and the inflammatory response associated with COVID-19, IL-6 can activate most cells, including endothelial cells, which do not express endogenous IL-6R but can be activated by the complex of soluble IL-6R and IL-6. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0040895 kallikrein signaling is a process that a signal is transmitted by the kallikrein. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 kallikrein signaling(very high) in severe COVID-19 HOIP_0040895 PMID:33077917 Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. HOIP:HOIP_0040896 Any biological process that results in permanent cessation of all vital functions of an endothelial cell. endothelial cell death HOIP_0040896 HOIP:HOIP_0040897 Any biological process that results in permanent cessation of all vital functions of an endothelial cell in lung. endothelial cell death in lung HOIP_0040897 HOIP:HOIP_0040898 Moving blood clot is a subtype of moving. A process that change the location of the blood clot. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 moving blood clot in COVID-19 associated with ARDS HOIP_0040898 PMID:32629875 An autopsy series showed the presence of deep venous thrombosis involving the lower extremities bilaterally in 56% (7/12) of cases, associated with massive pulmonary embolism in four of these cases, which was listed as the cause of death. Table 1. Clinical and pathological vascular manifestations in SARS-CoV-2 infection. A systematic search for pulmonary emboli in 26 COVID-19 patients on mechanical ventilation showed that they were detected in 23% (6/26) of patients, and venous thromboembolism (VTE) was detected in 69% (18/26). Results of 12 consecutive complete autopsies of patients with COVID-19 concluded that massive pulmonary embolism was the cause of death in 4/12 cases and that VTE was present in 7/12 (58%) patients. HOIP:HOIP_0040900 Endothelium damage in lung is a subtype of endothelium damage: A process that injuries the structure of the endothelium in lung as the direct or indirect result of an external force. endothelium damage in lung HOIP_0040900 HOIP:HOIP_0040901 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot in lung; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. blood coagulation in lung HOIP_0040901 HOIP:HOIP_0040902 Thrombus formation in liver is a subtype of thrombus formation: A process that construcs thrombus in liver. thrombus formation in liver HOIP_0040902 HOIP:HOIP_0040903 Thrombus formation in liver is a subtype of thrombus formation: A process that construcs thrombus in liver. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32629875 PMID:32651579 This process can constitute the course of COVID-19 in the liver. HOIP_0040903 PMID:32629875 Histopathology of post-mortem wedge liver biopsies obtained in 48 COVID-19 cases showed evidence of intrahepatic vascular abnormalities in all patients, including partial or complete luminal thrombosis of portal and sinusoidal vessels, associated with portal vessel dilation, fibrosis and focal hepatic tissue hemorrhage and necrosis. The presence of thrombi involving the portal venules was observed in 15/22 autopsies, occasionally associated with thrombi in some hepatic arteries and arterioles. PMID:32651579 Other histopathologic changes in the liver included hepatic steatosis, portal fibrosis, lymphocytic infiltrates and ductular proliferation, lobular cholestasis, and acute liver-cell necrosis, together with central-vein thrombosis. HOIP:HOIP_0040904 Thrombus formation in intestine is a subtype of thrombus formation: A process that construcs thrombus in intestine. thrombus formation in intestine HOIP_0040904 HOIP:HOIP_0040905 Thrombus formation in intestine is a subtype of thrombus formation: A process that construcs thrombus in intestine. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 thrombus formation in intestine in severe COVID-19 HOIP_0040905 PMID:32629875 Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. HOIP:HOIP_0040906 Systemic inflammatory response is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Systemic inflammatory response in severe COVID-19 HOIP_0040906 HOIP:HOIP_0040907 Inflammatory response in intestinal is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammation in intestinal inflammatory response in intestinal HOIP_0040907 HOIP:HOIP_0040908 Inflammatory response in intestinal is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 inflammation in intestinal inflammatory response in intestinal in severe COVID-19 HOIP_0040908 PMID:32629875 Histology of the specimens not only confirmed the presence of ischemic enteritis and patchy bowel necrosis but also showed the presence of thrombi and perivascular inflammation in the submucosal arterioles. HOIP:HOIP_0040909 Decreasing arterial filling is a subtype of decreasing quantity: A process that changes the amount of arterial filling to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 arterial underfilling decreasing arterial filling in COVID-19 in renal system HOIP_0040909 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. HOIP:HOIP_0040910 Vessel edema in lung is a subtype of vessel edema: A process that keeps fluids in the vessel in lung. vessel oedema in lung blood vessel wall oedema in lung vessel edema in lung HOIP_0040910 HOIP:HOIP_0040911 Vessel edema in lung is a subtype of vessel edema: A process that keeps fluids in the vessel in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32835247 PMID:33077917 vessel oedema in lung blood vessel wall oedema in lung vessel edema in lung in COVID-19 associated with ARDS HOIP_0040911 PMID:32835247 Some data have emerged from patients with COVID-19 pneumonia that show a similar pulmonary vascular picture with blood vessel wall oedema, modest vessel wall immune cell infiltration, hyaline thrombosis, haemorrhagic change, and infarction. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0040912 A type of brain cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 brain cell necrosis in COVID-19 in nervous system HOIP_0040912 PMID:32651579 In addition, meningoencephalitis, hemorrhagic posterior reversible encephalopathy syndrome, and acute necrotizing encephalopathy, including the brainstem and basal ganglia, have been described in case reports. HOIP:HOIP_0040913 Pulmonary alveoli damage is a subtype of damaging: A process that injuries the structure of the pulmonary alveoli as the direct or indirect result of an external force. pulmonary alveoli damage HOIP_0040913 HOIP:HOIP_0040914 Pulmonary alveoli damage is a subtype of damaging: A process that injuries the structure of the pulmonary alveoli as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 PMID:32422178 pulmonary alveoli damage in COVID-19 associated with ARDS HOIP_0040914 PMID:32307653 In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32422178 However, diffuse alveolar damage, which is the defining feature of ARDS, has been the characteristic histological feature in fatal COVID-19 cases with the added observation of microvascular thrombosis. HOIP:HOIP_0040915 Any process that activates or increases the frequency, rate or extent of the inflammatory response in lung. positive regulation of inflammatory response in lung HOIP_0040915 HOIP:HOIP_0040916 Endothelium malfunction in lung is a subtype of endothelium malfunction: A process that does not perform endothelium function in lung correctly or not functioning at all. Wikipedia:Endothelium endothelium dysfunction in lung HOIP_0040916 Wikipedia:Endothelium The endothelium normally provides a surface on which blood does not clot, because it contains and expresses substances that prevent clotting, including heparan sulfate which acts as a cofactor for activating antithrombin, a protease that inactivates several factors in the coagulation cascade. HOIP:HOIP_0040917 The movement of a macrophage in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 PMID:32697943 macrophage chemotaxis (very high)in COVID-19 associated with ARDS HOIP_0040917 PMID:32307653 Some regions of reactive epithelial hyperplasia had also abundant alveolar macrophages. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32697943 Upon infection, there is an accumulation of immune cells in the lungs, especially macrophages and monocytes. HOIP:HOIP_0040918 The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32843733 tumor necrosis factor production (very high) in COVID-19 associated with ARDS HOIP_0040918 PMID:32843733 Levels of inflammatory cytokines such as IL-1, TNF and IL-6 can be high in the lungs of patients with COVID-19; therefore, blocking one or more of these cytokines could potentially benefit these individuals by reducing the severity of the cytokine storm and ARDS. HOIP:HOIP_0040920 Inflammatory response in myocardium is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32651579 PMID:32690910 inflammatory response in myocardium in COVID-19 associated with myocarditis HOIP_0040920 PMID:32651579 Myocarditis is a presumed etiology of cardiac dysfunction, and the development of myocarditis may relate to viral load. PMID:32690910 SARS-CoV-2 might also infect the myocardium directly, resulting in viral myocarditis in a small proportion of patients with COVID-19. HOIP:HOIP_0040921 Microthrombus formation in lung is a subtype of microthrombus formation: A process that construcs microthrombus. Microthrombus formation in lung HOIP_0040921 HOIP:HOIP_0040922 Microthrombus formation in lung is a subtype of microthrombus formation: A process that construcs microthrombus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32422178 PMID:32629875 PMID:32651579 PMID:33077917 Microthrombus formation in lung in COVID-19 associated with ARDS HOIP_0040922 PMID:32422178 However, diffuse alveolar damage, which is the defining feature of ARDS, has been the characteristic histological feature in fatal COVID-19 cases with the added observation of microvascular thrombosis. PMID:32629875 Another autopsy series on 67 COVID-19 cases described the presence of vascular microthrombi in multiple organs, particularly in the lungs (in 23/25 cases) where it was associated with capillary sprouting and capillary inflammation, and in the brain (in 6/20 cases) where it was associated with evidence of patchy acute infarcts. The pulmonary capillary vessels of COVID-19 tissues contained microthrombi and evidence of intravascular (intussusceptive) neovascularization, which were more frequent than observed in the influenza cases. Similarly, thrombi/platelet aggregates were visualized microscopically in capillaries, arterioles and medium sized arteries of most COVID-19 lungs (21/23). PMID:32651579 Autopsy studies of patients who died due to COVID-19 have shown high rates of microvascular and macrovascular thromboses, especially in the pulmonary circulation. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. HOIP:HOIP_0040924 Tissue damage in lung is a subtype of tissue damage: A process that injuries the structure of the tissue in lung as the direct or indirect result of an external force. tissue damage in lung HOIP_0040924 HOIP:HOIP_0040925 Any biological process that results in permanent cessation of all vital functions of a cell in lung. cell death in lung HOIP_0040925 HOIP:HOIP_0040926 Increasing blood glucose level is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 with diabetes. PMID:32651579 PMID:32694793 PMID:32697943 PMID:33188364 hyperglycemia increasing blood glucose level in COVID-19 in patient with diabetes HOIP_0040926 PMID:32651579 Moreover, patients hospitalized with COVID-19 have exhibited a range of abnormalities of glucose metabolism, including worsened hyperglycemia, euglycemic ketosis, and classic diabetic ketoacidosis. Several mechanisms may account for the more severe disease course, including worsened hyperglycemia and ketosis, observed in patients with COVID-19 and diabetes. In addition, ACE2 expression has been reported in the endocrine pancreas, albeit inconsistently. This raises the possibility that direct binding of SARS-CoV-2 to ACE2 on beta-cells might contribute to insulin deficiency and hyperglycemia, as has been shown previously for infection with SARS-CoV. PMID:32694793 Glycaemic control is likely to be necessary to regulate the host inflammatory response, to limit tissue susceptibility to inflammatory damage signals and to sustain physiological function during the severe and critical stages of infection. PMID:32697943 Diabetic people with uncontrolled blood glucose levels have a greater risk to develop severe COVID-19 disease. Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Moreover, increased glucose levels further augmented TNF-a, IL-6, and IFN a, b, and l expression (Figure S1A). This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. Elevated glucose levels directly induce viral replication and proinflammatory cytokine expression. These data may explain why uncontrolled diabetes may lead to compromised adaptive immune response and lung dysfunction in patients with severe COVID-19 symptoms. PMID:33188364 As described already, glucotoxicity, endothelial damage by inflammation, oxidative stress and cytokine production contribute to an increased risk of thromboembolic complications and of damage to vital organs in patients with diabetes mellitus (fig. 1). Patients with COVID-19 also exhibit elevation of other inflammatory markers, such as D-dimer, ferritin and IL-6, which might contribute to an increased risk of microvascular and macrovascular complications originating from low-grade vascular inflammation in patients with underlying diabetes mellitus. HOIP:HOIP_0040928 Myocardium malfunction is a subtype of malfunctioning process: A process that cannot perform signaling [biological] appropriately or cannot realize it at all. myocardium malfunction HOIP_0040928 HOIP:HOIP_0040930 Right ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete right ventricular function. right ventricular failure right ventricular dysfunction HOIP_0040930 HOIP:HOIP_0040931 Increasing demand for response to oxidative stress in myocardium is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher in myocardium. This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 increasing demand for response to oxidative stress in myocardium in COVID-19 associated with myocarditis HOIP_0040931 PMID:32629875 Also, genetic and pharmacological studies in mice have shown that ACE2 regulates cardiac structure and function; decreased ACE2 in SARS-CoV-2-infected cardiomyocytes could disrupt these activities, particularly impairing cardiac remodeling and increasing oxidative stress in cardiomyocytes. HOIP:HOIP_0040932 Kidney congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the Kidney. renal congestion kidney congestion HOIP_0040932 HOIP:HOIP_0040933 Inflammatory response in myelin sheath is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in myelin sheath HOIP_0040933 HOIP:HOIP_0040934 Left ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete left ventricular function. left ventricular failure left ventricular dysfunction HOIP_0040934 HOIP:HOIP_0040935 A type of myocardial cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. myocardial cell necrosis in COVID-19 associated with myocarditis HOIP_0040935 HOIP:HOIP_0040936 Decreasing cardiac output is a subtype of decreasing quantity: A process that changes the amount of cardiac output to be lower. decreasing cardiac output HOIP_0040936 HOIP:HOIP_0040937 Inflammatory cell infiltration into myocardium is a subtype of inflammatory cell infiltration: A process that moves the outside inflammatory cell to the inside of myocardium in response to an inflammatory reaction. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis PMID:32651579 inflammatory cell infiltration into myocardium in COVID-19 associated with myocarditis HOIP_0040937 PMID:32651579 While isolation of the virus from myocardial tissue has been reported in a few autopsy studies, other pathological reports have described inflammatory infiltrates without myocardial evidence of SARS-CoV-2. HOIP:HOIP_0040938 Low cardiac output syndrome (LCOS) is a clinical condition that is caused by a transient decrease in systemic perfusion secondary to myocardial dysfunction. (PMID:16344207) low cardiac output syndrome HOIP_0040938 HOIP:HOIP_0040939 Decreasing arterial filling is a subtype of decreasing quantity: A process that changes the amount of arterial filling to be lower. arterial underfilling decreasing arterial filling HOIP_0040939 HOIP:HOIP_0040940 Myocardial damage is a subtype of damaging: A process that injuries the structure of the myocardial muscle as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 PMID:32651579 myocardial damage in COVID-19 associated with myocarditis HOIP_0040940 PMID:32629875 Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. PMID:32651579 Systemic inflammatory response syndrome (cytokine storm) is another putative mechanism of myocardial injury. HOIP:HOIP_0040941 Decreasing kidney perfusion is a subtype of decreasing quantity: A process that changes the amount of kidney perfusion to be lower. kidney hypoperfusion decreasing kidney perfusion HOIP_0040941 HOIP:HOIP_0040942 Myocardial damage is a subtype of damaging: A process that injuries the structure of the myocardial muscle as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of myocarditis. myocardial damage [myocarditis course] HOIP_0040942 HOIP:HOIP_0040943 Endothelium damage in kidney is a subtype of endothelium damage: A process that injuries the structure of the endothelium in kidney as the direct or indirect result of an external force. endothelium damage in kidney HOIP_0040943 HOIP:HOIP_0040944 Inflammatory response in myelin sheath is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in nervous system. PMID:32651579 inflammatory response in myelin sheath (very high) in COVID-19 in nervous system HOIP_0040944 PMID:32651579 Acute inflammatory demyelinating polyneuropathy (Guillain-Barré syndrome) has also been reported in some patients. HOIP:HOIP_0040946 Viral entry into bloodstream is a subtype of moving A to the inside of B: A process that of the movement of virus into bloodstream. viral entry into bloodstream HOIP_0040946 HOIP:HOIP_0040948 Epithelium damage is a subtype of damaging: A process that injuries the structure of the epithelium as the direct or indirect result of an external force. epithelium damage HOIP_0040948 HOIP:HOIP_0040949 Epithelium damage in lung is a subtype of epithelium damage : A process that injuries the structure of the epithelium in lung as the direct or indirect result of an external force. epithelium damage in lung HOIP_0040949 HOIP:HOIP_0040950 Epithelium damage in lung is a subtype of epithelium damage : A process that injuries the structure of the epithelium in lung as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32422178 epithelium damage in lung in COVID-19 associated with ARDS HOIP_0040950 PMID:32422178 Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. HOIP:HOIP_0040951 interferon-gamma production The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32422178 interferon-gamma production (severe)in COVID-19 associated with ARDS HOIP_0040951 PMID:32422178 Subsequent studies have found that exogenously administered as well as endogenously produced interferon might induce pulmonary vasculopathy, and this finding is important given that pulmonary vascular disease could play an important role in severe COVID-19 disease. Indeed, circulating IFN-gamma and CXCL10 concentrations are raised in patients with severe COVID-19. HOIP:HOIP_0040952 Increasing vascular permeabilization in lung is a subtype of increasing vascular permeabilization : A process that changes the permeability of the vascular to be higher in lung. increasing vascular permeabilization in lung HOIP_0040952 HOIP:HOIP_0040953 Loss of vessel barrier integrity in lung is a subtype of loss of function (process): A process that results in no longer having a loss of vessel barrier integrity function or the process in lung that gradually loses it. loss of vessel barrier integrity in lung HOIP_0040953 HOIP:HOIP_0040954 Any process that activates or increases the frequency, rate or extent of blood coagulation in lung. positive regulation of blood coagulation in lung HOIP_0040954 HOIP:HOIP_0040956 Vessel edema is a subtype of edema: A process that keeps fluids in the vessel. vessel oedema blood vessel wall oedema vessel edema HOIP_0040956 HOIP:HOIP_0040959 Innate immune responses in lung are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. innate immunity in lung innate immune response in lung HOIP_0040959 HOIP:HOIP_0040960 Dysregulation of immune response is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of immune response appropriately or cannot realize it at all. dysregulation of immune response HOIP_0040960 HOIP:HOIP_0040961 Dysregulation of immune response is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of immune response appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 PMID:33123165 dysregulation of immune response in severe COVID-19 HOIP_0040961 PMID:32651579 Dysregulated immune response and cytokine-release syndrome, due to overactivation of innate immunity in the setting of T cell lymphodepletion, characterize the presentations of severe COVID-19. PMID:33123165 Furthermore, IL-10 is an immunosuppressive cytokine suggesting dysregulated immune homeostasis rather than pure inflammation. HOIP:HOIP_0040962 T cell lymphodepletion is a subtype of decreasing T cells: A process that changes the amount of T lymphocytes to be depleted. T cell lymphodepletion HOIP_0040962 HOIP:HOIP_0040964 Increasing C-reactive protein concentration in blood is a subtype of increasing concentration: A process that changes the C-reactive protein concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 increasing C-reactive protein concentration in blood in COVID-19 HOIP_0040964 PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0040965 Increasing ferritin concentration in blood is a subtype of increasing concentration: A process that changes the ferritin concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 hyperferritinemia increasing ferritin concentration in blood in COVID-19 HOIP_0040965 PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0040966 Increasing D-dimer concentration is a subtype of increasing concentration: A process that changes the D-dimer concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 increasing D-dimer concentration in COVID-19 HOIP_0040966 PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0040967 Increasing fibrinogen concentration is a subtype of increasing concentration: A process that changes the fibrinogen concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 increasing fibrinogen concentration in COVID-19 HOIP_0040967 PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0040968 Increasing lactate dehydrogenase concentration is a subtype of increasing concentration: A process that changes the lactate dehydrogenase concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 increasing lactate dehydrogenase concentration in COVID-19 HOIP_0040968 PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. HOIP:HOIP_0040969 Increasing VEGF level is a subtype of increasing quantity: A process that changes the amount of VEGF level to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:33077917 Increasing VEGF level in COVID-19 HOIP_0040969 PMID:32629875 In addition, by promoting VEGF-A secretion from various cell types, IL-6 induces vascular hyper-permeability and sprouting angiogenesis. PMID:33077917 The recruited platelets release VEGF, which amplifies the expression of TF by endothelial cells, further stimulating the coagulation cascade. HOIP:HOIP_0040970 Decreasing T cells is a subtype of decreasing lymphoyte: A process that changes the amount of T cells to be lower. decreasing T cells HOIP_0040970 HOIP:HOIP_0040971 Decreasing T cells is a subtype of decreasing lymphoyte: A process that changes the amount of T cells to be lower. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 PMID:33077917 decreasing T cells in severe COVID-19 HOIP_0040971 PMID:32651579 Studies examining specific lymphocyte subsets have revealed decreases in both CD4+ T cells and CD8+ T cells to be associated with severe COVID-19. PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. HOIP:HOIP_0040972 The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. neutrophil activation in lung involved in immune response HOIP_0040972 HOIP:HOIP_0040973 The expansion of a leukocyte population by cell division. leukocyte proliferation HOIP_0040973 HOIP:HOIP_0040975 The migration of a neutrophil from the blood vessels into the lung tissues. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 PMID:33214651 neutrophil extravasation in lung (very high) in COVID-19 associated with ARDS HOIP_0040975 PMID:33077917 A transcriptome analysis of bronchoalveolar lavage fluid cells from eight patients with COVID-19 suggested that SARS-CoV-2 infection elicits more pronounced neutrophil infiltration than other forms of pneumonia. Infiltrating, activated neutrophils produce large amounts of histotoxic mediators, including reactive oxygen species, as well as NETs, which have been found in arterial microthrombi in the post-mortem lung specimens from four deceased patients with COVID-19. PMID:33214651 In addition to cytokine release, another important event in ARDS, as seen in COVID-19 pathology, is neutrophil recruitment to the pulmonary vasculature. HOIP:HOIP_0040976 The expansion of a neutrophile population by cell division. neutrophile proliferation HOIP_0040976 HOIP:HOIP_0040977 The expansion of a neutrophile population by cell division. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 PMID:32843733 neutrophile proliferation (very high) in severe COVID-19 HOIP_0040977 PMID:32651579 In addition, leukocytosis (especially neutrophilia), seen less commonly, is also a negative prognostic marker. PMID:32843733 In line with observations in lethal cases of SARS and MERS, patients infected with SARS-CoV-2 show increased numbers of neutrophils and macrophages in their airways and blood. HOIP:HOIP_0040978 Right ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete right ventricular function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32416769 PMID:32651579 Wikipedia:Pulmonary_heart_disease right ventricular failure right ventricular dysfunction in COVID-19 associated with ARDS HOIP_0040978 PMID:32416769 Cardiorenal syndrome, particularly right ventricular failure secondary to COVID-19 pneumonia, might lead to kidney congestion and subsequent AKI. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Isolated right ventricular failure with and without confirmed pulmonary embolism has also been reported. Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. HOIP:HOIP_0040979 Negative regulation of anticoagulant mechanism is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of anticoagulant mechanism. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. Wikipedia:Endothelium negative regulation of anticoagulant mechanism [endotheliitis course] HOIP_0040979 Wikipedia:Endothelium Blood clotting (thrombosis and fibrinolysis). The endothelium normally provides a surface on which blood does not clot, because it contains and expresses substances that prevent clotting, including heparan sulfate which acts as a cofactor for activating antithrombin, a protease that inactivates several factors in the coagulation cascade. HOIP:HOIP_0040980 Myocardial infarction dependent process is a subtype of disease course dependent process: A process that can constitute the course of myocardial infarction. myocardial infarction dependent process HOIP_0040980 HOIP:HOIP_0040981 The totality of all processes through which a given myocardial infarction instance is realized. myocardial infarction course HOIP_0040981 HOIP:HOIP_0040982 Narrowing of the coronary artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the coronary arteries to be smaller. coronary artery narrowing HOIP_0040982 HOIP:HOIP_0040983 Hepatobiliary system damage is a subtype of damaging: A process that injures the structure of the hepatobiliary system as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 hepatobiliary system damage in severe COVID-19 HOIP_0040983 PMID:32651579 Signs of hepatobiliary damage may be observed in patients with severe presentations of COVID-19. Elevated bilirubin at hospital admission has also been linked to disease severity and progression to critical illness in a few studies, although the association of longitudinal changes in bilirubin with prolonged ARDS is currently unclear. HOIP:HOIP_0040984 Narrowing of the coronary artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the coronary arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. coronary artery narrowing [myocardial infarction course] HOIP_0040984 HOIP:HOIP_0040986 Decreasing myocardial blood flow is a subtype of decreasing flow: A process that changes the amount of myocardial blood flow to be lower. decreasing myocardial blood flow HOIP_0040986 HOIP:HOIP_0040987 Decreasing myocardial blood flow is a subtype of decreasing flow: A process that changes the amount of myocardial blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. decreasing myocardial blood flow [myocardial infarction course] HOIP_0040987 HOIP:HOIP_0040989 Myocardial Ischemia is a changing process to lack enough to blood supply of Myocardium. myocardial ischemia HOIP_0040989 HOIP:HOIP_0040990 Myocardial Ischemia is a changing process to lack enough to blood supply of Myocardium. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. myocardial ischemia [myocardial infarction course] HOIP_0040990 HOIP:HOIP_0040991 Blood vessel damage is a subtype of damaging: A process that injures the structure of the blood vessel as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32694793 blood vessel damage in COVID-19 in cardiovascular system HOIP_0040991 PMID:32694793 The damage to the blood vessels caused by hypertension decreases blood flow to the kidneys and consequently results in kidney injury (Fig. 2). HOIP:HOIP_0040992 A type of myocardial cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. myocardial cell necrosis HOIP_0040992 HOIP:HOIP_0040993 A type of myocardial cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. myocardial cell necrosis [myocardial infarction course] HOIP_0040993 HOIP:HOIP_0040994 Increasing troponin concentration is a subtype of increasing concentration: A process that changes the troponin concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 PMID:32651579 Increasing troponin concentration in COVID-19 associated with myocarditis HOIP_0040994 PMID:32629875 Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. PMID:32651579 A greater frequency and magnitude of troponin elevations in hospitalized patients has been associated with more-severe disease and worse outcomes. HOIP:HOIP_0040995 An ischemia that is characterized by low blood supply to tissues in the limb due to interruption in the arterial blood supply. limb ischemia HOIP_0040995 HOIP:HOIP_0040996 Limb ischemia dependent process is a subtype of disease course dependent process: A process that can constitute the course of limb ischemia. limb ischemia dependent process HOIP_0040996 HOIP:HOIP_0040997 The totality of all processes through which a given limb ischemia instance is realized. limb ischemia course HOIP_0040997 HOIP:HOIP_0040998 Narrowing of the brain artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the cerebral arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of limb ischemia. limb artery narrowing [limb ischemia course] HOIP_0040998 HOIP:HOIP_0040999 Narrowing of the limb artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the limb arteries to be smaller. limb artery narrowing HOIP_0040999 HOIP:HOIP_0041000 Narrowing of the brain artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the cerebral arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 limb artery narrowing in severe COVID-19 HOIP_0041000 PMID:32651579 There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. HOIP:HOIP_0041001 Decreasing limb blood flow is a subtype of decreasing flow: A process that changes the amount of limb blood flow to be lower. decreasing limb blood flow HOIP_0041001 HOIP:HOIP_0041002 Decreasing limb blood flow is a subtype of decreasing flow: A process that changes the amount of limb blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of limb ischemia. decreasing limb blood flow [limb ischemia course] HOIP_0041002 HOIP:HOIP_0041003 Decreasing limb blood flow is a subtype of decreasing flow: A process that changes the amount of limb blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 decreasing limb blood flow in severe COVID-19 HOIP_0041003 PMID:32651579 There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. HOIP:HOIP_0041004 Limb Ischemia is a changing process to lack enough to blood supply of Limb. limb ischemia (process) HOIP_0041004 HOIP:HOIP_0041005 Limb Ischemia is a changing process to lack enough to blood supply of Limb. This entity is a specific course-dependent process. This process can constitute the course of limb Ischemia. limb ischemia (process) [limb ischemia course] HOIP_0041005 HOIP:HOIP_0041006 Limb Ischemia is a changing process to lack enough to blood supply of Limb. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 limb ischemia (process) in severe COVID-19 HOIP_0041006 PMID:32651579 There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. HOIP:HOIP_0041007 Negative regulation of lymphocyte proliferation is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the lymphocyte proliferation. Negative regulation of lymphocyte proliferation HOIP_0041007 HOIP:HOIP_0041008 Increasing blood pressure is a subtype of increasing pressure: A process that changes the blood pressure to be higher. increasing vascular pressure increasing blood pressure HOIP_0041008 HOIP:HOIP_0041009 The microvessels include terminal arterioles, metarterioles, capillaries, and venules. (https://en.wikipedia.org/wiki/Microcirculation) microvessel HOIP_0041009 HOIP:HOIP_0041010 Increasing blood pressure in lung is a subtype of increasing blood pressure : A process that changes the blood pressure to be higher in lung. increasing vascular pressure in lung increasing blood pressure in lung HOIP_0041010 HOIP:HOIP_0041011 Increasing blood pressure in lung is a subtype of increasing blood pressure : A process that changes the blood pressure to be higher in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32651579 Wikipedia:Pulmonary_heart_disease increasing vascular pressure in lung increasing blood pressure in lung in COVID-19 associated with ARDS HOIP_0041011 PMID:32651579 Isolated right ventricular failure with and without confirmed pulmonary embolism has also been reported. Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. HOIP:HOIP_0041012 Myocardium malfunction is a subtype of malfunctioning process: A process that cannot perform signaling [biological] appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 PMID:32651579 Myocardium malfunction in COVID-19 associated with myocarditis HOIP_0041012 PMID:32629875 COVID-19, however, appears to include an evolving set of clinical manifestation not previously reported in SARS and MERS, including stroke and cardiomyopathies associated with coagulopathy and vasculopathy, which can cause sudden death and other serious morbidities. However, cardiovascular disease is prevalent in patients with COVID-19; 7% of all patients and 22 % of severe cases experienced myocardial injury. Cases of cardiomyopathy have been reported in patients with COVID-19, raising the possibility that myocarditis-related cardiac events may be increased in COVID-19. Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. In one study, atrial arrhythmias were commonly detected in patients with severe COVID-19. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Biventricular cardiomyopathy has been reported in 7–33% of critically ill patients with COVID-19. HOIP:HOIP_0041013 Dysregulation of heartbeats is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of heartbeats appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32412710 PMID:32629875 PMID:32651579 cardiac arrhythmias dysregulation of heartbeats in COVID-19 associated with myocarditis HOIP_0041013 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. PMID:32629875 In one study, atrial arrhythmias were commonly detected in patients with severe COVID-19. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Cardiac arrhythmias, including new-onset atrial fibrillation, heart block, and ventricular arrhythmias, are also prevalent, occurring in 17% of hospitalized patients and 44% of patients in the ICU setting in a study of 138 patients from Wuhan, China. Among 393 patients with COVID-19 from a separate cohort from New York City, atrial arrhythmias were more common among patients who required mechanical ventilation than among those who did not (17.7% versus 1.9%). HOIP:HOIP_0041014 Ductular reaction (DR) is characterized by the proliferation of reactive bile ducts induced by liver injuries. (PMID: 31472030) ductular reaction ductular proliferation HOIP_0041014 HOIP:HOIP_0041015 Heart conduction diseasedependent process is a subtype of disease course dependent process: A process that can constitute the course of heart conduction disease. heart conduction disease dependent process HOIP_0041015 HOIP:HOIP_0041017 Cardiac conduction systemmalfunction is a subtype of malfunction: A process that does not perform cardiac conduction system function correctly or not functioning at all. cardiac conduction system malfunction HOIP_0041017 HOIP:HOIP_0041018 Ductular reaction (DR) is characterized by the proliferation of reactive bile ducts induced by liver injuries. (PMID: 31472030) This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 ductular reaction ductular proliferation in severe COVID-19 HOIP_0041018 PMID:32651579 Other histopathologic changes in the liver included hepatic steatosis, portal fibrosis, lymphocytic infiltrates and ductular proliferation, lobular cholestasis, and acute liver-cell necrosis, together with central-vein thrombosis. HOIP:HOIP_0041019 Myocardium malfunction is a subtype of malfunctioning process: A process that cannot perform signaling [biological] appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of myocarditis. Myocardium malfunction [myocarditis course] HOIP_0041019 HOIP:HOIP_0041020 Cardiac conduction systemmalfunction is a subtype of malfunction: A process that does not perform cardiac conduction system function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of heart conduction disease. cardiac conduction system malfunction [heart conduction disease] HOIP_0041020 HOIP:HOIP_0041021 Smooth muscle damage is a subtype of damaging: A process that injuries the structure of the smooth muscle as the direct or indirect result of an external force. smooth muscle damage HOIP_0041021 HOIP:HOIP_0041022 Renal tubule malfunction is a subtype of malfunction: A process that does not perform renal tubule function correctly or not functioning at all. renal tubule malfunction HOIP_0041022 HOIP:HOIP_0041023 Acute cor pulmonale dependent process is a subtype of disease course dependent process: A process that can constitute the course of acute cor pulmonale. acute cor pulmonale dependent process HOIP_0041023 HOIP:HOIP_0041025 Hepatoellular damage is a subtype of cellular damage: A process that injuries the structure of the hepatocell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 hepatocellular injury hepatocellular damage in COVID-19 in liver HOIP_0041025 PMID:32651579 In critically ill patients with COVID-19, a hepatocellular injury pattern is seen in 14–53% of hospitalized patients. Elevated bilirubin at hospital admission has also been linked to disease severity and progression to critical illness in a few studies, although the association of longitudinal changes in bilirubin with prolonged ARDS is currently unclear. HOIP:HOIP_0041027 Renal cell damage is a subtype of cellular damage: A process that injuries the structure of the renal cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. renal cell injury renal cell damage in COVID-19 in renal system HOIP_0041027 HOIP:HOIP_0041028 Systemic inflammatory response is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 Systemic inflammatory response in COVID-19 associated with ACS HOIP_0041028 PMID:32690910 The mechanisms underlying COVID-19-induced ACS might involve plaque rupture, coronary spasm or microthrombi owing to systemic inflammation or cytokine storm. For example, activated macrophages secrete collagenases that degrade collagen, a major constituent of the fibrous cap on atherosclerotic plaques, which can lead to plaque rupture. HOIP:HOIP_0041030 Right ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete right ventricular function. This entity is a specific course-dependent process. This process can constitute the course of acute cor pulmonale. Wikipedia:Pulmonary_heart_disease right ventricular failure right ventricular dysfunction [acute cor pulmonale course] HOIP_0041030 Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. HOIP:HOIP_0041031 Right ventricular damage is a subtype of damaging: A process that injuries the structure of the right ventricular as the direct or indirect result of an external force. right ventricular damage HOIP_0041031 HOIP:HOIP_0041032 Atheroma rupture is the tearing apart of an atheroma. 粥腫破綻 plaque rupture atheroma rupture HOIP_0041032 HOIP:HOIP_0041033 Right ventricular damage is a subtype of damaging: A process that injuries the structure of the right ventricular as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of acute cor pulmonale. Wikipedia:Pulmonary_heart_disease right ventricular damage [acute cor pulmonale course] HOIP_0041033 Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. HOIP:HOIP_0041034 Respiratory system blood vessel smooth muscle damage is a subtype of damaging: A process that injuries the structure of the respiratory system blood vessel smooth muscle as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32651579 respiratory system blood vessel smooth muscle damage in COVID-19 associated with ARDS HOIP_0041034 PMID:32651579 Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. HOIP:HOIP_0041035 Myocardial damage is a subtype of damaging: A process that injuries the structure of the myocardial muscle as the direct or indirect result of an external force. myocardial damage HOIP_0041035 HOIP:HOIP_0041036 An atheroma, or atheromatous plaque ("plaque"), is an abnormal accumulation of material in the inner layer of the wall of an artery. (Wikipedia:Atheroma) Wikipedia:Atheroma Wikipedia:Atheroma atheromatous plaque plaque atheroma HOIP_0041036 Wikipedia:Atheroma The material consists of mostly macrophage cells, or debris, containing lipids, calcium and a variable amount of fibrous connective tissue. The accumulated material forms a swelling in the artery wall, which may intrude into the lumen of the artery, narrowing it and restricting blood flow. Atheroma is the pathological basis for the disease entity atherosclerosis, a subtype of arteriosclerosis. HOIP:HOIP_0041037 Cholestasis is a subtype of stagnating: A process that changes the bile flow to be slower due to obstruction. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 cholestasis in severe COVID-19 HOIP_0041037 PMID:32651579 Other histopathologic changes in the liver included hepatic steatosis, portal fibrosis, lymphocytic infiltrates and ductular proliferation, lobular cholestasis, and acute liver-cell necrosis, together with central-vein thrombosis. HOIP:HOIP_0041039 Atheroma rupture is the tearing apart of an atheroma. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 粥腫破綻 plaque rupture atheroma rupture in COVID-19 associated with ACS HOIP_0041039 PMID:32690910 The mechanisms underlying COVID-19-induced ACS might involve plaque rupture, coronary spasm or microthrombi owing to systemic inflammation or cytokine storm. For example, activated macrophages secrete collagenases that degrade collagen, a major constituent of the fibrous cap on atherosclerotic plaques, which can lead to plaque rupture. HOIP:HOIP_0041040 Inflammatory response in nervous system is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in nervous system HOIP_0041040 HOIP:HOIP_0041041 Inflammatory response in myocardium is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in myocardium HOIP_0041041 HOIP:HOIP_0041042 Myocarditis dependent process is a subtype of disease course dependent process: A process that can constitute the course of myocarditis. myocarditis dependent process HOIP_0041042 HOIP:HOIP_0041043 The totality of all processes through which a given myocarditis instance is realized. myocarditis course HOIP_0041043 HOIP:HOIP_0041044 Inflammatory response in myocardium is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of myocarditis. inflammatory response in myocardium [myocarditis course] HOIP_0041044 HOIP:HOIP_0041045 Cardiac malfunction is a subtype of organ malfunction: A process that does not perform cardiac function correctly or not functioning at all. cardiac dysfunction cardiac malfunction HOIP_0041045 HOIP:HOIP_0041046 Thrombus formation in coronary artery is a subtype of thrombus formation: A process that construcs thrombus in coronary artery. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32651579 thrombus formation in coronary artery in COVID-19 associated with ACS HOIP_0041046 PMID:32651579 While patients with viral infections are at risk for MI in general, this risk may be exaggerated in patients with COVID-19, given reports of disproportionately increased hypercoagulability in affected people, which would lead to a possible increase in thrombotically mediated MI. HOIP:HOIP_0041047 Inflammatory cell infiltration into lung is a subtype of inflammatory cell infiltration: A process that moves the outside inflammatory cell to the inside of lung in response to an inflammatory reaction. inflammatory cell infiltration into lung HOIP_0041047 HOIP:HOIP_0041048 Inflammatory cell infiltration into pulmonary interstitium is a subtype of inflammatory cell infiltration: A process that that moves the outside inflammatory cell to the inside of pulmonary interstitium in response to an inflammatory reaction. inflammatory cell infiltration into pulmonary interstitium HOIP_0041048 HOIP:HOIP_0041049 An interstitium that is part of a lung pulmonary interstitium lung interstitium HOIP_0041049 HOIP:HOIP_0041050 Inflammatory cell infiltration into myocardium is a subtype of inflammatory cell infiltration: A process that moves the outside inflammatory cell to the inside of myocardium in response to an inflammatory reaction. inflammatory cell infiltration into myocardium HOIP_0041050 HOIP:HOIP_0041051 Narrowing of the coronary artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the coronary arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32651579 coronary artery narrowing in COVID-19 associated with ACS HOIP_0041051 PMID:32651579 There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. While patients with viral infections are at risk for MI in general, this risk may be exaggerated in patients with COVID-19, given reports of disproportionately increased hypercoagulability in affected people, which would lead to a possible increase in thrombotically mediated MI. HOIP:HOIP_0041052 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of myocardium. The process ends when the viral nucleic acid is released into the host cell cytoplasm. viral entry into host cell in myocardium HOIP_0041052 HOIP:HOIP_0041053 A type of myocardial cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32651579 myocardial cell necrosis in COVID-19 associated with ACS HOIP_0041053 PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. HOIP:HOIP_0041054 Guillain-Barre syndrome dependent process is a subtype of disease course dependent process: A process that can constitute the course of Guillain-Barre syndrome. Guillain-Barre syndrome dependent process HOIP_0041054 HOIP:HOIP_0041055 Increasing ketone body level is a subtype of increasing quantity: A process that changes the amount of ketone body level to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 with diabetes. PMID:32651579 PMID:32687793 Increasing ketone body level in COVID-19 in patient with diabetes HOIP_0041055 PMID:32651579 Moreover, patients hospitalized with COVID-19 have exhibited a range of abnormalities of glucose metabolism, including worsened hyperglycemia, euglycemic ketosis, and classic diabetic ketoacidosis. Several mechanisms may account for the more severe disease course, including worsened hyperglycemia and ketosis, observed in patients with COVID-19 and diabetes. Factors related to SARS-CoV-2 include substantially elevated cytokine levels, which may lead to impairments in pancreatic beta-cell function and apoptosis and, consequently, decreased insulin production and ketosis. PMID:32687793 The virus binds to ACE2 receptors, which, among other locations, are expressed in pancreatic tissue and β-cells in particular. Therefore, an acute loss of insulin secretory capacity along with a stress condition and the cytokine storm could lead to a rapid metabolic deterioration with development of diabetic ketoacidosis or hyperglycaemic hyperosmolar syndrome. The SARS-Cov-2 tropism for the β-cell could cause acute impairment of insulin secretion or destruction of β-cells resulting in de novo development of diabetes. HOIP:HOIP_0041056 Thrombus formation in coronary artery is a subtype of thrombus formation: A process that construcs thrombus in coronary artery. thrombus formation in coronary artery HOIP_0041056 HOIP:HOIP_0041057 Myocardial Ischemia is a changing process to lack enough to blood supply of Myocardium. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32651579 myocardial ischemia in COVID-19 associated with ACS HOIP_0041057 PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. HOIP:HOIP_0041058 Hepatobiliary system damage is a subtype of damaging: A process that injures the structure of the hepatobiliary system as the direct or indirect result of an external force. hepatobiliary system damage HOIP_0041058 HOIP:HOIP_0041059 angiotensin signaling is a process that a signal is transmitted by angiotensin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32336612 PMID:33077917 angiotensin signaling in COVID-19 associated with ARDS HOIP_0041059 PMID:32336612 Increased pulmonary inflammation and coagulation have been reported as unwanted effects of enhanced and unopposed angiotensin II effects via the ACE→Angiotensin II→AT1 receptor axis. In the lungs, such dysregulation would favor the progression of inflammatory and thrombotic processes triggered by local angiotensin II hyperactivity unopposed by angiotensin1-7. PMID:33077917 After binding by SARS-CoV-2, ACE2 is internalized and downregulated on endothelial cells, which favour the progression of inflammatory and pro-fibrotic processes in the lung triggered by local angiotensin II (Ang II) hyperactivity. HOIP:HOIP_0041060 Hepatoellular damage is a subtype of cellular damage: A process that injuries the structure of the hepatocell as the direct or indirect result of an external force. hepatocellular injury hepatocellular damage HOIP_0041060 HOIP:HOIP_0041061 Accumulation of abnormal proteins is a subtype of protein accumulation: A process that keeps Angiotensin II in a biological object. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 Angiotensin II accumulation (very high) in COVID-19 associated with ARDS HOIP_0041061 PMID:33077917 After binding by SARS-CoV-2, ACE2 is internalized and downregulated on endothelial cells, which favour the progression of inflammatory and pro-fibrotic processes in the lung triggered by local angiotensin II (Ang II) hyperactivity. HOIP:HOIP_0041063 Hepatitis dependent process is a subtype of disease course dependent process: A process that can constitute the course of hepatitis. hepatitis dependent process HOIP_0041063 HOIP:HOIP_0041064 The totality of all processes through which a given hepatitis instance is realized. hepatitis course HOIP_0041064 HOIP:HOIP_0041065 Inflammatory response in liver is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in liver HOIP_0041065 HOIP:HOIP_0041066 Inflammatory response in liver is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 inflammatory response in liver (very high) in COVID-19 in liver HOIP_0041066 PMID:32651579 Rarely, severe acute hepatitis has been reported. Hyperinflammation seen with cytokine storm and hypoxia-associated metabolic derangements are other potential mechanisms of liver damage. HOIP:HOIP_0041067 Inflammatory response in liver is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of hepatitis. inflammatory response in liver [hepatitis course'] HOIP_0041067 HOIP:HOIP_0041068 Negative regulation of angiotensin II hydrolysis is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of angiotensin II hydrolysis. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 ACE2 hydrolyzes Angiotensin II and produces Angiotensin-(1-7). negative regulation of Angiotensin II hydrolysis (very high) in COVID-19 associated with ARDS HOIP_0041068 PMID:33077917 After binding by SARS-CoV-2, ACE2 is internalized and downregulated on endothelial cells, which favour the progression of inflammatory and pro-fibrotic processes in the lung triggered by local angiotensin II (Ang II) hyperactivity. HOIP:HOIP_0041069 Increasing bilirubin concentration in blood is a subtype of increasing concentration: A process that changes the bilirubin concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 increasing bilirubin concentration in blood in COVID-19 in liver HOIP_0041069 PMID:32651579 Elevated bilirubin at hospital admission has also been linked to disease severity and progression to critical illness in a few studies, although the association of longitudinal changes in bilirubin with prolonged ARDS is currently unclear. HOIP:HOIP_0041071 Interacting selectively and non-covalently with a receptor on the host cell surface of lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 SARS-CoV-2 S binding to human ACE2 (very high) in lung in COVID-19 with ARDS HOIP_0041071 PMID:33077917 After binding by SARS-CoV-2, ACE2 is internalized and downregulated on endothelial cells, which favour the progression of inflammatory and pro-fibrotic processes in the lung triggered by local angiotensin II (Ang II) hyperactivity. HOIP:HOIP_0041073 Interacting selectively and non-covalently with a receptor on the host cell surface in liver. host cell surface receptor binding in liver HOIP_0041073 HOIP:HOIP_0041075 Bile duct damage is a subtype of damaging: A process that injures the structure of the bile duct as the direct or indirect result of an external force. bile duct damage HOIP_0041075 HOIP:HOIP_0041077 Interacting selectively and non-covalently with a receptor on the host cell surface in liver. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 host cell surface receptor binding in liver [COVID-19 in liver] SARS-CoV-2 S binding to human ACE2 in COVID-19 in liver HOIP_0041077 PMID:32651579 SARS-CoV-2 may directly damage the biliary ducts by binding to ACE2 on cholangiocytes. HOIP:HOIP_0041078 Bile duct is a subtype of damaging: A process that injures the structure of the bile duct as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 bile duct damage (very high) in COVID-19 in liver HOIP_0041078 PMID:32651579 SARS-CoV-2 may directly damage the biliary ducts by binding to ACE2 on cholangiocytes. HOIP:HOIP_0041079 Dysregulation of metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of metabolism appropriately or cannot realize it at all. dysregulation of metabolism HOIP_0041079 HOIP:HOIP_0041080 Dysregulation of metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of metabolism appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 dysregulation of metabolism in COVID-19 HOIP_0041080 PMID:32651579 Hyperinflammation seen with cytokine storm and hypoxia-associated metabolic derangements are other potential mechanisms of liver damage. HOIP:HOIP_0041081 Dysregulation of metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of metabolism appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 dysregulation of metabolism (very high) in severe COVID-19 HOIP_0041081 PMID:32651579 Hyperinflammation seen with cytokine storm and hypoxia-associated metabolic derangements are other potential mechanisms of liver damage. HOIP:HOIP_0041082 Interacting selectively and non-covalently with a receptor on the host cell surface of lung. host cell surface receptor binding in lung HOIP_0041082 HOIP:HOIP_0041083 Liver damage is a subtype of damaging: A process that injuries the structure of the liver as the direct or indirect result of an external force. liver damage HOIP_0041083 HOIP:HOIP_0041084 Negative regulation of ACE2 activation in cardiomyocytes is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 activation in lung. Negative regulation of ACE2 activation in lung HOIP_0041084 HOIP:HOIP_0041085 Negative regulation of ACE2 activation in lung is a subtype of Negative regulation of ACE2 activation: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 activation in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 negative regulation of ACE2 activation in lung (very high) in COVID-19 assiciated with ARDS HOIP_0041085 PMID:33077917 After binding by SARS-CoV-2, ACE2 is internalized and downregulated on endothelial cells, which favour the progression of inflammatory and pro-fibrotic processes in the lung triggered by local angiotensin II (Ang II) hyperactivity. HOIP:HOIP_0041086 The expansion of a macrophage population by cell division. macrophage proliferation HOIP_0041086 HOIP:HOIP_0041087 The expansion of a Kupffer cell population by cell division. Kupffer cell proliferation HOIP_0041087 HOIP:HOIP_0041089 Liver congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the liver. liver congestion HOIP_0041089 HOIP:HOIP_0041090 Liver congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the liver. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 liver congestion in COVID-19 in liver HOIP_0041090 PMID:32651579 In a prospective clinicopathologic series of 11 patients from Austria, Kupffer cell proliferation was seen in all patients, and chronic hepatic congestion was seen in 8 patients. HOIP:HOIP_0041091 The totality of all processes through which a given diabetic ketoacidosis instance is realized. diabetic ketoacidosis course HOIP_0041091 HOIP:HOIP_0041092 Acid-base homeostasis imbalance is a subtype of homeostasis imbalance: A process that becomes lacking a acid-base homeostastasis balance. acid-base homeostasis imbalance HOIP_0041092 HOIP:HOIP_0041093 Lipid storage in liver is a subtype of lipid storage: The accumulation and maintenance in cells or tissues of lipids in the liver. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 lipid storage in liver in COVID-19 in liver HOIP_0041093 PMID:32651579 Other histopathologic changes in the liver included hepatic steatosis, portal fibrosis, lymphocytic infiltrates and ductular proliferation, lobular cholestasis, and acute liver-cell necrosis, together with central-vein thrombosis. HOIP:HOIP_0041095 Portal fibrosis is a subtype of fibrosis: A process that replaces Portal tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. portal fibrosis HOIP_0041095 HOIP:HOIP_0041096 Portal fibrosis is a subtype of fibrosis: A process that replaces Portal tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 portal fibrosis in COVID-19 in liver HOIP_0041096 PMID:32651579 Other histopathologic changes in the liver included hepatic steatosis, portal fibrosis, lymphocytic infiltrates and ductular proliferation, lobular cholestasis, and acute liver-cell necrosis, together with central-vein thrombosis. HOIP:HOIP_0041097 Inflammatory cell infiltration into liver is a subtype of inflammatory cell infiltration: A process that moves the outside inflammatory cell to the inside of liver in response to an inflammatory reaction. inflammatory cell infiltration into liver HOIP_0041097 HOIP:HOIP_0041098 Inflammatory cell infiltration into liver is a subtype of inflammatory cell infiltration: A process that moves the outside inflammatory cell to the inside of liver in response to an inflammatory reaction. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the liver. PMID:32651579 inflammatory cell infiltration into liver in COVID-19 in liver HOIP_0041098 PMID:32651579 Other histopathologic changes in the liver included hepatic steatosis, portal fibrosis, lymphocytic infiltrates and ductular proliferation, lobular cholestasis, and acute liver-cell necrosis, together with central-vein thrombosis. HOIP:HOIP_0041099 Acid-base homeostasis imbalance is a subtype of homeostasis imbalance: A process that becomes lacking a acid-base homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of diabetic ketoacidosis. acid-base homeostasis imbalance [diabetic ketoacidosis course] HOIP_0041099 HOIP:HOIP_0041100 Increasing ketone body level is a subtype of increasing quantity: A process that changes the amount of ketone body level to be higher. This entity is a specific course-dependent process. This process can constitute the course of diabetic ketoacidosis. ケトンは酸性のため，血中pHの低下が起こる． Increasing ketone body level [diabetic ketoacidosis course] HOIP_0041100 HOIP:HOIP_0041101 Increasing blood glucose level is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of diabetic ketoacidosis. hyperglycemia increasing blood glucose level [diabetic ketoacidosis course] HOIP_0041101 HOIP:HOIP_0041102 Myelin sheath damage is a subtype of damaging: A process that injuries the structure of the myelin sheath as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of Guillain-Barre syndrome. myelin sheath damage [Guillain-Barre syndrome] HOIP_0041102 HOIP:HOIP_0041103 Myocardium malfunction is a subtype of malfunctioning process: A process that cannot perform signaling [biological] appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. myocardium malfunction [myocardial infarction course] HOIP_0041103 HOIP:HOIP_0041104 Decreasing blood pH is a subtype of decreasing pH: A process that changes the blood pH to be lower. decreasing blood pH HOIP_0041104 HOIP:HOIP_0041106 Decreasing blood pH is a subtype of decreasing pH: A process that changes the blood pH to be lower. This entity is a specific course-dependent process. This process can constitute the course of diabetic ketoacidosis. decreasing blood pH [diabetic ketoacidosis course] HOIP_0041106 HOIP:HOIP_0041107 Malfunctioning of glucose metabolism is a subtype of malfunctioning of metabolism process: A process that cannot perform a glucose metabolism appropriately or cannot realize it at all. malfunctioning of glucose metabolism HOIP_0041107 HOIP:HOIP_0041108 Malfunctioning of glucose metabolism is a subtype of malfunctioning of metabolism process: A process that cannot perform a glucose metabolism appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 PMID:33188364 malfunctioning of glucose metabolism in severe COVID-19 HOIP_0041108 PMID:32651579 Moreover, patients hospitalized with COVID-19 have exhibited a range of abnormalities of glucose metabolism, including worsened hyperglycemia, euglycemic ketosis, and classic diabetic ketoacidosis. PMID:33188364 Thus, during SARS-CoV-2 infection, the ensuing anti-viral immune and inflammatory responses can change insulin sensitivity, potentially aggravating impairments of glucose metabolism (fig. 1). HOIP:HOIP_0041109 Negative regulation of type B pancreatic cell function is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the type B pancreatic cell function. negative regulation of type B pancreatic cell function HOIP_0041109 HOIP:HOIP_0041111 Myocardial damage is a subtype of damaging: A process that injuries the structure of the myocardial muscle as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. myocardial damage [myocardial infarction course] HOIP_0041111 HOIP:HOIP_0041113 Any apoptotic process in a pancreatic β-cell. pancreatic β-cell apoptotic process HOIP_0041113 HOIP:HOIP_0041114 Any apoptotic process in a pancreatic β-cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 with diabetes. PMID:32651579 PMID:32687793 pancreatic β-cell apoptotic process in COVID-19 in patient with diabetes HOIP_0041114 PMID:32651579 Factors related to SARS-CoV-2 include substantially elevated cytokine levels, which may lead to impairments in pancreatic beta-cell function and apoptosis and, consequently, decreased insulin production and ketosis. PMID:32687793 The SARS-Cov-2 tropism for the β-cell could cause acute impairment of insulin secretion or destruction of β-cells resulting in de novo development of diabetes. HOIP:HOIP_0041116 Decreasing production quantity of insulin is a subtype of decreasing production quantity of peptide: A process that changes the production quantity of the insulin to be lower. decreasing insulin production decreasing amount of insulin secretion HOIP_0041116 HOIP:HOIP_0041117 Decreasing production quantity of insulin is a subtype of decreasing production quantity of peptide: A process that changes the production quantity of the insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 with diabetes. PMID:32651579 decreasing insulin production decreasing amount of insulin secretion in COVID-19 in patient with diabetes HOIP_0041117 PMID:32651579 Factors related to SARS-CoV-2 include substantially elevated cytokine levels, which may lead to impairments in pancreatic beta-cell function and apoptosis and, consequently, decreased insulin production and ketosis. HOIP:HOIP_0041118 Decreasing insulin level is a subtype of decreasing quantity: A process that changes the amount of insulin level to be lower. insulin depletion decreasing insulin level HOIP_0041118 HOIP:HOIP_0041121 Interacting selectively and non-covalently with a receptor on the host cell surface in pancreas. host cell surface receptor binding in pancreas HOIP_0041121 HOIP:HOIP_0041122 Interacting selectively and non-covalently with a receptor on the host cell surface in pancreas. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 infeccted diabetes. PMID:32651579 PMID:32687793 PMID:33188364 host cell surface receptor binding in type B pancreatic cell [COVID-19 in patient with diabetes] SARS-CoV-2 S binding to human ACE2 on type B pancreatic cell in COVID-19 infected diabetes patient HOIP_0041122 PMID:32651579 In addition, ACE2 expression has been reported in the endocrine pancreas, albeit inconsistently. This raises the possibility that direct binding of SARS-CoV-2 to ACE2 on beta-cells might contribute to insulin deficiency and hyperglycemia, as has been shown previously for infection with SARS-CoV. PMID:32687793 The SARS-Cov-2 tropism for the β-cell could cause acute impairment of insulin secretion or destruction of β-cells resulting in de novo development of diabetes. PMID:33188364 Some evidence suggests an association between ACE2 and glucose regulation. This finding and the localization of ACE2 expression in the endocrine pancreas together suggest that coronaviruses might specifically damages islets, potentially leading to hyperglycaemia. HOIP:HOIP_0041123 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of neural tissue. The process ends when the viral nucleic acid is released into the host cell cytoplasm. viral entry into host cell in neural tissue HOIP_0041123 HOIP:HOIP_0041124 Inflammatory response in meninx is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in meninx HOIP_0041124 HOIP:HOIP_0041125 Meninx damage is a subtype of organ damage: A process that injuries the structure of the meninx as the direct or indirect result of an external force. meninx damage HOIP_0041125 HOIP:HOIP_0041126 Meninx damage is a subtype of organ damage: A process that injuries the structure of the meninx as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in nervous system. PMID:32651579 meninx damage in COVID-19 in nervous system HOIP_0041126 PMID:32651579 In addition, meningoencephalitis, hemorrhagic posterior reversible encephalopathy syndrome, and acute necrotizing encephalopathy, including the brainstem and basal ganglia, have been described in case reports. HOIP:HOIP_0041128 Thrombus formation in deep vein is a subtype of thrombus formation: A process that construcs thrombus in deep vein. This entity is a specific course-dependent process. This process can constitute the course of pulmonary embolism. thrombus formation in deep vein [pulmonary embolism course] HOIP_0041128 HOIP:HOIP_0041129 Neutrophil extracellular trap formation is a subtype of biological structure formation: A process that constructs neutrophil extracellular trap. neutrophil extracellular trap formation HOIP_0041129 HOIP:HOIP_0041130 Increasing troponin concentration is a subtype of increasing concentration: A process that changes the troponin concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. Increasing troponin concentration [myocardial infarction] HOIP_0041130 HOIP:HOIP_0041131 Nervous system malfunction is a subtype of malfunction: A process that does not perform nervous system function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of demyelinating polyneuropathy. nervous system malfunction [demyelinating polyneuropathy course] HOIP_0041131 HOIP:HOIP_0041132 The directed movement of a virus, or part of a virus into central nervous system. transport of virus into central nervous system HOIP_0041132 HOIP:HOIP_0041133 Nervous system malfunction is a subtype of malfunction: A process that does not perform nervous system function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of Guillain-Barre syndrome. nervous system malfunction [Guillain-Barre syndrome] HOIP_0041133 HOIP:HOIP_0041134 The directed movement of a virus, or part of a virus into central nervous system via retrograde axonal transport. transport of virus into central nervous system via retrograde axonal transport HOIP_0041134 HOIP:HOIP_0041135 Inflammatory response in myelin sheath is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of demyelinating polyneuropathy. inflammatory response in myelin sheath [demyelinating polyneuropathy course] HOIP_0041135 HOIP:HOIP_0041136 Nasal epithelial cell HOIP_0041136 HOIP:HOIP_0041138 Inflammatory response in myelin sheath is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of Guillain-Barre syndrome. inflammatory response in myelin sheath [Guillain-Barre syndrome] HOIP_0041138 HOIP:HOIP_0041139 Interacting selectively and non-covalently with a receptor on the host cell surface in nasal epithelial cells. host cell surface receptor binding in nasal epithelial cells HOIP_0041139 HOIP:HOIP_0041140 Edema in brain is a subtype of edema: A process that keeps an excessive fluid in cells or intercellular tissues of brain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 cerebral edema in COVID-19 associated with cerebral infarction HOIP_0041140 PMID:32629875 A post-mortem imaging study involving 19 patients who had died of COVID-19 disease showed subcortical bleeds in 2/19 cases and edematous changes in the cortex/subcortical regions in 1/19 cases. HOIP:HOIP_0041141 Interacting selectively and non-covalently with a receptor on the host cell surface in nasal epithelial cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 SARS-CoV-2 S binding to human ACE2 on nasal epitherial cell in COVID-19 HOIP_0041141 PMID:32651579 A number of non-specific mild neurological symptoms are notable in hospitalized patients with COVID-19, including headache (8–42%), dizziness (12%), myalgia and/or fatigue (11–44%), anorexia (40%), anosmia (5%), and ageusia (5%), although the epidemiology may be different in milder outpatient presentations. Nasal epithelial cells display the highest expression of ACE2 (the receptor for SARS-CoV-2) in the respiratory tree; this may account for the symptoms of altered sense of taste or smell frequently reported retrospectively in the majority of outpatients with COVID-19. HOIP:HOIP_0041143 angiotensin signaling is a process that a signal is transmitted by angiotensin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 angiotensin signaling in COVID-19 in renal system HOIP_0041143 PMID:33077917 ACE2 internalization following SARS-CoV-2 infection could induce an imbalance in the renin–angiotensin–aldosterone system, with increased Ang II signalling leading to pro-inflammatory and profibrotic processes in the kidney. HOIP:HOIP_0041144 Inflammatory response in nervous system is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. neuroinflammtion in COVID-19 in nervous system HOIP_0041144 HOIP:HOIP_0041145 Brain vasculature damage is a subtype of damaging: A process that injures the structure of the brain vasculature as the direct or indirect result of an external force. brain vasculature damage HOIP_0041145 HOIP:HOIP_0041146 Brain blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform brain blood vessel function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 brain blood vessel disorder in COVID-19 associated with cerebral infarction HOIP_0041146 PMID:32629875 COVID-19, however, appears to include an evolving set of clinical manifestation not previously reported in SARS and MERS, including stroke and cardiomyopathies associated with coagulopathy and vasculopathy, which can cause sudden death and other serious morbidities. Oxley et al. reported on a small case series of five 33 to 50-year-old patients who presented with ischemic stroke during a two-week period (from March 23 to April 7, 2020) in a single center in New York City, and who were subsequently diagnosed with SARS-CoV-2 infection. In a subsequent prospective series over the following month involving a group of New York City Hospitals, the age range of ten SARS-CoV-2-infected patients presenting with stroke had broadened to include patients 27 to 75 years old. In a retrospective single-center study in Brescia, Italy, among neurological patients admitted in March, those diagnosed with COVID-19 (56 patients) were significantly more likely to have been admitted for stroke and transient ischemic attack (TIA) than those without the diagnosis of COVID-19 (117 patients), perhaps in part because the COVID-19 patients were older. In addition, a retrospective analysis on 214 patients hospitalized with COVID-19 in Wuhan found that acute cerebrovascular disease was present in one of 126 patients with non-severe COVID-19 and in five of 88 patients with severe COVID-19. Furthermore, histological examination of 20 brains from COVID-19 autopsies revealed the presence of anoxic brain injury in two patients with the clinical diagnosis of stroke. HOIP:HOIP_0041147 Blood brain barrier damage is a subtype of damaging: A process that injuries the structure of the blood brain barrier as the direct or indirect result of an external force. blood brain barrier damage HOIP_0041147 HOIP:HOIP_0041148 Brain microvascular dysfunction is a subtype of organ malfunction: A process that does not perform microvascular function correctly or not functioning at all in the brain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. bain microvascular dysfunction in COVID-19 associated with cerebral infarction HOIP_0041148 HOIP:HOIP_0041149 Edema in white matter of occipital lobe is a subtype of edema: A process that keeps an excessive fluid in cells or intercellular tissues of white matter of occipital lobe. edema (process) in white matter of occipital lobe HOIP_0041149 HOIP:HOIP_0041150 Vacuolar degeneration in kidney is a subtype of vacuolar degeneration: A process that degenerates vacuole. vacuolar degeneration in kidney HOIP_0041150 HOIP:HOIP_0041151 Multi-organ dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete multi-organ function. multi-organ dysfunction HOIP_0041151 HOIP:HOIP_0041153 The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 neutrophil activation involved in inflammatory response (very high) in COVID-19 associated with ARDS HOIP_0041153 PMID:33077917 Infiltrating, activated neutrophils produce large amounts of histotoxic mediators, including reactive oxygen species, as well as NETs, which have been found in arterial microthrombi in the post-mortem lung specimens from four deceased patients with COVID-19. A new study has also indicated that neutrophil activation and the formation of neutrophil extracellular traps (NETs) may have a prominent role in propagating the severe cytokine release observed in severe cases of COVID-19, representing a previously unrecognized, but powerful innate defence response that may exacerbate lung damage in affected patients. HOIP:HOIP_0041154 Thrombus formation in brain is a subtype of thrombus formation: A process that construcs thrombus in brain. thrombus formation in brain HOIP_0041154 HOIP:HOIP_0041155 Increasing vascular permeabilization in brain is a subtype of increasing vascular permeabilization : A process that changes the permeability of the vascular to be higher in brain. increasing vascular permeabilization in brain HOIP_0041155 HOIP:HOIP_0041156 Conjunctival congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the conjunctiva. conjunctival congestion HOIP_0041156 HOIP:HOIP_0041157 The chemical reaction resulting in the formation of reactive oxygen species in lung, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 reactive oxygen species biosynthetic process in lung (very high) in COVID-19 associated with ARDS HOIP_0041157 PMID:33077917 Infiltrating, activated neutrophils produce large amounts of histotoxic mediators, including reactive oxygen species, as well as NETs, which have been found in arterial microthrombi in the post-mortem lung specimens from four deceased patients with COVID-19. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0041158 Conjunctival congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the conjunctiva. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 conjunctival congestion in COVID-19 HOIP_0041158 PMID:32651579 Ocular manifestations, such as conjunctival congestion alone, conjunctivitis, and retinal changes, have also been reported in patients with COVID-19. HOIP:HOIP_0041159 Increasing vascular permeabilization in brain is a subtype of increasing vascular permeabilization : A process that changes the permeability of the vascular to be higher in brain. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. increasing vascular permeabilization in brain in COVID-19 in nervous system HOIP_0041159 HOIP:HOIP_0041161 Conjunctivitis dependent process is a subtype of disease course dependent process: A process that can constitute the course of conjunctivitis. conjunctivitis dependent process HOIP_0041161 HOIP:HOIP_0041163 Inflammatory response in conjunctiva is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in conjunctiva HOIP_0041163 HOIP:HOIP_0041164 Inflammatory response in conjunctiva is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 inflammatory response in conjunctiva in COVID-19 HOIP_0041164 PMID:32651579 Ocular manifestations, such as conjunctival congestion alone, conjunctivitis, and retinal changes, have also been reported in patients with COVID-19. HOIP:HOIP_0041165 Inflammatory response in conjunctiva is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of conjunctivitis. inflammatory response in conjunctiva [conjunctivitis] HOIP_0041165 HOIP:HOIP_0041166 Retinal damage is a subtype of damaging: A process that injuries the structure of the retina as the direct or indirect result of an external force. retinal damage HOIP_0041166 HOIP:HOIP_0041167 Demyelinating polyneuropathy dependent process is a subtype of disease course dependent process: A process that can constitute the course of demyelinating polyneuropathy. demyelinating polyneuropathy dependent process HOIP_0041167 HOIP:HOIP_0041168 The totality of all processes through which a given demyelinating polyneuropathy instance is realized. demyelinating polyneuropathy course HOIP_0041168 HOIP:HOIP_0041169 Myelin sheath damage is a subtype of organ damage: A process that injuries the structure of the myelin sheath as the direct or indirect result of an external force. myelin sheath damage HOIP_0041169 HOIP:HOIP_0041170 Leaking fluid from blood vessel is a subtype of leaking: A process that leaks fluid out from the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. leaking fluid from blood vessel in COVID-19 in nervous system HOIP_0041170 HOIP:HOIP_0041171 Myelin sheath damage is a subtype of damaging: A process that injuries the structure of the myelin sheath as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of demyelinating polyneuropathy. myelin sheath damage [demyelinating polyneuropathy course] HOIP_0041171 HOIP:HOIP_0041172 Endothelium damage in brain is a subtype of endothelium damage: A process that injuries the structure of the endothelium in brain as the direct or indirect result of an external force. endothelium damage in brain HOIP_0041172 HOIP:HOIP_0041173 Retinal damage is a subtype of damaging: A process that injuries the structure of the retina as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32651579 retinal damage in COVID-19 HOIP_0041173 PMID:32651579 Ocular manifestations, such as conjunctival congestion alone, conjunctivitis, and retinal changes, have also been reported in patients with COVID-19. HOIP:HOIP_0041174 Endothelium damage in brain is a subtype of endothelium damage: A process that injuries the structure of the endothelium in brain as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32629875 Wikipedia:Posterior_reversible_encephalopathy_syndrome endothelium damage in brain in COVID-19 in nervous system HOIP_0041174 PMID:32629875 Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. Wikipedia:Posterior_reversible_encephalopathy_syndrome While the precise mechanism is PRES is not fully understood, it is considered to be related to a problem with the blood vessels of the brain. There are several theories as to why these blood vessels may become inappropriately permeable and allow the surrounding brain tissue to become swollen. The excessive pressure damages the endothelial layer and the blood-brain barrier, leading to swelling (edema). There appears to be a role of cytokines in causing endothelial dysfunction HOIP:HOIP_0041175 Dysregulation of heartbeats is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of heartbeats appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. cardiac arrhythmias dysregulation of heartbeats [myocardial infarction course] HOIP_0041175 HOIP:HOIP_0041176 Dysregulation of heartbeats is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of heartbeats appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. cardiac arrhythmias dysregulation of heartbeats [cardiomyopathy course] HOIP_0041176 HOIP:HOIP_0041177 In response to several stimuli, neutrophils and eosinophils can release the so-called neutrophil extracellular traps (NETs), that is, microbicidal structures composed of nuclear chromatin, histones and granular antimicrobial proteins. Netotic cells exhibit massive vacuolization of the cytoplasm, rapid chromatin decondensation and breakdown of both the nuclear and granular membranes, which is required for proper NET formation. Netosis is insensitive to caspase inhibitors and necrostatin-1, further demonstrating that it constitutes a cell death subroutine distinct from apoptosis and regulated necrosis. Netosis might be defined as a cell death subroutine that is: (i) restricted to granulocytic cells; (ii) insensitive to (and perhaps dependent on)163 caspase inhibition; (iii) insensitive to necrostatin; (iv) dependent on NAPDH oxidase-mediated superoxide generation; and (v) dependent on (components of) the autophagic machinery https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:28792873 PMID:33077917 PMID:33214651 PMID:33214719 netosis in lung in COVID-19 associated with ARDS HOIP_0041177 PMID:33077917 A new study has also indicated that neutrophil activation and the formation of neutrophil extracellular traps (NETs) may have a prominent role in propagating the severe cytokine release observed in severe cases of COVID-19, representing a previously unrecognized, but powerful innate defence response that may exacerbate lung damage in affected patients. Infiltrating, activated neutrophils produce large amounts of histotoxic mediators, including reactive oxygen species, as well as NETs, which have been found in arterial microthrombi in the post-mortem lung specimens from four deceased patients with COVID-19. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. PMID:33214651 Neutrophil extracellular traps (NETs) have been shown to trigger thromboinflammation in patients with COVID-19, leading to vascular thrombosis and a high risk of death. PMID:33214719 Neutrophils entrapped inside inflamed pulmonary vessels can produce neutrophil extracellular traps (NETs) in a process termed ‘NETosis’, and these are thought to capture viral particles and thereby restrict viral dissemination63. However, NETosis can also aggravate damage to the pulmonary endothelia and epithelia in severe influenza-induced pneumonia64. NETs also activate the extrinsic and intrinsic coagulation pathway HOIP:HOIP_0041178 Myocardial damage is a subtype of damaging: A process that injuries the structure of the myocardial muscle as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. myocardial damage [cardiomyopathy course] HOIP_0041178 HOIP:HOIP_0041179 Increasing troponin concentration is a subtype of increasing concentration: A process that changes the troponin concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. Increasing troponin concentration [cardiomyopathy coursey] HOIP_0041179 HOIP:HOIP_0041180 Livedoid vasculitis dependent process is a subtype of disease course dependent process: A process that can constitute the course of livedoid vasculitis. livedoid vasculitis dependent process HOIP_0041180 HOIP:HOIP_0041182 Inflammatory response in blood vessels is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in blood vessels HOIP_0041182 HOIP:HOIP_0041183 Inflammatory response in blood vessels is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32651579 inflammatory response in blood vessels (very high) in severe COVID-19 HOIP_0041183 PMID:32651579 Other cutaneous findings included maculopapular rash, vesicular lesions, and livedoid and/or necrotic lesions. A transverse study included in this systematic review found chilblain-like lesions to be associated with less-severe COVID-19, while livedoid and/or necrotic lesions were seen in more-severe COVID-19. Biopsy of acrocutaneous lesions has shown diffuse and dense lymphoid infiltrates, along with signs of endothelial inflammation. HOIP:HOIP_0041184 Inflammatory response in blood vessels is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of livedoid vasculitis. inflammatory response in blood vessels [livedoid vasculitis] HOIP_0041184 HOIP:HOIP_0041185 A type of cutaneous cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. cutaneous cell necrosis HOIP_0041185 HOIP:HOIP_0041187 The appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 chemokine production (very high) in COVID-19 associated with ARDS HOIP_0041187 PMID:33077917 A further elegant single-cell RNA sequencing study confirmed an enrichment of SARS-CoV-2 RNA in the lung macrophage population of infected patients, and differential gene expression analysis revealed that infected macrophages had higher chemokine expression than non-infected macrophages. HOIP:HOIP_0041188 The movement of a lymphocyte into skin. lymphocyte migration into skin HOIP_0041188 HOIP:HOIP_0041191 The regulated release of bradykinin by a cell or tissue. bradykinin secretion HOIP_0041191 HOIP:HOIP_0041193 Moving blood clot is a subtype of moving. A process that change the location of the blood clot. This entity is a specific course-dependent process. This process can constitute the course of pulmonary embolism. moving blood clot [pulmonary embolism course] HOIP_0041193 HOIP:HOIP_0041194 Any process that activates or increases the frequency, rate or extent of thrombus formation in lung. positive regulation of thrombus formation in lung HOIP_0041194 HOIP:HOIP_0041195 Any process that activates or increases the frequency, rate or extent of thrombus formation in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 positive regulation of thrombus formation in lung in COVID-19 associated with ARDS HOIP_0041195 PMID:33077917 Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. HOIP:HOIP_0041196 The migration of a neutrophil from the blood vessels into the lung tissues. neutrophil extravasation in lung HOIP_0041196 HOIP:HOIP_0041197 Lung malfunction is a subtype of organ malfunction: A process that does not perform lung function correctly or not functioning at all. lung malfunction HOIP_0041197 HOIP:HOIP_0041198 Lung malfunction is a subtype of organ malfunction: A process that does not perform lung function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32651579 lung malfunction in COVID-19 associated with ARDS HOIP_0041198 PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. HOIP:HOIP_0041199 Neutrophil extracellular trap formation in lung is a subtype of neutrophil extracellular trap formation: A process that construcs neutrophil extracellular trap in lung. neutrophil extracellular trap formation in lung HOIP_0041199 HOIP:HOIP_0041200 In response to several stimuli, neutrophils and eosinophils can release the so-called neutrophil extracellular traps (NETs), that is, microbicidal structures composed of nuclear chromatin, histones and granular antimicrobial proteins. Netotic cells exhibit massive vacuolization of the cytoplasm, rapid chromatin decondensation and breakdown of both the nuclear and granular membranes, which is required for proper NET formation. Netosis is insensitive to caspase inhibitors and necrostatin-1, further demonstrating that it constitutes a cell death subroutine distinct from apoptosis and regulated necrosis. Netosis might be defined as a cell death subroutine that is: (i) restricted to granulocytic cells; (ii) insensitive to (and perhaps dependent on)163 caspase inhibition; (iii) insensitive to necrostatin; (iv) dependent on NAPDH oxidase-mediated superoxide generation; and (v) dependent on (components of) the autophagic machinery https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ PMID:24009232 netosis in lung HOIP_0041200 HOIP:HOIP_0041201 Any process involved in the activation of any of the steps of the classical pathway of the complement cascade which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 complement activation, classical pathway (very high) in COVID-19 associated with ARDS HOIP_0041201 PMID:33077917 In line with these findings, immunohistochemistry analyses in post-mortem lung tissue from SARS-CoV-2-infected patients revealed high expression of the complement components MBL, C4, C3 and C5b–9, in alveolar epithelial cells and pneumocytes, as well as in inflammatory cells, as reported by a preprint study. HOIP:HOIP_0041202 The chemical reaction resulting in the formation of reactive oxygen species in lung, any molecules or ions formed by the incomplete one-electron reduction of oxygen. reactive oxygen species biosynthesis reactive oxygen species formation reactive oxygen species synthesis reactive oxygen species synthesis reactive oxygen species biosynthetic process in lung HOIP_0041202 reactive oxygen species synthesis PMID:24252804 HOIP:HOIP_0041204 Expression of PDCD1 is a subtype of gene expression: The process in which a gene sequence is converted into a mature PDCD1 gene product or products (proteins or RNA). Expression of PDCD1 HOIP_0041204 HOIP:HOIP_0041205 Expression of PDCD1 is a subtype of gene expression: The process in which a gene sequence is converted into a mature PDCD1 gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 Expression of PDCD1 (very high) in severe COVID-19 HOIP_0041205 PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. HOIP:HOIP_0041207 Increasing body temperature is a subtype of increaseing temperature: A process that increases the temperature of the body. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation increasing body temperature in COVID-19 HOIP_0041207 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0041208 Negative regulation of cytotoxicity is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the cytotoxicity. negative regulation of cytotoxicity HOIP_0041208 HOIP:HOIP_0041209 Negative regulation of T cell mediated cytotoxicity is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the T cell mediated cytotoxicity. negative regulation of T cell mediated cytotoxicity HOIP_0041209 HOIP:HOIP_0041210 Negative regulation of natural killer cell mediated cytotoxicity is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the natural killer cell cytotoxicity. negative regulation of natural killer cell mediated cytotoxicity HOIP_0041210 HOIP:HOIP_0041211 Negative regulation of natural killer cell mediated cytotoxicity is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the natural killer cell cytotoxicity. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 negative regulation of natural killer cell mediated cytotoxicity in severe COVID-19 HOIP_0041211 PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. Similarly, NK cells exhibit increased levels of the inhibitory CD94–NK group 2 member A (NKG2A). Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0041212 Negative regulation of T cell mediated cytotoxicity is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the T cell mediated cytotoxicity. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 negative regulation of T cell mediated cytotoxicity in severe COVID-19 HOIP_0041212 PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0041213 Negative regulation of natural killer cell mediated immunity is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the natural killer cell mediated immunity. Negative regulation of natural killer cell mediated immunity HOIP_0041213 HOIP:HOIP_0041214 Negative regulation of natural killer cell mediated immunity is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the natural killer cell mediated immunity. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 Negative regulation of natural killer cell mediated immunity in severe COVID-19 HOIP_0041214 PMID:33077917 Increased numbers of exhausted T cells that express high levels of programmed cell death protein 1 (PD1), suggest decreased proliferation and activity of CD8+ T cells. Similarly, NK cells exhibit increased levels of the inhibitory CD94–NK group 2 member A (NKG2A). Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0041216 Any process that decreases the frequency, rate, or extent of neutrophil activation involved in immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 negative regulation of neutrophil activation involved in immune response in COVID-19 in patient with diabetes HOIP_0041216 PMID:30510205 Obesity and type 2 diabetes mellitus (T2DM) are associated to worsen outcomes and mortality caused by infection. The main cause of this vulnerability is the impaired innate immune functions in these two conditions, such as phagocytosis, cytokine and reactive oxygen species (ROS) production, bactericidal activity and chemotaxis. HOIP:HOIP_0041219 Cardiac blood vessel dysfunction is a subtype of vascular malfunction: A process that does not perform cardiac blood vessel function correctly or not functioning at all. cardiac blood vessel dysfunction HOIP_0041219 HOIP:HOIP_0041220 A protein that is a translation product of the human VCAM1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7412 NCBI-Mouse-GeneID:22329 NCBI-Rat-GeneID:25361 CD106 INCAM-100 V-CAM 1 VCAM 1 vascular cell adhesion protein 1 HOIP_0041220 NCBI-Human-GeneID:7412 http://www.ncbi.nlm.nih.gov/gene/7412 NCBI-Mouse-GeneID:22329 http://www.ncbi.nlm.nih.gov/gene/22329 NCBI-Rat-GeneID:25361 http://www.ncbi.nlm.nih.gov/gene/25361 HOIP:HOIP_0041223 Expression of cell adhesion molecule expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature cell adhesion molecule gene product or products (proteins or RNA). cell adhesion molecule expression HOIP_0041223 HOIP:HOIP_0041224 Expression of cell adhesion molecule expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature cell adhesion molecule gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 cell adhesion molecule expression (very high) in severe COVID-19 HOIP_0041224 PMID:33077917 Mechanistically, disruption of the endothelial barrier by SARS-CoV-2 spike protein is mediated by changes in the surface expression of intracellular adhesion molecule-1 (ICAM1), vascular cell adhesion protein-1 (VCAM1) and the tight junction scaffold protein zonula occludens-1 (ZO-1), as reported by a preprint study. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0041225 Any process that activates or increases the frequency, rate or extent of cell adhesion. positive regulation of cell adhesion HOIP_0041225 HOIP:HOIP_0041227 Expression of cell adhesion molecule expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature cell adhesion molecule gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 cell adhesion molecule expression (very high) in COVID-19 associated with ARDS HOIP_0041227 PMID:33077917 C5a may represent an alternative therapeutic target. C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma — pathological events that are all observed in severe cases of COVID-19. HOIP:HOIP_0041228 Any process that activates or increases the frequency, rate or extent of cell adhesion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 positive regulation of cell adhesion in COVID-19 associated with ARDS HOIP_0041228 PMID:33077917 C5a may represent an alternative therapeutic target. C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma — pathological events that are all observed in severe cases of COVID-19. HOIP:HOIP_0041229 The movement of a mononuclear cell into myocardium. mononuclear cell migration into myocardium HOIP_0041229 HOIP:HOIP_0041230 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot in coronary artery; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. blood coagulation in coronary artery HOIP_0041230 HOIP:HOIP_0041231 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot in coronary artery; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). blood coagulation in coronary artery in COVID-19 associated with ACS HOIP_0041231 HOIP:HOIP_0041232 Decreasing myocardial blood flow is a subtype of decreasing flow: A process that changes the amount of myocardial blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32651579 decreasing myocardial blood flow in COVID-19 associated with ACS HOIP_0041232 PMID:32651579 There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. HOIP:HOIP_0041233 Kidney congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the Kidney. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32416769 renal congestion kidney congestion in COVID-19 in cardiovascular system HOIP_0041233 PMID:32416769 Cardiorenal syndrome, particularly right ventricular failure secondary to COVID-19 pneumonia, might lead to kidney congestion and subsequent AKI. HOIP:HOIP_0041234 Increasing blood pressure in lung is a subtype of increasing blood pressure : A process that changes the blood pressure to be higher in lung. This entity is a specific course-dependent process. This process can constitute the course of acute cor pulmonale. Wikipedia:Pulmonary_heart_disease increasing vascular pressure in lung increasing blood pressure in lung [acute cor pulmonale] HOIP_0041234 Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. HOIP:HOIP_0041235 Right ventricular damage is a subtype of damaging: A process that injuries the structure of the right ventricular as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32651579 Wikipedia:Pulmonary_heart_disease right ventricular damage in COVID-19 associated with ARDS HOIP_0041235 PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. HOIP:HOIP_0041236 Pulmonary alveolar edema is a subtype of pulmonary edema: A process that keeps fluids in the pulmonary alveolus. 肺水腫 pulmonary alveolar edema HOIP_0041236 HOIP:HOIP_0041237 The regulated release of a collagenase from a cell or a tissue. collagenase secretion HOIP_0041237 HOIP:HOIP_0041238 Inflammatory response in myocardium is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. inflammatory response in myocardium [cardiomyopathy course] HOIP_0041238 HOIP:HOIP_0041239 Inflammatory response of myocardial capillary is a subtype of Inflammatory response in blood vessels: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in myocardial capillary HOIP_0041239 HOIP:HOIP_0041242 Myocardium malfunction is a subtype of malfunctioning process: A process that cannot perform signaling [biological] appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. myocardium malfunction [cardiomyopathy course] HOIP_0041242 HOIP:HOIP_0041243 Increasing temperature is a subtype of changing temperature: A process that increases the temperature of the object. increasing temperature HOIP_0041243 HOIP:HOIP_0041244 Systemic inflammatory response is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32690910 Systemic inflammatory response in COVID-19 associated with myocarditis HOIP_0041244 PMID:32690910 However, on the basis of the available clinical evidence, myocardial injury seems to be largely attributable to advanced systemic inflammation. HOIP:HOIP_0041246 Tubular epithelial cells injury is a subtype of cellular damage: A process that injuries the structure of tubular epithelial cell. tubular epithelial cell injury HOIP_0041246 HOIP:HOIP_0041247 A type of renal cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. renal cell necrosis HOIP_0041247 HOIP:HOIP_0041248 Narrowing of the coronary artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the coronary arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. coronary artery narrowing [cardiomyopathy course] HOIP_0041248 HOIP:HOIP_0041249 Decreasing blood is a subtype of decreasing quantity: A process that changes the quantity of the blood to be lower. hypovolaemia decreasing blood HOIP_0041249 HOIP:HOIP_0041250 A type of myocardial cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. myocardial cell necrosis [cardiomyopathy course] HOIP_0041250 HOIP:HOIP_0041252 Decreasing oral intake is a subtype of decreasing quantity: A process that changes the quantity of the oral (food) intake to be lower. decreasing oral intake HOIP_0041252 HOIP:HOIP_0041253 Myocardial Ischemia is a changing process to lack enough to blood supply of Myocardium. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. myocardial ischemia [cardiomyopathy course] HOIP_0041253 HOIP:HOIP_0041254 A type of nephron tubule epithelial cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 nephron tubule epithelial cell necrosis in COVID-19 in renal system HOIP_0041254 PMID:33077917 SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041258 Increasing temperature is a subtype of changing temperature: A process that increases the temperature of the object. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation heat increasing temperature in COVID-19 HOIP_0041258 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041259 Increasing demand for response to oxidative stress in myocardium is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher in myocardium. increasing demand for response to oxidative stress in myocardium HOIP_0041259 HOIP:HOIP_0041260 Any process involved in the activation of any of the steps of the lectin pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 complement activation, lectin pathway (very high)in COVID-19 associated with ARDS HOIP_0041260 PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. In line with these findings, immunohistochemistry analyses in post-mortem lung tissue from SARS-CoV-2-infected patients revealed high expression of the complement components MBL, C4, C3 and C5b–9, in alveolar epithelial cells and pneumocytes, as well as in inflammatory cells, as reported by a preprint study. HOIP:HOIP_0041261 Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 complement activation in COVID-19 HOIP_0041261 PMID:33077917 Insights into the pathogenic mechanisms underlying SARS-CoV-2 infection and COVID-19 progression are emerging and highlight the critical role of the immunological hyper-response — characterized by widespread endothelial damage, complement-induced blood clotting and systemic microangiopathy — in disease exacerbation. HOIP:HOIP_0041264 Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 complement activation (very high) in COVID-19 associated with ARDS HOIP_0041264 PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma — pathological events that are all observed in severe cases of COVID-19. HOIP:HOIP_0041265 Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 complement activation (severe)in severe COVID-19 HOIP_0041265 PMID:33077917 Use of an ultra-high-throughput clinical proteomic approach identified consistent activation of the classical complement pathway (specifically, complement components C1R, C1S and C8A) in the sera of patients with clinically severe COVID-19, along with increased activation of the alternative pathway component, complement factor B (CFB) and its modulators CFI and CFH144. Although clinical insights into complement activation following SARS-CoV-2 infection are limited, the above findings indicate that unrestrained complement activation - mainly at the downstream terminal phases of the complement cascades - may contribute to endothelial cell injury, thrombosis and intravascular coagulation, ultimately leading to multi-systemic organ failure in patients with COVID-19. Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma — pathological events that are all observed in severe cases of COVID-19. HOIP:HOIP_0041266 PMID:32690910 The totality of all processes through which COVID-19 infection accompanied by acute coronary syndrome is realized. COVID-19 course associated with acute coronary syndrome HOIP_0041266 PMID:32690910 In another study in Wuhan involving 187 patients hospitalized with COVID-19, those with elevated levels of troponin T were more likely to develop malignant arrhythmias, such as ventricular tachycardia and fibrillation, than those with normal levels of troponin T (12% versus 5%). HOIP:HOIP_0041267 The regulated release of a collagenase from a cell or a tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 collagenase secretion in COVID-19 associated with ACS HOIP_0041267 PMID:32690910 For example, activated macrophages secrete collagenases that degrade collagen, a major constituent of the fibrous cap on atherosclerotic plaques, which can lead to plaque rupture. HOIP:HOIP_0041269 The totality of all processes through which COVID-19 infection with diabetes is realized. COVID-19 course in patient with diabetes HOIP_0041269 HOIP:HOIP_0041270 Positive regulation of ACE2 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of ACE2 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 positive regulation of ACE2 gene expression (very high) in COVID-19 in patient with diabetes HOIP_0041270 PMID:32694793 In people with T2D, ACE2 expression is elevated in multiple target tissues of SARS-CoV-2, and this elevation has been proposed to be an adaptive mechanism that protects the body against diabetes-associated physiological dysfunction. This increased expression may enhance SARS-CoV-2’s entry and subsequent replication, as well as its spread within the body in individuals with T2D. HOIP:HOIP_0041271 Malfunctioning of glucose metabolism is a subtype of malfunctioning of metabolism process: A process that cannot perform a glucose metabolism appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32651579 malfunctioning of glucose metabolism in COVID-19 in patient with diabetes HOIP_0041271 PMID:32651579 Moreover, patients hospitalized with COVID-19 have exhibited a range of abnormalities of glucose metabolism, including worsened hyperglycemia, euglycemic ketosis, and classic diabetic ketoacidosis. HOIP:HOIP_0041272 Any process that activates or increases the frequency, rate or extent of the inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 PMID:32694793 PMID:33188364 positive regulation of inflammatory response (very high) in COVID-19 in patient with diabetes HOIP_0041272 PMID:32687793 Obesity and diabetes are characterised by chronic low-grade inflammation with increased concentrations of pro-inflammatory leptin and reduced anti-inflammatory adiponectin. PMID:32694793 Metabolic syndrome and T2D are chronic inflammatory states (Fig. 2). Because the severe and critical phases of COVID-19 are driven by an excessive inflammatory response to the infection (cytokine storm), the heightened baseline inflammatory state in patients with preexisting compromised metabolic health may increase the likelihood that the inflammatory response will reach pathogenic levels, as well as the likelihood of physiological damage20 (Fig. 2). PMID:33188364 As described already, glucotoxicity, endothelial damage by inflammation, oxidative stress and cytokine production contribute to an increased risk of thromboembolic complications and of damage to vital organs in patients with diabetes mellitus (fig. 1). Patients with COVID-19 also exhibit elevation of other inflammatory markers, such as D-dimer, ferritin and IL-6, which might contribute to an increased risk of microvascular and macrovascular complications originating from low-grade vascular inflammation in patients with underlying diabetes mellitus. HOIP:HOIP_0041273 Any process that stops, prevents, or reduces the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 PMID:32687793 PMID:32694793 Negative regulation of immune response in COVID-19 in patient with diabetes HOIP_0041273 PMID:30510205 Diabetes and obesity, due to hyperglycemia and high concentrations of plasma free fatty acids, are known to pre-activate leukocytes and lead them to a pro-inflammatory phenotype. This chronic stimulus by the altered metabolic state in these diseases may lead to the appearance of tolerant or “burned-out” leukocytes that are not able to fully respond to an infectious stimulus, allowing the microorganism to disseminate. PMID:32687793 Moreover, individuals with obesity have lower vitamin D concentrations, which could also reduce the immune response. PMID:32694793 For example, individuals with metabolic syndrome and T2D have impaired immune function in general, and their antiviral response against SARS-CoV-2 may consequently be impaired. HOIP:HOIP_0041274 Any process that decreases the frequency, rate, or extent of neutrophil mediated cytotoxicity. negative regulation of neutrophil mediated cytotoxicity HOIP_0041274 HOIP:HOIP_0041276 Pulmonary alveolar edema is a subtype of pulmonary edema: A process that keeps fluids in the pulmonary alveolus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). 肺水腫 pulmonary alveolar edema in COVID-19 associated with ARDS HOIP_0041276 HOIP:HOIP_0041279 Decreasing blood pressure is a subtype of decreasing pressure: A process that changes the blood pressure to be lower. decreasing vascular pressure decreasing blood pressure HOIP_0041279 HOIP:HOIP_0041284 A change in morphology and behavior of a tissue-resident leukocyte resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor. Wikipedia:Inflammation tissue-resident immune cell activation tissue-resident leukocyte activation HOIP_0041284 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0041286 The transport of a virus between tissues in a multicellular organism. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 spread of virus within host, tissue to tissue tissue to tissue spread of virus within host transport of virus in host, tissue to tissue in COVID-19 HOIP_0041286 PMID:32629875 However, hematogenous dissemination of the virus (discussed in Section 4.1) is more likely to explain the presumed presence of viral particles in the endothelial cells distant from the lungs, such as the renal glomerulus. HOIP:HOIP_0041287 The regulated release of inflammatory mediators from tissue-resident immune cells. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation release of inflammatory mediator from tissue-resident immune cells in COVID-19 HOIP_0041287 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041289 Increasing vascular lumen area is a subtype of increasing area: A process that changes the area of the vascular lumen area to be larger. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation Vasodilation 血管拡張 increasing vascular lumen area in COVID-19 HOIP_0041289 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041290 Increasing flow is a subtype of increaseing quantity: A process that changes the amount of flow to be higher. increasing flow HOIP_0041290 HOIP:HOIP_0041291 Increasing blood flow is a subtype of increaseing flow: A process that changes the amount of blood flow to be higher. Wikipedia:Inflammation Increasing blood flow HOIP_0041291 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041292 Increasing blood flow is a subtype of increaseing flow: A process that changes the amount of blood flow to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation increasing blood flow in COVID-19 HOIP_0041292 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041293 Edema is a subtype of accumulation of fluids: A process that keeps an excessive fluid in cells or intercellular tissues. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. HP:0000969 edema (process) in COVID-19 HOIP_0041293 HP:0000969 Edema may be related to one or more of the following factors: 1) increased capillary hydrostatic pressure, 2) decreased osmotic pressure of plasma, 3) decreased tissue tension and lymphatic drainage, 4) increased osmotic pressure of tissue fluids, and 5) increased capillary permeability. HOIP:HOIP_0041296 A change in morphology and behavior of a tissue-resident leukocyte resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation tissue-resident immune cell activation tissue-resident leukocyte activation in COVID-19 HOIP_0041296 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0041299 The movement of a macrophage in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. macrophage chemotaxis in COVID-19 HOIP_0041299 HOIP:HOIP_0041300 The orderly movement of a monocyte from one site to another. monocyte migration HOIP_0041300 HOIP:HOIP_0041301 The movement of a macrophage in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. macrophage chemotaxis (very high) in severe COVID-19 HOIP_0041301 HOIP:HOIP_0041302 The migration of a neutrophil from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 PMID:33123165 neutrophil extravasation in COVID-19 HOIP_0041302 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0041304 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32307653 PMID:32697943 PMID:33123165 macrophage cell differentiation macrophage differentiation in COVID-19 HOIP_0041304 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. ISBN:0781735149 PMID:32307653 Some regions of reactive epithelial hyperplasia had also abundant alveolar macrophages. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32697943 Upon infection, there is an accumulation of immune cells in the lungs, especially macrophages and monocytes. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0041306 The migration of a monocyte from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 PMID:32697943 monocyte extravasation (very high) in COVID-19 associated with ARDS HOIP_0041306 PMID:32307653 Some regions of reactive epithelial hyperplasia had also abundant alveolar macrophages. In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. PMID:32697943 Upon infection, there is an accumulation of immune cells in the lungs, especially macrophages and monocytes. HOIP:HOIP_0041307 Interaction between viral protein (or viral protein complex) and host complement activation protein (or host complement activation protein complex). This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 viral protein-host complement activation protein binding in COVID-19 associated with ARDS HOIP_0041307 PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. HOIP:HOIP_0041308 The migration of a monocyte from the blood vessels into kidney. monocyte extravasation into kidney HOIP_0041308 HOIP:HOIP_0041310 A change in morphology and behavior of a tissue-resident leukocyte resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation tissue-resident immune cell activation tissue-resident leukocyte activation (very high) in severe COVID-19 HOIP_0041310 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0041312 The regulated release of inflammatory mediators from tissue-resident immune cells. Wikipedia:Inflammation release of inflammatory mediator from tissue-resident immune cells HOIP_0041312 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041313 The synthesis or release of any molecular mediator of the inflammatory response following an inflammatory stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation synthesis or release of inflammatory mediator in COVID-19 HOIP_0041313 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041316 The migration of a T cell from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. T cell extravasation in COVID-19 HOIP_0041316 HOIP:HOIP_0041317 The migration of a T cell from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. T cell extravasation in severe COVID-19 HOIP_0041317 HOIP:HOIP_0041318 Leaking fluid from blood vessel is a subtype of leaking: A process that leaks fluid out from the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. leaking fluid from blood vessel in COVID-19 HOIP_0041318 HOIP:HOIP_0041319 The directed movement of a T cell in response to an external stimulus. A T cell is a type of lymphocyte whose defining characteristic is the expression of a T cell receptor complex. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 T cell chemotaxis in COVID-19 HOIP_0041319 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0041320 The directed movement of a T cell in response to an external stimulus. A T cell is a type of lymphocyte whose defining characteristic is the expression of a T cell receptor complex. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 T cell chemotaxis (severe)in severe COVID-19 HOIP_0041320 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0041322 The movement of a monocyte in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 monocyte chemotaxis in COVID-19 HOIP_0041322 PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell. HOIP:HOIP_0041329 Decreasing myocardial blood flow is a subtype of decreasing flow: A process that changes the amount of myocardial blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. decreasing myocardial blood flow [cardiomyopathy course] HOIP_0041329 HOIP:HOIP_0041330 Increasing volume of myocardium is a subtype of increasing volume: A process that changes the volume of the myocardium to be higher. This entity is a specific course-dependent process. This process can constitute the course of cardiomyopathy. increasing volume of myocardium [cardiomyopathy course] HOIP_0041330 HOIP:HOIP_0041333 Expression of cell adhesion molecule expression is a subtype of gene expression: The process in which a gene sequence is converted into a mature cell adhesion molecule gene product or products (proteins or RNA). This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 cell adhesion molecule expression in COVID-19 HOIP_0041333 PMID:33077917 Mechanistically, disruption of the endothelial barrier by SARS-CoV-2 spike protein is mediated by changes in the surface expression of intracellular adhesion molecule-1 (ICAM1), vascular cell adhesion protein-1 (VCAM1) and the tight junction scaffold protein zonula occludens-1 (ZO-1), as reported by a preprint study. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0041334 The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 neutrophil activation involved in inflammatory response in COVID-19 HOIP_0041334 PMID:33077917 Impaired cytotoxic activity results in persistent viral shedding that amplifies macrophage and neutrophil activation, leading to the massive production of cytokines (a process referred to as hypercytokinaemia). HOIP:HOIP_0041337 Neutrophil clearance insufficiency is a subtype of insufficient functioning: A process that lacks performing the function of neutrophil clearance required. neutrophil clearance insufficiency HOIP_0041337 HOIP:HOIP_0041338 Any process that activates or increases the frequency, rate or extent of cell adhesion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 positive regulation of cell adhesion in COVID-19 HOIP_0041338 PMID:33077917 Mechanistically, disruption of the endothelial barrier by SARS-CoV-2 spike protein is mediated by changes in the surface expression of intracellular adhesion molecule-1 (ICAM1), vascular cell adhesion protein-1 (VCAM1) and the tight junction scaffold protein zonula occludens-1 (ZO-1), as reported by a preprint study. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0041339 Any process that results in a change in state or activity of a cell as a result of a stimulus of pain sensation. response to pain sensation stimulus HOIP_0041339 HOIP:HOIP_0041340 Any process that results in a change in state or activity of a cell as a result of a stimulus of pain sensation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation response to pain sensation stimulus in COVID-19 HOIP_0041340 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041342 A developmental process, independent of morphogenetic (shape) change, that is required for a platelet to attain its fully functional state. A platelet is a non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 platelet maturation in COVID-19 HOIP_0041342 PMID:32629875 Acting on hepatocytes, IL-6 promotes the synthesis of fibrinogen, tissue factor and Factor VII. It also stimulates platelet production in the bone marrow. Thus, IL-6 can promote a pro-coagulant and pro-thrombotic vascular pathology, raising the possibility that an abnormally high level of IL-6 may contribute to the vascular phenotype in severe COVID-19. HOIP:HOIP_0041343 The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 natural killer cell mediated cytotoxicity in COVID-19 HOIP_0041343 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0041344 The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33123165 natural killer cell mediated cytotoxicity (very high) in severe COVID-19 HOIP_0041344 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0041345 The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 T cell mediated cytotoxicity in COVID-19 HOIP_0041345 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0041348 TNF signaling is a process that a signal is transmitted by TNF. PMID:28792873 PMID:32264791 PMID:32407672 PMID:32629875 TNF signaling in COVID-19 HOIP_0041348 PMID:28792873 PMID:28792873 Tumor necrosis factor mediated expression of tissue factor promotes platelet aggregation and microthrombus formation. PMID:32264791 Ang II increases ADAM17 activity. ADAM17 cleaves its primary substrate releasing soluble TNF-α. TNF-α along with systemic cytokines released due to SARS-CoV-2 infection and in conjunction with comorbidities such as diabetes mellitus and hypertension can lead to a cytokine storm. PMID:32407672 TNF-a and IL-1 are the main mediators drivinng a supression of endogeneous anticoagulant pathways. PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. HOIP:HOIP_0041349 Endotheliitis dependent process is a subtype of disease course dependent process: A process that can constitute the course of endotheliitis. endotheliitis dependent process HOIP_0041349 HOIP:HOIP_0041350 The totality of all processes through which a given endotheliitis instance is realized. endotheliitis course HOIP_0041350 HOIP:HOIP_0041351 Inflammatory response in endothelium is a subtype of inflammatory response in blood vessels: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammatory response in endothelium HOIP_0041351 HOIP:HOIP_0041352 Inflammatory response in endothelium is a subtype of inflammatory response in blood vessels: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. Wikipedia:Endotheliitis inflammatory response in endothelium [endotheliitis course] HOIP_0041352 Wikipedia:Endotheliitis Endotheliitis is an immune response within the endothelium in blood vessels, in which they become inflamed. The condition can cause oedema of the surrounding tissue, including the stroma, and can cause irritation and pain. HOIP:HOIP_0041353 Inflammatory response in endothelium is a subtype of inflammatory response in blood vessels: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32325026 PMID:32651579 inflammatory response in endothelium in severe COVID-19 HOIP_0041353 PMID:32325026 These findings suggest that SARS-CoV-2 infection facilitates the induction of endotheliitis in several organs as a direct consequence of viral involvement (as noted with presence of viral bodies) and of the host inflammatory response. In addition, induction of apoptosis and pyroptosis might have an important role in endothelial cell injury in patients with COVID-19. COVID-19-endotheliitis could explain the systemic impaired microcirculatory function in different vascular beds and their clinical sequelae in patients with COVID-19. PMID:32651579 Infection-mediated endothelial injury (characterized by elevated levels of von Willebrand factor) and endothelialitis (marked by the presence of activated neutrophils and macrophages), found in multiple vascular beds (including the lungs, kidney, heart, small intestine, and liver) in patients with COVID-19, can trigger excessive thrombin production, inhibit fibrinolysis, and activate complement pathways, initiating thromboinflammation and ultimately leading to microthrombi deposition and microvascular dysfunction. HOIP:HOIP_0041354 Endothelium inflammatory response in lung is a subtype of inflammatory response in endothelium: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. endothelium inflammatory response in lung HOIP_0041354 HOIP:HOIP_0041355 Any process that activates or increases the frequency, rate or extent of platelet aggregation. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules. positive regulation of platelet aggregation in COVID-19 HOIP_0041355 HOIP:HOIP_0041356 A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug. Wikipedia:Coagulation platelet activation in COVID-19 HOIP_0041356 Wikipedia:Coagulation When the endothelium is damaged, the normally isolated, underlying collagen is exposed to circulating platelets, which bind directly to collagen with collagen-specific glycoprotein Ia/IIa surface receptors. This adhesion is strengthened further by von Willebrand factor (vWF), which is released from the endothelium and from platelets; vWF forms additional links between the platelets' glycoprotein Ib/IX/V and A1 domain. Binding of collagen to glycoprotein VI triggers a signaling cascade that results in activation of platelet integrins Activated platelets release the contents of stored granules into the blood plasma. The main role of the tissue factor pathway is to generate a "thrombin burst", a process by which thrombin, the most important constituent of the coagulation cascade in terms of its feedback activation roles, is released very rapidly. HOIP:HOIP_0041357 The adhesion of one platelet to one or more other platelets via adhesion molecules. PMID:32629875 Wikipedia:Coagulation platelet aggregation in COVID-19 HOIP_0041357 PMID:32629875 Similarly, thrombi/platelet aggregates were visualized microscopically in capillaries, arterioles and medium sized arteries of most COVID-19 lungs (21/23). Wikipedia:Coagulation Activated integrins mediate tight binding of platelets to the extracellular matrix. This process adheres platelets to the site of injury. The coagulation cascade of secondary hemostasis has two initial pathways which lead to fibrin formation. These are the contact activation pathway (also known as the intrinsic pathway), and the tissue factor pathway (also known as the extrinsic pathway), which both lead to the same fundamental reactions that produce fibrin. HOIP:HOIP_0041358 Accumulation of abnormal proteins is a subtype of protein accumulation: A process that keeps Angiotensin II in a biological object. PMID:32264791 PMID:32629875 Angiotensin II accumulation in COVID-19 HOIP_0041358 PMID:32264791 Ang II levels elevate with increased activity of angiotensin 1 receptors (AT1R) at the cost of ACE2/ Ang 1–7 driven pathways leading to adverse fibrosis, hypertrophy, increased reactive oxygen species (ROS), vasoconstriction, and gut dysbiosis. PMID:32629875 However, a study in twelve patients with COVID-19 reported significantly increased plasma levels of angiotensin II, which appeared to directly correlate with circulating SARS-CoV-2 RNA levels and degree of hypoxia. HOIP:HOIP_0041359 angiotensin signaling is a process that a signal is transmitted by angiotensin. angiotensin signaling in COVID-19 HOIP_0041359 HOIP:HOIP_0041360 A decrease in the diameter of blood vessels, especially arteries, due to constriction of smooth muscle cells that line the vessels, and usually causing an increase in blood pressure. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32694793 vasoconstrictionin COVID-19 HOIP_0041360 PMID:32694793 Angiotensin II, the active RAS metabolite and a potent vasoconstrictor that increases peripheral vascular resistance, also causes insulin resistance and regulates sodium absorption in the kidneys. HOIP:HOIP_0041361 Interaction between viral protein (or viral protein complex) and host complement activation protein (or host complement activation protein complex). viral protein-host complement activation protein binding HOIP_0041361 HOIP:HOIP_0041364 Interaction between viral protein (or viral protein complex) and host complement activation protein (or host complement activation protein complex). This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 viral protein-host complement activation protein binding in COVID-19 HOIP_0041364 PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. HOIP:HOIP_0041365 Interaction between viral protein (or viral protein complex) and host complement activation protein (or host complement activation protein complex). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 viral protein-host complement activation protein binding (very high) in severe COVID-19 HOIP_0041365 PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. HOIP:HOIP_0041367 Any process involved in the activation of any of the steps of the lectin pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 complement activation, lectin pathway in COVID-19 HOIP_0041367 PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. Although clinical insights into complement activation following SARS-CoV-2 infection are limited, the above findings indicate that unrestrained complement activation - mainly at the downstream terminal phases of the complement cascades - may contribute to endothelial cell injury, thrombosis and intravascular coagulation, ultimately leading to multi-systemic organ failure in patients with COVID-19. HOIP:HOIP_0041368 Any process involved in the activation of any of the steps of the lectin pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 complement activation, lectin pathway (very high) in severe COVID-19 HOIP_0041368 PMID:33077917 Although clinical insights into complement activation following SARS-CoV-2 infection are limited, the above findings indicate that unrestrained complement activation - mainly at the downstream terminal phases of the complement cascades - may contribute to endothelial cell injury, thrombosis and intravascular coagulation, ultimately leading to multi-systemic organ failure in patients with COVID-19. Circulating levels of C5a were higher in patients with severe COVID-19 than in patients with mild disease who had levels of C5a similar to those of healthy controls. Use of an untargeted metabolomic approach also demonstrated upregulation of complement activation proteins, including membrane attack complex proteins such as C5, C6 and C8, in sera from 46 patients with severe disease. As seen in the lung, post-mortem examination of kidney specimens in a preprint study also identified deposition of C5b–9 on tubule cells and massive interstitial infiltration of macrophages as hallmarks of kidney complications in patients with severe disease. HOIP:HOIP_0041369 The release of bradykinin following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation bradykinin secretion involved in inflammatory response in COVID-19 HOIP_0041369 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Bradykinin: A vasoactive protein that is able to induce vasodilation, increase vascular permeability, cause smooth muscle contraction, and induce pain. HOIP:HOIP_0041370 The process in which a microorganism (or other particulate material) is rendered more susceptible to phagocytosis by coating with an opsonin, a blood serum protein such as a complement component or antibody. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 opsonization in COVID-19 HOIP_0041370 PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. All of these pathways converge on the formation of C3 convertases that cleave C3 to generate the pro-inflammatory peptide C3a and a large amount of C3b, which opsonizes pathogens. HOIP:HOIP_0041371 The process in which a microorganism (or other particulate material) is rendered more susceptible to phagocytosis by coating with an opsonin, a blood serum protein such as a complement component or antibody. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 opsonization (very high) in severe COVID-19 HOIP_0041371 PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. All of these pathways converge on the formation of C3 convertases that cleave C3 to generate the pro-inflammatory peptide C3a and a large amount of C3b, which opsonizes pathogens. HOIP:HOIP_0041372 The regulated release of anaphylatoxin from a cell. release of anaphylatoxin HOIP_0041372 HOIP:HOIP_0041373 Anaphylatoxins, or complement peptides, are fragments (C3a, C4a and C5a) that are produced as part of the activation of the complement system. (Wikipedia:Anaphylatoxin) Wikipedia:Anaphylatoxin Anaphylatoxin HOIP_0041373 Wikipedia:Anaphylatoxin Anaphylatoxins are able to trigger degranulation (release of substances) of endothelial cells, mast cells or phagocytes, which produce a local inflammatory response. If the degranulation is widespread, it can cause a shock-like syndrome similar to that of an allergic reaction. HOIP:HOIP_0041374 The regulated release of anaphylatoxin from a cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 WikiPedia:Anaphylatoxin release of anaphylatoxin in COVID-19 HOIP_0041374 PMID:33077917 All of these pathways converge on the formation of C3 convertases that cleave C3 to generate the pro-inflammatory peptide C3a and a large amount of C3b, which opsonizes pathogens. C3b also forms C5 convertase, which induces release of the potent anaphylatoxin C5a, as well as the fragment C5b that is responsible for the formation of the membrane attack complex C5b–9 on target cells — the terminal event of complement activation. C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma — pathological events that are all observed in severe cases of COVID-19. WikiPedia:Anaphylatoxin The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. They also mediate chemotaxis, inflammation, and generation of cytotoxic oxygen radicals. HOIP:HOIP_0041375 The regulated release of anaphylatoxin from a cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 WikiPedia:Anaphylatoxin release of anaphylatoxin (very high)in severe COVID-19 HOIP_0041375 PMID:33077917 All of these pathways converge on the formation of C3 convertases that cleave C3 to generate the pro-inflammatory peptide C3a and a large amount of C3b, which opsonizes pathogens. C3b also forms C5 convertase, which induces release of the potent anaphylatoxin C5a, as well as the fragment C5b that is responsible for the formation of the membrane attack complex C5b–9 on target cells — the terminal event of complement activation. C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma — pathological events that are all observed in severe cases of COVID-19. WikiPedia:Anaphylatoxin The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. They also mediate chemotaxis, inflammation, and generation of cytotoxic oxygen radicals. HOIP:HOIP_0041376 IL-1beta processing is a subtype of protein processing: A process that IL-1beta maturation process achieved by the cleavage of pro IL-1beta. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. IL-1beta processing in COVID-19 HOIP_0041376 HOIP:HOIP_0041377 The un-regulated release of cytokine from a ruptured cell. release of cytokine by cell rupture HOIP_0041377 HOIP:HOIP_0041378 The regulated release of histamine by a cell as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. WikiPedia:Anaphylatoxin Wikipedia:Inflammation histamine secretion involved in inflammatory response in COVID-19 HOIP_0041378 WikiPedia:Anaphylatoxin The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Redness and heat are due to increased blood flow at body core temperature to the inflamed site; swelling is caused by accumulation of fluid; pain is due to the release of chemicals such as bradykinin and histamine that stimulate nerve endings. Histamine: Stored in preformed granules, histamine is released in response to a number of stimuli. It causes arteriole dilation, increased venous permeability, and a wide variety of organ-specific effects. HOIP:HOIP_0041381 A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. WikiPedia:Anaphylatoxin smooth muscle contraction in COVID-19 HOIP_0041381 WikiPedia:Anaphylatoxin The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. HOIP:HOIP_0041384 The activation of the membrane attack complex components of the complement cascade which can result in death of a target cell through cytolysis. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 activation of membrane attack complex in COVID-19 HOIP_0041384 PMID:33077917 C3b also forms C5 convertase, which induces release of the potent anaphylatoxin C5a, as well as the fragment C5b that is responsible for the formation of the membrane attack complex C5b–9 on target cells — the terminal event of complement activation. HOIP:HOIP_0041385 The activation of the membrane attack complex components of the complement cascade which can result in death of a target cell through cytolysis. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 activation of membrane attack complex (very high) in severe COVID-19 HOIP_0041385 PMID:33077917 C3b also forms C5 convertase, which induces release of the potent anaphylatoxin C5a, as well as the fragment C5b that is responsible for the formation of the membrane attack complex C5b–9 on target cells — the terminal event of complement activation. HOIP:HOIP_0041386 The un-regulated release of DAMP (damage-associated molecular pattern) molecules from a ruptured cell. release of DAMP molecules by cell rupture HOIP_0041386 HOIP:HOIP_0041387 Any process involved in the activation of any of the steps of the classical pathway of the complement cascade which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 complement activation, classical pathway in COVID-19 HOIP_0041387 PMID:33077917 Use of an ultra-high-throughput clinical proteomic approach identified consistent activation of the classical complement pathway (specifically, complement components C1R, C1S and C8A) in the sera of patients with clinically severe COVID-19, along with increased activation of the alternative pathway component, complement factor B (CFB) and its modulators CFI and CFH144. HOIP:HOIP_0041388 Any process involved in the activation of any of the steps of the classical pathway of the complement cascade which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 complement activation, classical pathway (very high) in severe COVID-19 HOIP_0041388 PMID:33077917 Use of an ultra-high-throughput clinical proteomic approach identified consistent activation of the classical complement pathway (specifically, complement components C1R, C1S and C8A) in the sera of patients with clinically severe COVID-19, along with increased activation of the alternative pathway component, complement factor B (CFB) and its modulators CFI and CFH144. Circulating levels of C5a were higher in patients with severe COVID-19 than in patients with mild disease who had levels of C5a similar to those of healthy controls. Use of an untargeted metabolomic approach also demonstrated upregulation of complement activation proteins, including membrane attack complex proteins such as C5, C6 and C8, in sera from 46 patients with severe disease. As seen in the lung, post-mortem examination of kidney specimens in a preprint study also identified deposition of C5b–9 on tubule cells and massive interstitial infiltration of macrophages as hallmarks of kidney complications in patients with severe disease. HOIP:HOIP_0041389 Damage-associated molecular patterns (DAMPs), also known as danger-associated molecular patterns, danger signals, and alarmin, are host biomolecules that can initiate and perpetuate a noninfectious inflammatory response. (Wikipedia:Damage-associated molecular pattern) DAMP molecule HOIP_0041389 HOIP:HOIP_0041390 Any process involved in the activation of any of the steps of the alternative pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 complement activation, alternative pathway in COVID-19 HOIP_0041390 PMID:33077917 Use of an ultra-high-throughput clinical proteomic approach identified consistent activation of the classical complement pathway (specifically, complement components C1R, C1S and C8A) in the sera of patients with clinically severe COVID-19, along with increased activation of the alternative pathway component, complement factor B (CFB) and its modulators CFI and CFH144. HOIP:HOIP_0041391 Any process involved in the activation of any of the steps of the alternative pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 complement activation, alternative pathway (very high) in severe COVID-19 HOIP_0041391 PMID:33077917 Use of an ultra-high-throughput clinical proteomic approach identified consistent activation of the classical complement pathway (specifically, complement components C1R, C1S and C8A) in the sera of patients with clinically severe COVID-19, along with increased activation of the alternative pathway component, complement factor B (CFB) and its modulators CFI and CFH144. Circulating levels of C5a were higher in patients with severe COVID-19 than in patients with mild disease who had levels of C5a similar to those of healthy controls. Use of an untargeted metabolomic approach also demonstrated upregulation of complement activation proteins, including membrane attack complex proteins such as C5, C6 and C8, in sera from 46 patients with severe disease. As seen in the lung, post-mortem examination of kidney specimens in a preprint study also identified deposition of C5b–9 on tubule cells and massive interstitial infiltration of macrophages as hallmarks of kidney complications in patients with severe disease. HOIP:HOIP_0041396 Negative regulation of fibrinolysis is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of fibrinolysis. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. negative regulation of fibrinolysisin COVID-19 HOIP_0041396 HOIP:HOIP_0041398 A change in morphology and behavior of an inflammatory cell resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. inflammatory cell activation in COVID-19 HOIP_0041398 HOIP:HOIP_0041400 The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. natural killer cell activation (very high) in severe COVID-19 HOIP_0041400 HOIP:HOIP_0041401 Pain is a distressing feeling often caused by intense or damaging stimuli. (Wikipedia:Pain) pain 痛み Dolor HOIP_0041401 HOIP:HOIP_0041402 The controlled release of lysosomal enzymes by a cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation secretion of lysosomal enzymes involved in inflammatory response in COVID-19 HOIP_0041402 Wikipedia:Inflammation leukotriene B4: 'Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0041405 The controlled release of lysosomal enzymes by a cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation secretion of lysosomal enzymes involved in inflammatory response (very high) in severe COVID-19 HOIP_0041405 Wikipedia:Inflammation leukotriene B4: 'Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0041406 The regulated release of a prostaglandin that contributes to the immune response. Prostaglandins are a group of biologically active metabolites which contain a cyclopentane ring. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation prostaglandin secretion involved in inflammatory response in COVID-19 HOIP_0041406 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0041408 The regulated release of a leukotriene from a cell or a tissue. leukotriene secretion HOIP_0041408 HOIP:HOIP_0041409 JNK signaling is a process that a signal is transmitted by the JNK (a stress-activated protein kinase (SAPK) ). This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32422178 Wikipedia:c-Jun_N-terminal_kinases JNK signaling (very high) in severe COVID-19 HOIP_0041409 PMID:32422178 Furthermore, JNK family inhibition impairs synthesis of H5N1 viral RNA, and SARS-CoV-2 has been shown to stimulate pro-inflammatory pathways via JNK signalling pathways. Wikipedia:c-Jun_N-terminal_kinases Inflammatory signals, changes in levels of reactive oxygen species, ultraviolet radiation, protein synthesis inhibitors, and a variety of stress stimuli can activate JNK. Inflammatory signals, changes in levels of reactive oxygen species, ultraviolet radiation, protein synthesis inhibitors, and a variety of stress stimuli can activate JNK. JNK1 is involved in apoptosis, neurodegeneration, cell differentiation and proliferation, inflammatory conditions and cytokine production mediated by AP-1 (activation protein 1) such as RANTES, IL-8 and GM-CSF. HOIP:HOIP_0041410 The release of any leukotriene following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation leukotriene secretion involved in inflammatory response in COVID-19 HOIP_0041410 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. leukotriene B4: Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0041412 IL1 signaling is a process that a signal is transmitted by the cytokine IL1. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. IL1 signaling in COVID-19 HOIP_0041412 HOIP:HOIP_0041413 IL1 signaling is a process that a signal is transmitted by the cytokine IL1. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 IL1 signaling (very high) in severe COVID-19 HOIP_0041413 PMID:32697943 We observed that neutralization of IL-1b with anti-IL-1b (CM-aIL-1b) from UV-inactivated CM of CoV-2-infected monocytes restored T cell proliferation (Figures 4A and S4I). HOIP:HOIP_0041414 Thrombus formation in brain is a subtype of thrombus formation: A process that construcs thrombus in brain. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. Wikipedia:Cerebral_infarction thrombus formation in brain [brain infarction course] HOIP_0041414 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0041415 The regulated exocytosis of secretory granules containing preformed mediators such as histamine and serotonin by a platelet. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Coagulation platelet degranulation in COVID-19 HOIP_0041415 Wikipedia:Coagulation Activated platelets release the contents of stored granules into the blood plasma. The granules include ADP, serotonin, platelet-activating factor (PAF), vWF, platelet factor 4, and thromboxane A2 (TXA2), which, in turn, activate additional platelets. The granules' contents activate a Gq-linked protein receptor cascade, resulting in increased calcium concentration in the platelets' cytosol. The calcium activates protein kinase C, which, in turn, activates phospholipase A2 (PLA2). PLA2 then modifies the integrin membrane glycoprotein IIb/IIIa, increasing its affinity to bind fibrinogen. HOIP:HOIP_0041418 Glycation (sometimes incorrectly called non-enzymatic glycosylation) is the covalent attachment of a sugar to a protein or lipid.(Wikipedia:Glycation) Wikipedia:Glycation Glycation HOIP_0041418 Wikipedia:Glycation Glycation is the non-enzymatic process responsible for many (e.g. micro and macrovascular) complications in diabetes mellitus and is implicated in some diseases and in aging. HOIP:HOIP_0041421 Interacting selectively and non-covalently with fibrinogen, a highly soluble hexameric glycoprotein complex that is found in blood plasma and is converted to fibrin by thrombin in the coagulation cascade. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Coagulation fibrinogen binding in COVID-19 HOIP_0041421 Wikipedia:Coagulation The calcium activates protein kinase C, which, in turn, activates phospholipase A2 (PLA2). PLA2 then modifies the integrin membrane glycoprotein IIb/IIIa, increasing its affinity to bind fibrinogen. The activated platelets change shape from spherical to stellate, and the fibrinogen cross-links with glycoprotein IIb/IIIa aid in aggregation of adjacent platelets (completing primary hemostasis). HOIP:HOIP_0041422 A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 macrophage polarization macrophage activation involved in inflammatory response (very high) in COVID-19 in renal system HOIP_0041422 PMID:33077917 As seen in the lung, post-mortem examination of kidney specimens in a preprint study also identified deposition of C5b–9 on tubule cells and massive interstitial infiltration of macrophages as hallmarks of kidney complications in patients with severe disease. SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041423 A protein activation cascade that contributes to blood coagulation and consists of the cascade of enzymatic reactions initiated by physical damage to the wall of a blood vessel, leading to the formation of a formation of a fibrin clot at the site of the injury. The process also includes numerous positive and negative regulatory events. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Coagulation Wikipedia:Coagulation blood coagulation, fibrin clot formation in COVID-19 HOIP_0041423 Wikipedia:Coagulation The coagulation cascade of secondary hemostasis has two initial pathways which lead to fibrin formation. These are the contact activation pathway (also known as the intrinsic pathway), and the tissue factor pathway (also known as the extrinsic pathway), which both lead to the same fundamental reactions that produce fibrin. HOIP:HOIP_0041424 Platelet morphology changes is a subtype of changing shape: A process that changes the morphology of the platelet. platelet morphology change HOIP_0041424 HOIP:HOIP_0041425 Platelet morphology changes is a subtype of changing shape: A process that changes the morphology of the platelet. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Coagulation platelet morphology change in COVID-19 HOIP_0041425 Wikipedia:Coagulation The activated platelets change shape from spherical to stellate, and the fibrinogen cross-links with glycoprotein IIb/IIIa aid in aggregation of adjacent platelets (completing primary hemostasis).[ HOIP:HOIP_0041426 Platelet morphology changes is a subtype of changing shape: A process that changes the morphology of the platelet. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Coagulation platelet morphology change in severe COVID-19 HOIP_0041426 Wikipedia:Coagulation The activated platelets change shape from spherical to stellate, and the fibrinogen cross-links with glycoprotein IIb/IIIa aid in aggregation of adjacent platelets (completing primary hemostasis).[ HOIP:HOIP_0041427 thrombin-activated receptor signaling is a process that a signal is transmitted by the thrombin-activated receptor. thrombin-activated receptor signaling HOIP_0041427 HOIP:HOIP_0041428 A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 macrophage polarization macrophage activation involved in immune response (very high) in COVID-19 associated with ACS HOIP_0041428 PMID:32690910 The mechanisms underlying COVID-19-induced ACS might involve plaque rupture, coronary spasm or microthrombi owing to systemic inflammation or cytokine storm. For example, activated macrophages secrete collagenases that degrade collagen, a major constituent of the fibrous cap on atherosclerotic plaques, which can lead to plaque rupture. HOIP:HOIP_0041429 thrombin-activated receptor signaling is a process that a signal is transmitted by the thrombin-activated receptor. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Coagulation thrombin-activated receptor signaling in COVID-19 HOIP_0041429 Wikipedia:Coagulation The main role of the tissue factor pathway is to generate a "thrombin burst", a process by which thrombin, the most important constituent of the coagulation cascade in terms of its feedback activation roles, is released very rapidly. HOIP:HOIP_0041431 Interacting selectively and non-covalently with fibrinogen, a highly soluble hexameric glycoprotein complex that is found in blood plasma and is converted to fibrin by thrombin in the coagulation cascade. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Coagulation fibrinogen binding (very high) in severe COVID-19 HOIP_0041431 Wikipedia:Coagulation The calcium activates protein kinase C, which, in turn, activates phospholipase A2 (PLA2). PLA2 then modifies the integrin membrane glycoprotein IIb/IIIa, increasing its affinity to bind fibrinogen. The activated platelets change shape from spherical to stellate, and the fibrinogen cross-links with glycoprotein IIb/IIIa aid in aggregation of adjacent platelets (completing primary hemostasis). HOIP:HOIP_0041432 A protein activation cascade that contributes to blood coagulation and consists of the cascade of enzymatic reactions initiated by physical damage to the wall of a blood vessel, leading to the formation of a formation of a fibrin clot at the site of the injury. The process also includes numerous positive and negative regulatory events. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Coagulation Wikipedia:Coagulation PMID:32629875 blood coagulation, fibrin clot formation (severe)in severe COVID-19 HOIP_0041432 Wikipedia:Coagulation The coagulation cascade of secondary hemostasis has two initial pathways which lead to fibrin formation. These are the contact activation pathway (also known as the intrinsic pathway), and the tissue factor pathway (also known as the extrinsic pathway), which both lead to the same fundamental reactions that produce fibrin. PMID:32629875 Vascular platelet-fibrin clots are a common finding in COVID-19 autopsies. HOIP:HOIP_0041434 thrombin-activated receptor signaling is a process that a signal is transmitted by the thrombin-activated receptor. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Coagulation thrombin-activated receptor signaling (very high) in severe COVID-19 HOIP_0041434 Wikipedia:Coagulation The main role of the tissue factor pathway is to generate a "thrombin burst", a process by which thrombin, the most important constituent of the coagulation cascade in terms of its feedback activation roles, is released very rapidly. HOIP:HOIP_0041435 The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.　This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 tumor necrosis factor production (very high) in severe COVID-19 HOIP_0041435 PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). HOIP:HOIP_0041436 Any process that activates or increases the frequency, rate or extent of the inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. positive regulation of inflammatory response in coronavirus infection HOIP_0041436 HOIP:HOIP_0041437 The synthesis or release of any molecular mediator of the inflammatory response following an inflammatory stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation synthesis or release of inflammatory mediator in coronavirus infection HOIP_0041437 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041439 The appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. chemokine production in coronavirus infection HOIP_0041439 HOIP:HOIP_0041440 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.　This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 IL-1beta production (very high) in severe COVID-19 HOIP_0041440 PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). HOIP:HOIP_0041441 Any process that activates or increases the frequency, rate or extent of the inflammatory response in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32307653 positive regulation of inflammatory response in lung (very high) in COVID-19 associated with ARDS HOIP_0041441 PMID:32307653 In fact, the continuing injury to the alveolar zone caused by SARS-CoV-2 infections possibly origins a pro-inflammatory microenvironment triggering this aberrant response with partial replacement of normal tissue by fibrous tissue. HOIP:HOIP_0041443 The directed movement of a T cell in response to an external stimulus. A T cell is a type of lymphocyte whose defining characteristic is the expression of a T cell receptor complex. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T cell chemotaxis in coronavirus infection HOIP_0041443 HOIP:HOIP_0041444 The directed movement of a natural killer cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. natural killer cell chemotaxis in coronavirus infection HOIP_0041444 HOIP:HOIP_0041445 The movement of a monocyte in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:32697943 monocyte chemotaxis in coronavirus infection HOIP_0041445 PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell. HOIP:HOIP_0041447 The change in morphology and behavior of a monocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. monocyte activation involved in inflammatory response in coronavirus infection HOIP_0041447 HOIP:HOIP_0041448 The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. neutrophil activation involved in immune response in coronavirus infection HOIP_0041448 HOIP:HOIP_0041450 The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. PMID:33123165 natural killer cell mediated cytotoxicity in coronavirus infection HOIP_0041450 PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology. HOIP:HOIP_0041451 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. macrophage cell differentiation macrophage differentiation in coronavirus infection HOIP_0041451 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. ISBN:0781735149 HOIP:HOIP_0041452 The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific, leading to the initiation or perpetuation of an immune response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T cell activation involved in immune response in coronavirus infection HOIP_0041452 HOIP:HOIP_0041453 The movement of a macrophage in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. macrophage chemotaxis in coronavirus infection HOIP_0041453 HOIP:HOIP_0041454 The transport of a virus between tissues in a multicellular organism. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 transport of virus into central nervous system (very high) in severe COVID-19 HOIP_0041454 PMID:32629875 However, hematogenous dissemination of the virus (discussed in Section 4.1) is more likely to explain the presumed presence of viral particles in the endothelial cells distant from the lungs, such as the renal glomerulus. There is evidence for SARS-CoV-2 dissemination to the circulation since viral RNA was detected in 6/41(15%) plasma specimens from patients with severe COVID-19 disease (Figure 2). Hematological spread of infectious SARS-CoV-2 to different tissues is supported by detection of high viral RNA titers in the liver, kidney, or heart, but not in the pharynx or saphenous vein, from 5/12 patients who had died from COVID-19. Also, SARS-CoV-2 was detected by immunohistochemistry in tissue-resident ACE+CD169+ macrophages of all (6/6) autopsy-derived spleens and lymph nodes of patients who had succumbed of COVID-19, but not controls. HOIP:HOIP_0041455 The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. T cell mediated cytotoxicity in coronavirus infection HOIP_0041455 HOIP:HOIP_0041459 A change in morphology and behavior of a tissue-resident leukocyte resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation tissue-resident immune cell activation tissue-resident leukocyte activation in coronavirus infection HOIP_0041459 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0041460 The regulated release of inflammatory mediators from tissue-resident immune cells. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation release of inflammatory mediator from tissue-resident immune cells in coronavirus infection HOIP_0041460 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041461 Increasing vascular lumen area is a subtype of increasing area: A process that changes the area of the vascular lumen area to be larger. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation Vasodilation 血管拡張 increasing vascular lumen area in coronavirus infection HOIP_0041461 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041462 Increasing blood flow is a subtype of increaseing flow: A process that changes the amount of blood flow to be higher. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation increasing blood flow in coronavirus infection HOIP_0041462 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041463 Increasing temperature is a subtype of changing temperature: A process that increases the temperature of the object. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation heat increasing temperature in coronavirus infection HOIP_0041463 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041464 Increasing vascular permeabilization is a subtype of changing permeability: A process that changes the permeability of the vascular to be higher. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation increasing vascular permeabilization in coronavirus infection HOIP_0041464 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041467 The migration of a monocyte from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. monocyte extravasation in coronavirus infection HOIP_0041467 HOIP:HOIP_0041468 The migration of a neutrophil from the blood vessels into the surrounding tissue. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. neutrophil extravasation in coronavirus infection HOIP_0041468 HOIP:HOIP_0041469 The appearance of interleukin-6 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:32697943 interleukin-6 production (very high) in severe COVID-19 HOIP_0041469 PMID:32629875 When released rapidly, particularly from activated macrophages and in abnormally large amounts, IL-6, TNFα and other pro-inflammatory cytokines can cause severe clinical manifestations of high fevers, headache, low blood pressure, night sweats and multi-organ dysfunction referred to as “cytokine release syndrome”. PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). HOIP:HOIP_0041471 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32651579 cytokine storm in COVID-19 associated with myocarditis HOIP_0041471 PMID:32651579 Systemic inflammatory response syndrome (cytokine storm) is another putative mechanism of myocardial injury. HOIP:HOIP_0041472 The controlled release of lysosomal enzymes by a cell. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation secretion of lysosomal enzymes involved in inflammatory response in coronavirus infection HOIP_0041472 Wikipedia:Inflammation leukotriene B4: 'Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0041473 Any process that activates or increases the frequency, rate or extent of glycolytic process. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32697943 positive regulation of glycolysis positive regulation of glycolytic process in COVID-19 in patient with diabetes HOIP_0041473 PMID:32697943 Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Elevated Glucose Levels Favor SARS-CoV-2 Infection and Monocyte Response through a HIF-1a/ Glycolysis-Dependent Axis. HOIP:HOIP_0041474 Any process that activates or increases the frequency, rate or extent of glycolytic process. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 positive regulation of glycolysis positive regulation of glycolytic process in COVID-19 HOIP_0041474 PMID:32697943 Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Monocytes and macrophages are the most enriched immune cell types in the lungs of COVID-19 patients and appear to have a central role in the pathogenicity of the disease.These cells adapt their metabolism upon infection and become highly glycolytic, which facilitates SARS-CoV-2 replication. The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. HIF-1a-induced changes in monocyte metabolism by SARS- CoV-2 infection directly inhibit T cell response and reduce epithelial cell survival. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes HOIP:HOIP_0041475 Cellular damage is a subtype of damaging: A process that injuries the structure of the cell as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Cell damage (also known as cell injury) is a variety or changes of stress that a cell suffers due to external as well internal environmental changes. Among other causes, this can be due to physical, chemical, infectious, biological, nutritional or immunological factors. Cell damage can be reversible or irreversible. Depending on the extent of injury, the cellular response may be adaptive and where possible, homeostasis is restored. Cell death occurs when the severity of the injury exceeds the cell’s ability to repair itself. Cell death is relative to both the length of exposure to a harmful stimulus and the severity of the damage caused. Cell death may occur by necrosis or apoptosis. cell and tissue damage cell and tissue damage PMID:35615359 http://purl.jp/bio/4/id/200906069918862451 https://en.wikipedia.org/wiki/Cell_damage cellular damage in COVID-19 HOIP_0041475 cell and tissue damage http://purl.obolibrary.org/obo/MPATH_1 HOIP:HOIP_0041478 Any process that activates or increases the frequency, rate, or extent of fever generation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation positive regulation of fever generation in COVID-19 HOIP_0041478 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0041479 Any process that activates or increases the frequency, rate, or extent of fever generation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Inflammation positive regulation of fever generation (very high) in severe COVID-19 HOIP_0041479 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0041480 Interacting selectively and non-covalently with a receptor on the host cell surface. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 host cell surface receptor binding (severe)[COVID-19 in patient with diabetes] SARS-CoV-2 S binding to human ACE2 (very high) in COVID-19 infected diabetes patient HOIP_0041480 PMID:32694793 In people with T2D, ACE2 expression is elevated in multiple target tissues of SARS-CoV-2, and this elevation has been proposed to be an adaptive mechanism that protects the body against diabetes-associated physiological dysfunction. This increased expression may enhance SARS-CoV-2’s entry and subsequent replication, as well as its spread within the body in individuals with T2D. HOIP:HOIP_0041481 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 viral entry into host cell (very high) in COVID-19 in patient with diabetes SARS-CoV-2 entry to host cell in COVID-19 in patient with diabetes HOIP_0041481 PMID:32694793 In people with T2D, ACE2 expression is elevated in multiple target tissues of SARS-CoV-2, and this elevation has been proposed to be an adaptive mechanism that protects the body against diabetes-associated physiological dysfunction. This increased expression may enhance SARS-CoV-2’s entry and subsequent replication, as well as its spread within the body in individuals with T2D. HOIP:HOIP_0041482 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32629875 PMID:32697943 increasing demand for response to oxidative stress (severe) in COVID-19 in patient with diabetes HOIP_0041482 PMID:32629875 Also, genetic and pharmacological studies in mice have shown that ACE2 regulates cardiac structure and function; decreased ACE2 in SARS-CoV-2-infected cardiomyocytes could disrupt these activities, particularly impairing cardiac remodeling and increasing oxidative stress in cardiomyocytes. PMID:32697943 We observed that oxidative stress-associated genes are enriched in BAL of severe COVID-19 patients (Figure 3A). (A) Single-cell RNA-seq data showing enrichment of HIF-1, glycolysis, and oxidative stress pathways in SARS-CoV-2 (CoV-2)-infected human monocytes. HOIP:HOIP_0041483 A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. phagocytosis in COVID-19 HOIP_0041483 HOIP:HOIP_0041485 Any process that decreases the frequency, rate, or extent of neutrophil extracellular trap formation. negative regulation of neutrophil extracellular trap formation HOIP_0041485 HOIP:HOIP_0041487 Any process that activates or increases the frequency, rate or extent of phagocytosis. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. positive regulation of phagocytosis in COVID-19 HOIP_0041487 HOIP:HOIP_0041488 Any process that activates or increases the frequency, rate or extent of phagocytosis. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. positive regulation of phagocytosis (severe)in severe COVID-19 HOIP_0041488 HOIP:HOIP_0041489 A viral genome replication process where the template genome is positive stranded, single stranded RNA ((+)ssRNA). Replication of the positive strand leads to dsRNA formation, which in turn is transcribed into positive single stranded RNA. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 PMID:32697943 positive stranded viral RNA replication (very high) in COVID-19 in patient with diabetes HOIP_0041489 PMID:32694793 In people with T2D, ACE2 expression is elevated in multiple target tissues of SARS-CoV-2, and this elevation has been proposed to be an adaptive mechanism that protects the body against diabetes-associated physiological dysfunction. This increased expression may enhance SARS-CoV-2’s entry and subsequent replication, as well as its spread within the body in individuals with T2D. PMID:32697943 Codo et al. show that elevated glucose levels and glycolysis promote SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. Elevated glucose levels directly induce viral replication and proinflammatory cytokine expression. HOIP:HOIP_0041490 Endothelium damage is a subtype of damaging: A process that injuries the structure of the endothelium as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:33188364 PMID:33188364 endothelium damage (very high) in COVID-19 in patient with diabetes HOIP_0041490 PMID:33188364 As described already, glucotoxicity, endothelial damage by inflammation, oxidative stress and cytokine production contribute to an increased risk of thromboembolic complications and of damage to vital organs in patients with diabetes mellitus (fig. 1). HOIP:HOIP_0041491 Positive regulation of IFN alpha gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IFN alpha gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32697943 positive regulation of IFN alpha gene expression in COVID-19 in patient with diabetes HOIP_0041491 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0041492 Positive regulation of IFNB1 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IFNB1gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32697943 positive regulation of IFNB1 gene expression (severe) in COVID-19 in patient with diabetes HOIP_0041492 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0041493 Positive regulation of IL-6 gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IL-6 gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32697943 positive regulation of IL-6 gene expression (severe) in COVID-19 in patient with diabetes HOIP_0041493 PMID:32697943 Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0041494 Positive regulation of IL1B gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of IL1B gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32697943 positive regulation of IL1B gene expression (severe) in COVID-19 in patient with diabetes HOIP_0041494 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). We observed that neutralization of IL-1b with anti-IL-1b (CM-aIL-1b) from UV-inactivated CM of CoV-2-infected monocytes restored T cell proliferation (Figures 4A and S4I). HOIP:HOIP_0041495 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32697943 PMID:33077917 PMID:33188364 reactive oxygen species biosynthetic process (very high) in COVID-19 in patient with diabetes HOIP_0041495 PMID:32697943 Reactive oxygen species (ROS) are strong inducers of HIF-1a (Mills et al., 2016). We observed that CoV-2-infected monocytes have increased mtROS production as measured by mitoSOX (Figure 3J). These data indicate that RET is an important source of mtROS in CoV-2-infected monocytes. SARS-CoV-2 (CoV-2) replication and cytokine production in monocytes through a mitochondrial ROS/hypoxia-inducible factor-1a dependent pathway, resulting in T cell dysfunction and epithelial cell death. The infection triggers mitochondrial ROS production, which induces stabilization of hypoxia-inducible factor-1a (HIF-1a) and consequently promotes glycolysis. Mitochondrial ROS-Mediated HIF-1a Stabilization Sustains SARS-CoV-2 Replication and Cytokine Production in Monocytes This suggests that under high glucose conditions, CoV-2-infected monocytes can promote epithelial cell death in an mtROS/HIF-1a-dependent manner. PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. PMID:33188364 Through increasing oxidative stress, IL-6 can damage proteins, lipids and DNA, and impair the body’s structure and function, and we propose that this effect might lead to rapid progression of COVID-19 in patients with diabetes mellitus (fig. 1). HOIP:HOIP_0041496 Positive regulation of TNFΑ gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of TNFΑ gene expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32697943 positive regulation of TNFΑ gene expression (severe) in COVID-19 in patient with diabetes HOIP_0041496 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). The cytokines TNF-a, IL-1b, and IL-6, which were highly expressed in CoV-2-infected monocytes (Figure 1C), resemble the cytokine storm proposed in severe COVID-19 patients (Tay et al., 2020). HOIP:HOIP_0041497 A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. phagocytosis in coronavirus infection HOIP_0041497 HOIP:HOIP_0041500 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32694793 PMID:33188364 Insulin resistance (process) in severe COVID-19 HOIP_0041500 PMID:32694793 Angiotensin II, the active RAS metabolite and a potent vasoconstrictor that increases peripheral vascular resistance, also causes insulin resistance and regulates sodium absorption in the kidneys. PMID:33188364 ROS production and viral activation of the renin–angiotensin–aldosterone system (RAAS), (via increased angiotensin II expression) cause insulin resistance, hyperglycaemia and vascular endothelial damage, all of which contribute to cardiovascular events, thromboembolism and disseminated intravascular coagulation (DIC). HOIP:HOIP_0041503 Negative regulation of natural killer cell mediated cytotoxicity is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the natural killer cell cytotoxicity. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:33188364 negative regulation of natural killer cell mediated cytotoxicity in COVID-19 in patient with diabetes HOIP_0041503 PMID:33188364 Hyperglycaemia can affect immune function; conversely, a dysregulated immunological status is linked to macrovascular complications of diabetes mellitus. For example, NK cell activity was lower in patients with T2DM than in those with prediabetes or normal glucose tolerance. Thus, individuals with impaired glucose tolerance or diabetes mellitus have reduced NK cell activity, which might help to explain why patients with diabetes mellitus are more susceptible to COVID-19 and have a worse prognosis than those without diabetes mellitus. HOIP:HOIP_0041505 Any process that activates or increases the frequency, rate or extent of phagocytosis. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. positive regulation of phagocytosis in coronavirus infection HOIP_0041505 HOIP:HOIP_0041506 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of heart vasculature. The process ends when the viral nucleic acid is released into the host cell cytoplasm. viral entry into host cell in heart vasculature HOIP_0041506 HOIP:HOIP_0041507 Any process that stops, prevents, or reduces the frequency, rate or extent of phagocytosis. negative regulation of phagocytosis HOIP_0041507 HOIP:HOIP_0041508 Any process that stops, prevents, or reduces the frequency, rate or extent of phagocytosis. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 negative regulation of phagocytosis in COVID-19 in patient with diabetes HOIP_0041508 PMID:30510205 Obesity and type 2 diabetes mellitus (T2DM) are associated to worsen outcomes and mortality caused by infection. The main cause of this vulnerability is the impaired innate immune functions in these two conditions, such as phagocytosis, cytokine and reactive oxygen species (ROS) production, bactericidal activity and chemotaxis. The influence of diabetes (type 1 and 2) and obesity in neutrophil’s function is well-characterized. HOIP:HOIP_0041510 Any process that stops, prevents, or reduces the rate of production of a cytokine in neutrophil. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 negative regulation of cytokine production in neutrophil in COVID-19 in patient with diabetes HOIP_0041510 PMID:30510205 Obesity and type 2 diabetes mellitus (T2DM) are associated to worsen outcomes and mortality caused by infection. The main cause of this vulnerability is the impaired innate immune functions in these two conditions, such as phagocytosis, cytokine and reactive oxygen species (ROS) production, bactericidal activity and chemotaxis. The influence of diabetes (type 1 and 2) and obesity in neutrophil’s function is well-characterized. Neutrophils also exhibited impaired chemotaxis and cytokine production in diabetic patients. HOIP:HOIP_0041511 Any process that decreases the frequency, rate, or extent of G-CSF production. negative regulation of G-CSF production HOIP_0041511 HOIP:HOIP_0041512 Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ROS in neutrophil. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 negative regulation of reactive oxygen species biosynthetic process negative regulation of ROS formation in neutrophil in COVID-19 in patient with diabetes HOIP_0041512 PMID:30510205 Obesity and type 2 diabetes mellitus (T2DM) are associated to worsen outcomes and mortality caused by infection. The main cause of this vulnerability is the impaired innate immune functions in these two conditions, such as phagocytosis, cytokine and reactive oxygen species (ROS) production, bactericidal activity and chemotaxis. The influence of diabetes (type 1 and 2) and obesity in neutrophil’s function is well-characterized. HOIP:HOIP_0041513 Any process that stops, prevents, or reduces the rate of production of a cytokine in neutrophil. negative regulation of cytokine production in neutrophil HOIP_0041513 HOIP:HOIP_0041514 Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ROS in neutrophil. negative regulation of reactive oxygen species biosynthetic process negative regulation of ROS formation in neutrophil HOIP_0041514 HOIP:HOIP_0041515 Any process that decreases the frequency, rate, or extent of G-CSF production. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 negative regulation of G-CSF production in COVID-19 in patient with diabetes HOIP_0041515 PMID:30510205 Obesity and type 2 diabetes mellitus (T2DM) are associated to worsen outcomes and mortality caused by infection. The main cause of this vulnerability is the impaired innate immune functions in these two conditions, such as phagocytosis, cytokine and reactive oxygen species (ROS) production, bactericidal activity and chemotaxis. HOIP:HOIP_0041516 Any process that decreases the frequency, rate, or extent of neutrophil chemotaxis. Neutrophil chemotaxis is the directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 negative regulation of neutrophil chemotaxis in COVID-19 in patient with diabetes HOIP_0041516 PMID:30510205 Obesity and type 2 diabetes mellitus (T2DM) are associated to worsen outcomes and mortality caused by infection. The main cause of this vulnerability is the impaired innate immune functions in these two conditions, such as phagocytosis, cytokine and reactive oxygen species (ROS) production, bactericidal activity and chemotaxis. The influence of diabetes (type 1 and 2) and obesity in neutrophil’s function is well-characterized. Neutrophils also exhibited impaired chemotaxis and cytokine production in diabetic patients. HOIP:HOIP_0041517 Negative regulation of neutrophil function is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the neutrophil function. negative regulation of neutrophil function HOIP_0041517 HOIP:HOIP_0041519 A change in morphology and behavior of a leukocyte resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 immune cell activation leucocyte activation inflammatory cell activation (very high) in COVID-19 in patient with diabetes HOIP_0041519 PMID:30510205 Diabetes and obesity, due to hyperglycemia and high concentrations of plasma free fatty acids, are known to pre-activate leukocytes and lead them to a pro-inflammatory phenotype. This chronic stimulus by the altered metabolic state in these diseases may lead to the appearance of tolerant or “burned-out” leukocytes that are not able to fully respond to an infectious stimulus, allowing the microorganism to disseminate. HOIP:HOIP_0041520 Leukocyte exhaustion is a dysfunctional leukocytes that changes in transcriptional profiles and sustained expression of inhibitory receptors and leads to progressive loss of function. leukocyte exhaustion HOIP_0041520 HOIP:HOIP_0041521 Leukocyte exhaustion is a dysfunctional leukocytes that changes in transcriptional profiles and sustained expression of inhibitory receptors and leads to progressive loss of function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 leukocyte exhaustion in COVID-19 in patient with diabetes HOIP_0041521 PMID:30510205 This chronic stimulus by the altered metabolic state in these diseases may lead to the appearance of tolerant or “burned-out” leukocytes that are not able to fully respond to an infectious stimulus, allowing the microorganism to disseminate. HOIP:HOIP_0041522 Increasing free fatty acid concentration in blood is a subtype of increasing lipid concentration in blood: A process that changes the free fatty acid concentration in the blood to be higher. increasing free fatty acid concentration in blood HOIP_0041522 HOIP:HOIP_0041523 An increased concentration of free fatty acids in the blood. High blood free fatty acid HOIP_0041523 HOIP:HOIP_0041524 Any process that decreases the frequency, rate, or extent of GM-CSF production. negative regulation of GM-CSF production HOIP_0041524 HOIP:HOIP_0041525 Increasing free fatty acid concentration in blood is a subtype of increasing lipid concentration in blood: A process that changes the free fatty acid concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 increasing free fatty acid concentration in blood in COVID-19 in patient with diabetes HOIP_0041525 PMID:30510205 Diabetes and obesity, due to hyperglycemia and high concentrations of plasma free fatty acids, are known to pre-activate leukocytes and lead them to a pro-inflammatory phenotype. HOIP:HOIP_0041526 Any process that decreases the frequency, rate, or extent of GM-CSF production. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 negative regulation of GM-CSF production in COVID-19 in patient with diabetes HOIP_0041526 PMID:30510205 Obesity and type 2 diabetes mellitus (T2DM) are associated to worsen outcomes and mortality caused by infection. The main cause of this vulnerability is the impaired innate immune functions in these two conditions, such as phagocytosis, cytokine and reactive oxygen species (ROS) production, bactericidal activity and chemotaxis. HOIP:HOIP_0041527 Any process that decreases the frequency, rate, or extent of netosis. negative regulation of netosis HOIP_0041527 HOIP:HOIP_0041528 An abnormal elevation of theangiopoietin 2 level in serum. Elevated blood angiopoietin 2 level HOIP_0041528 HOIP:HOIP_0041529 Any process that decreases the frequency, rate, or extent of netosis. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:30510205 negative regulation of netosis in COVID-19 in patient with diabetes HOIP_0041529 PMID:30510205 Obesity and type 2 diabetes mellitus (T2DM) are associated to worsen outcomes and mortality caused by infection. The main cause of this vulnerability is the impaired innate immune functions in these two conditions, such as phagocytosis, cytokine and reactive oxygen species (ROS) production, bactericidal activity and chemotaxis. HOIP:HOIP_0041530 Vascular endothelial cell damage damage is a subtype of cellular damage: A process that injuries the structure of the vascular endothelial cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:33077917 Wikipedia:"Blood sugar level" vascular endothelial cell damage (very high) in COVID-19 in patient with diabetes HOIP_0041530 PMID:33077917 The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. Wikipedia:"Blood sugar level" A persistent elevation in blood glucose leads to glucose toxicity, which contributes to cell dysfunction and the pathology grouped together as complications of diabetes. HOIP:HOIP_0041532 The attachment of a platelet to basement membrane of the blood vessel platelet adhesion to basement membrane HOIP_0041532 HOIP:HOIP_0041533 Increasing interferon-beta level is a subtype of increasing quantity: A process that changes the amount of interferon-beta level to be higher. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32697943 increasing interferon-beta level (severe)in severe COVID-19 HOIP_0041533 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0041534 The attachment of a platelet to basement membrane of the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 Wikipedia:Coagulation platelet adhesion to basement membrane (very high) in severe COVID-19 HOIP_0041534 PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. Wikipedia:Coagulation When the endothelium is damaged, the normally isolated, underlying collagen is exposed to circulating platelets, which bind directly to collagen with collagen-specific glycoprotein Ia/IIa surface receptors. This adhesion is strengthened further by von Willebrand factor (vWF), which is released from the endothelium and from platelets; vWF forms additional links between the platelets' glycoprotein Ib/IX/V and A1 domain. Binding of collagen to glycoprotein VI triggers a signaling cascade that results in activation of platelet integrins. HOIP:HOIP_0041536 The attachment of a platelet to basement membrane of the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 Wikipedia:Coagulation platelet adhesion to basement membrane in COVID-19 HOIP_0041536 PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. Wikipedia:Coagulation When the endothelium is damaged, the normally isolated, underlying collagen is exposed to circulating platelets, which bind directly to collagen with collagen-specific glycoprotein Ia/IIa surface receptors. This adhesion is strengthened further by von Willebrand factor (vWF), which is released from the endothelium and from platelets; vWF forms additional links between the platelets' glycoprotein Ib/IX/V and A1 domain. Binding of collagen to glycoprotein VI triggers a signaling cascade that results in activation of platelet integrins. HOIP:HOIP_0041540 A temperature which is higher relative to the normal or average. high temperature increased temperature HOIP_0041540 HOIP:HOIP_0041541 Iecreasing circulating blood volume is a subtype of decreasing quantity: A process that changes the quantity of the blood volume to be higher. increasing circulating blood volume HOIP_0041541 HOIP:HOIP_0041542 A temperature which is relatively high. Calor heat HOIP_0041542 HOIP:HOIP_0041543 A body temperature which is higher relative to the normal or average. increased body temperature HOIP_0041543 HOIP:HOIP_0041544 A physical attribure of the thermal energy of a body. body temperature attribute HOIP_0041544 HOIP:HOIP_0041546 A series of molecular signals initiated by the binding of the C-C chemokine CCL3 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. CCL3-mediated signaling pathway chemokine (C-C motif) ligand 3 signaling pathway HOIP_0041546 HOIP:HOIP_0041547 Increasing blood pressure is a subtype of increasing pressure: A process that changes the blood pressure to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:29556093 PMID:32694793 increasing vascular pressure increasing blood pressure in COVID-19 in patient with diabetes HOIP_0041547 PMID:29556093 Patients with diabetes mellitus experience increased peripheral artery resistance caused by vascular remodeling and increased body fluid volume associated with insulin resistance-induced hyperinsulinemia and hyperglycemia. Both of these mechanisms elevate systemic blood pressure. PMID:32694793 The effects of obesity and diabetes on the blood vessels can lead to hypertension, which in turn affects haemodynamics and alters the heart structure (Fig. 2). HOIP:HOIP_0041548 Blood vessel damage is a subtype of damaging: A process that injures the structure of the blood vessel as the direct or indirect result of an external force. blood vessel damage HOIP_0041548 HOIP:HOIP_0041549 Blood vessel damage is a subtype of damaging: A process that injures the structure of the blood vessel as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 blood vessel damage in COVID-19 in patient with diabetes HOIP_0041549 PMID:32694793 The damage to the blood vessels caused by hypertension decreases blood flow to the kidneys and consequently results in kidney injury (Fig. 2). HOIP:HOIP_0041550 Decreasing kidney perfusion is a subtype of decreasing quantity: A process that changes the amount of kidney perfusion to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32416769 PMID:32694793 kidney hypoperfusion decreasing kidney perfusion in COVID-19 in patient with diabetes HOIP_0041550 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. PMID:32694793 The damage to the blood vessels caused by hypertension decreases blood flow to the kidneys and consequently results in kidney injury (Fig. 2). HOIP:HOIP_0041551 Blood vessel damage is a subtype of damaging: A process that injures the structure of the blood vessel as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32694793 blood vessel damage in severe COVID-19 HOIP_0041551 PMID:32694793 The damage to the blood vessels caused by hypertension decreases blood flow to the kidneys and consequently results in kidney injury (Fig. 2). HOIP:HOIP_0041552 Increasing volume of myocardium is a subtype of increasing volume: A process that changes the volume of the myocardium to be higher. increasing volume of myocardium HOIP_0041552 HOIP:HOIP_0041553 Detaching of blood clot is a subtype of detaching: A process of a blood clot detaching from the area of the blood stream where it coagulated and grew to obstruct the vessel. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. Wikipedia:Cerebral_infarction detaching of blood clot [brain infarction course] HOIP_0041553 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0041554 Increasing volume of myocardium is a subtype of increasing volume: A process that changes the volume of the myocardium to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 increasing volume of myocardium in COVID-19 in patient with diabetes HOIP_0041554 PMID:32694793 The effects of obesity and diabetes on the blood vessels can lead to hypertension, which in turn affects haemodynamics and alters the heart structure (Fig. 2). These changes can make the heart more susceptible to damage due to the host inflammatory response, hypoxia caused by ARDS, infection of the heart by the virus or other cardiac consequences in response to extrapulmonary multiorgan damage, thus potentially explain- ing why some people with COVID-19 exhibit cardiac damage and heart-attack-like signs of disease. HOIP:HOIP_0041556 Renin-angiotensin activation is a subtype of activating: A process that changes the activity of the renin-angiotensin system, which regulates blood pressure and fluid balance, to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 renin-angiotensin activation in COVID-19 in patient with diabetes HOIP_0041556 PMID:32694793 The prevalence of hypertension, cardiovascular disease, nephropathy and retinopathy in people with diabetes has implicated the renin–angiotensin system (RAS) in the pathogenesis of these disorders. HOIP:HOIP_0041557 The expansion of a neutrophile population by cell division. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 neutrophile proliferation (very high) in COVID-19 in patient with diabetes HOIP_0041557 PMID:32687793 In a Chinese retrospective study, patients with diabetes had more severe pneumonia, higher concentrations of lactate dehydrogenase, α-hydroxybutyrate dehydrogenase, alanine aminotransferase, and γ-glutamyl transferase, and fewer lymphocytes with a higher neutrophil count. HOIP:HOIP_0041559 The appearance of adipokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. adipocytokine production adipokine production HOIP_0041559 HOIP:HOIP_0041560 A series of molecular signals initiated by the binding of the chemokine CXCL10 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. CXCL10-mediated signaling pathway chemokine (C-X-C motif) ligand 10 signaling pathway HOIP_0041560 HOIP:HOIP_0041562 Negative regulation of cardiomyocyte function is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the cardiomyocyte function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 negative regulation of cellular function in COVID-19 in patient with diabetes HOIP_0041562 PMID:32687793 Myocarditis and cardiomyocyte dysfunction could be worsened by local biological effects of epicardial adipose tissue, a source of adipokines and pro-inflammatory mediators, and the volume of epicardial adipose tissue is directly associated with BMI. HOIP:HOIP_0041564 A process that changes the magnitude of the inflammation to be larger. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. Wikipedia:Inflammation expanding inflammation in COVID-19 in patient with diabetes HOIP_0041564 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. The inflammatory response must be actively terminated when no longer needed to prevent unnecessary "bystander" damage to tissues. Failure to do so results in chronic inflammation, and cellular destruction. HOIP:HOIP_0041565 Increasing vascular permeabilization is a subtype of changing permeability: A process that changes the permeability of the vascular to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. Wikipedia:Advanced_glycation_end-product increasing vascular permeabilization (very high) in COVID-19 in patient with diabetes HOIP_0041565 Wikipedia:Advanced_glycation_end-product AGEs have a range of pathological effects, such as: Increased vascular permeability. Increased arterial stiffness Inhibition of vascular dilation by interfering with nitric oxide. Oxidizing LDL. Binding cells—including macrophage, endothelial, and mesangial—to induce the secretion of a variety of cytokines. Enhanced oxidative stress. The activation of cellular RAGE on endothelium, mononuclear phagocytes, and lymphocytes triggers the generation of free radicals and the expression of inflammatory gene mediators. HOIP:HOIP_0041568 Hardening of artery is a subtype of changing hardness: A process that changes the hardness of the artery to become hard due to the replacement of normal artery to scar tissue. hardening of artery HOIP_0041568 HOIP:HOIP_0041569 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. Wikipedia:Inflammation inflammatory response (very high) in COVID-19 in patient with diabetes HOIP_0041569 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. The inflammatory response must be actively terminated when no longer needed to prevent unnecessary "bystander" damage to tissues.[10] Failure to do so results in chronic inflammation, and cellular destruction. HOIP:HOIP_0041570 The appearance of anti-inflammatory cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. anti-inflammatory cytokine production HOIP_0041570 HOIP:HOIP_0041571 Increasing lactate dehydrogenase concentration is a subtype of increasing concentration: A process that changes the lactate dehydrogenase concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 increasing lactate dehydrogenase concentration (very high) in COVID-19 in patient with diabetes HOIP_0041571 PMID:32687793 In a Chinese retrospective study, patients with diabetes had more severe pneumonia, higher concentrations of lactate dehydrogenase, α-hydroxybutyrate dehydrogenase, alanine aminotransferase, and γ-glutamyl transferase, and fewer lymphocytes with a higher neutrophil count. HOIP:HOIP_0041572 Increasing ALT concentration in blood is a subtype of increasing concentration: A process that changes the alanine aminotransferase (ALT) concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 http://purl.bioontology.org/ontology/MEDDRA/10001845 increasing blood GPT concentration increasing blood ALT concentration in COVID-19 in patient with diabetes HOIP_0041572 PMID:32687793 In a Chinese retrospective study, patients with diabetes had more severe pneumonia, higher concentrations of lactate dehydrogenase, α-hydroxybutyrate dehydrogenase, alanine aminotransferase, and γ-glutamyl transferase, and fewer lymphocytes with a higher neutrophil count. HOIP:HOIP_0041573 Decreasing vitamin D concentration is a subtype of decreasing concentration: A process that changes the concentration of the vitamin D to be lower. decreasing vitamin D concentration HOIP_0041573 HOIP:HOIP_0041575 Decreasing vitamin D concentration is a subtype of decreasing concentration: A process that changes the concentration of the vitamin D to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 Wikipedia:Vitamin D decreasing vitamin D concentration in COVID-19 in patient with diabetes HOIP_0041575 PMID:32687793 Moreover, individuals with obesity have lower vitamin D concentrations, which could also reduce the immune response. Wikipedia:Vitamin D In general, vitamin D functions to activate the innate and dampen the adaptive immune systems with antibacterial, antiviral and anti-inflammatory effects. Deficiency has been linked to increased risk or severity of viral infections, including HIV and COVID-19. HOIP:HOIP_0041576 Innate immune response insufficiency is a subtype of malfunctioning process: A process that lacks performing the function of innate immune response required. innate immune response insufficiency HOIP_0041576 HOIP:HOIP_0041578 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 cytokine storm in COVID-19 in patient with diabetes HOIP_0041578 PMID:32687793 The cytokine storm is more likely to develop in patients with diabetes, as diabetes is already characterised by low-grade chronic inflammation. For patients with COVID-19, those with diabetes are more susceptible to the destructive effect of the cytokine storm than those without diabetes. HOIP:HOIP_0041579 Negative regulation of fibrinolysis is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of fibrinolysis. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 negative regulation of fibrinolysis in COVID-19 in patient with diabetes HOIP_0041579 PMID:32687793 Diabetes is associated with a prothrombotic state, with an imbalance between clotting factors and fibrinolysis and an increased risk of thromboembolic events. HOIP:HOIP_0041580 A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 Wikipedia:Fibrinolysis fibrinolysis (very low) in COVID-19 in patient with diabetes HOIP_0041580 PMID:32687793 Diabetes is associated with a prothrombotic state, with an imbalance between clotting factors and fibrinolysis and an increased risk of thromboembolic events. HOIP:HOIP_0041581 Blood coagulation factor synthesis is a subtype of biosynthetic process: The chemical reactions resulting in the formation of substances with blood coagulation factor role. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 blood coagulation factor synthesis (severe) in COVID-19 in patient with diabetes HOIP_0041581 PMID:32687793 Diabetes is associated with a prothrombotic state, with an imbalance between clotting factors and fibrinolysis and an increased risk of thromboembolic events. HOIP:HOIP_0041583 Any process that activates or increases the frequency, rate or extent of thrombus formation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. positive regulation of thrombus formation (very high) in COVID-19 in patient with diabetes HOIP_0041583 HOIP:HOIP_0041584 Negative regulation of vasodilation is a subtype of negative regulation process: Any process that stops, prevents, or reduces the frequency, rate or extent of the vasodilation. negative regulation of vasodilation HOIP_0041584 HOIP:HOIP_0041585 Negative regulation of type B pancreatic cell function is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the type B pancreatic cell function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32687793 negative regulation of type B pancreatic cell function in COVID-19 in patient with diabetes HOIP_0041585 PMID:32687793 The virus binds to ACE2 receptors, which, among other locations, are expressed in pancreatic tissue and β-cells in particular. Therefore, an acute loss of insulin secretory capacity along with a stress condition and the cytokine storm could lead to a rapid metabolic deterioration with development of diabetic ketoacidosis or hyperglycaemic hyperosmolar syndrome. Moreover, consideration should be given for a direct effect of SARS-CoV-2 on β-cell function and survival, causing worsening rapid and severe deterioration of metabolic control in people with pre-existing diabetes or leading to the development of new-onset diabetes (figure). HOIP:HOIP_0041586 Negative regulation of vasodilation is a subtype of negative regulation process: Any process that stops, prevents, or reduces the frequency, rate or extent of the vasodilation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. Wikipedia:Advanced_glycation_end-product negative regulation of vasodilation in COVID-19 in patient with diabetes HOIP_0041586 Wikipedia:Advanced_glycation_end-product AGEs have a range of pathological effects, such as: Increased vascular permeability. Increased arterial stiffness Inhibition of vascular dilation by interfering with nitric oxide. Oxidizing LDL. Binding cells—including macrophage, endothelial, and mesangial—to induce the secretion of a variety of cytokines. Enhanced oxidative stress. The activation of cellular RAGE on endothelium, mononuclear phagocytes, and lymphocytes triggers the generation of free radicals and the expression of inflammatory gene mediators. HOIP:HOIP_0041587 Negative regulation of response to nitric oxide is a subtype of negative regulation of response to nitric oxide: A process that stops, prevents, or reduces the frequency, rate or extent of response to nitric oxide. Negative regulation of response to nitric oxide HOIP_0041587 HOIP:HOIP_0041589 Negative regulation of response to nitric oxide is a subtype of negative regulation of response to nitric oxide: A process that stops, prevents, or reduces the frequency, rate or extent of response to nitric oxide. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. Wikipedia:Endothelium-derived_relaxing_factor Negative regulation of response to nitric oxide in COVID-19 in patient with diabetes HOIP_0041589 Wikipedia:Endothelium-derived_relaxing_factor Endothelium produces NO which then diffuses to the vascular smooth muscle tissue, although there seems to be evidence that vasodilation may also be of neuronal origin, rather than endothelial. NO is produced by the enzyme nitric oxide synthase and it relaxes smooth muscle tissue by promoting the synthesis of cGMP. HOIP:HOIP_0041590 Negative regulation of response to nitric oxide is a subtype of negative regulation of response to nitric oxide: A process that stops, prevents, or reduces the frequency, rate or extent of response to nitric oxide. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 Wikipedia:Endothelium-derived_relaxing_factor Negative regulation of response to nitric oxide in COVID-19 associated with ARDS HOIP_0041590 PMID:33077917 Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection. Wikipedia:Endothelium-derived_relaxing_factor Endothelium produces NO which then diffuses to the vascular smooth muscle tissue, although there seems to be evidence that vasodilation may also be of neuronal origin, rather than endothelial. NO is produced by the enzyme nitric oxide synthase and it relaxes smooth muscle tissue by promoting the synthesis of cGMP. HOIP:HOIP_0041591 Negative regulation of vasodilation is a subtype of negative regulation process: Any process that stops, prevents, or reduces the frequency, rate or extent of the vasodilation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 Wikipedia:Endothelium-derived_relaxing_factor negative regulation of vasodilation in COVID-19 associated with ARDS HOIP_0041591 PMID:33077917 Additional mechanisms, such as a reduction of endothelial nitric oxide synthase activity and nitric oxide levels, as well as the release of vascular endothelial growth factor (VEGF) as a consequence of the systemic hypoxia induced by ARDS, have also been proposed as key pathogenic processes underlying endothelial dysfunction following SARS-CoV-2 infection. Wikipedia:Endothelium-derived_relaxing_factor Endothelium produces NO which then diffuses to the vascular smooth muscle tissue, although there seems to be evidence that vasodilation may also be of neuronal origin, rather than endothelial. NO is produced by the enzyme nitric oxide synthase and it relaxes smooth muscle tissue by promoting the synthesis of cGMP. HOIP:HOIP_0041592 Pulmonary congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the lung. pulmonary congestion HOIP_0041592 HOIP:HOIP_0041594 Blood vessel damage in lung is a subtype of blood vessel damage: A process that injures the structure of the blood vessel in lung as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32651579 blood vessel damage in lung in COVID-19 associated with ARDS HOIP_0041594 PMID:32651579 Isolated right ventricular failure with and without confirmed pulmonary embolism has also been reported. Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. HOIP:HOIP_0041596 Any apoptotic process in a neutrophil, any of the immature or mature forms of a granular leukocyte that in its mature form has a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation neutrophil apoptotic process in coronavirus infection HOIP_0041596 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0041597 CCL2 signaling is a process that a signal is transmitted by CCL2. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. CCL2 signaling in COVID-19 HOIP_0041597 HOIP:HOIP_0041598 CCL2 signaling is a process that a signal is transmitted by CCL2. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 CCL2 signaling in severe COVID-19 HOIP_0041598 PMID:32629875 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0041599 The selective elimination of senescent neutrophils from the body by autoregulatory mechanisms. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation neutrophil clearance in coronavirus infection HOIP_0041599 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0041600 IL-2 signaling is a process that a signal is transmitted by the cytokine IL-2. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Reactome:R-HSA-451927.2 IL-2 signaling in COVID-19 HOIP_0041600 HOIP:HOIP_0041601 NCBI-Human-GeneID:177 NCBI-Mouse-GeneID:11596 NCBI-Rat-GeneID:81722 AGER (mol) HOIP_0041601 NCBI-Human-GeneID:177 http://www.ncbi.nlm.nih.gov/gene/177 NCBI-Mouse-GeneID:11596 http://www.ncbi.nlm.nih.gov/gene/11596 NCBI-Rat-GeneID:81722 http://www.ncbi.nlm.nih.gov/gene/81722 HOIP:HOIP_0041602 The appearance of anti-inflammatory cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation anti-inflammatory cytokine production in coronavirus infection HOIP_0041602 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0041603 IL-2 signaling is a process that a signal is transmitted by the cytokine IL-2. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Reactome:R-HSA-451927.2 IL-2 signaling in severe COVID-19 HOIP_0041603 HOIP:HOIP_0041604 IL-10 signaling is a process that a signal is transmitted by the cytokine IL-10. IL-10 signaling HOIP_0041604 HOIP:HOIP_0041605 Tissue regeneration is a subtype of changing material: The regrowth of lost or destroyed tissues. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. tissue regeneration in coronavirus infection HOIP_0041605 HOIP:HOIP_0041606 IL-10 signaling is a process that a signal is transmitted by the cytokine IL-10. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. IL-10 signaling in COVID-19 HOIP_0041606 HOIP:HOIP_0041608 The selective elimination of senescent neutrophils from the body by autoregulatory mechanisms. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation neutrophil clearance in COVID-19 HOIP_0041608 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0041610 Any apoptotic process in a neutrophil, any of the immature or mature forms of a granular leukocyte that in its mature form has a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation neutrophil apoptotic process in COVID-19 HOIP_0041610 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0041611 The appearance of anti-inflammatory cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation anti-inflammatory cytokine production in COVID-19 HOIP_0041611 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. HOIP:HOIP_0041612 Tissue regeneration is a subtype of changing material: The regrowth of lost or destroyed tissues. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. tissue regeneration in COVID-19 HOIP_0041612 HOIP:HOIP_0041613 IL-10 signaling is a process that a signal is transmitted by the cytokine IL-10. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. IL-10 signaling in severe COVID-19 HOIP_0041613 HOIP:HOIP_0041616 Anti-inflammatory cytokine production insufficiency is a subtype of insufficient functioning: A process that lacks performing the function of anti-inflammatory cytokine production required. anti-inflammatory cytokine production insufficiency HOIP_0041616 HOIP:HOIP_0041618 Tissue regeneration insufficiency is a subtype of insufficient functioning: A process that lacks performing the function of tissue regeneration required. tissue regeneration insufficiency HOIP_0041618 HOIP:HOIP_0041624 Resolution of inflammation 炎症の解消 convergence of inflammatory response HOIP_0041624 HOIP:HOIP_0041628 The regulated release of histamine by a cell as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. WikiPedia:Anaphylatoxin Wikipedia:Inflammation histamine secretion involved in inflammatory response in coronavirus infection HOIP_0041628 WikiPedia:Anaphylatoxin The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Redness and heat are due to increased blood flow at body core temperature to the inflamed site; swelling is caused by accumulation of fluid; pain is due to the release of chemicals such as bradykinin and histamine that stimulate nerve endings. Histamine: Stored in preformed granules, histamine is released in response to a number of stimuli. It causes arteriole dilation, increased venous permeability, and a wide variety of organ-specific effects. HOIP:HOIP_0041629 A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. WikiPedia:Anaphylatoxin smooth muscle contraction in coronavirus infection HOIP_0041629 WikiPedia:Anaphylatoxin The C3a, C4a and C5a components are referred to as anaphylatoxins: they cause smooth muscle contraction, vasodilation, histamine release from mast cells, and enhanced vascular permeability. HOIP:HOIP_0041630 Increasing sensitivity to pain is a subtype of increasing sensitivity: A process that changes the sensitivity to be lhigher. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation response to pain sensation stimulus in coronavirus infection HOIP_0041630 Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. HOIP:HOIP_0041631 The release of bradykinin following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation bradykinin secretion involved in inflammatory response in coronavirus infection HOIP_0041631 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Bradykinin: A vasoactive protein that is able to induce vasodilation, increase vascular permeability, cause smooth muscle contraction, and induce pain. HOIP:HOIP_0041632 The regulated release of a prostaglandin that contributes to the immune response. Prostaglandins are a group of biologically active metabolites which contain a cyclopentane ring. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation prostaglandin secretion involved in inflammatory response in coronavirus infection HOIP_0041632 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0041633 Any process that activates or increases the frequency, rate, or extent of fever generation. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation positive regulation of fever generation in coronavirus infection HOIP_0041633 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0041634 Increasing body temperature is a subtype of increaseing temperature: A process that increases the temperature of the body. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation increasing body temperature in coronavirus infection HOIP_0041634 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. Prostaglandins: A group of lipids that can cause vasodilation, fever, and pain. HOIP:HOIP_0041635 The release of any leukotriene following a stimulus as part of an inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation leukotriene secretion involved in inflammatory response in coronavirus infection HOIP_0041635 Wikipedia:Inflammation Upon contact with PAMPs, tissue macrophages and mastocytes release vasoactive amines such as histamine and serotonin, as well as eicosanoids such as prostaglandin E2 and leukotriene B4 to remodel the local vasculature. leukotriene B4: Able to mediate leukocyte adhesion and activation, allowing them to bind to the endothelium and migrate across it. In neutrophils, it is also a potent chemoattractant, and is able to induce the formation of reactive oxygen species and the release of lysosomal enzymes by these cells. HOIP:HOIP_0041636 Leaking fluid from blood vessel is a subtype of leaking: A process that leaks fluid out from the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. leaking fluid from blood vessel in coronavirus infection HOIP_0041636 HOIP:HOIP_0041638 Arteriolosclerosis dependent process is a subtype of disease course dependent process: A process that can constitute the course of Arteriolosclerosis. arteriolosclerosis dependent process HOIP_0041638 HOIP:HOIP_0041640 Positive regulation of complement component gene expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of complement component gene expression. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 positive regulation of complement component gene expression in severe COVID-19 HOIP_0041640 PMID:33077917 Use of an untargeted metabolomic approach also demonstrated upregulation of complement activation proteins, including membrane attack complex proteins such as C5, C6 and C8, in sera from 46 patients with severe disease. HOIP:HOIP_0041641 Hypofunction of production of anti-inflammatory cytokine is a subtype of hypofunction of protein biosynthesis: A process that performs a decreased or insufficient production of anti-inflammatory cytokine. hypofunction of anti-inflammatory cytokine production HOIP_0041641 HOIP:HOIP_0041642 Accumulation of cellular wastes is a subtype of accumulation of substances in a biological object: A process that keeps cellular wastes in an organism, tissue, organelle, or cell. deposition of cellular wastes accumulation of cellular wastes HOIP_0041642 HOIP:HOIP_0041643 Hypofunction of production of anti-inflammatory cytokine is a subtype of hypofunction of biosynthesis: A process that performs a decreased or insufficient production of anti-inflammatory cytokine. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes.The functioning level is ow. PMID:32687793 hypofunction of anti-inflammatory cytokine production in COVID-19 in patient with diabetes HOIP_0041643 PMID:32687793 Obesity and diabetes are characterised by chronic low-grade inflammation with increased concentrations of pro-inflammatory leptin and reduced anti-inflammatory adiponectin. HOIP:HOIP_0041644 A biological waste that is discarded or not utilized further in cells. cellular wastes HOIP_0041644 HOIP:HOIP_0041646 Accumulation of cellular wastes is a subtype of accumulation of substances in a biological object: A process that keeps cellular wastes in an organism, tissue, organelle, or cell. This entity is a specific course-dependent process. This process can constitute the course of arteriosclerosis course. Wikipedia:Arteriosclerosis deposition of cellular wastes accumulation of cellular wastes [arteriosclerosis course] HOIP_0041646 Wikipedia:Arteriosclerosis Arteriosclerosis is the thickening, hardening, and loss of elasticity of the walls of arteries. This process gradually restricts the blood flow to one's organs and tissues. The lesions of arteriosclerosis begin as the intima (innermost layer of blood vessel wall) of the arterial wall start to fill up with the deposition of cellular wastes. As these start to mature, they can take different forms of arteriosclerosis. All are linked through common features such as the stiffening of arterial vessels, thickening of arterial walls and degenerative nature of the disease. HOIP:HOIP_0041647 Hardening of artery is a subtype of changing hardness: A process that changes the hardness of the artery to become hard due to the replacement of normal artery to scar tissue. This entity is a specific course-dependent process. This process can constitute the course of arteriosclerosis course. Wikipedia:Arteriosclerosis hardening of artery [arteriosclerosis course] HOIP_0041647 Wikipedia:Arteriosclerosis Arteriosclerosis is the thickening, hardening, and loss of elasticity of the walls of arteries. This process gradually restricts the blood flow to one's organs and tissues. The lesions of arteriosclerosis begin as the intima (innermost layer of blood vessel wall) of the arterial wall start to fill up with the deposition of cellular wastes. As these start to mature, they can take different forms of arteriosclerosis. All are linked through common features such as the stiffening of arterial vessels, thickening of arterial walls and degenerative nature of the disease. HOIP:HOIP_0041648 Changing thickness is a subtype of changing quality: A process that changes the thickness of the object. changing thickness HOIP_0041648 HOIP:HOIP_0041649 Increasing thickness is a subtype of changing thickness: A process that increases the thickness of the object. 肥厚 increasing thickness HOIP_0041649 HOIP:HOIP_0041650 IL-12 signaling is a process that a signal is transmitted by the cytokine IL-12. IL-12 signaling HOIP_0041650 HOIP:HOIP_0041652 Increasing thickness of artery wall is a subtype of increasing thickness: A process that increases the thickness of the artery wall. increasing thickness of artery wall HOIP_0041652 HOIP:HOIP_0041655 Increasing thickness of artery wall is a subtype of increasing thickness: A process that increases the thickness of the artery wall. This entity is a specific course-dependent process. This process can constitute the course of arteriosclerosis course. Wikipedia:Arteriosclerosis increasing thickness of artery wall [arteriosclerosis course] HOIP_0041655 Wikipedia:Arteriosclerosis Arteriosclerosis is the thickening, hardening, and loss of elasticity of the walls of arteries. This process gradually restricts the blood flow to one's organs and tissues. The lesions of arteriosclerosis begin as the intima (innermost layer of blood vessel wall) of the arterial wall start to fill up with the deposition of cellular wastes. As these start to mature, they can take different forms of arteriosclerosis. All are linked through common features such as the stiffening of arterial vessels, thickening of arterial walls and degenerative nature of the disease. HOIP:HOIP_0041656 Changing elasticity is a subtype of changing quality: A process that changes the elasticity of the object. changing elasticity HOIP_0041656 HOIP:HOIP_0041657 Decreasing elasticity is a subtype of changing elasticity: A process that decreases the elasticity of the object. decreasing elasticity HOIP_0041657 HOIP:HOIP_0041659 An elasticity which is relatively low. low elasticity decreased elasticity HOIP_0041659 HOIP:HOIP_0041660 Decreasing elasticity of artery wall is a subtype of decreasing elasticity: A process that decreases the elasticity of the artery wall. decreasing elasticity of artery wall HOIP_0041660 HOIP:HOIP_0041662 Decreasing elasticity of artery wall is a subtype of decreasing elasticity: A process that decreases the elasticity of the artery wall. This entity is a specific course-dependent process. This process can constitute the course of arteriosclerosis course. Wikipedia:Arteriosclerosis decreasing elasticity of artery wall [arteriosclerosis course] HOIP_0041662 Wikipedia:Arteriosclerosis Arteriosclerosis is the thickening, hardening, and loss of elasticity of the walls of arteries. This process gradually restricts the blood flow to one's organs and tissues. The lesions of arteriosclerosis begin as the intima (innermost layer of blood vessel wall) of the arterial wall start to fill up with the deposition of cellular wastes. As these start to mature, they can take different forms of arteriosclerosis. All are linked through common features such as the stiffening of arterial vessels, thickening of arterial walls and degenerative nature of the disease. HOIP:HOIP_0041663 IL-7 signaling is a process that a signal is transmitted by the cytokine IL-7. IL-7 signaling HOIP_0041663 HOIP:HOIP_0041664 Decreasing blood flow is a subtype of decreasing flow: A process that changes the blood flow to be smaller. This entity is a specific course-dependent process. This process can constitute the course of arteriosclerosis course. Wikipedia:Arteriosclerosis decreasing blood flow [arteriosclerosis course] HOIP_0041664 Wikipedia:Arteriosclerosis Arteriosclerosis is the thickening, hardening, and loss of elasticity of the walls of arteries. This process gradually restricts the blood flow to one's organs and tissues. The lesions of arteriosclerosis begin as the intima (innermost layer of blood vessel wall) of the arterial wall start to fill up with the deposition of cellular wastes. As these start to mature, they can take different forms of arteriosclerosis. All are linked through common features such as the stiffening of arterial vessels, thickening of arterial walls and degenerative nature of the disease. HOIP:HOIP_0041665 Inflammatory response in endothelium is a subtype of inflammatory response in blood vessels: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. Wikipedia:Atherosclerosis inflammatory response in endothelium in COVID-19 in patient with diabetes HOIP_0041665 Wikipedia:Atherosclerosis Low-density lipoprotein (LDL) particles in blood plasma invade the endothelium and become oxidized, creating risk of cardiovascular disease. Initial damage to the endothelium results in an inflammatory response. Monocytes enter the artery wall from the bloodstream, with platelets adhering to the area of insult. HOIP:HOIP_0041666 Atheromatous plaque formation is a subtype of biological structure formation: A process that construcs atheromatous plaque. atheromatous plaque formation HOIP_0041666 HOIP:HOIP_0041667 IL-7 signaling is a process that a signal is transmitted by the cytokine IL-7. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. IL-7 signaling in COVID-19 HOIP_0041667 HOIP:HOIP_0041679 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 cytokine storm in COVID-19 associated with ACS HOIP_0041679 PMID:32690910 The mechanisms underlying COVID-19-induced ACS might involve plaque rupture, coronary spasm or microthrombi owing to systemic inflammation or cytokine storm. For example, activated macrophages secrete collagenases that degrade collagen, a major constituent of the fibrous cap on atherosclerotic plaques, which can lead to plaque rupture. HOIP:HOIP_0041681 The totality of all processes through which COVID-19 infection in cardiovascular system is realized. The degree of clinical manifestation is severe. severe COVID-19 in cardiovascular system course HOIP_0041681 HOIP:HOIP_0041682 Increasing troponin concentration is a subtype of increasing concentration: A process that changes the troponin concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32629875 PMID:32651579 Increasing troponin concentration in COVID-19 in cardiovascular system HOIP_0041682 PMID:32629875 Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. PMID:32651579 A greater frequency and magnitude of troponin elevations in hospitalized patients has been associated with more-severe disease and worse outcomes. HOIP:HOIP_0041683 Decreasing arterial filling is a subtype of decreasing quantity: A process that changes the amount of arterial filling to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32416769 arterial underfilling decreasing arterial filling in COVID-19 in cardiovascular system HOIP_0041683 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. HOIP:HOIP_0041684 Right ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete right ventricular function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32416769 PMID:32651579 Wikipedia:Pulmonary_heart_disease right ventricular failure right ventricular dysfunction in COVID-19 in cardiovascular system HOIP_0041684 PMID:32416769 Cardiorenal syndrome, particularly right ventricular failure secondary to COVID-19 pneumonia, might lead to kidney congestion and subsequent AKI. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Isolated right ventricular failure with and without confirmed pulmonary embolism has also been reported. Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. HOIP:HOIP_0041685 Right ventricular damage is a subtype of damaging: A process that injuries the structure of the right ventricular as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32651579 Wikipedia:Pulmonary_heart_disease right ventricular damage in COVID-19 in cardiovascular system HOIP_0041685 PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. HOIP:HOIP_0041686 Left ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete left ventricular function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32416769 Wikipedia:heart_failure left ventricular failure left ventricular dysfunction in COVID-19 in cardiovascular system HOIP_0041686 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. Wikipedia:heart_failure Failure of the left side of the heart causes blood to back up (be congested) into the lungs, causing respiratory symptoms and fatigue due to insufficient supply of oxygenated blood. For example, left ventricular failure allows pulmonary edema and pulmonary hypertension to occur, which increase stress on the right ventricle. HOIP:HOIP_0041687 Dysregulation of heartbeats is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of heartbeats appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32412710 PMID:32629875 PMID:32651579 cardiac arrhythmias dysregulation of heartbeats in COVID-19 in cardiovascular system HOIP_0041687 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. PMID:32629875 In one study, atrial arrhythmias were commonly detected in patients with severe COVID-19. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Cardiac arrhythmias, including new-onset atrial fibrillation, heart block, and ventricular arrhythmias, are also prevalent, occurring in 17% of hospitalized patients and 44% of patients in the ICU setting in a study of 138 patients from Wuhan, China. Among 393 patients with COVID-19 from a separate cohort from New York City, atrial arrhythmias were more common among patients who required mechanical ventilation than among those who did not (17.7% versus 1.9%). HOIP:HOIP_0041688 Decreasing cardiac output is a subtype of decreasing quantity: A process that changes the amount of cardiac output to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32416769 decreasing cardiac output in COVID-19 in cardiovascular system HOIP_0041688 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. HOIP:HOIP_0041689 Cardiac malfunction is a subtype of organ malfunction: A process that does not perform cardiac function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32651579 cardiac dysfunction cardiac malfunction in COVID-19 in cardiovascular system HOIP_0041689 PMID:32651579 Myocarditis is a presumed etiology of cardiac dysfunction, and the development of myocarditis may relate to viral load. HOIP:HOIP_0041690 Brain damage is a subtype of Organ damage: A process that injuries the structure of the brain as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. Wikipedia:Cerebral_infarction brain damage [brain infarction course] HOIP_0041690 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0041691 The regulated release of a tissue factor from a cell or a tissue. tissue factor secretion HOIP_0041691 HOIP:HOIP_0041692 Embolus formation in brain is a subtype of embolus formation: A process that construcs embolus in brain. embolus formation in brain HOIP_0041692 HOIP:HOIP_0041693 Embolus formation in brain is a subtype of embolus formation: A process that construcs embolus in brain. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. Wikipedia:Cerebral_infarction embolus formation in brain [brain infarction course] HOIP_0041693 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0041694 The movement of a mononuclear cell into myocardium. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 mononuclear cell migration into myocardium in COVID-19 associated with myocarditis HOIP_0041694 PMID:32629875 Consistent with cardiomyopathy, COVID-19 autopsy reports revealed the presence of a few mononuclear cell infiltrates in the myocardium, presumably recruited from the circulation through inflamed capillaries, but no obvious histological changes in the heart tissue. HOIP:HOIP_0041695 Decreasing blood pressure is a subtype of decreasing pressure: A process that changes the blood pressure to be lower. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. Wikipedia:Cerebral_infarction decreasing vascular pressure decreasing blood pressure [brain infarction course] HOIP_0041695 HOIP:HOIP_0041696 Myocardial damage is a subtype of damaging: A process that injuries the structure of the myocardial muscle as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32629875 PMID:32651579 myocardial damage in COVID-19 in cardiovascular system HOIP_0041696 PMID:32629875 Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. PMID:32651579 Systemic inflammatory response syndrome (cytokine storm) is another putative mechanism of myocardial injury. HOIP:HOIP_0041697 Myocardium malfunction is a subtype of malfunctioning process: A process that cannot perform signaling [biological] appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32629875 PMID:32651579 Myocardium malfunction in COVID-19 in cardiovascular system HOIP_0041697 PMID:32629875 COVID-19, however, appears to include an evolving set of clinical manifestation not previously reported in SARS and MERS, including stroke and cardiomyopathies associated with coagulopathy and vasculopathy, which can cause sudden death and other serious morbidities. However, cardiovascular disease is prevalent in patients with COVID-19; 7% of all patients and 22 % of severe cases experienced myocardial injury. Cases of cardiomyopathy have been reported in patients with COVID-19, raising the possibility that myocarditis-related cardiac events may be increased in COVID-19. Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. In one study, atrial arrhythmias were commonly detected in patients with severe COVID-19. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Biventricular cardiomyopathy has been reported in 7–33% of critically ill patients with COVID-19. HOIP:HOIP_0041698 Inflammatory response of myocardial capillary is a subtype of Inflammatory response in blood vessels: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32629875 inflammatory response in myocardial capillary in COVID-19 associated with myocarditis HOIP_0041698 PMID:32629875 Consistent with cardiomyopathy, COVID-19 autopsy reports revealed the presence of a few mononuclear cell infiltrates in the myocardium, presumably recruited from the circulation through inflamed capillaries, but no obvious histological changes in the heart tissue. HOIP:HOIP_0041699 Endothelium malfunction is a subtype of organ malfunction: A process that does not perform endothelium function correctly or not functioning at all. endothelium dysfunction HOIP_0041699 HOIP:HOIP_0041700 A type of myocardial cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32651579 myocardial cell necrosis in COVID-19 in cardiovascular system HOIP_0041700 PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. There is also emerging evidence of thrombosis in intravenous catheters and extracorporeal circuits, and arterial vascular occlusive events, including acute myocardial infarction (MI), acute limb ischemia, and stroke, in severely affected people in studies from the USA, Italy and France. HOIP:HOIP_0041701 brain malfunction is a subtype of organ malfunction: A process that does not perform brain function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. brain malfunction [brain infarction course] HOIP_0041701 HOIP:HOIP_0041702 Cardiac conduction systemmalfunction is a subtype of malfunction: A process that does not perform cardiac conduction system function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32651579 cardiac conduction system malfunction in COVID-19 in cardiovascular system HOIP_0041702 PMID:32651579 Cardiac arrhythmias, including new-onset atrial fibrillation, heart block, and ventricular arrhythmias, are also prevalent, occurring in 17% of hospitalized patients and 44% of patients in the ICU setting in a study of 138 patients from Wuhan, China. HOIP:HOIP_0041703 Heart damage is a subtype of damaging: A process that injuries the structure of the heart as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32412710 PMID:32629875 cardiac injury heart injury heart damage in COVID-19 in cardiovascular system HOIP_0041703 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. PMID:32629875 Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. Also, genetic and pharmacological studies in mice have shown that ACE2 regulates cardiac structure and function; decreased ACE2 in SARS-CoV-2-infected cardiomyocytes could disrupt these activities, particularly impairing cardiac remodeling and increasing oxidative stress in cardiomyocytes. HOIP:HOIP_0041704 brain malfunction is a subtype of organ malfunction: A process that does not perform brain function correctly or not functioning at all. brain malfunction HOIP_0041704 HOIP:HOIP_0041706 Increasing blood pressure in lung is a subtype of increasing blood pressure : A process that changes the blood pressure to be higher in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32651579 Wikipedia:Pulmonary_heart_disease increasing vascular pressure in lung increasing blood pressure in lung in COVID-19 in cardiovascular system HOIP_0041706 PMID:32651579 Isolated right ventricular failure with and without confirmed pulmonary embolism has also been reported. Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS), Primary pulmonary hypertension etc. For example, left ventricular failure allows pulmonary edema and pulmonary hypertension to occur, which increase stress on the right ventricle. HOIP:HOIP_0041708 Decreasing kidney perfusion is a subtype of decreasing quantity: A process that changes the amount of kidney perfusion to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32416769 kidney hypoperfusion decreasing kidney perfusion in COVID-19 in cardiovascular system HOIP_0041708 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. HOIP:HOIP_0041709 Any process that activates or increases the frequency, rate or extent of thrombus formation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32629875 PMID:33077917 positive regulation of thrombus formation (very high) in COVID-19 in cardiovascular system HOIP_0041709 PMID:32629875 Second, to infect cells, SARS-CoV-2 binds to the cell surface ACE2 receptors, and in so doing compromises the vaso-protective functions of ACE2, an enzyme that attenuates the vasoconstrictive, pro-inflammatory, pro-apoptotic, pro-thrombotic and mitogenic effects of angiotensin II, as discussed in Section 4.2. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0041711 A vesicle-mediated transport process that results in the engulfment of external particulate material by inflammatory macrophages and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 phagocytosis by inflammatory macrophage (severe)in COVID-19 in renal system HOIP_0041711 PMID:33077917 As seen in the lung, post-mortem examination of kidney specimens in a preprint study also identified deposition of C5b–9 on tubule cells and massive interstitial infiltration of macrophages as hallmarks of kidney complications in patients with severe disease. SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041713 The regulated release of a tissue factor from a cell or a tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 tissue factor production in COVID-19 associated with ACS HOIP_0041713 PMID:32690910 Activated macrophages are also known to secrete tissue factor, a potent procoagulant that triggers thrombus formation when the plaque ruptures. HOIP:HOIP_0041715 A decrease in the diameter of coronary artery, due to constriction of smooth muscle cells that line the vessels. vasoconstriction of coronary artery HOIP_0041715 HOIP:HOIP_0041716 A decrease in the diameter of coronary artery, due to constriction of smooth muscle cells that line the vessels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 vasoconstriction of coronary artery in COVID-19 associated with ACS HOIP_0041716 PMID:32690910 The mechanisms underlying COVID-19-induced ACS might involve plaque rupture, coronary spasm or microthrombi owing to systemic inflammation or cytokine storm. HOIP:HOIP_0041717 Microthrombus formation is a subtype of thrombus formation: A process that construcs microthrombus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 microthrombus formation in COVID-19 associated with ACS HOIP_0041717 PMID:32690910 The mechanisms underlying COVID-19-induced ACS might involve plaque rupture, coronary spasm or microthrombi owing to systemic inflammation or cytokine storm. HOIP:HOIP_0041718 brain malfunction is a subtype of organ malfunction: A process that does not perform brain function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32651579 brain malfunction in COVID-19 associated with cerebral infarction HOIP_0041718 PMID:32651579 More-severe presentations of COVID-19 manifest with acute stroke of varying arterial and venous mechanisms (in up to 6% of those with severe illness), and confusion or impaired consciousness (8–9%). HOIP:HOIP_0041719 Endothelium damage in kidney is a subtype of endothelium damage: A process that injuries the structure of the endothelium in kidney as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32690910 endothelium damage in heart in COVID-19 associated with ACS HOIP_0041719 PMID:32690910 Direct endothelial or vascular injury caused by SARS- CoV-2 infection might also increase the risk of thrombus formation and ACS. HOIP:HOIP_0041720 Endothelium damage in heart is a subtype of endothelium damage: A process that injuries the structure of the endothelium in heart as the direct or indirect result of an external force. endothelium damage in heart HOIP_0041720 HOIP:HOIP_0041722 Increasing troponin concentration is a subtype of increasing concentration: A process that changes the troponin concentration to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32629875 PMID:32651579 Increasing troponin concentration in COVID-19 associated with ACS HOIP_0041722 PMID:32629875 Cardiac biomarker studies, particularly elevated troponin levels, have suggested a high prevalence of cardiac injury in hospitalized COVID-19 patients. PMID:32651579 A greater frequency and magnitude of troponin elevations in hospitalized patients has been associated with more-severe disease and worse outcomes. HOIP:HOIP_0041723 Dysregulation of heartbeats is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of heartbeats appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32412710 PMID:32629875 PMID:32651579 PMID:32690910 cardiac arrhythmias dysregulation of heartbeats in COVID-19 associated with ACS HOIP_0041723 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. PMID:32629875 In one study, atrial arrhythmias were commonly detected in patients with severe COVID-19. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Cardiac arrhythmias, including new-onset atrial fibrillation, heart block, and ventricular arrhythmias, are also prevalent, occurring in 17% of hospitalized patients and 44% of patients in the ICU setting in a study of 138 patients from Wuhan, China. Among 393 patients with COVID-19 from a separate cohort from New York City, atrial arrhythmias were more common among patients who required mechanical ventilation than among those who did not (17.7% versus 1.9%). PMID:32690910 In another study in Wuhan involving 187 patients hospitalized with COVID-19, those with elevated levels of troponin T were more likely to develop malignant arrhythmias, such as ventricular tachycardia and fibrillation, than those with normal levels of troponin T (12% versus 5%). HOIP:HOIP_0041724 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32651579 PMID:33077917 establishment of virus infection in COVID-19 in renal system HOIP_0041724 PMID:32651579 ACE2 expression has been demonstrated in arterial and venous endothelium of several organs, and histopathological studies have found microscopic evidence of SARS-CoV-2 viral particles in endothelial cells of the kidneys and lungs. PMID:33077917 SARS-CoV-2 has also been found in proximal tubular cells, which exhibit high levels of ACE2 in the apical brush border. SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. Infection of endothelial cells alters glomerular capillary haemostasis and induces the formation of fibrin thrombi. Also, in support of the hypothesis that SARS-CoV-2 exerts tropism in the kidney, electron microscopy examination of autopsy samples from 26 patients who had died with COVID-19 demonstrated clusters of viral particles in the tubular epithelium and podocytes. SARS-CoV-2-induced podocyte dysfunction is likely to induce impairment of glomerular filtration, leading to proteinuria and haematuria, which are often observed in patients with coronavirus disease 2019 (COVID-19). HOIP:HOIP_0041725 Cytokine storm is a subtype of hyperfunctioning: A process that performs an excessive cytokine secretion. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32292867 PMID:32775989 cytokine storm in COVID-19 in renal system HOIP_0041725 PMID:32292867 The renal biopsy findings in the case presented here are therefore concerning for an aggressive APOL1-associated collapsing glomerulopathy driven by a COVID-19–related cytokine storm. PMID:32775989 COVID-19 infection likely caused the interferon surge as a second hit causing podocyte injury leading to collapsing focal segmental glomerulosclerosis. HOIP:HOIP_0041726 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of heart vasculature. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). PMID:32651579 viral entry into host cell in heart vasculature in COVID-19 associated with ACS SARS-CoV-2 entry to host cell in COVID-19 associated with ACS HOIP_0041726 PMID:32651579 ACE2 has high expression in cardiovascular tissue, including cardiac myocytes, fibroblasts, endothelial cells, and smooth-muscle cells in support of a possible mechanism of direct viral injury. HOIP:HOIP_0041727 Right ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete right ventricular function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 PMID:32651579 right ventricular failure right ventricular dysfunction in COVID-19 in renal system HOIP_0041727 PMID:32416769 Cardiorenal syndrome, particularly right ventricular failure secondary to COVID-19 pneumonia, might lead to kidney congestion and subsequent AKI. PMID:32651579 SARS-CoV-2 can cause both direct cardiovascular sequelae and indirect cardiovascular sequelae, including myocardial injury, acute coronary syndromes (ACS), cardiomyopathy, acute cor pulmonale, arrhythmias, and cardiogenic shock, as well as the aforementioned thrombotic complications. Isolated right ventricular failure with and without confirmed pulmonary embolism has also been reported. HOIP:HOIP_0041728 Albumin leakage into urine is a subtype of leaking: A process that leaks the albumin leakage into urine from the kidney filters. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 albumin leakage into urine in COVID-19 in renal system HOIP_0041728 PMID:33077917 In some cases, however, proteinuria is abundant or contains albumin, suggesting glomerular impairment. HOIP:HOIP_0041729 Protein leakage into urine is a subtype of leaking: A process that leaks the protein leakage into urine from the kidney filters. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 PMID:32416769 PMID:32416769 protein leakage into urine in COVID-19 in renal system HOIP_0041729 PMID:33077917 Of the organs affected by COVID-19, the kidney is one of the main sites of COVID-19 complications (Fig. 4), and abnormal renal function is a significant risk factor for death in severely ill patients with COVID-19 in the ICU setting. On admission, 43.9% of patients had proteinuria and 26.7% haematuria, whereas 5.1% of patients experienced acute kidney injury (AKI) during the study. SARS-CoV-2-induced podocyte dysfunction is likely to induce impairment of glomerular filtration, leading to proteinuria and haematuria, which are often observed in patients with coronavirus disease 2019 (COVID-19). In most patients with COVID-19, abnormal kidney function in the presence of low-level proteinuria possibly reflects tubular injury. In some cases, however, proteinuria is abundant or contains albumin, suggesting glomerular impairment. PMID:32416769 Kidney involvement is frequent in COVID-19; >40% of cases have abnormal proteinuria at hospital admission. HOIP:HOIP_0041730 Blood leakage into urine is a subtype of leaking: A process that leaks the blood (or red blood cells) leakage into urine. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 blood leakage into urine in COVID-19 in renal system HOIP_0041730 PMID:33077917 Of the organs affected by COVID-19, the kidney is one of the main sites of COVID-19 complications (Fig. 4), and abnormal renal function is a significant risk factor for death in severely ill patients with COVID-19 in the ICU setting. On admission, 43.9% of patients had proteinuria and 26.7% haematuria, whereas 5.1% of patients experienced acute kidney injury (AKI) during the study. SARS-CoV-2-induced podocyte dysfunction is likely to induce impairment of glomerular filtration, leading to proteinuria and haematuria, which are often observed in patients with coronavirus disease 2019 (COVID-19). HOIP:HOIP_0041731 Inreasing urine albumin concentration is a subtype of increasing concentration: A process that changes the albumin concentration in the urine to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 inreasing urine albumin concentration in COVID-19 in renal system HOIP_0041731 PMID:33077917 In some cases, however, proteinuria is abundant or contains albumin, suggesting glomerular impairment. HOIP:HOIP_0041732 Inreasing urine protein concentration is a subtype of increasing concentration: A process that changes the protein concentration in the urine to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 PMID:33077917 inreasing urea protein concentration in COVID-19 in renal system HOIP_0041732 PMID:32416769 Kidney involvement is frequent in COVID-19; >40% of cases have abnormal proteinuria at hospital admission. PMID:33077917 In most patients with COVID-19, abnormal kidney function in the presence of low-level proteinuria possibly reflects tubular injury. In some cases, however, proteinuria is abundant or contains albumin, suggesting glomerular impairment. HOIP:HOIP_0041733 Inreasing blood protein concentration is a subtype of increasing concentration: A process that changes the blood concentration in the urine to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 inreasing urine blood concentration in COVID-19 in renal system HOIP_0041733 PMID:33077917 Of the organs affected by COVID-19, the kidney is one of the main sites of COVID-19 complications (Fig. 4), and abnormal renal function is a significant risk factor for death in severely ill patients with COVID-19 in the ICU setting. On admission, 43.9% of patients had proteinuria and 26.7% haematuria, whereas 5.1% of patients experienced acute kidney injury (AKI) during the study. SARS-CoV-2-induced podocyte dysfunction is likely to induce impairment of glomerular filtration, leading to proteinuria and haematuria, which are often observed in patients with coronavirus disease 2019 (COVID-19). HOIP:HOIP_0041734 Tubular epithelial cells injury is a subtype of cellular damage: A process that injuries the structure of tubular epithelial cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 tubular epithelial cell injury in COVID-19 in renal system HOIP_0041734 PMID:33077917 SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041735 Tubular damage is a subtype of organ damaging: A process that injuries the structure of the tubular as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 tubular injury tubular damage in COVID-19 in renal system HOIP_0041735 PMID:33077917 SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041736 Proximal convoluted tubule brush border damage is a subtype of organ damaging: A process that injuries the structure of the proximal convoluted tubule brush border as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 renal brush border damage proximal convoluted tubule brush border damage in COVID-19 in renal system HOIP_0041736 PMID:33077917 SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041737 Renal tubule malfunction is a subtype of malfunction: A process that does not perform renal tubule function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. renal tubule malfunction in COVID-19 in renal system HOIP_0041737 HOIP:HOIP_0041738 Left ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete left ventricular function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 left ventricular failure left ventricular dysfunction in COVID-19 in renal system HOIP_0041738 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. HOIP:HOIP_0041739 Moving blood clot is a subtype of moving. A process that change the location of the blood clot. This entity is a specific course-dependent process. This process can constitute the course of cerebral infarction. Wikipedia:Cerebral_infarction moving blood clot [brain infarction course] HOIP_0041739 Wikipedia:Cerebral_infarction A cerebral infarction is an area of necrotic tissue in the brain resulting from a blockage or narrowing in the arteries supplying blood and oxygen to the brain. The restricted oxygen due to the restricted blood supply causes an ischemic stroke that can result in an infarction if the blood flow is not restored within a relatively short period of time. The blockage can be due to a thrombus, an embolus or an atheromatous stenosis of one or more arteries. HOIP:HOIP_0041740 Glomerular damage is a subtype of organ damaging: A process that injuries the structure of the glomerular as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32292867 glomerular impairment glomerular damage in COVID-19 in renal system HOIP_0041740 PMID:32292867 The renal biopsy findings in the case presented here are therefore concerning for an aggressive APOL1-associated collapsing glomerulopathy driven by a COVID-19–related cytokine storm. HOIP:HOIP_0041741 IL-7 signaling is a process that a signal is transmitted by the cytokine IL-7. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. IL-7 signaling in severe COVID-19 HOIP_0041741 HOIP:HOIP_0041742 Glomerular filtration malfunction is a subtype of malfunction: A process that does not perform glomerular filtration function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 glomerular filtration malfunction in COVID-19 in renal system HOIP_0041742 PMID:33077917 SARS-CoV-2-induced podocyte dysfunction is likely to induce impairment of glomerular filtration, leading to proteinuria and haematuria, which are often observed in patients with coronavirus disease 2019 (COVID-19). In some cases, however, proteinuria is abundant or contains albumin, suggesting glomerular impairment. HOIP:HOIP_0041743 Hardening of glomeruli in kidney is a subtype of changing hardness: A process that changes the hardness of the glomeruli in the kidney to become hard due to the replacement of normal glomeruli to scar tissue. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32292867 PMID:32775989 PMID:33077917 hardening of glomeruli in kidney in COVID-19 in renal system HOIP_0041743 PMID:32292867 The renal biopsy findings in the case presented here are therefore concerning for an aggressive APOL1-associated collapsing glomerulopathy driven by a COVID-19–related cytokine storm. PMID:32775989 COVID-19 infection likely caused the interferon surge as a second hit causing podocyte injury leading to collapsing focal segmental glomerulosclerosis. PMID:33077917 However, renal vasculopathy has not been consistently found in the kidney and no significant glomerular disease has been described, with the exception of collapsing focal segmental glomerulosclerosis, which has been reported in a few patients and seems to be associated with the presence of genetic ‘risk’ variants of APOL1. HOIP:HOIP_0041744 Decreasing oral intake is a subtype of decreasing quantity: A process that changes the quantity of the oral (food) intake to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 decreasing oral intake in COVID-19 in renal system HOIP_0041744 PMID:33077917 Several non-specific mechanisms may contribute to the development of AKI in the setting of COVID-19, including haemodynamic alterations, cardiac dysfunction, hypovolaemia due to poor oral intake or high-grade fever, use of nephrotoxic drugs and nosocomial sepsis. HOIP:HOIP_0041745 Kidney congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the Kidney. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 renal congestion kidney congestion in COVID-19 in renal system HOIP_0041745 PMID:32416769 Cardiorenal syndrome, particularly right ventricular failure secondary to COVID-19 pneumonia, might lead to kidney congestion and subsequent AKI. HOIP:HOIP_0041746 Decreasing kidney perfusion is a subtype of decreasing quantity: A process that changes the amount of kidney perfusion to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 PMID:32694793 kidney hypoperfusion decreasing kidney perfusion in COVID-19 in renal system HOIP_0041746 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. PMID:32694793 The damage to the blood vessels caused by hypertension decreases blood flow to the kidneys and consequently results in kidney injury (Fig. 2). HOIP:HOIP_0041747 Narrowing of the renal artery is a subtype of decreasing cross-sectional area: A process that changes the cross-sectional area of the renal arteries to be smaller. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. narrowing of the retinal artery in COVID-19 in renal system HOIP_0041747 HOIP:HOIP_0041748 A type of renal cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. renal cell necrosis in COVID-19 in renal system HOIP_0041748 HOIP:HOIP_0041749 Renal fibrosis is a subtype of fibrosis: A process that replaces renal tissues to fibrous connective tissues, usually as a consequence of inflammation or other injury. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 renal fibrosis in COVID-19 in renal system HOIP_0041749 PMID:33077917 ACE2 internalization following SARS-CoV-2 infection could induce an imbalance in the renin–angiotensin–aldosterone system, with increased Ang II signalling leading to pro-inflammatory and profibrotic processes in the kidney. HOIP:HOIP_0041750 Negative regulation of ACE2 activation in kidney is a subtype of Negative regulation of enzyme activation: A process that stops, prevents, or reduces the frequency, rate or extent of ACE2 activation in kidney. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 Negative regulation of ACE2 activation in kidney (very high) in COVID-19 in renal system HOIP_0041750 PMID:33077917 ACE2 internalization following SARS-CoV-2 infection could induce an imbalance in the renin–angiotensin–aldosterone system, with increased Ang II signalling leading to pro-inflammatory and profibrotic processes in the kidney. HOIP:HOIP_0041751 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of kidney. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 PMID:33077917 viral entry into host cell in kidney in COVID-19 in renal system SARS-CoV-2 entry to host cell in COVID-19 in kidney in renal system HOIP_0041751 PMID:32416769 Furthermore, virus particles were reported to be present in renal endothelial cells, indicating viraemia as a possible cause of endothelial damage in the kidney and a probable contributor to AKI. PMID:33077917 SARS-CoV-2 has also been found in proximal tubular cells, which exhibit high levels of ACE2 in the apical brush border. SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. Infection of endothelial cells alters glomerular capillary haemostasis and induces the formation of fibrin thrombi. Also, in support of the hypothesis that SARS-CoV-2 exerts tropism in the kidney, electron microscopy examination of autopsy samples from 26 patients who had died with COVID-19 demonstrated clusters of viral particles in the tubular epithelium and podocytes. SARS-CoV-2-induced podocyte dysfunction is likely to induce impairment of glomerular filtration, leading to proteinuria and haematuria, which are often observed in patients with coronavirus disease 2019 (COVID-19). HOIP:HOIP_0041752 Inflammatory response in kidney is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 inflammation in kidney inflammatory response in kidney in COVID-19 in renal system HOIP_0041752 PMID:33077917 ACE2 internalization following SARS-CoV-2 infection could induce an imbalance in the renin–angiotensin–aldosterone system, with increased Ang II signalling leading to pro-inflammatory and profibrotic processes in the kidney. HOIP:HOIP_0041753 Any process that activates or increases the frequency, rate or extent of the inflammatory response in kidney. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 positive regulation of inflammatory response in kidney (very high) in COVID-19 in renal system HOIP_0041753 PMID:33077917 ACE2 internalization following SARS-CoV-2 infection could induce an imbalance in the renin–angiotensin–aldosterone system, with increased Ang II signalling leading to pro-inflammatory and profibrotic processes in the kidney. HOIP:HOIP_0041754 Vacuolar degeneration in kidney is a subtype of vacuolar degeneration: A process that degenerates vacuole. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 vacuolar degeneration in tubular epithelial cells in COVID-19 in renal system HOIP_0041754 PMID:33077917 SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041755 Positive regulation of cell adhesion molecule expression is a subtype of positive regulation of gene expression: A process that modulates the frequency, rate or extent of cell adhesion molecule expression. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 positive regulation of cell adhesion molecule expression in COVID-19 HOIP_0041755 PMID:33077917 C5a stimulates cytokine release, increases vascular permeability and induces the upregulation of adhesion molecules that favour leukocyte extravasation and transmigration into lung parenchyma - pathological events that are all observed in severe cases of COVID-19. Mechanistically, disruption of the endothelial barrier by SARS-CoV-2 spike protein is mediated by changes in the surface expression of intracellular adhesion molecule-1 (ICAM1), vascular cell adhesion protein-1 (VCAM1) and the tight junction scaffold protein zonula occludens-1 (ZO-1), as reported by a preprint study. The adhesive phenotype of endothelial cells induced by inflammatory cytokines and chemokines promotes infiltration of neutrophils, which produce large amounts of histotoxic mediators, including reactive oxygen species (ROS) and neutrophil extracellular traps (NETs), ultimately leading to injury of endothelial cells. HOIP:HOIP_0041756 Fibrin thrombus formation in glomerular capillary in COVID-19 in renal system is a subtype of thrombus formation: A process that construcs fibrin thrombus in glomerular capillaries. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 fibrin thrombus formation in glomerular capillary in COVID-19 in renal system HOIP_0041756 PMID:33077917 Infection of endothelial cells alters glomerular capillary haemostasis and induces the formation of fibrin thrombi. One autopsy study identified limited fibrin thrombi in glomerular capillaries of kidney specimens from patients with COVID-19 with severe disease. HOIP:HOIP_0041758 The migration of a monocyte from the blood vessels into kidney. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 monocyte extravasation into kidney (very high) in COVID-19 in renal system HOIP_0041758 PMID:33077917 As seen in the lung, post-mortem examination of kidney specimens in a preprint study also identified deposition of C5b–9 on tubule cells and massive interstitial infiltration of macrophages as hallmarks of kidney complications in patients with severe disease. SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041759 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of lung. The process ends when the viral nucleic acid is released into the host cell cytoplasm. viral entry into host cell in lung HOIP_0041759 HOIP:HOIP_0041760 Cell killing in kidney caused by the membrane attack complex formed following complement activation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 complement-dependent cytotoxicity in renal tubular cells in COVID-19 in renal system HOIP_0041760 PMID:33077917 SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041761 Kidney Ischemia is a changing process to lack enough to blood supply of kidney. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. kidney Ischemia in COVID-19 in renal system HOIP_0041761 HOIP:HOIP_0041762 Decreasing renal blood flow is a subtype of decreasing flow: A process that changes the amount of renal flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. decreasing renal blood flow in COVID-19 in renal system HOIP_0041762 HOIP:HOIP_0041763 kidney malfunction is a subtype of organ malfunction: A process that does not perform kidney function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32412710 PMID:32416769 PMID:32694793 PMID:33077917 renal malfunction kidney injury renal failure kidney malfunction in COVID-19 in renal system HOIP_0041763 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. PMID:32416769 Acute kidney injury (AKI) is common among critically ill patients with COVID-19, affecting approximately 20–40% of patients admitted to intensive care according to experience in Europe and the USA, and it is considered a marker of disease severity and a negative prognostic factor for survival. The cause of kidney involvement in COVID-19 is likely to be multifactorial, with cardiovascular comorbidity and predisposing factors (eg, sepsis, hypovolaemia, and nephrotoxins) as important contributors. PMID:32694793 The damage to the blood vessels caused by hypertension decreases blood flow to the kidneys and consequently results in kidney injury (Fig. 2). PMID:33077917 Of the organs affected by COVID-19, the kidney is one of the main sites of COVID-19 complications (Fig. 4), and abnormal renal function is a significant risk factor for death in severely ill patients with COVID-19 in the ICU setting. On admission, 43.9% of patients had proteinuria and 26.7% haematuria, whereas 5.1% of patients experienced acute kidney injury (AKI) during the study. As seen in the lung, post-mortem examination of kidney specimens in a preprint study also identified deposition of C5b–9 on tubule cells and massive interstitial infiltration of macrophages as hallmarks of kidney complications in patients with severe disease. In most patients with COVID-19, abnormal kidney function in the presence of low-level proteinuria possibly reflects tubular injury. In some cases, however, proteinuria is abundant or contains albumin, suggesting glomerular impairment. SARS-CoV-2- induced podocyte dysfunction is likely to induce impairment of glomerular filtration, leading to proteinuria and haematuria, which are often observed in patients with coronavirus disease 2019 (COVID-19). Infection of endothelial cells alters glomerular capillary haemostasis and induces the formation of fibrin thrombi. SARS-CoV-2 has also been found in proximal tubular cells, which exhibit high levels of ACE2 in the apical brush border. SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. HOIP:HOIP_0041764 Any process that activates or increases the frequency, rate or extent of thrombus formation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32629875 PMID:33077917 positive regulation of thrombus formation (very high) in COVID-19 in renal system HOIP_0041764 PMID:32629875 Second, to infect cells, SARS-CoV-2 binds to the cell surface ACE2 receptors, and in so doing compromises the vaso-protective functions of ACE2, an enzyme that attenuates the vasoconstrictive, pro-inflammatory, pro-apoptotic, pro-thrombotic and mitogenic effects of angiotensin II, as discussed in Section 4.2. PMID:33077917 Activated endothelial cells initiate coagulation by expressing P-selectin, von Willebrand factor (vWf) and fibrinogen, leading to massive platelet binding, fibrin formation and clotting of red blood cells (RBCs), ultimately resulting in systemic thrombosis and disseminated intravascular coagulation. HOIP:HOIP_0041765 Viral entry into bloodstream is a subtype of moving A to the inside of B: A process that of the movement of virus into bloodstream. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 viral entry into bloodstream in COVID-19 in renal system HOIP_0041765 PMID:32416769 Furthermore, virus particles were reported to be present in renal endothelial cells, indicating viraemia as a possible cause of endothelial damage in the kidney and a probable contributor to AKI. HOIP:HOIP_0041766 Decreasing blood is a subtype of decreasing quantity: A process that changes the quantity of the blood to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 PMID:33077917 decreasing blood in COVID-19 in renal system HOIP_0041766 PMID:32416769 The cause of kidney involvement in COVID-19 is likely to be multifactorial, with cardiovascular comorbidity and predisposing factors (eg, sepsis, hypovolaemia, and nephrotoxins) as important contributors. PMID:33077917 Several non-specific mechanisms may contribute to the development of AKI in the setting of COVID-19, including haemodynamic alterations, cardiac dysfunction, hypovolaemia due to poor oral intake or high-grade fever, use of nephrotoxic drugs and nosocomial sepsis. HOIP:HOIP_0041767 Blood vessel damage is a subtype of damaging: A process that injures the structure of the blood vessel as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32694793 blood vessel damage in COVID-19 in renal system HOIP_0041767 PMID:32694793 The damage to the blood vessels caused by hypertension decreases blood flow to the kidneys and consequently results in kidney injury (Fig. 2). HOIP:HOIP_0041768 The totality of all processes through which COVID-19 infection in nervous system is realized. COVID-19 course in nervous system HOIP_0041768 HOIP:HOIP_0041769 Thrombus formation in coronary artery is a subtype of thrombus formation: A process that construcs thrombus in coronary artery. This entity is a specific course-dependent process. This process can constitute the course of myocardial infarction. thrombus formation in coronary artery [myocardial infarction course] HOIP_0041769 HOIP:HOIP_0041770 Endothelium malfunction is a subtype of organ malfunction: A process that does not perform endothelium function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. endothelium dysfunction [endotheliitis course] HOIP_0041770 HOIP:HOIP_0041771 Malfunctioning of cognitive function is a subtype of malfunctioning process: A process that cannot perform cognitive function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. malfunctioning of cognitive function in COVID-19 in nervous system HOIP_0041771 HOIP:HOIP_0041772 brain malfunction is a subtype of organ malfunction: A process that does not perform brain function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. PMID:32651579 brain malfunction in COVID-19 in nervous system HOIP_0041772 PMID:32651579 More-severe presentations of COVID-19 manifest with acute stroke of varying arterial and venous mechanisms (in up to 6% of those with severe illness), and confusion or impaired consciousness (8–9%). HOIP:HOIP_0041773 Nervous system damage is a subtype of damaging: A process that injures the structure of the nervous system as the direct or indirect result of an external force. nervous system damage HOIP_0041773 HOIP:HOIP_0041774 Nervous system damage is a subtype of damaging: A process that injures the structure of the nervous system as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in nervous system. nervous system damage in COVID-19 in nervous system HOIP_0041774 HOIP:HOIP_0041775 Endothelium damage in brain is a subtype of endothelium damage: A process that injuries the structure of the endothelium in brain as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. PMID:32629875 endothelium damage in brain in COVID-19 associated with cerebral infarction HOIP_0041775 PMID:32629875 Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. HOIP:HOIP_0041777 Increasing intracranial pressure is a subtype of increasing pressure: A process that changes the intracranial pressure to be higher. increasing intracranial pressure HOIP_0041777 HOIP:HOIP_0041778 Increasing intracranial pressure is a subtype of increasing pressure: A process that changes the intracranial pressure to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. Wikipedia:Intracranial_hemorrhage increasing intracranial pressure in COVID-19 in nervous system HOIP_0041778 Wikipedia:Intracranial_hemorrhage Intracranial hemorrhage is a serious medical emergency because the buildup of blood within the skull can lead to increases in intracranial pressure, which can crush delicate brain tissue or limit its blood supply. HOIP:HOIP_0041779 Increasing intracranial pressure is a subtype of increasing pressure: A process that changes the intracranial pressure to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with cerebral infarction. increasing intracranial pressure in COVID-19 associated with cerebral infarction HOIP_0041779 HOIP:HOIP_0041780 Increasing blood pressure is a subtype of increasing pressure: A process that changes the blood pressure to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. Wikipedia:Posterior_reversible_encephalopathy_syndrome increasing vascular pressure increasing blood pressure in COVID-19 in nervous system HOIP_0041780 Wikipedia:Posterior_reversible_encephalopathy_syndrome Common underlying causes are severely elevated blood pressure, kidney failure, severe infections, certain medications, some autoimmune diseases, and pre-eclampsia. The excessive pressure damages the endothelial layer and the blood-brain barrier, leading to swelling (edema). HOIP:HOIP_0041781 Decreasing brain blood flow is a subtype of decreasing flow: A process that changes the amount of brain blood flow to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the nervous system. decreasing brain blood flow in COVID-19 in nervous system HOIP_0041781 HOIP:HOIP_0041782 Loss of vessel barrier integrity is a subtype of loss of function (process): A process that results in no longer having a loss of vessel barrier integrity function or the process that gradually loses it. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. loss of vessel barrier integrity [endotheliitis course] HOIP_0041782 HOIP:HOIP_0041783 Leaking fluid from blood vessel is a subtype of leaking: A process that leaks fluid out from the blood vessel. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. leaking fluid from blood vessel [endotheliitis course] HOIP_0041783 HOIP:HOIP_0041784 Edema in surrounding tissues is a subtype of edema: A process that keeps an excessive fluid in surrounding tissues. edema in the surrounding tissues HOIP_0041784 HOIP:HOIP_0041785 Edema in surrounding tissues is a subtype of edema: A process that keeps an excessive fluid in surrounding tissues. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. Wikipedia:Endotheliitis Wikipedia:Endothelium edema in the surrounding tissues [endotheliitis course] HOIP_0041785 Wikipedia:Endotheliitis Endotheliitis is an immune response within the endothelium in blood vessels, in which they become inflamed. The condition can cause oedema of the surrounding tissue, including the stroma, and can cause irritation and pain. Wikipedia:Endothelium Excessive or prolonged increases in permeability of the endothelium, as in cases of chronic inflammation, may lead to tissue swelling (edema). HOIP:HOIP_0041786 Increasing vascular permeabilization is a subtype of changing permeability: A process that changes the permeability of the vascular to be higher. This entity is a specific course-dependent process. This process can constitute the course of endotheliitis. Wikipedia:Endothelium increasing vascular permeabilization [endotheliitis course] HOIP_0041786 Wikipedia:Endothelium Excessive or prolonged increases in permeability of the endothelium, as in cases of chronic inflammation, may lead to tissue swelling (edema). HOIP:HOIP_0041789 Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:33077917 complement activation (very high) in COVID-19 in renal system HOIP_0041789 PMID:33077917 We also examine emerging data in support of a role for SARS-CoV-2 infection in inducing widespread endothelial damage, complement-associated blood clotting and systemic microangiopathy, and describe how these consequences may contribute to the development of kidney complications in severely ill patients with COVID-19. SARS-CoV-2 infection leads to loss of the brush border and vacuolar degeneration in tubular epithelial cells, with luminal debris composed of necrotic epithelium with evidence of complement activation and membrane attack complex (MAC) (C5b–9) deposition on tubular cells and massive macrophage infiltration in the kidney interstitium. As seen in the lung, post-mortem examination of kidney specimens in a preprint study also identified deposition of C5b–9 on tubule cells and massive interstitial infiltration of macrophages as hallmarks of kidney complications in patients with severe disease. HOIP:HOIP_0041790 Increasing blood pressure is a subtype of increasing pressure: A process that changes the blood pressure to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32694793 increasing vascular pressure increasing blood pressure in COVID-19 in renal system HOIP_0041790 PMID:32694793 The damage to the blood vessels caused by hypertension decreases blood flow to the kidneys and consequently results in kidney injury (Fig. 2). HOIP:HOIP_0041791 A decrease in the diameter of blood vessels in lung, due to constriction of smooth muscle cells that line the vessels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32651579 Wikipedia:Pulmonary_heart_disease vasoconstriction in lung in COVID-19 associated with ARDS HOIP_0041791 PMID:32651579 Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. Wikipedia:Pulmonary_heart_disease The pathophysiology of pulmonary heart disease (cor pulmonale) has always indicated that an increase in right ventricular afterload causes RV failure (pulmonary vasoconstriction, anatomic disruption/pulmonary vascular bed and increased blood viscosity are usually involved), however most of the time, the right ventricle adjusts to an overload in chronic pressure. HOIP:HOIP_0041792 A decrease in the diameter of blood vessels in lung, due to constriction of smooth muscle cells that line the vessels. vasoconstriction in lung HOIP_0041792 HOIP:HOIP_0041794 A decrease in the diameter of blood vessels in lung, due to constriction of smooth muscle cells that line the vessels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32651579 Wikipedia:Pulmonary_heart_disease vasoconstriction in lung in COVID-19 in cardiovascular system HOIP_0041794 PMID:32651579 Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. Wikipedia:Pulmonary_heart_disease The pathophysiology of pulmonary heart disease (cor pulmonale) has always indicated that an increase in right ventricular afterload causes RV failure (pulmonary vasoconstriction, anatomic disruption/pulmonary vascular bed and increased blood viscosity are usually involved), however most of the time, the right ventricle adjusts to an overload in chronic pressure. HOIP:HOIP_0041795 A decrease in the diameter of blood vessels in lung, due to constriction of smooth muscle cells that line the vessels. This entity is a specific course-dependent process. This process can constitute the course of acute cor pulmonale. Wikipedia:Pulmonary_heart_disease vasoconstriction in lung [acute cor pulmonale course] HOIP_0041795 Wikipedia:Pulmonary_heart_disease The pathophysiology of pulmonary heart disease (cor pulmonale) has always indicated that an increase in right ventricular afterload causes RV failure (pulmonary vasoconstriction, anatomic disruption/pulmonary vascular bed and increased blood viscosity are usually involved), however most of the time, the right ventricle adjusts to an overload in chronic pressure. HOIP:HOIP_0041796 Blood vessel damage in lung is a subtype of blood vessel damage: A process that injuries the structure of the blood vessel in lung as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of acute cor pulmonale. Wikipedia:Pulmonary_heart_disease blood vessel damage in lung [acute cor pulmonale course] HOIP_0041796 Wikipedia:Pulmonary_heart_disease The pathophysiology of pulmonary heart disease (cor pulmonale) has always indicated that an increase in right ventricular afterload causes RV failure (pulmonary vasoconstriction, anatomic disruption/pulmonary vascular bed and increased blood viscosity are usually involved), however most of the time, the right ventricle adjusts to an overload in chronic pressure. HOIP:HOIP_0041797 Blood vessel damage in lung is a subtype of blood vessel damage: A process that injures the structure of the blood vessel in lung as the direct or indirect result of an external force. blood vessel damage in lung HOIP_0041797 HOIP:HOIP_0041798 The directed movement of a virus, or part of a virus into kidney. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 transport of virus into kidne (very high) in COVID-19 in renal system HOIP_0041798 PMID:32416769 Furthermore, virus particles were reported to be present in renal endothelial cells, indicating viraemia as a possible cause of endothelial damage in the kidney and a probable contributor to AKI. HOIP:HOIP_0041799 Left ventricular dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete left ventricular function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). Wikipedia:heart_failure left ventricular failure left ventricular dysfunction in COVID-19 associated with ARDS HOIP_0041799 Wikipedia:heart_failure Failure of the left side of the heart causes blood to back up (be congested) into the lungs, causing respiratory symptoms and fatigue due to insufficient supply of oxygenated blood. For example, left ventricular failure allows pulmonary edema and pulmonary hypertension to occur, which increase stress on the right ventricle. HOIP:HOIP_0041800 Decreasing cardiac output is a subtype of decreasing quantity: A process that changes the amount of cardiac output to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). Wikipedia:heart_failure decreasing cardiac output in COVID-19 associated with ARDS HOIP_0041800 Wikipedia:heart_failure Failure of the left side of the heart causes blood to back up (be congested) into the lungs, causing respiratory symptoms and fatigue due to insufficient supply of oxygenated blood. For example, left ventricular failure allows pulmonary edema and pulmonary hypertension to occur, which increase stress on the right ventricle. HOIP:HOIP_0041801 Dysregulation of matrix metallopeptidase secretion is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of matrix metallopeptidase secretion process appropriately or cannot realize it at all. dysregulation of matrix metalloproteinase secretion in endothelium HOIP_0041801 HOIP:HOIP_0041803 Endothelium inflammatory response in heart is a subtype of inflammatory response in endothelium: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. endothelium inflammatory response in heart HOIP_0041803 HOIP:HOIP_0041804 The appearance of chemokine (C-C motif) ligand 2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 monocyte chemoattractant protein-1 production CCL2 production in COVID-19 HOIP_0041804 PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0041805 The appearance of chemokine (C-C motif) ligand 2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 monocyte chemoattractant protein-1 production CCL2 production (very high) in severe COVID-19 HOIP_0041805 PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0041806 Endothelium inflammatory response in heart is a subtype of inflammatory response in endothelium: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute coronary syndrome (ACS). endothelium inflammatory response in heart in COVID-19 associated with ACS HOIP_0041806 HOIP:HOIP_0041808 Dysregulation of matrix metallopeptidase secretion is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of matrix metallopeptidase secretion process appropriately or cannot realize it at all. PMID:32422178 dysregulation of matrix metalloproteinase secretion in endothelium in COVID-19 associated with ARDS HOIP_0041808 PMID:32422178 Multiple aberrant host pathways interconnect to result in pulmonary fibrosis in a subset of individuals who develop ARDS. Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. HOIP:HOIP_0041809 Innate immune responses in lung are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32843733 innate immunity in lung innate immune response in lung (very high)in COVID-19 associated with ARDS HOIP_0041809 PMID:32843733 The damaged cells in the lungs elicit a strong innate immune response, which seems to be largely mediated by pro-inflammatory macrophages and granulocytes. This response is thought to be responsible for the cytokine release syndrome or ‘cytokine storm’ that is believed to contribute to ARDS. HOIP:HOIP_0041811 Thrombus formation in lung is a subtype of thrombus formation: A process that construcs thrombus in lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 PMID:32651579 PMID:33077917 PMID:33214651 thrombus formation in lung (very high) in COVID-19 associated with ARDS HOIP_0041811 PMID:32629875 Most commonly in the lungs but also in other sites distant from the lungs, including the small bowel, brain, kidney, heart, liver and skin, the vessels display a combination of thrombosis, hemorrhage, edema, inflammation, endothelial cell death and intussusceptive vascular sprouting. Another report on 11 randomly selected COVID-19 autopsies described macroscopic pulmonary thrombi in all cases with associated pulmonary infarcts in 9/11 autopsies. Post-mortem histopathologic analysis of lung tissue from 38 COVID-19 patients documented the presence of platelet-fibrin thrombi in lung arterioles of most (33/38) cases, congested capillaries (33/38) proximal to hemorrhagic alveoli often containing CD61+ megakaryocytes, and dense capillary foci presumably resulting from vessel intussusceptive sprouting (18/38). PMID:32651579 Moreover, isolated right ventricular dysfunction may occur as a result of elevated pulmonary vascular pressures secondary to ARDS, pulmonary thromboembolism, or potentially virus-mediated injury to vascular endothelial and smoothmuscle tissue. PMID:33077917 Activation of the complement system leads to endothelial cell injury and death with subsequent vascular denudation and exposure of the thrombogenic basement membrane, which drives activation of clotting cascades. These events result in inflammation, microvascular thrombosis, vessel oedema and haemorrhagic sequelae - all of which are prominent features of the lung pathology of patients with COVID-19-associated pneumonia. PMID:33214651 Additionally, autopsy reports of patients with COVID-19 indicate that thrombosis in small vessels (platelet-rich thrombotic microangiopathy), with or without haemorrhage, is associated with ARDS. In these patients, increased small-vessel thrombosis was associated with the typical ARDS pathology of diffusely oedematous lungs. This platelet response involving IL-1beta and other cytokines might possibly contribute to COVID-19-associated ARDS. HOIP:HOIP_0041819 Any processes of signals generated as a consequence of a pattern recognition receptor (PRR) binding to damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. ダメージ関連分子パターン誘導パターン認識受容体シグナル伝達 DAMP-triggered pattern recognition receptor signaling HOIP_0041819 HOIP:HOIP_0041824 Pulmonary congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). Wikipedia:heart_failure pulmonary congestion in COVID-19 associated with ARDS HOIP_0041824 Wikipedia:heart_failure Failure of the left side of the heart causes blood to back up (be congested) into the lungs, causing respiratory symptoms and fatigue due to insufficient supply of oxygenated blood. For example, left ventricular failure allows pulmonary edema and pulmonary hypertension to occur, which increase stress on the right ventricle. HOIP:HOIP_0041825 NCBI-Human-GeneID:55922 NCBI-Mouse-GeneID:77286 NF-kappaB repressing factor NKRF (mol) HOIP_0041825 NCBI-Human-GeneID:55922 http://www.ncbi.nlm.nih.gov/gene/55922 NCBI-Mouse-GeneID:77286 http://www.ncbi.nlm.nih.gov/gene/77286 HOIP:HOIP_0041826 Decreasing cardiac output is a subtype of decreasing quantity: A process that changes the amount of cardiac output to be lower. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 decreasing cardiac output in COVID-19 in renal system HOIP_0041826 PMID:32416769 Similarly, left ventricular dysfunction might lead to low cardiac output, arterial underfilling, and kidney hypoperfusion. HOIP:HOIP_0041827 Glomerular visceral epithelial cell injury is a subtype of cellular damage: A process that injuries the structure of the glomerular visceral epithelial cell. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32775989 PMID:33077917 glomerular visceral epithelial cell injury in COVID-19 in renal system HOIP_0041827 PMID:32775989 COVID-19 infection likely caused the interferon surge as a second hit causing podocyte injury leading to collapsing focal segmental glomerulosclerosis. PMID:33077917 SARS-CoV-2-induced podocyte dysfunction is likely to induce impairment of glomerular filtration, leading to proteinuria and haematuria, which are often observed in patients with coronavirus disease 2019 (COVID-19). HOIP:HOIP_0041828 The appearance of interleukin-6 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32843733 interleukin-6 production (very high) in COVID-19 associated with ARDS HOIP_0041828 PMID:32843733 Levels of inflammatory cytokines such as IL-1, TNF and IL-6 can be high in the lungs of patients with COVID-19; therefore, blocking one or more of these cytokines could potentially benefit these individuals by reducing the severity of the cytokine storm and ARDS. HOIP:HOIP_0041829 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell of lung. The process ends when the viral nucleic acid is released into the host cell cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). viral entry into host cell in lung (very high) in COVID-19 associated with ARDS SARS-CoV-2 entry to host cell (very high) in COVID-19 associated with ARDS HOIP_0041829 HOIP:HOIP_0041830 kallikrein signaling is a process that a signal is transmitted by the kallikrein. kallikrein signaling HOIP_0041830 HOIP:HOIP_0041831 kallikrein signaling is a process that a signal is transmitted by the kallikrein. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 kallikrein signaling in COVID-19 HOIP_0041831 PMID:33077917 Furthermore, reduced expression of ACE2 might in turn indirectly activate the kallikrein–kinin system (KKS), which ultimately leads to increases in vascular permeability. Additionally, the reduction in levels of ACE2 limits the degradation of des-Arg9 bradykinin (DABK) into inactive peptides, ultimately leading to increased pro-thrombotic signalling via the activation of bradykinin receptors (BKRs). HOIP:HOIP_0041832 Any process that activates or increases the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33214651 positive regulation of innate immune response in COVID-19 associated with ARDS HOIP_0041832 PMID:33214651 Increased production of inflammatory chemokines and cytokines (many from platelets) and an excessive or uncontrolled innate immune response are typical characteristics of ARDS, including in the ARDS seen in COVID-19. HOIP:HOIP_0041836 Negative regulation of response to nitric oxide is a subtype of negative regulation of response to nitric oxide: A process that stops, prevents, or reduces the frequency, rate or extent of response to nitric oxide. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Endothelium-derived_relaxing_factor Negative regulation of response to nitric oxide in severe COVID-19 HOIP_0041836 Wikipedia:Endothelium-derived_relaxing_factor Endothelium produces NO which then diffuses to the vascular smooth muscle tissue, although there seems to be evidence that vasodilation may also be of neuronal origin, rather than endothelial. NO is produced by the enzyme nitric oxide synthase and it relaxes smooth muscle tissue by promoting the synthesis of cGMP. HOIP:HOIP_0041837 Negative regulation of vasodilation is a subtype of negative regulation process: Any process that stops, prevents, or reduces the frequency, rate or extent of the vasodilation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Endothelium-derived_relaxing_factor negative regulation of vasodilation in severe COVID-19 HOIP_0041837 Wikipedia:Endothelium-derived_relaxing_factor Endothelium produces NO which then diffuses to the vascular smooth muscle tissue, although there seems to be evidence that vasodilation may also be of neuronal origin, rather than endothelial. NO is produced by the enzyme nitric oxide synthase and it relaxes smooth muscle tissue by promoting the synthesis of cGMP. HOIP:HOIP_0041838 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32629875 PMID:32651579 PMID:32843733 establishment of virus infection in COVID-19 associated with ARDS HOIP_0041838 PMID:32629875 The presence of SARS-CoV-2 in the lung of patients with COVID-19 has been documented by immunostaining, detection of viral RNA, and electron microscopy. SARS-CoV-2 infects humans through the respiratory track by infecting and replicating in the epithelial cells that line the upper and lower respiratory track. In the lungs, the virus can cause COVID-19 pneumonia. PMID:32651579 ACE2 expression has been demonstrated in arterial and venous endothelium of several organs, and histopathological studies have found microscopic evidence of SARS-CoV-2 viral particles in endothelial cells of the kidneys and lungs. PMID:32843733 If the protective immune response is impaired, the virus is allowed to replicate and can cause widespread tissue damage. The lungs seem to be the main target, although other organs with high ACE2 expression, such as the intestine, heart, brain and kidney, might also be vulnerable. HOIP:HOIP_0041839 Pulmonary edema is a subtype of edema: A process that keeps fluids in the lung. pulmonary edema HOIP_0041839 HOIP:HOIP_0041840 Pulmonary edema is a subtype of edema: A process that keeps fluids in the lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32412710 pulmonary edema in COVID-19 associated with ARDS HOIP_0041840 PMID:32412710 Progressive respiratory failure develops in many patients with severe Covid-19 soon after the onset of dyspnea and hypoxemia. These patients commonly meet the criteria for the acute respiratory distress syndrome (ARDS), which is defined as the acute onset of bilateral infiltrates, severe hypoxemia, and lung edema that is not fully explained by cardiac failure or fluid overload. HOIP:HOIP_0041841 Pulmonary congestion is a subtype of hyperfunctioning of accumulation: A process that performs an excessive accumulation of blood in the lung. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. Wikipedia:heart_failure pulmonary congestion in COVID-19 in cardiovascular system HOIP_0041841 Wikipedia:heart_failure For example, left ventricular failure allows pulmonary edema and pulmonary hypertension to occur, which increase stress on the right ventricle. HOIP:HOIP_0041843 Virus proliferation is a subtype of increasing number of objects: A process becomes larger in the number of virus present in the host body. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. viral proliferation in COVID-19 HOIP_0041843 HOIP:HOIP_0041845 Negative regulation of bradykinin inactivation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of bradykinin inactivation. Negative regulation of bradykinin inactivation HOIP_0041845 HOIP:HOIP_0041846 Bradykinin inactivation is a subtype of molecular inactivation: A process that changes the activity of the bradykinin to be lower. bradykinin inactivation HOIP_0041846 HOIP:HOIP_0041847 Negative regulation of bradykinin inactivation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of bradykinin inactivation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33077917 Negative regulation of bradykinin inactivation in COVID-19 HOIP_0041847 PMID:33077917 Additionally, the reduction in levels of ACE2 limits the degradation of des-Arg9 bradykinin (DABK) into inactive peptides, ultimately leading to increased pro-thrombotic signalling via the activation of bradykinin receptors (BKRs). HOIP:HOIP_0041848 Negative regulation of bradykinin inactivation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of bradykinin inactivation. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:33077917 negative regulation of bradykinin inactivation (very high) in severe COVID-19 HOIP_0041848 PMID:33077917 Additionally, the reduction in levels of ACE2 limits the degradation of des-Arg9 bradykinin (DABK) into inactive peptides, ultimately leading to increased pro-thrombotic signalling via the activation of bradykinin receptors (BKRs). HOIP:HOIP_0041849 Negative regulation of bradykinin inactivation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of bradykinin inactivation. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 negative regulation of bradykinin inactivation (very high) in COVID-19 associated with ARDS HOIP_0041849 PMID:33077917 The reduction in pulmonary ACE2 impairs the inactivation of des-Arg9 bradykinin (DABK), leaving it free to bind its cognate receptors (Fig. 3a). Additionally, the reduction in levels of ACE2 limits the degradation of des-Arg9 bradykinin (DABK) into inactive peptides, ultimately leading to increased pro-thrombotic signalling via the activation of bradykinin receptors (BKRs). HOIP:HOIP_0041850 The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in patient with diabetes. PMID:32694793 viral release from host cell (very high) [COVID-19 in patient with diabetes] ウイルス排出 Previous HoIP ID: HOIP_0041850 SARS-CoV-2 shedding (very high) in COVID-19 infected diabeteis patients HOIP_0041850 PMID:32694793 In people with T2D, ACE2 expression is elevated in multiple target tissues of SARS-CoV-2, and this elevation has been proposed to be an adaptive mechanism that protects the body against diabetes-associated physiological dysfunction. This increased expression may enhance SARS-CoV-2’s entry and subsequent replication, as well as its spread within the body in individuals with T2D. HOIP:HOIP_0041851 Increasing demand for response to oxidative stress in myocardium is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher in myocardium. This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32629875 increasing demand for response to oxidative stress in myocardium in COVID-19 in cardiovascular system HOIP_0041851 PMID:32629875 Also, genetic and pharmacological studies in mice have shown that ACE2 regulates cardiac structure and function; decreased ACE2 in SARS-CoV-2-infected cardiomyocytes could disrupt these activities, particularly impairing cardiac remodeling and increasing oxidative stress in cardiomyocytes. HOIP:HOIP_0041852 Endothelium damage in kidney is a subtype of endothelium damage: A process that injuries the structure of the endothelium in kidney as the direct or indirect result of an external force. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in renal system. PMID:32416769 PMID:33077917 endothelium damage in kidney in COVID-19 in renal system HOIP_0041852 PMID:32416769 Autopsy data indicate that the endothelium is affected in the lung and in the kidney, where it is probably responsible for proteinuria (figure 1). Furthermore, virus particles were reported to be present in renal endothelial cells, indicating viraemia as a possible cause of endothelial damage in the kidney and a probable contributor to AKI. PMID:33077917 Infection of endothelial cells alters glomerular capillary haemostasis and induces the formation of fibrin thrombi. HOIP:HOIP_0041855 The totality of all processes through which COVID-19 infection in renal (-urinary) system is realized. COVID-19 course in renal system HOIP_0041855 HOIP:HOIP_0041856 NCBI-Human-GeneID:3559 NCBI-Mouse-GeneID:16184 NCBI-Rat-GeneID:25704 IL2RA (mol) HOIP_0041856 NCBI-Human-GeneID:3559 http://www.ncbi.nlm.nih.gov/gene/3559 NCBI-Mouse-GeneID:16184 http://www.ncbi.nlm.nih.gov/gene/16184 NCBI-Rat-GeneID:25704 http://www.ncbi.nlm.nih.gov/gene/25704 HOIP:HOIP_0041857 CCL3 signaling is a process that a signal is transmitted by CCL3. CCL3 signaling HOIP_0041857 HOIP:HOIP_0041858 NCBI-Human-GeneID:3561 NCBI-Mouse-GeneID:16186 NCBI-Rat-GeneID:140924 IL2RG (mol) HOIP_0041858 NCBI-Human-GeneID:3561 http://www.ncbi.nlm.nih.gov/gene/3561 NCBI-Mouse-GeneID:16186 http://www.ncbi.nlm.nih.gov/gene/16186 NCBI-Rat-GeneID:140924 http://www.ncbi.nlm.nih.gov/gene/140924 HOIP:HOIP_0041859 CCL3 signaling is a process that a signal is transmitted by CCL3. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:33123165 CCL3 signaling in COVID-19 HOIP_0041859 PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0041860 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. inflammatory response in coronavirus infection HOIP_0041860 HOIP:HOIP_0041861 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 PMID:32651579 PMID:32697943 inflammatory response in COVID-19 HOIP_0041861 PMID:32629875 Since soluble IL-6R is abnormally elevated in the plasma of COVID-19 patients, presumably secondary to cleavage from the cells surface by TACE/ADAM17 upon SARS-CoV-2 infection and the inflammatory response associated with COVID-19, IL-6 can activate most cells, including endothelial cells, which do not express endogenous IL-6R but can be activated by the complex of soluble IL-6R and IL-6. PMID:32651579 Elevation of serum inflammatory markers such as C-reactive protein, ferritin, erythrocyte sedimentation rate, D-dimer, fibrinogen, and lactate dehydrogenase is predictive of subsequent critical illness and mortality in patients with COVID-19. PMID:32697943 Our findings demonstrated that HIF-1a is necessary for the induction of glycolysis and the consequent proinflammatory state of CoV-2-infected monocytes. Exacerbated proinflammatory stimuli can negatively affect T cell response (de Marcken et al., 2019). HOIP:HOIP_0041862 CCL3 signaling is a process that a signal is transmitted by CCL3. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32629875 PMID:33123165 CCL3 signaling in severe COVID-19 HOIP_0041862 PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. PMID:33123165 Those COVID-19 patients requiring ICU admission demonstrated greater plasma levels of IL-2, IL-7, IL-10, granulocyte colony-stimulating factor (GCSF), interferon- inducible protein 10 (IP-10), monocyte chemoattractant protein- 1 (MCP-1), macrophage inflammatory protein-1alpha (MIP-1alpha) and TNF-alpha than the non-ICU COVID-19 patients, all supporting enhanced innate immunity in the sicker patients. HOIP:HOIP_0041863 CXCL10 signaling is a process that a signal is transmitted by CXCL10. CXCL10 signaling HOIP_0041863 HOIP:HOIP_0041864 CXCL10 signaling is a process that a signal is transmitted by CXCL10. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. CXCL10 signaling in COVID-19 HOIP_0041864 HOIP:HOIP_0041865 CXCL10 signaling is a process that a signal is transmitted by CXCL10. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:34046036 CXCL10 signaling in severe COVID-19 HOIP_0041865 PMID:34046036 CXCL10/IP10 is also secreted by many cells, including monocytes, endothelial cells, and fibroblasts, in response to IFN-gamma. Several clinical investigations involving autopsies have also provided evidence that thrombosis is an important consequence of hCoV diseases. These findings indicate that the thrombosis-related indicators (CXCL10/IP10, MCP-1) could be directly involved in different stages of hCoV infection and could be used as potential biomarkers to predict the risk of death in hCoV patients. HOIP:HOIP_0041867 Expanding inflammation in lung is a subtype of expanding inflammation : A process that changes the magnitude of the inflammation the object to be larger. expanding inflammation in lung HOIP_0041867 HOIP:HOIP_0041868 A process that changes the magnitude of the inflammation to be larger. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). Wikipedia:Inflammation expanding inflammation in lung in COVID-19 associated with ARDS HOIP_0041868 Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. The inflammatory response must be actively terminated when no longer needed to prevent unnecessary "bystander" damage to tissues. Failure to do so results in chronic inflammation, and cellular destruction. HOIP:HOIP_0041869 Inflammatory response in lung is a subtype of Inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:32422178 PMID:33077917 PMID:33123165 Wikipedia:Inflammation inflammatory response in lung (very high) in COVID-19 associated with ARDS HOIP_0041869 PMID:32422178 Multiple aberrant host pathways interconnect to result in pulmonary fibrosis in a subset of individuals who develop ARDS. Important mediators include the dysregulated release of matrix metalloproteinases during the inflammatory phase of ARDS, which causes epithelial and endothelial injury and unchecked fibroproliferation. PMID:33077917 As mentioned above, the nucleocapsid protein of SARS-CoV-2 can interact indirectly with MASP-2 and initiate the lectin pathway of complement, resulting in aberrant complement activation and aggravated inflammatory lung injury. PMID:33123165 Furthermore, uncontrolled local inflammation, or what has been described as “cytokine storm,” leading to tissue damage with inflammatory cell infiltration and the acute respiratory distress syndrome (ARDS) is thought to characterize late stage, severe manifestations of COVID-19. Wikipedia:Inflammation As a consequence, apoptotic neutrophils undergo phagocytosis by macrophages, leading to neutrophil clearance and release of anti-inflammatory and reparative cytokines such as transforming growth factor-β1. The anti-inflammatory program ends with the departure of macrophages through the lymphatics. The inflammatory response must be actively terminated when no longer needed to prevent unnecessary "bystander" damage to tissues.[10] Failure to do so results in chronic inflammation, and cellular destruction. HOIP:HOIP_0041872 Type III interferon signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by Type III interferon. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Type III interferon signaling in COVID-19 HOIP_0041872 HOIP:HOIP_0041873 Type III interferon signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by Type III interferon. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Type III interferon signaling in severe COVID-19 HOIP_0041873 HOIP:HOIP_0041874 Cytokine signaling is a process that a signal is transmitted by the cytokine. cytokine signaling HOIP_0041874 HOIP:HOIP_0041877 Chemokine signaling is a process that a signal is transmitted by the chemokine. chemokine signaling HOIP_0041877 HOIP:HOIP_0041878 Chemokine signaling is a process that a signal is transmitted by the chemokine. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 PMID:33077917 PMID:33123165 chemokine signaling in COVID-19 HOIP_0041878 PMID:32697943 These monocytes are likely recruited by chemokines produced by infected epithelial cells, while interferons (IFNs) induce angiotensin-converting enzyme 2 (ACE2), one of the proteins used by the virus to enter the cell (Hoffmann et al., 2020; Wrapp et al., 2020). PMID:33077917 Pro-inflammatory cells, cytokines and chemokines amplify the vicious cycle of vessel coagulation and thrombosis, by acting to simultaneously activate the coagulation system and dampen anticoagulant mechanisms. PMID:33123165 Upregulated chemoattractant chemokines further recruit inflammatory cells including neutrophils, macrophages, natural killer (NK) cells and T cells resulting in further immunopathology (Figure 2). HOIP:HOIP_0041880 Increasing chemokine level is a subtype of increasing quantity: A process that changes the amount of chemokine level to be higher. increasing chemokine level HOIP_0041880 HOIP:HOIP_0041881 Class of pro-inflammatory cytokines that have the ability to attract and activate leukocytes. They can be divided into at least three structural branches: C; (CHEMOKINES, C); CC; (CHEMOKINES, CC); and CXC; (CHEMOKINES, CXC); according to variations in a shared cysteine motif. (MeSH:Chemokines) chemokine HOIP_0041881 HOIP:HOIP_0041883 Increasing CXCL10 level is a subtype of increasing quantity: A process that changes the amount of CXCL10 level to be higher. increasing CXCL10 level HOIP_0041883 HOIP:HOIP_0041884 Increasing cytokine level is a subtype of increasing quantity: A process that changes the amount of cytokine level to be higher. increasing cytokine level HOIP_0041884 HOIP:HOIP_0041887 Increasing interferon-alpha level is a subtype of increasing quantity: A process that changes the amount of interferon-alpha level to be higher. increasing interferon-alpha level HOIP_0041887 HOIP:HOIP_0041890 Increasing interferon-beta level is a subtype of increasing quantity: A process that changes the amount of interferon-beta level to be higher. increasing interferon-beta level HOIP_0041890 HOIP:HOIP_0041891 Increasing interferon-beta level is a subtype of increasing quantity: A process that changes the amount of interferon-beta level to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 increasing interferon-beta level in COVID-19 HOIP_0041891 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). Inhibition of HIF-1a prevented the CoV-2-mediated increase in the expression of ACE2, IL-1b, TNF-a, IL-6, and IFN a, b, and l (Figures 3G, 3H, and S4E). HOIP:HOIP_0041892 The appearance of chemokine (C-C motif) ligand 10 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32629875 IP-10 production chemokine (C-C motif) ligand 10 production in COVID-19 HOIP_0041892 PMID:32629875 Expanding on these observations, another study found that severely affected COVID-19 patients (n = 13) admitted to the intensive care unit (ICU) not only had higher plasma levels of IL-10 and TNFα compared to less severely ill patients not admitted to the ICU (n = 28) but also increased levels of IP-10, IL-2, IL-7, G-CSF, MCP1 and MIP1A. These and other studies have concluded that the core pro-inflammatory cytokines TNFα, IL-1β, IL-6, G-CSF, GM-CSF as well as the chemokines MCP-1, IP-10 and MIP1α are elevated in patients with COVID-19, with higher levels in those patients who are critically ill compared with those with less serious illness. HOIP:HOIP_0041893 Increasing CCL2 level is a subtype of increasing quantity: A process that changes the amount of CCL2 level to be higher. increasing CCL2 level HOIP_0041893 HOIP:HOIP_0041896 Increasing CCL3 level is a subtype of increasing quantity: A process that changes the amount of CCL3 level to be higher. increasing CCL3 level HOIP_0041896 HOIP:HOIP_0041899 Increasing CXCL8 level is a subtype of increasing quantity: A process that changes the amount of CXCL8 level to be higher. increasing CXCL8 level HOIP_0041899 HOIP:HOIP_0041902 A series of molecular signals initiated by the binding of the chemokine CXCL8 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. CXCL8-mediated signaling pathway chemokine (C-X-C motif) ligand 8 signaling pathway HOIP_0041902 HOIP:HOIP_0041903 CXCL8 signaling is a process that a signal is transmitted by CXCL8. CXCL8 signaling HOIP_0041903 HOIP:HOIP_0041904 CXCL8 signaling is a process that a signal is transmitted by CXCL8. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. CXCL8 signaling in COVID-19 HOIP_0041904 HOIP:HOIP_0041906 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This process can constitute the course of coronavirus infectious disease. Inflammatory cytokine production in coronavirus infection HOIP_0041906 HOIP:HOIP_0041907 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. PMID:32697943 PMID:32887954 Inflammatory cytokine production in COVID-19 HOIP_0041907 PMID:32697943 Monocytes infected with CoV-2 expressed higher levels of IFN a, b, and l, and higher levels of the proinflammatory cytokines TNF-a, IL-1b, and IL-6, which are associated with the COVID-19 ‘‘cytokine storm’’ (Figure 1C). PMID:32887954 Cytokine profiles from patients infected with SARS-CoV-2 resemble those in macrophage activation syndrome and are characterized by high levels of inflammatory cytokines and chemokines. HOIP:HOIP_0041909 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. Inflammatory cytokine production (very low) in COVID-19 drug treatment HOIP_0041909 HOIP:HOIP_0041910 The appearance of an inflammatory cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 assiciated with acute respiratory distress syndrome (ARDS). PMID:33077917 PMID:33214651 Inflammatory cytokine production (very high)in COVID-19 associated with ARDS HOIP_0041910 PMID:33077917 The increase in pro-inflammatory cytokines within the lung leads to the recruitment of leukocytes, further propagating the local inflammatory response that underlies the pathology of atypical interstitial bilateral pneumonia observed in patients with COVID-19. PMID:33214651 Increased production of inflammatory chemokines and cytokines (many from platelets) and an excessive or uncontrolled innate immune response are typical characteristics of ARDS, including in the ARDS seen in COVID-19. HOIP:HOIP_0041911 Increasing IL-1B level is a subtype of increasing quantity: A process that changes the amount of IL-1B level to be higher. increasing IL-1B level HOIP_0041911 HOIP:HOIP_0041912 Increasing inflammatory cytokine level is a subtype of increasing quantity: A process that changes the amount of inflammatory cytokine level to be higher. increasing inflammatory cytokine level HOIP_0041912 HOIP:HOIP_0041916 A series of molecular signals initiated by the binding of a inflammatory c ytokine to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. inflammatory cytokine-mediated signaling pathway HOIP_0041916 HOIP:HOIP_0041917 Inflammatory cytokine signaling is a process that a signal is transmitted by the inflammatory cytokine. inflammatory cytokine signaling HOIP_0041917 HOIP:HOIP_0041918 Inflammatory cytokine signaling is a process that a signal is transmitted by the inflammatory cytokine. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. inflammatory cytokine signaling in COVID-19 HOIP_0041918 HOIP:HOIP_0041930 Increasing interferon-gamma level is a subtype of increasing quantity: A process that changes the amount of interferon-gamma level to be higher. increasing interferon-gamma level HOIP_0041930 HOIP:HOIP_0041934 Interaction between host pattern recognition receptor and any PAMPs (pathogen-associated molecular patterns). Wikipedia:Inflammation binding of pattern recognition receptor to PAMPs HOIP_0041934 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0041935 Interaction between host pattern recognition receptor and any PAMPs (pathogen-associated molecular patterns). This entity is a specific course-dependent process. This process can constitute the course of COVID-19. Wikipedia:Inflammation binding of pattern recognition receptor to PAMPs in COVID-19 HOIP_0041935 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0041937 Interaction between host pattern recognition receptor and any DAMPs (damage-associated molecular patterns). Wikipedia:Inflammation binding of pattern recognition receptor to DAMPs HOIP_0041937 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0041941 type I interferon production The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:25301932 type I interferon production (severe)in severe COVID-19 HOIP_0041941 HOIP:HOIP_0041943 Interaction between host pattern recognition receptor and any PAMPs (pathogen-associated molecular patterns). This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. Wikipedia:Inflammation binding of pattern recognition receptor to PAMPs in coronavirus infection HOIP_0041943 Wikipedia:Inflammation The process of acute inflammation is initiated by resident immune cells already present in the involved tissue, mainly resident macrophages, dendritic cells, histiocytes, Kupffer cells and mast cells. These cells possess surface receptors known as pattern recognition receptors (PRRs), which recognize (i.e., bind) two subclasses of molecules: pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). PAMPs are compounds that are associated with various pathogens, but which are distinguishable from host molecules. DAMPs are compounds that are associated with host-related injury and cell damage. HOIP:HOIP_0041946 Lymph node atrophy is a subtype of decreasing volume: A process that changes the volume of the lymph node to be relatively low. lymph node atrophy HOIP_0041946 HOIP:HOIP_0041947 Lymph node atrophy is a subtype of decreasing volume: A process that changes the volume of the lymph node to be relatively low. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32843733 lymph node atrophy in severe COVID-19 HOIP_0041947 PMID:32843733 The idea that the cytokine storm is mediated by leukocytes other than T or B cells is supported by observations of lymphocytopenia and sometimes atrophy of the lymphatic tissues, such as lymph nodes and spleen, in patients with severe COVID-19. HOIP:HOIP_0041948 Spleen atrophy is a subtype of decreasing volume: A process that changes the volume of the spleen to be relatively low. spleen atrophy HOIP_0041948 HOIP:HOIP_0041949 Spleen atrophy is a subtype of decreasing volume: A process that changes the volume of the spleen to be relatively low. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. PMID:32843733 spleen atrophy in severe COVID-19 HOIP_0041949 PMID:32843733 The idea that the cytokine storm is mediated by leukocytes other than T or B cells is supported by observations of lymphocytopenia and sometimes atrophy of the lymphatic tissues, such as lymph nodes and spleen, in patients with severe COVID-19. HOIP:HOIP_0042000 Hypofunction of IgG antibody production is a subtype of hypofunction of protein synthesis: A process that performs a decreased or insufficient IgG antibody production . hypofunction of IgG antibody production HOIP_0042000 HOIP:HOIP_0042001 Hypofunction of is a subtype of hypofunctioning: A process that performs a decreased or insufficient moving A to the outside of B. hypofunction of moving A to the outside of B HOIP_0042001 HOIP:HOIP_0042002 Hypofunction of cellular response to type I interferon is a subtype of hypofunctioning: A process that performs a decreased or insufficient cellular response to type I interferon. hypofunction of cellular response to type I interferon HOIP_0042002 HOIP:HOIP_0042003 Hypofunction of virion attachment to host cell is a subtype of hypofunctioning: A process that performs a decreased or insufficient virion attachment to host cell. hypofunction of virion attachment to host cell HOIP_0042003 HOIP:HOIP_0042004 Hypofunction of viral entry into host cell is a subtype of v: A process that performs a decreased or insufficient viral entry into host cell . hypofunction of viral entry into host cell HOIP_0042004 HOIP:HOIP_0042005 Hypofunction of leaking fluid to pulmonary interstitium is a subtype of hypofunctioning: A process that performs a decreased or insufficient leaking fluid to pulmonary interstitium. hypofunction of leaking fluid to pulmonary interstitium HOIP_0042005 HOIP:HOIP_0042006 Hypofunction of viral replication complex formation and maintenance is a subtype of hypofunction of assembling: A process that performs a decreased or insufficient viral replication complex formation and maintenance. hypofunction of viral replication complex formation and maintenance HOIP_0042006 HOIP:HOIP_0042007 Hypofunction of type I interferon production is a subtype of hypofunction of cytokine production: A process that performs a decreased or insufficient type I interferon production. hypofunction of type I interferon production HOIP_0042007 HOIP:HOIP_0042008 Hypofunction of host cell surface binding is a subtype of hypofunction of assembling: A process that performs a decreased or insufficient host cell surface binding. hypofunction of host cell surface binding HOIP_0042008 HOIP:HOIP_0042009 Hypofunction of positive regulation of MHC class II biosynthetic process is a subtype of hypofunction of positive regulation: A process that performs a decreased or insufficient positive regulation of MHC class II biosynthetic process . hypofunction of positive regulation of MHC class II biosynthetic process HOIP_0042009 HOIP:HOIP_0042010 Hypofunction of controlling is a subtype of hypofunctioning: A process that performs a decreased or insufficient controlling . hypofunction of controlling HOIP_0042010 HOIP:HOIP_0042011 Removing infected cell is a subtype of removing damaged object: A process that takes a infected cell from an organism or tissue.　This process can constitute the course of severe COVID-19. removing infected cell in severe COVID-19 HOIP_0042011 HOIP:HOIP_0042012 Hypofunction of production of inflammatory cytokine is a subtype of hypofunction of cytokine biosynthesis: A process that performs a decreased or insufficient production of inflammatory cytokine. hypofunction of cytokine production involved in inflammatory response HOIP_0042012 HOIP:HOIP_0042013 Hypofunction of immune response is a subtype of hypofunctioning: A process that performs a decreased or insufficient immune response. hypofunction of immune response HOIP_0042013 HOIP:HOIP_0042014 Hypofunction of antiviral innate immune response is a subtype of hypofunction of immune response: A process that performs a decreased or insufficientantiviral innate immune response. hypofunction of antiviral innate immune response HOIP_0042014 HOIP:HOIP_0042015 Hypofunction of viral gene expression is a subtype of hypofunction of transcription: A process that performs a decreased or insufficient viral gene expression. hypofunction of viral gene expression HOIP_0042015 HOIP:HOIP_0042016 Hypofunction of NfkB signaling is a subtype of hypofunction of signaling: A process that performs a decreased or insufficient NfkB signaling . hypofunction of NfkB signaling HOIP_0042016 HOIP:HOIP_0042017 Hypofunction of negative regulation process is is a subtype of hypofunctioning: A process that performs a decreased or insufficient negative regulation of process. hypofunction of negative regulation process HOIP_0042017 HOIP:HOIP_0042018 Hypofunction of positive regulation process is is a subtype of hypofunctioning: A process that performs a decreased or insufficient positive regulation of process. hypofunction of positive regulation process HOIP_0042018 HOIP:HOIP_0042019 Hypofunction of positive regulation of interferon-alpha production is a subtype of hypofunction of positive regulation: A process that performs a decreased or insufficient positive regulation ofpositive regulation of interferon-alpha production. hypofunction of positive regulation of interferon-alpha production HOIP_0042019 HOIP:HOIP_0042020 Hypofunction of translation for viral replication complex is a subtype of viral translation: A process that performs a decreased or insufficient translation for viral replication complex. hypofunction of translation for viral replication complex HOIP_0042020 HOIP:HOIP_0042022 A process that performs a decreased or insufficient of the cleavage of a peptide bond or bonds within a viral protein. hypofunction of viral polyprotein processing HOIP_0042022 HOIP:HOIP_0042023 The directed movement of cholesterol, cholest-5-en-3-beta-ol, or cholesterol-containing compounds, by membrane-bounded vesicles. vesicle-mediated cholesterol transport HOIP_0042023 HOIP:HOIP_0042024 Hypofunction vesicle-mediated cholesterol transport is a subtype of hypofunction of cholesterol transport: A process that performs a decreased or insufficient vesicle-mediated cholesterol transport. hypofunction vesicle-mediated cholesterol transport HOIP_0042024 HOIP:HOIP_0042025 Negative regulation of establishment of virus infection is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of establishment of virus infection. negative regulation of establishment of virus infection HOIP_0042025 HOIP:HOIP_0042026 Negative regulation of establishment of virus infection is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of establishment of virus infection. This process can constitute the course of COVID-19 vaccination. negative regulation of establishment of virus infection in COVID-19 vaccination HOIP_0042026 HOIP:HOIP_0042027 For ontology reasoning. possible cause of inflammatory response HOIP_0042027 HOIP:HOIP_0042028 For ontology reasoning. possible cause of IL-6 signaling and inflammatory response HOIP_0042028 HOIP:HOIP_0042029 For ontology reasoning. possible cause of "negative regulation of insulin receptor signaling pathway" HOIP_0042029 HOIP:HOIP_0042030 An establishment of localization in host process in which virus with pathogen role establishes itself in a host. The degree is very low. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 vaccination. PMID:32843733 establishment of virus infection (very low) in COVID-19 vaccination HOIP_0042030 PMID:32843733 If the protective immune response is impaired, the virus is allowed to replicate and can cause widespread tissue damage. The lungs seem to be the main target, although other organs with high ACE2 expression, such as the intestine, heart, brain and kidney, might also be vulnerable. HOIP:HOIP_0042031 A process by which viral mRNA is translated into viral protein, using the host cellular machinery. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 drug treatment. The functioning level is very low. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis viral translation (very low) in COVID-19 drug treatment HOIP_0042031 viral protein biosynthetic process ISBN:0781702534 HOIP:HOIP_0042032 Increasing creatinine concentration is a subtype of increasing concentration: A process that changes the creatine kinase concentration to be higher.This process can constitute the course of severe COVID-19. PMID:33923710 increasing creatine kinase concentration in severe COVID-19 HOIP_0042032 HOIP:HOIP_0042033 Any processes of signals generated as a consequence of a pattern recognition receptor (PRR) binding to damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. ダメージ関連分子パターン誘導パターン認識受容体シグナル伝達 DAMP-triggered pattern recognition receptor signaling in severe COVID-19 HOIP_0042033 HOIP:HOIP_0042034 Negative regulation of inflammatory response is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of coronavirus infectious disease. convergence of inflammatory response in coronavirus infection HOIP_0042034 HOIP:HOIP_0042035 Anatomical system damage is a subtype of damaging: A process that injures the structure of the anatomical syatem as the direct or indirect result of an external force. anatomical system damage HOIP_0042035 HOIP:HOIP_0042036 Vasculature damage is a subtype of damaging: A process that injures the structure of the brain vasculature as the direct or indirect result of an external force. vasculature damage HOIP_0042036 HOIP:HOIP_0042038 The un-regulated release of DAMP (damage-associated molecular pattern) molecules from a ruptured cell. This entity is a specific course-dependent process. This process can constitute the course of severe COVID-19. Wikipedia:Pyroptosis release of DAMP molecules by cell rupture (very high) in severe COVID-19 HOIP_0042038 Wikipedia:Pyroptosis Formation of pores causes cell membrane rupture and release of cytokines, as well as various damage-associated molecular pattern (DAMP) molecules such as HMGB-1, ATP and DNA, out of the cell. These molecules recruit more immune cells and further perpetuate the inflammatory cascade in the tissue. HOIP:HOIP_0042039 The movement of a leukocyte in response to an external stimulus. This entity is a specific course-dependent process. This process can constitute the course of COVID-19. immune cell chemotaxis leucocyte chemotaxis inflammatory cell chemotaxis in COVID-19 HOIP_0042039 HOIP:HOIP_0042040 Hypofunction of glicolytic process is a subtype of hyperfunctioning: A process that performs a decreased or insufficient glycolytic process. dysfunction of glycolytic process HOIP_0042040 HOIP:HOIP_0042041 The appearance of adipokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32687793 adipocytokine production adipokine production in COVID-19 associated with myocarditis HOIP_0042041 PMID:32687793 Myocarditis and cardiomyocyte dysfunction could be worsened by local biological effects of epicardial adipose tissue, a source of adipokines and pro-inflammatory mediators, and the volume of epicardial adipose tissue is directly associated with BMI. HOIP:HOIP_0042042 Negative regulation of cardiomyocyte function is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the cardiomyocyte function. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 associated with myocarditis. PMID:32687793 negative regulation of cellular function in COVID-19 associated with myocarditis HOIP_0042042 PMID:32687793 Myocarditis and cardiomyocyte dysfunction could be worsened by local biological effects of epicardial adipose tissue, a source of adipokines and pro-inflammatory mediators, and the volume of epicardial adipose tissue is directly associated with BMI. HOIP:HOIP_0042043 Increasing volume of myocardium is a subtype of increasing volume: A process that changes the volume of the myocardium to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. PMID:32694793 increasing volume of myocardium in COVID-19 in cardiovascular system HOIP_0042043 PMID:32694793 The effects of obesity and diabetes on the blood vessels can lead to hypertension, which in turn affects haemodynamics and alters the heart structure (Fig. 2). These changes can make the heart more susceptible to damage due to the host inflammatory response, hypoxia caused by ARDS, infection of the heart by the virus or other cardiac consequences in response to extrapulmonary multiorgan damage, thus potentially explain- ing why some people with COVID-19 exhibit cardiac damage and heart-attack-like signs of disease. HOIP:HOIP_0042044 Increasing blood pressure is a subtype of increasing pressure: A process that changes the blood pressure to be higher. This entity is a specific course-dependent process. This process can constitute the course of COVID-19 in the cardiovascular system. increasing vascular pressure increasing blood pressure in COVID-19 in cardiovascular system HOIP_0042044 HOIP:HOIP_0042046 Any process that decreases the frequency, rate, or extent of neutrophil activation involved in immune response. negative regulation of neutrophil activation involved in immune response HOIP_0042046 HOIP:HOIP_0042047 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of coronavirus infectious disease. inflammatory cell infiltration in coronavirus infection HOIP_0042047 HOIP:HOIP_0042051 A role played by the entity which negatively the glycolytic process. glycolysis inhibitor role HOIP_0042051 HOIP:HOIP_0042053 Any heteroorganic entity containing at least one carbon-nitrogen bond. organonitrogen compound HOIP_0042053 HOIP:HOIP_0042054 An inhibitor of virus protease, an enzyme required for production of proteins needed for viral assembly. viral protease inhibitor HOIP_0042054 HOIP:HOIP_0042055 A protein that is a translation product of the human IL1RN gene or a 1:1 ortholog thereof. ICIL-1RA IL-1RN IL-1ra anakinra interleukin-1 receptor antagonist protein HOIP_0042055 HOIP:HOIP_0042056 The directed movement of lipid nano particle (LNP) to lymph node via lymphatics. LNPs are carriers to protect the mRNA of vaccines. PMID: 33674759 transport of mRNA vaccine to lymph nodes by LNP HOIP_0042056 PMID: 33674759 The LNP carrier further protects the mRNA, can target delivery to lymphatics and promote protein translation in lymph nodes (LNs)7. Once in the LN, the LNP is engulfed by dendritic cells (DCs), which subsequently produce and present the antigen to T cells for activation of the adaptive immune response. HOIP:HOIP_0042057 The directed movement of lipid nano particle (LNP) to lymph node via lymphatics. LNPs are carriers to protect the mRNA of vaccines. PMID: 33674759 transport of mRNA vaccine to lymph nodes by LNP in COVID-19 vaccination HOIP_0042057 PMID: 33674759 The LNP carrier further protects the mRNA, can target delivery to lymphatics and promote protein translation in lymph nodes (LNs)7. Once in the LN, the LNP is engulfed by dendritic cells (DCs), which subsequently produce and present the antigen to T cells for activation of the adaptive immune response. HOIP:HOIP_0050001 The first few specialized divisions of an activated animal egg; Stage consisting of division of cells in the early embryo. The zygotes of many species undergo rapid cell cycles with no significant growth, producing a cluster of cells the same size as the original zygote. The different cells derived from cleavage are called blastomeres and form a compact mass called the morula. Cleavage ends with the formation of the blastula. cleavage stage HOIP_0050001 HOIP:HOIP_0050002 Generating the anterior-posterior embryonic axis in the one-cell embryo dependent process in C. elegans is a subtype of course dependent process: A process that can constitute the course of generating the anterior-posterior embryonic axis in the one-cell embryo in C.elegans. doi/10.1895/wormbook.1.30.2 generating the anterior-posterior embryonic axis in the one-cell embryo dependent process in C.elegans HOIP_0050002 doi/10.1895/wormbook.1.30.2 Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook) http://www.wormbook.org. HOIP:HOIP_0050003 The division of the C.elegans zygote into two daughter cells that will adopt developmentally distinct potentials. doi/10.1895/wormbook.1.30.2 asymmetric cell division in the C.elegans embryo HOIP_0050003 doi/10.1895/wormbook.1.30.2 During development, cells acquire distinct fates, and one prominent mechanism by which this is achieved is asymmetric division. In the early embryo of C. elegans, five asymmetric divisions produce six founder cells: AB, MS, E, C, D, and P4 (Figure 1). The first asymmetric division cleaves the one-cell zygote into a larger anterior blastomere, AB, and a smaller posterior blastomere, P1. Thereafter, P1 undergoes an asymmetric division that gives rise to EMS and P2. Subsequent asymmetric divisions of EMS into MS and E, then of P2 into C and P3, and finally of P3 into D and P4, complete the generation of the six founder cells whose descendants each produce specific cell types (Sulston et al., 1983) (Figure 1). http://www.wormbook.org. HOIP:HOIP_0050023 The totality of all processes through which early embryonic development in C.elegans is realized. ISBN13:9784895928052 doi/10.1895/wormbook.1.30.2 C. elegans embryonic development course HOIP_0050023 ISBN13:9784895928052 Gilbert, Scott F. , 阿形, 清和, 高橋, 淑子, ギルバート発生生物学,5章初期発生，C. elegansにおける卵割と軸形成, メディカル・サイエンス・インターナショナル, 2015 doi/10.1895/wormbook.1.30.2 Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook. HOIP:HOIP_0050024 The first division of the C.elegans zygote into two daughter cells that will adopt developmentally distinct potentials. doi/10.1895/wormbook.1.30.2 first asymmetric cell division in the C.elegans embryo HOIP_0050024 doi/10.1895/wormbook.1.30.2 During development, cells acquire distinct fates, and one prominent mechanism by which this is achieved is asymmetric division. In the early embryo of C. elegans, five asymmetric divisions produce six founder cells: AB, MS, E, C, D, and P4 (Figure 1). The first asymmetric division cleaves the one-cell zygote into a larger anterior blastomere, AB, and a smaller posterior blastomere, P1. Thereafter, P1 undergoes an asymmetric division that gives rise to EMS and P2. Subsequent asymmetric divisions of EMS into MS and E, then of P2 into C and P3, and finally of P3 into D and P4, complete the generation of the six founder cells whose descendants each produce specific cell types (Sulston et al., 1983) (Figure 1). http://www.wormbook.org. HOIP:HOIP_0050025 first zygote asymmetric cell division in C.elegans The second division of the C.elegans zygote into two daughter cells that will adopt developmentally distinct potentials. doi/10.1895/wormbook.1.30.2 second asymmetric cell division in the C.elegans embryo HOIP_0050025 doi/10.1895/wormbook.1.30.2 During development, cells acquire distinct fates, and one prominent mechanism by which this is achieved is asymmetric division. In the early embryo of C. elegans, five asymmetric divisions produce six founder cells: AB, MS, E, C, D, and P4 (Figure 1). The first asymmetric division cleaves the one-cell zygote into a larger anterior blastomere, AB, and a smaller posterior blastomere, P1. Thereafter, P1 undergoes an asymmetric division that gives rise to EMS and P2. Subsequent asymmetric divisions of EMS into MS and E, then of P2 into C and P3, and finally of P3 into D and P4, complete the generation of the six founder cells whose descendants each produce specific cell types (Sulston et al., 1983) (Figure 1). http://www.wormbook.org. HOIP:HOIP_0050026 first zygote asymmetric cell division in C.elegans The third division of the C.elegans zygote into two daughter cells that will adopt developmentally distinct potentials. doi/10.1895/wormbook.1.30.2 third asymmetric cell division in the C.elegans embryo HOIP_0050026 doi/10.1895/wormbook.1.30.2 During development, cells acquire distinct fates, and one prominent mechanism by which this is achieved is asymmetric division. In the early embryo of C. elegans, five asymmetric divisions produce six founder cells: AB, MS, E, C, D, and P4 (Figure 1). The first asymmetric division cleaves the one-cell zygote into a larger anterior blastomere, AB, and a smaller posterior blastomere, P1. Thereafter, P1 undergoes an asymmetric division that gives rise to EMS and P2. Subsequent asymmetric divisions of EMS into MS and E, then of P2 into C and P3, and finally of P3 into D and P4, complete the generation of the six founder cells whose descendants each produce specific cell types (Sulston et al., 1983) (Figure 1). http://www.wormbook.org. HOIP:HOIP_0050027 first zygote asymmetric cell division in C.elegans The fourth division of the C.elegans zygote into two daughter cells that will adopt developmentally distinct potentials. doi/10.1895/wormbook.1.30.2 fourth asymmetric cell division in the C.elegans embryo HOIP_0050027 doi/10.1895/wormbook.1.30.2 During development, cells acquire distinct fates, and one prominent mechanism by which this is achieved is asymmetric division. In the early embryo of C. elegans, five asymmetric divisions produce six founder cells: AB, MS, E, C, D, and P4 (Figure 1). The first asymmetric division cleaves the one-cell zygote into a larger anterior blastomere, AB, and a smaller posterior blastomere, P1. Thereafter, P1 undergoes an asymmetric division that gives rise to EMS and P2. Subsequent asymmetric divisions of EMS into MS and E, then of P2 into C and P3, and finally of P3 into D and P4, complete the generation of the six founder cells whose descendants each produce specific cell types (Sulston et al., 1983) (Figure 1). http://www.wormbook.org. HOIP:HOIP_0050028 first zygote asymmetric cell division in C.elegans The fifth division of the C.elegans zygote into two daughter cells that will adopt developmentally distinct potentials. doi/10.1895/wormbook.1.30.2 fifth asymmetric cell division in the C.elegans embryo HOIP_0050028 doi/10.1895/wormbook.1.30.2 During development, cells acquire distinct fates, and one prominent mechanism by which this is achieved is asymmetric division. In the early embryo of C. elegans, five asymmetric divisions produce six founder cells: AB, MS, E, C, D, and P4 (Figure 1). The first asymmetric division cleaves the one-cell zygote into a larger anterior blastomere, AB, and a smaller posterior blastomere, P1. Thereafter, P1 undergoes an asymmetric division that gives rise to EMS and P2. Subsequent asymmetric divisions of EMS into MS and E, then of P2 into C and P3, and finally of P3 into D and P4, complete the generation of the six founder cells whose descendants each produce specific cell types (Sulston et al., 1983) (Figure 1). http://www.wormbook.org. HOIP:HOIP_0050029 Any process resulting in the establishment of cell polarity along the anterior/posterior axis. polarity specification of anterior/posterior axis in the one-cell embryo dependent process in C.elegans HOIP_0050029 HOIP:HOIP_0050030 Changing contractility is a subtype of changing quality: A process that changes the contractility of the object. changing contractility HOIP_0050030 HOIP:HOIP_0050031 Decreasing contractility is a subtype of changing elasticity: A process that decreases the contractility of the object. decreasing contractility HOIP_0050031 HOIP:HOIP_0050032 Decreasing actomyosin contractility is a subtype of changing contractility: A process that decreases the contractility of the actomyosin. decreasing actomyosin contractility HOIP_0050032 HOIP:HOIP_0050037 A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber. stress fiber HOIP_0050037 HOIP:HOIP_0050038 Decreasing local actomyosin contractility in cell cortex in C. elegans is a subtype of changing contractility: A process that decreases the local actomyosin contractility in the C.elegans cell cortex in cell cortex in the one-cell embryo. PMID:32829680 doi/10.1895/wormbook.1.30.2 decreasing local actomyosin contractility in cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050038 PMID:32829680 Upon fertilization and completion of maternal meiosis, the sperm-donated centrosome induces a local inhibition of actomyosin contractility at the posterior pole of the zygote. This leads to flow of the actomyosin network towards the anterior, leaving a smoothened posterior cortex (akin to placing an elastic band under tension and then cutting one end) (figures 1c,d(ii)). doi/10.1895/wormbook.1.30.2 The earliest sign of symmetry-breaking is the local cessation of surface contractions where centrosomes become juxtaposed to the cortex after a random walk that relies on short cortical microtubules (Bienkowska and Cowan, 2012; Cheeks et al., 2004; Cowan and Hyman, 2004b; Munro et al., 2004; Cuenca et al., 2003) HOIP:HOIP_0050040 Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation. localization HOIP_0050040 HOIP:HOIP_0050048 Rotation is a subtype of generating motion: A process that generates a rotational motion. rotation HOIP_0050048 HOIP:HOIP_0050050 The rotation of centrosomes and associated pronuclei in one-cell embryos in Caenorhabditis elegans, occurring as a transition between pronuclear migration and pronuclear fusion. doi/10.1895/wormbook.1.30.2 centrosomal and pronuclear rotation in the one-cell embryo dependent process in C.elegans HOIP_0050050 doi/10.1895/wormbook.1.30.2 After pronuclear meeting, the centrosomes and the joined pronuclei move towards the embryo center, while undergoing a 90° rotation. This process is referred to collectively as centration/rotation and results in the centrosomes becoming aligned along the AP axis in preparation for cell division Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook HOIP:HOIP_0050063 The C. elegans cell cycle process in which the distance is lengthened between poles of the mitotic spindle. Mitotic spindle elongation begins during mitotic prophase and ends during mitotic anaphase B. doi/10.1895/wormbook.1.30.2 mitotic spindle elongation in the one-cell embryo dependent process in C.elegans HOIP_0050063 doi/10.1895/wormbook.1.30.2 Chromosome segregation typically consists of two components: (1) anaphase A, in which the chromosomes move towards the spindle poles and, (2) anaphase B in which the spindle poles separate from each other with the chromosomes in tow. In C. elegans the majority of chromosome movement is due to anaphase B (Oegema et al., 2001), powered by a combination of cortical forces that pull on the centrosomal microtubule asters to separate them, and pushing forces generated by the array of overlapping microtubules, called the central spindle, that forms between the separating chromosomes. If the mitotic spindle is severed during anaphase using a UV micro beam, the two spindle poles separate with increased velocity (Grill et al., 2001). This experiment demonstrates the existence of pulling forces during the first mitotic division and suggests that the central spindle normally acts to limit the rate of pole separation. However, in embryos in which G protein signaling that mediates cortical pulling forces is disrupted, spindles still elongate (Colombo et al., 2003) albeit at a slower rate, indicating that other spindle intrinsic forces contribute to anaphase spindle elongation. HOIP:HOIP_0050075 Mitotic bipolar spindle assembly begins with spindle microtubule nucleation from the separated spindle pole body, includes spindle elongation during prometaphase, and is complete when all kinetochores are stably attached the spindle, and the spindle assembly checkpoint is satisfied. mitotic spindle assembly in C. elegans HOIP_0050075 HOIP:HOIP_0050076 C.elegans embryonic development dependent chemical entity is a subtype of course dependent chemical entity. This entity can participate in the embryonic development in C. elegans. C.elegans embryonic development dependent chemical entity HOIP_0050076 HOIP:HOIP_0050077 C.elegans embryonic development dependent molecule (C.elegans) is a subtype of course dependent chemical entity. This entity can participate in the embryonic development in C. elegans as a gene product. Gene profile:C.elegans C.elegans embryonic development dependent molecule (C.elegans) HOIP_0050077 HOIP:HOIP_0050082 A protein that is a translation product of the par-2 gene in worm. Enables lipid binding activity; microtubule binding activity; and protein kinase binding activity. Is involved in asymmetric cell division; asymmetric protein localization involved in cell fate determination; and establishment of mitotic spindle orientation. Located in P granule; posterior cell cortex; and protein-containing complex. Is expressed in germ line. Enables lipid binding activity; microtubule binding activity; and protein kinase binding activity. Is involved in asymmetric cell division; asymmetric protein localization involved in cell fate determination; and establishment of mitotic spindle orientation. Located in P granule; posterior cell cortex; and protein-containing complex. Is expressed in germ line. par-2 encodes a protein containing a C3HC4-type RING-finger, a specialized type of zinc-finger found in E3 ubiquitin ligase subunits; PAR-2 is required maternally for polarization of the C. elegans zygote along the anterior-posterior (A-P) axis and is asymmetrically localized to the posterior cortex of the one- and two-cell embryo via interdependent interactions with PAR-3, PAR-6, and PKC-3. evidence par-2 encodes a protein containing a C3HC4-type RING-finger, a specialized type of zinc-finger found in E3 ubiquitin ligase subunits; PAR-2 is required maternally for polarization of the C. elegans zygote along the anterior-posterior (A-P) axis and is asymmetrically localized to the posterior cortex of the one- and two-cell embryo via interdependent interactions with PAR-3, PAR-6, and PKC-3. evidence UniProtKB:Q965F9 http://www.wormbase.org/species/c_elegans/gene/WBGene00003917 PAR2 (worm) HOIP_0050082 Enables lipid binding activity; microtubule binding activity; and protein kinase binding activity. Is involved in asymmetric cell division; asymmetric protein localization involved in cell fate determination; and establishment of mitotic spindle orientation. Located in P granule; posterior cell cortex; and protein-containing complex. Is expressed in germ line. http://www.wormbase.org/species/c_elegans/gene/WBGene00003917 par-2 encodes a protein containing a C3HC4-type RING-finger, a specialized type of zinc-finger found in E3 ubiquitin ligase subunits; PAR-2 is required maternally for polarization of the C. elegans zygote along the anterior-posterior (A-P) axis and is asymmetrically localized to the posterior cortex of the one- and two-cell embryo via interdependent interactions with PAR-3, PAR-6, and PKC-3. evidence http://www.wormbase.org/species/c_elegans/gene/WBGene00003917 HOIP:HOIP_0050083 A protein that is a translation product of the par-1 gene in worm. Enables myosin II tail binding activity; protein serine/threonine kinase activity; and ubiquitin protein ligase binding activity. Is involved in several processes, including cell differentiation; peptidyl-serine phosphorylation; and vulval development. Located in P granule and cell cortex. Is expressed in germ line and vulva. Human ortholog(s) of this gene are implicated in visual impairment and progressive phthisis bulbi. Is an ortholog of human MARK2 (microtubule affinity regulating kinase 2) and MARK3 (microtubule affinity regulating kinase 3). Enables myosin II tail binding activity; protein serine/threonine kinase activity; and ubiquitin protein ligase binding activity. Is involved in several processes, including cell differentiation; peptidyl-serine phosphorylation; and vulval development. Located in P granule and cell cortex. Is expressed in germ line and vulva. Human ortholog(s) of this gene are implicated in visual impairment and progressive phthisis bulbi. Is an ortholog of human MARK2 (microtubule affinity regulating kinase 2) and MARK3 (microtubule affinity regulating kinase 3). par-1 encodes a serine-threonine kinase; maternally provided PAR-1 is essential for establishing early embryonic polarity; PAR-1 is present in the cytoplasm and in the cell cortex and asymmetrically localized to the posterior cortex of late one-cell stage embryos; PAR-1 is continuously asymmetrically localized to the P lineage (germline blastomeres) at each subsequent division, and evenly distributed to the Z2 and Z3 germline precursors before eventually fading at embryonic morphogenesis; PAR-1 kinase activity is required for the asymmetric distribution of MEX-5 in the early embryo via a phosphorylation/dephosphorylation cycle that regulates MEX-5's association with slow- or fast-diffusing RNA-containing complexes; PAR-1 can phosphorylate MEX-5 in vitro and in vivo. evidence par-1 encodes a serine-threonine kinase; maternally provided PAR-1 is essential for establishing early embryonic polarity; PAR-1 is present in the cytoplasm and in the cell cortex and asymmetrically localized to the posterior cortex of late one-cell stage embryos; PAR-1 is continuously asymmetrically localized to the P lineage (germline blastomeres) at each subsequent division, and evenly distributed to the Z2 and Z3 germline precursors before eventually fading at embryonic morphogenesis; PAR-1 kinase activity is required for the asymmetric distribution of MEX-5 in the early embryo via a phosphorylation/dephosphorylation cycle that regulates MEX-5's association with slow- or fast-diffusing RNA-containing complexes; PAR-1 can phosphorylate MEX-5 in vitro and in vivo. evidence UniProtKB:Q9TW45 http://www.wormbase.org/species/c_elegans/gene/WBGene00003916 PAR1 (worm) HOIP_0050083 Enables myosin II tail binding activity; protein serine/threonine kinase activity; and ubiquitin protein ligase binding activity. Is involved in several processes, including cell differentiation; peptidyl-serine phosphorylation; and vulval development. Located in P granule and cell cortex. Is expressed in germ line and vulva. Human ortholog(s) of this gene are implicated in visual impairment and progressive phthisis bulbi. Is an ortholog of human MARK2 (microtubule affinity regulating kinase 2) and MARK3 (microtubule affinity regulating kinase 3). http://www.wormbase.org/species/c_elegans/gene/WBGene00003916 par-1 encodes a serine-threonine kinase; maternally provided PAR-1 is essential for establishing early embryonic polarity; PAR-1 is present in the cytoplasm and in the cell cortex and asymmetrically localized to the posterior cortex of late one-cell stage embryos; PAR-1 is continuously asymmetrically localized to the P lineage (germline blastomeres) at each subsequent division, and evenly distributed to the Z2 and Z3 germline precursors before eventually fading at embryonic morphogenesis; PAR-1 kinase activity is required for the asymmetric distribution of MEX-5 in the early embryo via a phosphorylation/dephosphorylation cycle that regulates MEX-5's association with slow- or fast-diffusing RNA-containing complexes; PAR-1 can phosphorylate MEX-5 in vitro and in vivo. evidence http://www.wormbase.org/species/c_elegans/gene/WBGene00003916 HOIP:HOIP_0050084 A protein that is a translation product of the par-4 gene in worm. Enables calmodulin binding activity and protein serine/threonine kinase activity. Is involved in several processes, including asymmetric protein localization involved in cell fate determination; cell division; and positive regulation of dauer larval development. Located in cell cortex. Is expressed widely. Is used to study Peutz-Jeghers syndrome. Human ortholog(s) of this gene are implicated in several diseases, including Peutz-Jeghers syndrome; female reproductive organ cancer (multiple); and pancreatic cancer. Is an ortholog of human STK11 (serine/threonine kinase 11). Enables calmodulin binding activity and protein serine/threonine kinase activity. Is involved in several processes, including asymmetric protein localization involved in cell fate determination; cell division; and positive regulation of dauer larval development. Located in cell cortex. Is expressed widely. Is used to study Peutz-Jeghers syndrome. Human ortholog(s) of this gene are implicated in several diseases, including Peutz-Jeghers syndrome; female reproductive organ cancer (multiple); and pancreatic cancer. Is an ortholog of human STK11 (serine/threonine kinase 11). par-4 encodes a serine-threonine kinase that is homologous to the human LKB1 kinase, mutations in which are associated with the cancer predisposition Peutz-Jeghers syndrome; par-4 activity is required for several development processes, including establishment of embryonic asymmetry, lifespan extension, response to oxidative stress and inhibition of germline proliferation during dauer larvae formation; genetic analyses suggest that in regulating the response to oxidative stress, par-4 acts upstream of aak-2 and that in regulating germ cell proliferation in dauers, par-4 acts upstream of aak-1 and in parallel to aak-2; PAR-4 is present in embryos, L4 larvae, males, and adult hermaphrodites; in the hermaphrodite gonad, PAR-4 is present at the actin-rich boundaries between syncytial nuclei, while in early embryos PAR-4 is present in the cytoplasm and at the cellular cortex; PAR-4 binds bovine calmodulin in vitro in a calcium-dependent manner. par-4 encodes a serine-threonine kinase that is homologous to the human LKB1 kinase, mutations in which are associated with the cancer predisposition Peutz-Jeghers syndrome; par-4 activity is required for several development processes, including establishment of embryonic asymmetry, lifespan extension, response to oxidative stress and inhibition of germline proliferation during dauer larvae formation; genetic analyses suggest that in regulating the response to oxidative stress, par-4 acts upstream of aak-2 and that in regulating germ cell proliferation in dauers, par-4 acts upstream of aak-1 and in parallel to aak-2; PAR-4 is present in embryos, L4 larvae, males, and adult hermaphrodites; in the hermaphrodite gonad, PAR-4 is present at the actin-rich boundaries between syncytial nuclei, while in early embryos PAR-4 is present in the cytoplasm and at the cellular cortex; PAR-4 binds bovine calmodulin in vitro in a calcium-dependent manner. UniProtKB:Q9GN62 http://www.wormbase.org/species/c_elegans/gene/WBGene00003919 PAR4 (worm) HOIP_0050084 Enables calmodulin binding activity and protein serine/threonine kinase activity. Is involved in several processes, including asymmetric protein localization involved in cell fate determination; cell division; and positive regulation of dauer larval development. Located in cell cortex. Is expressed widely. Is used to study Peutz-Jeghers syndrome. Human ortholog(s) of this gene are implicated in several diseases, including Peutz-Jeghers syndrome; female reproductive organ cancer (multiple); and pancreatic cancer. Is an ortholog of human STK11 (serine/threonine kinase 11). http://www.wormbase.org/species/c_elegans/gene/WBGene00003919 par-4 encodes a serine-threonine kinase that is homologous to the human LKB1 kinase, mutations in which are associated with the cancer predisposition Peutz-Jeghers syndrome; par-4 activity is required for several development processes, including establishment of embryonic asymmetry, lifespan extension, response to oxidative stress and inhibition of germline proliferation during dauer larvae formation; genetic analyses suggest that in regulating the response to oxidative stress, par-4 acts upstream of aak-2 and that in regulating germ cell proliferation in dauers, par-4 acts upstream of aak-1 and in parallel to aak-2; PAR-4 is present in embryos, L4 larvae, males, and adult hermaphrodites; in the hermaphrodite gonad, PAR-4 is present at the actin-rich boundaries between syncytial nuclei, while in early embryos PAR-4 is present in the cytoplasm and at the cellular cortex; PAR-4 binds bovine calmodulin in vitro in a calcium-dependent manner. http://www.wormbase.org/species/c_elegans/gene/WBGene00003919 HOIP:HOIP_0050085 A protein that is a translation product of the nmy-2 gene in worm. Enables calmodulin binding activity and protein kinase binding activity. Is involved in several processes, including cell division; multicellular organism development; and regulation of anatomical structure morphogenesis. Located in several cellular components, including cleavage furrow; contractile ring; and mitotic spindle. Is expressed in several structures, including distal tip cell; germ line; hypodermal cell; neuroblasts; and rectal gland cell. Human ortholog(s) of this gene are implicated in several diseases, including aortic aneurysm (multiple); auditory system disease (multiple); and blood platelet disease (multiple). Is an ortholog of several human genes including MYH10 (myosin heavy chain 10); MYH11 (myosin heavy chain 11); and MYH9 (myosin heavy chain 9). Enables calmodulin binding activity and protein kinase binding activity. Is involved in several processes, including cell division; multicellular organism development; and regulation of anatomical structure morphogenesis. Located in several cellular components, including cleavage furrow; contractile ring; and mitotic spindle. Is expressed in several structures, including distal tip cell; germ line; hypodermal cell; neuroblasts; and rectal gland cell. Human ortholog(s) of this gene are implicated in several diseases, including aortic aneurysm (multiple); auditory system disease (multiple); and blood platelet disease (multiple). Is an ortholog of several human genes including MYH10 (myosin heavy chain 10); MYH11 (myosin heavy chain 11); and MYH9 (myosin heavy chain 9). nmy-2 encodes a non-muscle myosin II; NMY-2 is required for polarized cytoplasmic flow, polarized distribution of the PAR proteins, cytokinesis, and for proper anterior-posterior polarity in early embryos; NMY-2 functions with PAR-5 in the onset of the establishment phase of polarization in the C. elegans zygote along the anterior-posterior axis, and nmy-2 is partially redundant with nmy-1 with respect to embryonic elongation; NMY-2 localization is dynamic in oocytes and embryos, with localization seen at the cell cortex, cleavage furrow, and spindle; once embryonic polarization is established, cortical NMY-2 localizes asymmetrically, with higher levels seen in the anterior cortex; NMY-2 binds bovine calmodulin in vitro in a calcium-dependent manner; during larval development, NMY-2 is required for correct fate specification in seam cell divisions. nmy-2 encodes a non-muscle myosin II; NMY-2 is required for polarized cytoplasmic flow, polarized distribution of the PAR proteins, cytokinesis, and for proper anterior-posterior polarity in early embryos; NMY-2 functions with PAR-5 in the onset of the establishment phase of polarization in the C. elegans zygote along the anterior-posterior axis, and nmy-2 is partially redundant with nmy-1 with respect to embryonic elongation; NMY-2 localization is dynamic in oocytes and embryos, with localization seen at the cell cortex, cleavage furrow, and spindle; once embryonic polarization is established, cortical NMY-2 localizes asymmetrically, with higher levels seen in the anterior cortex; NMY-2 binds bovine calmodulin in vitro in a calcium-dependent manner; during larval development, NMY-2 is required for correct fate specification in seam cell divisions. UniProtKB:G5EBY3 http://www.wormbase.org/species/c_elegans/gene/WBGene00003777 https://wormbase.org/species/c_elegans/protein/CE27133 NMY2 (worm) HOIP_0050085 Enables calmodulin binding activity and protein kinase binding activity. Is involved in several processes, including cell division; multicellular organism development; and regulation of anatomical structure morphogenesis. Located in several cellular components, including cleavage furrow; contractile ring; and mitotic spindle. Is expressed in several structures, including distal tip cell; germ line; hypodermal cell; neuroblasts; and rectal gland cell. Human ortholog(s) of this gene are implicated in several diseases, including aortic aneurysm (multiple); auditory system disease (multiple); and blood platelet disease (multiple). Is an ortholog of several human genes including MYH10 (myosin heavy chain 10); MYH11 (myosin heavy chain 11); and MYH9 (myosin heavy chain 9). http://www.wormbase.org/species/c_elegans/gene/WBGene00003777 nmy-2 encodes a non-muscle myosin II; NMY-2 is required for polarized cytoplasmic flow, polarized distribution of the PAR proteins, cytokinesis, and for proper anterior-posterior polarity in early embryos; NMY-2 functions with PAR-5 in the onset of the establishment phase of polarization in the C. elegans zygote along the anterior-posterior axis, and nmy-2 is partially redundant with nmy-1 with respect to embryonic elongation; NMY-2 localization is dynamic in oocytes and embryos, with localization seen at the cell cortex, cleavage furrow, and spindle; once embryonic polarization is established, cortical NMY-2 localizes asymmetrically, with higher levels seen in the anterior cortex; NMY-2 binds bovine calmodulin in vitro in a calcium-dependent manner; during larval development, NMY-2 is required for correct fate specification in seam cell divisions. http://www.wormbase.org/species/c_elegans/gene/WBGene00003777 HOIP:HOIP_0050087 A protein that is a translation product of the lgl-1 gene in worm. Is predicted to enable GTPase activator activity; myosin II binding activity; and syntaxin binding activity. Is involved in establishment of spindle orientation and protein localization. Located in basolateral plasma membrane and cell cortex. Is expressed in epithelial cell; intestine; spermathecal cell; and vulval cell. Is an ortholog of human LLGL1 (LLGL scribble cell polarity complex component 1) and LLGL2 (LLGL scribble cell polarity complex component 2). Is predicted to enable GTPase activator activity; myosin II binding activity; and syntaxin binding activity. Is involved in establishment of spindle orientation and protein localization. Located in basolateral plasma membrane and cell cortex. Is expressed in epithelial cell; intestine; spermathecal cell; and vulval cell. Is an ortholog of human LLGL1 (LLGL scribble cell polarity complex component 1) and LLGL2 (LLGL scribble cell polarity complex component 2). lgl-1 encodes a protein that is related to the Drosophila tumor suppressor Lethal giant larvae (Lgl), a basolateral junction component that regulates cell polarity by controlling localization of proteins to specific regions of the plasma membrane; lgl-1 functions redundantly with par-2 to generate and maintain cell polarity in the early elegans embryo; lgl-1 is involved in the asymmetric partitioning of the PAR (PAR-3/PAR-6/PKC-3) complex most likely by associating with PAR-6 and PKC-3; the association of lgl-1 with the PAR complex is dependent on phosphorylation of lgl-1 by PKC-3; lgl-1 is also required for the proper localization of myosin NMY-2; lgl-1 localizes asymmetrically to the posterior cortex in a PKC-3 dependent manner. lgl-1 encodes a protein that is related to the Drosophila tumor suppressor Lethal giant larvae (Lgl), a basolateral junction component that regulates cell polarity by controlling localization of proteins to specific regions of the plasma membrane; lgl-1 functions redundantly with par-2 to generate and maintain cell polarity in the early elegans embryo; lgl-1 is involved in the asymmetric partitioning of the PAR (PAR-3/PAR-6/PKC-3) complex most likely by associating with PAR-6 and PKC-3; the association of lgl-1 with the PAR complex is dependent on phosphorylation of lgl-1 by PKC-3; lgl-1 is also required for the proper localization of myosin NMY-2; lgl-1 localizes asymmetrically to the posterior cortex in a PKC-3 dependent manner. UniProtKB:G5EEI1 doi/10.1895/wormbook.1.30.2 http://www.wormbase.org/species/c_elegans/gene/WBGene00018987 https://wormbase.org/species/c_elegans/protein/CE45655 LGL1 (worm) HOIP_0050087 Is predicted to enable GTPase activator activity; myosin II binding activity; and syntaxin binding activity. Is involved in establishment of spindle orientation and protein localization. Located in basolateral plasma membrane and cell cortex. Is expressed in epithelial cell; intestine; spermathecal cell; and vulval cell. Is an ortholog of human LLGL1 (LLGL scribble cell polarity complex component 1) and LLGL2 (LLGL scribble cell polarity complex component 2). http://www.wormbase.org/species/c_elegans/gene/WBGene00018987 lgl-1 encodes a protein that is related to the Drosophila tumor suppressor Lethal giant larvae (Lgl), a basolateral junction component that regulates cell polarity by controlling localization of proteins to specific regions of the plasma membrane; lgl-1 functions redundantly with par-2 to generate and maintain cell polarity in the early elegans embryo; lgl-1 is involved in the asymmetric partitioning of the PAR (PAR-3/PAR-6/PKC-3) complex most likely by associating with PAR-6 and PKC-3; the association of lgl-1 with the PAR complex is dependent on phosphorylation of lgl-1 by PKC-3; lgl-1 is also required for the proper localization of myosin NMY-2; lgl-1 localizes asymmetrically to the posterior cortex in a PKC-3 dependent manner. http://www.wormbase.org/species/c_elegans/gene/WBGene00018987 doi/10.1895/wormbook.1.30.2 Apart from the actomyosin network and the PAR proteins, other components participate in generating AP polarity in the one-cell embryo. This includes LGL-1, the worm homologue of the Drosophila tumor-suppressor protein Lethal Giant Larvae, which functions redundantly with PAR-2 during polarity maintenance (Beatty et al., 2010; Hoege et al., 2010). LGL-1 is enriched on the posterior cortex, and its depletion, while not resulting in a phenotype on its own, affects the distribution of cortical NMY-2 and enhances the lethality incurred from partial PAR-2 inactivation. Conversely, increasing LGL-1 levels alleviates aspects of the par-2(RNAi) phenotype. Therefore, LGL-1 can be thought of as defining a second pathway that contributes to polarity establishment in the absence of PAR-2. HOIP:HOIP_0050090 A cell division control protein 42 that is encoded in the genome of worm. CDC42 (worm) Enables GTP binding activity and GTPase activity. Is involved in several processes, including establishment of mitotic spindle orientation; positive regulation of nematode male tail tip morphogenesis; and regulation of cellular component organization. Located in centrosome; cytoplasm; and plasma membrane. Is integral component of membrane. Is expressed in several structures, including AIY; P8.pa; hermaphrodite gonad; hypodermal cell; and nerve ring. Is used to study cerebral cavernous malformation. Human ortholog(s) of this gene are implicated in several diseases, including Alzheimer's disease; bipolar disorder; fibrosarcoma; and rhinitis. Is an ortholog of human CDC42 (cell division cycle 42). Enables GTP binding activity and GTPase activity. Is involved in several processes, including establishment of mitotic spindle orientation; positive regulation of nematode male tail tip morphogenesis; and regulation of cellular component organization. Located in centrosome; cytoplasm; and plasma membrane. Is integral component of membrane. Is expressed in several structures, including AIY; P8.pa; hermaphrodite gonad; hypodermal cell; and nerve ring. Is used to study cerebral cavernous malformation. Human ortholog(s) of this gene are implicated in several diseases, including Alzheimer's disease; bipolar disorder; fibrosarcoma; and rhinitis. Is an ortholog of human CDC42 (cell division cycle 42). UniProtKB:Q05062 http://www.wormbase.org/species/c_elegans/gene/WBGene00000390 https://wormbase.org/species/c_elegans/protein/CE02020 CDC42Ce (worm) cell division control protein 42 homolog (worm) R07G3.1 cdc-42 CDC42 (worm) HOIP_0050090 Enables GTP binding activity and GTPase activity. Is involved in several processes, including establishment of mitotic spindle orientation; positive regulation of nematode male tail tip morphogenesis; and regulation of cellular component organization. Located in centrosome; cytoplasm; and plasma membrane. Is integral component of membrane. Is expressed in several structures, including AIY; P8.pa; hermaphrodite gonad; hypodermal cell; and nerve ring. Is used to study cerebral cavernous malformation. Human ortholog(s) of this gene are implicated in several diseases, including Alzheimer's disease; bipolar disorder; fibrosarcoma; and rhinitis. Is an ortholog of human CDC42 (cell division cycle 42). http://www.wormbase.org/species/c_elegans/gene/WBGene00000390 HOIP:HOIP_0050099 A physical attribute inhering in a bearer by virtue of the bearer's disposition to recover its size and shape after deformation in any way. elasticity (attribute) HOIP_0050099 HOIP:HOIP_0050100 A physical attribute that is the ability to contract or shrink. contractility (attribute) HOIP_0050100 HOIP:HOIP_0050112 The process that occurs after sperm attachment, fusion of the plasma membrane and enters into an oocyte. ISBN13:9784895928052 doi/10.1895/wormbook.1.30.2 C. elegans sperm entry into oocyte_2 HOIP_0050112 ISBN13:9784895928052 Gilbert, Scott F. , 阿形, 清和, 高橋, 淑子, ギルバート発生生物学, メディカル・サイエンス・インターナショナル, 2015 doi/10.1895/wormbook.1.30.2 Fertilization initiates a cascade of events that leads to breaking the symmetry of the oocyte, as evidenced by a local cessation of actomyosin contractility. What is the nature of the symmetry-breaking cue? It is not the sperm entry site nor paternal genetic material (Sadler and Shakes, 2000 Goldstein and Hird, 1996). Instead, centrioles are key. As in most metazoan organisms, the sperm contributes the sole pair of centrioles to the zygote. These centrioles recruit pericentriolar material (PCM) from maternal stores and thus assemble centrosomes that nucleate microtubules. After an initial phase during which centrosome maturation is suppressed (McNally et al., 2012), the earliest sign of symmetry-breaking is the local cessation of surface contractions where centrosomes become juxtaposed to the cortex after a random walk that relies on short cortical microtubules (Bienkowska and Cowan, 2012; Cheeks et al., 2004; Cowan and Hyman, 2004b; Munro et al., 2004; Cuenca et al., 2003). HOIP:HOIP_0050123 Cell cortex contraction is a subtype of contraction: A process that generates the directed movement in which the cell cortex decreases in volume. cell cortex contraction in the one-cell embryo dependent process in C.elegans HOIP_0050123 HOIP:HOIP_0050124 The process of creating PAR-3 oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. PAR3 oligomerization in the one-cell embryo dependent process in C.elegans HOIP_0050124 HOIP:HOIP_0050125 aPKC kinase acculumation at the anterior cortex is a subtype of protein accumulation: A process that keeps aPKC kinas in the anterior cortex. aPKC kinase acculumation at the anterior cortex in the one-cell embryo dependent process in C.elegans HOIP_0050125 HOIP:HOIP_0050127 PAR2 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into PAR2. PMID:21983565 PMID:32829680 doi/10.1895/wormbook.1.30.2 PAR2 phosphorylation in the one-cell embryo dependent process in C.elegans HOIP_0050127 PMID:21983565 Before polarization, cortical aPKC excludes PAR-1 kinase and its binding partner PAR-2 by phosphorylation. During symmetry breaking, microtubules nucleated by the centrosome locally protect PAR-2 from phosphorylation by aPKC, allowing PAR-2 and PAR-1 to access the cortex nearest the centrosome. PMID:32829680 The posterior PARs can be phosphorylated by aPKC, which drives their dissociation from the membrane, and similarly, the PAR-1 kinase, recruited by membrane-associated PAR-2, removes cortical aPARs via phosphorylation of PAR-3 (figure 1a). doi/10.1895/wormbook.1.30.2 Live imaging revealed that PAR-2 associates with centrosomes, whereas biochemical experiments established that PAR-2 is a microtubule binding protein (Motegi et al., 2011). Interestingly, microtubule association protects PAR-2 from phosphorylation by PKC-3 in vitro. Thus, in vivo, association of PAR-2 with microtubules emanating from the centrosomes at the posterior would prevent the action of PKC-3, which would otherwise inhibit PAR-2 cortical localization (Motegi et al., 2011). HOIP:HOIP_0050128 PAR3 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into PAR3. PMID:32829680 PAR3 phosphorylation in the one-cell embryo dependent process in C.elegans HOIP_0050128 PMID:32829680 The posterior PARs can be phosphorylated by aPKC, which drives their dissociation from the membrane, and similarly, the PAR-1 kinase, recruited by membrane-associated PAR-2, removes cortical aPARs via phosphorylation of PAR-3 (figure 1a). HOIP:HOIP_0050129 Any process that stops, prevents, or reduces the frequency, rate or extent of anterior PARs (aPARs) localization to posterior cortex. doi/10.1895/wormbook.1.30.2 negative regulation of anterior PARs (aPARs) localization to posterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050129 HOIP:HOIP_0050131 Any process that stops, prevents, or reduces the frequency, rate or extent of posterior PARs (pPARs) localization to anterior cortex. doi/10.1895/wormbook.1.30.2 negative regulation of posterior PARs (pPARs) localization to anterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050131 HOIP:HOIP_0050132 PAR1-PAR-2 complex assembly in the one-cell embryo dependent process in C.elegans The aggregation, arrangement and bonding together of a set of components to form a PAR1-PAR2 complex. HOIP_0050132 HOIP:HOIP_0050133 The aggregation, arrangement and bonding together of a set of components to form a PAR3-PAR6-aPKC complex. doi/10.1895/wormbook.1.30.2 PAR3-PAR6-aPKC complex formation in the one-cell embryo dependent process in C.elegans HOIP_0050133 doi/10.1895/wormbook.1.30.2 PAR-3 and PAR-6 are PDZ-containing proteins that, together with the atypical protein kinase C PKC-3, form the so-called “anterior PAR complex”. HOIP:HOIP_0050134 A process that stops, prevents, or reduces the frequency, rate or extent of PAR2 binding to cellular membrane phospholipids. PMID:21983565 PMID:32829680 negative regulation of PAR2 binding to cellular membrane phospholipid in the one-cell embryo dependent process in C.elegans HOIP_0050134 PMID:21983565 Using a protein-lipid binding assay, we found that PAR-2 interacts with phospholipids including phosphoinositides (Fig. 2e,f and Supplementary Fig. S7). Phosphorylation by aPKC, or phosphomimetic mutations in the PKC-3 sites, interfered with PAR-2 binding to lipids (Fig. 2e,f and Supplementary Fig. S7), as they interfere with PAR-2 cortical localization in vivo. PMID:32829680 The posterior PARs can be phosphorylated by aPKC, which drives their dissociation from the membrane, and similarly, the PAR-1 kinase, recruited by membrane-associated PAR-2, removes cortical aPARs via phosphorylation of PAR-3 (figure 1a). HOIP:HOIP_0050135 A process that stops, prevents, or reduces the frequency, rate or extent of PAR1 binding to cellular membrane phospholipids. negative regulation of PAR1 binding to cellular membrane phospholipid in the one-cell embryo dependent process in C.elegans HOIP_0050135 HOIP:HOIP_0050136 PMID:32829680 doi/10.1895/wormbook.1.30.2 maintenance of anterior-posterior polarity in the one-cell embryo dependent process in C.elegans HOIP_0050136 PMID:32829680 Posterior-directed cytoplasmic flow and centrosomal MT asters synergize to position the PN/centrosome complex close to the cortex at the posterior pole, ensuring robust polarization of the zygote (figure 1d(ii)). This initiates a mechanochemical-positive feedback loop whereby the signal emanating from the centrosomes promotes actomyosin flow, which maintains centrosome–cortex proximity and strengthens the polarity signal. doi/10.1895/wormbook.1.30.2 The AP embryonic axis is put in place during the first cell cycle and this process can be decomposed into three principal steps: symmetry breaking, establishment of AP polarity, and maintenance of this polarity. HOIP:HOIP_0050137 doi/10.1895/wormbook.1.30.2 formation of anterior-posterior polarity in the one-cell embryo dependent process in C.elegans HOIP_0050137 doi/10.1895/wormbook.1.30.2 The AP embryonic axis is put in place during the first cell cycle and this process can be decomposed into three principal steps: symmetry breaking, establishment of AP polarity, and maintenance of this polarity. HOIP:HOIP_0050141 Rho signaling is a process that a signal is transmitted by the Rho. Rho signaling HOIP_0050141 HOIP:HOIP_0050144 A series of molecular signals within the cell that are mediated by a member of the Rho family of proteins switching to a GTP-bound active state. Rho protein signal transduction HOIP_0050144 HOIP:HOIP_0050148 A cellular process that results in the assembly of one or more centrioles. doi/10.1895/wormbook.1.30.2 centriole assembly in the one-cell embryo dependent process in C.elegans HOIP_0050148 doi/10.1895/wormbook.1.30.2 What is the nature of the symmetry-breaking cue? It is not the sperm entry site nor paternal genetic material (Sadler and Shakes, 2000 Goldstein and Hird, 1996). Instead, centrioles are key. As in most metazoan organisms, the sperm contributes the sole pair of centrioles to the zygote. These centrioles recruit pericentriolar material (PCM) from maternal stores and thus assemble centrosomes that nucleate microtubules. HOIP:HOIP_0050153 Negative regulation of actomyosin contraction is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of contractile movement of actomyosin. negative regulation of actomyosin contraction HOIP_0050153 HOIP:HOIP_0050154 Actomyosin contraction is a subtype of contraction: A process that generates the directed movement in which the actomyosin decreases in volume. actomyosin contraction HOIP_0050154 HOIP:HOIP_0050155 Negative regulation of actomyosin contraction is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of contractile movement of actomyosin. PMID:31636075 PMID:32829680 doi/10.1895/wormbook.1.30.2 negative regulation of local actomyosin contraction in the one-cell embryo dependent process in C.elegans HOIP_0050155 PMID:31636075 Notably, ECT-2 is excluded from the posterior cortex at the onset of symmetry breaking, and this event is correlated with the disappearance of the non-muscle myosin II (NMY-2) from the posterior cortex (Munro et al., 2004; Motegi and Sugimoto, 2006). A Rho GEF, ECT-2, acts downstream of AIR-1 in regulating contractility and PAR-2 localisation, and, notably, AIR-1 depletion influences ECT-2 cortical localisation. PMID:32829680 Figure 1 (d) Temporal snapshots during SB: (i) after fertilization, aPARs initially occupy the entire membrane, while pPARs are mostly cytoplasmic. The sperm-derived centrosomes (purple spheres) are positioned close to the cortex at the future posterior pole. (ii) A diffusive cue of Aurora A from the centrosomes inhibits actomyosin contractility in the posterior pole, resulting in a cortical flow towards the anterior domain. Upon fertilization and completion of maternal meiosis, the sperm-donated centrosome induces a local inhibition of actomyosin contractility at the posterior pole of the zygote. This leads to flow of the actomyosin network towards the anterior, leaving a smoothened posterior cortex (akin to placing an elastic band under tension and then cutting one end) (figures 1c,d(ii)). doi/10.1895/wormbook.1.30.2 What are the mechanisms leading to the local cessation of cortical contractions following symmetry breaking? A critical event is the inactivation of RHO-1 in the vicinity of centrosomes. Like other small G proteins, RHO-1 is regulated positively by guanine-nucleotide-exchange factors (GEFs) and negatively by GTPase-activating proteins (GAPs). Thus, the RHO-1 GEF ECT-2 promotes generation of active RHO-1-GTP, and the novel protein NOP-1 is important for ECT-2 activity (Tse et al., 2012). Interestingly, ECT-2 is distributed uniformly on the cortex before symmetry breaking, but removed in the vicinity of centrosomes concomitantly with the appearance of non-contractile cortex (Motegi and Sugimoto, 2006; Schonegg and Hyman, 2006). How the presence of centrosomes results in local ECT-2 removal is not clear. In addition, the GAP CYK-4, which might promote the generation of inactive RHO-1-GDP, has been proposed to play a role (Jenkins et al., 2006). CYK-4 is present in sperm and persists in the newly fertilized zygote on membranous organelles in the vicinity of the centrosome, as well as on the cortex, where it could conceivably contribute to local RHO-1 inactivation. I HOIP:HOIP_0050156 Actomyosin contraction is a subtype of contraction: A process that generates the directed movement in which the actomyosin decreases in volume. PMID:32829680 doi/10.1895/wormbook.1.30.2 actomyosin contraction in the one-cell embryo dependent process in C.elegans HOIP_0050156 Starting from the time of anaphase of meiosis II, the entire actomyosin network located in the cell cortex that underlies the plasma membrane undergoes contractions that depend on the non-muscle myosin II heavy chain NMY-2 and the associated non-muscle myosin light chain 4 MLC-4 (Munro et al., 2004; Shelton et al., 1999) doi/10.1895/wormbook.1.30.2 Starting from the time of anaphase of meiosis II, the entire actomyosin network located in the cell cortex that underlies the plasma membrane undergoes contractions that depend on the non-muscle myosin II heavy chain NMY-2 and the associated non-muscle myosin light chain 4 MLC-4 (Munro et al., 2004; Shelton et al., 1999) doi/10.1895/wormbook.1.30.2 PMID:32829680 Prior to polarization, a highly contractile cortex, involving a dynamic network of actin filaments and non-muscle myosin II foci, occupies the entire zygote. doi/10.1895/wormbook.1.30.2 Fertilization occurs in the spermatheca, with the union of a mature oocyte and a sperm cell. The newly fertilized zygote is then displaced into the uterus where meiosis is completed and early embryogenesis takes place. Starting from the time of anaphase of meiosis II, the entire actomyosin network located in the cell cortex that underlies the plasma membrane undergoes contractions that depend on the non-muscle myosin II heavy chain NMY-2 and the associated non-muscle myosin light chain 4 MLC-4 (Munro et al., 2004; Shelton et al., 1999) (Figure 2A). Moreover, such surface contractions require the Rho family GTPase RHO-1 and the Rho-binding kinase LET-502, which together promote NMY-2 activity and contraction of the cortical actomyosin network (Kumfer et al., 2010; Motegi and Sugimoto, 2006; Schonegg and Hyman, 2006). HOIP:HOIP_0050159 A myosin regulatory light chain MRLC3 that is encoded in the genome of worm. [OMA:Q09510, PRO:DNx] myosin RLC (human) HGNC:16701 MYL12A HEL-S-24 (human) MLC-2B (human) epididymis secretory protein Li 24 (human) hMYL12A myosin regulatory light chain 2, nonsarcomeric (human) myosin regulatory light chain MRLC3 (human) MLCB MRLC3 MYL12A RLC mlc-4 myosin regulatory light chain 12A (human) HOIP_0050159 HOIP:HOIP_0050160 Positive regulation of actomyosin contraction is a subtype of positive regulation process: A processthat activates or increases the frequency, rate or extent of contractile movement of actomyosin. positive regulation of actomyosin contraction HOIP_0050160 HOIP:HOIP_0050161 Positive regulation of actomyosin contraction is a subtype of positive regulation process: A processthat activates or increases the frequency, rate or extent of contractile movement of actomyosin. PMID:32829680 doi/10.1895/wormbook.1.30.2 positive regulation of actomyosin contraction in the one-cell embryo dependent process in C.elegans HOIP_0050161 PMID:32829680 aPARs stimulate cortical contractility, further promoting flow and, hence, their own asymmetric localization. actomyosin contractility is primarily dependent on the small GTPase RhoA homologue, RHO-1, the activity of which is regulated by the GEF ECT-2 (guanine nucleotide exchange factor) and the GAPs (GTPase-activating proteins), RGA-3 and RGA-4(figure 2f ). The precise molecular mechanism(s) of how PARs regulate actomyosin flow are still under investigation; however, aPARs have been described to stabilize myosin II at the anterior domain and might regulate RHO-1 via the TAO kinase KIN-18. doi/10.1895/wormbook.1.30.2 Fertilization occurs in the spermatheca, with the union of a mature oocyte and a sperm cell. The newly fertilized zygote is then displaced into the uterus where meiosis is completed and early embryogenesis takes place. Starting from the time of anaphase of meiosis II, the entire actomyosin network located in the cell cortex that underlies the plasma membrane undergoes contractions that depend on the non-muscle myosin II heavy chain NMY-2 and the associated non-muscle myosin light chain 4 MLC-4 (Munro et al., 2004; Shelton et al., 1999) (Figure 2A). Moreover, such surface contractions require the Rho family GTPase RHO-1 and the Rho-binding kinase LET-502, which together promote NMY-2 activity and contraction of the cortical actomyosin network (Kumfer et al., 2010; Motegi and Sugimoto, 2006; Schonegg and Hyman, 2006). HOIP:HOIP_0050163 A protein that is a translation product of the let-502 gene in worm. UniProtKB:P92199 WormBase:WBGene00002694 let-502 LET502 (worm) HOIP_0050163 WormBase:WBGene00002694 let-502 http://www.wormbase.org/species/c_elegans/gene/WBGene00002694 HOIP:HOIP_0050164 NMY activation is a subtype of molecular activation: A process that changes the activity of the NMY to be higher. NMY activation HOIP_0050164 HOIP:HOIP_0050165 NMY activation is a subtype of molecular activation: A process that changes the activity of the NMY to be higher. doi/10.1895/wormbook.1.30.2 NMY activation in the one-cell embryo dependent process in C.elegans HOIP_0050165 doi/10.1895/wormbook.1.30.2 Starting from the time of anaphase of meiosis II, the entire actomyosin network located in the cell cortex that underlies the plasma membrane undergoes contractions that depend on the non-muscle myosin II heavy chain NMY-2 and the associated non-muscle myosin light chain 4 MLC-4 (Munro et al., 2004; Shelton et al., 1999) (Figure 2A). Moreover, such surface contractions require the Rho family GTPase RHO-1 and the Rho-binding kinase LET-502, which together promote NMY-2 activity and contraction of the cortical actomyosin network (Kumfer et al., 2010; Motegi and Sugimoto, 2006; Schonegg and Hyman, 2006). HOIP:HOIP_0050166 The process in which pericentriolar material (PCM) from maternal stores required for centrosome assembly become associated with the centrioles. doi/10.1895/wormbook.1.30.2 recruitment of pericentriolar material in the one-cell embryo dependent process in C.elegans HOIP_0050166 Starting from the time of anaphase of meiosis II, the entire actomyosin network located in the cell cortex that underlies the plasma membrane undergoes contractions that depend on the non-muscle myosin II heavy chain NMY-2 and the associated non-muscle myosin light chain 4 MLC-4 (Munro et al., 2004; Shelton et al., 1999) doi/10.1895/wormbook.1.30.2 doi/10.1895/wormbook.1.30.2 As in most metazoan organisms, the sperm contributes the sole pair of centrioles to the zygote. These centrioles recruit pericentriolar material (PCM) from maternal stores and thus assemble centrosomes that nucleate microtubules. HOIP:HOIP_0050167 PMID:20066102 PMID:31327978 doi/10.1895/wormbook.1.30.2 cellular cortical flow generation to anterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050167 PMID:20066102 Movement of the sperm MTOC toward the cortex causes a rapid local cessation of focal contractility and an asymmetrical contraction of the remaining actomyosin network, causing a flow of cortical actomyosin toward the opposite (future anterior) pole. PMID:31327978 Contractility in the actomyosin cortex is increased via RhoA activation [18], and a local down-regulation of non-muscle myosin II (NMY-2, referred to as myosin) at the posterior pole [19] initiates cortical flows. doi/10.1895/wormbook.1.30.2 The AP embryonic axis is put in place during the first cell cycle and this process can be decomposed into three principal steps: symmetry breaking, establishment of AP polarity, and maintenance of this polarity. HOIP:HOIP_0050168 .A process that changes the direction of the fluid. changing direction of flow HOIP_0050168 HOIP:HOIP_0050169 A liquid, gas, or other material that continuously deforms (flows) under an applied shear stress, or external force. A liquid, gas, or other material that continuously deforms (flows) under an applied shear stress, or external force. fluid HOIP_0050169 A liquid, gas, or other material that continuously deforms (flows) under an applied shear stress, or external force. https://en.wikipedia.org/wiki/Fluid HOIP:HOIP_0050170 A process that generates the directed movement of cortical flow. cortical flow generation HOIP_0050170 HOIP:HOIP_0050179 PMID:31636075 UniprotKB:G5EDL3 WormBase:WBGene00000098 https://www.ncbi.nlm.nih.gov/gene/179202 air-1 Aurora kinase (worm) HOIP_0050179 PMID:31636075 a Rho GEF, ECT-2, acts downstream of AIR-1 in regulating contractility and PAR-2 localisation, and AIR-1 depletion influences ECT-2 cortical localisation UniprotKB:G5EDL3 https://www.uniprot.org/uniprot/G5EDL3 WormBase:WBGene00000098 https://www.wormbase.org/search/gene/WBGene00000098 HOIP:HOIP_0050180 The directed movement of the centrosome to a specific location to the cell cortex.. PMID:22425158 doi/10.1895/wormbook.1.30.2 establishment of centrosome localization in cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050180 PMID:22425158 Furthermore, centrosomes did not move to the cortex in embryos that had a disrupted actomyosin cortex and lacked cortical flow or did not establish polarity. Cytoplasmic flow, generated by polarity establishment, may move centrosomes to the cortex after symmetry breaking. The close approximation of centrosomes to the cortex appeared to be a consequence, rather than a cause, of polarity establishment. doi/10.1895/wormbook.1.30.2 After an initial phase during which centrosome maturation is suppressed (McNally et al., 2012), the earliest sign of symmetry-breaking is the local cessation of surface contractions where centrosomes become juxtaposed to the cortex after a random walk that relies on short cortical microtubules. Centrosomes can also break symmetry at a slight distance from the cortex, although subsequent AP polarity establishment is delayed in these instances, as is the case when microtubules are lacking and, as a consequence, centrosomes approach the cortex only after a lag time (Bienkowska and Cowan, 2012). This partial reliance on cortical microtubules may help resolve apparent contradictions in the literature concerning the requirement of microtubules for polarization in the one-cell embryo (Tsai and Ahringer, 2007; Cowan and Hyman, 2004b; Sonneville and Gönczy, 2004). HOIP:HOIP_0050181 A process that chenges the location of centrioles. centriole migration HOIP_0050181 HOIP:HOIP_0050185 A process in which a PAR3 is transported to, or maintained in, the anterior cell cortex. doi/10.1895/wormbook.1.30.2 PAR3 localization to anterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050185 doi/10.1895/wormbook.1.30.2 The anterior PAR complex marked by GFP::PAR-6 is present throughout the cortex initially, but recedes from the posterior following symmetry breaking, concomitant with the anteriorly-directed movement of the contractile cortex (Munro et al., 2004; Cuenca et al., 2003) HOIP:HOIP_0050187 The directed movement of the centrosome to a specific location to the cell cortex.. PMID:22425158 doi/10.1895/wormbook.1.30.2 centrosome localization in cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050187 PMID:22425158 Furthermore, centrosomes did not move to the cortex in embryos that had a disrupted actomyosin cortex and lacked cortical flow or did not establish polarity. Cytoplasmic flow, generated by polarity establishment, may move centrosomes to the cortex after symmetry breaking. The close approximation of centrosomes to the cortex appeared to be a consequence, rather than a cause, of polarity establishment. doi/10.1895/wormbook.1.30.2 After an initial phase during which centrosome maturation is suppressed (McNally et al., 2012), the earliest sign of symmetry-breaking is the local cessation of surface contractions where centrosomes become juxtaposed to the cortex after a random walk that relies on short cortical microtubules. Centrosomes can also break symmetry at a slight distance from the cortex, although subsequent AP polarity establishment is delayed in these instances, as is the case when microtubules are lacking and, as a consequence, centrosomes approach the cortex only after a lag time (Bienkowska and Cowan, 2012). This partial reliance on cortical microtubules may help resolve apparent contradictions in the literature concerning the requirement of microtubules for polarization in the one-cell embryo (Tsai and Ahringer, 2007; Cowan and Hyman, 2004b; Sonneville and Gönczy, 2004). HOIP:HOIP_0050190 A process in which a PAR2 is transported to, or maintained in, the posterior cell cortex. PAR2 localization to poterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050190 HOIP:HOIP_0050191 PAR3 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into PAR3. PAR3 phosphorylation HOIP_0050191 HOIP:HOIP_0050192 PAR2 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into PAR2. PAR2 phosphorylation HOIP_0050192 HOIP:HOIP_0050193 Any process that keeps the spatial arrangement of PAR3 between and within cell cortex. doi/10.1895/wormbook.1.30.2 PAR3 distribution in cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050193 doi/10.1895/wormbook.1.30.2 The anterior PAR complex marked by GFP::PAR-6 is present throughout the cortex initially, but recedes from the posterior following symmetry breaking, concomitant with the anteriorly-directed movement of the contractile cortex (Munro et al., 2004; Cuenca et al., 2003) HOIP:HOIP_0050194 The process in which PAR-3 is released from the posterior cell cortex. dissociation of PAR3 from posterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050194 HOIP:HOIP_0050195 The process in which PAR-3 is released from the posterior cell cortex. dissociation of PAR-3 from posterior cell cortex HOIP_0050195 HOIP:HOIP_0050196 PMID:32829680 doi/10.1895/wormbook.1.30.2 cytiplasimic flow generation in the one-cell embryo dependent process in C.elegans HOIP_0050196 PMID:32829680 Upon fertilization and completion of maternal meiosis, the sperm-donated centrosome induces a local inhibition of actomyosin contractility at the posterior pole of the zygote. This leads to flow of the actomyosin network towards the anterior, leaving a smoothened posterior cortex (akin to placing an elastic band under tension and then cutting one end) (figures 1c,d(ii), 2a, b ). As a result of this actomyosin retraction, cytoplasmic flow is generated; an anterior-directed cortical flow, which subsequently produces countercurrent posterior-directed central flow owing to the fluid-like properties of the cytoplasm and geometry of the zygote (figure 1c, zygote). doi/10.1895/wormbook.1.30.2 The AP embryonic axis is put in place during the first cell cycle and this process can be decomposed into three principal steps: symmetry breaking, establishment of AP polarity, and maintenance of this polarity. HOIP:HOIP_0050197 A process that generates the directed movement of cytoplasmic flow. cytoplasmic flow generation HOIP_0050197 HOIP:HOIP_0050198 Any process in which a male pronucleus-centrosome complex is transported to, and/or maintained in, a specific location within the posterior cell. PMID:31327978 PMID:32829680 male pronucleus-centrosome complex localization close to the posterior cortex in the one-cell embryo dependent process in C.elegans HOIP_0050198 PMID:32829680 Posterior-directed cytoplasmic flow and centrosomal MT asters synergize to position the PN/centrosome complex close to the cortex at the posterior pole, ensuring robust polarization of the zygote (figure 1d(ii)). HOIP:HOIP_0050199 doi/10.1895/wormbook.1.30.2 regulation of posterior axis specification in the one-cell embryo dependent process in C.elegans HOIP_0050199 doi/10.1895/wormbook.1.30.2 The AP embryonic axis is put in place during the first cell cycle and this process can be decomposed into three principal steps: symmetry breaking, establishment of AP polarity, and maintenance of this polarity. HOIP:HOIP_0050200 The directed movement of the male and female pronuclei towards each other prior to their fusion. doi/10.1895/wormbook.1.30.2 pronuclear migration in the one-cell embryo dependent process in C.elegans HOIP_0050200 doi/10.1895/wormbook.1.30.2 Centrosomes and the associated male pronucleus are located initially close to the posterior cortex, and then migrate jointly towards the anterior. Concomitantly, the female pronucleus migrates towards the posterior, resulting in the meeting of the two pronuclei in the posterior half of the embryo. Migration of both male and female pronuclei depends on microtubules and microtubule associated proteins, including the minus-end directed motor dynein and members of the dynein complex (reviewed in McNally, 2013; Morin and Bellaiche, 2011; Galli and van den Heuvel, 2008). Dynein present on the surface of the female pronucleus is thought to capture the plus-ends of astral microtubules nucleated by the centrosomes, and thus power migration of the female pronucleus towards the male pronucleus associated with the centrosomes (Gönczy et al., 1999). After pronuclear meeting, the centrosomes and the joined pronuclei move towards the embryo center, while undergoing a 90° rotation. This process is referred to collectively as centration/rotation and results in the centrosomes becoming aligned along the AP axis in preparation for cell division. Following nuclear envelope breakdown (NEBD), the spindle assembles in the cell center and along the AP axis, but is displaced posteriorly during metaphase and anaphase (reviewed in Asymmetric cell division and axis formation in the embryo). Moreover, the posterior spindle pole exhibits vigorous transverse oscillations during anaphase. As a result of the asymmetric spindle position achieved at the end of mitosis, the first cleavage is unequal and generates the larger anterior blastomere AB and the smaller posterior blastomere P1. Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook HOIP:HOIP_0050202 The merging of two pronuclei in a fertilized egg to fuse and produce a single zygotic genome. doi/10.1895/wormbook.1.30.2 pronuclear fusion in the one-cell embryo dependent process in C.elegans HOIP_0050202 doi/10.1895/wormbook.1.30.2 Centrosomes and the associated male pronucleus are located initially close to the posterior cortex, and then migrate jointly towards the anterior. Concomitantly, the female pronucleus migrates towards the posterior, resulting in the meeting of the two pronuclei in the posterior half of the embryo. Migration of both male and female pronuclei depends on microtubules and microtubule associated proteins, including the minus-end directed motor dynein and members of the dynein complex (reviewed in McNally, 2013; Morin and Bellaiche, 2011; Galli and van den Heuvel, 2008). HOIP:HOIP_0050203 The controlled breakdown of the nuclear membranes, for example during cellular division. doi/10.1895/wormbook.1.72.1 nuclear envelope breakdown nuclear envelope catabolism nuclear envelope degradation mitotic nuclear membrane disassembly in the one-cell embryo dependent process in C.elegans HOIP_0050203 doi/10.1895/wormbook.1.72.1 Concomitant with nuclear envelope break down, centrosomal microtubules penetrate the nuclear space and begin to interact with chromosomes. Spindle assembly is completed in the subsequent ~2.5 minute period between nuclear envelope breakdown and anaphase onset. Oegema, K. and Hyman, A. A. Cell division (January 19, 2006), WormBook, ed. The C. elegans Research Community, WormBook HOIP:HOIP_0050205 A complex that comprises male pronucleus derived from sperm and centrosome. pronucleus centrosome complex HOIP_0050205 HOIP:HOIP_0050206 Any process that activates or increases the frequency, rate or extent of cellular cortical flow generation PMID:20066102 PMID:31327978 PMID:32829680 doi/10.1895/wormbook.1.30.2 positive regulation of cellular cortical flow generation to anterior cell cortex in the one-cell embryo dependent process in C.elegans (positive feedback) HOIP_0050206 PMID:20066102 Movement of the sperm MTOC toward the cortex causes a rapid local cessation of focal contractility and an asymmetrical contraction of the remaining actomyosin network, causing a flow of cortical actomyosin toward the opposite (future anterior) pole. PMID:31327978 Contractility in the actomyosin cortex is increased via RhoA activation [18], and a local down-regulation of non-muscle myosin II (NMY-2, referred to as myosin) at the posterior pole [19] initiates cortical flows. PMID:32829680 Posterior-directed cytoplasmic flow and centrosomal MT asters synergize to position the PN/centrosome complex close to the cortex at the posterior pole, ensuring robust polarization of the zygote (figure 1d(ii)). This initiates a mechanochemical-positive feedback loop whereby the signal emanating from the centrosomes promotes actomyosin flow, which maintains centrosome–cortex proximity and strengthens the polarity signal. doi/10.1895/wormbook.1.30.2 The AP embryonic axis is put in place during the first cell cycle and this process can be decomposed into three principal steps: symmetry breaking, establishment of AP polarity, and maintenance of this polarity. HOIP:HOIP_0050207 Any process in which a centrosome is maintained in a specific location within a cell and prevented from moving elsewhere. PMID:32829680 maintenance of centrosome location in cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050207 PMID:32829680 Posterior-directed cytoplasmic flow and centrosomal MT asters synergize to position the PN/centrosome complex close to the cortex at the posterior pole, ensuring robust polarization of the zygote (figure 1d(ii)). This initiates a mechanochemical-positive feedback loop whereby the signal emanating from the centrosomes promotes actomyosin flow, which maintains centrosome–cortex proximity and strengthens the polarity signal. HOIP:HOIP_0050209 PAR6-aPKC stabilization t membrane is a subtype of keeping structure: A process that maintains the membrane association of PAR6-aPKC in the anterior domain. In the anterior domain, CDC-42 and PAR-3 are required for stable membrane association of the PAR-6/aPKC heterodimer. PAR-3 can form clusters that recruit PAR-6/aPKC, which can switch between PAR-3- and CDC-42-dependent states. PAR6-aPKC stabilization in the one-cell embryo dependent process in C.elegans HOIP_0050209 HOIP:HOIP_0050210 A protein complex that is required for the establishment of a cell polarity axis during the cell division cycle. It contains a PAR6 protein and an atypical PKC in worm. PAR6/aPKC PAR6-aPKC heterodimer HOIP_0050210 HOIP:HOIP_0050211 PAR6-aPKC stabilization at membrane is a subtype of keeping structure: A process that maintains the membrane association of PAR6-aPKC in the anterior domain. In the anterior domain, CDC-42 and PAR-3 are required for stable membrane association of the PAR-6/aPKC heterodimer. PAR-3 can form clusters that recruit PAR-6/aPKC, which can switch between PAR-3- and CDC-42-dependent states. PAR6-aPKC stabilization at membrane HOIP_0050211 HOIP:HOIP_0050212 Any process that stops, prevents, or reduces the frequency, rate or extent of anterior PARs (aPARs) localization to posterior cortex. negative regulation of anterior PARs (aPARs) localization to posterior cell cortex HOIP_0050212 HOIP:HOIP_0050215 Any process that stops, prevents or reduces the frequency, rate or extent of localization. negative regulation of protein localization HOIP_0050215 HOIP:HOIP_0050217 The aggregation, arrangement and bonding together of a set of components to form a PAR1-PAR2 complex. PAR1-PAR2 complex formation PAR1-PAR2 complex assembly HOIP_0050217 HOIP:HOIP_0050218 A complex that is required for the establishment of a cell polarity axis. It contains a PAR1 protein and PAR2 protein. PAR1/PAR2 aPAR complex PAR1-PAR2 complex HOIP_0050218 HOIP:HOIP_0050219 Any process that stops, prevents, or reduces the frequency, rate or extent of posterior PARs (pPARs) localization to anterior cortex. negative regulation of posterior PARs (pPARs) localization to anterior cell cortex HOIP_0050219 HOIP:HOIP_0050220 The process in which PAR-2 is released from the anterior cell cortex. PMID:21983565 PMID:32829680 dissociation of PAR2 from anterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050220 PMID:21983565 Using a protein-lipid binding assay, we found that PAR-2 interacts with phospholipids including phosphoinositides (Fig. 2e,f and Supplementary Fig. S7). Phosphorylation by aPKC, or phosphomimetic mutations in the PKC-3 sites, interfered with PAR-2 binding to lipids (Fig. 2e,f and Supplementary Fig. S7), as they interfere with PAR-2 cortical localization in vivo. PMID:32829680 The posterior PARs can be phosphorylated by aPKC, which drives their dissociation from the membrane, and similarly, the PAR-1 kinase, recruited by membrane-associated PAR-2, removes cortical aPARs via phosphorylation of PAR-3 (figure 1a). HOIP:HOIP_0050221 The process in which PAR-2 is released from the cell cortex. dissociation of PAR2 from cell cortex HOIP_0050221 HOIP:HOIP_0050222 Any process that activates or increases the frequency, rate or extent of the binding of PAR2 to membrane phospholipids . PMID:32829680 positive regulation of binding of PAR2 to membrane phospholipid in the one-cell embryo dependent process in C.elegans HOIP_0050222 PMID:32829680 The posterior PARs can be phosphorylated by aPKC, which drives their dissociation from the membrane, and similarly, the PAR-1 kinase, recruited by membrane-associated PAR-2, removes cortical aPARs via phosphorylation of PAR-3 (figure 1a). HOIP:HOIP_0050223 Cell cortex contraction is a subtype of contraction: A process that generates the directed movement in which the cell cortex decreases in volume. cell cortex contaction HOIP_0050223 HOIP:HOIP_0050224 aPKC kinase acculumation is a subtype of protein accumulation: A process that keeps aPKC kinas in an object. aPKC kinase accumulation HOIP_0050224 HOIP:HOIP_0050225 Any process that modulates the frequency, rate or extent of specification of axis polarity. regulation of specification of axis polarity HOIP_0050225 HOIP:HOIP_0050228 Any process that activates or increases the frequency, rate or extent of cellular cortical flow generation PMID:20066102 PMID:31327978 PMID:32829680 positive regulation of cellular cortical flow generation HOIP_0050228 PMID:20066102 Movement of the sperm MTOC toward the cortex causes a rapid local cessation of focal contractility and an asymmetrical contraction of the remaining actomyosin network, causing a flow of cortical actomyosin toward the opposite (future anterior) pole. PMID:31327978 Contractility in the actomyosin cortex is increased via RhoA activation [18], and a local down-regulation of non-muscle myosin II (NMY-2, referred to as myosin) at the posterior pole [19] initiates cortical flows. PMID:32829680 Posterior-directed cytoplasmic flow and centrosomal MT asters synergize to position the PN/centrosome complex close to the cortex at the posterior pole, ensuring robust polarization of the zygote (figure 1d(ii)). This initiates a mechanochemical-positive feedback loop whereby the signal emanating from the centrosomes promotes actomyosin flow, which maintains centrosome–cortex proximity and strengthens the polarity signal. HOIP:HOIP_0050229 Any process that activates or increases the frequency, rate or extent of the binding to menrane phospholipids. positive regulation of membrane phospholipid binding process HOIP_0050229 HOIP:HOIP_0050230 A protein that is a translation product of the ect-2 gene in worm. UniProtKB: Q9U364 Wormbase:WBGene00002297 etc-2 ECT2 (worm) HOIP_0050230 Wormbase:WBGene00002297 etc-2 http://www.wormbase.org/species/c_elegans/gene/WBGene00004357 HOIP:HOIP_0050232 A process that stops, prevents, or reduces the frequency, rate or extent of cellular cortex localization mutually between anterior PARs and posterior PARs, resulting in the establishment or maintenance of each specific localization in the cell cortex. mutual negative regulation of localization to cell cortex between aPARs and pPARs HOIP_0050232 HOIP:HOIP_0050233 PAR1 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into PAR1. PMID:21983565 PMID:32829680 PAR1 phosphorylation in the one-cell embryo dependent process in C.elegans HOIP_0050233 PMID:21983565 Before polarization, cortical aPKC excludes PAR-1 kinase and its binding partner PAR-2 by phosphorylation. During symmetry breaking, microtubules nucleated by the centrosome locally protect PAR-2 from phosphorylation by aPKC, allowing PAR-2 and PAR-1 to access the cortex nearest the centrosome. PMID:32829680 The posterior PARs can be phosphorylated by aPKC, which drives their dissociation from the membrane, and similarly, the PAR-1 kinase, recruited by membrane-associated PAR-2, removes cortical aPARs via phosphorylation of PAR-3 (figure 1a). HOIP:HOIP_0050234 PAR1 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into PAR1. PAR1 phosphorylation HOIP_0050234 HOIP:HOIP_0050235 The process in which PAR-2 is released from the anterior cell cortex. dissociation of PAR1 from anterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050235 HOIP:HOIP_0050236 The process in which PAR-2 is released from the cell cortex. dissociation of PAR1 from cell cortex HOIP_0050236 HOIP:HOIP_0050237 A process in which a PAR1 is transported to, or maintained in, the posterior cell cortex. PAR1 localization to poterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050237 HOIP:HOIP_0050238 A process in which a PAR protein transported to, or maintained in, the cell cortex. PAR localization to cell cortex HOIP_0050238 HOIP:HOIP_0050239 The directed movement of the male pronucleus-centrosome complex to a specific location to the the posterior cell. PMID:31327978 PMID:32829680 male pronucleus-centrosome complex localization HOIP_0050239 PMID:32829680 Posterior-directed cytoplasmic flow and centrosomal MT asters synergize to position the PN/centrosome complex close to the cortex at the posterior pole, ensuring robust polarization of the zygote (figure 1d(ii)). HOIP:HOIP_0050243 Changing positional polarity is a subtype of changing quality: A process that changes the positional polarity of the object. changing positional polarity HOIP_0050243 HOIP:HOIP_0050244 Asymmetric cell division in the one-cell embryo dependent process in C. elegans is a subtype of course dependent process: A process that can constitute the course of assymmetric cell division in the one-cell embryo in C.elegans. doi/10.1895/wormbook.1.30.2 asymmetric cell division in the early embryo dependent process in C. elegans HOIP_0050244 doi/10.1895/wormbook.1.30.2 Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook) http://www.wormbook.org. HOIP:HOIP_0050245 A process in which posterior PARs (pPARs) are transported to, or maintained in, the posterior cell cortex. posterior PARs (pPARs) localization to posterior cortex in the one-cell embryo dependent process in C.elegans. HOIP_0050245 HOIP:HOIP_0050246 A process in which anterior PARs (aPARs) are transported to, or maintained in, the anterior cell cortex. doi/10.1895/wormbook.1.30.2 anterior PARs (aPARs) localization to anterior cortex in the one-cell embryo dependent process in C.elegans. HOIP_0050246 doi/10.1895/wormbook.1.30.2 The anterior PAR complex marked by GFP::PAR-6 is present throughout the cortex initially, but recedes from the posterior following symmetry breaking, concomitant with the anteriorly-directed movement of the contractile cortex (Munro et al., 2004; Cuenca et al., 2003). Conversely, GFP::PAR-2 is first detected on the posterior cortex shortly after the local cessation of cortical contractions and then expands anteriorly to approximately 50% egg-length (Movie 2) (Bienkowska and Cowan, 2012; Cuenca et al., 2003). HOIP:HOIP_0050247 A process that stops, prevents, or reduces the frequency, rate or extent of PAR2 phosphorylation. PMID:21983565 doi/10.1895/wormbook.1.30.2 negative regulation of PAR2 phosphorylation in the one-cell embryo dependent process in C.elegans HOIP_0050247 PMID:21983565 Before polarization, cortical aPKC excludes PAR-1 kinase and its binding partner PAR-2 by phosphorylation. During symmetry breaking, microtubules nucleated by the centrosome locally protect PAR-2 from phosphorylation by aPKC, allowing PAR-2 and PAR-1 to access the cortex nearest the centrosome. doi/10.1895/wormbook.1.30.2 Live imaging revealed that PAR-2 associates with centrosomes, whereas biochemical experiments established that PAR-2 is a microtubule binding protein (Motegi et al., 2011). Interestingly, microtubule association protects PAR-2 from phosphorylation by PKC-3 in vitro. Thus, in vivo, association of PAR-2 with microtubules emanating from the centrosomes at the posterior would prevent the action of PKC-3, which would otherwise inhibit PAR-2 cortical localization (Motegi et al., 2011). HOIP:HOIP_0050248 A process that stops, prevents, or reduces the frequency, rate or extent of PAR phosphorylation. PMID:21983565 doi/10.1895/wormbook.1.30.2 negative regulation of PAR phosphorylation HOIP_0050248 PMID:21983565 Before polarization, cortical aPKC excludes PAR-1 kinase and its binding partner PAR-2 by phosphorylation. During symmetry breaking, microtubules nucleated by the centrosome locally protect PAR-2 from phosphorylation by aPKC, allowing PAR-2 and PAR-1 to access the cortex nearest the centrosome. doi/10.1895/wormbook.1.30.2 Live imaging revealed that PAR-2 associates with centrosomes, whereas biochemical experiments established that PAR-2 is a microtubule binding protein (Motegi et al., 2011). Interestingly, microtubule association protects PAR-2 from phosphorylation by PKC-3 in vitro. Thus, in vivo, association of PAR-2 with microtubules emanating from the centrosomes at the posterior would prevent the action of PKC-3, which would otherwise inhibit PAR-2 cortical localization (Motegi et al., 2011). HOIP:HOIP_0050249 PAR phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into PAR. PAR phosphorylation HOIP_0050249 HOIP:HOIP_0050250 The process in which ECT is released from the posterior cell cortex. PMID:31636075 dissociation of ECT2 from posterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050250 PMID:31636075 Notably, ECT-2 is excluded from the posterior cortex at the onset of symmetry breaking, and this event is correlated with the disappearance of the non-muscle myosin II (NMY-2) from the posterior cortex (Munro et al., 2004; Motegi and Sugimoto, 2006). A Rho GEF, ECT-2, acts downstream of AIR-1 in regulating contractility and PAR-2 localisation, and, notably, AIR-1 depletion influences ECT-2 cortical localisation. HOIP:HOIP_0050251 The process in which ECT is released from the posterior cell cortex. PMID:31636075 dissociation of ECT from posterior cell cortex HOIP_0050251 PMID:31636075 Notably, ECT-2 is excluded from the posterior cortex at the onset of symmetry breaking, and this event is correlated with the disappearance of the non-muscle myosin II (NMY-2) from the posterior cortex (Munro et al., 2004; Motegi and Sugimoto, 2006). A Rho GEF, ECT-2, acts downstream of AIR-1 in regulating contractility and PAR-2 localisation, and, notably, AIR-1 depletion influences ECT-2 cortical localisation. HOIP:HOIP_0050253 A protein that is a translation product of the CHN-1 gene in worm. Predicted to enable GTPase activator activity. Involved in protein localization and regulation of GTPase activity. Located in cell cortex. Human ortholog(s) of this gene implicated in Duane retraction syndrome. Is an ortholog of human CHN1 (chimerin 1). Predicted to enable GTPase activator activity. Involved in protein localization and regulation of GTPase activity. Located in cell cortex. Human ortholog(s) of this gene implicated in Duane retraction syndrome. Is an ortholog of human CHN1 (chimerin 1). PMID:19923324 UniprotKB:Q965N4 CHImaeriN (Rac-GTPase-activating protein) homolog (worm) CHN1 (worm) HOIP_0050253 Predicted to enable GTPase activator activity. Involved in protein localization and regulation of GTPase activity. Located in cell cortex. Human ortholog(s) of this gene implicated in Duane retraction syndrome. Is an ortholog of human CHN1 (chimerin 1). https://wormbase.org/species/c_elegans/gene/WBGene00015267 HOIP:HOIP_0050254 A process that changes the activity of the CDC42 to be lower. PMID:19923324 PMID:23536568 PMID:28974638 doi/10.1895/wormbook.1.30.2 CDC42 inactivation in the one-cell embryo dependent process in C.elegans HOIP_0050254 PMID:28974638 Analysis of a biosensor for CDC-42 activity suggests that active CDC-42 is enriched at the posterior pole during polarity establishment and at the anterior pole during polarity maintenance (Kumfer et al., 2010; Sailer et al., 2015). CDC-42 activation requires the GEF cGEF-1, which is uniformly enriched at the cortex of zygotes (Chan and Nance, 2013; Kumfer et al., 2010), while spatial restriction of CDC-42 activity during maintenance phase depends on its local inhibition by CHIN-1 (Beatty et al., 2013; Kumfer et al., 2010; Sailer et al., 2015) (see below). The mechanism(s) that localize CDC-42 activity during polarity establishment remain unclear. During polarity maintenance, actomyosin contractility is primarily controlled by CDC-42 through MRCK-1 (Kumfer et al., 2010). Anterior restriction of CDC-42 activity by CHIN-1 biases Myosin II activation at the anterior cortex. In addition, PAR-2 (and possibly LGL-1) act downstream of CDC-42 to inhibit posterior accumulation and/or activation of Myosin II (Beatty et al., 2010; Munro et al., 2004; Sailer et al., 2015). PAR-3/PAR-6/PKC-3 indirectly promote anterior contractility by locally inhibiting PAR-2 and CHIN-1 accumulation as discussed above (Beatty et al., 2010; Munro et al., 2004; Sailer et al., 2015). Whether they also act more directly to promote contractility during polarity maintenance remains unclear (Beatty et al., 2013; Zonies et al., 2010). doi/10.1895/wormbook.1.30.2 A targeted RNAi screen amongst potential GEFs and GAPs using this reporter led to the identification of the GEF CGEF-1 and the GAP CHIN-1 as regulators of CDC-42 activity (Kumfer et al., 2010). CGEF-1 depletion results in lower cortical CDC-42 GTP throughout the cell cycle, whereas CHIN-1 depletion affects CDC-42 activity specifically when GFP::GBDWSP-1 is normally present on the anterior cortex. Compatible with antagonistic influences on cortical CDC-42, CGEF-1 depletion leads to reduction of the domain occupied by cortical PAR-6, whereas CHIN-1 depletion leads to an increase in this domain (Beatty et al., 2013). Embryos lacking both PAR-2 and LGL-1 function still exhibit polarized CDC-42 GTP distribution in a CGEF-1- and CHIN-1-dependent manner. Together with other supporting evidence, these results suggests that CHIN-1 and CGEF-1 are part of a third pathway that acts in parallel to the principal PAR-2-dependent pathway and the redundant LGL-1-dependent pathway for polarity maintenance (Beatty et al., 2013) HOIP:HOIP_0050255 A process that changes the activity of the LGL1 to be lower. PMID:28974638 doi/10.1895/wormbook.1.30.2 LGL1 inactivation in the one-cell embryo dependent process in C.elegans HOIP_0050255 PMID:28974638 One of these signals, still poorly defined, acts locally to inhibit RhoA-dependent cortical actomyosin contractility (Motegi and Sugimoto, 2006; Munro et al., 2004). This creates a spatial gradient of contractility and anterior-directed cortical flows that segregate PAR-3, PAR-6 and PKC-3 towards the anterior pole, allowing PAR-1, PAR-2 and LGL-1 to accumulate on the posterior cortex (Cheeks et al., 2004; Goehring et al., 2011b; Mayer et al., 2010; Munro et al., 2004). Phosphorylation of PAR-1, PAR-2 and LGL-1 by PKC-3 is both necessary and sufficient to prevent them from binding to the anterior cortex (Hao et al., 2006; Hoege et al., 2010; Motegi et al., 2011). doi/10.1895/wormbook.1.30.2 Apart from the actomyosin network and the PAR proteins, other components participate in generating AP polarity in the one-cell embryo. This includes LGL-1, the worm homologue of the Drosophila tumor-suppressor protein Lethal Giant Larvae, which functions redundantly with PAR-2 during polarity maintenance (Beatty et al., 2010; Hoege et al., 2010). LGL-1 is enriched on the posterior cortex, and its depletion, while not resulting in a phenotype on its own, affects the distribution of cortical NMY-2 and enhances the lethality incurred from partial PAR-2 inactivation. Conversely, increasing LGL-1 levels alleviates aspects of the par-2(RNAi) phenotype. Therefore, LGL-1 can be thought of as defining a second pathway that contributes to polarity establishment in the absence of PAR-2. What restricts LGL-1 cortical distribution to the posterior? Phosphorylation by PKC-3 is key here as well. Mutating three PKC-3 predicted phosphorylation sites to non-phosphorylatable residues leads to uniform cortical distribution of GFP::LGL-1, whereas the converse phosphomimetic variant does not localize (Hoege et al., 2010) or localizes less well (Beatty et al., 2010) to the cell cortex. These and other observations suggest that a PAR-6/PAR-3/LGL-1 complex forms initially, but that PKC-3-mediated phosphorylation of LGL-1 prevents its localization on the anterior side during the course of polarity establishment (Beatty et al., 2010; Hoege et al., 2010). HOIP:HOIP_0050256 A process that changes the activity of the CDC42 to be lower. PMID:19923324 PMID:23536568 PMID:28974638 doi/10.1895/wormbook.1.30.2 CDC42 inactivation HOIP_0050256 PMID:28974638 Analysis of a biosensor for CDC-42 activity suggests that active CDC-42 is enriched at the posterior pole during polarity establishment and at the anterior pole during polarity maintenance (Kumfer et al., 2010; Sailer et al., 2015). CDC-42 activation requires the GEF cGEF-1, which is uniformly enriched at the cortex of zygotes (Chan and Nance, 2013; Kumfer et al., 2010), while spatial restriction of CDC-42 activity during maintenance phase depends on its local inhibition by CHIN-1 (Beatty et al., 2013; Kumfer et al., 2010; Sailer et al., 2015) (see below). The mechanism(s) that localize CDC-42 activity during polarity establishment remain unclear. During polarity maintenance, actomyosin contractility is primarily controlled by CDC-42 through MRCK-1 (Kumfer et al., 2010). Anterior restriction of CDC-42 activity by CHIN-1 biases Myosin II activation at the anterior cortex. In addition, PAR-2 (and possibly LGL-1) act downstream of CDC-42 to inhibit posterior accumulation and/or activation of Myosin II (Beatty et al., 2010; Munro et al., 2004; Sailer et al., 2015). PAR-3/PAR-6/PKC-3 indirectly promote anterior contractility by locally inhibiting PAR-2 and CHIN-1 accumulation as discussed above (Beatty et al., 2010; Munro et al., 2004; Sailer et al., 2015). Whether they also act more directly to promote contractility during polarity maintenance remains unclear (Beatty et al., 2013; Zonies et al., 2010). doi/10.1895/wormbook.1.30.2 A targeted RNAi screen amongst potential GEFs and GAPs using this reporter led to the identification of the GEF CGEF-1 and the GAP CHIN-1 as regulators of CDC-42 activity (Kumfer et al., 2010). CGEF-1 depletion results in lower cortical CDC-42 GTP throughout the cell cycle, whereas CHIN-1 depletion affects CDC-42 activity specifically when GFP::GBDWSP-1 is normally present on the anterior cortex. Compatible with antagonistic influences on cortical CDC-42, CGEF-1 depletion leads to reduction of the domain occupied by cortical PAR-6, whereas CHIN-1 depletion leads to an increase in this domain (Beatty et al., 2013). Embryos lacking both PAR-2 and LGL-1 function still exhibit polarized CDC-42 GTP distribution in a CGEF-1- and CHIN-1-dependent manner. Together with other supporting evidence, these results suggests that CHIN-1 and CGEF-1 are part of a third pathway that acts in parallel to the principal PAR-2-dependent pathway and the redundant LGL-1-dependent pathway for polarity maintenance (Beatty et al., 2013) HOIP:HOIP_0050257 A process that changes the activity of the LGL1 to be lower. PMID:19923324 PMID:23536568 PMID:28974638 doi/10.1895/wormbook.1.30.2 LGL1 inactivation HOIP_0050257 PMID:28974638 Analysis of a biosensor for CDC-42 activity suggests that active CDC-42 is enriched at the posterior pole during polarity establishment and at the anterior pole during polarity maintenance (Kumfer et al., 2010; Sailer et al., 2015). CDC-42 activation requires the GEF cGEF-1, which is uniformly enriched at the cortex of zygotes (Chan and Nance, 2013; Kumfer et al., 2010), while spatial restriction of CDC-42 activity during maintenance phase depends on its local inhibition by CHIN-1 (Beatty et al., 2013; Kumfer et al., 2010; Sailer et al., 2015) (see below). The mechanism(s) that localize CDC-42 activity during polarity establishment remain unclear. During polarity maintenance, actomyosin contractility is primarily controlled by CDC-42 through MRCK-1 (Kumfer et al., 2010). Anterior restriction of CDC-42 activity by CHIN-1 biases Myosin II activation at the anterior cortex. In addition, PAR-2 (and possibly LGL-1) act downstream of CDC-42 to inhibit posterior accumulation and/or activation of Myosin II (Beatty et al., 2010; Munro et al., 2004; Sailer et al., 2015). PAR-3/PAR-6/PKC-3 indirectly promote anterior contractility by locally inhibiting PAR-2 and CHIN-1 accumulation as discussed above (Beatty et al., 2010; Munro et al., 2004; Sailer et al., 2015). Whether they also act more directly to promote contractility during polarity maintenance remains unclear (Beatty et al., 2013; Zonies et al., 2010). doi/10.1895/wormbook.1.30.2 A targeted RNAi screen amongst potential GEFs and GAPs using this reporter led to the identification of the GEF CGEF-1 and the GAP CHIN-1 as regulators of CDC-42 activity (Kumfer et al., 2010). CGEF-1 depletion results in lower cortical CDC-42 GTP throughout the cell cycle, whereas CHIN-1 depletion affects CDC-42 activity specifically when GFP::GBDWSP-1 is normally present on the anterior cortex. Compatible with antagonistic influences on cortical CDC-42, CGEF-1 depletion leads to reduction of the domain occupied by cortical PAR-6, whereas CHIN-1 depletion leads to an increase in this domain (Beatty et al., 2013). Embryos lacking both PAR-2 and LGL-1 function still exhibit polarized CDC-42 GTP distribution in a CGEF-1- and CHIN-1-dependent manner. Together with other supporting evidence, these results suggests that CHIN-1 and CGEF-1 are part of a third pathway that acts in parallel to the principal PAR-2-dependent pathway and the redundant LGL-1-dependent pathway for polarity maintenance (Beatty et al., 2013) HOIP:HOIP_0050258 A process that changes the activity of the LGL1 to be lower. PMID:28974638 doi/10.1895/wormbook.1.30.2 LGL1 phosphorylation in the one-cell embryo dependent process in C.elegans HOIP_0050258 PMID:28974638 Phosphorylation of PAR-1, PAR-2 and LGL-1 by PKC-3 is both necessary and sufficient to prevent them from binding to the anterior cortex (Hao et al., 2006; Hoege et al., 2010; Motegi et al., 2011). doi/10.1895/wormbook.1.30.2 Apart from the actomyosin network and the PAR proteins, other components participate in generating AP polarity in the one-cell embryo. This includes LGL-1, the worm homologue of the Drosophila tumor-suppressor protein Lethal Giant Larvae, which functions redundantly with PAR-2 during polarity maintenance (Beatty et al., 2010; Hoege et al., 2010). LGL-1 is enriched on the posterior cortex, and its depletion, while not resulting in a phenotype on its own, affects the distribution of cortical NMY-2 and enhances the lethality incurred from partial PAR-2 inactivation. Conversely, increasing LGL-1 levels alleviates aspects of the par-2(RNAi) phenotype. Therefore, LGL-1 can be thought of as defining a second pathway that contributes to polarity establishment in the absence of PAR-2. What restricts LGL-1 cortical distribution to the posterior? Phosphorylation by PKC-3 is key here as well. Mutating three PKC-3 predicted phosphorylation sites to non-phosphorylatable residues leads to uniform cortical distribution of GFP::LGL-1, whereas the converse phosphomimetic variant does not localize (Hoege et al., 2010) or localizes less well (Beatty et al., 2010) to the cell cortex. These and other observations suggest that a PAR-6/PAR-3/LGL-1 complex forms initially, but that PKC-3-mediated phosphorylation of LGL-1 prevents its localization on the anterior side during the course of polarity establishment (Beatty et al., 2010; Hoege et al., 2010). HOIP:HOIP_0050259 A process that changes the activity of the LGL1 to be lower. PMID:28974638 doi/10.1895/wormbook.1.30.2 LGL1 phosphorylation HOIP_0050259 PMID:28974638 Phosphorylation of PAR-1, PAR-2 and LGL-1 by PKC-3 is both necessary and sufficient to prevent them from binding to the anterior cortex (Hao et al., 2006; Hoege et al., 2010; Motegi et al., 2011). doi/10.1895/wormbook.1.30.2 Apart from the actomyosin network and the PAR proteins, other components participate in generating AP polarity in the one-cell embryo. This includes LGL-1, the worm homologue of the Drosophila tumor-suppressor protein Lethal Giant Larvae, which functions redundantly with PAR-2 during polarity maintenance (Beatty et al., 2010; Hoege et al., 2010). LGL-1 is enriched on the posterior cortex, and its depletion, while not resulting in a phenotype on its own, affects the distribution of cortical NMY-2 and enhances the lethality incurred from partial PAR-2 inactivation. Conversely, increasing LGL-1 levels alleviates aspects of the par-2(RNAi) phenotype. Therefore, LGL-1 can be thought of as defining a second pathway that contributes to polarity establishment in the absence of PAR-2. What restricts LGL-1 cortical distribution to the posterior? Phosphorylation by PKC-3 is key here as well. Mutating three PKC-3 predicted phosphorylation sites to non-phosphorylatable residues leads to uniform cortical distribution of GFP::LGL-1, whereas the converse phosphomimetic variant does not localize (Hoege et al., 2010) or localizes less well (Beatty et al., 2010) to the cell cortex. These and other observations suggest that a PAR-6/PAR-3/LGL-1 complex forms initially, but that PKC-3-mediated phosphorylation of LGL-1 prevents its localization on the anterior side during the course of polarity establishment (Beatty et al., 2010; Hoege et al., 2010). HOIP:HOIP_0050276 MEX5 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into MEX5. MEX5 phosphorylation HOIP_0050276 HOIP:HOIP_0050277 MEX5 phosphorylation is a subtype of phosphorylation: A process that The process of introducing a phosphate group into MEX5. doi/10.1895/wormbook.1.30.2 MEX5 phosphorylation in the one-cell embryo dependent process in C.elegans HOIP_0050277 doi/10.1895/wormbook.1.30.2 MEX-5 is localized at higher levels in the anterior cytoplasm by the end of the one-cell stage, and thus is inherited primarily by the AB daughter cell upon division (Figure 5A, B) (Cuenca et al., 2003; Schubert et al., 2000). Several sites in MEX-5 are phosphorylated in vivo in a PAR-4- and PAR-1-dependent manner and are needed for normal MEX-5 asymmetry and function (Griffin et al., 2011; Tenlen et al., 2008). PAR-1 is likely to be the direct regulator of MEX-5 asymmetry. Phosphorylation by a gradient of cytoplasmic PAR-1 promotes the release of MEX-5 from RNA-containing complexes in the posterior (Griffin et al., 2011). The resulting increased mobility of MEX-5 allows it to diffuse to the anterior where the lower levels of PAR-1 are insufficient to counteract dephosphorylation of MEX-5 by PP2A. Dephosphorylated MEX-5 associates with RNP complexes and cannot redistribute into the posterior as readily, generating a stable anterior to posterior gradient of MEX-5. HOIP:HOIP_0050278 MEX5 dephosphorylation is a subtype of dephosphorylation: removing one or more phosphoric (ester or anhydride) residues from MEX5. MEX5 dephosphorylation HOIP_0050278 HOIP:HOIP_0050279 MEX5 dephosphorylation is a subtype of dephosphorylation: removing one or more phosphoric (ester or anhydride) residues from MEX5. doi/10.1895/wormbook.1.30.2 MEX5 dephosphorylation in the one-cell embryo dependent process in C.elegans HOIP_0050279 doi/10.1895/wormbook.1.30.2 MEX-5 is localized at higher levels in the anterior cytoplasm by the end of the one-cell stage, and thus is inherited primarily by the AB daughter cell upon division (Figure 5A, B) (Cuenca et al., 2003; Schubert et al., 2000). Several sites in MEX-5 are phosphorylated in vivo in a PAR-4- and PAR-1-dependent manner and are needed for normal MEX-5 asymmetry and function (Griffin et al., 2011; Tenlen et al., 2008). PAR-1 is likely to be the direct regulator of MEX-5 asymmetry. Phosphorylation by a gradient of cytoplasmic PAR-1 promotes the release of MEX-5 from RNA-containing complexes in the posterior (Griffin et al., 2011). The resulting increased mobility of MEX-5 allows it to diffuse to the anterior where the lower levels of PAR-1 are insufficient to counteract dephosphorylation of MEX-5 by PP2A. Dephosphorylated MEX-5 associates with RNP complexes and cannot redistribute into the posterior as readily, generating a stable anterior to posterior gradient of MEX-5. HOIP:HOIP_0050280 A protein that is a translation product of the mex-3 gene in worm. Enables single-stranded RNA binding activity. Involved in several processes, including negative regulation of muscle cell differentiation; organelle inheritance; and regulation of gene expression. Located in P granule. Expressed in distal tip cell and embryonic cell. Is an ortholog of human MEX3A (mex-3 RNA binding family member A). Enables single-stranded RNA binding activity. Involved in several processes, including negative regulation of muscle cell differentiation; organelle inheritance; and regulation of gene expression. Located in P granule. Expressed in distal tip cell and embryonic cell. Is an ortholog of human MEX3A (mex-3 RNA binding family member A). mex-3 encodes two KH domain-containing RNA binding proteins; in the early embryo, maternally provided MEX-3 is required for specifying the identities of the anterior AB blastomere and its descendants, as well as for the identity of the P3 blastomere and proper segregation of the germline P granules; mex-3 mRNA is distributed uniformly in the syncytial core of the adult distal gonad, mature oocytes, and early 1-cell stage embryos, but then becomes more prominent in the AB blastomere and its daughters by the 4-cell stage after which it is rapidly degraded save for the D and P4 blastomeres; MEX-3 protein is also detected uniformly in the cytoplasm of oocytes and 1-cell stage embryos, but like the mRNA, becomes more abundant in AB and its daughters at the 2- and 4-cell stages, respectively, before disappearing; MEX-3 is also detected in association with P granules from the 2-cell stage until the late stages of embryogenesis. mex-3 encodes two KH domain-containing RNA binding proteins; in the early embryo, maternally provided MEX-3 is required for specifying the identities of the anterior AB blastomere and its descendants, as well as for the identity of the P3 blastomere and proper segregation of the germline P granules; mex-3 mRNA is distributed uniformly in the syncytial core of the adult distal gonad, mature oocytes, and early 1-cell stage embryos, but then becomes more prominent in the AB blastomere and its daughters by the 4-cell stage after which it is rapidly degraded save for the D and P4 blastomeres; MEX-3 protein is also detected uniformly in the cytoplasm of oocytes and 1-cell stage embryos, but like the mRNA, becomes more abundant in AB and its daughters at the 2- and 4-cell stages, respectively, before disappearing; MEX-3 is also detected in association with P granules from the 2-cell stage until the late stages of embryogenesis. PMID:25445286 UniProtKB:H2L067 https://wormbase.org/species/c_elegans/gene/WBGene00003229 mex-3 (worm) MEX3 (worm) HOIP_0050280 Enables single-stranded RNA binding activity. Involved in several processes, including negative regulation of muscle cell differentiation; organelle inheritance; and regulation of gene expression. Located in P granule. Expressed in distal tip cell and embryonic cell. Is an ortholog of human MEX3A (mex-3 RNA binding family member A). https://wormbase.org/species/c_elegans/gene/WBGene00003229 mex-3 encodes two KH domain-containing RNA binding proteins; in the early embryo, maternally provided MEX-3 is required for specifying the identities of the anterior AB blastomere and its descendants, as well as for the identity of the P3 blastomere and proper segregation of the germline P granules; mex-3 mRNA is distributed uniformly in the syncytial core of the adult distal gonad, mature oocytes, and early 1-cell stage embryos, but then becomes more prominent in the AB blastomere and its daughters by the 4-cell stage after which it is rapidly degraded save for the D and P4 blastomeres; MEX-3 protein is also detected uniformly in the cytoplasm of oocytes and 1-cell stage embryos, but like the mRNA, becomes more abundant in AB and its daughters at the 2- and 4-cell stages, respectively, before disappearing; MEX-3 is also detected in association with P granules from the 2-cell stage until the late stages of embryogenesis. https://wormbase.org/species/c_elegans/gene/WBGene00003229 HOIP:HOIP_0050281 A protein that is a translation product of the pos-1 gene in worm. Enables mRNA 3'-UTR binding activity; poly(U) RNA binding activity; and transcription corepressor activity. Involved in several processes, including cell fate specification; embryonic pattern specification; and negative regulation of transcription by RNA polymerase II. Located in P granule. Expressed in several structures, including Psub4; germ line; neurons; oocyte; and rectal gland cell. Is an ortholog of human ZFP36 (ZFP36 ring finger protein); ZFP36L1 (ZFP36 ring finger protein like 1); and ZFP36L2 (ZFP36 ring finger protein like 2). Enables mRNA 3'-UTR binding activity; poly(U) RNA binding activity; and transcription corepressor activity. Involved in several processes, including cell fate specification; embryonic pattern specification; and negative regulation of transcription by RNA polymerase II. Located in P granule. Expressed in several structures, including Psub4; germ line; neurons; oocyte; and rectal gland cell. Is an ortholog of human ZFP36 (ZFP36 ring finger protein); ZFP36L1 (ZFP36 ring finger protein like 1); and ZFP36L2 (ZFP36 ring finger protein like 2). pos-1 encodes a CCCH-type zinc-finger protein; during embryogenesis, maternally provided POS-1 is essential for proper fate specification of germ cells, intestine, pharynx, and hypodermis; POS-1's role in cell fate specification is likely as a translational regulator, as POS-1 is required, in posterior blastomeres, for positive regulation of apx-1 mRNA translation and negative regulation of glp-1 mRNA translation via direct binding to the spatial control region (SCR) in the glp-1 mRNA 3' UTR; in regulating mRNA translation, POS-1 interacts with SPN-4, an RNP-type RNA binding protein, that may function to negatively regulate POS-1 activity; POS-1 can also bind the mex-6 3'-UTR in vitro, although expression of a MEX-6 reporter fusion protein does not appear to be affected in pos-1 mutant animals; pos-1 mRNA is first detected in the gonads of L4 and adult animals, and is present uniformly in oocytes and newly fertilized embryos; during early embryonic divisions, pos-1 mRNA is present at higher levels in germline blastomeres until it disappears following the division of P4; POS-1 protein is first apparent at low levels in 1-cell embryos, with subsequent expression mirroring that of pos-1 mRNA: high levels in germline blastomeres until its disappearance after the P4 division; in the germline blastomeres P1, P2, P3, and P4, POS-1 colocalizes with cytoplasmic and perinuclear P granules. pos-1 encodes a CCCH-type zinc-finger protein; during embryogenesis, maternally provided POS-1 is essential for proper fate specification of germ cells, intestine, pharynx, and hypodermis; POS-1's role in cell fate specification is likely as a translational regulator, as POS-1 is required, in posterior blastomeres, for positive regulation of apx-1 mRNA translation and negative regulation of glp-1 mRNA translation via direct binding to the spatial control region (SCR) in the glp-1 mRNA 3' UTR; in regulating mRNA translation, POS-1 interacts with SPN-4, an RNP-type RNA binding protein, that may function to negatively regulate POS-1 activity; POS-1 can also bind the mex-6 3'-UTR in vitro, although expression of a MEX-6 reporter fusion protein does not appear to be affected in pos-1 mutant animals; pos-1 mRNA is first detected in the gonads of L4 and adult animals, and is present uniformly in oocytes and newly fertilized embryos; during early embryonic divisions, pos-1 mRNA is present at higher levels in germline blastomeres until it disappears following the division of P4; POS-1 protein is first apparent at low levels in 1-cell embryos, with subsequent expression mirroring that of pos-1 mRNA: high levels in germline blastomeres until its disappearance after the P4 division; in the germline blastomeres P1, P2, P3, and P4, POS-1 colocalizes with cytoplasmic and perinuclear P granules. PMID:29276126 UniProtKB:G5EF15 https://wormbase.org/species/c_elegans/gene/WBGene00004078 pos-1 (worm) POS1 (worm) HOIP_0050281 Enables mRNA 3'-UTR binding activity; poly(U) RNA binding activity; and transcription corepressor activity. Involved in several processes, including cell fate specification; embryonic pattern specification; and negative regulation of transcription by RNA polymerase II. Located in P granule. Expressed in several structures, including Psub4; germ line; neurons; oocyte; and rectal gland cell. Is an ortholog of human ZFP36 (ZFP36 ring finger protein); ZFP36L1 (ZFP36 ring finger protein like 1); and ZFP36L2 (ZFP36 ring finger protein like 2). https://wormbase.org/species/c_elegans/gene/WBGene00004078 pos-1 encodes a CCCH-type zinc-finger protein; during embryogenesis, maternally provided POS-1 is essential for proper fate specification of germ cells, intestine, pharynx, and hypodermis; POS-1's role in cell fate specification is likely as a translational regulator, as POS-1 is required, in posterior blastomeres, for positive regulation of apx-1 mRNA translation and negative regulation of glp-1 mRNA translation via direct binding to the spatial control region (SCR) in the glp-1 mRNA 3' UTR; in regulating mRNA translation, POS-1 interacts with SPN-4, an RNP-type RNA binding protein, that may function to negatively regulate POS-1 activity; POS-1 can also bind the mex-6 3'-UTR in vitro, although expression of a MEX-6 reporter fusion protein does not appear to be affected in pos-1 mutant animals; pos-1 mRNA is first detected in the gonads of L4 and adult animals, and is present uniformly in oocytes and newly fertilized embryos; during early embryonic divisions, pos-1 mRNA is present at higher levels in germline blastomeres until it disappears following the division of P4; POS-1 protein is first apparent at low levels in 1-cell embryos, with subsequent expression mirroring that of pos-1 mRNA: high levels in germline blastomeres until its disappearance after the P4 division; in the germline blastomeres P1, P2, P3, and P4, POS-1 colocalizes with cytoplasmic and perinuclear P granules. https://wormbase.org/species/c_elegans/gene/WBGene00004078 PMID:29276126 During the asymmetric division of the C. elegans zygote, the RNA-binding protein MEX-5 forms an anterior-rich cytoplasmic gradient that causes the RNA-binding protein POS-1 to form an opposing, posterior-rich gradient. We demonstrate that the polo-like kinase PLK-1 mediates the repulsive coupling between MEX-5 and POS-1 by increasing the mobility of POS-1 in the anterior. PLK-1 is enriched in the anterior cytoplasm and phosphorylates POS-1, which is both necessary and sufficient to increase POS-1 mobility. Regulation of POS-1 mobility depends on both the interaction between PLK-1 and MEX-5 and between MEX-5 and RNA, suggesting that MEX-5 may recruit PLK-1 to RNA in the anterior. The low concentration of MEX-5/PLK-1 in the posterior cytoplasm provides a permissive environment for the retention of POS-1, which depends on POS-1 RNA binding. HOIP:HOIP_0050284 A serine/threonine-protein kinase PLK1 that is encoded in the genome of human. HGNC:9077 PLK1 UniProtKB:P53350 PLK-1 (human) Polo-like kinase 1 (human) serine/threonine-protein kinase PLK1 (human) hPLK1 HOIP_0050284 HOIP:HOIP_0050285 Any process that stops, prevents, or reduces the frequency, rate or extent of MEX5 localization to posterior cell. negative regulation of MEX5 localization to posterior cell in the one-cell embryo dependent process in C.elegans HOIP_0050285 HOIP:HOIP_0050286 Any process that stops, prevents or reduces the frequency, rate or extent of cellular protein localization to posterior cell. negative reuglation of cellular protein localization to posterior cell HOIP_0050286 HOIP:HOIP_0050287 Any process that stops, prevents, or reduces the frequency, rate or extent of MEX5/6 localization to posterior cell. negative regulation of MEX5/6 localization to posterior cell HOIP_0050287 HOIP:HOIP_0050288 A process in which MEX5 is transported to, or maintained in, the anterior cell. PMID:20627961 doi/10.1895/wormbook.1.30.2 MEX5 localization to anterior cell in the one-cell embryo dependent process in C.elegans HOIP_0050288 doi/10.1895/wormbook.1.30.2 MEX-5 is localized at higher levels in the anterior cytoplasm by the end of the one-cell stage, and thus is inherited primarily by the AB daughter cell upon division (Figure 5A, B) (Cuenca et al., 2003; Schubert et al., 2000). Analysis of the dynamics of GFP::MEX-5 fusions gave no evidence for directed transport to the anterior, but revealed that the cytoplasmic mobility of MEX-5 is faster in the posterior compared to the anterior (Daniels et al., 2010; Tenlen et al., 2008). Examination of a photoconvertible Dendra::MEX-5 fusion, which allows proteins to be marked and then monitored over time, yielded similar results and further showed that neither degradation nor synthesis promotes MEX-5 asymmetry (Griffin et al., 2011). Several sites in MEX-5 are phosphorylated in vivo in a PAR-4- and PAR-1-dependent manner and are needed for normal MEX-5 asymmetry and function (Griffin et al., 2011; Tenlen et al., 2008). PAR-1 is likely to be the direct regulator of MEX-5 asymmetry. HOIP:HOIP_0050289 A process in which MEX6 is transported to, or maintained in, the anterior cell. MEX6 localization to anterior cell in the one-cell embryo dependent process in C.elegans HOIP_0050289 HOIP:HOIP_0050293 Any process that activates or increases the frequency, rate or extent of asymmetric protein localization involved in cell fate determination. PMID:32829680 doi/10.1895/wormbook.1.30.2 positive regulation of asymmetric protein localization involved in cell fate determination in the one-cell embryo dependent process in C.elegans HOIP_0050293 PMID:32829680 In the anterior domain, MEX-5 outcompetes MEG-3 and PGL-3 for RNA-binding, whereas in the posterior, MEG-3 and PGL-3 can bind RNA and undergo phase separation, leading to P granule formation. MEG-3 phase separates into more stable gel-like condensates at the surface of P granules (see phase separation inset); hence, MEG-3 gradient can lead to granule stability at the posterior. HOIP:HOIP_0050296 A process in which a Pgranule is transported to, or maintained in, the posterior cell. P granule localization to posterior cell HOIP_0050296 HOIP:HOIP_0050298 A protein role that Interacts selectively and non-covalently with an RNA molecule or a portion thereof. RNA binding protein role HOIP_0050298 HOIP:HOIP_0050300 A process involved in germ cell fate commitment. Once determination has taken place, a cell becomes committed to differentiate down a particular pathway regardless of its environment. germ cell fate specification HOIP_0050300 HOIP:HOIP_0050302 Any process that activates or increases the frequency, rate or extent of the P granule localization to poterior germ line. PMID:32829680 doi/10.1895/wormbook.1.30.2 positive regulation of P granule localization to posterior germline blastomere in early embryo dependent process in C.elegans HOIP_0050302 PMID:32829680 In the anterior domain, MEX-5 outcompetes MEG-3 and PGL-3 for RNA-binding, whereas in the posterior, MEG-3 and PGL-3 can bind RNA and undergo phase separation, leading to P granule formation. MEG-3 phase separates into more stable gel-like condensates at the surface of P granules (see phase separation inset); hence, MEG-3 gradient can lead to granule stability at the posterior. HOIP:HOIP_0050303 Any process that activates or increases the frequency, rate or extent of the P granule localization to poterior cell. positive regulation of organelle localization HOIP_0050303 HOIP:HOIP_0050304 Any process that activates or increases the frequency, rate or extent of the P granule localization to poterior cell. PMID:32829680 doi/10.1895/wormbook.1.30.2 positive regulation of P granule localization to posterior germ line HOIP_0050304 PMID:32829680 In the anterior domain, MEX-5 outcompetes MEG-3 and PGL-3 for RNA-binding, whereas in the posterior, MEG-3 and PGL-3 can bind RNA and undergo phase separation, leading to P granule formation. MEG-3 phase separates into more stable gel-like condensates at the surface of P granules (see phase separation inset); hence, MEG-3 gradient can lead to granule stability at the posterior. HOIP:HOIP_0050305 A process involved in germ cell fate commitment. Once determination has taken place, a cell becomes committed to differentiate down a particular pathway regardless of its environment. doi/10.1895/wormbook.1.30.2 germ cell fate specification in early embryo dependent process in C.elegans HOIP_0050305 doi/10.1895/wormbook.1.30.2 We use the term cell fate regulators for those molecules that directly regulate the fate of one or a few founder cells. These regulators include PIE-1 and NOS-2 (P cell fate), SKN-1 and POP-1 (EMS fates), PAL-1 (C and D fate), as well as GLP-1 and APX-1 (AB fates). HOIP:HOIP_0050306 A process in which a PAR1 is maintained in the posterior cell cortex. maintenance of PAR1 location in posterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050306 HOIP:HOIP_0050307 A process in which posterior PARs are maintained in the posterior cell cortex. doi/10.1895/wormbook.1.30.2 maintenance of posterior PARs location in posterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050307 doi/10.1895/wormbook.1.30.2 The RING finger of PAR-2 is critical to counteract the impact of PKC-3, perhaps by making PAR-2 a poorer substrate for the kinase (Hao et al., 2006). In turn, the presence of PAR-2 at the cell cortex promotes the recruitment of PAR-1 through a direct interaction between the two proteins (Motegi et al., 2011), although PAR-1 can localize to the cortex in a PAR-2-independent manner when PAR-3 is lacking (reviewed in Kemphues and Strome, 1997). In addition, PAR-1 can phosphorylate PAR-3 in vitro, and PAR-1 kinase activity is required for the exclusion of the anterior PAR complex from the posterior cortex in embryos that rely solely on the PAR-2-dependent pathway described above (Motegi et al., 2011). HOIP:HOIP_0050308 A process in which anterior PARs are maintained in the anterior cell cortex. doi/10.1895/wormbook.1.30.2 maintenance of posterior PARs location in posterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050308 doi/10.1895/wormbook.1.30.2 During polarity maintenance, mutual inhibition between the anterior and posterior cortical domains is critical and par-2 is essential to maintain the anterior PAR complex restricted to the embryo anterior. Thus, in par-2 mutants, GFP::PAR-6, which had been restricted to the anterior during the establishment phase, returns to the posterior to occupy the entire cortical circumference (Cuenca et al., 2003), concomitantly with abnormal posterior-directed cortical movements of NMY-2::GFP (Munro et al., 2004). Although it has been proposed that these NMY-2 movements contribute to preventing the maintenance of PAR asymmetries (Munro et al., 2004), more recent evidence indicates that cortical NMY-2 plays a minor role in this phase (Beatty et al., 2013). HOIP:HOIP_0050309 Any process that stops, prevents, or reduces the frequency, rate or extent of MEX6 localization to posterior cell. negative regulation of MEX6 localization to posterior cell HOIP_0050309 HOIP:HOIP_0050311 Any process that stops, prevents, or reduces the frequency, rate or extent of the somatic cell fate factor transcription mediated by RNA polymerase II. doi/10.1895/wormbook.1.30.2 negative regulation of somatic cell fate factor transcription by RNA polymerase II in early embryo dependent process in C.elegans HOIP_0050311 doi/10.1895/wormbook.1.30.2 Although present, neither SKN-1 nor PAL-1 activates gene expression in the P cells. This is because the germ line precursors are protected from activating somatic programs of gene expression by PIE-1, which is restricted to the P cell at each asymmetric division (Figure 5) (Mello et al., 1996). Germ-line precursors in C. elegans, as in many organisms, are transcriptionally quiescent. Inhibition of transcription correlates with the failure to phosphorylate the C-terminal domain of RNA polymerase on Serine-5 (Ser-5) and Ser-2, which are needed for transcription initiation and elongation, respectively. These phophorylation events are inhibited by PIE-1 in the P cells of early C. elegans embryos (Tenenhaus et al., 1998). In vitro studies indicate that PIE-1 directly binds to, and inhibits, the kinase needed for Ser-2 phosphorylation (Batchelder et al., 1999). Altered forms of PIE-1 that do not bind the kinase fail to inhibit Ser-2 phosphorylation in vivo, but can still suppress transcription and promote germ-line fate through effects on Ser-5 phosphorylation (Ghosh and Seydoux, 2008). Inhibition of transcription is thought to prevent SKN-1, PAL-1 and other transcription factors from activating gene expression in the P cells. However, after asymmetric division of P2, the degradation of PIE-1 from the somatic daughter via the MEX-5/ZIF-1 pathway described above relieves transcriptional repression, allowing SKN-1 activation of target genes in EMS. Similarly, after the P2 and P3 divisions, disappearance of PIE-1 allows PAL-1 activation of target genes to commence. PIE-1 is also important for activating the translation of NOS-2 in the P4 cell; although the mechanism is unknown, this function of PIE-1 is separable from its role in preventing transcription (D'Agostino et al., 2006; Tenenhaus et al., 2001). HOIP:HOIP_0050314 A protein that is a translation product of the pal-1 gene in worm. Enables DNA-binding transcription factor activity, RNA polymerase II-specific and RNA polymerase II transcription regulatory region sequence-specific DNA binding activity. Involved in several processes, including cell fate commitment; embryonic pattern specification; and positive regulation of transcription by RNA polymerase II. Located in condensed nuclear chromosome. Expressed in several structures, including ABprpppppaa; enteric muscle; oocyte; rectal epithelial cell; and tail spike. Human ortholog(s) of this gene implicated in Barrett's esophagus. Is an ortholog of human CDX1 (caudal type homeobox 1). Enables DNA-binding transcription factor activity, RNA polymerase II-specific and RNA polymerase II transcription regulatory region sequence-specific DNA binding activity. Involved in several processes, including cell fate commitment; embryonic pattern specification; and positive regulation of transcription by RNA polymerase II. Located in condensed nuclear chromosome. Expressed in several structures, including ABprpppppaa; enteric muscle; oocyte; rectal epithelial cell; and tail spike. Human ortholog(s) of this gene implicated in Barrett's esophagus. Is an ortholog of human CDX1 (caudal type homeobox 1). pal-1 encodes a homeodomain protein that is the C. elegans Caudal ortholog; PAL-1 is required maternally and embryonically for specification of the C and D posterior blastomere fates and thus, for proper bodywall muscle and hypodermal development during embryogenesis; PAL-1 is also required postembryonically for fate specification of the posterior V6 neuroectoblast during male tail development; in regulating embryonic bodywall muscle specification, PAL-1 binds to an enhancer element in the promoter of hlh-1, the sole C. elegans MRF family member, to positively regulate hlh-1 transcription; PAL-1 is expressed in posterior blastomeres beginning at the four-cell stage of embryogenesis and its expression continues during embryogenesis in posterior-derived tissues and cells undergoing movement or forming midline structures; pal-1 is subject to both transcriptional and translational regulation. pal-1 encodes a homeodomain protein that is the C. elegans Caudal ortholog; PAL-1 is required maternally and embryonically for specification of the C and D posterior blastomere fates and thus, for proper bodywall muscle and hypodermal development during embryogenesis; PAL-1 is also required postembryonically for fate specification of the posterior V6 neuroectoblast during male tail development; in regulating embryonic bodywall muscle specification, PAL-1 binds to an enhancer element in the promoter of hlh-1, the sole C. elegans MRF family member, to positively regulate hlh-1 transcription; PAL-1 is expressed in posterior blastomeres beginning at the four-cell stage of embryogenesis and its expression continues during embryogenesis in posterior-derived tissues and cells undergoing movement or forming midline structures; pal-1 is subject to both transcriptional and translational regulation. UniProtKB:P34766 WormBase:WBGene00003912 homeobox protein pal-1 (worm) pal-1 (worm) PAL1 (worm) HOIP_0050314 Enables DNA-binding transcription factor activity, RNA polymerase II-specific and RNA polymerase II transcription regulatory region sequence-specific DNA binding activity. Involved in several processes, including cell fate commitment; embryonic pattern specification; and positive regulation of transcription by RNA polymerase II. Located in condensed nuclear chromosome. Expressed in several structures, including ABprpppppaa; enteric muscle; oocyte; rectal epithelial cell; and tail spike. Human ortholog(s) of this gene implicated in Barrett's esophagus. Is an ortholog of human CDX1 (caudal type homeobox 1). https://wormbase.org/species/c_elegans/gene/WBGene00003912 pal-1 encodes a homeodomain protein that is the C. elegans Caudal ortholog; PAL-1 is required maternally and embryonically for specification of the C and D posterior blastomere fates and thus, for proper bodywall muscle and hypodermal development during embryogenesis; PAL-1 is also required postembryonically for fate specification of the posterior V6 neuroectoblast during male tail development; in regulating embryonic bodywall muscle specification, PAL-1 binds to an enhancer element in the promoter of hlh-1, the sole C. elegans MRF family member, to positively regulate hlh-1 transcription; PAL-1 is expressed in posterior blastomeres beginning at the four-cell stage of embryogenesis and its expression continues during embryogenesis in posterior-derived tissues and cells undergoing movement or forming midline structures; pal-1 is subject to both transcriptional and translational regulation. https://wormbase.org/species/c_elegans/gene/WBGene00003912 HOIP:HOIP_0050315 A process in which PIE1 is transported to, or maintained in, the posterior P1 cell. ISBN:4895928055 doi/10.1895/wormbook.1.30.1 PIE1 localization to poterior P1 cell in early embryo dependent process in C.elegans HOIP_0050315 doi/10.1895/wormbook.1.30.1 Figure 3. Sequential relationships between AP polarity components in one-cell stage embryos. Contact between the centrosome and the cortex breaks the symmetry of the zygote and results in PAR-3/PAR-6/PKC-3 receding from the posterior in an NMY-2-dependent manner. Meanwhile, PAR-2 enrichment at the posterior occurs concomitant with that of PAR-3/PAR-6/PKC-3 at the anterior. In turn, PAR-1 prevents MEX-5/6 accumulation at the posterior. The presence of MEX-5/6 at the anterior prevents the presence of P granules and PIE-1 on that side of the embryo, and also reinforces anterior PAR-3/PAR-6/PKC-3 distribution. As a result of this sequence of interactions, P granules and PIE-1 are segregated to the posterior of one-cell stage embryos. HOIP:HOIP_0050316 The chemical reactions and pathways resulting in the breakdown of PIE-1 by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein in the anterior cell. ISBN:4895928055 PMID:18199581 doi/10.1895/wormbook.1.30.1 PIE1 catabolic process at the anterior cell in the one-cell embryo dependent process in C.elegans HOIP_0050316 PMID:18199581 The small amount of PIE-1 segregated to the somatic sister after each division is degraded by a ZIF-1-containing CUL-2 E3 ligase complex (DeRenzo et al.,2003; Reese et al.,2000). Both asymmetric distribution of PIE-1 before division, as well as asymmetric degradation after division, require the function of MEX-5/6(DeRenzo et al., 2003; Schubert et al., 2000). MEX-5/6 are themselves also substrates for this ZIF-1-containing E3 ligase complex (DeRenzo et al.,2003). doi/10.1895/wormbook.1.30.1 Figure 3. Sequential relationships between AP polarity components in one-cell stage embryos. Contact between the centrosome and the cortex breaks the symmetry of the zygote and results in PAR-3/PAR-6/PKC-3 receding from the posterior in an NMY-2-dependent manner. Meanwhile, PAR-2 enrichment at the posterior occurs concomitant with that of PAR-3/PAR-6/PKC-3 at the anterior. In turn, PAR-1 prevents MEX-5/6 accumulation at the posterior. The presence of MEX-5/6 at the anterior prevents the presence of P granules and PIE-1 on that side of the embryo, and also reinforces anterior PAR-3/PAR-6/PKC-3 distribution. As a result of this sequence of interactions, P granules and PIE-1 are segregated to the posterior of one-cell stage embryos. HOIP:HOIP_0050317 The chemical reactions and pathways resulting in the breakdown of PIE-1 by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein. ISBN:4895928055 doi/10.1895/wormbook.1.30.2 proteasomal PIE1 catabolic process PIE1 catabolic process HOIP_0050317 doi/10.1895/wormbook.1.30.2 Figure 3. Sequential relationships between AP polarity components in one-cell stage embryos. Contact between the centrosome and the cortex breaks the symmetry of the zygote and results in PAR-3/PAR-6/PKC-3 receding from the posterior in an NMY-2-dependent manner. Meanwhile, PAR-2 enrichment at the posterior occurs concomitant with that of PAR-3/PAR-6/PKC-3 at the anterior. In turn, PAR-1 prevents MEX-5/6 accumulation at the posterior. The presence of MEX-5/6 at the anterior prevents the presence of P granules and PIE-1 on that side of the embryo, and also reinforces anterior PAR-3/PAR-6/PKC-3 distribution. As a result of this sequence of interactions, P granules and PIE-1 are segregated to the posterior of one-cell stage embryos. HOIP:HOIP_0050318 The process in which LGL-1 is released from the anterior cell cortex. doi/10.1895/wormbook.1.30.2 dissociation of LGL1 from anterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050318 doi/10.1895/wormbook.1.30.2 a PAR-6/PAR-3/LGL-1 complex forms initially, but that PKC-3-mediated phosphorylation of LGL-1 prevents its localization on the anterior side during the course of polarity establishment (Beatty et al., 2010; Hoege et al., 2010). HOIP:HOIP_0050319 The process in which LGL-1 is released from the anterior cell cortex. dissociation of LGL1 from anterior cell cortex HOIP_0050319 HOIP:HOIP_0050320 A process in which a LGL1 is transported to, or maintained in, the posterior cell cortex. doi/10.1895/wormbook.1.30.2 LGL1 localization to poterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050320 doi/10.1895/wormbook.1.30.2 a PAR-6/PAR-3/LGL-1 complex forms initially, but that PKC-3-mediated phosphorylation of LGL-1 prevents its localization on the anterior side during the course of polarity establishment (Beatty et al., 2010; Hoege et al., 2010). HOIP:HOIP_0050321 A process in which a LGL1 is transported to, or maintained in, the cell cortex. LGL1 localization to cell cortex HOIP_0050321 HOIP:HOIP_0050322 A protein that is a translation product of the par family gene. partitioning defective protein PAR HOIP_0050322 HOIP:HOIP_0050323 Increasing distance between nterior and posterioe PARs is a subtype of increasing distance between cells: A process that places a distance between anterior PARs (aPARs) and poserior PARs (pPARs). increasing distance between anterior and posterior PARs HOIP_0050323 HOIP:HOIP_0050324 Increasing distance between nterior and posterioe PARs is a subtype of increasing distance between cells: A process that places a distance between anterior PARs (aPARs) and poserior PARs (pPARs). increasing distance between anterior and posterior PARs in the one-cell embryo dependent process in C.elegans HOIP_0050324 HOIP:HOIP_0050325 A protein that is a translation product of the par family gene and distributed the anterior cell cortex. partitioning defective protein aPAR anterior PAR (worm) HOIP_0050325 HOIP:HOIP_0050326 A protein that is a translation product of the par family gene and distributed the posterior cell cortex. pPAR posterior PAR (worm) HOIP_0050326 HOIP:HOIP_0050327 A protein that is a translation product of the meg-3 gene in worm. Involved in embryo development; gamete generation; and organelle localization. Located in P granule. Expressed in several structures, including germ cell and oocyte. Involved in embryo development; gamete generation; and organelle localization. Located in P granule. Expressed in several structures, including germ cell and oocyte. meg-3 encodes a novel protein that affects embryonic viability and development of the hypodermis; MEG-3 interacts with GEX-3 in yeast two-hybrid assays, and is expressed in all somatic cells. meg-3 encodes a novel protein that affects embryonic viability and development of the hypodermis; MEG-3 interacts with GEX-3 in yeast two-hybrid assays, and is expressed in all somatic cells. UniProtKB:Q9TXM1 WormBase:WBGene00001569 meg-3 (worm) MEG3 (worm) HOIP_0050327 Involved in embryo development; gamete generation; and organelle localization. Located in P granule. Expressed in several structures, including germ cell and oocyte. https://wormbase.org/species/c_elegans/gene/WBGene00001569 meg-3 encodes a novel protein that affects embryonic viability and development of the hypodermis; MEG-3 interacts with GEX-3 in yeast two-hybrid assays, and is expressed in all somatic cells. https://wormbase.org/species/c_elegans/gene/WBGene00001569 HOIP:HOIP_0050328 The role played by the molecule that contributes to the structural stabilization or tethering them into complexes. related molecular function GO:0005200 scaffold protein role HOIP_0050328 HOIP:HOIP_0050329 A process that matintains the P granule structure in the posterior cell. PMID:32829680 P granule stabilization at posterior cell in the one-cell embryo dependent process in C.elegans HOIP_0050329 PMID:32829680 Interestingly, despite the similar requirements and regulations for PGL-3 and MEG-3 in P granule formation, they occupy different sites in the condensates. MEG-3 can surround the granule, while the majority of PGL-3 is localized to the interior of the structure (figure 3a phase separation inset) . This variant structural distribution of MEG-3 in the P granule reflects a recently identified role. MEG-3 can phase separate into more stable gel-like condensates, which further enhances granule stability at the posterior. HOIP:HOIP_0050330 A process that matintains the P granule structure in the posterior cell. P granule stabilization at posterior germline cell HOIP_0050330 HOIP:HOIP_0050331 A protein that is a translation product of the pgl-3 gene in worm. Enables endoribonuclease activity and identical protein binding activity. Involved in RNA phosphodiester bond hydrolysis, endonucleolytic. Located in P granule. Expressed in Psub1 and germ line. evidence Enables endoribonuclease activity and identical protein binding activity. Involved in RNA phosphodiester bond hydrolysis, endonucleolytic. Located in P granule. Expressed in Psub1 and germ line. evidence pgl-3 encodes a novel protein that is a member of the PGL (P Granule Abnormality) family of C. elegans proteins that are associated with germline P granules; pgl-3 functions redundantly with pgl-1 in hermaphrodite germline development by controlling the extent of germline proliferation as well as gametogenesis and embryonic development; PGL-3 and PGL-1 interact in vitro and in vivo, suggesting that they function are part of the same complex; PGL-3 also interacts with PGL-2 in vitro; PGL-3 localizes to P granules in both sexes at all stages of development except during spermatogenesis; PGL-3 localization to P granules requires the GLH-1 germline helicase, a constitutive P granule component. pgl-3 encodes a novel protein that is a member of the PGL (P Granule Abnormality) family of C. elegans proteins that are associated with germline P granules; pgl-3 functions redundantly with pgl-1 in hermaphrodite germline development by controlling the extent of germline proliferation as well as gametogenesis and embryonic development; PGL-3 and PGL-1 interact in vitro and in vivo, suggesting that they function are part of the same complex; PGL-3 also interacts with PGL-2 in vitro; PGL-3 localizes to P granules in both sexes at all stages of development except during spermatogenesis; PGL-3 localization to P granules requires the GLH-1 germline helicase, a constitutive P granule component. UniProtKB:G5EBV6 WormBase:WBGene00003994 pgl-3 (worm) PGL3 (worm) HOIP_0050331 Enables endoribonuclease activity and identical protein binding activity. Involved in RNA phosphodiester bond hydrolysis, endonucleolytic. Located in P granule. Expressed in Psub1 and germ line. evidence https://wormbase.org/species/c_elegans/gene/WBGene00003994 pgl-3 encodes a novel protein that is a member of the PGL (P Granule Abnormality) family of C. elegans proteins that are associated with germline P granules; pgl-3 functions redundantly with pgl-1 in hermaphrodite germline development by controlling the extent of germline proliferation as well as gametogenesis and embryonic development; PGL-3 and PGL-1 interact in vitro and in vivo, suggesting that they function are part of the same complex; PGL-3 also interacts with PGL-2 in vitro; PGL-3 localizes to P granules in both sexes at all stages of development except during spermatogenesis; PGL-3 localization to P granules requires the GLH-1 germline helicase, a constitutive P granule component. https://wormbase.org/species/c_elegans/gene/WBGene00003994 HOIP:HOIP_0050332 The process that occurs after sperm attachment, fusion of the plasma membrane and enters into an oocyte. ISBN13:9784895928052 doi/10.1895/wormbook.1.30.2 C.elegans sperm entry into oocyte 2 HOIP_0050332 ISBN13:9784895928052 Gilbert, Scott F. , 阿形, 清和, 高橋, 淑子, ギルバート発生生物学, メディカル・サイエンス・インターナショナル, 2015 doi/10.1895/wormbook.1.30.2 Fertilization occurs in the spermatheca, with the union of a mature oocyte and a sperm cell. The newly fertilized zygote is then displaced into the uterus where meiosis is completed and early embryogenesis takes place. HOIP:HOIP_0050333 The process that sperm pronucleus enters into an oocyte cytoplasm. sperm pronucleus entry into oocyte cytoplasm HOIP_0050333 HOIP:HOIP_0050337 The directed movement of the male and female pronuclei towards each other prior to their fusion. doi/10.1895/wormbook.1.30.2 female pronuclear migration in the one-cell embryo dependent process in C.elegans HOIP_0050337 doi/10.1895/wormbook.1.30.2 Centrosomes and the associated male pronucleus are located initially close to the posterior cortex, and then migrate jointly towards the anterior. Concomitantly, the female pronucleus migrates towards the posterior, resulting in the meeting of the two pronuclei in the posterior half of the embryo. Migration of both male and female pronuclei depends on microtubules and microtubule associated proteins, including the minus-end directed motor dynein and members of the dynein complex (reviewed in McNally, 2013; Morin and Bellaiche, 2011; Galli and van den Heuvel, 2008). Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook HOIP:HOIP_0050338 The directed movement of the male pronuclei towards each other prior to their fusion. doi/10.1895/wormbook.1.30.2 male pronuclear migration in the one-cell embryo dependent process in C.elegans HOIP_0050338 doi/10.1895/wormbook.1.30.2 Centrosomes and the associated male pronucleus are located initially close to the posterior cortex, and then migrate jointly towards the anterior. Concomitantly, the female pronucleus migrates towards the posterior, resulting in the meeting of the two pronuclei in the posterior half of the embryo. Migration of both male and female pronuclei depends on microtubules and microtubule associated proteins, including the minus-end directed motor dynein and members of the dynein complex (reviewed in McNally, 2013; Morin and Bellaiche, 2011; Galli and van den Heuvel, 2008). Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook HOIP:HOIP_0050339 The cell cycle process in which chromosomes are aligned at the metaphase plate, a plane halfway between the poles of the mitotic spindle, during mitosis. ISBN:9784895928052 mitotic metaphase plate congression in the one-cell embryo dependent process in C.elegans HOIP_0050339 ISBN:9784895928052 第一分裂の際，中期板が後極近くに形成され，受精卵は後方PAR（PAR-6とPAR-3）を持つ細胞と，前方PAＲ（PAR-1とPAR-2）を持つ細胞に分裂する． Gilbert, Scott F. , 阿形, 清和, 高橋, 淑子, ギルバート発生生物学, メディカル・サイエンス・インターナショナル, 2015 HOIP:HOIP_0050345 The cell cycle process in which replicated homologous chromosomes are organized and then physically separated and apportioned to two sets during the mitotic cell cycle. Each replicated chromosome, composed of two sister chromatids, aligns at the cell equator, paired with its homologous partner. One homolog of each morphologic type goes into each of the resulting chromosome sets. doi/10.1895/wormbook.1.30.2 mitotic sister chromatid segregation in the one-cell embryo dependent process in C.elegans HOIP_0050345 doi/10.1895/wormbook.1.30.2 The formation of mitotic chromosomes begins when cohesin is loaded onto chromosomes and establishes cohesion between the duplicated chromosomes (sister chromatids) during DNA replication in S phase. Proteolytic cleavage of one of the cohesin subunits later in the cell cycle is thought to release the linkage between the sister chromatids to allow their segregation during anaphase (Haering and Nasmyth, 2003). The components of the C. elegans cohesin complex have been identified and depletion has revealed roles in mitotic chromosome segregation and the pairing of homologous chromosomes during meiosis (Table 3; Chan et al., 2003; Mito et al., 2003; Pasierbek et al., 2003). HOIP:HOIP_0050349 The cell cycle process in which paired chromosomes are detached from each other. Chromosome separation begins with the release of cohesin complexes from chromosomes; in budding yeast, this includes the cleavage of cohesin complexes along the chromosome arms, followed by the separation of the centromeric regions. Chromosome separation also includes formation of chromatid axes mediated by condensins, and ends with the disentangling of inter-sister catenation catalyzed by topoisomerase II (topo II). doi/10.1895/wormbook.1.30.2 chromosome separation in the one-cell embryo dependent process in C.elegans HOIP_0050349 doi/10.1895/wormbook.1.30.2 Chromosome segregation typically consists of two components: (1) anaphase A, in which the chromosomes move towards the spindle poles and, (2) anaphase B in which the spindle poles separate from each other with the chromosomes in tow. In C. elegans the majority of chromosome movement is due to anaphase B (Oegema et al., 2001), powered by a combination of cortical forces that pull on the centrosomal microtubule asters to separate them, and pushing forces generated by the array of overlapping microtubules, called the central spindle, that forms between the separating chromosomes. If the mitotic spindle is severed during anaphase using a UV micro beam, the two spindle poles separate with increased velocity (Grill et al., 2001). This experiment demonstrates the existence of pulling forces during the first mitotic division and suggests that the central spindle normally acts to limit the rate of pole separation. However, in embryos in which G protein signaling that mediates cortical pulling forces is disrupted, spindles still elongate (Colombo et al., 2003) albeit at a slower rate, indicating that other spindle intrinsic forces contribute to anaphase spindle elongation. HOIP:HOIP_0050353 The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis. doi/10.1895/wormbook.1.72.1 doi/10.1895/wormbook.1.72.1 mitotic chromosome movement towards spindle pole in the one-cell embryo dependent process in C.elegans HOIP_0050353 doi/10.1895/wormbook.1.72.1 Chromosome segregation typically consists of two components: (1) anaphase A, in which the chromosomes move towards the spindle poles and, (2) anaphase B in which the spindle poles separate from each other with the chromosomes in tow. In C. elegans the majority of chromosome movement is due to anaphase B (Oegema et al., 2001), powered by a combination of cortical forces that pull on the centrosomal microtubule asters to separate them, and pushing forces generated by the array of overlapping microtubules, called the central spindle, that forms between the separating chromosomes. If the mitotic spindle is severed during anaphase using a UV micro beam, the two spindle poles separate with increased velocity (Grill et al., 2001). This experiment demonstrates the existence of pulling forces during the first mitotic division and suggests that the central spindle normally acts to limit the rate of pole separation. However, in embryos in which G protein signaling that mediates cortical pulling forces is disrupted, spindles still elongate (Colombo et al., 2003) albeit at a slower rate, indicating that other spindle intrinsic forces contribute to anaphase spindle elongation. Oegema, K. and Hyman, A. A. Cell division (January 19, 2006), WormBook, ed. The C. elegans Research Community, WormBook, doi/10.1895/wormbook.1.72.1 HOIP:HOIP_0050357 The mitotic cell cycle process involving ESCRTIII that results in reformation of the nuclear envelope after mitotic nuclear division. In organisms undergoing closed mitosis this involves resealing or 'repair' of the nuclear envelope in the nuclear bridge. doi/10.1895/wormbook.1.72.1 mitotic nuclear membrane reassembly in the one-cell embryo dependent process in C.elegans HOIP_0050357 doi/10.1895/wormbook.1.72.1 Oegema, K. and Hyman, A. A. Cell division (January 19, 2006), WormBook, ed. The C. elegans Research Community, WormBook HOIP:HOIP_0050360 The division of the cytoplasm and the plasma membrane of a cell and its partitioning into two daughter cells. mitotic cytokinesis in the one-cell embryo dependent process in C.elegans HOIP_0050360 HOIP:HOIP_0050362 Making existence of pulling force is a subtype of making existence of force: A process that makes a pulling force to be present in another object. making existence of pulling force HOIP_0050362 HOIP:HOIP_0050363 making exitence of pulling force on microtube is a subtype of making existence of force: A process that makes a pulling force to be present on microtube. doi/10.1895/wormbook.1.30.2 making exitence of pulling force on microtube in the one-cell embryo dependent process in C.elegans HOIP_0050363 doi/10.1895/wormbook.1.30.2 For male pronuclear migration, computer simulations indicate that pulling forces act in a length-dependent manner, with larger forces pulling on longer microtubules (Kimura and Onami, 2005). A related type of mechanism has been proposed to predominate during centration/rotation (Kimura and Kimura, 2011). In a length-dependent type of mechanism, force generators must be distributed throughout the cytoplasm, for instance by being anchored on endomembranes, which could thus generate pulling forces on astral microtubules and associated centrosomes. It has been suggested that small movements of endomembranes towards the minus-end of microtubules could generate a net overall movement of the centrosome in the opposite direction (Kimura and Kimura, 2011). In support of this mechanism, there is a good correlation between centrosome-directed movements of early endosomes marked by GFP::EEA-1 and that of centrosomes in the opposite direction (Kimura and Kimura, 2011). Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook. HOIP:HOIP_0050364 Making existence of pushing forceis a subtype of making existence of force: A process that makes a pushing force to be present in another object. making existence of pushing force HOIP_0050364 HOIP:HOIP_0050365 pulling force generation is a subtype of generating: A process that generates the pulling force of structure. making exitence of pushing force in the one-cell embryo dependent process in C.elegans HOIP_0050365 HOIP:HOIP_0050366 The totality of all processes through which early embryonic asymmetric division in C.elegans is realized. doi/10.1895/wormbook.1.30.2 C. elegans early embryonic asymmetric division course HOIP_0050366 doi/10.1895/wormbook.1.30.2 Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook. HOIP:HOIP_0050368 A ZIF-1 containing ubiquitin ligase complex in which a cullin from the Cul2 family and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein. ZIF-1-containing CUL-2 E3 ligase complex (worm) HOIP_0050368 HOIP:HOIP_0050372 The cell cycle process in which the second meiotic division occurs in the female germline. doi/10.1895/wormbook.1.30.2 female meiosis II in the one-cell embryo dependent process in C.elegans HOIP_0050372 doi/10.1895/wormbook.1.30.2 Fertilization occurs in the spermatheca, with the union of a mature oocyte and a sperm cell. The newly fertilized zygote is then displaced into the uterus where meiosis is completed and early embryogenesis takes place. Starting from the time of anaphase of meiosis II, the entire actomyosin network located in the cell cortex that underlies the plasma membrane undergoes contractions that depend on the non-muscle myosin II heavy chain NMY-2 and the associated non-muscle myosin light chain 4 MLC-4 (Munro et al., 2004; Shelton et al., 1999) . HOIP:HOIP_0050373 A process that produces a female pronucleus. female pronucleus formation HOIP_0050373 HOIP:HOIP_0050374 doi/10.1895/wormbook.1.72.1 A process that produces a female pronucleus. female pronucleus formation in the one-cell embryo dependent process in C.elegans HOIP_0050374 doi/10.1895/wormbook.1.72.1 Prior to fertilization, C. elegans oocytes are arrested in meiotic prophase with nuclei containing two copies of the diploid genome packaged into recombined bivalent chromosomes. The two rounds of meiotic chromosome segregation that generate the haploid oocyte pronucleus are completed in the zygote after the oocytes are fertilized. During each meiotic division, chromosome segregation is accomplished by a small acentriolar meiotic spindle that forms in the embryo anterior. During anaphase of meiosis I and again in meiosis II, the meiotic spindle associates with the cortex in an end-on fashion, and a highly asymmetric cytokinesis-like event extrudes a polar body (Figure 2; Albertson and Thomson, 1993; Clark-Maguire and Mains, 1994; Yang et al., 2003). In addition to the haploid pronucleus, the sperm brings a pair of centrioles into the oocyte, which lacks centrioles due to their degradation during oogenesis. As meiosis completes, the haploid oocyte and sperm-derived pronuclei, located at opposite ends of the embryo increase in size, becoming visible by DIC microscopy. After entering the oocyte, the sperm-derived centriole pair recruits pericentriolar material and acquires the ability to nucleate microtubules (O'Connell, 2000; Pelletier et al., 2004). Subsequently, the two sperm-derived centrioles separate, forming two centrosomes positioned on either side of the paternal pronucleus. Coincident with chromosome condensation during mitotic prophase, the pronuclei migrate towards each other. After the pronuclei meet, the nuclear-centrosome complex moves to the center of the embryo and rotates to align with the long axis of the embryo (Albertson, 1984; Hyman and White, 1987). The miotitc spindle begins to move towards the embryo posterior during metaphase (Labbe et al., 2004; Oegema et al., 2001), and asymmetric elongation during anaphase contributes to its posterior displacement (Albertson, 1984; Grill et al., 2001). Since the cleavage furrow bisects the mitotic spindle, this displacement results in an asymmetric first cleavage Oegema, K. and Hyman, A. A. Cell division (January 19, 2006), WormBook, ed. The C. elegans Research Community, WormBook, HOIP:HOIP_0050375 A process that produces a male pronucleus. male pronucleus formation HOIP_0050375 HOIP:HOIP_0050376 A process that produces a pronucleus. pronucleus formation HOIP_0050376 HOIP:HOIP_0050379 The totality of all processes through which early embryonic founder cell in C.elegans is realized. doi/10.1895/wormbook.1.30.2 generation of founder cells in the early embryo HOIP_0050379 doi/10.1895/wormbook.1.30.2 Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook. HOIP:HOIP_0050380 A cell that is closest to the anterior as defined by the developing, or existing, anterior-posterior axis. anterior cell HOIP_0050380 HOIP:HOIP_0050382 A cell that is closest to the posterior as defined by the developing, or existing, anerior-posterior axis. posterior cell HOIP_0050382 HOIP:HOIP_0050383 A process that matintains the P granule structure in the posterior cell. PMID:32829680 P granule stabilization at posterior germline blastomere in the early embryo dependent process in C.elegans HOIP_0050383 PMID:32829680 Interestingly, despite the similar requirements and regulations for PGL-3 and MEG-3 in P granule formation, they occupy different sites in the condensates. MEG-3 can surround the granule, while the majority of PGL-3 is localized to the interior of the structure (figure 3a phase separation inset) . This variant structural distribution of MEG-3 in the P granule reflects a recently identified role. MEG-3 can phase separate into more stable gel-like condensates, which further enhances granule stability at the posterior. HOIP:HOIP_0050384 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of polar granules, cytoplasmic, non-membranous RNA/protein complex aggregates in the primordial germ cells of many higher eukaryotes. P granule organization at posterior cell in the one-cell embryo dependent process in C.elegans HOIP_0050384 HOIP:HOIP_0050386 A process in which a Pgranule is transported to, or maintained in, the posterior cell. ISBN:0878932437 P granule localization to posterior germline blastomere in the early embryo dependent process in C.elegans. HOIP_0050386 ISBN:0878932437 P-granules are ribonucleoprotein complexes that probably function in specifying the germ cells. Using fluorescent antibodies to a component of the P-granules, Strome and Wood (1983) discovered that shortly after fertilization, the randomly scattered P-granules move toward the posterior end of the zygote, so that they enter only the blastomere (P1) formed from the posterior cytoplasm (Figure 8.43). The P-granules of the P1 cell remain in the posterior of the P1 cell and are thereby passed to the P2 cell when P1 divides. During the division of P2 and P3, however, the P-granules become associated with the nucleus that enters the P3 cytoplasm. Eventually, the P-granules will reside in the P4 cell, whose progeny become the sperm and eggs of the adult. Developmental Biology. 6th edition. Gilbert SF. HOIP:HOIP_0050387 A process in which PIE1 is transported to, or maintained in, the posterior cell in the one-cell embryo. ISBN:4895928055 doi/10.1895/wormbook.1.30.2 PIE1 localization to poterior cell in the one-cell embryo dependent process in C.elegans HOIP_0050387 doi/10.1895/wormbook.1.30.2 Figure 3. Sequential relationships between AP polarity components in one-cell stage embryos. Contact between the centrosome and the cortex breaks the symmetry of the zygote and results in PAR-3/PAR-6/PKC-3 receding from the posterior in an NMY-2-dependent manner. Meanwhile, PAR-2 enrichment at the posterior occurs concomitant with that of PAR-3/PAR-6/PKC-3 at the anterior. In turn, PAR-1 prevents MEX-5/6 accumulation at the posterior. The presence of MEX-5/6 at the anterior prevents the presence of P granules and PIE-1 on that side of the embryo, and also reinforces anterior PAR-3/PAR-6/PKC-3 distribution. As a result of this sequence of interactions, P granules and PIE-1 are segregated to the posterior of one-cell stage embryos. HOIP:HOIP_0050388 A role played by the entity that modulates the transcription of specific gene sets transcribed by RNA polymerase II. GO:0000981 RNA polymerase II specific transcription factor role HOIP_0050388 HOIP:HOIP_0050389 A protein that is a translation product of the taf-1 gene in worm. Predicted to contribute to transcription cis-regulatory region binding activity. Involved in embryo development and transcription initiation from RNA polymerase II promoter. Located in nucleus. Predicted to be part of transcription factor TFIID complex. Human ortholog(s) of this gene implicated in X-linked dystonia-parkinsonism and syndromic X-linked intellectual disability. Is an ortholog of human TAF1 (TATA-box binding protein associated factor 1) and TAF1L (TATA-box binding protein associated factor 1 like). Predicted to contribute to transcription cis-regulatory region binding activity. Involved in embryo development and transcription initiation from RNA polymerase II promoter. Located in nucleus. Predicted to be part of transcription factor TFIID complex. Human ortholog(s) of this gene implicated in X-linked dystonia-parkinsonism and syndromic X-linked intellectual disability. Is an ortholog of human TAF1 (TATA-box binding protein associated factor 1) and TAF1L (TATA-box binding protein associated factor 1 like). The taf-1 gene encodes an ortholog of human TATA-binding protein associated factor TAF1L (TAFII250) that possesses histone acetyl transferase (HAT) activity and is a component of the TFIID general transcription factor that recognizes the transcription start site; TAF-1 is required for proper embryonic and larval development. The taf-1 gene encodes an ortholog of human TATA-binding protein associated factor TAF1L (TAFII250) that possesses histone acetyl transferase (HAT) activity and is a component of the TFIID general transcription factor that recognizes the transcription start site; TAF-1 is required for proper embryonic and larval development. PMID:14726532 PMID:25261697 PMID:29212961 UniProtKB:G5EGM3 taf1 (worm) HOIP_0050389 Predicted to contribute to transcription cis-regulatory region binding activity. Involved in embryo development and transcription initiation from RNA polymerase II promoter. Located in nucleus. Predicted to be part of transcription factor TFIID complex. Human ortholog(s) of this gene implicated in X-linked dystonia-parkinsonism and syndromic X-linked intellectual disability. Is an ortholog of human TAF1 (TATA-box binding protein associated factor 1) and TAF1L (TATA-box binding protein associated factor 1 like). https://wormbase.org/species/c_elegans/gene/WBGene00006382 The taf-1 gene encodes an ortholog of human TATA-binding protein associated factor TAF1L (TAFII250) that possesses histone acetyl transferase (HAT) activity and is a component of the TFIID general transcription factor that recognizes the transcription start site; TAF-1 is required for proper embryonic and larval development. https://wormbase.org/species/c_elegans/gene/WBGene00006382 PMID:29212961 Maternal RNA/protein degradation and zygotic genome activation (ZGA), occurring during maternal-to-zygotic transition (MZT), are the first essential events for the development of pre-implantation embryos. Previously, we have shown the importance of the ubiquitin-proteasome system (UPS) for initiation of minor ZGA at the 1-cell stage of mouse embryos. As shown in Fig. 2, the delay in recruitment and phosphorylation of Pol II in transient MG132-treated 1-cell embryos are resultants of improper chromatin remodeling for Pol II recruitment. In general, UPS regulates gene expression and interacts with chromatin at multiple steps. Transcriptional activators cannot translocate into nucleus or bind to DNA due to the failure of degrading their repressive regulators; a large number of transcription factors and cofactors have been reported to be regulated by UPS, indicating that UPS-mediated proteolysis of those factors is inherently linked to the way they stimulate transcription. For example, in Caenorhabditis elegans, zinc-finger proteins OMA-1/2 bind to TBP-associated factor-4 (TAF-4), which is a component of the transcription factor-II D (TFIID) and pre-initiation complex of Pol II, sequestering TAF-4 into the cytoplasm during 1- and 2-cell stages. After the cell division, OMA-1/2 is degraded by UPS, TAF-4 is translocated into the nucleus, and is involved in TFIID-mediated transcriptional activation of the zygotic genome. Furthermore, many histone modification enzymes, which are related to transcriptional silencing and activation, such as histone deacetylases (HDACs), methyltransferases (HMTs), and demethyltransferases (HDMs) are regulated by ubiquitin-mediated proteasomal degradation. At present, the molecular mechanisms of UPS governing minor ZGA in 1-cell embryos remain to be determined. UniProtKB:G5EGM3 https://www.uniprot.org/uniprot/G5EGM3 HOIP:HOIP_0050390 A protein that is a translation product of the ect-2 gene in worm. Enables GTPase activator activity. Involved in cytoskeleton-dependent cytokinesis; mitotic spindle midzone assembly; and positive regulation of GTPase activity. Located in mitotic spindle midzone and plasma membrane. Part of centralspindlin complex. Expressed in germ cell; gonad; and tail. Is an ortholog of human RACGAP1 (Rac GTPase activating protein 1) Enables GTPase activator activity. Involved in cytoskeleton-dependent cytokinesis; mitotic spindle midzone assembly; and positive regulation of GTPase activity. Located in mitotic spindle midzone and plasma membrane. Part of centralspindlin complex. Expressed in germ cell; gonad; and tail. Is an ortholog of human RACGAP1 (Rac GTPase activating protein 1) cyk-4 encodes a Rho GAP (Rho guanosine triphosphatase (GTPase) activating protein); during development, cyk-4 is required for two different processes: 1) paternally provided CYK-4 regulates anterior-posterior polarity in the one-cell embryo by controlling the actomyosin cytoskeletal network, and 2) together with ZEN-4, CYK-4 is sufficient to promote formation of the large bundles of microtubules that form the central spindle during anaphase and polarize the foregut epithelium; in addition, CYK-4 is required for fertility and coordinated locomotion postembryonically; CYK-4 is enriched in sperm and also localizes to the central spindle during anaphase interdependently with ZEN-4; CYK-4 interacts with ZEN-4 in vitro and in vivo. cyk-4 encodes a Rho GAP (Rho guanosine triphosphatase (GTPase) activating protein); during development, cyk-4 is required for two different processes: 1) paternally provided CYK-4 regulates anterior-posterior polarity in the one-cell embryo by controlling the actomyosin cytoskeletal network, and 2) together with ZEN-4, CYK-4 is sufficient to promote formation of the large bundles of microtubules that form the central spindle during anaphase and polarize the foregut epithelium; in addition, CYK-4 is required for fertility and coordinated locomotion postembryonically; CYK-4 is enriched in sperm and also localizes to the central spindle during anaphase interdependently with ZEN-4; CYK-4 interacts with ZEN-4 in vitro and in vivo. PMID:18431399 UniProtKB: Q9XUS9 Wormbase:WBGene00000875 cyk-4 doi/10.1895/wormbook.1.30.2 CYK4 (worm) HOIP_0050390 Enables GTPase activator activity. Involved in cytoskeleton-dependent cytokinesis; mitotic spindle midzone assembly; and positive regulation of GTPase activity. Located in mitotic spindle midzone and plasma membrane. Part of centralspindlin complex. Expressed in germ cell; gonad; and tail. Is an ortholog of human RACGAP1 (Rac GTPase activating protein 1) https://wormbase.org/species/c_elegans/gene/WBGene00000875 cyk-4 encodes a Rho GAP (Rho guanosine triphosphatase (GTPase) activating protein); during development, cyk-4 is required for two different processes: 1) paternally provided CYK-4 regulates anterior-posterior polarity in the one-cell embryo by controlling the actomyosin cytoskeletal network, and 2) together with ZEN-4, CYK-4 is sufficient to promote formation of the large bundles of microtubules that form the central spindle during anaphase and polarize the foregut epithelium; in addition, CYK-4 is required for fertility and coordinated locomotion postembryonically; CYK-4 is enriched in sperm and also localizes to the central spindle during anaphase interdependently with ZEN-4; CYK-4 interacts with ZEN-4 in vitro and in vivo. https://wormbase.org/species/c_elegans/gene/WBGene00000875 PMID:18431399 One essential paternally-contributed component is the Rho GTPase-activating protein (GAP) CYK-4. CYK-4 is present in sperm and is transferred into the zygote upon fertilization, where it persists on membranous organelles in the vicinity of the male pronucleus. A Rho GAP that is present at that location has been proposed to accelerate GTP hydrolysis and thus inactivate Rho, resulting in local actomyosin relaxation. Wormbase:WBGene00000875 cyk-4 http://www.wormbase.org/species/c_elegans/gene/WBGene00000875 doi/10.1895/wormbook.1.30.2 In addition, the GAP CYK-4, which might promote the generation of inactive RHO-1-GDP, has been proposed to play a role (Jenkins et al., 2006). CYK-4 is present in sperm and persists in the newly fertilized zygote on membranous organelles in the vicinity of the centrosome, as well as on the cortex, where it could conceivably contribute to local RHO-1 inactivation. In line with this view, depletion of CYK-4 from sperm compromises symmetry breaking, with the cortical actomyosin network remaining uniformly contractile in a fraction of embryos (Jenkins et al., 2006). However, the mechanisms by which CYK-4 may contribute to polarity establishment remain to be further clarified, and it has been suggested that CYK-4 might be largely inactive during this stage (Tse et al., 2012). Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook HOIP:HOIP_0050392 A general transcription initiation factor activity that contributes to transcription start site selection and transcription initiation of genes transcribed by RNA polymerase II. The general transcription factors for RNA polymerase II include TFIIB, TFIID, TFIIE, TFIIF, TFIIH and TATA-binding protein (TBP). In most species, RNA polymerase II transcribes all messenger RNAs (mRNAs), most untranslated regulatory RNAs, the majority of the snoRNAs, four of the five snRNAs (U1, U2, U4, and U5), and other small noncoding RNAs. For some small RNAs there is variability between species as to whether it is transcribed by RNA polymerase II or RNA polymerase III. However there are also rare exceptions, such as Trypanosoma brucei, where RNA polymerase I transcribes certain mRNAs in addition to its normal role in rRNA transcription GO:0016251 RNA polymerase II general transcription initiation factor HOIP_0050392 HOIP:HOIP_0050401 RHO1 is a protein that is a translation product of the rho-1 gene in worm. RHO-1 GDP is a inactive GDP-bound form RHO-1. GAPs control the ability of the GTPase to hydrolyze GTP to GDP to the inactive conformation. UniProtKB:Q22038 WormBase:WBGene00004357 rho-1 Ras-like GTP-binding protein rhoA (GDP bound form) (worm) rho-1_gdp (worm) Y51H4A.3 rhoa RHO1_GDP (worm) HOIP_0050401 WormBase:WBGene00004357 rho-1 http://www.wormbase.org/species/c_elegans/gene/WBGene00004357 HOIP:HOIP_0050402 The specification of the anterior/posterior axis of the embryo by the products of genes expressed maternally and genes expressed in the zygote. anterior/posterior axis specification, embryo HOIP_0050402 HOIP:HOIP_0050403 The process of creating PAR-3 oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. PAR-3 oligomerization HOIP_0050403 HOIP:HOIP_0050404 A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC. PAR3/PAR6/aPKC aPAR complex PAR6-PAR3-aPKC complex HOIP_0050404 HOIP:HOIP_0050405 The aggregation, arrangement and bonding together of a set of components to form a PAR3-PAR6-aPKC complex. PAR3-PAR6-aPKC complex formation PAR3-PAR6-aPKC complex assembly HOIP_0050405 HOIP:HOIP_0050406 The aggregation, arrangement and bonding together of a set of components to form a PAR complex. PAR complex formation HOIP_0050406 HOIP:HOIP_0050407 RHO inactivation is a subtype of molecular inactivation: A process that changes the activity of the Rho to be lower. RHO iactivation HOIP_0050407 HOIP:HOIP_0050408 RHO1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the Rho to be lower. PMID:33537308 doi/10.1895/wormbook.1.30.2 RHO1 iactivation in the one-cell embryo dependent process in C.elegans HOIP_0050408 PMID:33537308 As a potential candidate, RhoGAPs stimulate hydrolysis of the RHO-1 GTPase. Rho-GAP domain-containing protein RGA-3, RGA-4, and cytokinesis defect CYK-4 have been characterized as RhoGAPs that act on RHO-1 in C. elegans. CYK-4 is required for reorganization of the actomyosin network during SB and cytokinesis (Jantsch-Plunger et al., 2000; Jenkins et al., 2006). Jenkins et al. showed that depletion of CYK-4 blocked SB in the actomyosin network and cortical PAR distribution in 33–50% of zygotes (Jenkins et al., 2006). Notably, the contribution of CYK-4 to SB is strictly paternal (Jenkins et al., 2006), indicating that CYK-4 provided by sperm triggers SB. Consistent with this paternal contribution, immunostaining revealed that CYK-4 was enriched around the sperm pronucleus (Jenkins et al., 2006). These findings support a model in which CYK-4 acts as a GAP that inactivates RHO-1 at the cortex around the sperm pronucleus during SB. However, this model is contradictory to the findings of several recent studies, which demonstrated that a function of CYK-4 is the local stimulation of RHO-1 activity during cytokinesis. CYK-4 can directly interact with RhoGEF ECT-2 and promote RHO-1 activation at the cleavage furrow during cytokinesis (Zhang and Glotzer, 2015; Gómez-Cavazos et al., 2020). Given that CYK-4 carrying the E448K mutation in the GAP domain has no effect on SB, the GAP activity of CYK-4 might be dispensable during SB (Tse et al., 2012). It is paradoxical that without GAP activity during SB, CYK-4 can serve as an inhibitor of RHO-1, but this does not exclude the possibility that CYK-4 may require other associated proteins or posttranscriptional modifications to sense centrosomal AIR-1 and inhibit cortical contractility. The hypothesis of CYK-4 as downstream target of AIR-1 warrants further investigations. doi/10.1895/wormbook.1.30.2 In addition, the GAP CYK-4, which might promote the generation of inactive RHO-1-GDP, has been proposed to play a role (Jenkins et al., 2006). CYK-4 is present in sperm and persists in the newly fertilized zygote on membranous organelles in the vicinity of the centrosome, as well as on the cortex, where it could conceivably contribute to local RHO-1 inactivation. In line with this view, depletion of CYK-4 from sperm compromises symmetry breaking, with the cortical actomyosin network remaining uniformly contractile in a fraction of embryos (Jenkins et al., 2006). However, the mechanisms by which CYK-4 may contribute to polarity establishment remain to be further clarified, and it has been suggested that CYK-4 might be largely inactive during this stage (Tse et al., 2012). HOIP:HOIP_0050409 A process in which a PAR2 is maintained in the posterior cell cortex. doi/10.1895/wormbook.1.30.2 maintenance of PAR2 location in posterior cell cortex in the one-cell embryo dependent process in C.elegans HOIP_0050409 HOIP:HOIP_0050410 A process that stops, prevents, or reduces the frequency, rate or extent of cellular cortex localization mutually between anterior PARs and posterior PARs, resulting in the establishment or maintenance of each specific localization in the cell cortex. doi/10.1895/wormbook.1.30.2 mutual negative regulation of localization to cell cortex between aPARs and pPARs in the one-cell embryo dependent process in C.elegans HOIP_0050410 doi/10.1895/wormbook.1.30.2 The phase of polarity establishment is followed by a maintenance phase during which centrosome ablation no longer interferes with AP polarity (Cowan and Hyman, 2004b), although microtubules have been suggested to contribute to refining polarity during this phase (Ai et al., 2011). During polarity maintenance, mutual inhibition between the anterior and posterior cortical domains is critical and par-2 is essential to maintain the anterior PAR complex restricted to the embryo anterior. Thus, in par-2 mutants, GFP::PAR-6, which had been restricted to the anterior during the establishment phase, returns to the posterior to occupy the entire cortical circumference (Cuenca et al., 2003), concomitantly with abnormal posterior-directed cortical movements of NMY-2::GFP (Munro et al., 2004). Although it has been proposed that these NMY-2 movements contribute to preventing the maintenance of PAR asymmetries (Munro et al., 2004), more recent evidence indicates that cortical NMY-2 plays a minor role in this phase (Beatty et al., 2013). HOIP:HOIP_0050411 Smooth cortical area expansion is a subtype of increasing area: A process that changes the area of the smooth cortex to be larger. PMID:20066102 PMID:20392744 doi/10.1895/wormbook.1.30.2 smooth cortical area expansion in the one-cell embryo dependent process in C.elegans HOIP_0050411 PMID:20066102 In wild-type embryos, polarity establishment is associated with the appearance and progressive growth of a smooth posterior domain, which lacks focal contractions and cortical ruffling and contains high levels of Par-2. Growth of the smooth domain coincides with a progressive depletion of both Rho and Ect-2/RhoGEF from the posterior (Jenkins et al. 2006; Motegi and Sugimoto 2006), implying the growth of a zone of relative myosin inactivity. doi/10.1895/wormbook.1.30.2 Figure 2. Anterior-posterior in one-cell stage embryos. (A) At symmetry breaking, surface contractions of the cortical actomyosin network (red, wiggled line) cease in the vicinity of the centrosome, resulting in the generation of a small smooth cortical domain (blue, smooth line). (B) During polarity establishment, the smooth cortical area expands anteriorly to eventually reach 50% egg-length. Concomitantly, GFP::PAR-2 expands towards the anterior, whereas GFP::PAR-6 retracts from the posterior. (C, D) During centration/rotation (C) and mitosis (D, anaphase shown here), AP polarity is maintained by the mutual inhibition of the anterior and posterior cortical domains. See also Table 1. HOIP:HOIP_0050412 The process in which pericentriolar material (PCM) from maternal stores required for centrosome assembly become associated with the centrioles. doi/10.1895/wormbook.1.30.2 recruitment of pericentriolar material HOIP_0050412 Starting from the time of anaphase of meiosis II, the entire actomyosin network located in the cell cortex that underlies the plasma membrane undergoes contractions that depend on the non-muscle myosin II heavy chain NMY-2 and the associated non-muscle myosin light chain 4 MLC-4 (Munro et al., 2004; Shelton et al., 1999) doi/10.1895/wormbook.1.30.2 doi/10.1895/wormbook.1.30.2 As in most metazoan organisms, the sperm contributes the sole pair of centrioles to the zygote. These centrioles recruit pericentriolar material (PCM) from maternal stores and thus assemble centrosomes that nucleate microtubules. HOIP:HOIP_0050413 Any process that keeps the spatial arrangement of objects between and within cell cortex. doi/10.1895/wormbook.1.30.2 distribution in cell cortex HOIP_0050413 doi/10.1895/wormbook.1.30.2 The anterior PAR complex marked by GFP::PAR-6 is present throughout the cortex initially, but recedes from the posterior following symmetry breaking, concomitant with the anteriorly-directed movement of the contractile cortex (Munro et al., 2004; Cuenca et al., 2003) HOIP:HOIP_0050414 Making existence of force is a subtype of making existence: A process that makes a force to be present in another object. making existence of force HOIP_0050414 HOIP:HOIP_0050416 Any process in which centrosomes are arranged in a location along with the anterior-posterior axis within the cell. doi/10.1895/wormbook.1.30.2 centrosome arrangement along with anterior-posterior axis in the one-cell embryo dependent process in C.elegans HOIP_0050416 doi/10.1895/wormbook.1.30.2 After pronuclear meeting, the centrosomes and the joined pronuclei move towards the embryo center, while undergoing a 90° rotation. This process is referred to collectively as centration/rotation and results in the centrosomes becoming aligned along the AP axis in preparation for cell division HOIP:HOIP_0050417 Accumulation of sperm is a subtype of accumulation of substances in a biological object: A process that keeps sperm in an organism, tissue, organelle, or cell. This entity is a specific course-dependent process. This process can constitute the course od hermaphrodite fertilization in C. elegans. C.elegans accumulation of sperm [hermaphrodite fertilization course in C. elegans'] HOIP_0050417 HOIP:HOIP_0050420 A partial differential equation (PDE) is a differential equation in which the unknown function is a function of multiple independent variables and the equation involves its partial derivatives. partial differential equation HOIP_0050420 HOIP:HOIP_0050422 The diffusion equation is a parabolic partial differential equation. In physics, it describes the macroscopic behavior of many micro-particles in Brownian motion, resulting from the random movements and collisions of the particles (see Fick's laws of diffusion). In mathematics, it is related to Markov processes, such as random walks, and applied in many other fields, such as materials science, information theory, and biophysics. The diffusion equation is a special case of convection–diffusion equation, when bulk velocity is zero. The diffusion equation is a parabolic partial differential equation. In physics, it describes the macroscopic behavior of many micro-particles in Brownian motion, resulting from the random movements and collisions of the particles (see Fick's laws of diffusion). In mathematics, it is related to Markov processes, such as random walks, and applied in many other fields, such as materials science, information theory, and biophysics. The diffusion equation is a special case of convection–diffusion equation, when bulk velocity is zero. If the diffusion coefficient depends on the density then the equation is nonlinear, otherwise it is linear. If \, D is constant, then the equation reduces to the following linear equation: The diffusion equation is a partial differential equation which describes density fluctuations in a material undergoing diffusion. It is also used to describe processes exhibiting diffusive-like behaviour, for instance the 'diffusion' of alleles in a population in population genetics. The equation is usually written as: \frac{\partial\phi(\mathbf{r},t)}{\partial t} = \nabla \cdot \big[ D(\phi,\mathbf{r}) \, \nabla\phi(\mathbf{r},t) \big], where \, \phi(\mathbf{r},t) is the density of the diffusing material at location \mathbf{r} and time t and \, D(\phi,\mathbf{r}) is the collective diffusion coefficient for density \,\phi at location \mathbf{r}; the nabla symbol \, \nabla represents the vector differential operator del acting on the space coordinates. If the diffusion coefficient depends on the density then the equation is nonlinear, otherwise it is linear. The diffusion equation is a partial differential equation which describes density fluctuations in a material undergoing diffusion. It is also used to describe processes exhibiting diffusive-like behaviour, for instance the 'diffusion' of alleles in a population in population genetics. The equation is usually written as: \frac{\partial\phi(\mathbf{r},t)}{\partial t} = \nabla \cdot \big[ D(\phi,\mathbf{r}) \, \nabla\phi(\mathbf{r},t) \big], where \, \phi(\mathbf{r},t) is the density of the diffusing material at location \mathbf{r} and time t and \, D(\phi,\mathbf{r}) is the collective diffusion coefficient for density \,\phi at location \mathbf{r}; the nabla symbol \, \nabla represents the vector differential operator del acting on the space coordinates. If the diffusion coefficient depends on the density then the equation is nonlinear, otherwise it is linear. PMID:20457535 https://en.wikipedia.org/wiki/Diffusion_equation reaction-diffusion equation diffusion equation HOIP_0050422 The diffusion equation is a parabolic partial differential equation. In physics, it describes the macroscopic behavior of many micro-particles in Brownian motion, resulting from the random movements and collisions of the particles (see Fick's laws of diffusion). In mathematics, it is related to Markov processes, such as random walks, and applied in many other fields, such as materials science, information theory, and biophysics. The diffusion equation is a special case of convection–diffusion equation, when bulk velocity is zero. Wikipedia:diffusion equation The diffusion equation is a partial differential equation which describes density fluctuations in a material undergoing diffusion. It is also used to describe processes exhibiting diffusive-like behaviour, for instance the 'diffusion' of alleles in a population in population genetics. The equation is usually written as: \frac{\partial\phi(\mathbf{r},t)}{\partial t} = \nabla \cdot \big[ D(\phi,\mathbf{r}) \, \nabla\phi(\mathbf{r},t) \big], where \, \phi(\mathbf{r},t) is the density of the diffusing material at location \mathbf{r} and time t and \, D(\phi,\mathbf{r}) is the collective diffusion coefficient for density \,\phi at location \mathbf{r}; the nabla symbol \, \nabla represents the vector differential operator del acting on the space coordinates. If the diffusion coefficient depends on the density then the equation is nonlinear, otherwise it is linear. https://wikimedia.org/api/rest_v1/media/math/render/svg/948a15942a9ac71f7c08edb85cb28c88d3d3cfdf HOIP:HOIP_0050424 making exitence of pulling force on spindle during metaphase and anaphase is a subtype of making existence of force: A process that makes a pulling force to be present on spindle. doi/10.1895/wormbook.1.30.2 making exitence of pulling force on spindle during metaphase and anaphase in the one-cell embryo dependent process in C.elegans HOIP_0050424 doi/10.1895/wormbook.1.30.2 Whereas force generators distributed throughout the cell appear important for force generation during male pronuclear migration and centration/rotation, forces driving posterior spindle displacement seem to be cortically-based. Severing of the spindle or fragmentation of the spindle poles with a UV laser microbeam results in outward movements of the liberated spindle poles or spindle pole fragments (Labbé et al., 2004; Grill et al., 2003; Grill et al., 2001). Because these fragments move all the way to the cortex, the force generators acting during mitosis appear to be cortically-based (Labbé et al., 2004; Grill et al., 2003; Grill et al., 2001). Compatible with this view, pulling forces can be observed as invaginations of the plasma membrane following weakening of the actomyosin cytoskeleton (Redemann et al., 2010). The frequency of these invaginations is dramatically reduced when the spindle is severed with a UV laser microbeam or in embryos lacking components required for force generation (see Section 3.2 below). Importantly, the spindle severing and spindle pole fragmentation experiments also establish that the net pulling force acting on the posterior spindle pole is larger than that acting on the anterior one, thus explaining the overall posterior spindle displacement (Grill et al., 2003; Grill et al., 2001). This asymmetry in net pulling forces is under the control of AP polarity cues and serves to couple cell polarity with spindle positioning during the first division (Grill et al., 2001). Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook. HOIP:HOIP_0050428 A Stokes equation is an equation[s] of Stokes flow, a linearised form of the Navier Stokes equation. A Stokes equation is an equation[s] of Stokes flow, a linearised form of the Navier Stokes equation. equation of Stokes flow Stokes equation HOIP_0050428 A Stokes equation is an equation[s] of Stokes flow, a linearised form of the Navier Stokes equation. http://en.wikipedia.org/wiki/Stokes_equation HOIP:HOIP_0050430 The quality of fluid flow the fluids (liquids and gases) in motion. fluid dynamics quality HOIP_0050430 HOIP:HOIP_0050431 A model is a representation of some thing. model HOIP_0050431 HOIP:HOIP_0050437 A simulation is the imitation of the operation of a real-world process or system over time. Simulations require the use of models; the model represents the key characteristics or behaviors of the selected system or process, whereas the simulation represents the evolution of the model over time. Often, computers are used to execute the simulation. A simulation is the imitation of the operation of a real-world process or system over time. Simulations require the use of models; the model represents the key characteristics or behaviors of the selected system or process, whereas the simulation represents the evolution of the model over time. Often, computers are used to execute the simulation. simulation HOIP_0050437 A simulation is the imitation of the operation of a real-world process or system over time. Simulations require the use of models; the model represents the key characteristics or behaviors of the selected system or process, whereas the simulation represents the evolution of the model over time. Often, computers are used to execute the simulation. https://en.wikipedia.org/wiki/Simulation HOIP:HOIP_0050440 Organelle dynamics model is a dynamics model that mathematically describes features of the motions of organelles. organelle dynamics model HOIP_0050440 HOIP:HOIP_0050441 male pronuclear migration model is a dynamics model that mathematically describes features of the motions of male pronucleus. male pronuclear migration model in the one-cell embryo dependent process in C.elegans HOIP_0050441 HOIP:HOIP_0060001 aging related disease course HOIP_0060001 HOIP:HOIP_0060002 Under construction aging related disease HOIP_0060002 HOIP:HOIP_0060003 cardiovascular disease associated with aging HOIP_0060003 HOIP:HOIP_0060004 ischemic heart disease associated with aging HOIP_0060004 HOIP:HOIP_0060005 heart failure associated with aging HOIP_0060005 HOIP:HOIP_0060006 arteriosclerosis associated with aging HOIP_0060006 HOIP:HOIP_0060007 hypertension associated with aging HOIP_0060007 HOIP:HOIP_0060008 low blood pressure associated with aging HOIP_0060008 HOIP:HOIP_0060009 metabolic disease associated with aging HOIP_0060009 HOIP:HOIP_0060010 respiratory disease associated with aging HOIP_0060010 HOIP:HOIP_0060011 diabetes associated with aging HOIP_0060011 HOIP:HOIP_0060012 dyslipidemia associated with aging HOIP_0060012 HOIP:HOIP_0060013 pneumonia associated with aging HOIP_0060013 HOIP:HOIP_0060014 COPD associated with aging HOIP_0060014 HOIP:HOIP_0060015 osteoporosis associated with aging HOIP_0060015 HOIP:HOIP_0060016 rheumatoid arthritis associated with aging HOIP_0060016 HOIP:HOIP_0060017 hypothyroidism associated with aging HOIP_0060017 HOIP:HOIP_0060018 nervous system disease associated with aging HOIP_0060018 HOIP:HOIP_0060019 Parkinson's disease associated with aging HOIP_0060019 HOIP:HOIP_0060020 cognitive disorder associated with aging HOIP_0060020 HOIP:HOIP_0060021 The cellular senescence course-specific process is a subtype of the course-dependent process: A process that can constitute the course of cellular senescence and its subclasses. cellular senescence course-specific process HOIP_0060021 HOIP:HOIP_0060024 The totality of all processes through which cellular senescence is realized. cellular senescence course HOIP_0060024 HOIP:HOIP_0060025 Cellular morphology change is a subtype of changing shape: A process that changes the morphology of the cell. cellular morphology change HOIP_0060025 HOIP:HOIP_0060026 Cellular morphology change is a subtype of changing shape: A process that changes the morphology of the cell. cellular morphology change [cellular senescence] HOIP_0060026 HOIP:HOIP_0060027 A nucleated process having more than one nucleus. multinucleated process HOIP_0060027 HOIP:HOIP_0060028 A nucleated process having more than one nucleus. ISBN:9780815345671 multinucleated process in cellular senescence HOIP_0060028 ISBN:9780815345671 Senescent cells typically display cellular enlargement, including an increase in size of the nucleus and multinucleated cells. HOIP:HOIP_0060029 A cell that loses the ability to divide through irreversible cell cycle arrest. senescent cell HOIP_0060029 HOIP:HOIP_0060030 A role played by the cell that loses the ability to divide through irreversible cell cycle arrest. senescent cell role HOIP_0060030 HOIP:HOIP_0060032 Hypofunction of splitting is a subtype of hypofunctioning: A process that performs a decreased or insufficient splitting. hypofunction of splitting HOIP_0060032 HOIP:HOIP_0060033 Arrest of cell division is a subtype of arresting: A process that that results in the cessation of cell division. arrest of cell division HOIP_0060033 HOIP:HOIP_0060035 A symptom is a perceived change in function, sensation, loss, disturbance or appearance reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 symptom associated with aging HOIP_0060035 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060040 Hypofunction of DNA repair is a subtype of hypofunctioning: A process that performs a decreased or insufficient DNA repair. hypofunction of DNA repair HOIP_0060040 HOIP:HOIP_0060041 Hypofunction of DNA repair is a subtype of hypofunctioning: A process that performs a decreased or insufficient DNA repair. PMID:26822533 DNA修復 (low) hypofunction of DNA repair [chronic cellular senescence] HOIP_0060041 PMID:26822533 We show that unlike fibroblasts, senescent epithelial cells do not activate an ATM-or ATR-dependent DNA damage response (DDR), but accumulate oxidative-stress-induced DNA single-strand breaks (SSBs). These breaks remain unrepaired because of a decrease in PARP1 expression and activity. This leads to the formation of abnormally large and persistent XRCC1 foci that engage a signalling cascade involving the p38MAPK and leading to p16 upregulation and cell cycle arrest.Importantly, the default in SSB repair also leads to the emergence of post-senescent transformed and mutated precancerous cells. In human-aged skin, XRCC1 foci accumulate in the epidermal cells in correlation with a decline of PARP1, whereas DDR foci accumulate mainly in dermal fibroblasts. HOIP:HOIP_0060044 Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins and lengthening the telomeric DNA. telomere maintenance via telomere lengthening HOIP_0060044 HOIP:HOIP_0060048 A process that keeps the length of the object constant. keeping length HOIP_0060048 HOIP:HOIP_0060049 A process that changes the telomere length to be short. MeSH:D059506 telomere attrition telomere erosion telomere shortening HOIP_0060049 HOIP:HOIP_0060050 A process that changes the telomere length to be short. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:9780815345671 ISBN:9781437717815 PMID:10669743 PMID:33450206 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ telomere attrition telomere erosion telomere shortening [chronic cellular senescence] HOIP_0060050 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ ISBN:9780815345671 Short or uncapped telomeres arise in somatic cells after several replictive cycles. The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. ISBN:9781437717815 Telomere length is maintained by nucleotide addition mediated by an enzyme called telomerase. Telomerase is a specialized RNA protein complex that uses its own RNA as a template for adding nucleotides to the end of chromosomes. Telomerase activity is expressed in germ cells and is present at low levels in stem cells, but it is absent in most somatic cells. Therefore, as most somatic cells age their telomeres become shorter and they exit just cell cycle resulting in an inability to generate new cells to replicate damaged ones. Robbins Basic Pathology 9th ed. Chapter1 PMID:10669743 Overexpression of TRF2 results in the progressive shortening of telomere length, similar to the phenotype observed with TRF1. PMID:33450206 In 2000, further analysis of late-generation mTERC−/−;p53+/− mice (Artandi et al., 2000) revealed a humanized tumor spectrum of epithelial cancers possessing chromosomal rearrangements and nonreciprocal translocations typical of human cancer genomes. Thus, mice engineered to experience telomere-based crisis in the context of deactivated DNA damage signaling (p53 deficiency) illuminated a major mechanism driving the preponderance of epithelial cancers in aged humans and explained why such cancers develop radically altered cytogenetic profiles. PMID:33450206 Overexpression of TRF1 or deregulation of POT1 impairs telomerase binding to telomere ends, causing telomere shortening (Loayza and De Lange, 2003; Smogorzewska et al., 2000) https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ Telomere Erosion jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig1.jpg HOIP:HOIP_0060051 Hypofunction of telomere maintenance in response to DNA damage is a subtype of hypofunctioning: A process that performs a decreased or insufficient telomere maintenance in response to DNA damage. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. WikiPathway:WP3565 hypofunction of telomere maintenance in response to DNA damage [chronic cellular senescence] HOIP_0060051 HOIP:HOIP_0060052 Hypofunction of telomere maintenance in response to DNA damage is a subtype of hypofunctioning: A process that performs a decreased or insufficient telomere maintenance in response to DNA damage. hypofunction of telomere maintenance in response to DNA damage HOIP_0060052 HOIP:HOIP_0060053 A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:978081534567 PMID:35165420 cell cycle arrest (sustained) [chronic cellular senescence] HOIP_0060053 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:35165420 As telomeres reach a critical length, they become unable to bind enough telomere-capping proteins and are sensed as exposed DNA ends, which activates the DDR pathways that, through the induction of the cell cycle inhibitors p21 and p16, arrest proliferation. Such short telomeres, however, retain a sufficient number of telomere-binding proteins to inhibit DNA repair and avoid fusions, and consequently fuel a persistent DNA damage signal that enforces a permanent DNA damage-induced proliferative arrest. HOIP:HOIP_0060054 A series of molecular signals transduced with the regulation of transcription of target genes by p16. p16 signaling pathway HOIP_0060054 HOIP:HOIP_0060055 P53 signaling is a process that a signal is transmitted by the p53. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:978081534567 p53 signaling [adult cellular senescence] HOIP_0060055 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060065 Regulation of gene expression by p53 is a subtype of regulation of gene expression: Any process that modulates the frequency, rate or extent of gene expression. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24848057 regulation of gene expression by p53 [adult cellular senescence] HOIP_0060065 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060066 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. regulation of cell cycle [cellular senescence] HOIP_0060066 HOIP:HOIP_0060069 Ensembl: ENSG00000123374 HGNC:1771 NCBI-Human-GeneID:1017 UniProtKB:P24941 cell division protein kinase 2 (human) cyclin-dependent kinase 2 (human) p33 protein kinase (human) hCDK2 HOIP_0060069 NCBI-Human-GeneID:1017 http://view.ncbi.nlm.nih.gov/gene/1017 HOIP:HOIP_0060072 cyclin E1-CDK2 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin E1-CDK2 complex to be lower. cyclin E1-CDK2 complex inactivation HOIP_0060072 HOIP:HOIP_0060073 Cyclin E1-CDK2 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin E1-CDK2 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24848057 cyclin E1-CDK2 complex inactivation [cellular senescence] HOIP_0060073 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. HOIP:HOIP_0060074 RB activation is a subtype of molecular activation: A process that changes the activity of the RB ( protein kinase C) to be higher. RB activation HOIP_0060074 HOIP:HOIP_0060077 RB activation is a subtype of molecular activation: A process that changes the activity of the RB ( protein kinase C) to be higher. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 RB activation (sustained) [chronic cellular senescence] HOIP_0060077 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060080 A role played by the entity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. IMR:0000424 (obsolete) related molecular function GO:0003713 transcription corepressor HOIP_0060080 HOIP:HOIP_0060083 Any signalling pathway that decreases or inhibits the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:978081534567 negative regulation of cell cycle G1/S phase transition [cellular senescence] HOIP_0060083 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060086 A process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). arrest of cell cycle progression cessation of cell cycle termination of cell cycle cell cycle arrest HOIP_0060086 HOIP:HOIP_0060088 Arrest of nuclear DNA replication is a subtype of arresting: A process that results in the cessation of a nuclear DNA replication. arrest of nuclear DNA replication HOIP_0060088 HOIP:HOIP_0060090 Any process that stops, prevents or reduces the frequency, rate or extent of nuclear cell cycle DNA replication. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. down regulation of DNA replication involved in S phase negative regulation of nuclear cell cycle DNA replication [cellular senescence] HOIP_0060090 HOIP:HOIP_0060091 Mitochondrial dysfunction is a subtype of dysfunctioning: A process that performs an abnormal and incomplete mitochondrial function. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:29114066 PMID:33328614 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ mitochondrial dysfunction [chronic cellular senescence] HOIP_0060091 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ PMID:29114066 Telomere damage, epigenetic dysregulation, DNA damage, and mitochondrial dysfunction are primary drivers of damage in aging. Several of these drivers of damage can induce senescence. Senescence can in turn drive the consequential aging hallmarks in response to damage: stem cell exhaustion and chronic inflammation. Other responses to damage, such as proteostatic dysfunction and nutrient signaling disruption, are also integrally linked with the senescence response. PMID:29114066 senescent cells display decreased mitophagy, resulting in an “old,” defective mitochondrial network that may contribute to metabolic dysfunction in age. PMID:33328614 Increased oxidative stress in senescent cells has been linked to the accumulation of dysfunctional mitochondria. Indeed, senescent cells are characterized by changes in mitochondrial mass, membrane potential and mitochondrial morphology. Dysfunctional mitochondria may play an important role in senescence establishment, as depletion of mitochondrial sirtuins, a group of evolutionarily conserved proteins that regulate ageing across different species, as well as selective chemical inhibition of mitochondrial function, triggers senescence. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ Mitochondrial dysfunction https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig1.jpg jpg HOIP:HOIP_0060092 P16 signaling is a process that a signal is transmitted by the p16. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. ISBN:978081534567 PMID:24848057 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ p16 signaling (transient) [acute cellular senescence] HOIP_0060092 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ p16 jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig2.jpg HOIP:HOIP_0060093 P16 signaling is a process that a signal is transmitted by the p16. p16 signaling HOIP_0060093 HOIP:HOIP_0060094 Cyclin D-CDK4/6 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin D-CDK4/6 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24848057 PMID:26646499 PMID:29114066 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ Cyclin D-CDK4/6 complex inactivation [cellular senescence] HOIP_0060094 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. PMID:26646499 Embryonic senescence is noncanonical, whereby an arrest maintained by p21 or the alternative CDK4 and CDK6 inhibitor p15Ink4b drives tissue patterning without involvement of p16Ink4a PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. HOIP:HOIP_0060095 Decreaing stem cell is a subtype of decreasing number of cells: A process that becomes smaller in number of stem cell. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence PMID:29114066 PMID:33328614 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ decreasing stem cell [chronic cellular senescence] stem cell exhaustion HOIP_0060095 PMID:29114066 Senescence also influences the integrative aging hallmarks. Somatic multipotent stem cells facilitate tissue homeostasis; for example, hematopoietic stem cells (HSCs) renew the blood system. Stem cell exhaustion occurs with age, and the consequent decline in stem cell functionality and their capacity for renewal leads to tissue deterioration. For example, HSCs display a decreased success rate of transplantation when isolated from elderly patients (Kollman et al., 2001). This decline correlates with increased numbers of senescent HSCs (Chang et al., 2016) and diminished immunity (Geiger and Van Zant, 2002), decreased numbers of naive B and T cells (Min et al., 2005), and reduced natural killer cell activity (Mocchegiani and Malavolta, 2004). Somatic stem cell decline is not limited to high-turnover tissues. Neural stem cells (NSCs) experience reduced functionality, with limited neurogenesis capacity with age. This is marked by a twofold reduction in NSC numbers and a decreased proliferation, which correlates with increased expression of senescence markers in the regions where NSCs reside (Molofsky et al., 2006). Mesenchymal stem cells (Raggi and Berardi, 2012) and their descendants, satellite cells (Shefer et al., 2006; Lavasani et al., 2012; Sousa-Victor et al., 2014), chondrocytes (Loeser, 2009), adipocytes (Tchkonia et al., 2010), and osteoclasts (Chung et al., 2014), also display a reduced ability to self-renew with age that correlates with increased levels of senescence markers. This may have an impact in age-associated pathologies such as sarcopenia, cachexia, osteoporosis, and osteoarthritis (Fried et al., 2001). PMC:5748990 PMID:29114066 Telomere damage, epigenetic dysregulation, DNA damage, and mitochondrial dysfunction are primary drivers of damage in aging. Several of these drivers of damage can induce senescence. Senescence can in turn drive the consequential aging hallmarks in response to damage: stem cell exhaustion and chronic inflammation. Other responses to damage, such as proteostatic dysfunction and nutrient signaling disruption, are also integrally linked with the senescence response. PMC:5748990 PMID:33328614 When stem or progenitor cells enter senescence due to upregulation of the cell cycle inhibitory proteins, such as p16 and p21, they can no longer perform their function in supporting tissues by providing new cells, thus limiting tissue regenerative potential. Senescent cells also promote reprograming to an embryonic state, at least partially through IL-6. The reprograming, on one hand, can support tissue regeneration and, on the other hand, favours tumour development. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ Stem cell exahstion jpg HOIP:HOIP_0060096 Cyclin D-CDK4/6 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin D-CDK4/6 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. Cyclin D-CDK4/6 complex inactivation HOIP_0060096 HOIP:HOIP_0060097 Arrest of nuclear DNA replication is a subtype of arresting: A process that results in the cessation of a nuclear DNA replication. arrest of nuclear DNA replication [cellular senescence] HOIP_0060097 HOIP:HOIP_0060098 Arrest of cell division is a subtype of arresting: A process that that results in the cessation of of cell cycle G1/S phase transition. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. arrest of cell cycle G1/S phase transition [cellular senescence] HOIP_0060098 HOIP:HOIP_0060099 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:9780071802154 PMID:24449267 PMID:24848057 ROS biosynthetic process [cellular senescence] reactive oxygen species biosynthetic process [adult cellular senescence] HOIP_0060099 ISBN:9780071802154 Oxidants are oxygen-based free-radicals that include the hydroxyl free radical, superoxide, and hydrogen peroxide. Most cellular oxidants are generated by mitochondria during the production of ATP from oxygen. It is now established that old age in most species is associated with oxidative stress, for example to DNA (8-hydroxyguanosine derivatives), proteins (carbonyls), lipids (lipoperoxides, malondialdehydes), and prostaglandins (isoprostanes). Harrison's principles of internal medicine., 19th ed. New York : McGraw Hill Education, 2015 Chapter 94e, The biology of aging. PMID:24449267 However, RNAi-mediated depletion of LMNB1 appears to be associated with reduced cell proliferation to various degrees in most (Shimi et al. 2011; Dreesen et al. 2013; Sadaie et al. 2013; Shah et al. 2013). Shimi et al. (2011) showed that depletion of LMNB1 is sufficient to induce senescence through modulation of reactive oxygen species (ROS) production. Perhaps paradoxically, they showed that depletion of LMNB1 leads to a reduction of ROS in a p53-depenent manner. Similarly, Barascu et al. (2012) showed that increased levels of LMNB1 are associated with ROS up-regulation and senescence. Generally, ROS is thought to be a cause of cellular damage, and it has been shown that ROS is increased during senescence. Furthermore, high levels of exogenous oxidative stress can induce senescence (Passos et al. 2007). However, increasing evidence suggests that modest levels of ROS can also contribute to cellular proliferation and survival (Sena and Chandel 2012). Thus, alterations in LMNB1 might contribute to a fine-tuning of ROS levels. PMID:24848057 For example, DNA damage initially halts cell-cycle progression through p53-mediated induction of p21, but if lesions persist, this activates p16Ink4a through p38-MAPK-mediated mitochondrial dysfunction and ROS production. In certain cases, the SASP is dependent on persistent DNA damage signalling, such as that created through a positive feedback loop between DDR signalling and ROS. Both types of DDR signalling were found to cause mitochondrial dysfunction and production of ROS which led to new DNA damage and continued DDR signalling. Consistent with this, primary human fibroblasts overexpressing p16Ink4a or p21 undergo senescent growth arrest but fail to activate the DDR and do not produce a SASP. Importantly, several senescence-inducing stimuli produce SASPs independent of DNA damage, implying the existence of DDR-independent mechanisms. HOIP:HOIP_0060100 Arrest of cell division is a subtype of arresting: A process that that results in the cessation of of cell cycle G1/S phase transition. arrest of cell cycle G1/S phase transition HOIP_0060100 HOIP:HOIP_0060101 ATM signaling is a process that a signal is transmitted by ATM. ATM signaling HOIP_0060101 HOIP:HOIP_0060102 The release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:9780815345671 PMID:23140366 PMID:29114066 PMID:33328614 senescence-associated secretory phenotype (SASP) factor secretion (sustained) [chronic cellular senescence] HOIP_0060102 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID:23140366 In addition, some SASP factors induce an epithelial-to-mesenchymal transition in susceptible cells; others (for example, SFRP1, GROα, and IL-6) can alter stem cell proliferation or differentiation or modify stem cell niches. PMID:23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. PMID:29114066 Besides growth arrest, the production of a complex mixture of secreted factors, termed the SASP or senescence-messaging secretome, is the most relevant phenotypic program implemented in senescent cells. Senescent cells secrete hundreds of factors that include proinflammatory cytokines, chemokines, growth factors, and proteases (Kuilman and Peeper, 2009; Coppé et al., 2010). PMID:29114066 The SASP is responsible for many of the positive and negative functions attributed to senescent cells (Fig. 3) (Kuilman and Peeper, 2009). One of the major functions of the SASP is to recruit the immune system to eliminate senescent cells. The SASP mediates the activation and recruitment of both adaptive and innate immune cells (Xue et al., 2007; Kang et al., 2011). In general terms, the effects are positive. During tumor initiation, SASP-mediated immune recruitment acts as an extrinsic tumor suppressor mechanism (Xue et al., 2007; Kang et al., 2011), and the recruitment of macrophages is a key step in fibrosis resolution (Krizhanovsky et al., 2008). In contrast, SASP-mediated recruitment of immature myeloid cells has immune suppressive effects on prostate and liver cancer (Di Mitri et al., 2014; Eggert et al., 2016). In addition, the SASP can stimulate tumorigenesis by promoting angiogenesis (e.g., via VEGF and CCL5; Coppé et al., 2006; Eyman et al., 2009) or tumor growth (e.g., via GROα and Osteopontin; Krtolica et al., 2001; Pazolli et al., 2009), among other mechanisms. Specific components of the SASP have other physiological functions, such as contributing to fibrotic tissue remodeling, whereby matrix metalloproteinases (MMPs) contribute to degrade fibrotic plaques in the ECM that may be beneficial in the context of liver fibrosis and wound healing (Krizhanovsky et al., 2008; Demaria et al., 2014). PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. PMID:33328614 Senescence-associated secretory phenotype (SASP) activation is a dynamic process that accompanies cell cycle exit initiated by senescence triggers. A core SASP programme comprises mainly proinflammatory interleukin-6 (IL-6), IL-8 and monocyte chemoattractant protein 1 (MCP1), regulated in an IL-1-dependent manner, and enzymes involved in extracellular matrix (ECM) remodelling, such as matrix metalloproteinases (MMPs), serine/cysteine proteinase inhibitors (SERPINs) and tissue inhibitors of metalloproteinases (TIMPs). More recently, additional core SASP effectors released as soluble molecules or in exosomes were identified, including GDF15, STC1 and MMP1. HOIP:HOIP_0060103 A cyclin D1:Cdk6 whose components are encoded in the genome of human. cyclin D1:Cdk6 (human) HOIP_0060103 HOIP:HOIP_0060104 Loss of telomere maintenance via telomeraseis a subtype of loss of function (process): A process that results in no longer having a loss of telomere maintenance function via telomerase or the process that gradually loses it. loss of telomere maintenance via telomerase HOIP_0060104 HOIP:HOIP_0060107 Loss of telomere maintenance via telomerase is a subtype of loss of function (process): A process that results in no longer having a loss of telomere maintenance function via telomerase in human somatic cells. loss of telomere maintenance via telomeraseis in somatic cell HOIP_0060107 HOIP:HOIP_0060108 Loss of telomere maintenance via telomerase is a subtype of loss of function (process): A process that results in no longer having a loss of telomere maintenance function via telomerase in human somatic cells. ISBN:9781437717815 loss of telomere maintenance via telomeraseis in somatic cell [chronic cellular senescence] HOIP_0060108 ISBN:9781437717815 Telomere length is maintained by nucleotide addition mediated by an enzyme called telomerase. Telomerase is a specialized RNA protein complex that uses its own RNA as a template for adding nucleotides to the end of chromosomes. Telomerase activity is expressed in germ cells and is present at low levels in stem cells, but it is absent in most somatic cells. Therefore, as most somatic cells age their telomeres become shorter and they exit just cell cycle resulting in an inability to generate new cells to replicate damaged ones. Robbins Basic Pathology 9th ed. Chpter1 HOIP:HOIP_0060109 Repeating is a subtype of changing temporal distribution: A process that repeats the process. A process that occurs repetitively. repeating HOIP_0060109 HOIP:HOIP_0060110 ATM signaling is a process that a signal is transmitted by ATM. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24848057 ATM signaling [adult cellular senescence] HOIP_0060110 PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS). What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. HOIP:HOIP_0060112 A process that replaces tissues to fibrous connective tissues. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 PMID:29114066 http://purl.obolibrary.org/obo/MPATH_181 fibrosis [chronic cellular senescence] HOIP_0060112 PMID:24848057 SASP components, including IL-6 and IL-8, may stimulate tissue fibrosis in certain epithelial tissues by inducing EMT. PMID:29114066 Secretion of MMPs, which occurs as part of the SASP, could help in the resolution of fibrotic plaques (Craig et al., 2015). Conversely, fibroblasts and tissues isolated from IPF patients display increased levels of SA-β-Gal staining and p21CIP1, suggesting a link with senescence (Yanai et al., 2015; Schafer et al., 2017). The detrimental nature of senescence in IPF was recently demonstrated using senolytics. Elimination of senescent fibroblasts in a mouse model of lung fibrosis reduced expression of profibrotic SASP components and improved pulmonary function (Schafer et al., 2017). HOIP:HOIP_0060113 Chronic inflammatory response is a subtype of the inflammatory response: A process of chronic defensive reactions (by vertebrate tissues) to infection or injury. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. chronic inflammation [chronic cellular senescence] HOIP_0060113 HOIP:HOIP_0060114 A process that changes the temporal distribution pattern of process occurrences within a regulation/reference process. changing temporal distribution HOIP_0060114 HOIP:HOIP_0060115 Changing prossual quality is a subtype of changing an operand: A process that changes the quality of the process. changing processual quality HOIP_0060115 HOIP:HOIP_0060116 Increasing number of cell division is a subtype of increasing number of actions: A process that becomes larger in the number of the cell division. increasing number of cell division HOIP_0060116 HOIP:HOIP_0060117 Increasing number of cell division is a subtype of increasing number of actions: A process that becomes larger in the number of the cell division. This process can constitute the course of chronic cellular senescence. increasing number of cell division [chronic cellular senescence] HOIP_0060117 HOIP:HOIP_0060118 Increasing cell size is a subtype of increasing size: A process that changes the size of the cell to be larger. increasing cell size HOIP_0060118 HOIP:HOIP_0060119 Increasing cell size is a subtype of increasing size: A process that changes the size of the cell to be larger. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:9780815345671 increasing cell size [cellular senescence] HOIP_0060119 ISBN:9780815345671 Senescent cells typically display cellular enlargement, including an increase in size of the nucleus and multinucleated cells. Biology of Aging 2nd Ed. Chapter 4, cellular aging HOIP:HOIP_0060120 Increasing distance between cells is a subtype of increasing distance: A process that places a distance between cells. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:9780815345671 Increasing distance between cells [cellular senescence] HOIP_0060120 ISBN:9780815345671 The distance between cells becomes greater due to an increase in the cellular secretion of extracellular matrix proteases and collagenase. Biology of Aging 2nd Ed. Chapter 4, cellular aging HOIP:HOIP_0060121 The chemical reaction resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:9780071802154 ATP biosynthetic process [adult cellular senescence] HOIP_0060121 ISBN:9780071802154 Oxidants are oxygen-based free-radicals that include the hydroxyl free radical, superoxide, and hydrogen peroxide. Most cellular oxidants are generated by mitochondria during the production of ATP from oxygen. It is now established that old age in most species is associated with oxidative stress, for example to DNA (8-hydroxyguanosine derivatives), proteins (carbonyls), lipids (lipoperoxides, malondialdehydes), and prostaglandins (isoprostanes). Harrison's principles of internal medicine., 19th ed. New York : McGraw Hill Education, 2015 Chapter 94e, The biology of aging. HOIP:HOIP_0060122 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. increasing oxidative stress [adult cellular senescence] HOIP_0060122 HOIP:HOIP_0060125 A process that keeps senescent cell in an organism, tissue or cell. accumulation of senescent cell HOIP_0060125 HOIP:HOIP_0060126 Cellular membrane lipoperoxidation is a subtype of lipoperoxidation: A process that the degradation of lipids of cellular membrane caused by an oxidative attack from free radicals. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. phospholipid peroxidation in mitochondrial membrane [chronic cellular senescence] HOIP_0060126 HOIP:HOIP_0060127 Accumulation of misfolded/unfolded protein is a subtype of accumulation of abnormal proteins: A process that keeps misfolded or unfolded protein(s). This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:9780815345671 accumulation of unfolded/mifolded protein [adult cellular senescence] HOIP_0060127 ISBN:9780815345671 It seems that proteins involved in the removal of damaged proteins from the cell are also affected by ROS. That is, accumulation of damaged proteins is exacerbated by a decline in the function of waste removal by the cell. Biology of Aging 2nd Ed. Chapter 4, cellular aging HOIP:HOIP_0060128 A process that changes the fluidity of the membrane. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. mitochondrial membrane fluidity change [chronic cellular senescence] HOIP_0060128 HOIP:HOIP_0060129 A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. Cellular senescence represents a cell fate that is characterized by stable proliferative arrest in response to various stressors. PMID:29114066 PMID:31675495 PMID:33328614 cellular senescence [cellular senescence course] HOIP_0060129 Cellular senescence represents a cell fate that is characterized by stable proliferative arrest in response to various stressors. PMID:31674195 PMID:29114066 Senescence, a cellular response that limits the proliferation of aged or damaged cells (Muñoz-Espín et al., 2013; Muñoz-Espín and Serrano, 2014), belongs to the antagonistic class (Fig. 1). Although senescence plays physiological roles during normal development and it is needed for tissue homeostasis, senescence constitutes a stress response triggered by insults associated with aging such as genomic instability and telomere attrition, which are primary aging hallmarks themselves. There is also an intimate link between senescence and the other antagonistic hallmarks of aging. PMID:31675495 Cellular senescence is a cell state triggered by stressful insults and certain physiological processes, characterized by a prolonged and generally irreversible cell-cycle arrest with secretory features, macromolecular damage, and altered metabolism. PMID:33328614 Besides prolonged DDR activation, senescence features include cell cycle arrest (by upregulation of p21 and p16 cell cycle inhibitors), oxidative damage (as detected by increased ROS levels), upregulation of the BCL-2 family of antiapoptotic proteins, which induce resistance to apoptosis, metabolic changes (including senescence-associated-β-galactosidase (SA-β-gal) accumulation), senescence-associated heterochromatin foci (SAHF) and a senescence-associated secretory phenotype (SASP). HOIP:HOIP_0060130 Any process that activates or increases the frequency, rate or extent of reactive oxygen species biosynthetic process. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24449267 positive regulation of reactive oxygen species biosynthetic process [adult cellular senescence] HOIP_0060130 PMID:24449267 However, RNAi-mediated depletion of LMNB1 appears to be associated with reduced cell proliferation to various degrees in most (Shimi et al. 2011; Dreesen et al. 2013; Sadaie et al. 2013; Shah et al. 2013). Shimi et al. (2011) showed that depletion of LMNB1 is sufficient to induce senescence through modulation of reactive oxygen species (ROS) production. Perhaps paradoxically, they showed that depletion of LMNB1 leads to a reduction of ROS in a p53-depenent manner. Similarly, Barascu et al. (2012) showed that increased levels of LMNB1 are associated with ROS up-regulation and senescence. Generally, ROS is thought to be a cause of cellular damage, and it has been shown that ROS is increased during senescence. Furthermore, high levels of exogenous oxidative stress can induce senescence (Passos et al. 2007). However, increasing evidence suggests that modest levels of ROS can also contribute to cellular proliferation and survival (Sena and Chandel 2012). Thus, alterations in LMNB1 might contribute to a fine-tuning of ROS levels. HOIP:HOIP_0060131 A process that results in the breakdown of things in lysosomes. degradation in lysosome HOIP_0060131 HOIP:HOIP_0060132 A process that results in the breakdown of LMNB1 in the lysosomes. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:31675495 PMID:33328614 LMNB1degradation in lysosome [chronic cellular senescence] HOIP_0060132 PMID:33328614 PMID:31675495 Downregulation of lamin B1, a major component of the nuclear lamina, is another key feature of senescence (Dou et al., 2015, Freund et al., 2012, Shah et al., 2013, Shimi et al., 2011). Lamin B1 loss correlates with epigenetic profiles (Salama et al., 2014), as well as senescence-associated chromatin structures (SAHFs and SADSs) (Salama et al., 2014, Swanson et al., 2013). Its reduction occurs predominantly at H3K9me3-rich regions, a process that appears to liberate H3K9me3 from the nuclear lamina promoting spatial rearrangement of H3K9me3 heterochromatin to form SAHFs (Salama et al., 2014). Hi-C analysis (genome-wide mapping of chromatin contacts) in OIS revealed a reduction in local connectivity at regions enriched for H3K9me3 and lamin B1, perturbing these long-range interactions (Chandra et al., 2015). Replicative senescence, on the other hand, showed loss of long-range and gain of short-range interactions within chromosomes (Criscione et al., 2016), implying that the nature of senescence-associated high-order chromatin interactions is stimulus and context dependent (Zirkel et al., 2018). Furthermore, lamin B1 loss and reduced nuclear integrity is suggested to fuel the SASP by contributing to CCF formation (Dou et al., 2015, Ivanov et al., 2013), thereby stimulating the cGAS-STING pathway and interferon response (see Secretion) (Li and Chen, 2018). Autophagy-mediated CCF formation (Dou et al., 2015) together with reduced histone synthesis (O’Sullivan et al., 2010) might also lead to a global loss of core histones during senescence, affecting the chromatin landscape (Chan and Narita, 2019, Ivanov et al., 2013). PMID:33328614 Indeed, it was reported that a selective autophagy pathway, via mammalian target of rapamycin (mTOR) activation, contributes to sustain the protein synthesis of many senescence-associated secretory phenotype factors mainly in oncogene-induced senescent cells and that downregulation of several autophagy regulators delays the establishment of oncogene-induced senescence. more recently, LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. Inhibition of autophagy prevents lamin B1 degradation and ensures nuclear envelope integrity in senescent cells. HOIP:HOIP_0060133 Transgenic mouse model with drug-inducible caspase 8 under the control of a minimal p16 promoter element active in senescent cells to allow selective elimination of p16-expressing senescent cells. Transgenic mouse model with drug-inducible caspase 8 under the control of a minimal p16 promoter element active in senescent cells to allow selective elimination of p16-expressing senescent cells. PMID:33328614 INK-ATTAC HOIP_0060133 Transgenic mouse model with drug-inducible caspase 8 under the control of a minimal p16 promoter element active in senescent cells to allow selective elimination of p16-expressing senescent cells. PMID:33328614 HOIP:HOIP_0060135 Catalysis role of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. metalloendopeptidase role HOIP_0060135 HOIP:HOIP_0060136 NfkB signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by NF-kappaB. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 Wikipedia:NF-κB NfkB signaling [chronic cellular senescence] HOIP_0060136 PMID:33328614 NF-κB and the transcription factor CCAAT/enhancer-binding protein-β (C/EBPβ) bind promoters of SASP genes and regulate their activation. Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. Because GATA4 levels increase following DDR activation and in senescent cells, it was proposed that GATA4 acts as the molecular link between DDR signalling and the subsequent NF-κB activation for full SASP establishment, although GATA4 regulation of the NF-κB pathway happens indirectly through increased expression and secretion of IL-1α, an upstream regulator of NF-κB. Wikipedia:NF-κB NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) is a protein complex that controls transcription of DNA, cytokine production and cell survival. HOIP:HOIP_0060137 Inflammatory gene expression by NF-kappa B is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the inflammation by NF-kappa B. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 SASP related protein expression by NF-kappa B [chronic cellular senescence] HOIP_0060137 PMID:33328614 NF-κB and the transcription factor CCAAT/enhancer-binding protein-β (C/EBPβ) bind promoters of SASP genes and regulate their activation. Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. Because GATA4 levels increase following DDR activation and in senescent cells, it was proposed that GATA4 acts as the molecular link between DDR signalling and the subsequent NF-κB activation for full SASP establishment, although GATA4 regulation of the NF-κB pathway happens indirectly through increased expression and secretion of IL-1α, an upstream regulator of NF-κB. HOIP:HOIP_0060138 Transgenic mouse model expressing a trimodal reporter of red fluorescent protein, luciferase and herpes simplex virus thymidine kinase under the control of the p16 promoter to allow tracking and elimination of p16-expressing senescent cells. Transgenic mouse model expressing a trimodal reporter of red fluorescent protein, luciferase and herpes simplex virus thymidine kinase under the control of the p16 promoter to allow tracking and elimination of p16-expressing senescent cells. PMID:33328614 p16-3MR HOIP_0060138 Transgenic mouse model expressing a trimodal reporter of red fluorescent protein, luciferase and herpes simplex virus thymidine kinase under the control of the p16 promoter to allow tracking and elimination of p16-expressing senescent cells. PMID:33328614 HOIP:HOIP_0060139 Model that is a representation of senescence or aging. senescence model HOIP_0060139 HOIP:HOIP_0060140 ATR signaling is a process that a signal is transmitted by ATR. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24848057 PMID:33328614 ATR signaling [adult cellular senescence] HOIP_0060140 PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS). What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:33328614 At the bottom of the DDR cascade, the tumour suppressor p53, which is a target of ATM and its paralogue ATR, is activated and stimulates the expression of the cyclin-dependent kinase inhibitor p21, an essential mediator of senescence-associated cell cycle arrest. p16, an inhibitor of CDK4 and CDK6, is also key in several types of senescence; p21 is activated early on senescence entry and p16 is activated later, probably to maintain the senescence phenotype. HOIP:HOIP_0060141 ATR signaling is a process that a signal is transmitted by ATR. ATR signaling HOIP_0060141 HOIP:HOIP_0060142 Catalysis role of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. metallopeptidase HOIP_0060142 HOIP:HOIP_0060143 CHK signaling is a process that a signal is transmitted by CHK. CHK signaling HOIP_0060143 HOIP:HOIP_0060144 CHK1 signaling is a process that a signal is transmitted by CHK1. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 CHK1 signaling [adult cellular senescence] HOIP_0060144 PMID:33328614 Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. HOIP:HOIP_0060145 CHK2 signaling is a process that a signal is transmitted by CHK2. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 CHK2 signaling [adult cellular senescence] HOIP_0060145 PMID:33328614 Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. HOIP:HOIP_0060146 An NF-kappaB p50/p65 complex whose components are encoded in the genome of human. NFKBp50:RelA NF-kB complex (human) NF-kappaB p50/p65 complex (human) HOIP_0060146 HOIP:HOIP_0060147 A nuclear factor NF-kappa-B p50 subunit in human. p50 UniProtKB:P19838-1 NF-KAPPA-B P50 (human) NFKB1 p50 (human) nuclear factor NF-kappa-B p50 subunit (human) P19838-1, 1-433 hNFKBp50 HOIP_0060147 HOIP:HOIP_0060148 Any process that activates or increases the frequency, rate or extent of NfkB signaling. positive regulation of NfkB signaling HOIP_0060148 HOIP:HOIP_0060149 Any process that activates or increases the frequency, rate or extent of signaling. positive regulation of signaling HOIP_0060149 HOIP:HOIP_0060150 CHK1 signaling is a process that a signal is transmitted by CHK1. This entity is a specific course-dependent process. Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. CHK1 signaling HOIP_0060150 Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. PMID:33328614 HOIP:HOIP_0060151 CHK2 signaling is a process that a signal is transmitted by CHK2. Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. CHK2 signaling HOIP_0060151 Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. PMID:33328614 HOIP:HOIP_0060152 Any process that activates or increases the frequency, rate or extent of NfkB signaling. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 positive regulation of NfkB signaling [chronic cellular senescence] HOIP_0060152 PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. Because GATA4 levels increase following DDR activation and in senescent cells, it was proposed that GATA4 acts as the molecular link between DDR signalling and the subsequent NF-κB activation for full SASP establishment, although GATA4 regulation of the NF-κB pathway happens indirectly through increased expression and secretion of IL-1α, an upstream regulator of NF-κB. HOIP:HOIP_0060153 Dynamic structural changes to eukaryotic chromatin occurring throughout the cell division cycle. These changes range from the local changes necessary for transcriptional regulation to global changes necessary for chromosome segregation. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24848057 chromatin remodeling [chronic cellular senescence] HOIP_0060153 PMID:24848057 For the progression to full senescence, it seems that lamin B1 downregulation triggers both global and local modifications in chromatin methylation (Fig. 2). Some mammalian cell types form regions of highly condensed chromatin called senescence-associated heterochromatin foci (SAHFs) . SAHFs, which are enriched in chromatin modifications such as S83-HP1γ, HIRA, ASF1, macroH2A, H3K9me3 and γH2AX, sequester genes implicated in cell-cycle control, a phenomenon that seems to reinforce the senescence-associated growth arrest. Decondensation of (peri)centromeric satellite heterochromatin has been identified as a universal hallmark of senescence that precedes SAHF formation. Senescence-related chromatin remodelling leads to profound transcriptional changes. Among the assortment of upregulated genes is a prominent subset of genes that encode secreted proteins, including cytokines and chemokines with proinflammatory properties, as well as various growth factors and proteases that together alter tissue structure and function. Collectively, these factors are referred to as the senescence-associated secretory phenotype (SASP) or senescence-messaging secretome (SMS). PMID:24848057 The resulting early senescent cells progress to full senescence by downregulating lamin B1, thereby triggering extensive chromatin remodelling underlying the production of a SASP. Certain components of the SASP are highly conserved, whereas others may vary depending on cell type, nature of the senescence-inducing stressor, or cell-to-cell variability in chromatin remodelling. Progression to deep or late senescence may be driven by additional genetic and epigenetic changes, including chromatin budding, histone proteolysis and retrotransposition, driving further transcriptional change and SASP heterogeneity. HOIP:HOIP_0060154 LMNB1 activation is a subtype of molecular activation: A process that changes the activity of the LMNB1 (Lamin-B1) to be higher. LMNB1 activation HOIP_0060154 HOIP:HOIP_0060155 Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases. Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases. Other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily. matrix metallopeptidase HOIP_0060155 Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases. Wikipedia:Matrix_metalloproteinase HOIP:HOIP_0060156 The appearance of interleukin-1 alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 IL-1 alpha production interleukin-1 alpha biosynthetic process interleukin-1 alpha secretion interleukin-1 alpha production [chronic cellular senescence] HOIP_0060156 PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060157 IL-1 signaling is a process that a signal is transmitted by the cytokine IL1. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 IL-1 signaling [chronic cellular senescence] HOIP_0060157 PMID:33328614 Because GATA4 levels increase following DDR activation and in senescent cells, it was proposed that GATA4 acts as the molecular link between DDR signalling and the subsequent NF-κB activation for full SASP establishment, although GATA4 regulation of the NF-κB pathway happens indirectly through increased expression and secretion of IL-1α, an upstream regulator of NF-κB. HOIP:HOIP_0060158 p38 signaling is a process that a signal is transmitted by the p38 (a Mitogen-Activated Protein Kinase). This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:21399611 PMID:24848057 PMID:33328614 p38 signaling [chronic cellular senescence] HOIP_0060158 PMID:24848057 For example, DNA damage initially halts cell-cycle progression through p53-mediated induction of p21, but if lesions persist, this activates p16Ink4a through p38-MAPK-mediated mitochondrial dysfunction and ROS production. PMID:33328614 Indeed, the activation of the stress-inducible MAPK p38 was proven both necessary and sufficient to trigger growth arrest and SASP even in the absence of DNA damage. Like ATM, p38 induces the expression of SASP transcripts by increasing the activity of nuclear factor-κB (NF-κB), suggesting that although DDR and p38 activation are independent, they can converge on SASP activation. HOIP:HOIP_0060159 Drug-, radiation-induced, or spontaneous injuries to mitochondrial DNA that introduce deviations from its normal double-helical conformation. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:9781437717815 PMID:33450206 Mitochondrial DNA damage [chronic cellular senescence] HOIP_0060159 ISBN:9781437717815 A variety of metabolic insults that accumulate over time may result in damage to nuclear and mitochondrial DNA. Although most DNA damage is repaired by DNA repair enzymes, some persist and accumulate as cells age. Robbins Basic Pathology 9th ed. PMID:33450206 Increased oxidative stress in senescent cells has been linked to the accumulation of dysfunctional mitochondria. Indeed, senescent cells are characterized by changes in mitochondrial mass, membrane potential and mitochondrial morphology. Dysfunctional mitochondria may play an important role in senescence establishment, as depletion of mitochondrial sirtuins, a group of evolutionarily conserved proteins that regulate ageing across different species, as well as selective chemical inhibition of mitochondrial function, triggers senescence. There is evidence in support of a reciprocal influence between nuclear DNA damage and mitochondrial dysfunction. HOIP:HOIP_0060160 LMNB1 inactivation is a subtype of molecular inactivation: A process that changes the activity of the LMNB1 (Lamin-B1) to be lower. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. LMNB1 inactivation HOIP_0060160 HOIP:HOIP_0060161 A process that constructs a transcriptionally-silent heterochromatin structure present in senescent cells. SAHF formation senescence-associated heterochromatin focus formation HOIP_0060161 HOIP:HOIP_0060162 A process that constructs a transcriptionally-silent heterochromatin structure present in senescent cells. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24848057 PMID:33328614 SAHF formation senescence-associated heterochromatin focus formation [chronic cellular senescence] HOIP_0060162 For the progression to full senescence, it seems that lamin B1 downregulation triggers both global and local modifications in chromatin methylation (Fig. 2). Some mammalian cell types form regions of highly condensed chromatin called senescence-associated heterochromatin foci (SAHFs) . SAHFs, which are enriched in chromatin modifications such as S83-HP1γ, HIRA, ASF1, macroH2A, H3K9me3 and γH2AX, sequester genes implicated in cell-cycle control, a phenomenon that seems to reinforce the senescence-associated growth arrest. Decondensation of (peri)centromeric satellite heterochromatin has been identified as a universal hallmark of senescence that precedes SAHF formation. Senescence-related chromatin remodelling leads to profound transcriptional changes. Among the assortment of upregulated genes is a prominent subset of genes that encode secreted proteins, including cytokines and chemokines with proinflammatory properties, as well as various growth factors and proteases that together alter tissue structure and function. Collectively, these factors are referred to as the senescence-associated secretory phenotype (SASP) or senescence-messaging secretome (SMS). PMID:24848057 PMID:24848057 For the progression to full senescence, it seems that lamin B1 downregulation triggers both global and local modifications in chromatin methylation (Fig. 2). Some mammalian cell types form regions of highly condensed chromatin called senescence-associated heterochromatin foci (SAHFs). SAHFs, which are enriched in chromatin modifications such as S83-HP1γ, HIRA, ASF1, macroH2A, H3K9me3 and γH2AX, sequester genes implicated in cell-cycle control, a phenomenon that seems to reinforce the senescence-associated growth arrest. Decondensation of (peri)centromeric satellite heterochromatin has been identified as a universal hallmark of senescence that precedes SAHF formation. PMID:33328614 Senescence-associated heterochromatin foci (SAHF) are spatially organized heterochromatic domains that can be detected as dense 4′,6-diamidino-2-phenylindole (DAPI)-positive nuclear structures that are enriched in repressive chromatin marks and proteins, including trimethylated histone H3 Lys9 (H3K9me3), heterochromatin protein 1 (HP1), high mobility group protein A (HMGA) factors, histone variant macroH2A and histone co-chaperones HIRA and ASF1A. However, SAHF are not universal markers of senescence; they are most robustly observed upon oncogene activation and form in a DNA replication- and ATR-dependent manner. SAHF were originally proposed to repress genes promoting cell cycle progression. Rather, SAHF enforce a DDR-resistant heterochromatin structure that restrains DDR signalling. Indeed, treatment with histone deacetylase (HDAC) inhibitors, which induce chromatin relaxation, boosts DDR signalling with consequent cell death by apoptosis. This treatment is probably the first reported example of a successful senolytic approac, which was later supported by the reported senolytic activity of the HDAC inhibitor panobinostat. HDAC inhibitors can also induce cellular senescence in normal human fibroblasts, which may be related to their impact on the DDR. HOIP:HOIP_0060163 Any process that activates or increases the frequency, rate or extent of senescence-associated heterochromatin focus (SAHF) formation. positive regulation of senescence-associated heterochromatin focus formation HOIP_0060163 HOIP:HOIP_0060164 Any process that activates or increases the frequency, rate or extent of senescence-associated heterochromatin focus (SAHF) formation. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. positive regulation of senescence-associated heterochromatin focus formation [chronic cellular senescence] HOIP_0060164 HOIP:HOIP_0060165 Expression of LMNB1 is a subtype of gene expression: The process in which a gene sequence is converted into a mature LMNB1 (Lamin-B1) gene product or products (proteins or RNA). Expression of LMNB1 HOIP_0060165 HOIP:HOIP_0060166 A process that performs a decreased or insufficient LMNB1 (Lamin-B1) expression. This process can constitute the course of cellular senescence. hypofunction of expression of LMNB1 [cellular senescence] HOIP_0060166 HOIP:HOIP_0060167 A process that performs a decreased or insufficient LMNB1 (Lamin-B1) expression. This process can constitute the course of chronic cellular senescence. PMID:23964094 PMID:24848057 PMID:28759028 hypofunction of expression of LMNB1 [chronic cellular senescence] HOIP_0060167 PMID:23964094 Genome-wide mapping reveals that LMNB1 is depleted during senescence, preferentially from the central regions of lamina-associated domains (LADs), which are enriched for Lys9 trimethylation on histone H3 (H3K9me3). LMNB1 knockdown facilitates the spatial relocalization of perinuclear H3K9me3-positive heterochromatin, thus promoting SAHF formation, which could be inhibited by ectopic LMNB1 expression. Furthermore, despite the global reduction in LMNB1 protein levels, LMNB1 binding increases during senescence in a small subset of gene-rich regions where H3K27me3 also increases and gene expression becomes repressed. These results suggest that LMNB1 may contribute to senescence in at least two ways due to its uneven genome-wide redistribution: first, through the spatial reorganization of chromatin and, second, through gene repression. PMID:24848057 For the progression to full senescence, it seems that lamin B1 downregulation triggers both global and local modifications in chromatin methylation (Fig. 2). Some mammalian cell types form regions of highly condensed chromatin called senescence-associated heterochromatin foci (SAHFs). SAHFs, which are enriched in chromatin modifications such as S83-HP1γ, HIRA, ASF1, macroH2A, H3K9me3 and γH2AX, sequester genes implicated in cell-cycle control, a phenomenon that seems to reinforce the senescence-associated growth arrest. Decondensation of (peri)centromeric satellite heterochromatin has been identified as a universal hallmark of senescence that precedes SAHF formation. PMID:28759028 To assess whether the loss of nuclear integrity might itself be sufficient to activate cGAS-STING signalling, we knocked down lamin B1 with two distinct siRNAs in primary MEFs (Fig. 4e, f). Down-regulation of lamin B1 induced leakage of chromatin into the cytosol (Fig. 4g). More important, MEFs with reduced expression of lamin B1 displayed an elevated ISG response (Ifi44 induction), which was dependent on cGAS (Fig. 4e). Thus, it appears that the mere de-stabilization of the nuclear membrane is sufficient to engage cGAS. Consistent with this idea, we observed that cGAS enriched on chromatin containing blebs in cells knocked down for lamin B1 (Fig. 4g). Together, these results suggest that activation of cGAS in senescent cells is caused by its interaction with endogenous DNA arising from defective, senescent nuclei. HOIP:HOIP_0060168 P21 signaling is a process that a signal is transmitted by the p21. The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. p21 signaling HOIP_0060168 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. ISBN:978081534567 What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:24848057 p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. PMID: 33328614 HOIP:HOIP_0060169 Catalysis of the reaction: ATP + GTP = 2 diphosphate + cyclic GMP-AMP. A process that changes the activity of the cyclic GMP–AMP synthase (cGAS) to be higher. PMID:33833439 PMID:34676498 cyclic GMP-AMP synthase activity [cellular senescence] cGAS activation [chronic cellular senescence] HOIP_0060169 PMID:33833439 DNA damage or replication stress may lead to direct nuclear DNA leakage, third, in senescence, chromatin herniations can bud off the main nucleus leading to accumulation of cytoplasmic chromatin fragments (CCFs) or, alternatively, in the context of genomic instability nuclear DNA may be encapsulated in micronuclei after mitosis. Both of these latter two events can promote cGAS activity on rupture of the aberrant micro-organelle membrane. Mechanistically, cGAS was found to be enriched on cytosolic chromatin that can accumulate within senescent cells and represent a bona fide activator for cGAS in this context. As potential sources, cytosolic DNA fragments may derive from ruptured micronuclei or chromatin herniations, as a consequence of chronic DNA damage of disrupted nuclear envelope integrity, both of which are features of senescent cells. PMID:34676498 Here, we identify cGAS as an essential regulator in inhibiting mitotic DNA double-strand break (DSB) repair and protecting short telomeres from end-to-end fusion independent of the canonical cGAS-STING pathway. cGAS associates with telomeric/subtelomeric DNA during mitosis when TRF1/TRF2/POT1 are deficient on telomeres. Depletion of cGAS leads to mitotic chromosome end-to-end fusions predominantly occurring between short telomeres. Mechanistically, cGAS interacts with CDK1 and positions them to chromosome ends. Thus, CDK1 inhibits mitotic non-homologous end joining (NHEJ) by blocking the recruitment of RNF8. cGAS-deficient human primary cells are defective in entering replicative senescence and display chromosome end-to-end fusions, genome instability and prolonged growth arrest. Altogether, cGAS safeguards genome stability by controlling mitotic DSB repair to inhibit mitotic chromosome end-to-end fusions, thus facilitating replicative senescence. HOIP:HOIP_0060170 A process of tissue organization that results in the restoration of the tissue following damage. tissue repair HOIP_0060170 HOIP:HOIP_0060172 DNA damage or replication stress may lead to direct nuclear DNA leakage, third, in senescence, chromatin herniations can bud off the main nucleus leading to accumulation of cytoplasmic chromatin fragments (CCFs) or, alternatively, in the context of genomic instability nuclear DNA may be encapsulated in micronuclei after mitosis. Both of these latter two events can promote cGAS activity on rupture of the aberrant micro-organelle membrane. DNA damage or replication stress may lead to direct nuclear DNA leakage, third, in senescence, chromatin herniations can bud off the main nucleus leading to accumulation of cytoplasmic chromatin fragments (CCFs) or, alternatively, in the context of genomic instability nuclear DNA may be encapsulated in micronuclei after mitosis. Both of these latter two events can promote cGAS activity on rupture of the aberrant micro-organelle membrane. cGAS signaling is a process that a signal is transmitted by cyclic GMP–AMP synthase (cGAS) This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:28533362 PMID:28759028 cGAS signaling [chronic cellular senescence] HOIP_0060172 DNA damage or replication stress may lead to direct nuclear DNA leakage, third, in senescence, chromatin herniations can bud off the main nucleus leading to accumulation of cytoplasmic chromatin fragments (CCFs) or, alternatively, in the context of genomic instability nuclear DNA may be encapsulated in micronuclei after mitosis. Both of these latter two events can promote cGAS activity on rupture of the aberrant micro-organelle membrane. PMID:33833439 PMID:28759028 To assess whether the loss of nuclear integrity might itself be sufficient to activate cGAS-STING signalling, we knocked down lamin B1 with two distinct siRNAs in primary MEFs (Fig. 4e, f). Down-regulation of lamin B1 induced leakage of chromatin into the cytosol (Fig. 4g). More important, MEFs with reduced expression of lamin B1 displayed an elevated ISG response (Ifi44 induction), which was dependent on cGAS (Fig. 4e). Thus, it appears that the mere de-stabilization of the nuclear membrane is sufficient to engage cGAS. Consistent with this idea, we observed that cGAS enriched on chromatin containing blebs in cells knocked down for lamin B1 (Fig. 4g). Together, these results suggest that activation of cGAS in senescent cells is caused by its interaction with endogenous DNA arising from defective, senescent nuclei. PMID:28759028 We find that cyclic GMP-AMP synthase (cGAS) recognizes cytosolic chromatin fragments in senescent cells. The activation of cGAS, in turn, triggers the production of SASP factors via stimulator of interferon genes (STING), thereby promoting paracrine senescence. We demonstrate that diverse stimuli of cellular senescence engage the cGAS-STING pathway in vitro and we show cGAS-dependent regulation of senescence following irradiation and oncogene activation in vivo. HOIP:HOIP_0060173 cGAS signaling is a process that a signal is transmitted by cyclic GMP–AMP synthase (cGAS). This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. cGAS signaling HOIP_0060173 HOIP:HOIP_0060174 Any process that activates or increases the frequency, rate or extent of carcinogenesis. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:26822533 PMID:33833439 positive regulation of carcinogenesis [chronic cellular senescence] HOIP_0060174 PMID:26822533 We show that unlike fibroblasts, senescent epithelial cells do not activate an ATM-or ATR-dependent DNA damage response (DDR), but accumulate oxidative-stress-induced DNA single-strand breaks (SSBs). These breaks remain unrepaired because of a decrease in PARP1 expression and activity. This leads to the formation of abnormally large and persistent XRCC1 foci that engage a signalling cascade involving the p38MAPK and leading to p16 upregulation and cell cycle arrest.Importantly, the default in SSB repair also leads to the emergence of post-senescent transformed and mutated precancerous cells. In human-aged skin, XRCC1 foci accumulate in the epidermal cells in correlation with a decline of PARP1, whereas DDR foci accumulate mainly in dermal fibroblasts. PMID:33833439 Activation of STING initiates cascades that support anti-proliferative cell states, including cellular senescence, and ultimately cell death (a more detailed discussion of senescence is provided further below). To that end, STING promotes induction of cell-cycle inhibitors (such as p21) and pro-apoptotic BH3-only proteins. Alternatively, and in a more direct mode of action, phosphorylated IRF3 can also interact with the pro-apoptotic proteins BAX and BAK and thereby lead to transcription-independent induction of apoptosis downstream of STING. HOIP:HOIP_0060175 A series of molecular signals mediated by CGAS and STING. CGAS-STING signal transduction pathway HOIP_0060175 HOIP:HOIP_0060176 A process that performs a decreased or insufficient keeping stem cell niche. This entity is a specific course-dependent process. This process can constitute the course of celllular senescence. PMID:24848057 hypofunction of keeping stem cell niche [chronic cellular senescence] HOIP_0060176 PMID:24848057 In this way, senescence interferes with tissue homeostasis and regeneration, and lays the groundwork for its cell-non-autonomous detrimental actions involving the SASP. There are at least five distinct paracrine mechanisms by which senescent cells could promote tissue dysfunction, including perturbation of the stem cell niche (causing stem cell dysfunction), disruption of extracellular matrix, induction of aberrant cell differentiation (both creating abnormal tissue architecture), stimulation of sterile tissue inflammation, and induction of senescence in neighbouring cells (paracrine senescence). HOIP:HOIP_0060177 Any process that activates or increases the frequency, rate or extent of carcinogenesis. positive regulation of carcinogenesis HOIP_0060177 HOIP:HOIP_0060178 STING signaling is a process that a signal is transmitted by STING. STING signaling HOIP_0060178 HOIP:HOIP_0060179 STING signaling is a process that a signal is transmitted by STING. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:28759028 PMID:32424334 PMID:33328614 PMID:33833439 STING signaling [chronic cellular senescence] HOIP_0060179 PMID:28759028 To assess whether the loss of nuclear integrity might itself be sufficient to activate cGAS-STING signalling, we knocked down lamin B1 with two distinct siRNAs in primary MEFs (Fig. 4e, f). Down-regulation of lamin B1 induced leakage of chromatin into the cytosol (Fig. 4g). More important, MEFs with reduced expression of lamin B1 displayed an elevated ISG response (Ifi44 induction), which was dependent on cGAS (Fig. 4e). Thus, it appears that the mere de-stabilization of the nuclear membrane is sufficient to engage cGAS. Consistent with this idea, we observed that cGAS enriched on chromatin containing blebs in cells knocked down for lamin B1 (Fig. 4g). Together, these results suggest that activation of cGAS in senescent cells is caused by its interaction with endogenous DNA arising from defective, senescent nuclei. PMID:28759028 We find that cyclic GMP-AMP synthase (cGAS) recognizes cytosolic chromatin fragments in senescent cells. The activation of cGAS, in turn, triggers the production of SASP factors via stimulator of interferon genes (STING), thereby promoting paracrine senescence. We demonstrate that diverse stimuli of cellular senescence engage the cGAS-STING pathway in vitro and we show cGAS-dependent regulation of senescence following irradiation and oncogene activation in vivo. PMID:33328614 More recently, the DNA sensor cyclic GMP–AMP synthase (cGAS) and the adaptor stimulator of interferon genes (STING) have been reported to be major regulators of the SASP programme across species and senescence modes, presumably by activating NF-κB and interferon response factor IRF3 on recognition of cytosol DNA and cytosolic chromatin fragments (CCFs). PMID:33833439 Activation of STING initiates cascades that support anti-proliferative cell states, including cellular senescence, and ultimately cell death (a more detailed discussion of senescence is provided further below). To that end, STING promotes induction of cell-cycle inhibitors (such as p21) and pro-apoptotic BH3-only proteins. Alternatively, and in a more direct mode of action, phosphorylated IRF3 can also interact with the pro-apoptotic proteins BAX and BAK and thereby lead to transcription-independent induction of apoptosis downstream of STING. HOIP:HOIP_0060180 Any process that activates or increases the frequency, rate or extent of apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33833439 positive regulation of apoptotic process [chronic cellular senescence] HOIP_0060180 PMID:33833439 Activation of STING initiates cascades that support anti-proliferative cell states, including cellular senescence, and ultimately cell death (a more detailed discussion of senescence is provided further below). To that end, STING promotes induction of cell-cycle inhibitors (such as p21) and pro-apoptotic BH3-only proteins. Alternatively, and in a more direct mode of action, phosphorylated IRF3 can also interact with the pro-apoptotic proteins BAX and BAK and thereby lead to transcription-independent induction of apoptosis downstream of STING. HOIP:HOIP_0060181 A process that performs a decreased or insufficient keeping stem cell niche. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. hypofunction of keeping stem cell niche HOIP_0060181 HOIP:HOIP_0060182 Any process that stops, prevents, or reduces the frequency, rate or extent of tissue regeneration. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 negative regulation of tissue regeneration [chronic cellular senescence] HOIP_0060182 PMID:24848057 In this way, senescence interferes with tissue homeostasis and regeneration, and lays the groundwork for its cell-non-autonomous detrimental actions involving the SASP. There are at least five distinct paracrine mechanisms by which senescent cells could promote tissue dysfunction, including perturbation of the stem cell niche (causing stem cell dysfunction), disruption of extracellular matrix, induction of aberrant cell differentiation (both creating abnormal tissue architecture), stimulation of sterile tissue inflammation, and induction of senescence in neighbouring cells (paracrine senescence). HOIP:HOIP_0060183 IRF3 activation is a subtype of molecular activation: A process that changes the activity of the IRF3 to be higher. This process can constitute the course of cellular senescence. PMID:33328614 PMID:33833439 IRF activation [chronic cellular senescence] HOIP_0060183 PMID:33328614 The DNA sensor cGAS and the adaptor protein STING have been reported to be major regulators of the SASP programme across species, presumably by activating NF-κB and the interferon response factor IRF3. PMID:33833439 Activation of STING initiates cascades that support anti-proliferative cell states, including cellular senescence, and ultimately cell death. To that end, STING promotes induction of cell-cycle inhibitors (such as p21) and pro-apoptotic BH3-only proteins. Alternatively, and in a more direct mode of action, phosphorylated IRF3 can also interact with the pro-apoptotic proteins BAX and BAK and thereby lead to transcription-independent induction of apoptosis downstream of STING. HOIP:HOIP_0060184 The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 type I interferon production [chronic cellular senescence] HOIP_0060184 PMID:33328614 Senescent cells, especially when persisting for extended periods in culture or in vivo, display a profound activation of type I interferon response and downstream targets. This distinctively strong induction of type I interferon was found to be partly caused by reactivation of transposable elements and consequent to cGAS–STING activation. Treatment with nucleoside reverse-transcriptase inhibitors, which inhibit retrotransposition of transposable elements, limits the senescence-associated detrimental effects of SASP and ameliorates chronic inflammation in aged animals. HOIP:HOIP_0060185 P21 signaling is a process that a signal is transmitted by the p21. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24848057 PMID:33328614 p21 signaling [cellular senescence] HOIP_0060185 PMID:24848057 What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:33328614 p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. HOIP:HOIP_0060186 A histone H3.2 (human) that has had the initiator methionine removed and that has been trimethylated at the position equivalent to Lys-10 of the amino acid sequence represented by UniProtKB:Q71DI3. UniProtKB:Q71DI3, 2-136, Lys-10, MOD:00083. H3.2:H3K9me3 histone H3.2, initiator methionine removed trimethylated 5 (human) hH3.2/InitMet-/Me3:5 HOIP_0060186 HOIP:HOIP_0060189 The process in which fragments of chromatin are released into the cytosolic compartment. Loss of nuclear lamina can lead to the release of cytosolic chromatin fragments (CCFs) in the cytoplasm of senescent cells. Although yet unprobed, in the context of oncogene-induced DNA replication, hard-to-replicate genomic regions such as fragile sites, telomeric sequences and repetitive DNA probably contribute to CCFs. It remains unclear whether CCFs are formed only in deeply senescent cells. Importantly, CCFs dictate senescence-associated paracrine functions through the activation of the cyclic GMP–AMP synthase (cGAS) and the adaptor stimulator of interferon genes (STING) pathway (discussed later). Low doses of HDAC inhibitors have been reported to reduce CCFs and suppress the senescence-associated secretory phenotype (SASP). PMID:33328614 release of cytosolic chromatin fragments (CCFs) HOIP_0060189 Loss of nuclear lamina can lead to the release of cytosolic chromatin fragments (CCFs) in the cytoplasm of senescent cells. Although yet unprobed, in the context of oncogene-induced DNA replication, hard-to-replicate genomic regions such as fragile sites, telomeric sequences and repetitive DNA probably contribute to CCFs. It remains unclear whether CCFs are formed only in deeply senescent cells. Importantly, CCFs dictate senescence-associated paracrine functions through the activation of the cyclic GMP–AMP synthase (cGAS) and the adaptor stimulator of interferon genes (STING) pathway (discussed later). Low doses of HDAC inhibitors have been reported to reduce CCFs and suppress the senescence-associated secretory phenotype (SASP). PMID:33328614 HOIP:HOIP_0060190 The process in which fragments of chromatin are released into the cytosolic compartment. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 release of cytosolic chromatin fragments (CCFs) [chronic cellular senescence] HOIP_0060190 PMID:33328614 Loss of nuclear lamina can lead to the release of cytosolic chromatin fragments (CCFs) in the cytoplasm of senescent cells. Although yet unprobed, in the context of oncogene-induced DNA replication, hard-to-replicate genomic regions such as fragile sites, telomeric sequences and repetitive DNA probably contribute to CCFs. It remains unclear whether CCFs are formed only in deeply senescent cells. Importantly, CCFs dictate senescence-associated paracrine functions through the activation of the cyclic GMP–AMP synthase (cGAS) and the adaptor stimulator of interferon genes (STING) pathway (discussed later). Low doses of HDAC inhibitors have been reported to reduce CCFs and suppress the senescence-associated secretory phenotype (SASP). HOIP:HOIP_0060191 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:9780815345671 PMID:24848057 PMID:33328614 cellular response to DNA damage stimulus (sustained) [chronic cellular senescence] HOIP_0060191 ISBN:9780815345671 Short or uncapped telomeres arise in somatic cells after several replictive cycles. The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Biology of Aging 2nd Ed. PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS)17–19. What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:33328614 Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). HOIP:HOIP_0060192 Any process that activates or increases the frequency, rate or extent of cellular senescence in neigbor cells. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 positive regulation of cellular senescence in neighboring cell [chronic cellular senescence] HOIP_0060192 PMID:24848057 In this way, senescence interferes with tissue homeostasis and regeneration, and lays the groundwork for its cell-non-autonomous detrimental actions involving the SASP. There are at least five distinct paracrine mechanisms by which senescent cells could promote tissue dysfunction, including perturbation of the stem cell niche (causing stem cell dysfunction), disruption of extracellular matrix, induction of aberrant cell differentiation (both creating abnormal tissue architecture), stimulation of sterile tissue inflammation, and induction of senescence in neighbouring cells (paracrine senescence). HOIP:HOIP_0060193 Loss of nuclear lamina is a subtype of structural defect: A process in which a part of a nuclear lamina is lost. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 loss of nuclear lamina [chronic cellular senescence] HOIP_0060193 PMID:33328614 Loss of nuclear lamina can lead to the release of cytosolic chromatin fragments (CCFs) in the cytoplasm of senescent cells. HOIP:HOIP_0060194 Loss of nuclear lamina is a subtype of structural defect: A process in which a part of a nuclear lamina is lost. loss of nuclear lamina HOIP_0060194 HOIP:HOIP_0060195 The totality of all processes having slow progressive through which cellular senescence is realized. PMID:26646499 chronic cellular senescence course HOIP_0060195 PMID:26646499 Chronic senescence results from long-term, slow macromolecular damage due to stresses such as protein misfolding, protein aggregation, dysfunction of the nuclear lamina, epigenetic changes and various kinds of DNA damage including telomere shortening (Fig. 1). HOIP:HOIP_0060196 The totality of all processes through which cellular senescence is realized with sudden onset, sharp rise, and short . PMID:26646499 acute cellular senescence course HOIP_0060196 PMID:26646499 Acute senescence occurs in response to discrete stresses that are required for tissue homeostasis, including CCN1-induced myofibroblast senescence in wound healing, HLAG-induced neutrophil senescence in the placenta and oncogene-induced senescence (OIS) in neoplastic lesions (Fig. 1). Both acute and embryonic senescent cells appear to be beneficial, and their elimination seems programmed, presumably through involvement of the immune system HOIP:HOIP_0060197 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. cellular response to stress [cellular senescence] HOIP_0060197 HOIP:HOIP_0060198 Any process that stops, prevents, or reduces the frequency, rate or extent of the transcription mediated by RNA polymerase II E2F. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. doi/10.1895/wormbook.1.30.2 negative regulation of transcription by RNA polymerase II E2F [cellular senescence] HOIP_0060198 doi/10.1895/wormbook.1.30.2 Although present, neither SKN-1 nor PAL-1 activates gene expression in the P cells. This is because the germ line precursors are protected from activating somatic programs of gene expression by PIE-1, which is restricted to the P cell at each asymmetric division (Figure 5) (Mello et al., 1996). Germ-line precursors in C. elegans, as in many organisms, are transcriptionally quiescent. Inhibition of transcription correlates with the failure to phosphorylate the C-terminal domain of RNA polymerase on Serine-5 (Ser-5) and Ser-2, which are needed for transcription initiation and elongation, respectively. These phophorylation events are inhibited by PIE-1 in the P cells of early C. elegans embryos (Tenenhaus et al., 1998). In vitro studies indicate that PIE-1 directly binds to, and inhibits, the kinase needed for Ser-2 phosphorylation (Batchelder et al., 1999). Altered forms of PIE-1 that do not bind the kinase fail to inhibit Ser-2 phosphorylation in vivo, but can still suppress transcription and promote germ-line fate through effects on Ser-5 phosphorylation (Ghosh and Seydoux, 2008). Inhibition of transcription is thought to prevent SKN-1, PAL-1 and other transcription factors from activating gene expression in the P cells. However, after asymmetric division of P2, the degradation of PIE-1 from the somatic daughter via the MEX-5/ZIF-1 pathway described above relieves transcriptional repression, allowing SKN-1 activation of target genes in EMS. Similarly, after the P2 and P3 divisions, disappearance of PIE-1 allows PAL-1 activation of target genes to commence. PIE-1 is also important for activating the translation of NOS-2 in the P4 cell; although the mechanism is unknown, this function of PIE-1 is separable from its role in preventing transcription (D'Agostino et al., 2006; Tenenhaus et al., 2001). HOIP:HOIP_0060199 A Rb:E2F1 whose components are encoded in the genome of human. retinoblastoma-E2F complex (human) Rb-E2F complex (human) HOIP_0060199 HOIP:HOIP_0060200 Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 positive regulation of autophagy [chronic cellular senescence] HOIP_0060200 PMID:33328614 Indeed, it was reported that a selective autophagy pathway, via mammalian target of rapamycin (mTOR) activation, contributes to sustain the protein synthesis of many senescence-associated secretory phenotype factors mainly in oncogene-induced senescent cells and that downregulation of several autophagy regulators delays the establishment of oncogene-induced senescence. more recently, LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. Inhibition of autophagy prevents lamin B1 degradation and ensures nuclear envelope integrity in senescent cells. HOIP:HOIP_0060201 The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:26524528 PMID:29114066 PMID:33328614 autophagy [chronic cellular senescence] HOIP_0060201 PMID:26524528 PMID:26524528 The autophagy protein LC3/Atg8, which is involved in autophagy membrane trafficking and substrate delivery, is present in the nucleus and directly interacts with the nuclear lamina protein Lamin B1, and binds to lamin-associated domains (LADs) on chromatin. This LC3-Lamin B1 interaction does not downregulate Lamin B1 during starvation, but mediates its degradation upon oncogenic insults, such as by activated Ras. Lamin B1 degradation is achieved by nucleus-to-cytoplasm transport that delivers Lamin B1 to the lysosome. Inhibiting autophagy or the LC3-Lamin B1 interaction prevents activated Ras-induced Lamin B1 loss and attenuates oncogene-induced senescence in primary human cells. PMID:29114066 The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011). PMID:33328614 LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. Inhibition of autophagy prevents lamin B1 degradation and ensures nuclear envelope integrity in senescent cells HOIP:HOIP_0060202 TOR signaling is a process that a signal is transmitted by the TOR (Target of rapamycin) . This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:29114066 PMID:33328614 mTOR signaling [chronic cellular senescence] HOIP_0060202 PMID:29114066 mTORC1 integrates inputs from nutrient and growth signals to regulate general cellular processes such as protein and lipid synthesis, autophagy, and metabolism (Saxton and Sabatini, 2017). In this regard, mTOR is able to regulate the senescence-associated secretory phenotype (SASP), autophagy, and senescent growth arrest (Herranz et al., 2015; Laberge et al., 2015). The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060203 A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:978081534567 PMID:35165420 cell cycle arrest [cellular senescence] HOIP_0060203 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:35165420 As telomeres reach a critical length, they become unable to bind enough telomere-capping proteins and are sensed as exposed DNA ends, which activates the DDR pathways that, through the induction of the cell cycle inhibitors p21 and p16, arrest proliferation. Such short telomeres, however, retain a sufficient number of telomere-binding proteins to inhibit DNA repair and avoid fusions, and consequently fuel a persistent DNA damage signal that enforces a permanent DNA damage-induced proliferative arrest. HOIP:HOIP_0060229 The transfer of information from one cell to another, where the signal travels from the signal-producing cell to the receiving cell by passive diffusion or bulk flow in intercellular fluid. The signaling cell and the receiving cell are usually in the vicinity of each other. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. paracrine signaling [chronic cellular senescence] HOIP_0060229 HOIP:HOIP_0060230 Negative regulation of tumor cell proliferation is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of tumor cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33833439 negative regulation of tumor cell proliferation [acute cellular senescence] HOIP_0060230 PMID:33833439 Activation of STING initiates cascades that support anti-proliferative cell states, including cellular senescence, and ultimately cell death (a more detailed discussion of senescence is provided further below). To that end, STING promotes induction of cell-cycle inhibitors (such as p21) and pro-apoptotic BH3-only proteins. Alternatively, and in a more direct mode of action, phosphorylated IRF3 can also interact with the pro-apoptotic proteins BAX and BAK and thereby lead to transcription-independent induction of apoptosis downstream of STING. HOIP:HOIP_0060231 Hypofunction of cell division is a subtype of hypofunctioning: A process that performs the decreased or insufficient cell devision. hypofunction of cell division HOIP_0060231 HOIP:HOIP_0060232 Changing cell division balance is a subtype of changing balance: A process that changes the steady state of cell division. changing cell division balance HOIP_0060232 HOIP:HOIP_0060233 Cellular stress-response imbalance is a subtype of stress response imbalance: A process that lacks the balance between the cellular stress and its response. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. cellular stress-response imbalance [cellular senescence] HOIP_0060233 HOIP:HOIP_0060234 Increasing demand for embryonic pattern specification is a subtype of increasing functional demand: A process that changes the functional demand for the embryonic pattern specification to be higher. increasing demand for embryonic pattern specification HOIP_0060234 HOIP:HOIP_0060235 Increasing demand for embryonic pattern specification is a subtype of increasing functional demand: A process that changes the functional demand for the embryonic pattern specification to be higher. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. increasing demand for embryonic pattern specification [embryonic cellular senescence] HOIP_0060235 HOIP:HOIP_0060236 A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. Wikipedia:Aging aging [chronic cellular senescence] HOIP_0060236 HOIP:HOIP_0060237 Changing time is a subtype of changing quality: A process that changes the time quality. changing time quality HOIP_0060237 HOIP:HOIP_0060238 Changing age quality is a subtype of changing time quality: A process that changes the age quality. changing age quality HOIP_0060238 HOIP:HOIP_0060239 Increasing age is a subtype of changing age quality: A process that changes the age to be larger. increasing age HOIP_0060239 HOIP:HOIP_0060240 A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:29114066 PMID:33328614 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ cellular senescence (sustained) [chronic cellular senescence course] HOIP_0060240 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ PMID:29114066 Senescence, a cellular response that limits the proliferation of aged or damaged cells (Muñoz-Espín et al., 2013; Muñoz-Espín and Serrano, 2014), belongs to the antagonistic class (Fig. 1). Although senescence plays physiological roles during normal development and it is needed for tissue homeostasis, senescence constitutes a stress response triggered by insults associated with aging such as genomic instability and telomere attrition, which are primary aging hallmarks themselves. PMC:5748990 PMID:33328614 Besides prolonged DDR activation, senescence features include cell cycle arrest (by upregulation of p21 and p16 cell cycle inhibitors), oxidative damage (as detected by increased ROS levels), upregulation of the BCL-2 family of antiapoptotic proteins, which induce resistance to apoptosis, metabolic changes (including senescence-associated-β-galactosidase (SA-β-gal) accumulation), senescence-associated heterochromatin foci (SAHF) and a senescence-associated secretory phenotype (SASP). https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ Senescence jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig1.jpg HOIP:HOIP_0060241 A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33328614 cellular senescence (transient) [acute cellular senescence course] HOIP_0060241 PMID:33328614 Besides prolonged DDR activation, senescence features include cell cycle arrest (by upregulation of p21 and p16 cell cycle inhibitors), oxidative damage (as detected by increased ROS levels), upregulation of the BCL-2 family of antiapoptotic proteins, which induce resistance to apoptosis, metabolic changes (including senescence-associated-β-galactosidase (SA-β-gal) accumulation), senescence-associated heterochromatin foci (SAHF) and a senescence-associated secretory phenotype (SASP). HOIP:HOIP_0060242 A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. ISBN:978081534567 PMID:35165420 cell cycle arrest (transient) [acute cellular senescence] HOIP_0060242 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:35165420 As telomeres reach a critical length, they become unable to bind enough telomere-capping proteins and are sensed as exposed DNA ends, which activates the DDR pathways that, through the induction of the cell cycle inhibitors p21 and p16, arrest proliferation. Such short telomeres, however, retain a sufficient number of telomere-binding proteins to inhibit DNA repair and avoid fusions, and consequently fuel a persistent DNA damage signal that enforces a permanent DNA damage-induced proliferative arrest. HOIP:HOIP_0060243 Increasing demand for cellular stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the cellular stress to be higher. increasing demand for cellular stress response HOIP_0060243 HOIP:HOIP_0060244 Increasing demand for cellular stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the cellular stress to be higher. This process can constitute the course of cellular senescence. increasing demand for cellular stress response [adult cellular senescence] HOIP_0060244 HOIP:HOIP_0060245 Increasing demand for response to ER stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the endoplasmic reticulum (ER) stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. Increasing demand for response to ER stress [adult cellular senescence] HOIP_0060245 HOIP:HOIP_0060246 The process in which selective elimination of senescent cells from the body. senescence cell clearance HOIP_0060246 HOIP:HOIP_0060247 The selective elimination of senescent cells from the body. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. senescence cell immune clearance [acute cellular senescence] HOIP_0060247 HOIP:HOIP_0060248 Cellular stress-response imbalance is a subtype of stress response imbalance: A process that lacks the balance between the cellular stress and its response. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. cellular stress-response imbalance [chronic cellular senescence] HOIP_0060248 HOIP:HOIP_0060249 Any process that results in a change in the state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. cellular response to stress (sustained) [chronic cellular senescence] HOIP_0060249 HOIP:HOIP_0060251 The selective elimination of senescent cells from the body. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. senescence cell immune clearance (low) [chronic cellular senescence] HOIP_0060251 HOIP:HOIP_0060254 Oncogene activation is a subtype of activation: A process that changes the activity of the oncogene to be higher. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. oncogene activation [chronic cellular senescence] HOIP_0060254 HOIP:HOIP_0060255 Cellular stress-response imbalance is a subtype of stress response imbalance: A process that lacks the balance between the cellular stress and its response. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. cellular stress-response imbalance [acute cellular senescence] HOIP_0060255 HOIP:HOIP_0060256 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. regulation of cell cycle [chronic cellular senescence] HOIP_0060256 HOIP:HOIP_0060257 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. regulation of cell cycle [acute cellular senescence] HOIP_0060257 HOIP:HOIP_0060258 RB activation is a subtype of molecular activation: A process that changes the activity of the RB ( protein kinase C) to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24848057 RB activation (transient) [acute cellular senescence] HOIP_0060258 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060259 RB activation is a subtype of molecular activation: A process that changes the activity of the RB ( protein kinase C) to be higher. PMID:24848057 RB activation [cellular senescence] HOIP_0060259 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060260 Any signalling pathway that decreases or inhibits the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:978081534567 negative regulation of cell cycle G1/S phase transition [acute cellular senescence] HOIP_0060260 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060261 Any signalling pathway that decreases or inhibits the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:978081534567 negative regulation of cell cycle G1/S phase transition [chronic cellular senescence] HOIP_0060261 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060262 Arrest of cell division is a subtype of arresting: A process that that results in the cessation of of cell cycle G1/S phase transition. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. arrest of cell cycle G1/S phase transition (transient) [acute cellular senescence] HOIP_0060262 HOIP:HOIP_0060263 Arrest of cell division is a subtype of arresting: A process that that results in the cessation of of cell cycle G1/S phase transition. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. arrest of cell cycle G1/S phase transition (sustained) [chronic cellular senescence] HOIP_0060263 HOIP:HOIP_0060264 Arrest of nuclear DNA replication is a subtype of arresting: A process that results in the cessation of a nuclear DNA replication. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. arrest of nuclear DNA replication (sustained) [chronic cellular senescence] HOIP_0060264 HOIP:HOIP_0060265 Arrest of nuclear DNA replication is a subtype of arresting: A process that results in the cessation of a nuclear DNA replication. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. arrest of nuclear DNA replication (trasient) [acute cellular senescence] HOIP_0060265 HOIP:HOIP_0060266 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:9780071802154 PMID:24449267 PMID:24848057 ROS biosynthetic process [cellular senescence] reactive oxygen species biosynthetic process (sustained) [chronic cellular senescence] HOIP_0060266 ISBN:9780071802154 Oxidants are oxygen-based free-radicals that include the hydroxyl free radical, superoxide, and hydrogen peroxide. Most cellular oxidants are generated by mitochondria during the production of ATP from oxygen. It is now established that old age in most species is associated with oxidative stress, for example to DNA (8-hydroxyguanosine derivatives), proteins (carbonyls), lipids (lipoperoxides, malondialdehydes), and prostaglandins (isoprostanes). Harrison's principles of internal medicine., 19th ed. New York : McGraw Hill Education, 2015 Chapter 94e, The biology of aging. PMID:24449267 However, RNAi-mediated depletion of LMNB1 appears to be associated with reduced cell proliferation to various degrees in most (Shimi et al. 2011; Dreesen et al. 2013; Sadaie et al. 2013; Shah et al. 2013). Shimi et al. (2011) showed that depletion of LMNB1 is sufficient to induce senescence through modulation of reactive oxygen species (ROS) production. Perhaps paradoxically, they showed that depletion of LMNB1 leads to a reduction of ROS in a p53-depenent manner. Similarly, Barascu et al. (2012) showed that increased levels of LMNB1 are associated with ROS up-regulation and senescence. Generally, ROS is thought to be a cause of cellular damage, and it has been shown that ROS is increased during senescence. Furthermore, high levels of exogenous oxidative stress can induce senescence (Passos et al. 2007). However, increasing evidence suggests that modest levels of ROS can also contribute to cellular proliferation and survival (Sena and Chandel 2012). Thus, alterations in LMNB1 might contribute to a fine-tuning of ROS levels. PMID:24848057 For example, DNA damage initially halts cell-cycle progression through p53-mediated induction of p21, but if lesions persist, this activates p16Ink4a through p38-MAPK-mediated mitochondrial dysfunction and ROS production. In certain cases, the SASP is dependent on persistent DNA damage signalling, such as that created through a positive feedback loop between DDR signalling and ROS. Both types of DDR signalling were found to cause mitochondrial dysfunction and production of ROS which led to new DNA damage and continued DDR signalling. Consistent with this, primary human fibroblasts overexpressing p16Ink4a or p21 undergo senescent growth arrest but fail to activate the DDR and do not produce a SASP. Importantly, several senescence-inducing stimuli produce SASPs independent of DNA damage, implying the existence of DDR-independent mechanisms. HOIP:HOIP_0060267 The totality of all processes through which cellular senescence is realized in the progression of an embryo. PMID:26646499 embryonic cellular senescence HOIP_0060267 PMID:26646499 Embryonic senescence is noncanonical, whereby an arrest maintained by p21 or the alternative CDK4 and CDK6 inhibitor p15Ink4b drives tissue patterning without involvement of p16Ink4a . Both acute and embryonic senescent cells appear to be beneficial, and their elimination seems programmed, presumably through involvement of the immune system. HOIP:HOIP_0060268 TGF beta signaling is a subtype of signaling starting with the TGF beta (transforming growth factor beta) as a ligand binding to a TGFR ( transforming growth factor beta receptor). TGF beta signaling HOIP_0060268 HOIP:HOIP_0060269 TGF beta signaling is a subtype of signaling starting with the TGF beta (transforming growth factor beta) as a ligand binding to a TGFR ( transforming growth factor beta receptor). This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. PMID:26646499 TGF beta signaling [embryonic cellular senescence] HOIP_0060269 PMID:26646499 In embryonic senescence, elevated TGFβ and reduced PTEN activity upregulate SMAD-FOXO transcriptional activation of the cyclin-dependent kinase inhibitor p21, as well as activation of p15Ink4b through unclear means. HOIP:HOIP_0060270 TGF beta signaling is a subtype of signaling starting with the TGF beta (transforming growth factor beta) as a ligand binding to a TGFR ( transforming growth factor beta receptor). This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. PMID:26646499 TGF beta receptor signaling [embryonic cellular senescence] HOIP_0060270 PMID:26646499 In embryonic senescence, elevated TGFβ and reduced PTEN activity upregulate SMAD-FOXO transcriptional activation of the cyclin-dependent kinase inhibitor p21, as well as activation of p15Ink4b through unclear means. HOIP:HOIP_0060271 SMAD signaling is a subtype of signaling transmitted by SMAD. SMAD signaling HOIP_0060271 HOIP:HOIP_0060272 Increasing demand for cellular stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the cellular stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. increasing demand for cellular stress response (transient) [acute cellular senescence] HOIP_0060272 HOIP:HOIP_0060273 Increasing demand for cellular stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the cellular stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. increasing demand for cellular stress response (sustained) [chronic cellular senescence] HOIP_0060273 HOIP:HOIP_0060274 A protein complex consisting of SMAD and cyclin-dependent kinase 1 (FOXO). SMAD-FOXO complex HOIP_0060274 HOIP:HOIP_0060275 Increasing demand for cellular stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the cellular stress to be higher. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. increasing demand for cellular stress response [embryonic cellular senescence] HOIP_0060275 HOIP:HOIP_0060276 Regulation of gene expression by SMAD is a subtype of regulation of gene expression: Any process that modulates the frequency, rate or extent of gene expression. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. PMID:26646499 Regulation of gene expression by SMAD [embryonic cellular senescence] HOIP_0060276 PMID:26646499 In embryonic senescence, elevated TGFβ and reduced PTEN activity upregulate SMAD-FOXO transcriptional activation of the cyclin-dependent kinase inhibitor p21, as well as activation of p15Ink4b through unclear means. HOIP:HOIP_0060277 Regulation of gene expression by SMAD is a subtype of regulation of gene expression: Any process that modulates the frequency, rate or extent of gene expression. PMID:24848057 Regulation of gene expression by SMAD HOIP_0060277 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060278 P15 signaling is a process that a signal is transmitted by the p15. p15 signaling HOIP_0060278 HOIP:HOIP_0060279 A series of molecular signals transduced with the regulation of transcription of target genes by p15. p16 signaling pathway HOIP_0060279 HOIP:HOIP_0060280 P15signaling is a process that a signal is transmitted by the p15. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. PMID:24238961 PMID:26646499 PMID:33328614 p15 signaling (transient) [embryonic cellular senescence] HOIP_0060280 PMID:24238961 Here we describe senescence as a normal developmental mechanism found throughout the embryo, including the apical ectodermal ridge (AER) and the neural roof plate, two signaling centers in embryonic patterning. Embryonic senescent cells are nonproliferative and share features with oncogene-induced senescence (OIS), including expression of p21, p15, and mediators of the senescence-associated secretory phenotype (SASP). PMID:26646499 Embryonic senescence is noncanonical, whereby an arrest maintained by p21 or the alternative CDK4 and CDK6 inhibitor p15Ink4b drives tissue patterning without involvement of p16Ink4a (refs. 14,15). PMID:33328614 Consistent with this observation, it was reported that senescence occurs in a programmed manner and contributes to mammalian embryonic development and tissue patterning, although mainly via induction of p21, p15 and mediators of the SASP rather than through overt DDR signalling HOIP:HOIP_0060281 Cyclin D-CDK4/6 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin D-CDK4/6 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. PMID:24848057 PMID:26646499 PMID:29114066 Cyclin D-CDK4/6 complex inactivation (transient) [embryonic cellular senescence] HOIP_0060281 PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. PMID:26646499 Embryonic senescence is noncanonical, whereby an arrest maintained by p21 or the alternative CDK4 and CDK6 inhibitor p15Ink4b drives tissue patterning without involvement of p16Ink4a PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. HOIP:HOIP_0060282 Increasing demand for cellular stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the cellular stress to be higher. This process can constitute the course of cellular senescence. increasing demand for cellular stress response [cellular senescence] HOIP_0060282 HOIP:HOIP_0060283 Any process that results in a change in the state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. cellular response to stress (transient) [acute cellular senescence] HOIP_0060283 HOIP:HOIP_0060284 Cyclin D-CDK4/6 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin D-CDK4/6 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24848057 PMID:26646499 PMID:29114066 Cyclin D-CDK4/6 complex inactivation (transient) [acute cellular senescence] HOIP_0060284 PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. PMID:26646499 Embryonic senescence is noncanonical, whereby an arrest maintained by p21 or the alternative CDK4 and CDK6 inhibitor p15Ink4b drives tissue patterning without involvement of p16Ink4a PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. HOIP:HOIP_0060285 Cyclin D-CDK4/6 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin D-CDK4/6 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 PMID:26646499 PMID:29114066 Cyclin D-CDK4/6 complex inactivation (sustained) [chronic cellular senescence] HOIP_0060285 PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. PMID:26646499 Embryonic senescence is noncanonical, whereby an arrest maintained by p21 or the alternative CDK4 and CDK6 inhibitor p15Ink4b drives tissue patterning without involvement of p16Ink4a PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. HOIP:HOIP_0060286 RB activation is a subtype of molecular activation: A process that changes the activity of the RB ( protein kinase C) to be higher. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. PMID:24848057 RB activation (transient) [embryonic cellular senescence] HOIP_0060286 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060287 Any signalling pathway that decreases or inhibits the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:978081534567 negative regulation of cell cycle G1/S phase transition [embryonic cellular senescence] HOIP_0060287 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060288 Arrest of cell division is a subtype of arresting: A process that that results in the cessation of of cell cycle G1/S phase transition. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. arrest of cell cycle G1/S phase transition (transient) [embryonic cellular senescence] HOIP_0060288 HOIP:HOIP_0060289 Arrest of nuclear DNA replication is a subtype of arresting: A process that results in the cessation of a nuclear DNA replication.This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. arrest of nuclear DNA replication (trasient) [embryonic cellular senescence] HOIP_0060289 HOIP:HOIP_0060290 SMAD signaling is a subtype of signaling transmitted by SMAD. PMID:26646499 SMAD signaling [embryonic cellular senescence] HOIP_0060290 PMID:26646499 In embryonic senescence, elevated TGFβ and reduced PTEN activity upregulate SMAD-FOXO transcriptional activation of the cyclin-dependent kinase inhibitor p21, as well as activation of p15Ink4b through unclear means. HOIP:HOIP_0060291 P21 signaling is a process that a signal is transmitted by the p21. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24848057 PMID:29114066 PMID:33328614 p21 signaling (transient) [acute cellular senescence] HOIP_0060291 PMID:24848057 What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:29114066 Senescence inducers such as telomeric attrition and oncogenic or oxidative stress cause DNA damage. DNA damage results in increased deposition of γH2Ax and 53BP1 in chromatin that in turn activates a kinase cascade involving first ATM and ATR and then CHK1 and CHK2, eventually resulting in p53 activation (d’Adda di Fagagna, 2008; Fumagalli et al., 2012). p53 induces transcription of the cyclin-dependent kinase inhibitor p21CIP1. In turn, p21CIP1 blocks CDK4/6 activity, resulting in hypophosphorylated Rb and cell cycle exit (d’Adda di Fagagna, 2008). Although transient increases in p53 levels can enact a quiescent state and activate DNA repair processes, during senescence, there is a sustained induction of p53 (Salama et al., 2014; Kruiswijk et al., 2015). PMID:33328614 p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. HOIP:HOIP_0060293 P21 signaling is a process that a signal is transmitted by the p21. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 PMID:29114066 PMID:33328614 p21 signaling (sustained) [chronic cellular senescence] HOIP_0060293 PMID:24848057 What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:29114066 Senescence inducers such as telomeric attrition and oncogenic or oxidative stress cause DNA damage. DNA damage results in increased deposition of γH2Ax and 53BP1 in chromatin that in turn activates a kinase cascade involving first ATM and ATR and then CHK1 and CHK2, eventually resulting in p53 activation (d’Adda di Fagagna, 2008; Fumagalli et al., 2012). p53 induces transcription of the cyclin-dependent kinase inhibitor p21CIP1. In turn, p21CIP1 blocks CDK4/6 activity, resulting in hypophosphorylated Rb and cell cycle exit (d’Adda di Fagagna, 2008). Although transient increases in p53 levels can enact a quiescent state and activate DNA repair processes, during senescence, there is a sustained induction of p53 (Salama et al., 2014; Kruiswijk et al., 2015). This is a result of damage occurring in repair-resistant regions of the genome known as DNA segments with chromatin alterations reinforcing senescence, such as telomeres (Rodier et al., 2011; Fumagalli et al., 2012), that allow for a permanent arrest of the cell cycle by persistent induction of p21cip1. PMID:33328614 p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. HOIP:HOIP_0060294 P16 signaling is a process that a signal is transmitted by the p16. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 PMID:33328614 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ p16 signaling (sustained) [chronic cellular senescence] HOIP_0060294 PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. PMID:33328614 p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ p16 jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig2.jpg HOIP:HOIP_0060295 Cyclin E1-CDK2 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin E1-CDK2 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 cyclin E1-CDK2 complex inactivation (sustained) [chronic cellular senescence] HOIP_0060295 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. HOIP:HOIP_0060296 Cyclin E1-CDK2 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin E1-CDK2 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24848057 cyclin E1-CDK2 complex inactivation (transient) [acute cellular senescence] HOIP_0060296 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. HOIP:HOIP_0060297 Cyclin E1-CDK2 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin E1-CDK2 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24848057 cyclin E1-CDK2 complex inactivation (transient) [embryonic cellular senescence] HOIP_0060297 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. HOIP:HOIP_0060298 Tissue repair is a subtype of repairing: A process of tissue organization that results in the restoration of the tissue following damage. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. tissue repair [acute cellular senescence] HOIP_0060298 HOIP:HOIP_0060299 A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. PMID:33328614 cellular senescence (transient) [embryonic cellular senescence course] HOIP_0060299 PMID:33328614 Besides prolonged DDR activation, senescence features include cell cycle arrest (by upregulation of p21 and p16 cell cycle inhibitors), oxidative damage (as detected by increased ROS levels), upregulation of the BCL-2 family of antiapoptotic proteins, which induce resistance to apoptosis, metabolic changes (including senescence-associated-β-galactosidase (SA-β-gal) accumulation), senescence-associated heterochromatin foci (SAHF) and a senescence-associated secretory phenotype (SASP). HOIP:HOIP_0060301 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. regulation of cell cycle [embryonic cellular senescence] HOIP_0060301 HOIP:HOIP_0060302 Any process that stops, prevents or reduces the frequency, rate or extent of nuclear cell cycle DNA replication. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. down regulation of DNA replication involved in S phase negative regulation of nuclear cell cycle DNA replication (transient) [acute cellular senescence] HOIP_0060302 HOIP:HOIP_0060303 Any process that stops, prevents or reduces the frequency, rate or extent of nuclear cell cycle DNA replication. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. down regulation of DNA replication involved in S phase negative regulation of nuclear cell cycle DNA replication (transient) [embryonic cellular senescence] HOIP_0060303 HOIP:HOIP_0060304 Any process that stops, prevents or reduces the frequency, rate or extent of nuclear cell cycle DNA replication. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. down regulation of DNA replication involved in S phase negative regulation of nuclear cell cycle DNA replication (sustained) [chronic cellular senescence] HOIP_0060304 HOIP:HOIP_0060305 Cellular stress-response imbalance is a subtype of stress response imbalance: A process that lacks the balance between the cellular stress and its response. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. cellular stress-response imbalance [embryonic cellular senescence] HOIP_0060305 HOIP:HOIP_0060306 Accumulation of senescent cell is a subtype of accumulation of substances in a biological object: A process that keeps senescent cell in an organism, tissue. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. accumulation of senescent cell (transient) [acute cellular senescence] HOIP_0060306 HOIP:HOIP_0060307 Accumulation of senescent cell is a subtype of accumulation of substances in a biological object: A process that keeps senescent cell in an organism, tissue. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. accumulation of senescent cell (transient) [embryonic cellular senescence] HOIP_0060307 HOIP:HOIP_0060308 Accumulation of senescent cell is a subtype of accumulation of substances in a biological object: A process that keeps senescent cell in an organism, tissue. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:34756162 accumulation of senescent cell (sustained) [chronic cellular senescence] HOIP_0060308 PMID:34756162 The mechanisms behind SC accumulation with age and their influence on disease progression are still unclear. Some hypothesize that SCs develop ways to escape from immunosurveillance. In support of this, authors have shown that senescent dermal fibroblasts express atypical levels of MHC molecule HLA-E, induced by SASP-associated cytokines and regulated by p38MAPK (Pereira et al., 2019). HLA-E interacts with the inhibitory receptor NKG2A expressed by natural killer (NK) and highly differentiated CD8+ T cells, allowing senescent fibroblasts to evade immune clearance. Others theorize that, with age, the immune system becomes progressively compromised (immunosenescence) and cannot efficiently clear SCs as it should or that the generation rate of SCs is just too big to cope with (Furman et al., 2019). In any case, there is a very important notion to take from the relationship between senescence and aging: a persistent accumulation of SCs without a controlled clearance is detrimental for tissue function. HOIP:HOIP_0060309 Any process that results in a change in the state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus under stress. This process can constitute the course of embrryonic cellular senescence. cellular response to stress (transient) [embryonic cellular senescence] HOIP_0060309 HOIP:HOIP_0060311 The reorganization or renovation of existing tissues. This process can either change the characteristics of a tissue such as in blood vessel remodeling, or result in the dynamic equilibrium of a tissue such as in bone remodeling. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. tissue remodeling [acute cellular senescence] HOIP_0060311 HOIP:HOIP_0060312 The reorganization or renovation of existing tissues. This process can either change the characteristics of a tissue such as in blood vessel remodeling, or result in the dynamic equilibrium of a tissue such as in bone remodeling. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. tissue remodeling [embryonic cellular senescence] HOIP_0060312 HOIP:HOIP_0060313 A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:978081534567 PMID:35165420 cell cycle arrest (transient) [embryonic cellular senescence] HOIP_0060313 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:35165420 As telomeres reach a critical length, they become unable to bind enough telomere-capping proteins and are sensed as exposed DNA ends, which activates the DDR pathways that, through the induction of the cell cycle inhibitors p21 and p16, arrest proliferation. Such short telomeres, however, retain a sufficient number of telomere-binding proteins to inhibit DNA repair and avoid fusions, and consequently fuel a persistent DNA damage signal that enforces a permanent DNA damage-induced proliferative arrest. HOIP:HOIP_0060314 Any process that results in a change in the state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. cellular response to stress [adult cellular senescence] HOIP_0060314 HOIP:HOIP_0060315 The totality of all processes through which cellular senescence is realized in adults. adult cellular senescence course HOIP_0060315 HOIP:HOIP_0060316 P16 signaling is a process that a signal is transmitted by the p16. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:978081534567 PMID:24848057 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ p16 signaling [adult cellular senescence] HOIP_0060316 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ p16 jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig2.jpg HOIP:HOIP_0060317 Cellular stress-response imbalance is a subtype of stress response imbalance: A process that lacks the balance between the cellular stress and its response. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. cellular stress-response imbalance [adult cellular senescence] HOIP_0060317 HOIP:HOIP_0060319 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. ISBN:9780815345671 PMID:24848057 PMID:33328614 cellular response to DNA damage stimulus [acute cellular senescence] HOIP_0060319 ISBN:9780815345671 Short or uncapped telomeres arise in somatic cells after several replictive cycles. The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Biology of Aging 2nd Ed. PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS)17–19. What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:33328614 Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). HOIP:HOIP_0060320 P53 signaling is a process that a signal is transmitted by the p53. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. ISBN:978081534567 p53 signaling [acute cellular senescence] HOIP_0060320 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060321 P53 signaling is a process that a signal is transmitted by the p53. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:978081534567 p53 signaling [chronic cellular senescence] HOIP_0060321 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060322 Regulation of gene expression by p53 is a subtype of regulation of gene expression: Any process that modulates the frequency, rate or extent of gene expression. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24848057 regulation of gene expression by p53 [acute cellular senescence] HOIP_0060322 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060323 Regulation of gene expression by p53 is a subtype of regulation of gene expression: Any process that modulates the frequency, rate or extent of gene expression. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 regulation of gene expression by p53 [chronic cellular senescence] HOIP_0060323 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060324 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:9780815345671 PMID:24848057 PMID:33328614 cellular response to DNA damage stimulus [adult cellular senescence] HOIP_0060324 ISBN:9780815345671 Short or uncapped telomeres arise in somatic cells after several replictive cycles. The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Biology of Aging 2nd Ed. PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS)17–19. What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:33328614 Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). HOIP:HOIP_0060325 P21 signaling is a process that a signal is transmitted by the p21. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24848057 PMID:29114066 PMID:33328614 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ p21 signaling [adult cellular senescence] HOIP_0060325 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ PMID:24848057 What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:29114066 Senescence inducers such as telomeric attrition and oncogenic or oxidative stress cause DNA damage. DNA damage results in increased deposition of γH2Ax and 53BP1 in chromatin that in turn activates a kinase cascade involving first ATM and ATR and then CHK1 and CHK2, eventually resulting in p53 activation (d’Adda di Fagagna, 2008; Fumagalli et al., 2012). p53 induces transcription of the cyclin-dependent kinase inhibitor p21CIP1. In turn, p21CIP1 blocks CDK4/6 activity, resulting in hypophosphorylated Rb and cell cycle exit (d’Adda di Fagagna, 2008). Although transient increases in p53 levels can enact a quiescent state and activate DNA repair processes, during senescence, there is a sustained induction of p53 (Salama et al., 2014; Kruiswijk et al., 2015). This is a result of damage occurring in repair-resistant regions of the genome known as DNA segments with chromatin alterations reinforcing senescence, such as telomeres (Rodier et al., 2011; Fumagalli et al., 2012), that allow for a permanent arrest of the cell cycle by persistent induction of p21cip1. PMC:5748990 PMID:33328614 p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig2/ p21 jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig2.jpg HOIP:HOIP_0060326 Cyclin E1-CDK2 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin E1-CDK2 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24848057 cyclin E1-CDK2 complex inactivation [adult cellular senescence] HOIP_0060326 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. HOIP:HOIP_0060327 RB activation is a subtype of molecular activation: A process that changes the activity of the RB ( protein kinase C) to be higher. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24848057 RB activation [adult cellular senescence] HOIP_0060327 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060328 Any signalling pathway that decreases or inhibits the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:978081534567 negative regulation of cell cycle G1/S phase transition [adult cellular senescence] HOIP_0060328 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060329 Arrest of cell division is a subtype of arresting: A process that that results in the cessation of of cell cycle G1/S phase transition. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. arrest of cell cycle G1/S phase transition [adult cellular senescence] HOIP_0060329 HOIP:HOIP_0060330 Arrest of nuclear DNA replication is a subtype of arresting: A process that results in the cessation of a nuclear DNA replication. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. arrest of nuclear DNA replication [adult cellular senescence] HOIP_0060330 HOIP:HOIP_0060331 A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:978081534567 PMID:35165420 cell cycle arrest [adult cellular senescence] HOIP_0060331 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:35165420 As telomeres reach a critical length, they become unable to bind enough telomere-capping proteins and are sensed as exposed DNA ends, which activates the DDR pathways that, through the induction of the cell cycle inhibitors p21 and p16, arrest proliferation. Such short telomeres, however, retain a sufficient number of telomere-binding proteins to inhibit DNA repair and avoid fusions, and consequently fuel a persistent DNA damage signal that enforces a permanent DNA damage-induced proliferative arrest. HOIP:HOIP_0060332 A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:33328614 cellular senescence [adult cellular senescence course] HOIP_0060332 PMID:33328614 Besides prolonged DDR activation, senescence features include cell cycle arrest (by upregulation of p21 and p16 cell cycle inhibitors), oxidative damage (as detected by increased ROS levels), upregulation of the BCL-2 family of antiapoptotic proteins, which induce resistance to apoptosis, metabolic changes (including senescence-associated-β-galactosidase (SA-β-gal) accumulation), senescence-associated heterochromatin foci (SAHF) and a senescence-associated secretory phenotype (SASP). HOIP:HOIP_0060333 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. regulation of cell cycle [adult cellular senescence] HOIP_0060333 HOIP:HOIP_0060334 Cyclin D-CDK4/6 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin D-CDK4/6 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24848057 PMID:26646499 PMID:29114066 Cyclin D-CDK4/6 complex inactivation [adult cellular senescence] HOIP_0060334 PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. PMID:26646499 Embryonic senescence is noncanonical, whereby an arrest maintained by p21 or the alternative CDK4 and CDK6 inhibitor p15Ink4b drives tissue patterning without involvement of p16Ink4a PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. HOIP:HOIP_0060335 DNA damage response siganaling is a process that a signal of DNA damage is transmitted within a cell. DNA damage response siganaling HOIP_0060335 HOIP:HOIP_0060337 DNA damage response signaling is a process that a signal of DNA damage is transmitted within a cell. This process can constitute the course of adult cellular senescence. DNA damage response signaling [adult cellular senescence] HOIP_0060337 HOIP:HOIP_0060338 DNA damage response signaling is a process that a signal of DNA damage is transmitted within a cell. This process can constitute the course of acute cellular senescence. DNA damage response signaling [acute cellular senescence] HOIP_0060338 HOIP:HOIP_0060339 DNA damage response signaling is a process that a signal of DNA damage is transmitted within a cell. This process can constitute the course of chronic cellular senescence. PMID:24848057 DNA damage response siganaling (sustained) [chronic cellular senescence] HOIP_0060339 PMID:24848057 What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. HOIP:HOIP_0060340 Any process that stops, prevents, or reduces the frequency, rate or extent of the transcription mediated by RNA polymerase II E2F. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. doi/10.1895/wormbook.1.30.2 negative regulation of transcription by RNA polymerase II E2F [adult cellular senescence] HOIP_0060340 doi/10.1895/wormbook.1.30.2 Although present, neither SKN-1 nor PAL-1 activates gene expression in the P cells. This is because the germ line precursors are protected from activating somatic programs of gene expression by PIE-1, which is restricted to the P cell at each asymmetric division (Figure 5) (Mello et al., 1996). Germ-line precursors in C. elegans, as in many organisms, are transcriptionally quiescent. Inhibition of transcription correlates with the failure to phosphorylate the C-terminal domain of RNA polymerase on Serine-5 (Ser-5) and Ser-2, which are needed for transcription initiation and elongation, respectively. These phophorylation events are inhibited by PIE-1 in the P cells of early C. elegans embryos (Tenenhaus et al., 1998). In vitro studies indicate that PIE-1 directly binds to, and inhibits, the kinase needed for Ser-2 phosphorylation (Batchelder et al., 1999). Altered forms of PIE-1 that do not bind the kinase fail to inhibit Ser-2 phosphorylation in vivo, but can still suppress transcription and promote germ-line fate through effects on Ser-5 phosphorylation (Ghosh and Seydoux, 2008). Inhibition of transcription is thought to prevent SKN-1, PAL-1 and other transcription factors from activating gene expression in the P cells. However, after asymmetric division of P2, the degradation of PIE-1 from the somatic daughter via the MEX-5/ZIF-1 pathway described above relieves transcriptional repression, allowing SKN-1 activation of target genes in EMS. Similarly, after the P2 and P3 divisions, disappearance of PIE-1 allows PAL-1 activation of target genes to commence. PIE-1 is also important for activating the translation of NOS-2 in the P4 cell; although the mechanism is unknown, this function of PIE-1 is separable from its role in preventing transcription (D'Agostino et al., 2006; Tenenhaus et al., 2001). HOIP:HOIP_0060341 Any process that stops, prevents or reduces the frequency, rate or extent of nuclear cell cycle DNA replication. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. down regulation of DNA replication involved in S phase negative regulation of nuclear cell cycle DNA replication [adult cellular senescence] HOIP_0060341 HOIP:HOIP_0060342 Any process that stops, prevents, or reduces the frequency, rate or extent of the transcription mediated by RNA polymerase II E2F. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. doi/10.1895/wormbook.1.30.2 negative regulation of transcription by RNA polymerase II E2F (transient) [acute cellular senescence] HOIP_0060342 doi/10.1895/wormbook.1.30.2 Although present, neither SKN-1 nor PAL-1 activates gene expression in the P cells. This is because the germ line precursors are protected from activating somatic programs of gene expression by PIE-1, which is restricted to the P cell at each asymmetric division (Figure 5) (Mello et al., 1996). Germ-line precursors in C. elegans, as in many organisms, are transcriptionally quiescent. Inhibition of transcription correlates with the failure to phosphorylate the C-terminal domain of RNA polymerase on Serine-5 (Ser-5) and Ser-2, which are needed for transcription initiation and elongation, respectively. These phophorylation events are inhibited by PIE-1 in the P cells of early C. elegans embryos (Tenenhaus et al., 1998). In vitro studies indicate that PIE-1 directly binds to, and inhibits, the kinase needed for Ser-2 phosphorylation (Batchelder et al., 1999). Altered forms of PIE-1 that do not bind the kinase fail to inhibit Ser-2 phosphorylation in vivo, but can still suppress transcription and promote germ-line fate through effects on Ser-5 phosphorylation (Ghosh and Seydoux, 2008). Inhibition of transcription is thought to prevent SKN-1, PAL-1 and other transcription factors from activating gene expression in the P cells. However, after asymmetric division of P2, the degradation of PIE-1 from the somatic daughter via the MEX-5/ZIF-1 pathway described above relieves transcriptional repression, allowing SKN-1 activation of target genes in EMS. Similarly, after the P2 and P3 divisions, disappearance of PIE-1 allows PAL-1 activation of target genes to commence. PIE-1 is also important for activating the translation of NOS-2 in the P4 cell; although the mechanism is unknown, this function of PIE-1 is separable from its role in preventing transcription (D'Agostino et al., 2006; Tenenhaus et al., 2001). HOIP:HOIP_0060343 Any process that stops, prevents, or reduces the frequency, rate or extent of the transcription mediated by RNA polymerase II E2F. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. doi/10.1895/wormbook.1.30.2 negative regulation of transcription by RNA polymerase II E2F (sustained) [chronic cellular senescence] HOIP_0060343 doi/10.1895/wormbook.1.30.2 Although present, neither SKN-1 nor PAL-1 activates gene expression in the P cells. This is because the germ line precursors are protected from activating somatic programs of gene expression by PIE-1, which is restricted to the P cell at each asymmetric division (Figure 5) (Mello et al., 1996). Germ-line precursors in C. elegans, as in many organisms, are transcriptionally quiescent. Inhibition of transcription correlates with the failure to phosphorylate the C-terminal domain of RNA polymerase on Serine-5 (Ser-5) and Ser-2, which are needed for transcription initiation and elongation, respectively. These phophorylation events are inhibited by PIE-1 in the P cells of early C. elegans embryos (Tenenhaus et al., 1998). In vitro studies indicate that PIE-1 directly binds to, and inhibits, the kinase needed for Ser-2 phosphorylation (Batchelder et al., 1999). Altered forms of PIE-1 that do not bind the kinase fail to inhibit Ser-2 phosphorylation in vivo, but can still suppress transcription and promote germ-line fate through effects on Ser-5 phosphorylation (Ghosh and Seydoux, 2008). Inhibition of transcription is thought to prevent SKN-1, PAL-1 and other transcription factors from activating gene expression in the P cells. However, after asymmetric division of P2, the degradation of PIE-1 from the somatic daughter via the MEX-5/ZIF-1 pathway described above relieves transcriptional repression, allowing SKN-1 activation of target genes in EMS. Similarly, after the P2 and P3 divisions, disappearance of PIE-1 allows PAL-1 activation of target genes to commence. PIE-1 is also important for activating the translation of NOS-2 in the P4 cell; although the mechanism is unknown, this function of PIE-1 is separable from its role in preventing transcription (D'Agostino et al., 2006; Tenenhaus et al., 2001). HOIP:HOIP_0060344 Increasing extrachromosomal telomeric repeat DNA is a subtype of increasing quantity: A process that changes the amount of extrachromosomal telomeric repeat DNA to be larger. increasing extrachromosomal telomeric repeat DNA HOIP_0060344 HOIP:HOIP_0060345 The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:23637286 protein refolding [adult cellular senescence] HOIP_0060345 HOIP:HOIP_0060346 Increasing extrachromosomal telomeric repeat DNA is a subtype of increasing quantity: A process that changes the amount of extrachromosomal telomeric repeat DNA to be larger. PMID:32424334 increasing extrachromosomal telomeric repeat DNA [chronic cellular senescence] HOIP_0060346 PMID:32424334 cGAS also detects cytosolic DNA arising from dysfunctional telomeres. Precancerous cells escaping senescence-associated cell cycle arrest enter replicative crisis due to shortening, deprotection and fusion of telomeres. The resulting mitotic delay and problems with dicentric chromosomes lead to increased amounts of cytosolic chromatin and micronuclei that are detected by cGAS. Extrachromosomal telomere repeat DNA — a hallmark of cancer cells, which is caused by activation of the alternative lengthening of telomeres (ALT) pathway — is also sensed by cGAS. HOIP:HOIP_0060347 Any process that activates or increases the frequency, rate or extent of the inflammatory response. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33833439 positive regulation of inflammatory response [chronic cellular senescence] HOIP_0060347 PMID:33833439 Activation of STING initiates cascades that support anti-proliferative cell states, including cellular senescence, and ultimately cell death (a more detailed discussion of senescence is provided further below). To that end, STING promotes induction of cell-cycle inhibitors (such as p21) and pro-apoptotic BH3-only proteins. Alternatively, and in a more direct mode of action, phosphorylated IRF3 can also interact with the pro-apoptotic proteins BAX and BAK and thereby lead to transcription-independent induction of apoptosis downstream of STING. HOIP:HOIP_0060352 ATM signaling is a process that a signal is transmitted by ATM. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24848057 ATM signaling (transient) [acute cellular senescence] HOIP_0060352 PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS). What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. HOIP:HOIP_0060353 ATM signaling is a process that a signal is transmitted by ATM. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 ATM signaling (sustained) [chronic cellular senescence] HOIP_0060353 PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS). What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. HOIP:HOIP_0060354 ATR signaling is a process that a signal is transmitted by ATR. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24848057 PMID:33328614 ATR signaling (transient) [acute cellular senescence] HOIP_0060354 PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS). What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:33328614 At the bottom of the DDR cascade, the tumour suppressor p53, which is a target of ATM and its paralogue ATR, is activated and stimulates the expression of the cyclin-dependent kinase inhibitor p21, an essential mediator of senescence-associated cell cycle arrest. p16, an inhibitor of CDK4 and CDK6, is also key in several types of senescence; p21 is activated early on senescence entry and p16 is activated later, probably to maintain the senescence phenotype. HOIP:HOIP_0060355 ATR signaling is a process that a signal is transmitted by ATR. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24848057 PMID:33328614 ATR signaling (sustained) [chronic cellular senescence] HOIP_0060355 PMID:24848057 In addition to telomere erosion, several other tumour-associated stresses have been shown to induce a senescent growth arrest in vitro, including certain DNA lesions and reactive oxygen species (ROS). What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:33328614 At the bottom of the DDR cascade, the tumour suppressor p53, which is a target of ATM and its paralogue ATR, is activated and stimulates the expression of the cyclin-dependent kinase inhibitor p21, an essential mediator of senescence-associated cell cycle arrest. p16, an inhibitor of CDK4 and CDK6, is also key in several types of senescence; p21 is activated early on senescence entry and p16 is activated later, probably to maintain the senescence phenotype. HOIP:HOIP_0060356 CHK1 signaling is a process that a signal is transmitted by CHK1. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33328614 CHK1 signaling (transient) [acute cellular senescence] HOIP_0060356 PMID:33328614 Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. HOIP:HOIP_0060357 CHK1 signaling is a process that a signal is transmitted by CHK1. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 CHK1 signaling (sustained) [chronic cellular senescence] HOIP_0060357 PMID:33328614 Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. HOIP:HOIP_0060358 CHK2 signaling is a process that a signal is transmitted by CHK2. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 CHK2 signaling (sustained) [chronic cellular senescence] HOIP_0060358 PMID:33328614 Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. HOIP:HOIP_0060359 CHK2 signaling is a process that a signal is transmitted by CHK2. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33328614 CHK2 signaling (transient) [acute cellular senescence] HOIP_0060359 PMID:33328614 Nuclear DNA damage is often causatively associated with senescence establishment. DNA damage activates a signalling cascade defined as DNA damage response (DDR), characterized by phosphorylated histone H2AX (γH2AX), 53BP1 and MDC1, the apical kinases ataxia telangiectasia mutated (ATM) and ATR and the downstream kinases CHK2 and CHK1. Signals ultimately converge on p53 activation, which in turn elicits cell cycle arrest. HOIP:HOIP_0060360 Any process that stops, prevents, or reduces the frequency, rate or extent of the transcription mediated by RNA polymerase II E2F. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. doi/10.1895/wormbook.1.30.2 negative regulation of transcription by RNA polymerase II E2F (transient) [embryonic cellular senescence] HOIP_0060360 doi/10.1895/wormbook.1.30.2 Although present, neither SKN-1 nor PAL-1 activates gene expression in the P cells. This is because the germ line precursors are protected from activating somatic programs of gene expression by PIE-1, which is restricted to the P cell at each asymmetric division (Figure 5) (Mello et al., 1996). Germ-line precursors in C. elegans, as in many organisms, are transcriptionally quiescent. Inhibition of transcription correlates with the failure to phosphorylate the C-terminal domain of RNA polymerase on Serine-5 (Ser-5) and Ser-2, which are needed for transcription initiation and elongation, respectively. These phophorylation events are inhibited by PIE-1 in the P cells of early C. elegans embryos (Tenenhaus et al., 1998). In vitro studies indicate that PIE-1 directly binds to, and inhibits, the kinase needed for Ser-2 phosphorylation (Batchelder et al., 1999). Altered forms of PIE-1 that do not bind the kinase fail to inhibit Ser-2 phosphorylation in vivo, but can still suppress transcription and promote germ-line fate through effects on Ser-5 phosphorylation (Ghosh and Seydoux, 2008). Inhibition of transcription is thought to prevent SKN-1, PAL-1 and other transcription factors from activating gene expression in the P cells. However, after asymmetric division of P2, the degradation of PIE-1 from the somatic daughter via the MEX-5/ZIF-1 pathway described above relieves transcriptional repression, allowing SKN-1 activation of target genes in EMS. Similarly, after the P2 and P3 divisions, disappearance of PIE-1 allows PAL-1 activation of target genes to commence. PIE-1 is also important for activating the translation of NOS-2 in the P4 cell; although the mechanism is unknown, this function of PIE-1 is separable from its role in preventing transcription (D'Agostino et al., 2006; Tenenhaus et al., 2001). HOIP:HOIP_0060361 The selective elimination of senescent cells from the body. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. senescence cell immune clearance [adult cellular senescence] HOIP_0060361 HOIP:HOIP_0060362 Tissue malfunction is a subtype of malfunctioning process: A process that cannot perform tissues function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. tissue dysfunction [chronic cellular senescence] HOIP_0060362 HOIP:HOIP_0060363 Organ malfunction is a subtype of malfunctioning process: A process that cannot perform organ(s) function appropriately or cannot realize it at all. This process can constitute the course of chronic cell senescence. organ malfunction [chronic cellular senescence] HOIP_0060363 HOIP:HOIP_0060364 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. PMID:33328614 response to oxidative stress [adult cellular senescence] HOIP_0060364 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. PMID:121115731 HOIP:HOIP_0060365 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. response to endoplasmic reticulum stress [adult cellular senescence] HOIP_0060365 HOIP:HOIP_0060366 Increasing demand for oncogenic stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oncogenesis to be higher. increasing demand for oncogenic stress response HOIP_0060366 HOIP:HOIP_0060367 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a tumor cell. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:33328614 response to tumor cell proliferation [adult cellular senescence] HOIP_0060367 PMID:33328614 PMID:33328614 In the context of therapy-induced senescence for cancer cells, it was also shown that autophagy was triggered as a consequence of senescence establishment to cope with the increased load of accumulating toxic macromolecules, and its pharmacological targeting led to senescent cell elimination. However, autophagy has also been considered to suppress senescence by promoting the degradation of damaged organelles and other cellular components, and several studies have supported such a view. Together, these seemingly opposite roles may reflect a complex and reciprocal regulation of autophagy and cell senescence that can be linked to several senescence triggers, distinct cell types and a unique spatio-temporal activation of the autophagic programme acting in the senescence regulatory network. PMID:33328614 Oncogene activation is a powerful inducer of cellular senescence. Oncogene expression triggers an initial hyperproliferative phase that is intrinsically associated with altered DNA replication, which eventually engages DDR pathways and causes senescence. This process is known as oncogene-induced senescence (OIS). Loss of tumour suppressor expression can also induce proliferation arrest, as exemplified by PTEN loss-induced cellular senescence (PICS). Although initially PTEN loss-induced cellular senescence was not associated with DDR activation, it was later found to be associated with hyperproliferation, DDR engagement and cellular senescence in vivo. Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation4 suggesting distinct underlying mechanisms. HOIP:HOIP_0060368 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:33328614 phosphatidylinositol 3-kinase signaling [adult cellular senescence] HOIP_0060368 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation4, suggesting distinct underlying mechanisms. HOIP:HOIP_0060369 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:33328614 AKT signaling [adult cellular senescence] HOIP_0060369 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation, suggesting distinct underlying mechanisms. MH - *Aging MH - Animals MH - Cell Proliferation MH - *Cellular Senescence MH - DNA Damage MH - Humans MH - Phenotype MH - *Telomere MH - *Translational Research, Biomedical MESH:D000375 Aging HOIP:HOIP_0060370 Increasing demand for oncogenic stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oncogenesis to be higher. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:33328614 increasing demand for oncogenic stress response [adult cellular senescence] HOIP_0060370 PMID:33328614 Cellular senescence occurs in response to many different triggers, including DNA damage, telomere dysfunction, oncogene activation and organelle stress, and has been linked to processes such as tumour suppression, tissue repair, embryogenesis and organismal ageing. PMID:33328614 Oncogene activation is also a powerful senescence trigger. Specifically, most activated oncogenes, partly via reactive oxygen species (ROS) production, induce hyperproliferation and altered DNA replication patterns that ultimately result in replication stress and DNA damage accumulation at fragile sites, which include telomeres. HOIP:HOIP_0060371 Increasing demand for metabolic stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oncogenesis to be higher. increasing demand for metabolic stress HOIP_0060371 HOIP:HOIP_0060372 Increasing demand for metabolic stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oncogenesis to be higher. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. increasing demand for metabolic stress [adult cellular senescence] HOIP_0060372 HOIP:HOIP_0060373 Dameged molecule accumulattion in cell is a subtype of accumulation of substances in a biological object: A process that keeps damaged molecules in a cell. dameged molecule accumulattion in cell HOIP_0060373 HOIP:HOIP_0060375 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:23230272 DNA repair [acute cellular senescence] HOIP_0060375 PMID:23230272 Herein, we describe a direct link between rapid and short-lived poly(ADP-ribose) (PAR) polymerase 1 (PARP1) activation and PARylation at DNA damage sites, PAR-dependent recruitment of the BAL1 macrodomain-containing protein and its partner E3 ligase, local BBAP-mediated ubiquitylation, and subsequent recruitment of the checkpoint mediators 53BP1 and BRCA1. The PARP1-dependent localization of BAL1-BBAP functionally limits both early and delayed DNA damage and enhances cellular viability independent of ATM, MDC1, and RNF8. These data establish that BAL1 and BBAP are bona fide members of a DNA damage response pathway and are directly associated with PARP1 activation, BRCA1 recruitment, and double-strand break repair. HOIP:HOIP_0060376 Drug-, radiation-induced, or spontaneous injuries to DNA that introduce deviations from its normal double-helical conformation. These changes include structural distortions that interfere with replication and transcription, as well as point mutations that disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. If the damage is minor, it can often be repaired (DNA repair); extensive damage can induce apoptosis. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:9781437717815 PMID:29114066 PMID:33450206 WikiPathway:WP3565 DNA damage [adult cellular senescence] HOIP_0060376 ISBN:9781437717815 A variety of metabolic insults that accumulate over time may result in damage to nuclear and mitochondrial DNA. Although most DNA damage is repaired by DNA repair enzymes, some persist and accumulate as cells age. Robbins Basic Pathology 9th ed. PMID:29114066 Telomere damage, epigenetic dysregulation, DNA damage, and mitochondrial dysfunction are primary drivers of damage in aging. Several of these drivers of damage can induce senescence. Senescence can in turn drive the consequential aging hallmarks in response to damage: stem cell exhaustion and chronic inflammation. Other responses to damage, such as proteostatic dysfunction and nutrient signaling disruption, are also integrally linked with the senescence response. PMC:5748990 PMID:33450206 In 2000, further analysis of late-generation mTERC−/−;p53+/− mice (Artandi et al., 2000) revealed a humanized tumor spectrum of epithelial cancers possessing chromosomal rearrangements and nonreciprocal translocations typical of human cancer genomes. Thus, mice engineered to experience telomere-based crisis in the context of deactivated DNA damage signaling (p53 deficiency) illuminated a major mechanism driving the preponderance of epithelial cancers in aged humans and explained why such cancers develop radically altered cytogenetic profiles. HOIP:HOIP_0060377 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a tumor cell. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 response to tumor cell proliferation [chronic cellular senescence] HOIP_0060377 PMID:33328614 It was reported that a selective autophagy pathway, via mammalian target of rapamycin (mTOR) activation, contributes to sustain the protein synthesis of many senescence-associated secretory phenotype factors mainly in oncogene-induced senescent cells and that downregulation of several autophagy regulators delays the establishment of oncogene-induced senescence. more recently, LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. PMID:33328614 Oncogene activation is a powerful inducer of cellular senescence. Oncogene expression triggers an initial hyperproliferative phase that is intrinsically associated with altered DNA replication, which eventually engages DDR pathways and causes senescence. This process is known as oncogene-induced senescence (OIS). Loss of tumour suppressor expression can also induce proliferation arrest, as exemplified by PTEN loss-induced cellular senescence (PICS). Although initially PTEN loss-induced cellular senescence was not associated with DDR activation40, it was later found to be associated with hyperproliferation, DDR engagement and cellular senescence in vivo. Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation4, suggesting distinct underlying mechanisms. HOIP:HOIP_0060378 Any process that activates or increases the frequency, rate or extent of the release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:9780815345671 PMID:23140366 PMID:33328614 positive regulation of senescence-associated secretory phenotype (SASP) secretion [chronic cellular senescence] HOIP_0060378 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID:23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. PMID:33328614 It was reported that a selective autophagy pathway, via mammalian target of rapamycin (mTOR) activation, contributes to sustain the protein synthesis of many senescence-associated secretory phenotype factors mainly in oncogene-induced senescent cells and that downregulation of several autophagy regulators delays the establishment of oncogene-induced senescence. more recently, LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. HOIP:HOIP_0060379 Any process that activates or increases the frequency, rate or extent of the release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:9780815345671 PMID: 23140366 positive regulation of senescence-associated secretory phenotype (SASP) secretion HOIP_0060379 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID: 23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. HOIP:HOIP_0060380 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a tumor cell. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33328614 response to tumor cell proliferation[acute cellular senescence] HOIP_0060380 PMID:33328614 It was reported that a selective autophagy pathway, via mammalian target of rapamycin (mTOR) activation, contributes to sustain the protein synthesis of many senescence-associated secretory phenotype factors mainly in oncogene-induced senescent cells and that downregulation of several autophagy regulators delays the establishment of oncogene-induced senescence. more recently, LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. PMID:33328614 Oncogene activation is a powerful inducer of cellular senescence. Oncogene expression triggers an initial hyperproliferative phase that is intrinsically associated with altered DNA replication, which eventually engages DDR pathways and causes senescence. This process is known as oncogene-induced senescence (OIS). Loss of tumour suppressor expression can also induce proliferation arrest, as exemplified by PTEN loss-induced cellular senescence (PICS). Although initially PTEN loss-induced cellular senescence was not associated with DDR activation, it was later found to be associated with hyperproliferation, DDR engagement and cellular senescence in vivo. Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation, suggesting distinct underlying mechanisms. HOIP:HOIP_0060381 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence . PMID:33328614 negative regulation of apoptotic process [chronic cellular senescence] HOIP_0060381 PMID:33328614 Senescent cells frequently upregulate negative modulators of apoptosis, including members of the BCL-2 family (including BCL-2, BCL-W and BCL-XL), which confers resistance to apoptosis-inducing signals14,15. The senolytic agents ABT-737 and ABT-263 (also known as navitoclax) inhibit the activity of the BCL-2 family members, thereby permitting senescent cells to initiate apoptosis. Additionally, A-1331852 and A-1155463, which are thought to inhibit BCL-XL, have also been shown to exhibit senolytic activity202. HOIP:HOIP_0060382 Any process that activates or increases the rate or extent of tumor cell proliferation. positive regulation of tumor cell population proliferation positive regulation of tumor cell proliferation HOIP_0060382 HOIP:HOIP_0060383 Any process that activates or increases the rate or extent of cell proliferation. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:33328614 positive regulation of tumor cell population proliferation positive regulation of cell proliferation [adult cellular senescence] HOIP_0060383 HOIP:HOIP_0060384 Tumor cell proliferation is a subtype of cell proliferation: A process of the multiplication or reproduction of tumor cells, resulting in the rapid expansion of a tumor cell population. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:33328614 tumor cell proliferation [adult cellular senesence] HOIP_0060384 HOIP:HOIP_0060385 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of adult cellular senescence. inflammatory cell infiltration [adult cellular senescence] HOIP_0060385 HOIP:HOIP_0060386 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of adult cellular senescence. inflammatory cell infiltration [chronic cellular senescence] HOIP_0060386 HOIP:HOIP_0060387 Inflammatory cell infiltration is a subtype of moving A to the inside of B: A process that that moves the outside inflammatory cell to the inside in response to an inflammatory reaction. This entity is a specific course dependent process. This process can constitute the course of adult cellular senescence. inflammatory cell infiltration (transient) [acute cellular senescence] HOIP_0060387 HOIP:HOIP_0060388 HMGB1 activation is a subtype of molecular activation: A process that changes the activity of the HMGB1 to be higher. HMGB1 activation HOIP_0060388 HOIP:HOIP_0060389 HMGB1 activation is a subtype of molecular activation: A process that changes the activity of the HMGB1 to be higher. PMID:33328614 HMGB1 activation [chronic cellular senescence] HOIP_0060389 PMID:33328614 HMGB proteins also regulate the SASP. HMGB2 directly binds and specifically regulates SASP gene expression in oncogene-induced senescent cells, and its depletion diminishes SASP without affecting the senescence growth arrest. HMGB1 functions mainly as one of the damage-associated molecular patterns, also known as alarmins, that are released extracellularly to induce SASP-mediated paracrine senescence and alert the immune system. Furthermore, increased nuclear pore density during OIS, which is key to establish SAHF, regulates SASP expression by mediating heterochromatin reorganization. HOIP:HOIP_0060390 Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. innate immunity innate immune response [adult cellular senescence] HOIP_0060390 HOIP:HOIP_0060391 Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. innate immunity innate immune response [acute cellular senescence] HOIP_0060391 HOIP:HOIP_0060392 Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. innate immunity innate immune response [chronic cellular senescence] HOIP_0060392 HOIP:HOIP_0060393 Any process that activates or increases the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. positive regulation of innate immune response [adult cellular senescence] HOIP_0060393 HOIP:HOIP_0060394 Any process that activates or increases the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. positive regulation of innate immune response [chronic cellular senescence] HOIP_0060394 HOIP:HOIP_0060395 Any process that activates or increases the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. positive regulation of innate immune response [acute cellular senescence] HOIP_0060395 HOIP:HOIP_0060396 Any process that activates or increases the frequency, rate or extent of reactive oxygen species biosynthetic process. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24449267 positive regulation of reactive oxygen species biosynthetic process [chronic cellular senescence] HOIP_0060396 PMID:24449267 However, RNAi-mediated depletion of LMNB1 appears to be associated with reduced cell proliferation to various degrees in most (Shimi et al. 2011; Dreesen et al. 2013; Sadaie et al. 2013; Shah et al. 2013). Shimi et al. (2011) showed that depletion of LMNB1 is sufficient to induce senescence through modulation of reactive oxygen species (ROS) production. Perhaps paradoxically, they showed that depletion of LMNB1 leads to a reduction of ROS in a p53-depenent manner. Similarly, Barascu et al. (2012) showed that increased levels of LMNB1 are associated with ROS up-regulation and senescence. Generally, ROS is thought to be a cause of cellular damage, and it has been shown that ROS is increased during senescence. Furthermore, high levels of exogenous oxidative stress can induce senescence (Passos et al. 2007). However, increasing evidence suggests that modest levels of ROS can also contribute to cellular proliferation and survival (Sena and Chandel 2012). Thus, alterations in LMNB1 might contribute to a fine-tuning of ROS levels. HOIP:HOIP_0060397 Drug-, radiation-induced, or spontaneous injuries to DNA that introduce deviations from its normal double-helical conformation. These changes include structural distortions that interfere with replication and transcription, as well as point mutations that disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. If the damage is minor, it can often be repaired (DNA repair); extensive damage can induce apoptosis. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. ISBN:9781437717815 PMID:29114066 PMID:33450206 WikiPathway:WP3565 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ DNA damage (sustained) [chronic cellular senescence] HOIP_0060397 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ ISBN:9781437717815 A variety of metabolic insults that accumulate over time may result in damage to nuclear and mitochondrial DNA. Although most DNA damage is repaired by DNA repair enzymes, some persist and accumulate as cells age. Robbins Basic Pathology 9th ed. PMID:29114066 Telomere damage, epigenetic dysregulation, DNA damage, and mitochondrial dysfunction are primary drivers of damage in aging. Several of these drivers of damage can induce senescence. Senescence can in turn drive the consequential aging hallmarks in response to damage: stem cell exhaustion and chronic inflammation. Other responses to damage, such as proteostatic dysfunction and nutrient signaling disruption, are also integrally linked with the senescence response. PMC:5748990 PMID:33450206 In 2000, further analysis of late-generation mTERC−/−;p53+/− mice (Artandi et al., 2000) revealed a humanized tumor spectrum of epithelial cancers possessing chromosomal rearrangements and nonreciprocal translocations typical of human cancer genomes. Thus, mice engineered to experience telomere-based crisis in the context of deactivated DNA damage signaling (p53 deficiency) illuminated a major mechanism driving the preponderance of epithelial cancers in aged humans and explained why such cancers develop radically altered cytogenetic profiles. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ DNA damage jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig1.jpg HOIP:HOIP_0060398 Cell hyperproliferation signaling is a process that a signal of cell proliferation is transmitted. This process can constitute the course of adult cellular senescence. cell hyperproliferation signaling [adult cellular senescence] HOIP_0060398 HOIP:HOIP_0060399 The process that results in the patterns of cell differentiation that will arise in an embryo. embryonic pattern biosynthesis embryonic pattern specification embryonic pattern specification [embryonic cellular senescence] HOIP_0060399 HOIP:HOIP_0060400 Any biological process involved in returnig to a trajectory in the dynamical systems. https://doi.org/10.4324/9781315765471 homeorhesis process HOIP_0060400 https://doi.org/10.4324/9781315765471 The Strategy of the Genes HOIP:HOIP_0060401 Any biological process involved in returnig to a trajectory in the dynamical systems. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. https://doi.org/10.4324/9781315765471 embryonic developmental homeorhesis process [embryonic cellular senescence] HOIP_0060401 HOIP:HOIP_0060402 The process whose specific outcome is the progression of an embryo from its formation until the end of its embryonic life stage. The end of the embryonic stage is organism-specific. For example, for mammals, the process would begin with zygote formation and end with birth. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. Wikipedia:Embryogenesis embryogenesis embryo development [embryonic cellular senescence] HOIP_0060402 HOIP:HOIP_0060404 Increasing demand for response to oxidative stress is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oxidative stress to be higher. This entity is a specific course-dependent process. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. increasing demand for response to oxidative stress [chronic cellular senescence] HOIP_0060404 HOIP:HOIP_0060405 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. PMID:33328614 response to oxidative stress (sustained) [chronic cellular senescence] HOIP_0060405 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. PMID:121115731 HOIP:HOIP_0060406 Cell proliferation response signaling is a process that a signal of cell proliferation is transmitted. cell proliferation response signaling HOIP_0060406 HOIP:HOIP_0060407 Any process that results in induction of genomic instability. genomic instability [chronic cellular senescence] HOIP_0060407 HOIP:HOIP_0060408 Cell proliferation signaling is a process that a signal of cell proliferation is transmitted. This process can constitute the course of chroinc cellular senescence. cell hyperproliferation signaling (sustained) [chronic cellular senescence] HOIP_0060408 HOIP:HOIP_0060409 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33328614 AKT signaling (transient) [acute cellular senescence] HOIP_0060409 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation, suggesting distinct underlying mechanisms. HOIP:HOIP_0060410 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 AKT signaling (sustained) [chronic cellular senescence] HOIP_0060410 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation, suggesting distinct underlying mechanisms. HOIP:HOIP_0060411 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33328614 PI3K signaling (transient) [acute cellular senescence] HOIP_0060411 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation4, suggesting distinct underlying mechanisms. HOIP:HOIP_0060412 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 PI3K signaling (sustained) [chronic cellular senescence] HOIP_0060412 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation4, suggesting distinct underlying mechanisms. HOIP:HOIP_0060413 Any process that activates or increases the rate or extent of cell proliferation.This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 positive regulation of tumor cell population proliferation positive regulation of cell proliferation [chronic cellular senescence] HOIP_0060413 HOIP:HOIP_0060414 Tumor cell proliferation is a subtype of cell proliferation: A process of the multiplication or reproduction of tumor cells, resulting in the rapid expansion of a tumor cell population. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 tumor cell proliferation [chronic cellular senescence] HOIP_0060414 HOIP:HOIP_0060415 Increasing demand for oncogenic stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oncogenesis to be higher. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 increasing demand for oncogenic stress response [chronic cellular senescence] HOIP_0060415 PMID:33328614 Cellular senescence occurs in response to many different triggers, including DNA damage, telomere dysfunction, oncogene activation and organelle stress, and has been linked to processes such as tumour suppression, tissue repair, embryogenesis and organismal ageing. HOIP:HOIP_0060416 Any process that activates or increases the frequency, rate or extent of the insulin resistance. positive regulation of insulin resistance HOIP_0060416 HOIP:HOIP_0060417 Any process that stops, prevents, or reduces the frequency, rate, or extent of NfkB signaling. This entity is a specific course-dependent process. This process can constitute the course of senolytics. PMID:33328614 negative regulation of NfkB signaling [senolytics] HOIP_0060417 PMID:33328614 Compounds that modulate NF-κB signalling, including metformin, apigenin, kaempferol and BAY 11–7082, have also been shown to decrease SASP production. HOIP:HOIP_0060418 The totality of all processes through which the elimination of senescent cells by pharmacological agents is realized. PMID:26646499 PMID:33328614 under construction senolytics course HOIP_0060418 PMID:26646499 Chronic senescence results from long-term, slow macromolecular damage due to stresses such as protein misfolding, protein aggregation, dysfunction of the nuclear lamina, epigenetic changes and various kinds of DNA damage including telomere shortening (Fig. 1). PMID:33328614 These ‘senotherapeutic’ strategies can be broadly categorized into two categories: pharmacological agents termed ‘senolytics’, which eliminate senescent cells, and senomorphics, which prevent the detrimental cell-extrinsic effects of senescent cells and include SASP inhibitors. HOIP:HOIP_0060420 Any compound role which eliminates senescent cells. anti-cellular senescence agents senolytics agent HOIP_0060420 HOIP:HOIP_0060421 Any process that activates or increases the frequency, rate or extent of the insulin resistance. This entity is a specific course-dependent process. This process can constitute the course of chronic acute senescence with type 2 diabetes. PMID:26646499 positive regulation of insulin resistance [acute cellular senescence with type 2 diabetes] HOIP_0060421 HOIP:HOIP_0060422 Hypofunction of insulin secretion is a subtype of hypofunctioning: A process that performs a decreased or insufficient secretion of insulin. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. hypofunction of insulin secretion [chronic cellular senescence with type 2 diabetes] HOIP_0060422 HOIP:HOIP_0060423 PMID:26646499 chronic cellular senescence course associated with type 2 diabetes mellitus HOIP_0060423 HOIP:HOIP_0060424 Insulin deficiency is a subtype of malfunctioning process: A process that lacks performing the insulin function required. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with diabetes. insulin deficiency [chronic cellular senescence with type 2 diabetes] HOIP_0060424 HOIP:HOIP_0060425 Increasing blood glucose level is a subtype of increasing concentration: A process that changes the blood glucose concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with diabetes. hyperglycemia increasing blood glucose level [chronic cellular senescence with type 2 diabetes] HOIP_0060425 HOIP:HOIP_0060426 Microvascular dysfunction is a subtype of organ malfunction: A process that does not perform microvascular function correctly or not functioning at all. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. microvascular dysfunction [chronic cellular senescence with type 2 diabetes] HOIP_0060426 HOIP:HOIP_0060427 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with diabetes. PMID:26646499 insulin resistance (very high) [chronic cellular senescence with type 2 diabetes] HOIP_0060427 PMID:26646499 It appears that senescence is generated as a direct consequence of T2DM in both the fat and pancreas and drives progression of the disease. On the basis of this conclusion, we hypothesize that an increase in fat and β-cell senescence with age could explain the age-related increase in prevalence of T2DM. In the pancreas and fat, p16Ink4a levels increase with age in mice62 and humans101. This could restrict β-cell regenerative potential, limiting the adaptive response to insulin resistance101. In fat, levels of the SASP factors IL-6 and IL-1β increase with age, and these are known to cause insulin resistance when chronically high. HOIP:HOIP_0060429 Hypofunction of insulin secretion is a subtype of hypofunctioning: A process that performs a decreased or insufficient secretion of insulin. This entity is a specific course-dependent process. hypofunction of insulin secretion HOIP_0060429 HOIP:HOIP_0060430 The multiplication or reproduction of pancreatic B cells, resulting in the expansion of an pancreatic B cell population. Pancreatic B cell are cells of the pancreas that secrete insulin. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:26646499 type B pancreatic cell proliferation [acute cellular senescence with type 2 diabetes] HOIP_0060430 PMID:26646499 Proliferation of insulin-secreting pancreatic β cells is required to meet demand. If peripheral tissue insulin demand exceeds supply, T2DM can result. Consistent with this, the regenerative capacity of β cells is a very important factor in the development of T2DM. As in other diseases, increased replication of β cells lead to senescence through telomere attrition, in principle restricting the adaptive response to insulin resistance and driving T2DM. Accordingly, nutrient-induced diabetic mice have increased SA-β-GAL–positive β cells and a reduction in the proliferation marker Ki67 in late-stage disease. Further, deletion of CDKN2A rescues blood fasting glucose levels and improves β-cell proliferation in streptozocin-induced diabetes. HOIP:HOIP_0060431 A process that changes the telomere length to be short. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. ISBN:9780815345671 ISBN:9781437717815 PMID:26646499 telomere attrition telomere erosion telomere shortening [chronic cellular senescence with type 2 diabetes] HOIP_0060431 ISBN:9780815345671 Short or uncapped telomeres arise in somatic cells after several replictive cycles. The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. ISBN:9781437717815 Telomere length is maintained by nucleotide addition mediated by an enzyme called telomerase. Telomerase is a specialized RNA protein complex that uses its own RNA as a template for adding nucleotides to the end of chromosomes. Telomerase activity is expressed in germ cells and is present at low levels in stem cells, but it is absent in most somatic cells. Therefore, as most somatic cells age their telomeres become shorter and they exit just cell cycle resulting in an inability to generate new cells to replicate damaged ones. Robbins Basic Pathology 9th ed. Chapter1 PMID:26646499 Senescence may also predispose fat to becoming insulin resistant, as has been observed in fourth-generation Tert knockout mice, which have short telomeres, enhanced senescence in fat tissue and glucose intolerance. Surgical removal of Tert−/− fat tissue attenuates glucose intolerance, consistent with senescence in the fat driving insulin resistance. HOIP:HOIP_0060432 The release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. ISBN:9780815345671 PMID:26646499 senescence-associated secretory phenotype (SASP) factor secretion [chronic cellular senescence with type 2 diabetes] HOIP_0060432 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID:26646499 In fat, levels of the SASP factors IL-6 and IL-1β increase with age, and these are known to cause insulin resistance when chronically high. HOIP:HOIP_0060433 Chronic inflammatory response is a subtype of the inflammatory response: A process of chronic defensive reactions (by vertebrate tissues) to infection or injury. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. chronic inflammation [chronic cellular senescence with type 2 diabetes] HOIP_0060433 HOIP:HOIP_0060434 Insulin resistance (process) is a subtype of decreasing sensitivity: A process that changes the sensitivity to the circulating insulin to be lower. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence with diabetes. PMID:26646499 insulin resistance [chronic cellular senescence with type 2 diabetes] HOIP_0060434 PMID:26646499 Proliferation of insulin-secreting pancreatic β cells is required to meet demand. If peripheral tissue insulin demand exceeds supply, T2DM can result. Consistent with this, the regenerative capacity of β cells is a very important factor in the development of T2DM. As in other diseases, increased replication of β cells lead to senescence through telomere attrition99, in principle restricting the adaptive response to insulin resistance and driving T2DM. Accordingly, nutrient-induced diabetic mice have increased SA-β-GAL–positive β cells and a reduction in the proliferation marker Ki67 in late-stage disease. Further, deletion of CDKN2A rescues blood fasting glucose levels and improves β-cell proliferation in streptozocin-induced diabetes. HOIP:HOIP_0060435 PMID:26646499 acute cellular senescence course associated with type 2 diabetes mellitus HOIP_0060435 HOIP:HOIP_0060436 Increasing p16 level is a subtype of increasing quantity: A process that changes the amount of p16 level to be higher. increasing p16 level HOIP_0060436 HOIP:HOIP_0060437 Increasing p16 level is a subtype of increasing quantity: A process that changes the amount of p16 level to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence with type 2 diabetes. PMID:26646499 increasing p16 level [chronic cellular senescence with type 2 diabetes] HOIP_0060437 PMID:26646499 In the pancreas and fat, p16Ink4a levels increase with age in mice and humans. This could restrict β-cell regenerative potential, limiting the adaptive response to insulin resistance. HOIP:HOIP_0060438 Negative regulation of hyperglycemia is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of increasing of blood glucose level. negative regulation of hyperglycemia HOIP_0060438 HOIP:HOIP_0060439 Negative regulation of hyperglycemia is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of increasing of blood glucose level. negative regulation of hyperglycemia [acute cellular senescence with type two diabetes] HOIP_0060439 HOIP:HOIP_0060440 Hyperfunctioning of insulin secreation is a subtype of hyperfunctioning: A process that performs an excesssive secretion of insulin. hyperfunctioning of inslin secretion HOIP_0060440 HOIP:HOIP_0060441 Hyperfunctioning of insulin secreation is a subtype of hyperfunctioning: A process that performs an excesssive secretion of insulin. This process can constitute the course of acute cellular senescence with diabetes. hyperfunction of insulin secreation [acute cellular senescence with type two diabetes] HOIP_0060441 HOIP:HOIP_0060442 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:33328614 AKT signaling [chronic cellular senescence with type two diabetes] HOIP_0060442 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation, suggesting distinct underlying mechanisms. HOIP:HOIP_0060443 P53 signaling is a process that a signal is transmitted by the p53. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. ISBN:978081534567 PMID:26646499 p53 signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060443 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:26646499 Additional support for a causal role of fat senescence in T2DM progression comes from disruption of the p53-p21 pathway. Global or adipose-specific deletion of TP53 improves glucose tolerance in obese mice, reduces adipose senescent cell burden and attenuates insulin resistance mediated by p53-dependent inflammation. HOIP:HOIP_0060444 Regulation of gene expression by p53 is a subtype of regulation of gene expression: Any process that modulates the frequency, rate or extent of gene expression. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:26646499 regulation of gene expression by p53 [chronic cellular senescence with type 2 diabetes] HOIP_0060444 PMID:26646499 Additional support for a causal role of fat senescence in T2DM progression comes from disruption of the p53-p21 pathway. Global or adipose-specific deletion of TP53 improves glucose tolerance in obese mice, reduces adipose senescent cell burden and attenuates insulin resistance mediated by p53-dependent inflammation. HOIP:HOIP_0060445 Any process that activates or increases the frequency, rate or extent of the release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence with diabetes. ISBN:9780815345671 PMID:23140366 PMID:33328614 positive regulation of senescence-associated secretory phenotype (SASP) secretion [chronic cellular senescence with type two diabetes] HOIP_0060445 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID:23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. PMID:33328614 It was reported that a selective autophagy pathway, via mammalian target of rapamycin (mTOR) activation, contributes to sustain the protein synthesis of many senescence-associated secretory phenotype factors mainly in oncogene-induced senescent cells and that downregulation of several autophagy regulators delays the establishment of oncogene-induced senescence. more recently, LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. HOIP:HOIP_0060446 TOR signaling is a process that a signal is transmitted by the TOR (Target of rapamycin) . This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:33328614 mTOR signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060446 PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060447 P21 signaling is a process that a signal is transmitted by the p21. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:26646499 p21 signaling (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060447 PMID:26646499 Senescence may also predispose fat to becoming insulin resistant, as has been observed in fourth-generation Tert knockout mice, which have short telomeres, enhanced senescence in fat tissue and glucose intolerance59. Surgical removal of Tert−/− fat tissue attenuates glucose intolerance59, consistent with senescence in the fat driving insulin resistance. Additional support for a causal role of fat senescence in T2DM progression comes from disruption of the p53-p21 pathway. Global or adipose-specific deletion of TP53 improves glucose tolerance in obese mice, reduces adipose senescent cell burden and attenuates insulin resistance mediated by p53-dependent inflammation HOIP:HOIP_0060448 Increasing free fatty acid concentration in blood is a subtype of increasing lipid concentration in blood: A process that changes the free fatty acid concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:26646499 PMID:30510205 increasing free fatty acid concentration in blood [chronic cellular senescence with type 2 diabetes] HOIP_0060448 PMID:26646499 Chronic, high levels of free fatty acids in the circulation, due to obesity and a high-fat diet, can drive insulin resistance in peripheral adipose tissue by inducing proinflammatory senescent cells in fat. The pancreas can initially meet the increased demand for insulin through proliferation of insulin-producing β cells, maintaining normoglycemia with hyperinsulinemia. However, following telomere erosion, the capacity of β cells to expand production of insulin is limited by senescence. If insulin resistance worsens further, hyperglycemia and T2DM develop with accumulation of additional senescent cells in the fat. In contrast to T2DM development in youth, in advanced age, a form of peripheral insulin resistance already exists in the absence of overt dietary stresses that is due in part to the accumulation of senescent cells in aged fat. Therefore, the aged pancreas and fat can develop T2DM when stressed with a high-fat diet that is quite mild when compared to what is required for pathology to develop in youth. PMID:30510205 Diabetes and obesity, due to hyperglycemia and high concentrations of plasma free fatty acids, are known to pre-activate leukocytes and lead them to a pro-inflammatory phenotype. HOIP:HOIP_0060449 Obesity is a subtype of increasing weight: A process that changes the body weight to be higher. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type two diabetes. PMID:26646499 obesity [chronic cellular senescence with type two diabetes] HOIP_0060449 PMID:26646499 Chronic, high levels of free fatty acids in the circulation, due to obesity and a high-fat diet, can drive insulin resistance in peripheral adipose tissue by inducing proinflammatory senescent cells in fat. The pancreas can initially meet the increased demand for insulin through proliferation of insulin-producing β cells, maintaining normoglycemia with hyperinsulinemia. However, following telomere erosion, the capacity of β cells to expand production of insulin is limited by senescence. If insulin resistance worsens further, hyperglycemia and T2DM develop with accumulation of additional senescent cells in the fat. In contrast to T2DM development in youth, in advanced age, a form of peripheral insulin resistance already exists in the absence of overt dietary stresses that is due in part to the accumulation of senescent cells in aged fat. Therefore, the aged pancreas and fat can develop T2DM when stressed with a high-fat diet that is quite mild when compared to what is required for pathology to develop in youth. HOIP:HOIP_0060450 Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:29114066 negative regulation of autophagy [adult cellular senescence] HOIP_0060450 PMID:29114066 The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. HOIP:HOIP_0060451 Cell proliferation signaling is a process that a signal of cell proliferation is transmitted. type B pancreatic cell proliferation HOIP_0060451 HOIP:HOIP_0060452 Type B pancreatic cell exhaustion is a dysfunctional type B pancreatic cell.A process that performs a decreased or insufficient functioning of type B pancreatic cell. type B pancreatic cell exhaustion HOIP_0060452 HOIP:HOIP_0060453 Type B pancreatic cell exhaustion is a dysfunctional type B pancreatic cell.A process that performs a decreased or insufficient functioning of type B pancreatic cell. PMID:26646499 PMID:27018285 hupofunction of type B pancreatic cell [chronic cellular senescence with type two diabetes] Type B pancreatic cell exhaustion [chronic cellular senescence with type 2 diabetes] HOIP_0060453 PMID:26646499 The pancreas can initially meet the increased demand for insulin through proliferation of insulin-producing β cells, maintaining normoglycemia with hyperinsulinemia. However, following telomere erosion, the capacity of β cells to expand production of insulin is limited by senescence. If insulin resistance worsens further, hyperglycemia and T2DM develop with accumulation of additional senescent cells in the fat. PMID:27018285 Telomere attrition in β-cells further induces senescence and loss of β-cells, and impairment of insulin secretion, which leads to hyperglycemia. Telomere attrition in adipocytes further induces insulin resistance, which also leads to hyperglycemia. Thus, two vicious cycles are formed between hyperglycemia and telomere attrition, and p53 plays a crucial role in both processes. HOIP:HOIP_0060454 Overeating is a subtype of increasing quantity: A process that changes the ingestion amount of food to be larger. This entity is a specific course-dependent process. This process can constitute the course of acute senescence with type 2 diabetes. overeating [acute cellular senescence with type 2 diabetes] HOIP_0060454 HOIP:HOIP_0060455 Increasing amount of carbohydrate is a subtype of increasing quantity: A process that changes the amount of carbohydrates to be higher. This process can constitute the course of acute cellular senescence with type 2 diabetes. increasing amount of carbohydrate [acute cellular senescence with type 2 diabetes] HOIP_0060455 HOIP:HOIP_0060456 Increasing demand for metabolic stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oncogenesis to be higher. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. increasing demand for metabolic stress [chronic cellular senescence with type 2 diabetes] HOIP_0060456 HOIP:HOIP_0060457 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of metabolic change. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:33328614 response to metabolic stress [chronic cellular senescence with type 2 diabetes] HOIP_0060457 HOIP:HOIP_0060458 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of metabolic change stress. response to metabolic stress HOIP_0060458 HOIP:HOIP_0060459 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of metabolic change. response to metabolic stress [adult cellular senescence] HOIP_0060459 HOIP:HOIP_0060460 Any process that results in a change in the state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. cellular response to stress (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060460 HOIP:HOIP_0060461 P16 signaling is a process that a signal is transmitted by the p16. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 dibetes. PMID:26646499 p16 signaling (sustained) [chronic cellular senescence with type 2 dibetes] HOIP_0060461 PMID:26646499 In the pancreas and fat, p16Ink4a levels increase with age in mice and humans. This could restrict β-cell regenerative potential, limiting the adaptive response to insulin resistance. HOIP:HOIP_0060462 Cyclin D-CDK4/6 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin D-CDK4/6 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:24848057 PMID:26646499 PMID:29114066 Cyclin D-CDK4/6 complex inactivation (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060462 PMID:24848057 p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. PMID:26646499 Embryonic senescence is noncanonical, whereby an arrest maintained by p21 or the alternative CDK4 and CDK6 inhibitor p15Ink4b drives tissue patterning without involvement of p16Ink4a PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. HOIP:HOIP_0060463 RB activation is a subtype of molecular activation: A process that changes the activity of the RB ( protein kinase C) to be higher. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:24848057 RB activation (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060463 PMID:24848057 Activated p53 induces p21, which induces a temporal cell-cycle arrest by inhibiting cyclin E–Cdk2. p16Ink4a also inhibits cell-cycle progression but does so by targeting cyclin D–Cdk4 and cyclin D–Cdk6 complexes. Both p21 and p16Ink4a act by preventing the inactivation of Rb, thus resulting in continued repression of E2F target genes required for S-phase onset. HOIP:HOIP_0060464 Arrest of cell division is a subtype of arresting: A process that that results in the cessation of of cell cycle G1/S phase transition. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. arrest of cell cycle G1/S phase transition (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060464 HOIP:HOIP_0060465 Arrest of nuclear DNA replication is a subtype of arresting: A process that results in the cessation of a nuclear DNA replication. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. arrest of nuclear DNA replication (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060465 HOIP:HOIP_0060466 Any signalling pathway that decreases or inhibits the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. ISBN:978081534567 negative regulation of cell cycle G1/S phase transition [chronic cellular senescence with type 2 diabetes] HOIP_0060466 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. HOIP:HOIP_0060467 Any process that stops, prevents or reduces the frequency, rate or extent of nuclear cell cycle DNA replication. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. down regulation of DNA replication involved in S phase negative regulation of nuclear cell cycle DNA replication (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060467 HOIP:HOIP_0060468 Any process that modulates the rate or extent of progression through the cell cycle. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. regulation of cell cycle [chronic cellular senescence with type 2 diabetes] HOIP_0060468 HOIP:HOIP_0060469 A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. ISBN:978081534567 PMID:35165420 cell cycle arrest (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060469 ISBN:978081534567 The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. PMID:35165420 As telomeres reach a critical length, they become unable to bind enough telomere-capping proteins and are sensed as exposed DNA ends, which activates the DDR pathways that, through the induction of the cell cycle inhibitors p21 and p16, arrest proliferation. Such short telomeres, however, retain a sufficient number of telomere-binding proteins to inhibit DNA repair and avoid fusions, and consequently fuel a persistent DNA damage signal that enforces a permanent DNA damage-induced proliferative arrest. HOIP:HOIP_0060470 A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:33328614 cellular senescence (sustained) [chronic cellular senescence course with type 2 diabetes] HOIP_0060470 PMID:33328614 Besides prolonged DDR activation, senescence features include cell cycle arrest (by upregulation of p21 and p16 cell cycle inhibitors), oxidative damage (as detected by increased ROS levels), upregulation of the BCL-2 family of antiapoptotic proteins, which induce resistance to apoptosis, metabolic changes (including senescence-associated-β-galactosidase (SA-β-gal) accumulation), senescence-associated heterochromatin foci (SAHF) and a senescence-associated secretory phenotype (SASP). HOIP:HOIP_0060471 Tissue malfunction is a subtype of malfunctioning process: A process that cannot perform tissues function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. tissue dysfunction [chronic cellular senescence with type 2 diabetes] HOIP_0060471 HOIP:HOIP_0060472 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of metabolic change. This process can constitute the course of acute cellular senescence with type 2 diabetes. PMID:33328614 response to metabolic stress [acute cellular senescence with type 2 diabetes] HOIP_0060472 HOIP:HOIP_0060473 Hypofunction of insulin signaling is a subtype of hypofunction of signaling: A process that performs a decreased or insufficient insulin receptor signaling. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. hupofunction of insulin receptor signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060473 HOIP:HOIP_0060474 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. cellular response to insulin stimulus [acute cellular senescence with type 2 diabetes] HOIP_0060474 HOIP:HOIP_0060475 Any process that activates or increases the frequency, rate or extent of NfkB signaling. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 positive regulation of NfkB signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060475 PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. Because GATA4 levels increase following DDR activation and in senescent cells, it was proposed that GATA4 acts as the molecular link between DDR signalling and the subsequent NF-κB activation for full SASP establishment, although GATA4 regulation of the NF-κB pathway happens indirectly through increased expression and secretion of IL-1α, an upstream regulator of NF-κB. HOIP:HOIP_0060476 Increasing demand for metabolic stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oncogenesis to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. increasing demand for metabolic stress [acute cellular senescence with type 2 diabetes] HOIP_0060476 HOIP:HOIP_0060477 Overeating is a subtype of increasing quantity: A process that changes the ingestion amount of food to be larger. This entity is a specific course-dependent process. This process can constitute the course of chronic acute senescence with type 2 diabetes. overeating [chronic cellular senescence with type 2 diabetes] HOIP_0060477 HOIP:HOIP_0060478 Increasing free fatty acid concentration in blood is a subtype of increasing lipid concentration in blood: A process that changes the free fatty acid concentration in the blood to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence with type 2 diabetes. PMID:26646499 PMID:30510205 increasing free fatty acid concentration in blood [acute cellular senescence with type 2 diabetes] HOIP_0060478 PMID:26646499 Chronic, high levels of free fatty acids in the circulation, due to obesity and a high-fat diet, can drive insulin resistance in peripheral adipose tissue by inducing proinflammatory senescent cells in fat. The pancreas can initially meet the increased demand for insulin through proliferation of insulin-producing β cells, maintaining normoglycemia with hyperinsulinemia. However, following telomere erosion, the capacity of β cells to expand production of insulin is limited by senescence. If insulin resistance worsens further, hyperglycemia and T2DM develop with accumulation of additional senescent cells in the fat. In contrast to T2DM development in youth, in advanced age, a form of peripheral insulin resistance already exists in the absence of overt dietary stresses that is due in part to the accumulation of senescent cells in aged fat. Therefore, the aged pancreas and fat can develop T2DM when stressed with a high-fat diet that is quite mild when compared to what is required for pathology to develop in youth. PMID:30510205 Diabetes and obesity, due to hyperglycemia and high concentrations of plasma free fatty acids, are known to pre-activate leukocytes and lead them to a pro-inflammatory phenotype. HOIP:HOIP_0060479 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:33328614 PI3K signaling (sustained) [[chronic cellular senescence with type 2 diabetes] HOIP_0060479 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation4, suggesting distinct underlying mechanisms. HOIP:HOIP_0060480 Insulin receptor signaling is a subtype of signaling, in which a signal mediated by the insulin receptor. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence with type 2 diabetes. insulin receptor signaling [acute cellular senescence with type 2 diabetes] HOIP_0060480 HOIP:HOIP_0060481 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. cellular response to insulin stimulus [chronic cellular senescence with type 2 diabetes] HOIP_0060481 HOIP:HOIP_0060483 NfkB signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by NF-kappaB. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:33328614 Wikipedia:NF-κB NfkB signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060483 PMID:33328614 NF-κB and the transcription factor CCAAT/enhancer-binding protein-β (C/EBPβ) bind promoters of SASP genes and regulate their activation. Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. Because GATA4 levels increase following DDR activation and in senescent cells, it was proposed that GATA4 acts as the molecular link between DDR signalling and the subsequent NF-κB activation for full SASP establishment, although GATA4 regulation of the NF-κB pathway happens indirectly through increased expression and secretion of IL-1α, an upstream regulator of NF-κB. Wikipedia:NF-κB NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) is a protein complex that controls transcription of DNA, cytokine production and cell survival. HOIP:HOIP_0060484 The directed movement of the hexose monosaccharide glucose into a cell as a result of an insulin stimulus. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. glucose import in response to insulin stimulus [acute cellular senescence with type 2 diabetes] HOIP_0060484 HOIP:HOIP_0060486 MK2 signaling is a process that a signal is transmitted by the MK2 (MAP kinase-activated protein kinase 2) . This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:33328614 MK2 signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060486 PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060487 MK2 signaling is a process that a signal is transmitted by the MK2 (MAP kinase-activated protein kinase 2) . This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 MK2 signaling [chronic cellular senescence] HOIP_0060487 PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060488 MK2 signaling is a process that a signal is transmitted by the MK2 (MAP kinase-activated protein kinase 2) . This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 MK2 signaling HOIP_0060488 PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060490 Dysregulation of metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of metabolism appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:29114066 malfunctioning of metabolism [adult cellular senescence] HOIP_0060490 PMID:29114066 The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. PMC:5748990 HOIP:HOIP_0060491 Dehydration is a subtype of decreasing concentration: A process that changes the concentration of the body fulids to be lower. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. dehydration [chronic cellular senescence with type 2 diabetes] HOIP_0060491 HOIP:HOIP_0060492 Increasing osmotic pressure is a subtype of increasing pressure: A process that changes the osmotic pressure of the object to be higher. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. increasing osmotic pressure [chronic cellular senescence with type 2 diabetes] HOIP_0060492 HOIP:HOIP_0060493 Malfunction of protein biosynthesis is a subtype of malfunctioning: A process that cannot perform the protein biosynthesis function appropriately or cannot realize it at all. malfunction of protein biosynthesis HOIP_0060493 HOIP:HOIP_0060494 Malfunction of protein biosynthesis is a subtype of malfunctioning: A process that cannot perform the protein biosynthesis function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:29114066 malfunction of protein biosynthesis [adult cellular senescence] HOIP_0060494 PMID:29114066 The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. HOIP:HOIP_0060495 Increasing urine production is a subtype of increasing quantity: A process that changes the production amount of urine to be higher. increasing urine production HOIP_0060495 HOIP:HOIP_0060496 Increasing urine production is a subtype of increasing quantity: A process that changes the production amount of urine to be higher. increasing urine production [chronic cellular senescence with type 2 diabetes] HOIP_0060496 HOIP:HOIP_0060497 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of metabolic change. This process can constitute the course of acute cellular senescence. PMID:33328614 response to metabolic stress [acute cellular senescence] HOIP_0060497 HOIP:HOIP_0060498 The release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:9780815345671 PMID: 23140366 PMID:23140366 PMID:33328614 senescence-associated secretory phenotype (SASP) factor secretion (transient) [acute cellular senescence] HOIP_0060498 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID: 23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. PMID:23140366 In addition, some SASP factors induce an epithelial-to-mesenchymal transition in susceptible cells; others (for example, SFRP1, GROα, and IL-6) can alter stem cell proliferation or differentiation or modify stem cell niches. PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. PMID:33328614 Senescence-associated secretory phenotype (SASP) activation is a dynamic process that accompanies cell cycle exit initiated by senescence triggers. A core SASP programme comprises mainly proinflammatory interleukin-6 (IL-6), IL-8 and monocyte chemoattractant protein 1 (MCP1), regulated in an IL-1-dependent manner, and enzymes involved in extracellular matrix (ECM) remodelling, such as matrix metalloproteinases (MMPs), serine/cysteine proteinase inhibitors (SERPINs) and tissue inhibitors of metalloproteinases (TIMPs). More recently, additional core SASP effectors released as soluble molecules or in exosomes were identified, including GDF15, STC1 and MMP1. HOIP:HOIP_0060499 The release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. ISBN:9780815345671 PMID: 23140366 PMID:23140366 PMID:33328614 senescence-associated secretory phenotype (SASP) factor secretion [adult cellular senescence] HOIP_0060499 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID: 23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. PMID:23140366 In addition, some SASP factors induce an epithelial-to-mesenchymal transition in susceptible cells; others (for example, SFRP1, GROα, and IL-6) can alter stem cell proliferation or differentiation or modify stem cell niches. PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. PMID:33328614 Senescence-associated secretory phenotype (SASP) activation is a dynamic process that accompanies cell cycle exit initiated by senescence triggers. A core SASP programme comprises mainly proinflammatory interleukin-6 (IL-6), IL-8 and monocyte chemoattractant protein 1 (MCP1), regulated in an IL-1-dependent manner, and enzymes involved in extracellular matrix (ECM) remodelling, such as matrix metalloproteinases (MMPs), serine/cysteine proteinase inhibitors (SERPINs) and tissue inhibitors of metalloproteinases (TIMPs). More recently, additional core SASP effectors released as soluble molecules or in exosomes were identified, including GDF15, STC1 and MMP1. HOIP:HOIP_0060500 Any process that results in a change in the state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence with type 2 diabetes. cellular response to stress (transient) [acute cellular senescence with type 2 diabetes] HOIP_0060500 HOIP:HOIP_0060501 Phosphatidylinositol 3-kinase signaling is a subtype of signaling that a signal is transmitted by the phosphatidylinositol 3-kinase (PI3K). This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence with type 2 diabetes. PMID:33328614 PI3K signaling (transient) [acute cellular senescence with type 2 diabetes] HOIP_0060501 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation4, suggesting distinct underlying mechanisms. HOIP:HOIP_0060502 AKT signaling is a subtype of signaling that a signal is transmitted by the intracellular serine/threonine kinase protein kinase B (also called AKT). This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence with type 2 diabetes. PMID:33328614 AKT signaling (transient) [acute cellular senescence with type 2 diabetes] HOIP_0060502 PMID:33328614 Noteworthy, unlike oncogenic RAS or BRAF, activation of the PI3K–AKT pathway promotes p53-dependent senescence often in the absence of detectable hyperproliferation and strong DNA damage accumulation, suggesting distinct underlying mechanisms. HOIP:HOIP_0060503 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of metabolic change. This process can constitute the course of chronic cellular senescence. PMID:33328614 response to metabolic stress (sustained) [chronic cellular senescence] HOIP_0060503 HOIP:HOIP_0060504 FOXO signaling is a process that a signal is transmitted by the FOXO (forkhead box protein) . This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:21045807 PMID:27207509 PMID:33328614 FOXO signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060504 PMID:21045807 The transcriptional factor FoxO1 is a key regulator of cell metabolism, cell cycle and cell death. Its activity is tightly regulated by the phosphoinositide-3-kinase-AKT (PI3K-Akt) pathway, which leads to phosphorylation, cytoplasmic retention and inactivation of FoxO1. Here, we show that FoxO1 promotes inflammation by enhancing Tlr4-mediated signalling in mature macrophages. .Given the central role of macrophage Tlr4 in transducing extrinsic proinflammatory signals, the novel functions for FoxO1 in macrophages as a transcriptional regulator of the Tlr4 gene and its inflammatory pathway, highlights FoxO1 as a key molecular adaptor integrating inflammatory responses in the context of obesity and insulin resistance. PMID:27207509 In contrast, insulin, but not LPS, induced mammalian target of rapamycin complex 2 (mTORC2)-dependent phosphorylation of Akt on Ser(473) and FoxO1/O3a on Thr(24/32) in leukocytes and neutrophils. PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060505 FOXO signaling is a process that a signal is transmitted by the FOXO (forkhead box protein O3) family. PMID:33328614 FOXO signaling HOIP_0060505 PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060506 A process that performs a decreased or insufficient mTORC2 signaling. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:27207509 PMID:33328614 hypofunction of mTORC2 signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060506 PMID:27207509 In contrast, insulin, but not LPS, induced mammalian target of rapamycin complex 2 (mTORC2)-dependent phosphorylation of Akt on Ser(473) and FoxO1/O3a on Thr(24/32) in leukocytes and neutrophils. PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060507 Oncogene activation is a subtype of activation: A process that changes the activity of the oncogene to be higher. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:19345328 oncogene activation [adult cellular senescence] HOIP_0060507 HOIP:HOIP_0060508 Any process that stops, prevents, or reduces the frequency, rate or extent of the transcription mediated by RNA polymerase II E2F. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. doi/10.1895/wormbook.1.30.2 negative regulation of transcription by RNA polymerase II E2F (sustained) [chronic cellular senescence with type 2 diabetes] HOIP_0060508 doi/10.1895/wormbook.1.30.2 Although present, neither SKN-1 nor PAL-1 activates gene expression in the P cells. This is because the germ line precursors are protected from activating somatic programs of gene expression by PIE-1, which is restricted to the P cell at each asymmetric division (Figure 5) (Mello et al., 1996). Germ-line precursors in C. elegans, as in many organisms, are transcriptionally quiescent. Inhibition of transcription correlates with the failure to phosphorylate the C-terminal domain of RNA polymerase on Serine-5 (Ser-5) and Ser-2, which are needed for transcription initiation and elongation, respectively. These phophorylation events are inhibited by PIE-1 in the P cells of early C. elegans embryos (Tenenhaus et al., 1998). In vitro studies indicate that PIE-1 directly binds to, and inhibits, the kinase needed for Ser-2 phosphorylation (Batchelder et al., 1999). Altered forms of PIE-1 that do not bind the kinase fail to inhibit Ser-2 phosphorylation in vivo, but can still suppress transcription and promote germ-line fate through effects on Ser-5 phosphorylation (Ghosh and Seydoux, 2008). Inhibition of transcription is thought to prevent SKN-1, PAL-1 and other transcription factors from activating gene expression in the P cells. However, after asymmetric division of P2, the degradation of PIE-1 from the somatic daughter via the MEX-5/ZIF-1 pathway described above relieves transcriptional repression, allowing SKN-1 activation of target genes in EMS. Similarly, after the P2 and P3 divisions, disappearance of PIE-1 allows PAL-1 activation of target genes to commence. PIE-1 is also important for activating the translation of NOS-2 in the P4 cell; although the mechanism is unknown, this function of PIE-1 is separable from its role in preventing transcription (D'Agostino et al., 2006; Tenenhaus et al., 2001). HOIP:HOIP_0060509 A protein complex that contains at least TOR (target of rapamycin) and Rictor (rapamycin-insensitive companion of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of PKB (also called AKT). In Saccharomyces, the complex contains Avo1p, Avo2p, Tsc11p, Lst8p, Bit61p, Slm1p, Slm2p, and Tor2p. TOR complex 2 mTORC2 complex TORC2 complex HOIP_0060509 HOIP:HOIP_0060510 A protein complex that contains at least TOR (target of rapamycin) and Rictor (rapamycin-insensitive companion of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of PKB (also called AKT). In Saccharomyces, the complex contains Avo1p, Avo2p, Tsc11p, Lst8p, Bit61p, Slm1p, Slm2p, and Tor2p. mTOR complex 2 mTORC2 complex mTORC2 complex HOIP_0060510 HOIP:HOIP_0060511 A protein complex that contains at least mTOR (target of rapamycin) and Raptor (regulatory-associated protein of mTOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. Wikipedia:MTORC1 TOR complex 1 mTORC1 complex mTORC1 complex HOIP_0060511 HOIP:HOIP_0060512 TLR4 signaling is a subtype of TLR biological signaling: Any processes of molecular signals generated as a consequence of binding to toll-like receptor 4. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. PMID:27207509 PMID:31623280 TLR4 signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060512 PMID:27207509 In contrast, insulin, but not LPS, induced mammalian target of rapamycin complex 2 (mTORC2)-dependent phosphorylation of Akt on Ser(473) and FoxO1/O3a on Thr(24/32) in leukocytes and neutrophils. Insulin suppressed LPS-induced responses in a dose- and time-dependent manner. AS1842856, a FoxO1 inhibitor, also suppressed TLR4 signaling. We propose that insulin is a homeostatic regulator of leukocyte responses to LPS/TLR4 and that the signaling intermediates expressed in leukocytes of patients with type 2 diabetes indicate TLR4 signaling dominance and deficient insulin signaling. The data suggest that insulin suppresses LPS/TLR4 signals in leukocytes through the mTORC2-Akt-FoxO signaling axis. PMID:31623280 Gan et al. showed that mitochondrial-free cholesterol deposition causes hepatocyte apoptosis and necrosis through c-Jun N-terminal kinase (JNK) activation, associated with increased high-mobility group box 1 (HMGB1), and cytolytic effects on neighboring hepatocytes driven by Toll-like receptor 4 (TLR4). Hepatocyte free cholesterol lipotoxicity results from JNK1-mediated mitochondrial injury and is HMGB1 and TLR4-dependent. HOIP:HOIP_0060513 Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence with type 2 diabetes. innate immunity innate immune response [chronic cellular senescence with type 2 diabetes] HOIP_0060513 HOIP:HOIP_0060514 NfkB signaling is a subtype of biological signaling: Any processes of molecular signals transduced with the regulation of transcription of target genes by NF-kappaB. This entity is a specific course-dependent process. This process can constitute the course of senolytics. PMID:33328614 Wikipedia:NF-κB NfkB signaling [senolytics] HOIP_0060514 PMID:33328614 NF-κB and the transcription factor CCAAT/enhancer-binding protein-β (C/EBPβ) bind promoters of SASP genes and regulate their activation. Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. Because GATA4 levels increase following DDR activation and in senescent cells, it was proposed that GATA4 acts as the molecular link between DDR signalling and the subsequent NF-κB activation for full SASP establishment, although GATA4 regulation of the NF-κB pathway happens indirectly through increased expression and secretion of IL-1α, an upstream regulator of NF-κB. Wikipedia:NF-κB NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) is a protein complex that controls transcription of DNA, cytokine production and cell survival. HOIP:HOIP_0060515 mTORC2 signaling is a process that intracellular molecular signals mediated by TORC2; TOR (rapamycin-insensitive companion of TOR) in complex with at least Rictor (regulatory-associated protein of TOR), or orthologs of, and other signaling components. PMID:27207509 mTORC2 signaling HOIP_0060515 PMID:27207509 In contrast, insulin, but not LPS, induced mammalian target of rapamycin complex 2 (mTORC2)-dependent phosphorylation of Akt on Ser(473) and FoxO1/O3a on Thr(24/32) in leukocytes and neutrophils. HOIP:HOIP_0060516 A process that performs a decreased or insufficient mTOR signaling (mTORC2) . hypofunction of mTORC2 signaling HOIP_0060516 HOIP:HOIP_0060517 TOR signaling is a process that a signal is transmitted by the mTOR (mammalian target of rapamycin) . PMID:33328614 mTOR signaling HOIP_0060517 PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060518 Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 positive regulation of autophagy [chronic cellular senescence with type 2 diabetes] HOIP_0060518 PMID:33328614 Indeed, it was reported that a selective autophagy pathway, via mammalian target of rapamycin (mTOR) activation, contributes to sustain the protein synthesis of many senescence-associated secretory phenotype factors mainly in oncogene-induced senescent cells and that downregulation of several autophagy regulators delays the establishment of oncogene-induced senescence. more recently, LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. Inhibition of autophagy prevents lamin B1 degradation and ensures nuclear envelope integrity in senescent cells. PMID:33328614 The mammalian target of rapamycin (mTOR) pathway also promotes SASP production through increased translation of subsets of mRNAs, including that encoding for IL-1α. In concert with transcription factors, the epigenetic reader bromodomain-containing protein 4 (BRD4), an acetylated histone-binding protein involved in oncogenesis, is recruited to superenhancers adjacent to SASP genes, thus contributing to the proper execution of cellular senescence. HOIP:HOIP_0060519 The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:26524528 PMID:33328614 autophagy [chronic cellular senescence with type 2 diabetes] HOIP_0060519 PMID:26524528 PMID:26524528 The autophagy protein LC3/Atg8, which is involved in autophagy membrane trafficking and substrate delivery, is present in the nucleus and directly interacts with the nuclear lamina protein Lamin B1, and binds to lamin-associated domains (LADs) on chromatin. This LC3-Lamin B1 interaction does not downregulate Lamin B1 during starvation, but mediates its degradation upon oncogenic insults, such as by activated Ras. Lamin B1 degradation is achieved by nucleus-to-cytoplasm transport that delivers Lamin B1 to the lysosome. Inhibiting autophagy or the LC3-Lamin B1 interaction prevents activated Ras-induced Lamin B1 loss and attenuates oncogene-induced senescence in primary human cells. PMID:33328614 LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. Inhibition of autophagy prevents lamin B1 degradation and ensures nuclear envelope integrity in senescent cells HOIP:HOIP_0060520 mTORC1 signaling is a process that intracellular molecular signals mediated by mTORC1; mTOR (mammalian target of rapamycin) in complex with at least Raptor (regulatory-associated protein of TOR), or orthologs of, and other signaling components. PMID:27207509 PMID:33328614 mTORC1 signaling HOIP_0060520 PMID:27207509 In contrast, insulin, but not LPS, induced mammalian target of rapamycin complex 2 (mTORC2)-dependent phosphorylation of Akt on Ser(473) and FoxO1/O3a on Thr(24/32) in leukocytes and neutrophils. PMID:33328614 For example, the mammalian target of rapamycin (mTOR) pathway, which coordinates cell growth and metabolism in response to nutrients, and also promotes SASP production through increased translation of subsets of mRNAs, including the membrane-bound and upstream regulator of NF-κB, IL-1α and the serine/threonine kinase MK2, which indirectly stabilizes many cytokine-encoding transcripts. HOIP:HOIP_0060521 Hypofunction of cellular response to insulin stimulus is a subtype of hypofunctioning: A process that performs a decreased or insufficient cellular response to insulin stimulus. hupofunction of cellular response to insulin stimulus HOIP_0060521 HOIP:HOIP_0060522 Hypofunction of insulin signaling is a subtype of hypofunction of signaling: A process that performs a decreased or insufficient insulin receptor signaling. hypofunction of insulin receptor signaling HOIP_0060522 HOIP:HOIP_0060524 A signaling process that controls cell cycle progression by monitoring the integrity of specific cell cycle events. cell cycle checkpoint signaling process HOIP_0060524 HOIP:HOIP_0060526 A signal transduction process that contributes to a DNA damage checkpoint DNA damage checkpoint signaling process HOIP_0060526 HOIP:HOIP_0060528 A signal transduction process that contributes to a DNA damage checkpoint.This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. DNA damage checkpoint signaling process [adult cellular senescence] HOIP_0060528 HOIP:HOIP_0060529 A signal transduction process that contributes to a DNA damage checkpoint.This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. DNA damage checkpoint signaling process [acute cellular senescence] HOIP_0060529 HOIP:HOIP_0060530 A signal transduction process that contributes to a DNA damage checkpoint.This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. DNA damage checkpoint signaling process [chronic cellular senescence] HOIP_0060530 HOIP:HOIP_0060533 A signal transduction process that contributes to a DNA replication checkpoint, that prevents the initiation of nuclear division until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome. DNA replication checkpoint signal transduction involved in DNA replication checkpoint signal transduction resulting in cell cycle arrest DNA replication checkpoint signaling process HOIP_0060533 HOIP:HOIP_0060535 A signal transduction process that contributes to a DNA replication checkpoint, that prevents the initiation of nuclear division until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome. This process can constitute the course of adult cellular senescence. DNA replication checkpoint signal transduction involved in DNA replication checkpoint signal transduction resulting in cell cycle arrest DNA replication checkpoint signaling process [adult cellular senescence] HOIP_0060535 HOIP:HOIP_0060536 A signal transduction process that contributes to a DNA replication checkpoint, that prevents the initiation of nuclear division until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome. This process can constitute the course of acute cellular senescence. DNA replication checkpoint signal transduction involved in DNA replication checkpoint signal transduction resulting in cell cycle arrest DNA replication checkpoint signaling process [acute cellular senescence] HOIP_0060536 HOIP:HOIP_0060537 A signal transduction process that contributes to a DNA replication checkpoint, that prevents the initiation of nuclear division until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome. This process can constitute the course of acute cellular senescence. DNA replication checkpoint signal transduction involved in DNA replication checkpoint signal transduction resulting in cell cycle arrest DNA replication checkpoint signaling process [chronic cellular senescence] HOIP_0060537 HOIP:HOIP_0060539 Inflammatory gene expression by NF-kappa B is a subtype of gene expression by transcriptional factor: The process in which a gene sequence is converted into a mature gene product or products (proteins or RNA) related to the inflammation by NF-kappa B. This entity is a specific course-dependent process. This process can constitute the course of senolytics. PMID:33328614 SASP related protein expression by NF-kappa B [senolytics] HOIP_0060539 PMID:33328614 NF-κB and the transcription factor CCAAT/enhancer-binding protein-β (C/EBPβ) bind promoters of SASP genes and regulate their activation. Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. Because GATA4 levels increase following DDR activation and in senescent cells, it was proposed that GATA4 acts as the molecular link between DDR signalling and the subsequent NF-κB activation for full SASP establishment, although GATA4 regulation of the NF-κB pathway happens indirectly through increased expression and secretion of IL-1α, an upstream regulator of NF-κB. HOIP:HOIP_0060540 The release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of senolytics. ISBN:9780815345671 PMID: 23140366 PMID:23140366 PMID:33328614 senescence-associated secretory phenotype (SASP) factor secretion [senolytics] HOIP_0060540 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID: 23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. PMID:23140366 In addition, some SASP factors induce an epithelial-to-mesenchymal transition in susceptible cells; others (for example, SFRP1, GROα, and IL-6) can alter stem cell proliferation or differentiation or modify stem cell niches. PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. PMID:33328614 Senescence-associated secretory phenotype (SASP) activation is a dynamic process that accompanies cell cycle exit initiated by senescence triggers. A core SASP programme comprises mainly proinflammatory interleukin-6 (IL-6), IL-8 and monocyte chemoattractant protein 1 (MCP1), regulated in an IL-1-dependent manner, and enzymes involved in extracellular matrix (ECM) remodelling, such as matrix metalloproteinases (MMPs), serine/cysteine proteinase inhibitors (SERPINs) and tissue inhibitors of metalloproteinases (TIMPs). More recently, additional core SASP effectors released as soluble molecules or in exosomes were identified, including GDF15, STC1 and MMP1. HOIP:HOIP_0060541 Chronic inflammatory response is a subtype of the inflammatory response: A process of chronic defensive reactions (by vertebrate tissues) to infection or injury. This entity is a specific course-dependent process. This process can constitute the course of senolytics. chronic inflammation [senolytics] HOIP_0060541 HOIP:HOIP_0060546 Any process that responds of a cell to the demand of embryonic pattern specification. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. response to embryonic pattern specification demand (transient) [embryonic cellular senescence] HOIP_0060546 HOIP:HOIP_0060547 Any process that responds of a cell to the demand of embryonic pattern specification. response to embryonic pattern specification demand HOIP_0060547 HOIP:HOIP_0060548 P21 signaling is a process that a signal is transmitted by the p21. This entity is a specific course-dependent process. This process can constitute the course of embryonic cellular senescence. PMID:24848057 PMID:33328614 p21 signaling (transient) [embryonic cellular senescence] HOIP_0060548 PMID:24848057 What both these stresses have in common with telomere damage is that they activate the DNA damage response (DDR), a signalling pathway in which ATM or ATR kinases block cell-cycle progression through stabilization of p53 and transcriptional activation of the cyclin-dependent kinase (Cdk) inhibitor p21. PMID:33328614 p21 and p16 are two cyclin-dependent kinase inhibitors that are components of the tumour suppressor pathways governed by p53 and RB, and often accumulate in senescent cells. Because p21 and p16 expression levels are sufficient to establish and maintain the senescence-associated growth arrest, they are used to identify senescent cells in tissues and cultured cells. HOIP:HOIP_0060551 A process that prevents non-homologous end joining at telomere, thereby ensuring that telomeres do not fuse. protection from NHEJ-mediated telomere fusion protection from non-homologous end joining at telomere HOIP_0060551 HOIP:HOIP_0060553 Negative regulation of telomere fusion is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the telomere fusion. negative regulation of telomere fusion HOIP_0060553 2 HOIP:HOIP_0060554 A process in which telomeres fuse, thereby leading to chromosome instability. PMID:17908935 telomere fusion HOIP_0060554 PMID:17908935 The loss of telomere function can result in telomeric fusion events that lead to the types of genomic rearrangements, such as nonreciprocal translocations, that typify early-stage carcinogenesis. HOIP:HOIP_0060555 cyclin B1-CDK1 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin B1-CDK1 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:24746669 cyclin B1-CDK1 complex inactivation (sustained) [chronic cellular senescence] HOIP_0060555 PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. HOIP:HOIP_0060556 A cyclin B1:Cdk1 whose components are encoded in the genome of human. cyclin B1-CDK1 complex (human) HOIP_0060556 HOIP:HOIP_0060557 Negative regulation of telomere fusion is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of the telomere fusion. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:34676498 negative regulation of telomere fusion [chronic cellular senescence] HOIP_0060557 HOIP:HOIP_0060559 cyclin A1-CDK1 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin A1-CDK1 complex to be lower. cyclin A1-CDK1 complex inactivation HOIP_0060559 HOIP:HOIP_0060563 A cyclin A1:Cdk1 whose components are encoded in the genome of human. http://purl.obolibrary.org/obo/PR_000029190 cyclin A1-CDK1 complex (human) HOIP_0060563 HOIP:HOIP_0060565 The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:23230272 double-strand break repair [acute cellular senescence] HOIP_0060565 PMID:23230272 The PARP1-dependent localization of BAL1-BBAP functionally limits both early and delayed DNA damage and enhances cellular viability independent of ATM, MDC1, and RNF8. These data establish that BAL1 and BBAP are bona fide members of a DNA damage response pathway and are directly associated with PARP1 activation, BRCA1 recruitment, and double-strand break repair. HOIP:HOIP_0060566 Any process that stops, prevents or reduces the frequency, rate or extent of double-strand break repair via homologous recombination. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:3035621 PMID:31544964 negative regulation of HDR negative regulation of double-strand break repair via homologous recombination [chronic cellular senescence] HOIP_0060566 PMID:3035621 Here we demonstrate that cGAS inhibits homologous recombination in mouse and human models. DNA damage induces nuclear translocation of cGAS in a manner that is dependent on importin-α, and the phosphorylation of cGAS at tyrosine 215-mediated by B-lymphoid tyrosine kinase-facilitates the cytosolic retention of cGAS. In the nucleus, cGAS is recruited to double-stranded breaks and interacts with PARP1 via poly(ADP-ribose). The cGAS-PARP1 interaction impedes the formation of the PARP1-Timeless complex, and thereby suppresses homologous recombination. Nuclear cGAS suppresses DNA repair and promotes tumorigenesis PMID:31544964 We demonstrate that cGAS is constantly present in the nucleus as a chromatin‐bound protein where it acts as a negative regulator of homologous recombination‐mediated DNA repair, thereby accelerating micronucleus generation and death of cells under genomic stress. We show that this non‐canonical cGAS function is independent of the STING axis. DSB repair occurs via two major pathways: non‐homologous end‐joining (NHEJ) that is active throughout the cell cycle and homologous recombination (HR) that occurs during the S and G2 cell cycle (Chapman et al, 2012; Ceccaldi et al, 2016). HOIP:HOIP_0060567 A cyclin A1:Cdk2 whose components are encoded in the genome of human. http://purl.obolibrary.org/obo/PR_000029190 cyclin A1-CDK2 complex (human) HOIP_0060567 HOIP:HOIP_0060568 cyclin A2-CDK1 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin A1-CDK2 complex to be lower. cyclin A1-CDK2 complex inactivation HOIP_0060568 HOIP:HOIP_0060570 Any process that stops, prevents or reduces the frequency, rate or extent of double-strand break repair via nonhomologous end joining. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:34676498 negative regulation of double-strand break repair via nonhomologous end joining [chronic cellular senescence] HOIP_0060570 PMID:34676498 Here, we identify cGAS as an essential regulator in inhibiting mitotic DNA double-strand break (DSB) repair and protecting short telomeres from end-to-end fusion independent of the canonical cGAS-STING pathway. cGAS associates with telomeric/subtelomeric DNA during mitosis when TRF1/TRF2/POT1 are deficient on telomeres. Depletion of cGAS leads to mitotic chromosome end-to-end fusions predominantly occurring between short telomeres. Mechanistically, cGAS interacts with CDK1 and positions them to chromosome ends. Thus, CDK1 inhibits mitotic non-homologous end joining (NHEJ) by blocking the recruitment of RNF8. HOIP:HOIP_0060571 Negative regulation of p53 degradation by ubiquitin-protein ligase is a subtype of negative regulation of protein catabolic process: A process that stops, prevents, or reduces the frequency, rate or extent of p53 degradation by by ubiquitin-protein ligase MDM2 . This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33328614 negative regulation of p53 degradation by ubiquitin-protein ligase Mdm2 [acute cellular senescence] HOIP_0060571 PMID:33328614 In addition to the DDR cascade being activated, the tumour suppressor ARF stabilizes p53, which contributes to the induction of senescence. Efforts have been devoted to assessing the contribution of these two major routes, the DDR and ARF pathways, to p53-dependent senescence establishment especially in response to oncogenic challenges. The original view, based mainly on murine studies, was that the DDR and ARF play antagonistic roles, as ARF was transcriptionally activated during tumorigenesis in a DDR-independent manner. More recently, a tight regulatory network in human cancer models was reported, whereby ATM suppresses ARF levels and ARF acts as a secondary barrier to cancer progression when ATM is inactivated. Consistent with this temporal regulation, DDR precedes ARF engagement, whose activation is detected at later stages of cancer progression and less frequently than DDR. HOIP:HOIP_0060572 Any process that stops, prevents or reduces the frequency, rate or extent of double-strand break repair. negative regulation of double-strand break repair HOIP_0060572 HOIP:HOIP_0060573 Any process that activates or increases the frequency, rate or extent of apoptotic process. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33833439 positive regulation of tumor cell apoptotic process [acute cellular senescence] HOIP_0060573 PMID:33833439 Activation of STING initiates cascades that support anti-proliferative cell states, including cellular senescence, and ultimately cell death (a more detailed discussion of senescence is provided further below). To that end, STING promotes induction of cell-cycle inhibitors (such as p21) and pro-apoptotic BH3-only proteins. Alternatively, and in a more direct mode of action, phosphorylated IRF3 can also interact with the pro-apoptotic proteins BAX and BAK and thereby lead to transcription-independent induction of apoptosis downstream of STING. HOIP:HOIP_0060574 MDM2 inactivation is a subtype of molecular inactivation: A process that changes the activity of MDM2 to be lower. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:29114066 PMID:33328614 MDM2 inactivation [acute cellular senescence] HOIP_0060574 PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. PMID:33328614 In addition to the DDR cascade being activated, the tumour suppressor ARF stabilizes p53, which contributes to the induction of senescence. Efforts have been devoted to assessing the contribution of these two major routes, the DDR and ARF pathways, to p53-dependent senescence establishment especially in response to oncogenic challenges. The original view, based mainly on murine studies, was that the DDR and ARF play antagonistic roles, as ARF was transcriptionally activated during tumorigenesis in a DDR-independent manner. More recently, a tight regulatory network in human cancer models was reported, whereby ATM suppresses ARF levels and ARF acts as a secondary barrier to cancer progression when ATM is inactivated. Consistent with this temporal regulation, DDR precedes ARF engagement, whose activation is detected at later stages of cancer progression and less frequently than DDR. HOIP:HOIP_0060575 MDM2 inactivation is a subtype of molecular inactivation: A process that changes the activity of MDM2 to be lower. PMID:29114066 MDM2 inactivation HOIP_0060575 PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. HOIP:HOIP_0060576 Decreasing PARP1 level is a subtype of decreasing quantity: A process that changes the amount of PARP1 level to be lower. decreasing PARP1 level HOIP_0060576 HOIP:HOIP_0060577 Decreasing PARP1 level is a subtype of decreasing quantity: A process that changes the amount of PARP1 level to be lower. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:26822533 decreasing PARP1 level [chronic cellular senescence] HOIP_0060577 PMID:26822533 We show that unlike fibroblasts, senescent epithelial cells do not activate an ATM-or ATR-dependent DNA damage response (DDR), but accumulate oxidative-stress-induced DNA single-strand breaks (SSBs). These breaks remain unrepaired because of a decrease in PARP1 expression and activity. This leads to the formation of abnormally large and persistent XRCC1 foci that engage a signalling cascade involving the p38MAPK and leading to p16 upregulation and cell cycle arrest.Importantly, the default in SSB repair also leads to the emergence of post-senescent transformed and mutated precancerous cells. In human-aged skin, XRCC1 foci accumulate in the epidermal cells in correlation with a decline of PARP1, whereas DDR foci accumulate mainly in dermal fibroblasts. HOIP:HOIP_0060578 Negative regulation of cell cycle G2/M phase transition is a subtype of negative regulation of cell cycle: Any process that stops, prevents or reduces the frequency, rate or extent of cell cycle G2/M phase transition. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24746669 negative regulation of cell cycle G2/M phase transition [cellular senescence] HOIP_0060578 PMID:24746669 Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0060579 Negative regulation of cell cycle G2/M phase transition is a subtype of negative regulation of cell cycle: Any process that stops, prevents or reduces the frequency, rate or extent of cell cycle G2/M phase transition. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24746669 negative regulation of cell cycle G2/M phase transition (transient) [acute cellular senescence] HOIP_0060579 PMID:24746669 Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0060580 Negative regulation of cell cycle G2/M phase transition is a subtype of negative regulation of cell cycle: Any process that stops, prevents or reduces the frequency, rate or extent of cell cycle G2/M phase transition. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24746669 negative regulation of cell cycle G2/M phase transition (sustained) [chronic cellular senescence] HOIP_0060580 PMID:24746669 Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0060581 Negative regulation of cell cycle G2/M phase transition is a subtype of negative regulation of cell cycle: Any process that stops, prevents or reduces the frequency, rate or extent of cell cycle G2/M phase transition. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24746669 negative regulation of cell cycle G2/M phase transition [adult cellular senescence] HOIP_0060581 PMID:24746669 Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. As expected, in vivo phosphorylation of each subunit at G2/M phase was inhibited in cells transfected with Cdk1 siRNA (Figure 4C, lane 3), which arrested cells at the G2/M phase (Figure S5). HOIP:HOIP_0060582 cyclin B1-CDK1 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin B1-CDK1 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. PMID:24746669 cyclin B1-CDK1 complex inactivation [cellular senescence] HOIP_0060582 PMID:24746669 Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. HOIP:HOIP_0060583 cyclin B1-CDK1 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin B1-CDK1 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:24746669 cyclin B1-CDK1 complex inactivation (transient) [acute cellular senescence] HOIP_0060583 PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. HOIP:HOIP_0060584 cyclin B1-CDK1 complex inactivation is a subtype of molecular inactivation: A process that changes the activity of the cyclin B1-CDK1 complex to be lower. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:24746669 cyclin B1-CDK1 complex inactivation [adult cellular senescence] HOIP_0060584 PMID:24746669 not reported in the liver. Mitochondria-targeted cyclin B1/Cdk1 increases mitochondrial respiration with enhanced oxygen consumption and ATP generation, which provides cells with efficient bioenergy for G2/M transition and shortens overall cell-cycle time. HOIP:HOIP_0060585 Negative regulation of p53 degradation by MDM2 is a subtype of negative regulation of protein catabolic process: A process that stops, prevents, or reduces the frequency, rate or extent of p53 degradation. negative regulation of p53 degradation HOIP_0060585 HOIP:HOIP_0060586 Dizziness is a neurological and physiological symptom characterized by a sensation of unsteadiness accompanied by a feeling of movement within the head. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 dizziness associated with aging HOIP_0060586 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060587 Dehydration is a nutrition, metabolism, and development symptom characterized by an abnormal depletion of body fluids. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 PMID:2194700 dehydration associated with aging HOIP_0060587 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060588 Inspiration of a foreign object into the airway. aspiration HOIP_0060588 HOIP:HOIP_0060589 Keeping activation is a subtype of changing activity: A process that maintains the activity of the object at a constant level. keeping activation HOIP_0060589 HOIP:HOIP_0060590 A phenotypic abnormality reported by a patient indicative of a disease associated with the age of the cell or organism. Phenotypic abnormality associated with aging HOIP_0060590 HOIP:HOIP_0060591 Inspiration of a foreign object into the airway. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 Aspiration associated with aging (phenotype) HOIP_0060591 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060594 ISBN:9784890134304 dehydration associated with aging (phenotype) HOIP_0060594 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060595 An abnormal sensation of spinning while the body is actually stationary. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 Vertigo associated with aging (phenotype) HOIP_0060595 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060596 A dizziness that is characterized by a specific type of dizziness, a major symptom of a balance disorder. It is the sensation of spinning or swaying while the body is stationary with respect to the surroundings. vertigo associated with aging HOIP_0060596 HOIP:HOIP_0060597 Inspiration of a foreign object into the airway. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 aspiration associated with aging HOIP_0060597 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060598 Genetic defect is a subtype of gene defect: A process in which a part of a chromosome or a sequence of PTEN DNA is lost. PTEN loss HOIP_0060598 HOIP:HOIP_0060599 A type of ulcer that is caused when an area of skin is subject to pressure over a prolonged period of time, ranging in range in severity from patches of discolored skin to open wounds that expose the underlying bone or muscle. The most common sites are the sacrum, coccyx, heels and the hips. Bedsore Decubitus Ulcer Pressure Sore Pressure ulcer decubitus HOIP_0060599 HOIP:HOIP_0060600 Genetic defect is a subtype of gene defect: A process in which a part of a chromosome or a sequence of PTEN DNA is lost. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:21241890 PTEN loss [acute cellular senescence] HOIP_0060600 PMID:21241890 In this study, we have demonstrated that Pten-loss induced senescence is dependent on the Cdh1-Ets2-p16 pathway. On the basis of these data, we propose that PTEN loss elicits a potent senescence response through both phosphatase-dependent (superactivation of a PI3K/mTOR/p53 pathway (Alimonti et al., 2010; Chen et al., 2005)) and phosphatase-independent (loss of APC-CDH1 function, unrelated to Arf or p53/p21 pathway) activities, in turn highlighting the complexity of the dose-dependent tumor promoting and fail safe cellular responses evoked by PTEN loss (Fig. 7G). HOIP:HOIP_0060602 The term gait disturbance can refer to any disruption of the ability to walk. In general, this can refer to neurological diseases but also fractures or other sources of pain that is triggered upon walking. However, in the current context gait disturbance refers to difficulty walking on the basis of a neurological or muscular disease. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 Abnormal gait associated with aging Abnormal walk associated with aging Gait abnormalities associated with aging Gait difficulties associated with aging Gait disturbances associated with aging Impaired gait associated with aging Gait disturbance associated with aging (phenotype) HOIP_0060602 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060603 A type of ulcer that is caused when an area of skin is subject to pressure over a prolonged period of time, ranging in range in severity from patches of discolored skin to open wounds that expose the underlying bone or muscle. The most common sites are the sacrum, coccyx, heels and the hips. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 Bedsore associated with aging Decubitus Ulcer associated with aging Pressure Sore associated with aging Pressure ulcer associated with aging pressure ulcer associated with aging (phenotype) HOIP_0060603 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060604 ETS2 activation is a subtype of molecular activation: A process that changes the activity of the ETS2 to be higher. ETS2 activation HOIP_0060604 HOIP:HOIP_0060605 Abnormal cognition with deficits in thinking, reasoning, or remembering. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 Abnormality of cognition associated with aging Cognitive abnormality associated with aging Cognitive defects associated with aging Cognitive deficits associated with aging Cognitive impairment associated with aging Intellectual impairment associated with aging Cognitive impairment associated with aging (phenotype) HOIP_0060605 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060606 ETS2 activation is a subtype of molecular activation: A process that changes the activity of the ETS2 to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:21241890 ETS2 activation [acute cellular senescence] HOIP_0060606 PMID:21241890 In this study, we have demonstrated that Pten-loss induced senescence is dependeInt on the Cdh1-Ets2-p16 pathway. On the basis of these data, we propose that PTEN loss elicits a potent senescence response through both phosphatase-dependent (superactivation of a PI3K/mTOR/p53 pathway (Alimonti et al., 2010; Chen et al., 2005)) and phosphatase-independent (loss of APC-CDH1 function, unrelated to Arf or p53/p21 pathway) activities, in turn highlighting the complexity of the dose-dependent tumor promoting and fail safe cellular responses evoked by PTEN loss (Fig. 7G). HOIP:HOIP_0060607 A state of sudden and severe confusion. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 Delirium associated with aging (phenotype) HOIP_0060607 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060608 Increasing demand for oncogenic stress response is a subtype of increasing the demand for response to stress: A process that changes the functional demand for the response to the oncogenesis to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:33328614 increasing demand for oncogenic stress response [acute cellular senescence] HOIP_0060608 PMID:33328614 Cellular senescence occurs in response to many different triggers, including DNA damage, telomere dysfunction, oncogene activation and organelle stress, and has been linked to processes such as tumour suppression, tissue repair, embryogenesis and organismal ageing. PMID:33328614 Oncogene activation is also a powerful senescence trigger. Specifically, most activated oncogenes, partly via reactive oxygen species (ROS) production, induce hyperproliferation and altered DNA replication patterns that ultimately result in replication stress and DNA damage accumulation at fragile sites, which include telomeres. HOIP:HOIP_0060609 A neurological and physiological symptom that is characterized by a mental disturbance characterized by confusion, disordered speech, and hallucinations. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 delirium associated with aging HOIP_0060609 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060610 ETS1 activation is a subtype of molecular activation: A process that changes the activity of the ETS1 to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:34773072 ETS1 activation [acute cellular senescence] HOIP_0060610 PMID:34773072 Moreover, the expression of MZF1 is induced by oncogenic ras in senescent cells through the c-Jun and Ets1 transcriptional factors upon their activation by the Ras-Raf-1-MEK-ERK signaling pathway HOIP:HOIP_0060611 Frequent feelings of being down, miserable, and/or hopeless; difficulty recovering from such moods; pessimism about the future; pervasive shame; feeling of inferior self-worth; thoughts of suicide and suicidal behavior. ISBN:9784890134304 Depression associated with aging Depressivity associated with aging Depressive disorder associated with aging Depression associated with aging (phenotype) HOIP_0060611 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060612 ETS1 activation is a subtype of molecular activation: A process that changes the activity of the ETS1 to be higher. This entity is a specific course-dependent process. ETS1 activation HOIP_0060612 HOIP:HOIP_0060613 A neurological and physiological symptom that is characterized by a chronic feeling of emptiness, sadness, or inability to feel pleasure that may appear to happen for no clear reason. Additionally one may experience feelings of hopelessness, pessimism, irritability, frustration, or restlessness, guilt, worthlessness and thoughts of death or suicide. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 symptoms depression associated with aging HOIP_0060613 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060615 Loss of the ability to control the urinary bladder leading to involuntary urination. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 Bladder incontinence Loss of bladder control Urinary incontinence associated with aging (phenotype) HOIP_0060615 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060616 Lipofuscin deposition is a subtype of accumulation of pigments: The aggregation of lipofuscin in a particular location in an organism, tissue or cell. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. lipofuscin deposition [chronic cellular senescence] HOIP_0060616 HOIP:HOIP_0060617 Hypofunction of maintaining lysosome homeostasis is a subtype of hypofunctioning: A process that performs a decreased or insufficient maintaining lysosome homeostasis. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. hypofunction of lysosome [chronic cellular senescence] HOIP_0060617 HOIP:HOIP_0060620 A clinically recognizable state of increased vulnerability resulting from a decline in reserve and function across multiple physiologic systems such that the ability to cope with everyday or acute stressors is compromised. It is reported by a patient indicative of a disease associated with the age of the cell or organism. ISBN:9784890134304 Frailty associated with aging (phenotype) HOIP_0060620 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060622 ISBN:9784890134304 Stool holding associated with aging Stool soiling associated with aging Encopresis associated with aging (phenotype) HOIP_0060622 ISBN:9784890134304 老年医学系統講義テキスト HOIP:HOIP_0060623 A role played by the entity that shows an expression change according to the degree of cellular senescence. cellular senescence marker HOIP_0060623 HOIP:HOIP_0060624 Catalysis of the hydrolysis of galactosyl compounds, substances containing a group derived from a cyclic form of galactose or a galactose derivative. SA-β-gal senescence-associated-β-galactosidase HOIP_0060624 HOIP:HOIP_0060625 SA-β-GAL acculumation is a subtype of protein accumulation: A process that keeps SA-β-GAL (senescence-associated beta-galactosidase) in a cell. SA-β-GAL accumulation HOIP_0060625 HOIP:HOIP_0060626 SA-β-GAL acculumation is a subtype of protein accumulation: A process that keeps SA-β-GAL (senescence-associated beta-galactosidase) in a cell. SA-β-GAL acculumation [chronic cellular senescence] HOIP_0060626 HOIP:HOIP_0060627 For ontology reasoning. possible cause of IL-8 signaling and inflammatory response HOIP_0060627 HOIP:HOIP_0060628 For ontology reasoning. possible process that negatively regulates chronic inflammmation in cellular senescence HOIP_0060628 HOIP:HOIP_0060629 For ontology reasoning. possible cause of IL-8 signaling in senescence HOIP_0060629 HOIP:HOIP_0060630 A Bcl-2-like protein 2 that is encoded in the genome of human. BCL2L2-PABPN1 protein (human) Bcl-2-like protein 2 (human) Bcl2-L-2 (human) apoptosis regulator Bcl-W (human) BCLW (human) hBCL2L2 HOIP_0060630 HOIP:HOIP_0060631 The totality of all processes through which acute cor pulmonale is realized. Acute cor pulmonale is a form of acute right heart failure produced by a sudden increase in resistance to blood flow in the pulmonary circulation, which is now rapidly recognized by bedside echocardiography. (PMID: 19186411) Wikipedia:Pulmonary_heart_disease Pulmonary heart disease acute cor pulmonale course HOIP_0060631 Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS) etc. HOIP:HOIP_0060632 Protein production associated SASP is a subtype of protein production: A process that synthesizessenescence-associated secretory phenotype (SASP) related protein (s) resulting in having output (s). This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. protein production associated with SASP [chronic cellular senescence] HOIP_0060632 HOIP:HOIP_0060633 TOR signaling is a process that a signal is transmitted by the TOR (Target of rapamycin) . This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:29114066 mTOR signaling [acute cellular senescence] HOIP_0060633 PMID:29114066 mTORC1 integrates inputs from nutrient and growth signals to regulate general cellular processes such as protein and lipid synthesis, autophagy, and metabolism (Saxton and Sabatini, 2017). In this regard, mTOR is able to regulate the senescence-associated secretory phenotype (SASP), autophagy, and senescent growth arrest (Herranz et al., 2015; Laberge et al., 2015). The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. HOIP:HOIP_0060634 Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:29114066 regulation of autophagy [acute cellular senescence] HOIP_0060634 PMID:29114066 mTORC1 integrates inputs from nutrient and growth signals to regulate general cellular processes such as protein and lipid synthesis, autophagy, and metabolism. HOIP:HOIP_0060635 Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:29114066 regulation of autophagy [adult cellular senescence] HOIP_0060635 PMID:29114066 The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. HOIP:HOIP_0060636 TOR signaling is a process that a signal is transmitted by the TOR (Target of rapamycin) . This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:29114066 mTOR signaling [adult cellular senescence] HOIP_0060636 PMID:29114066 mTORC1 integrates inputs from nutrient and growth signals to regulate general cellular processes such as protein and lipid synthesis, autophagy, and metabolism (Saxton and Sabatini, 2017). In this regard, mTOR is able to regulate the senescence-associated secretory phenotype (SASP), autophagy, and senescent growth arrest (Herranz et al., 2015; Laberge et al., 2015). The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. HOIP:HOIP_0060637 Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B. This entity is a specific course-dependent process. This process can constitute the course of mitochondrial disorder. PMID:31649547 negative regulation of AKT signaling [chronic cellular senescence with type 2 diabetes] HOIP_0060637 PMID:31649547 Aging Moreover, ceramide also activates PKC to suppress protein kinase AKT and further inhibits insulin signal pathway. HOIP:HOIP_0060639 IL-6 signaling is a subtype of biological signaling: Any processes of molecular signals generated as a consequence of binding to Interleukin 6. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 IL-6 signaling [chronic cellular senescence] HOIP_0060639 PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. HOIP:HOIP_0060640 CXCL8 signaling is a process that a signal is transmitted by CXCL8.This process can constitute the course of chronic cellular senescence. PMID:33328614 CXCL8 signaling [chronic cellular senescence] HOIP_0060640 PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. HOIP:HOIP_0060641 CCL2 signaling is a process that a signal is transmitted by CCL2.This process can constitute the course of chronic cellular senescence. PMID:33328614 CCL2 signaling [chronic cellular senescence] HOIP_0060641 PMID:33328614 Senescence-associated secretory phenotype (SASP) activation is a dynamic process that accompanies cell cycle exit initiated by senescence triggers. A core SASP programme comprises mainly proinflammatory interleukin-6 (IL-6), IL-8 and monocyte chemoattractant protein 1 (MCP1), regulated in an IL-1-dependent manner, and enzymes involved in extracellular matrix (ECM) remodelling, such as matrix metalloproteinases (MMPs), serine/cysteine proteinase inhibitors (SERPINs) and tissue inhibitors of metalloproteinases (TIMPs). More recently, additional core SASP effectors released as soluble molecules or in exosomes were identified, including GDF15, STC1 and MMP1. HOIP:HOIP_0060642 For ontology reasoning. possible cause of cytokine or chemokine signaling and inflammatory response HOIP_0060642 HOIP:HOIP_0060643 For ontology reasoning. possible cause of "blood coagulation" HOIP_0060643 HOIP:HOIP_0060644 CXCL1 signaling is a process that a signal is transmitted by CXCL1.This process can constitute the course of chronic cellular senescence. PMID:23140366 PMID:33328614 CXCL1 signaling [chronic cellular senescence] HOIP_0060644 PMID:23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. HOIP:HOIP_0060645 CXCL1 signaling is a process that a signal is transmitted by CXCL1. CXCL1 signaling HOIP_0060645 HOIP:HOIP_0060646 A series of molecular signals initiated by the binding of the chemokine CXCL1 to a receptor on the surface of a cell. CXCL1-mediated signaling pathway chemokine (C-X-C motif) ligand 1 signaling pathway HOIP_0060646 HOIP:HOIP_0060647 Any process that activates or increases the frequency, rate or extent of the release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. ISBN:9780815345671 PMID:23140366 positive regulation of senescence-associated secretory phenotype (SASP) secretion [acute cellular senescence] HOIP_0060647 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID:23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. HOIP:HOIP_0060650 Any process that activates or increases the frequency, rate or extent of chemokine signaling. positive regulation of chemokine signaling HOIP_0060650 HOIP:HOIP_0060652 Any process that activates or increases the frequency, rate or extent of the release of the senescence-associated secretory phenotype (SASP) from a cell. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. ISBN:9780815345671 PMID:23140366 positive regulation of senescence-associated secretory phenotype (SASP) secretion [adult cellular senescence] HOIP_0060652 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID:23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. HOIP:HOIP_0060654 A role played by the molecule related to the senescence-associated secretory phenotype (SASP) . SASP factor role HOIP_0060654 HOIP:HOIP_0060655 Any process that activates or increases the rate or extent of cell proliferation.This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:33328614 positive regulation of tumor cell population proliferation positive regulation of tumor cell proliferation [chronic cellular senescence] HOIP_0060655 HOIP:HOIP_0060656 Any process that activates or increases the frequency, rate or extent of the P granule localization to poterior germ line. PMID:32829680 doi/10.1895/wormbook.1.30.2 positive regulation of P granule localization to posterior germline blastomere in one-cell embryo dependent process in C.elegans HOIP_0060656 PMID:32829680 In the anterior domain, MEX-5 outcompetes MEG-3 and PGL-3 for RNA-binding, whereas in the posterior, MEG-3 and PGL-3 can bind RNA and undergo phase separation, leading to P granule formation. MEG-3 phase separates into more stable gel-like condensates at the surface of P granules (see phase separation inset); hence, MEG-3 gradient can lead to granule stability at the posterior. HOIP:HOIP_0060658 The totality of all processes through which a given arteriosclerosis instance is realized. arteriosclerosis course HOIP_0060658 HOIP:HOIP_0060659 The selective elimination of senescent cells from the body. removing senescent cell HOIP_0060659 HOIP:HOIP_0060660 The selective elimination of senescent cells from the body. This process can constitute the course of cellular senescence. removing senescent cell [cellular senescence] HOIP_0060660 HOIP:HOIP_0060661 The selective elimination of senescent cells from the body. This process can constitute the course of adult cellular senescence. removing senescent cell [adult cellular senescence] HOIP_0060661 HOIP:HOIP_0060662 The selective elimination of senescent cells from the body. This process can constitute the course of embryonic cellular senescence. removing senescent cell [embryonic cellular senescence] HOIP_0060662 HOIP:HOIP_0060669 BCL format A data format specification that is a binary file containing base calling data. These files are created by sequencing machines during the act of sequencing, and contain data about each of the nucleotide clusters on a sequencing flow cell. IVision format HOIP_0060669 HOIP:HOIP_0060677 A process that results in the breakdown of LMNB1 in the lysosomes. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:31675495 PMID:33328614 LMNB1degradation in lysosome (transient) [acute cellular senescence] HOIP_0060677 PMID:33328614 PMID:31675495 Downregulation of lamin B1, a major component of the nuclear lamina, is another key feature of senescence (Dou et al., 2015, Freund et al., 2012, Shah et al., 2013, Shimi et al., 2011). Lamin B1 loss correlates with epigenetic profiles (Salama et al., 2014), as well as senescence-associated chromatin structures (SAHFs and SADSs) (Salama et al., 2014, Swanson et al., 2013). Its reduction occurs predominantly at H3K9me3-rich regions, a process that appears to liberate H3K9me3 from the nuclear lamina promoting spatial rearrangement of H3K9me3 heterochromatin to form SAHFs (Salama et al., 2014). Hi-C analysis (genome-wide mapping of chromatin contacts) in OIS revealed a reduction in local connectivity at regions enriched for H3K9me3 and lamin B1, perturbing these long-range interactions (Chandra et al., 2015). Replicative senescence, on the other hand, showed loss of long-range and gain of short-range interactions within chromosomes (Criscione et al., 2016), implying that the nature of senescence-associated high-order chromatin interactions is stimulus and context dependent (Zirkel et al., 2018). Furthermore, lamin B1 loss and reduced nuclear integrity is suggested to fuel the SASP by contributing to CCF formation (Dou et al., 2015, Ivanov et al., 2013), thereby stimulating the cGAS-STING pathway and interferon response (see Secretion) (Li and Chen, 2018). Autophagy-mediated CCF formation (Dou et al., 2015) together with reduced histone synthesis (O’Sullivan et al., 2010) might also lead to a global loss of core histones during senescence, affecting the chromatin landscape (Chan and Narita, 2019, Ivanov et al., 2013). PMID:33328614 Indeed, it was reported that a selective autophagy pathway, via mammalian target of rapamycin (mTOR) activation, contributes to sustain the protein synthesis of many senescence-associated secretory phenotype factors mainly in oncogene-induced senescent cells and that downregulation of several autophagy regulators delays the establishment of oncogene-induced senescence. more recently, LC3B, a ubiquitin-like autophagic protein, was found to be associated with the nuclear envelope protein lamin B1 and to contribute to its degradation in the lysosomes in oncogene-induced senescent cells. Importantly, lamin-associated chromatin domains are also transported out from the nucleus to the lysosomes via the same mechanism and contribute to the presence of cytosolic chromatin fragments that accumulate in senescent cells. Inhibition of autophagy prevents lamin B1 degradation and ensures nuclear envelope integrity in senescent cells. HOIP:HOIP_0060679 A data item that is the specified output of an imaging assay. imaging datum HOIP_0060679 HOIP:HOIP_0060680 a genetic transformation to introduce siRNA into a cell siRNA transfection HOIP_0060680 HOIP:HOIP_0060681 https://ssbd.riken.jp/omero/webclient/img_detail/1/?dataset=1 img0000.ipm HOIP_0060681 HOIP:HOIP_0060682 Lysosomal cholesterol storage is a subtype of cholesterol storage: A process that keeps cholesterol in the lysosome moderately. This entity is a specific course-dependent process. This process can constitute the course of Phospholipidosis(moderate). lysosomal cholesterol storage (moderate) [phospholipidosis via obese] HOIP_0060682 HOIP:HOIP_0060683 Cell homeostasis imbalance is a subtype of homeostasis imbalance: A process that becomes lacking a cell homeostastasis balance. This entity is a specific course-dependent process. This process can constitute the course of phospholipidosis (imbalance course). cell homeostasis imbalance [phospholipidosis (imbalance course)] HOIP_0060683 HOIP:HOIP_0060684 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis by alcoholic liver injury. necrosis [hepatic fibrosis by alcoholic liver injury] HOIP_0060684 HOIP:HOIP_0060685 Inflammatory response in liver is a subtype of inflammatory response: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. This entity is a specific course-dependent process. This process can constitute the course of hepatic fibrosis. inflammatory response in liver [hepatic fibrosis course] HOIP_0060685 HOIP:HOIP_0060687 Hyperfunction of fatty acid biosynthesis is a subtype of hyperfunction of biosynthesis: A process that performs an excessive fatty acid biosynthesis. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). hyperfunction of fatty acid biosynthesis [non-alcoholic fatty liver disease (NAFLD)] HOIP_0060687 HOIP:HOIP_0060688 Hyperfunction of lipid synthetic gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive lipid biosynthetic gene expression. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). hyperfunction of lipid synthetic gene expression [non-alcoholic fatty liver disease (NAFLD)] HOIP_0060688 HOIP:HOIP_0060689 Increaing in fatty acid inflow into hepatocyte is a subtype of increasing quantity: A process that changes the fatty acid inflow into the hepatocyte to be larger. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). increaing in fatty acid inflow into hepatocyte [diabetic ketoacidosis course] HOIP_0060689 HOIP:HOIP_0060690 Hypofunction of mitochondrial fatty acid beta-oxidation is a subtype of hypofunction of fatty acid beta-oxidation: A process that performs a decreased or insufficient fatty acid beta-oxidation. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). hypofunction of mitochondrial fatty acid beta-oxidation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0060690 HOIP:HOIP_0060691 Hypofunction of fatty acid degradation is a subtype of hypofunctioning: A process that performs a decreased or insufficient lipid degradation. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). hypofunction of mitochondrial fatty acid beta-oxidation [non-alcoholic fatty liver disease (NAFLD)] HOIP_0060691 HOIP:HOIP_0060692 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. nevrosis [alcoholic fatty liver] HOIP_0060692 HOIP:HOIP_0060693 Decreasing mitochondrial membrane potential is a subtype of decreasing membrane potential: A process that changes the electrical potential of a mitochondrial membrane to be lower. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. decreasing mitochondrial membrane potential [alcoholic fatty liver] HOIP_0060693 HOIP:HOIP_0060694 sequestering of triglyceride (severe) is a subtype of lipid strorage in hepatocyte: A process that keeps triglycerides in hepatocytes. And the degree is severe. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic steatohepatitis (course). sequestering of triglyceride (severe) [non-alcoholic steatohepatitis (course)] HOIP_0060694 HOIP:HOIP_0060695 SREBP activation is a subtype of molecular activation: A process that changes the activity of the SREBP to be higher. This entity is a specific course-dependent process. This process can constitute the course of non-alcoholic fatty liver disease (NAFLD). PMID:17854140 SREBP activation [alcoholic fatty liver] HOIP_0060695 PMID:17854140 When ethanol is added to cultured hepatoma cells that oxidize ethanol, it induces transcription of an SREBP-regulated promoter and increases the levels of the mature form of SREBP-1. AMPK regulates the ethanol-elicited SREBP-1 activation and the development of steatosis. The mechanism of ethanol-elicited SREBP-1 activation is also partly due to inhibition of the AMP-activated protein kinase (AMPK), described in greater detail below. AMPK catalyzes the phosphorylation of target enzymes, some of which are important rate-limiting enzymes in hepatic lipid metabolism. By inhibiting the activity of AMPK, ethanol relieves suppression of SREBP-1, causing its activation and increasing its levels in the nucleus. HOIP:HOIP_0060696 AMPK is a highly evolutionarily conserved serine/threonine kinase, and orthologs of the AMPK subunits are found in all eukaryotic species. At the molecular level, AMPK is a heterotrimer complex comprising a catalytic alpha subunit, with a conventional serine/threonine protein kinase domain, and two regulatory subunits, beta and gamma. In mammals, each subunit is encoded by multiple genes (alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3), which results in 12 possible combinations of AMPK complex. The AMPK molecule is inactivated state. AMPK - inactivation state (canonical)[lipidosis] HOIP_0060696 HOIP:HOIP_0060697 Hyperfunction of lipid synthetic gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive lipid biosynthetic gene expression. This entity is a specific course-dependent process. This process can constitute the course of alcoholic fatty liver. hyperfunction of lipid synthetic gene expression [alcoholic fatty liver] HOIP_0060697 HOIP:HOIP_0060698 Dissociation of FLCN:FNIP complex is a subtype of detaching: A process that disaggregates the FLCN:FNIP complex. This entity is a specific course-dependent process. This process can constitute the course of ER stress. Dissociation of FLCN:FNIP complex [ER stress] HOIP_0060698 HOIP:HOIP_0060699 Any process that stops, prevents, or reduces the frequency, rate or extent of the release of lipid storage in liver. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:18556558 PMID:26977301 PMID:27325692 negative regulation of lipid storage the liver [ER stress] HOIP_0060699 PMID:18556558 X-box binding protein 1 (XBP1), known as a key regulator of the unfolded protein response (UPR) secondary to ER stress, is a only recently characterized regulator of hepatic lipogenesis. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 2008; 320: 1492-1496. XBP1 protein expression in mice was elevated after feeding carbohydrates and corresponded with the induction of critical genes involved in fatty acid synthesis. Inducible, selective deletion of XBP1 in the liver resulted in marked hypocholesterolemia and hypotriglyceridemia, secondary to a decreased production of lipids from the liver. This phenotype was not accompanied by hepatic steatosis or compromise in protein secretory function. The identification of XBP1 as a regulator of lipogenesis has important implications for human dyslipidemias. PMID:26977301 In liver, the lesions observed in tunicamycin‐intoxicated animals include steatosis, bile ductular hyperplasia, swollen hepatocytes, and the presence of apoptotic bodies (Finnie and O'Shea 1989; Finnie and O'Shea 1990b; Finnie et al. 2004; Rutkowski et al. 2008). HOIP:HOIP_0060700 Any process that stops, prevents, or reduces the frequency, rate or extent of the release of lipid storage in liver. This entity is a specific course-dependent process. This process can constitute the course of ER stress. PMID:18556558 PMID:26977301 PMID:27325692 negative regulation of lipid storage the liver HOIP_0060700 PMID:18556558 X-box binding protein 1 (XBP1), known as a key regulator of the unfolded protein response (UPR) secondary to ER stress, is a only recently characterized regulator of hepatic lipogenesis. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 2008; 320: 1492-1496. XBP1 protein expression in mice was elevated after feeding carbohydrates and corresponded with the induction of critical genes involved in fatty acid synthesis. Inducible, selective deletion of XBP1 in the liver resulted in marked hypocholesterolemia and hypotriglyceridemia, secondary to a decreased production of lipids from the liver. This phenotype was not accompanied by hepatic steatosis or compromise in protein secretory function. The identification of XBP1 as a regulator of lipogenesis has important implications for human dyslipidemias. PMID:26977301 In liver, the lesions observed in tunicamycin‐intoxicated animals include steatosis, bile ductular hyperplasia, swollen hepatocytes, and the presence of apoptotic bodies (Finnie and O'Shea 1989; Finnie and O'Shea 1990b; Finnie et al. 2004; Rutkowski et al. 2008). HOIP:HOIP_0060701 IRE1 activation is a subtype of molecular activation: A process that changes the activity of the IRE1 to be higher. This entity is a specific course-dependent process. This process is dependent on RIDD and can constitute the course of ER stress. IRE1 activation [ER stress - RIDD] HOIP_0060701 HOIP:HOIP_0060702 The process of creating IRE1 oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. IRE1 oligomerization HOIP_0060702 HOIP:HOIP_0060704 A process of degradation of mRNAs regulatrd by IRE-1. RIDD regulated IRE1-dependent decay [ER stress] HOIP_0060704 HOIP:HOIP_0060705 A process of degradation of mRNAs regulatrd by IRE-1. RIDD regulated IRE1-dependent decay HOIP_0060705 HOIP:HOIP_0060706 The totality of all processes through which pulmonary infarction is realized. pulmonary infarction course HOIP_0060706 HOIP:HOIP_0060707 ER stress dependent process (under construction) HOIP_0060707 HOIP:HOIP_0060708 a genetic transformation to introduce shRNA into a cell shRNA transfection HOIP_0060708 HOIP:HOIP_0060709 For ontology reasoning. possible cause of negative regulation of tissue repair HOIP_0060709 HOIP:HOIP_0060710 a genetic transformation to introduce dsRNA into a cell dsRNA transfection HOIP_0060710 HOIP:HOIP_0060711 For ontology reasoning. possible cause of negative regulation of tumor cell proliferation HOIP_0060711 HOIP:HOIP_0060714 A gene knockdown that silences genes through artificially-induced RNA interference. This is accomplished by introducing gene knockdown by siRNA complementary to the target mRNA to be silenced. gene knockdown by siRNA transfection HOIP_0060714 HOIP:HOIP_0060715 A gene knockdown that silences genes through artificially-induced RNA interference. This is accomplished by introducing gene knockdown by shRNA complementary to the target mRNA to be silenced. gene knockdown by shRNA transfection HOIP_0060715 HOIP:HOIP_0060716 A gene knockdown assay in which RNAi gene knockdown by shRNA is used to disrupt gene transcripts. RNAi knockdown assay by shRNA transfection HOIP_0060716 HOIP:HOIP_0060717 A gene knockdown assay in which RNAi gene knockdown by siRNA is used to disrupt gene transcripts. RNAi knockdown assay by siRNA transfection HOIP_0060717 HOIP:HOIP_0060719 An assay with the objective to characterize the function of an object and and change to information. functional analysis assay HOIP_0060719 HOIP:HOIP_0060720 rpl-23 175796 3 Predicted to enable large ribosomal subunit rRNA binding activity. Predicted to be a structural constituent of ribosome. Predicted to be involved in translation. Predicted to be located in ribosome. Predicted to be part of cytosolic large ribosomal subunit. Is expressed in body wall musculature; excretory cell; intestine; nervous system; and pharynx. Orthologous to human RPL23 (ribosomal protein L23). rpl-23 encodes a large ribosomal subunit L23 protein. ENSEMBL:WBGene00004435 https://www.wormbase.org/search/gene/WBGene00004435 B0336.10 CELE_B0336.10 Ribosomal Protein, Large subunit 23 HOIP_0060720 Predicted to enable large ribosomal subunit rRNA binding activity. Predicted to be a structural constituent of ribosome. Predicted to be involved in translation. Predicted to be located in ribosome. Predicted to be part of cytosolic large ribosomal subunit. Is expressed in body wall musculature; excretory cell; intestine; nervous system; and pharynx. Orthologous to human RPL23 (ribosomal protein L23). https://www.alliancegenome.org/gene/WB:WBGene00004435 HOIP:HOIP_0060721 3D time-lapse microscopy images about nuclear division dynamics in C02F5.1(RNAi) embryo (knl-1(RNAi) embryo) RNAi_C02F5.1_061219_02 HOIP_0060721 HOIP:HOIP_0060722 gene of the nematode Caenorhabditis elegans. HOIP_0060722 HOIP:HOIP_0060723 3D time-lapse microscopy images about nuclear division dynamics in B0336.10(RNAi) embryo (rpl-23(RNAi) embryo) PMID:23172286 https://ssbd.riken.jp/database/dataset/2/ https://ssbd.riken.jp/omero/webclient/?show=dataset-1 RNAi_B0336.10_040518_01 HOIP_0060723 HOIP:HOIP_0060724 An assay with the objective to characterize the function of genes and proteins and change to information. Wikipedia:Functional_genomics functional genomics assay HOIP_0060724 Wikipedia:Functional_genomics Functional genomics is a field of molecular biology that attempts to describe gene (and protein) functions and interactions. Functional genomics make use of the vast data generated by genomic and transcriptomic projects (such as genome sequencing projects and RNA sequencing). Functional genomics focuses on the dynamic aspects such as gene transcription, translation, regulation of gene expression and protein–protein interactions, as opposed to the static aspects of the genomic information such as DNA sequence or structures. A key characteristic of functional genomics studies is their genome-wide approach to these questions, generally involving high-throughput methods rather than a more traditional "candidate-gene" approach. HOIP:HOIP_0060726 An assay with the objective to characterize the function of genesand change to information. functional anaysis of gene HOIP_0060726 HOIP:HOIP_0060727 An assay with the objective to characterize the function of proteins and change to information. functional anaysis of protein HOIP_0060727 HOIP:HOIP_0060742 An objective describing a study designed to examine or characterize the function of a biological entity. biological function identification objective HOIP_0060742 HOIP:HOIP_0060743 An objective describing a study designed to examine or characterize the function of genes. genetic function identification objective HOIP_0060743 HOIP:HOIP_0060744 An objective describing a study designed to examine or characterize the function of genomes. genome function identification objective HOIP_0060744 HOIP:HOIP_0060745 An objective describing a study designed to examine or characterize the function of proteins. protein function identification objective HOIP_0060745 HOIP:HOIP_0060748 An attribute describing an epigenetic process where a gene is inactivated at transcriptional or translational level. silenced (attribute) HOIP_0060748 HOIP:HOIP_0060749 A quality describing an epigenetic process where a gene is inactivated at transcriptional or translational level. silenced HOIP_0060749 HOIP:HOIP_0060800 A process that changes the telomere length to be short. This entity is a specific course-dependent process. This process can constitute the course of cellular senescence. ISBN:9780815345671 ISBN:9781437717815 PMID:10669743 PMID:29114066 PMID:33450206 telomere attrition telomere erosion telomere shortening [cellular senescence] HOIP_0060800 ISBN:9780815345671 Short or uncapped telomeres arise in somatic cells after several replictive cycles. The DNA damage and repair mechanism reads the telomeres as a strand break and initiates thorough various signals of the p53 protein. Inhibition of the cyclin-CDK complex then halts the cell cycle in G1. Since there is no repair mechanism that will elongate or cap the telomere - that is no telomerase - the cell enters permanently, resulting in cell senescence. Biology of Aging 2nd Ed. ISBN:9781437717815 Telomere length is maintained by nucleotide addition mediated by an enzyme called telomerase. Telomerase is a specialized RNA protein complex that uses its own RNA as a template for adding nucleotides to the end of chromosomes. Telomerase activity is expressed in germ cells and is present at low levels in stem cells, but it is absent in most somatic cells. Therefore, as most somatic cells age their telomeres become shorter and they exit just cell cycle resulting in an inability to generate new cells to replicate damaged ones. Robbins Basic Pathology 9th ed. Chapter1 PMID:10669743 Overexpression of TRF2 results in the progressive shortening of telomere length, similar to the phenotype observed with TRF1. PMID:29114066 Senescence, a cellular response that limits the proliferation of aged or damaged cells (Muñoz-Espín et al., 2013; Muñoz-Espín and Serrano, 2014), belongs to the antagonistic class (Fig. 1). Although senescence plays physiological roles during normal development and it is needed for tissue homeostasis, senescence constitutes a stress response triggered by insults associated with aging such as genomic instability and telomere attrition, which are primary aging hallmarks themselves. PMC:5748990 PMID:33450206 In 2000, further analysis of late-generation mTERC−/−;p53+/− mice (Artandi et al., 2000) revealed a humanized tumor spectrum of epithelial cancers possessing chromosomal rearrangements and nonreciprocal translocations typical of human cancer genomes. Thus, mice engineered to experience telomere-based crisis in the context of deactivated DNA damage signaling (p53 deficiency) illuminated a major mechanism driving the preponderance of epithelial cancers in aged humans and explained why such cancers develop radically altered cytogenetic profiles. PMID:33450206 Overexpression of TRF1 or deregulation of POT1 impairs telomerase binding to telomere ends, causing telomere shortening (Loayza and De Lange, 2003; Smogorzewska et al., 2000) HOIP:HOIP_0060803 Dysregulation of metabolism is a subtype of malfunctioning of controlling: A process that cannot perform a regulation of metabolism appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:29114066 PMID:29114066 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ malfunctioning of metabolism [chronic cellular senescence] HOIP_0060803 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ PMID:29114066 Telomere damage, epigenetic dysregulation, DNA damage, and mitochondrial dysfunction are primary drivers of damage in aging. Several of these drivers of damage can induce senescence. Senescence can in turn drive the consequential aging hallmarks in response to damage: stem cell exhaustion and chronic inflammation. Other responses to damage, such as proteostatic dysfunction and nutrient signaling disruption, are also integrally linked with the senescence response. PMID:29114066 The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. PMC:5748990 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig1.jpg HOIP:HOIP_0060804 Malfunction of protein biosynthesis is a subtype of malfunctioning: A process that cannot perform the protein biosynthesis function appropriately or cannot realize it at all. This entity is a specific course-dependent process. This process can constitute the course of adult cellular senescence. PMID:29114066 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ malfunction of protein biosynthesis [chronic cellular senescence] HOIP_0060804 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ PMID:29114066 The connection between autophagy and senescence is complex; although there is an increase in autophagy during senescence that serves to regulate SASP production (Narita et al., 2011), inhibition of autophagy can induce senescence through metabolic and proteostatic dysfunction (García-Prat et al., 2016), further emphasizing the intricate connection between metabolic stress and senescence in aging. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/figure/fig1/ jpg https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig1.jpg HOIP:HOIP_0060805 Hyperfunction of oxidant gene expression is a subtype of hyperfunction of gene expression: A process that performs an excesssive oncogene expression. hyperfunction of oncogene expression HOIP_0060805 HOIP:HOIP_0060806 Ink4-ARF activation is a subtype of molecular activation: A process that changes the activity of Ink4-ARF to be higher. This entity is a specific course-dependent process. This process can constitute the course of acute cellular senescence. PMID:29114066 PMID:33328614 Ink4-ARF activation [acute cellular senescence] HOIP_0060806 PMID:29114066 Conversely, during senescence, the H3K27 histone demethylase JMJD3 plays a role in removing the repressive marks around the INK4/ARF locus, facilitating its induction (Agger et al., 2009; Barradas et al., 2009). INK4/ARF induction can be observed in tissues during natural aging (Krishnamurthy et al., 2004; Burd et al., 2013). In particular, p16INK4a is considered an aging biomarker. With exceptions (such as during senescence-induced during development), p16INK4a is also one of the best markers of senescence. An analysis of the pathways regulating p16INK4a shows coincidences with those controlling development. This has been argued to formulate the theory that aging might be driven by gradual functional decay of developmental pathways (Martin et al., 2014). PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. PMID:33328614 In addition to the DDR cascade being activated, the tumour suppressor ARF stabilizes p53, which contributes to the induction of senescence. Efforts have been devoted to assessing the contribution of these two major routes, the DDR and ARF pathways, to p53-dependent senescence establishment especially in response to oncogenic challenges. The original view, based mainly on murine studies, was that the DDR and ARF play antagonistic roles, as ARF was transcriptionally activated during tumorigenesis in a DDR-independent manner. More recently, a tight regulatory network in human cancer models was reported, whereby ATM suppresses ARF levels and ARF acts as a secondary barrier to cancer progression when ATM is inactivated. Consistent with this temporal regulation, DDR precedes ARF engagement, whose activation is detected at later stages of cancer progression and less frequently than DDR. HOIP:HOIP_0060807 Ink4-ARF activation is a subtype of molecular activation: A process that changes the activity of Ink4-ARF to be higher. This entity is a specific course-dependent process. PMID:29114066 PMID:33328614 Ink4-ARF activation HOIP_0060807 PMID:29114066 Conversely, during senescence, the H3K27 histone demethylase JMJD3 plays a role in removing the repressive marks around the INK4/ARF locus, facilitating its induction (Agger et al., 2009; Barradas et al., 2009). INK4/ARF induction can be observed in tissues during natural aging (Krishnamurthy et al., 2004; Burd et al., 2013). In particular, p16INK4a is considered an aging biomarker. With exceptions (such as during senescence-induced during development), p16INK4a is also one of the best markers of senescence. An analysis of the pathways regulating p16INK4a shows coincidences with those controlling development. This has been argued to formulate the theory that aging might be driven by gradual functional decay of developmental pathways (Martin et al., 2014). PMID:29114066 Three tumor suppressors reside in the INK4/ARF locus: p16INK4a and ARF, which are both encoded by the CDKN2A gene, and p15INK4b, which is encoded by CDKN2B. Two of these, p15INK4b and p16INK4a, are CDKIs, like p21CIP1, that affect the cell cycle by binding and inhibiting CDK4 and CDK6. In contrast, ARF inhibits MDM2, thereby allowing cross talk with the p53/p21CIP1 pathways. PMID:33328614 In addition to the DDR cascade being activated, the tumour suppressor ARF stabilizes p53, which contributes to the induction of senescence. Efforts have been devoted to assessing the contribution of these two major routes, the DDR and ARF pathways, to p53-dependent senescence establishment especially in response to oncogenic challenges. The original view, based mainly on murine studies, was that the DDR and ARF play antagonistic roles, as ARF was transcriptionally activated during tumorigenesis in a DDR-independent manner. More recently, a tight regulatory network in human cancer models was reported, whereby ATM suppresses ARF levels and ARF acts as a secondary barrier to cancer progression when ATM is inactivated. Consistent with this temporal regulation, DDR precedes ARF engagement, whose activation is detected at later stages of cancer progression and less frequently than DDR. HOIP:HOIP_0060814 A process that changes the mass of the object. changing mass HOIP_0060814 HOIP:HOIP_0060815 A process that a mass is lower than normal or average. decreasing mass HOIP_0060815 HOIP:HOIP_0060817 A muscle mass which is lower than normal or average. decreased muscle mass HOIP_0060817 HOIP:HOIP_0060819 The release of the senescence-associated secretory phenotype (SASP) from a cell. ISBN:9780815345671 PMID: 23140366 PMID:23140366 PMID:33328614 senescence-associated secretory phenotype (SASP) (process) HOIP_0060819 ISBN:9780815345671 Senescent cells have an increased secretion of proteins that include a variety of inflammatory site cytokines, proteins that activate the inflammatory response protein released by the senescent cells are so ubiquitous that they have been given their own name, the senescence-associated secretory phenotype (SASP). Biology of Aging 2nd Ed. Chapter 4, cellular aging PMID: 23140366 In human cells, IL-6, IL-8, and IGFBP7 (insulin-like growth factor–binding protein 7) reinforce the senescence growth arrest caused by the oncogenic forms of RAS and BRAF. RAS and BRAF are cytoplasmic proteins that participate in transducing growth factor and other extracellular signals to the cell interior; the genes that encode both proteins are frequently mutated in human cancer. Likewise, GROα, a potent mitogen that is a SASP component and is induced by oncogenic RAS, promotes the senescence of normal human ovarian fibroblasts. Thus, at least some SASP factors (in these examples, IL-6, IL-8, IGFBP7, and GROα) help establish the oncogene-induced senescence response. In the cases of IL-6 and IL-8, these SASP components appear to act by instituting a self-sustaining intracellular signaling loop that ultimately activates the NF-κB and C/EBP-β transcription factors. PMID:23140366 In addition, some SASP factors induce an epithelial-to-mesenchymal transition in susceptible cells; others (for example, SFRP1, GROα, and IL-6) can alter stem cell proliferation or differentiation or modify stem cell niches. PMID:33328614 Moreover, the transcription factor GATA4 activates a plethora of genes involved in immune response and inflammation, including those encoding IL-6, IL-8, CXCL1 (also known as GROα), granulocyte–macrophage colony-stimulating factor, and ECM proteases and their inhibitors. PMID:33328614 Senescence-associated secretory phenotype (SASP) activation is a dynamic process that accompanies cell cycle exit initiated by senescence triggers. A core SASP programme comprises mainly proinflammatory interleukin-6 (IL-6), IL-8 and monocyte chemoattractant protein 1 (MCP1), regulated in an IL-1-dependent manner, and enzymes involved in extracellular matrix (ECM) remodelling, such as matrix metalloproteinases (MMPs), serine/cysteine proteinase inhibitors (SERPINs) and tissue inhibitors of metalloproteinases (TIMPs). More recently, additional core SASP effectors released as soluble molecules or in exosomes were identified, including GDF15, STC1 and MMP1. HOIP:HOIP_0060820 SASP factor is a substance with SASP factor role. Tthe production of a complex mixture of secreted factors, termed the SASP or senescence-messaging secretome, is the most relevant phenotypic program implemented in senescent cells. This entity is inferred from Description Logic. SASP factor HOIP_0060820 HOIP:HOIP_0060832 Loss of nuclear lamina can lead to the release of cytosolic chromatin fragments (CCFs) in the cytoplasm of senescent cells. CCFs cytosolic chromatin fragments HOIP_0060832 Loss of nuclear lamina can lead to the release of cytosolic chromatin fragments (CCFs) in the cytoplasm of senescent cells. PMID:33328614 HOIP:HOIP_0060833 Damaged senescent cells permanently arrest growth, secrete inflammatory cytokines and other proteins and harbor persistent nuclear foci that contain DNA damage response (DDR) proteins. To understand how persistent damage foci differ from transient foci that mark repairable DNA lesions, we identify sequential events that differentiate transient foci from persistent foci, which we term 'DNA segments with chromatin alterations reinforcing senescence' (DNA-SCARS). http://www.ebi.ac.uk/efo/EFO_0008480 DNA segments with chromatin alterations reinforcing senescence DNA-SCARS HOIP_0060833 Damaged senescent cells permanently arrest growth, secrete inflammatory cytokines and other proteins and harbor persistent nuclear foci that contain DNA damage response (DDR) proteins. To understand how persistent damage foci differ from transient foci that mark repairable DNA lesions, we identify sequential events that differentiate transient foci from persistent foci, which we term 'DNA segments with chromatin alterations reinforcing senescence' (DNA-SCARS). PMID:21118958 HOIP:HOIP_0060834 A process that performs a decreased or insufficient LMNB1 (Lamin-B1) expression. hypofunction of expression of LMNB1 HOIP_0060834 HOIP:HOIP_0060836 A process in which cell changes structural and/or functional phenotypes. cell plasticity HOIP_0060836 HOIP:HOIP_0060838 Any process that modulates the occurrence or rate of senescence cell clearance. regulation of senescence cell clearance HOIP_0060838 HOIP:HOIP_0060841 A process that stops, prevents, or reduces the frequency, rate or extent of tumorigenesis. negative regulation of tumorigenesis HOIP_0060841 HOIP:HOIP_0060842 A processthat activates or increases the frequency, rate or extent of tumorigenesis. positive regulation of tumorigenesis HOIP_0060842 HOIP:HOIP_0060844 The process injures the structure as the direct or indirect result of mechanical stress. mechanical damage HOIP_0060844 HOIP:HOIP_0060848 A process that performs an abnormal and incomplete function of mitophagy. mitophagy dysfunction HOIP_0060848 HOIP:HOIP_0060849 A process that damaged mitochondria are accumulated within in an organism, tissue or cell. accumulation of damaged mitochondoria HOIP_0060849 HOIP:HOIP_0060858 A gene with a cell cycle regulator role. cell cycle gene HOIP_0060858 HOIP:HOIP_0060860 A multisubunit complex formed by the assembly of p130 and p107 with their dimerization partner, E2F4/5, and a multi-vulva class-B core complex. DREAM complex HOIP_0060860 A multisubunit complex formed by the assembly of p130 and p107 with their dimerization partner, E2F4/5, and a multi-vulva class-B core complex. PMID:35922662 HOIP:HOIP_0060872 A gene with a tumor inhibition role. tumor suppressor gene 腫瘍抑制遺伝子 HOIP_0060872 HOIP:HOIP_0060873 An agent and endogenous substances that antagonize or inhibit the development of tumor. tumor inhibitor HOIP_0060873 HOIP:HOIP_0060874 A process that performs an abnormal and incomplete cell proliferation. dysfunction of cell proliferation HOIP_0060874 HOIP:HOIP_0060875 When induced pluripotent stem cells (iPSCs) are generated from somatic cells, their gene expression returns to an undifferentiated state and they acquire pluripotency. This process is called iPSCreprogramming. iPSC reprogramming HOIP_0060875 HOIP:HOIP_0060879 cytoplasmic DNA HOIP_0060879 HOIP:HOIP_0060886 The process in which substances (e.g., senescence cells) are eliminated by immune cells. immune clearance HOIP_0060886 HOIP:HOIP_0060887 Any process that activates or increases the rate or extent of immune clearance, the increase in size or mass of all or part of an organism. positive regulation of immune clearance HOIP_0060887 HOIP:HOIP_0060888 A process that stops, prevents, or reduces the frequency, rate or extent of mutation. negative regulation of mutation HOIP_0060888 HOIP:HOIP_0060892 A process that stops, prevents, or reduces the frequency, rate or extent of fibrosis negative regulation of fibrosis HOIP_0060892 HOIP:HOIP_0060897 Any substances that modulates the changes in gene expression without a change in DNA sequence. Epigenetics is the study of heritable changes in gene expression that occur without a change in DNA sequence. PMID:26153137 epigenetic factor HOIP_0060897 Any substances that modulates the changes in gene expression without a change in DNA sequence. Epigenetics is the study of heritable changes in gene expression that occur without a change in DNA sequence. PMID:10521337 PMID:26153137 We defined epigenetic factors as Proteins acting as histones, histone variants or protamines; Proteins performing post-translational modifications of histones or recognizing such modifications (histone modification ‘writers’, ‘erasers’ or ‘readers’); Proteins changing the general structure of chromatin (performing chromatin remodeling), including Proteins that move, eject or restructure nucleosomes (ATP-dependent chromatin remodelers); Proteins that incorporate histone variants into the nucleosomes. Proteins assisting histone folding and assembly; Proteins acting upon modifications of DNA or RNA in such a way that it affects gene expression, but not through RNA processing; Protein cofactors forming complexes with epigenetic factors, where complex formation is important for the activity. HOIP:HOIP_0060898 A role played by entities that modulates the changes in gene expression without a change in DNA sequence. Epigenetics is the study of heritable changes in gene expression that occur without a change in DNA sequence. PMID:26153137 epigenetic factor role HOIP_0060898 A role played by entities that modulates the changes in gene expression without a change in DNA sequence. Epigenetics is the study of heritable changes in gene expression that occur without a change in DNA sequence. PMID:10521337 PMID:26153137 We defined epigenetic factors as Proteins acting as histones, histone variants or protamines; Proteins performing post-translational modifications of histones or recognizing such modifications (histone modification ‘writers’, ‘erasers’ or ‘readers’); Proteins changing the general structure of chromatin (performing chromatin remodeling), including Proteins that move, eject or restructure nucleosomes (ATP-dependent chromatin remodelers); Proteins that incorporate histone variants into the nucleosomes. Proteins assisting histone folding and assembly; Proteins acting upon modifications of DNA or RNA in such a way that it affects gene expression, but not through RNA processing; Protein cofactors forming complexes with epigenetic factors, where complex formation is important for the activity. HOIP:HOIP_1000000 NCBI-Human-GeneID:64241 NCBI-Mouse-GeneID:67470 NCBI-Rat-GeneID:155192 ABCG8 (mol) HOIP_1000000 NCBI-Human-GeneID:64241 http://www.ncbi.nlm.nih.gov/gene/64241 NCBI-Mouse-GeneID:67470 http://www.ncbi.nlm.nih.gov/gene/67470 NCBI-Rat-GeneID:155192 http://www.ncbi.nlm.nih.gov/gene/155192 HOIP:HOIP_1000001 NCBI-Human-GeneID:60312 NCBI-Mouse-GeneID:70292 NCBI-Rat-GeneID:140935 AFAP1 (mol) HOIP_1000001 NCBI-Human-GeneID:60312 http://www.ncbi.nlm.nih.gov/gene/60312 NCBI-Mouse-GeneID:70292 http://www.ncbi.nlm.nih.gov/gene/70292 NCBI-Rat-GeneID:140935 http://www.ncbi.nlm.nih.gov/gene/140935 HOIP:HOIP_1000002 NCBI-Human-GeneID:51129 NCBI-Mouse-GeneID:57875 NCBI-Rat-GeneID:362850 ANGPTL4 (mol) HOIP_1000002 NCBI-Human-GeneID:51129 http://www.ncbi.nlm.nih.gov/gene/51129 NCBI-Mouse-GeneID:57875 http://www.ncbi.nlm.nih.gov/gene/57875 NCBI-Rat-GeneID:362850 http://www.ncbi.nlm.nih.gov/gene/362850 HOIP:HOIP_1000003 NCBI-Human-GeneID:10053 NCBI-Mouse-GeneID:11768 NCBI-Rat-GeneID:367038 AP1M2 (mol) HOIP_1000003 NCBI-Human-GeneID:10053 http://www.ncbi.nlm.nih.gov/gene/10053 NCBI-Mouse-GeneID:11768 http://www.ncbi.nlm.nih.gov/gene/11768 NCBI-Rat-GeneID:367038 http://www.ncbi.nlm.nih.gov/gene/367038 HOIP:HOIP_1000004 NCBI-Human-GeneID:1174 NCBI-Mouse-GeneID:11769 NCBI-Rat-GeneID:360785 AP1S1 (mol) HOIP_1000004 NCBI-Human-GeneID:1174 http://www.ncbi.nlm.nih.gov/gene/1174 NCBI-Mouse-GeneID:11769 http://www.ncbi.nlm.nih.gov/gene/11769 NCBI-Rat-GeneID:360785 http://www.ncbi.nlm.nih.gov/gene/360785 HOIP:HOIP_1000005 NCBI-Human-GeneID:317 NCBI-Mouse-GeneID:11783 NCBI-Rat-GeneID:78963 APAF1 (mol) HOIP_1000005 NCBI-Human-GeneID:317 http://www.ncbi.nlm.nih.gov/gene/317 NCBI-Mouse-GeneID:11783 http://www.ncbi.nlm.nih.gov/gene/11783 NCBI-Rat-GeneID:78963 http://www.ncbi.nlm.nih.gov/gene/78963 HOIP:HOIP_1000006 NCBI-Human-GeneID:348 NCBI-Mouse-GeneID:11816 NCBI-Rat-GeneID:25728 APOE (mol) HOIP_1000006 NCBI-Human-GeneID:348 http://www.ncbi.nlm.nih.gov/gene/348 NCBI-Mouse-GeneID:11816 http://www.ncbi.nlm.nih.gov/gene/11816 NCBI-Rat-GeneID:25728 http://www.ncbi.nlm.nih.gov/gene/25728 HOIP:HOIP_1000007 NCBI-Human-GeneID:81575 NCBI-Mouse-GeneID:381823 NCBI-Rat-GeneID:444983 APOLD1 (mol) HOIP_1000007 NCBI-Human-GeneID:81575 http://www.ncbi.nlm.nih.gov/gene/81575 NCBI-Mouse-GeneID:381823 http://www.ncbi.nlm.nih.gov/gene/381823 NCBI-Rat-GeneID:444983 http://www.ncbi.nlm.nih.gov/gene/444983 HOIP:HOIP_1000008 Acute Phase Response gene APR molecule HOIP_1000008 HOIP:HOIP_1000009 NCBI-Human-GeneID:427 NCBI-Mouse-GeneID:11886 NCBI-Rat-GeneID:84431 ASAH1 (mol) HOIP_1000009 NCBI-Human-GeneID:427 http://www.ncbi.nlm.nih.gov/gene/427 NCBI-Mouse-GeneID:11886 http://www.ncbi.nlm.nih.gov/gene/11886 NCBI-Rat-GeneID:84431 http://www.ncbi.nlm.nih.gov/gene/84431 HOIP:HOIP_1000010 NCBI-Human-GeneID:10926 NCBI-Mouse-GeneID:27214 NCBI-Rat-GeneID:312046 DBF4 (mol) HOIP_1000010 NCBI-Human-GeneID:10926 http://www.ncbi.nlm.nih.gov/gene/10926 NCBI-Mouse-GeneID:27214 http://www.ncbi.nlm.nih.gov/gene/27214 NCBI-Rat-GeneID:312046 http://www.ncbi.nlm.nih.gov/gene/312046 HOIP:HOIP_1000011 NCBI-Human-GeneID:467 NCBI-Mouse-GeneID:11910 NCBI-Rat-GeneID:25389 activating transcription factor 3 ATF3 (mol) HOIP_1000011 NCBI-Human-GeneID:467 http://www.ncbi.nlm.nih.gov/gene/467 NCBI-Mouse-GeneID:11910 http://www.ncbi.nlm.nih.gov/gene/11910 NCBI-Rat-GeneID:25389 http://www.ncbi.nlm.nih.gov/gene/25389 HOIP:HOIP_1000012 NCBI-Human-GeneID:468 NCBI-Mouse-GeneID:11911 NCBI-Rat-GeneID:79255 activating transcription factor 4 ATF4 (mol) HOIP_1000012 NCBI-Human-GeneID:468 http://www.ncbi.nlm.nih.gov/gene/468 NCBI-Mouse-GeneID:11911 http://www.ncbi.nlm.nih.gov/gene/11911 NCBI-Rat-GeneID:79255 http://www.ncbi.nlm.nih.gov/gene/79255 HOIP:HOIP_1000013 NCBI-Human-GeneID:22926 NCBI-Mouse-GeneID:226641 NCBI-Rat-GeneID:304962 ATF6 (mol) HOIP_1000013 NCBI-Human-GeneID:22926 http://www.ncbi.nlm.nih.gov/gene/22926 NCBI-Mouse-GeneID:226641 http://www.ncbi.nlm.nih.gov/gene/226641 NCBI-Rat-GeneID:304962 http://www.ncbi.nlm.nih.gov/gene/304962 HOIP:HOIP_1000014 ATP-binding cassette (ABC) transporter superfamily HOIP_1000014 HOIP:HOIP_1000015 Abc1b1 (mol) HOIP_1000015 HOIP:HOIP_1000016 NCBI-Human-GeneID:84696 NCBI-Mouse-GeneID:57742 NCBI-Rat-GeneID:313917 Abhd1 (mol) HOIP_1000016 NCBI-Human-GeneID:84696 http://www.ncbi.nlm.nih.gov/gene/84696 NCBI-Mouse-GeneID:57742 http://www.ncbi.nlm.nih.gov/gene/57742 NCBI-Rat-GeneID:313917 http://www.ncbi.nlm.nih.gov/gene/313917 HOIP:HOIP_1000017 NCBI-Human-GeneID:30 NCBI-Mouse-GeneID:113868 NCBI-Rat-GeneID:24157 Acaa1a (mol) HOIP_1000017 NCBI-Human-GeneID:30 http://www.ncbi.nlm.nih.gov/gene/30 NCBI-Mouse-GeneID:113868 http://www.ncbi.nlm.nih.gov/gene/113868 NCBI-Rat-GeneID:24157 http://www.ncbi.nlm.nih.gov/gene/24157 HOIP:HOIP_1000018 NCBI-Human-GeneID:84320 NCBI-Mouse-GeneID:72482 NCBI-Rat-GeneID:289125 Acbd6 (mol) HOIP_1000018 NCBI-Human-GeneID:84320 http://www.ncbi.nlm.nih.gov/gene/84320 NCBI-Mouse-GeneID:72482 http://www.ncbi.nlm.nih.gov/gene/72482 NCBI-Rat-GeneID:289125 http://www.ncbi.nlm.nih.gov/gene/289125 HOIP:HOIP_1000019 NCBI-Human-GeneID:340485 NCBI-Mouse-GeneID:230379 NCBI-Rat-GeneID:313339 Acer2 (mol) HOIP_1000019 NCBI-Human-GeneID:340485 http://www.ncbi.nlm.nih.gov/gene/340485 NCBI-Mouse-GeneID:230379 http://www.ncbi.nlm.nih.gov/gene/230379 NCBI-Rat-GeneID:313339 http://www.ncbi.nlm.nih.gov/gene/313339 HOIP:HOIP_1000020 NCBI-Human-GeneID:55331 NCBI-Mouse-GeneID:66190 NCBI-Rat-GeneID:499210 Acer3 (mol) HOIP_1000020 NCBI-Human-GeneID:55331 http://www.ncbi.nlm.nih.gov/gene/55331 NCBI-Mouse-GeneID:66190 http://www.ncbi.nlm.nih.gov/gene/66190 NCBI-Rat-GeneID:499210 http://www.ncbi.nlm.nih.gov/gene/499210 HOIP:HOIP_1000021 NCBI-Human-GeneID:134526 NCBI-Mouse-GeneID:74156 NCBI-Rat-GeneID:170570 Acot12 (mol) HOIP_1000021 NCBI-Human-GeneID:134526 http://www.ncbi.nlm.nih.gov/gene/134526 NCBI-Mouse-GeneID:74156 http://www.ncbi.nlm.nih.gov/gene/74156 NCBI-Rat-GeneID:170570 http://www.ncbi.nlm.nih.gov/gene/170570 HOIP:HOIP_1000022 NCBI-Human-GeneID:10965 NCBI-Mouse-GeneID:171210 NCBI-Rat-GeneID:192272 Acot2 (mol) HOIP_1000022 NCBI-Human-GeneID:10965 http://www.ncbi.nlm.nih.gov/gene/10965 NCBI-Mouse-GeneID:171210 http://www.ncbi.nlm.nih.gov/gene/171210 NCBI-Rat-GeneID:192272 http://www.ncbi.nlm.nih.gov/gene/192272 HOIP:HOIP_1000023 NCBI-Mouse-GeneID:171281 NCBI-Rat-GeneID:314304 Acot3 (mol) HOIP_1000023 NCBI-Mouse-GeneID:171281 http://www.ncbi.nlm.nih.gov/gene/171281 NCBI-Rat-GeneID:314304 http://www.ncbi.nlm.nih.gov/gene/314304 HOIP:HOIP_1000024 NCBI-Human-GeneID:122970 NCBI-Mouse-GeneID:171282 NCBI-Rat-GeneID:681337 Acot4 (mol) HOIP_1000024 NCBI-Human-GeneID:122970 http://www.ncbi.nlm.nih.gov/gene/122970 NCBI-Mouse-GeneID:171282 http://www.ncbi.nlm.nih.gov/gene/171282 NCBI-Rat-GeneID:681337 http://www.ncbi.nlm.nih.gov/gene/681337 HOIP:HOIP_1000025 NCBI-Human-GeneID:11332 NCBI-Mouse-GeneID:70025 NCBI-Rat-GeneID:26759 Acot7 (mol) HOIP_1000025 NCBI-Human-GeneID:11332 http://www.ncbi.nlm.nih.gov/gene/11332 NCBI-Mouse-GeneID:70025 http://www.ncbi.nlm.nih.gov/gene/70025 NCBI-Rat-GeneID:26759 http://www.ncbi.nlm.nih.gov/gene/26759 HOIP:HOIP_1000026 NCBI-Human-GeneID:10005 NCBI-Mouse-GeneID:170789 NCBI-Rat-GeneID:170588 Acot8 (mol) HOIP_1000026 NCBI-Human-GeneID:10005 http://www.ncbi.nlm.nih.gov/gene/10005 NCBI-Mouse-GeneID:170789 http://www.ncbi.nlm.nih.gov/gene/170789 NCBI-Rat-GeneID:170588 http://www.ncbi.nlm.nih.gov/gene/170588 HOIP:HOIP_1000027 NCBI-Human-GeneID:51 NCBI-Mouse-GeneID:11430 NCBI-Rat-GeneID:50681 Acox1 (mol) HOIP_1000027 NCBI-Human-GeneID:51 http://www.ncbi.nlm.nih.gov/gene/51 NCBI-Mouse-GeneID:11430 http://www.ncbi.nlm.nih.gov/gene/11430 NCBI-Rat-GeneID:50681 http://www.ncbi.nlm.nih.gov/gene/50681 HOIP:HOIP_1000028 NCBI-Human-GeneID:101 NCBI-Mouse-GeneID:11501 NCBI-Rat-GeneID:499285 Adam8 (mol) HOIP_1000028 NCBI-Human-GeneID:101 http://www.ncbi.nlm.nih.gov/gene/101 NCBI-Mouse-GeneID:11501 http://www.ncbi.nlm.nih.gov/gene/11501 NCBI-Rat-GeneID:499285 http://www.ncbi.nlm.nih.gov/gene/499285 HOIP:HOIP_1000029 NCBI-Human-GeneID:64782 NCBI-Mouse-GeneID:68048 NCBI-Rat-GeneID:361594 Aen (mol) HOIP_1000029 NCBI-Human-GeneID:64782 http://www.ncbi.nlm.nih.gov/gene/64782 NCBI-Mouse-GeneID:68048 http://www.ncbi.nlm.nih.gov/gene/68048 NCBI-Rat-GeneID:361594 http://www.ncbi.nlm.nih.gov/gene/361594 HOIP:HOIP_1000030 NCBI-Human-GeneID:196 NCBI-Mouse-GeneID:11622 NCBI-Rat-GeneID:25690 Ahr (mol) HOIP_1000030 NCBI-Human-GeneID:196 http://www.ncbi.nlm.nih.gov/gene/196 NCBI-Mouse-GeneID:11622 http://www.ncbi.nlm.nih.gov/gene/11622 NCBI-Rat-GeneID:25690 http://www.ncbi.nlm.nih.gov/gene/25690 HOIP:HOIP_1000031 NCBI-Human-GeneID:51390 NCBI-Mouse-GeneID:66253 NCBI-Rat-GeneID:292486 Aig1 (mol) HOIP_1000031 NCBI-Human-GeneID:51390 http://www.ncbi.nlm.nih.gov/gene/51390 NCBI-Mouse-GeneID:66253 http://www.ncbi.nlm.nih.gov/gene/66253 NCBI-Rat-GeneID:292486 http://www.ncbi.nlm.nih.gov/gene/292486 HOIP:HOIP_1000032 NCBI-Human-GeneID:7965 NCBI-Mouse-GeneID:231872 NCBI-Rat-GeneID:288480 Aimp2 (mol) HOIP_1000032 NCBI-Human-GeneID:7965 http://www.ncbi.nlm.nih.gov/gene/7965 NCBI-Mouse-GeneID:231872 http://www.ncbi.nlm.nih.gov/gene/231872 NCBI-Rat-GeneID:288480 http://www.ncbi.nlm.nih.gov/gene/288480 HOIP:HOIP_1000033 NCBI-Human-GeneID:22977 NCBI-Rat-GeneID:26760 Akr7a3 (mol) HOIP_1000033 NCBI-Human-GeneID:22977 http://www.ncbi.nlm.nih.gov/gene/22977 NCBI-Rat-GeneID:26760 http://www.ncbi.nlm.nih.gov/gene/26760 HOIP:HOIP_1000034 NCBI-Human-GeneID:211 NCBI-Mouse-GeneID:11655 NCBI-Rat-GeneID:65155 Alas1 (mol) HOIP_1000034 NCBI-Human-GeneID:211 http://www.ncbi.nlm.nih.gov/gene/211 NCBI-Mouse-GeneID:11655 http://www.ncbi.nlm.nih.gov/gene/11655 NCBI-Rat-GeneID:65155 http://www.ncbi.nlm.nih.gov/gene/65155 HOIP:HOIP_1000035 NCBI-Human-GeneID:216 NCBI-Mouse-GeneID:11668 NCBI-Rat-GeneID:24188 ALDH1A1 (mol) HOIP_1000035 NCBI-Human-GeneID:216 http://www.ncbi.nlm.nih.gov/gene/216 NCBI-Mouse-GeneID:11668 http://www.ncbi.nlm.nih.gov/gene/11668 NCBI-Rat-GeneID:24188 http://www.ncbi.nlm.nih.gov/gene/24188 HOIP:HOIP_1000036 NCBI-Human-GeneID:353322 NCBI-Mouse-GeneID:654824 NCBI-Rat-GeneID:361149 Ankrd37 (mol) HOIP_1000036 NCBI-Human-GeneID:353322 http://www.ncbi.nlm.nih.gov/gene/353322 NCBI-Mouse-GeneID:654824 http://www.ncbi.nlm.nih.gov/gene/654824 NCBI-Rat-GeneID:361149 http://www.ncbi.nlm.nih.gov/gene/361149 HOIP:HOIP_1000037 NCBI-Human-GeneID:26286 NCBI-Mouse-GeneID:66251 NCBI-Rat-GeneID:503165 Arfgap3 (mol) HOIP_1000037 NCBI-Human-GeneID:26286 http://www.ncbi.nlm.nih.gov/gene/26286 NCBI-Mouse-GeneID:66251 http://www.ncbi.nlm.nih.gov/gene/66251 NCBI-Rat-GeneID:503165 http://www.ncbi.nlm.nih.gov/gene/503165 HOIP:HOIP_1000038 Ataxn10 (mol) HOIP_1000038 HOIP:HOIP_1000040 A protein that is a translation product of the human BAK1 gene or a 1:1 ortholog thereof. The BAK2 gene is a recent duplication in humans and gives rise to a very similar protein. NCBI-Human-GeneID:578 NCBI-Mouse-GeneID:12018 NCBI-Rat-GeneID:116502 Bcl-2 homologous antagonist/killer Bcl-2-like protein 7 Bcl2 homologous antagonist/killer Bcl2-L-7 apoptosis regulator BAK BAK BCL2L7 CDN1 BAK1 HOIP_1000040 NCBI-Human-GeneID:578 http://www.ncbi.nlm.nih.gov/gene/578 NCBI-Mouse-GeneID:12018 http://www.ncbi.nlm.nih.gov/gene/12018 NCBI-Rat-GeneID:116502 http://www.ncbi.nlm.nih.gov/gene/116502 HOIP:HOIP_1000043 NCBI-Human-GeneID:27241 NCBI-Mouse-GeneID:319845 NCBI-Rat-GeneID:315484 Bbs9 (mol) HOIP_1000043 NCBI-Human-GeneID:27241 http://www.ncbi.nlm.nih.gov/gene/27241 NCBI-Mouse-GeneID:319845 http://www.ncbi.nlm.nih.gov/gene/319845 NCBI-Rat-GeneID:315484 http://www.ncbi.nlm.nih.gov/gene/315484 HOIP:HOIP_1000044 NCBI-Human-GeneID:602 NCBI-Mouse-GeneID:12051 NCBI-Rat-GeneID:680611 Bcl3 (mol) HOIP_1000044 NCBI-Human-GeneID:602 http://www.ncbi.nlm.nih.gov/gene/602 NCBI-Mouse-GeneID:12051 http://www.ncbi.nlm.nih.gov/gene/12051 NCBI-Rat-GeneID:680611 http://www.ncbi.nlm.nih.gov/gene/680611 HOIP:HOIP_1000045 NCBI-Human-GeneID:168620 NCBI-Mouse-GeneID:17341 NCBI-Rat-GeneID:25334 Bhlha15 (mol) HOIP_1000045 NCBI-Human-GeneID:168620 http://www.ncbi.nlm.nih.gov/gene/168620 NCBI-Mouse-GeneID:17341 http://www.ncbi.nlm.nih.gov/gene/17341 NCBI-Rat-GeneID:25334 http://www.ncbi.nlm.nih.gov/gene/25334 HOIP:HOIP_1000046 NCBI-Human-GeneID:635 NCBI-Mouse-GeneID:12116 NCBI-Rat-GeneID:81508 Bhmt (mol) HOIP_1000046 NCBI-Human-GeneID:635 http://www.ncbi.nlm.nih.gov/gene/635 NCBI-Mouse-GeneID:12116 http://www.ncbi.nlm.nih.gov/gene/12116 NCBI-Rat-GeneID:81508 http://www.ncbi.nlm.nih.gov/gene/81508 HOIP:HOIP_1000047 NCBI-Human-GeneID:3309 NCBI-Mouse-GeneID:14828 NCBI-Rat-GeneID:25617 Bip- stress sensor complex (mol) HOIP_1000047 NCBI-Human-GeneID:3309 http://www.ncbi.nlm.nih.gov/gene/3309 NCBI-Mouse-GeneID:14828 http://www.ncbi.nlm.nih.gov/gene/14828 NCBI-Rat-GeneID:25617 http://www.ncbi.nlm.nih.gov/gene/25617 HOIP:HOIP_1000048 NCBI-Human-GeneID:6046 NCBI-Mouse-GeneID:14312 NCBI-Rat-GeneID:294276 Brd2 (mol) HOIP_1000048 NCBI-Human-GeneID:6046 http://www.ncbi.nlm.nih.gov/gene/6046 NCBI-Mouse-GeneID:14312 http://www.ncbi.nlm.nih.gov/gene/14312 NCBI-Rat-GeneID:294276 http://www.ncbi.nlm.nih.gov/gene/294276 HOIP:HOIP_1000050 NCBI-Human-GeneID:7832 NCBI-Mouse-GeneID:12227 NCBI-Rat-GeneID:29619 Btg2 (mol) HOIP_1000050 NCBI-Human-GeneID:7832 http://www.ncbi.nlm.nih.gov/gene/7832 NCBI-Mouse-GeneID:12227 http://www.ncbi.nlm.nih.gov/gene/12227 NCBI-Rat-GeneID:29619 http://www.ncbi.nlm.nih.gov/gene/29619 HOIP:HOIP_1000051 C18ORF (mol) HOIP_1000051 HOIP:HOIP_1000052 NCBI-Human-GeneID:128346 C1orf162 (mol) HOIP_1000052 NCBI-Human-GeneID:128346 http://www.ncbi.nlm.nih.gov/gene/128346 HOIP:HOIP_1000053 NCBI-Human-GeneID:51250 C6orf203 (mol) HOIP_1000053 NCBI-Human-GeneID:51250 http://www.ncbi.nlm.nih.gov/gene/51250 HOIP:HOIP_1000054 NCBI-Human-GeneID:203228 NCBI-Mouse-GeneID:73205 C9orf72 (mol) HOIP_1000054 NCBI-Human-GeneID:203228 http://www.ncbi.nlm.nih.gov/gene/203228 NCBI-Mouse-GeneID:73205 http://www.ncbi.nlm.nih.gov/gene/73205 HOIP:HOIP_1000055 NCBI-Human-GeneID:771 CA12 (mol) HOIP_1000055 NCBI-Human-GeneID:771 http://www.ncbi.nlm.nih.gov/gene/771 HOIP:HOIP_1000056 NCBI-Human-GeneID:782 NCBI-Mouse-GeneID:12295 NCBI-Rat-GeneID:50688 CACNB1 (mol) HOIP_1000056 NCBI-Human-GeneID:782 http://www.ncbi.nlm.nih.gov/gene/782 NCBI-Mouse-GeneID:12295 http://www.ncbi.nlm.nih.gov/gene/12295 NCBI-Rat-GeneID:50688 http://www.ncbi.nlm.nih.gov/gene/50688 HOIP:HOIP_1000057 LRRC16B (mol) HOIP_1000057 HOIP:HOIP_1000058 NCBI-Human-GeneID:841 NCBI-Mouse-GeneID:12370 NCBI-Rat-GeneID:64044 CASP8 (mol) HOIP_1000058 NCBI-Human-GeneID:841 http://www.ncbi.nlm.nih.gov/gene/841 NCBI-Mouse-GeneID:12370 http://www.ncbi.nlm.nih.gov/gene/12370 NCBI-Rat-GeneID:64044 http://www.ncbi.nlm.nih.gov/gene/64044 HOIP:HOIP_1000059 NCBI-Human-GeneID:9994 NCBI-Mouse-GeneID:26885 NCBI-Rat-GeneID:313128 CASP8AP2 (mol) HOIP_1000059 NCBI-Human-GeneID:9994 http://www.ncbi.nlm.nih.gov/gene/9994 NCBI-Mouse-GeneID:26885 http://www.ncbi.nlm.nih.gov/gene/26885 NCBI-Rat-GeneID:313128 http://www.ncbi.nlm.nih.gov/gene/313128 HOIP:HOIP_1000060 NCBI-Human-GeneID:90693 NCBI-Mouse-GeneID:57895 NCBI-Rat-GeneID:500117 CCDC126 (mol) HOIP_1000060 NCBI-Human-GeneID:90693 http://www.ncbi.nlm.nih.gov/gene/90693 NCBI-Mouse-GeneID:57895 http://www.ncbi.nlm.nih.gov/gene/57895 NCBI-Rat-GeneID:500117 http://www.ncbi.nlm.nih.gov/gene/500117 HOIP:HOIP_1000062 NCBI-Human-GeneID:4345 NCBI-Mouse-GeneID:17470 NCBI-Rat-GeneID:24560 CD200 (mol) HOIP_1000062 NCBI-Human-GeneID:4345 http://www.ncbi.nlm.nih.gov/gene/4345 NCBI-Mouse-GeneID:17470 http://www.ncbi.nlm.nih.gov/gene/17470 NCBI-Rat-GeneID:24560 http://www.ncbi.nlm.nih.gov/gene/24560 HOIP:HOIP_1000063 NCBI-Human-GeneID:8851 NCBI-Mouse-GeneID:12569 NCBI-Rat-GeneID:116671 CDK5R1 (mol) HOIP_1000063 NCBI-Human-GeneID:8851 http://www.ncbi.nlm.nih.gov/gene/8851 NCBI-Mouse-GeneID:12569 http://www.ncbi.nlm.nih.gov/gene/12569 NCBI-Rat-GeneID:116671 http://www.ncbi.nlm.nih.gov/gene/116671 HOIP:HOIP_1000064 NCBI-Human-GeneID:1062 NCBI-Mouse-GeneID:229841 NCBI-Rat-GeneID:362044 CENPE (mol) HOIP_1000064 NCBI-Human-GeneID:1062 http://www.ncbi.nlm.nih.gov/gene/1062 NCBI-Mouse-GeneID:229841 http://www.ncbi.nlm.nih.gov/gene/229841 NCBI-Rat-GeneID:362044 http://www.ncbi.nlm.nih.gov/gene/362044 HOIP:HOIP_1000065 NCBI-Human-GeneID:8837 NCBI-Mouse-GeneID:12633 NCBI-Rat-GeneID:117279 CFLAR (mol) HOIP_1000065 NCBI-Human-GeneID:8837 http://www.ncbi.nlm.nih.gov/gene/8837 NCBI-Mouse-GeneID:12633 http://www.ncbi.nlm.nih.gov/gene/12633 NCBI-Rat-GeneID:117279 http://www.ncbi.nlm.nih.gov/gene/117279 HOIP:HOIP_1000066 NCBI-Human-GeneID:79094 NCBI-Mouse-GeneID:69065 NCBI-Rat-GeneID:362196 CHAC1 (mol) HOIP_1000066 NCBI-Human-GeneID:79094 http://www.ncbi.nlm.nih.gov/gene/79094 NCBI-Mouse-GeneID:69065 http://www.ncbi.nlm.nih.gov/gene/69065 NCBI-Rat-GeneID:362196 http://www.ncbi.nlm.nih.gov/gene/362196 HOIP:HOIP_1000067 NCBI-Human-GeneID:1649 NCBI-Mouse-GeneID:13198 NCBI-Rat-GeneID:29467 DDIT3 (mol) HOIP_1000067 NCBI-Human-GeneID:1649 http://www.ncbi.nlm.nih.gov/gene/1649 NCBI-Mouse-GeneID:13198 http://www.ncbi.nlm.nih.gov/gene/13198 NCBI-Rat-GeneID:29467 http://www.ncbi.nlm.nih.gov/gene/29467 HOIP:HOIP_1000068 NCBI-Human-GeneID:26973 NCBI-Mouse-GeneID:66917 NCBI-Rat-GeneID:315447 CHORDC1 (mol) HOIP_1000068 NCBI-Human-GeneID:26973 http://www.ncbi.nlm.nih.gov/gene/26973 NCBI-Mouse-GeneID:66917 http://www.ncbi.nlm.nih.gov/gene/66917 NCBI-Rat-GeneID:315447 http://www.ncbi.nlm.nih.gov/gene/315447 HOIP:HOIP_1000069 CITCO 6-(4-chlorophenyl)imidazo[2,1-b][1,3]thiazole-5-carbaldehyde O-(3,4-dichlorobenzyl)oxime HOIP_1000069 HOIP:HOIP_1000070 NCBI-Human-GeneID:1191 NCBI-Mouse-GeneID:12759 NCBI-Rat-GeneID:24854 CLU (mol) HOIP_1000070 NCBI-Human-GeneID:1191 http://www.ncbi.nlm.nih.gov/gene/1191 NCBI-Mouse-GeneID:12759 http://www.ncbi.nlm.nih.gov/gene/12759 NCBI-Rat-GeneID:24854 http://www.ncbi.nlm.nih.gov/gene/24854 HOIP:HOIP_1000071 NCBI-Human-GeneID:246175 NCBI-Mouse-GeneID:231464 NCBI-Rat-GeneID:360917 CNOT6L (mol) HOIP_1000071 NCBI-Human-GeneID:246175 http://www.ncbi.nlm.nih.gov/gene/246175 NCBI-Mouse-GeneID:231464 http://www.ncbi.nlm.nih.gov/gene/231464 NCBI-Rat-GeneID:360917 http://www.ncbi.nlm.nih.gov/gene/360917 HOIP:HOIP_1000072 NCBI-Human-GeneID:1284 NCBI-Mouse-GeneID:12827 NCBI-Rat-GeneID:306628 COL4A2 (mol) HOIP_1000072 NCBI-Human-GeneID:1284 http://www.ncbi.nlm.nih.gov/gene/1284 NCBI-Mouse-GeneID:12827 http://www.ncbi.nlm.nih.gov/gene/12827 NCBI-Rat-GeneID:306628 http://www.ncbi.nlm.nih.gov/gene/306628 HOIP:HOIP_1000073 NCBI-Human-GeneID:1340 NCBI-Mouse-GeneID:110323 NCBI-Rat-GeneID:688869 COX6B1 (mol) HOIP_1000073 NCBI-Human-GeneID:1340 http://www.ncbi.nlm.nih.gov/gene/1340 NCBI-Mouse-GeneID:110323 http://www.ncbi.nlm.nih.gov/gene/110323 NCBI-Rat-GeneID:688869 http://www.ncbi.nlm.nih.gov/gene/688869 HOIP:HOIP_1000074 CRBPH (mol) HOIP_1000074 HOIP:HOIP_1000075 NCBI-Human-GeneID:79174 NCBI-Mouse-GeneID:76737 NCBI-Rat-GeneID:362978 CRELD2 (mol) HOIP_1000075 NCBI-Human-GeneID:79174 http://www.ncbi.nlm.nih.gov/gene/79174 NCBI-Mouse-GeneID:76737 http://www.ncbi.nlm.nih.gov/gene/76737 NCBI-Rat-GeneID:362978 http://www.ncbi.nlm.nih.gov/gene/362978 HOIP:HOIP_1000076 A protein that is a translation product of the human CRP gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:1401 NCBI-Mouse-GeneID:12944 NCBI-Rat-GeneID:25419 CRP PTX1 C-reactive protein HOIP_1000076 NCBI-Human-GeneID:1401 http://www.ncbi.nlm.nih.gov/gene/1401 NCBI-Mouse-GeneID:12944 http://www.ncbi.nlm.nih.gov/gene/12944 NCBI-Rat-GeneID:25419 http://www.ncbi.nlm.nih.gov/gene/25419 HOIP:HOIP_1000077 NCBI-Human-GeneID:2833 NCBI-Mouse-GeneID:12766 NCBI-Rat-GeneID:84475 CXCR3 (mol) HOIP_1000077 NCBI-Human-GeneID:2833 http://www.ncbi.nlm.nih.gov/gene/2833 NCBI-Mouse-GeneID:12766 http://www.ncbi.nlm.nih.gov/gene/12766 NCBI-Rat-GeneID:84475 http://www.ncbi.nlm.nih.gov/gene/84475 HOIP:HOIP_1000078 NCBI-Human-GeneID:1555 Orthologs of the human CYP2B6 genes can be found in other species including rats, mice, and dogs, which are termed Cyp2b1, Cyp2b10, and CYP2B11, respectively Orthologs of the human CYP2B6 genes can be found in other species including rats, mice, and dogs, which are termed Cyp2b1, Cyp2b10, and CYP2B11, respectively CYP2B6 (mol) HOIP_1000078 NCBI-Human-GeneID:1555 http://www.ncbi.nlm.nih.gov/gene/1555 Orthologs of the human CYP2B6 genes can be found in other species including rats, mice, and dogs, which are termed Cyp2b1, Cyp2b10, and CYP2B11, respectively PMID:15128046 HOIP:HOIP_1000079 NCBI-Human-GeneID:1557 CYP2C19 (mol) HOIP_1000079 NCBI-Human-GeneID:1557 http://www.ncbi.nlm.nih.gov/gene/1557 HOIP:HOIP_1000080 NCBI-Human-GeneID:1565 CYP2D6 (mol) HOIP_1000080 NCBI-Human-GeneID:1565 http://www.ncbi.nlm.nih.gov/gene/1565 HOIP:HOIP_1000081 NCBI-Human-GeneID:1571 NCBI-Mouse-GeneID:13106 NCBI-Rat-GeneID:25086 CYP2E1 (mol) HOIP_1000081 NCBI-Human-GeneID:1571 http://www.ncbi.nlm.nih.gov/gene/1571 NCBI-Mouse-GeneID:13106 http://www.ncbi.nlm.nih.gov/gene/13106 NCBI-Rat-GeneID:25086 http://www.ncbi.nlm.nih.gov/gene/25086 HOIP:HOIP_1000082 NCBI-Human-GeneID:1576 CYP3A4 (mol) HOIP_1000082 NCBI-Human-GeneID:1576 http://www.ncbi.nlm.nih.gov/gene/1576 HOIP:HOIP_1000083 NCBI-Human-GeneID:1577 CYP3A5 (mol) HOIP_1000083 NCBI-Human-GeneID:1577 http://www.ncbi.nlm.nih.gov/gene/1577 HOIP:HOIP_1000084 NCBI-Human-GeneID:260293 NCBI-Mouse-GeneID:81906 NCBI-Rat-GeneID:246767 CYP4X1 (mol) HOIP_1000084 NCBI-Human-GeneID:260293 http://www.ncbi.nlm.nih.gov/gene/260293 NCBI-Mouse-GeneID:81906 http://www.ncbi.nlm.nih.gov/gene/81906 NCBI-Rat-GeneID:246767 http://www.ncbi.nlm.nih.gov/gene/246767 HOIP:HOIP_1000085 NCBI-Human-GeneID:760 Car2 (mol) HOIP_1000085 NCBI-Human-GeneID:760 http://www.ncbi.nlm.nih.gov/gene/760 HOIP:HOIP_1000089 NCBI-Human-GeneID:900 NCBI-Mouse-GeneID:12450 NCBI-Rat-GeneID:25405 Ccng1 (mol) HOIP_1000089 NCBI-Human-GeneID:900 http://www.ncbi.nlm.nih.gov/gene/900 NCBI-Mouse-GeneID:12450 http://www.ncbi.nlm.nih.gov/gene/12450 NCBI-Rat-GeneID:25405 http://www.ncbi.nlm.nih.gov/gene/25405 HOIP:HOIP_1000090 NCBI-Human-GeneID:997 NCBI-Mouse-GeneID:216150 NCBI-Rat-GeneID:299602 Cdc34 (mol) HOIP_1000090 NCBI-Human-GeneID:997 http://www.ncbi.nlm.nih.gov/gene/997 NCBI-Mouse-GeneID:216150 http://www.ncbi.nlm.nih.gov/gene/216150 NCBI-Rat-GeneID:299602 http://www.ncbi.nlm.nih.gov/gene/299602 HOIP:HOIP_1000092 NCBI-Human-GeneID:387103 NCBI-Mouse-GeneID:66311 NCBI-Rat-GeneID:689399 Cenpw (mol) HOIP_1000092 NCBI-Human-GeneID:387103 http://www.ncbi.nlm.nih.gov/gene/387103 NCBI-Mouse-GeneID:66311 http://www.ncbi.nlm.nih.gov/gene/66311 NCBI-Rat-GeneID:689399 http://www.ncbi.nlm.nih.gov/gene/689399 HOIP:HOIP_1000093 NCBI-Human-GeneID:55571 NCBI-Mouse-GeneID:52846 NCBI-Rat-GeneID:363221 Cnot11 (mol) HOIP_1000093 NCBI-Human-GeneID:55571 http://www.ncbi.nlm.nih.gov/gene/55571 NCBI-Mouse-GeneID:52846 http://www.ncbi.nlm.nih.gov/gene/52846 NCBI-Rat-GeneID:363221 http://www.ncbi.nlm.nih.gov/gene/363221 HOIP:HOIP_1000094 catenin beta 1 NCBI-Human-GeneID:1499 NCBI-Mouse-GeneID:12387 NCBI-Rat-GeneID:84353 Ctnnb1 (mol) HOIP_1000094 NCBI-Human-GeneID:1499 http://www.ncbi.nlm.nih.gov/gene/1499 NCBI-Mouse-GeneID:12387 http://www.ncbi.nlm.nih.gov/gene/12387 NCBI-Rat-GeneID:84353 http://www.ncbi.nlm.nih.gov/gene/84353 HOIP:HOIP_1000095 NCBI-Human-GeneID:54951 NCBI-Mouse-GeneID:27784 NCBI-Rat-GeneID:289603 Commd8 (mol) HOIP_1000095 NCBI-Human-GeneID:54951 http://www.ncbi.nlm.nih.gov/gene/54951 NCBI-Mouse-GeneID:27784 http://www.ncbi.nlm.nih.gov/gene/27784 NCBI-Rat-GeneID:289603 http://www.ncbi.nlm.nih.gov/gene/289603 HOIP:HOIP_1000096 NCBI-Human-GeneID:10404 NCBI-Mouse-GeneID:54381 NCBI-Rat-GeneID:58952 Cpq (mol) HOIP_1000096 NCBI-Human-GeneID:10404 http://www.ncbi.nlm.nih.gov/gene/10404 NCBI-Mouse-GeneID:54381 http://www.ncbi.nlm.nih.gov/gene/54381 NCBI-Rat-GeneID:58952 http://www.ncbi.nlm.nih.gov/gene/58952 HOIP:HOIP_1000097 NCBI-Human-GeneID:1374 NCBI-Mouse-GeneID:12894 NCBI-Rat-GeneID:25757 Cpt1 (mol) HOIP_1000097 NCBI-Human-GeneID:1374 http://www.ncbi.nlm.nih.gov/gene/1374 NCBI-Mouse-GeneID:12894 http://www.ncbi.nlm.nih.gov/gene/12894 NCBI-Rat-GeneID:25757 http://www.ncbi.nlm.nih.gov/gene/25757 HOIP:HOIP_1000098 NCBI-Human-GeneID:1376 NCBI-Mouse-GeneID:12896 NCBI-Rat-GeneID:25413 Cpt2 (mol) HOIP_1000098 NCBI-Human-GeneID:1376 http://www.ncbi.nlm.nih.gov/gene/1376 NCBI-Mouse-GeneID:12896 http://www.ncbi.nlm.nih.gov/gene/12896 NCBI-Rat-GeneID:25413 http://www.ncbi.nlm.nih.gov/gene/25413 HOIP:HOIP_1000100 NCBI-Human-GeneID:1543 NCBI-Mouse-GeneID:13076 NCBI-Rat-GeneID:24296 Cyp1A1 (mol) HOIP_1000100 NCBI-Human-GeneID:1543 http://www.ncbi.nlm.nih.gov/gene/1543 NCBI-Mouse-GeneID:13076 http://www.ncbi.nlm.nih.gov/gene/13076 NCBI-Rat-GeneID:24296 http://www.ncbi.nlm.nih.gov/gene/24296 HOIP:HOIP_1000101 NCBI-Rat-GeneID:24300 Cyp2b1 (mol) HOIP_1000101 NCBI-Rat-GeneID:24300 http://www.ncbi.nlm.nih.gov/gene/24300 HOIP:HOIP_1000102 NCBI-Mouse-GeneID:13088 Cyp2b10 (mol) HOIP_1000102 NCBI-Mouse-GeneID:13088 http://www.ncbi.nlm.nih.gov/gene/13088 HOIP:HOIP_1000103 NCBI-Rat-GeneID:293989 Cyp2c6v1 (mol) HOIP_1000103 NCBI-Rat-GeneID:293989 http://www.ncbi.nlm.nih.gov/gene/293989 HOIP:HOIP_1000104 NCBI-Rat-GeneID:24303 Cyp2d3 (mol) HOIP_1000104 NCBI-Rat-GeneID:24303 http://www.ncbi.nlm.nih.gov/gene/24303 HOIP:HOIP_1000105 NCBI-Rat-GeneID:171522 Cyp2d4 (mol) HOIP_1000105 NCBI-Rat-GeneID:171522 http://www.ncbi.nlm.nih.gov/gene/171522 HOIP:HOIP_1000106 NCBI-Mouse-GeneID:13112 Cyp3a11 (mol) HOIP_1000106 NCBI-Mouse-GeneID:13112 http://www.ncbi.nlm.nih.gov/gene/13112 HOIP:HOIP_1000107 NCBI-Rat-GeneID:50549 Cyp4a1 (mol) HOIP_1000107 NCBI-Rat-GeneID:50549 http://www.ncbi.nlm.nih.gov/gene/50549 HOIP:HOIP_1000108 NCBI-Rat-GeneID:298423 Cyp4a3 (mol) HOIP_1000108 NCBI-Rat-GeneID:298423 http://www.ncbi.nlm.nih.gov/gene/298423 HOIP:HOIP_1000109 NCBI-Rat-GeneID:286904 Cyp4f4 (mol) HOIP_1000109 NCBI-Rat-GeneID:286904 http://www.ncbi.nlm.nih.gov/gene/286904 HOIP:HOIP_1000110 NCBI-Human-GeneID:54541 NCBI-Mouse-GeneID:74747 NCBI-Rat-GeneID:140942 DDIT4 (mol) HOIP_1000110 NCBI-Human-GeneID:54541 http://www.ncbi.nlm.nih.gov/gene/54541 NCBI-Mouse-GeneID:74747 http://www.ncbi.nlm.nih.gov/gene/74747 NCBI-Rat-GeneID:140942 http://www.ncbi.nlm.nih.gov/gene/140942 HOIP:HOIP_1000111 NCBI-Human-GeneID:65992 NCBI-Mouse-GeneID:77006 NCBI-Rat-GeneID:296162 DDRGK1 (mol) HOIP_1000111 NCBI-Human-GeneID:65992 http://www.ncbi.nlm.nih.gov/gene/65992 NCBI-Mouse-GeneID:77006 http://www.ncbi.nlm.nih.gov/gene/77006 NCBI-Rat-GeneID:296162 http://www.ncbi.nlm.nih.gov/gene/296162 HOIP:HOIP_1000112 NCBI-Human-GeneID:29118 NCBI-Mouse-GeneID:30959 NCBI-Rat-GeneID:58856 DDX25 (mol) HOIP_1000112 NCBI-Human-GeneID:29118 http://www.ncbi.nlm.nih.gov/gene/29118 NCBI-Mouse-GeneID:30959 http://www.ncbi.nlm.nih.gov/gene/30959 NCBI-Rat-GeneID:58856 http://www.ncbi.nlm.nih.gov/gene/58856 HOIP:HOIP_1000113 NCBI-Human-GeneID:84649 NCBI-Mouse-GeneID:67800 NCBI-Rat-GeneID:252900 DGAT2 (mol) HOIP_1000113 NCBI-Human-GeneID:84649 http://www.ncbi.nlm.nih.gov/gene/84649 NCBI-Mouse-GeneID:67800 http://www.ncbi.nlm.nih.gov/gene/67800 NCBI-Rat-GeneID:252900 http://www.ncbi.nlm.nih.gov/gene/252900 HOIP:HOIP_1000114 NCBI-Human-GeneID:4189 NCBI-Mouse-GeneID:27362 NCBI-Rat-GeneID:24908 DNAJB9 (mol) HOIP_1000114 NCBI-Human-GeneID:4189 http://www.ncbi.nlm.nih.gov/gene/4189 NCBI-Mouse-GeneID:27362 http://www.ncbi.nlm.nih.gov/gene/27362 NCBI-Rat-GeneID:24908 http://www.ncbi.nlm.nih.gov/gene/24908 HOIP:HOIP_1000115 NCBI-Human-GeneID:5611 NCBI-Mouse-GeneID:100037258 NCBI-Rat-GeneID:63880 DNAJC3 (mol) HOIP_1000115 NCBI-Human-GeneID:5611 http://www.ncbi.nlm.nih.gov/gene/5611 NCBI-Mouse-GeneID:100037258 http://www.ncbi.nlm.nih.gov/gene/100037258 NCBI-Rat-GeneID:63880 http://www.ncbi.nlm.nih.gov/gene/63880 HOIP:HOIP_1000116 NCBI-Human-GeneID:89978 NCBI-Mouse-GeneID:66632 NCBI-Rat-GeneID:362191 DPH6 (mol) HOIP_1000116 NCBI-Human-GeneID:89978 http://www.ncbi.nlm.nih.gov/gene/89978 NCBI-Mouse-GeneID:66632 http://www.ncbi.nlm.nih.gov/gene/66632 NCBI-Rat-GeneID:362191 http://www.ncbi.nlm.nih.gov/gene/362191 HOIP:HOIP_1000118 NCBI-Human-GeneID:115265 NCBI-Mouse-GeneID:73284 NCBI-Rat-GeneID:100363484 Ddit4l (mol) HOIP_1000118 NCBI-Human-GeneID:115265 http://www.ncbi.nlm.nih.gov/gene/115265 NCBI-Mouse-GeneID:73284 http://www.ncbi.nlm.nih.gov/gene/73284 NCBI-Rat-GeneID:100363484 http://www.ncbi.nlm.nih.gov/gene/100363484 HOIP:HOIP_1000119 NCBI-Human-GeneID:9188 NCBI-Mouse-GeneID:56200 NCBI-Rat-GeneID:317399 Ddx21 (mol) HOIP_1000119 NCBI-Human-GeneID:9188 http://www.ncbi.nlm.nih.gov/gene/9188 NCBI-Mouse-GeneID:56200 http://www.ncbi.nlm.nih.gov/gene/56200 NCBI-Rat-GeneID:317399 http://www.ncbi.nlm.nih.gov/gene/317399 HOIP:HOIP_1000120 NCBI-Human-GeneID:1656 NCBI-Mouse-GeneID:13209 NCBI-Rat-GeneID:500988 Ddx6 (mol) HOIP_1000120 NCBI-Human-GeneID:1656 http://www.ncbi.nlm.nih.gov/gene/1656 NCBI-Mouse-GeneID:13209 http://www.ncbi.nlm.nih.gov/gene/13209 NCBI-Rat-GeneID:500988 http://www.ncbi.nlm.nih.gov/gene/500988 HOIP:HOIP_1000121 NCBI-Human-GeneID:7266 NCBI-Mouse-GeneID:56354 NCBI-Rat-GeneID:303536 Dnajc7 (mol) HOIP_1000121 NCBI-Human-GeneID:7266 http://www.ncbi.nlm.nih.gov/gene/7266 NCBI-Mouse-GeneID:56354 http://www.ncbi.nlm.nih.gov/gene/56354 NCBI-Rat-GeneID:303536 http://www.ncbi.nlm.nih.gov/gene/303536 HOIP:HOIP_1000123 NCBI-Human-GeneID:319118 EIF4BP1 (mol) HOIP_1000123 NCBI-Human-GeneID:319118 http://www.ncbi.nlm.nih.gov/gene/319118 HOIP:HOIP_1000124 NCBI-Human-GeneID:1996 NCBI-Mouse-GeneID:15572 NCBI-Rat-GeneID:432358 ELAVL4 (mol) HOIP_1000124 NCBI-Human-GeneID:1996 http://www.ncbi.nlm.nih.gov/gene/1996 NCBI-Mouse-GeneID:15572 http://www.ncbi.nlm.nih.gov/gene/15572 NCBI-Rat-GeneID:432358 http://www.ncbi.nlm.nih.gov/gene/432358 HOIP:HOIP_1000125 NCBI-Human-GeneID:79071 NCBI-Mouse-GeneID:170439 NCBI-Rat-GeneID:171402 ELOVL6 (mol) HOIP_1000125 NCBI-Human-GeneID:79071 http://www.ncbi.nlm.nih.gov/gene/79071 NCBI-Mouse-GeneID:170439 http://www.ncbi.nlm.nih.gov/gene/170439 NCBI-Rat-GeneID:171402 http://www.ncbi.nlm.nih.gov/gene/171402 HOIP:HOIP_1000126 NCBI-Mouse-GeneID:67475 ERO1LB (mol) HOIP_1000126 NCBI-Mouse-GeneID:67475 http://www.ncbi.nlm.nih.gov/gene/67475 HOIP:HOIP_1000127 NCBI-Human-GeneID:54431 NCBI-Mouse-GeneID:66861 NCBI-Rat-GeneID:295690 DNAJC10 (mol) HOIP_1000127 NCBI-Human-GeneID:54431 http://www.ncbi.nlm.nih.gov/gene/54431 NCBI-Mouse-GeneID:66861 http://www.ncbi.nlm.nih.gov/gene/66861 NCBI-Rat-GeneID:295690 http://www.ncbi.nlm.nih.gov/gene/295690 HOIP:HOIP_1000128 NCBI-Human-GeneID:1906 NCBI-Mouse-GeneID:13614 NCBI-Rat-GeneID:24323 ET-1 (mol) HOIP_1000128 NCBI-Human-GeneID:1906 http://www.ncbi.nlm.nih.gov/gene/1906 NCBI-Mouse-GeneID:13614 http://www.ncbi.nlm.nih.gov/gene/13614 NCBI-Rat-GeneID:24323 http://www.ncbi.nlm.nih.gov/gene/24323 HOIP:HOIP_1000129 NCBI-Human-GeneID:1891 NCBI-Mouse-GeneID:51798 NCBI-Rat-GeneID:64526 Ech1 (mol) HOIP_1000129 NCBI-Human-GeneID:1891 http://www.ncbi.nlm.nih.gov/gene/1891 NCBI-Mouse-GeneID:51798 http://www.ncbi.nlm.nih.gov/gene/51798 NCBI-Rat-GeneID:64526 http://www.ncbi.nlm.nih.gov/gene/64526 HOIP:HOIP_1000131 NCBI-Human-GeneID:1962 NCBI-Mouse-GeneID:74147 NCBI-Rat-GeneID:171142 Ehhadh (mol) HOIP_1000131 NCBI-Human-GeneID:1962 http://www.ncbi.nlm.nih.gov/gene/1962 NCBI-Mouse-GeneID:74147 http://www.ncbi.nlm.nih.gov/gene/74147 NCBI-Rat-GeneID:171142 http://www.ncbi.nlm.nih.gov/gene/171142 HOIP:HOIP_1000132 NCBI-Human-GeneID:1965 NCBI-Mouse-GeneID:13665 NCBI-Rat-GeneID:54318 Eif2s1 (mol) HOIP_1000132 NCBI-Human-GeneID:1965 http://www.ncbi.nlm.nih.gov/gene/1965 NCBI-Mouse-GeneID:13665 http://www.ncbi.nlm.nih.gov/gene/13665 NCBI-Rat-GeneID:54318 http://www.ncbi.nlm.nih.gov/gene/54318 HOIP:HOIP_1000133 NCBI-Human-GeneID:1973 NCBI-Mouse-GeneID:13681 NCBI-Rat-GeneID:287436 Eif4a1 (mol) HOIP_1000133 NCBI-Human-GeneID:1973 http://www.ncbi.nlm.nih.gov/gene/1973 NCBI-Mouse-GeneID:13681 http://www.ncbi.nlm.nih.gov/gene/13681 NCBI-Rat-GeneID:287436 http://www.ncbi.nlm.nih.gov/gene/287436 HOIP:HOIP_1000134 NCBI-Human-GeneID:64787 NCBI-Mouse-GeneID:98845 NCBI-Rat-GeneID:361674 Eps8l2 (mol) HOIP_1000134 NCBI-Human-GeneID:64787 http://www.ncbi.nlm.nih.gov/gene/64787 NCBI-Mouse-GeneID:98845 http://www.ncbi.nlm.nih.gov/gene/98845 NCBI-Rat-GeneID:361674 http://www.ncbi.nlm.nih.gov/gene/361674 HOIP:HOIP_1000135 Ero1 (mol) HOIP_1000135 HOIP:HOIP_1000136 NCBI-Human-GeneID:55224 NCBI-Mouse-GeneID:214253 NCBI-Rat-GeneID:360843 Etnk2 (mol) HOIP_1000136 NCBI-Human-GeneID:55224 http://www.ncbi.nlm.nih.gov/gene/55224 NCBI-Mouse-GeneID:214253 http://www.ncbi.nlm.nih.gov/gene/214253 NCBI-Rat-GeneID:360843 http://www.ncbi.nlm.nih.gov/gene/360843 HOIP:HOIP_1000137 NCBI-Human-GeneID:2168 NCBI-Mouse-GeneID:14080 NCBI-Rat-GeneID:24360 FABP1 (mol) HOIP_1000137 NCBI-Human-GeneID:2168 http://www.ncbi.nlm.nih.gov/gene/2168 NCBI-Mouse-GeneID:14080 http://www.ncbi.nlm.nih.gov/gene/14080 NCBI-Rat-GeneID:24360 http://www.ncbi.nlm.nih.gov/gene/24360 HOIP:HOIP_1000138 NCBI-Human-GeneID:11124 NCBI-Mouse-GeneID:14084 NCBI-Rat-GeneID:140657 FAF1 (mol) HOIP_1000138 NCBI-Human-GeneID:11124 http://www.ncbi.nlm.nih.gov/gene/11124 NCBI-Mouse-GeneID:14084 http://www.ncbi.nlm.nih.gov/gene/14084 NCBI-Rat-GeneID:140657 http://www.ncbi.nlm.nih.gov/gene/140657 HOIP:HOIP_1000139 NCBI-Human-GeneID:355 NCBI-Mouse-GeneID:14102 NCBI-Rat-GeneID:246097 FAS (mol) HOIP_1000139 NCBI-Human-GeneID:355 http://www.ncbi.nlm.nih.gov/gene/355 NCBI-Mouse-GeneID:14102 http://www.ncbi.nlm.nih.gov/gene/14102 NCBI-Rat-GeneID:246097 http://www.ncbi.nlm.nih.gov/gene/246097 HOIP:HOIP_1000140 NCBI-Human-GeneID:356 NCBI-Rat-GeneID:25385 FASLG (mol) HOIP_1000140 NCBI-Human-GeneID:356 http://www.ncbi.nlm.nih.gov/gene/356 NCBI-Rat-GeneID:25385 http://www.ncbi.nlm.nih.gov/gene/25385 HOIP:HOIP_1000141 NCBI-Human-GeneID:2259 NCBI-Mouse-GeneID:14169 NCBI-Rat-GeneID:63851 FGF14 (mol) HOIP_1000141 NCBI-Human-GeneID:2259 http://www.ncbi.nlm.nih.gov/gene/2259 NCBI-Mouse-GeneID:14169 http://www.ncbi.nlm.nih.gov/gene/14169 NCBI-Rat-GeneID:63851 http://www.ncbi.nlm.nih.gov/gene/63851 HOIP:HOIP_1000142 NCBI-Human-GeneID:8817 NCBI-Mouse-GeneID:14172 NCBI-Rat-GeneID:29369 FGF18 (mol) HOIP_1000142 NCBI-Human-GeneID:8817 http://www.ncbi.nlm.nih.gov/gene/8817 NCBI-Mouse-GeneID:14172 http://www.ncbi.nlm.nih.gov/gene/14172 NCBI-Rat-GeneID:29369 http://www.ncbi.nlm.nih.gov/gene/29369 HOIP:HOIP_1000143 NCBI-Human-GeneID:9965 NCBI-Rat-GeneID:170582 FGF19 (mol) HOIP_1000143 NCBI-Human-GeneID:9965 http://www.ncbi.nlm.nih.gov/gene/9965 NCBI-Rat-GeneID:170582 http://www.ncbi.nlm.nih.gov/gene/170582 HOIP:HOIP_1000144 NCBI-Human-GeneID:2247 NCBI-Mouse-GeneID:14173 NCBI-Rat-GeneID:54250 FGF2 (mol) HOIP_1000144 NCBI-Human-GeneID:2247 http://www.ncbi.nlm.nih.gov/gene/2247 NCBI-Mouse-GeneID:14173 http://www.ncbi.nlm.nih.gov/gene/14173 NCBI-Rat-GeneID:54250 http://www.ncbi.nlm.nih.gov/gene/54250 HOIP:HOIP_1000145 NCBI-Human-GeneID:26291 NCBI-Mouse-GeneID:56636 NCBI-Rat-GeneID:170580 FGF21 (mol) HOIP_1000145 NCBI-Human-GeneID:26291 http://www.ncbi.nlm.nih.gov/gene/26291 NCBI-Mouse-GeneID:56636 http://www.ncbi.nlm.nih.gov/gene/56636 NCBI-Rat-GeneID:170580 http://www.ncbi.nlm.nih.gov/gene/170580 HOIP:HOIP_1000146 NCBI-Human-GeneID:114827 NCBI-Mouse-GeneID:329977 NCBI-Rat-GeneID:500577 FHAD1 (mol) HOIP_1000146 NCBI-Human-GeneID:114827 http://www.ncbi.nlm.nih.gov/gene/114827 NCBI-Mouse-GeneID:329977 http://www.ncbi.nlm.nih.gov/gene/329977 NCBI-Rat-GeneID:500577 http://www.ncbi.nlm.nih.gov/gene/500577 HOIP:HOIP_1000147 NCBI-Human-GeneID:2272 NCBI-Mouse-GeneID:14198 NCBI-Rat-GeneID:60398 FHIT (mol) HOIP_1000147 NCBI-Human-GeneID:2272 http://www.ncbi.nlm.nih.gov/gene/2272 NCBI-Mouse-GeneID:14198 http://www.ncbi.nlm.nih.gov/gene/14198 NCBI-Rat-GeneID:60398 http://www.ncbi.nlm.nih.gov/gene/60398 HOIP:HOIP_1000148 NCBI-Human-GeneID:201163 NCBI-Mouse-GeneID:216805 NCBI-Rat-GeneID:303185 FLCN (mol) HOIP_1000148 NCBI-Human-GeneID:201163 http://www.ncbi.nlm.nih.gov/gene/201163 NCBI-Mouse-GeneID:216805 http://www.ncbi.nlm.nih.gov/gene/216805 NCBI-Rat-GeneID:303185 http://www.ncbi.nlm.nih.gov/gene/303185 HOIP:HOIP_1000149 NCBI-Human-GeneID:2335 NCBI-Mouse-GeneID:14268 NCBI-Rat-GeneID:25661 FN1 (mol) HOIP_1000149 NCBI-Human-GeneID:2335 http://www.ncbi.nlm.nih.gov/gene/2335 NCBI-Mouse-GeneID:14268 http://www.ncbi.nlm.nih.gov/gene/14268 NCBI-Rat-GeneID:25661 http://www.ncbi.nlm.nih.gov/gene/25661 HOIP:HOIP_1000150 NCBI-Human-GeneID:64838 NCBI-Mouse-GeneID:64339 FNDC4 (mol) HOIP_1000150 NCBI-Human-GeneID:64838 http://www.ncbi.nlm.nih.gov/gene/64838 NCBI-Mouse-GeneID:64339 http://www.ncbi.nlm.nih.gov/gene/64339 HOIP:HOIP_1000152 NCBI-Human-GeneID:2166 NCBI-Mouse-GeneID:14073 NCBI-Rat-GeneID:29347 Faah (mol) HOIP_1000152 NCBI-Human-GeneID:2166 http://www.ncbi.nlm.nih.gov/gene/2166 NCBI-Mouse-GeneID:14073 http://www.ncbi.nlm.nih.gov/gene/14073 NCBI-Rat-GeneID:29347 http://www.ncbi.nlm.nih.gov/gene/29347 HOIP:HOIP_1000153 NCBI-Human-GeneID:2171 NCBI-Mouse-GeneID:16592 NCBI-Rat-GeneID:140868 Fabp5 (mol) HOIP_1000153 NCBI-Human-GeneID:2171 http://www.ncbi.nlm.nih.gov/gene/2171 NCBI-Mouse-GeneID:16592 http://www.ncbi.nlm.nih.gov/gene/16592 NCBI-Rat-GeneID:140868 http://www.ncbi.nlm.nih.gov/gene/140868 HOIP:HOIP_1000154 NCBI-Human-GeneID:2195 NCBI-Mouse-GeneID:14107 NCBI-Rat-GeneID:83720 Fat1 (mol) HOIP_1000154 NCBI-Human-GeneID:2195 http://www.ncbi.nlm.nih.gov/gene/2195 NCBI-Mouse-GeneID:14107 http://www.ncbi.nlm.nih.gov/gene/14107 NCBI-Rat-GeneID:83720 http://www.ncbi.nlm.nih.gov/gene/83720 HOIP:HOIP_1000156 NCBI-Human-GeneID:2339 NCBI-Mouse-GeneID:14272 NCBI-Rat-GeneID:25318 Fnta (mol) HOIP_1000156 NCBI-Human-GeneID:2339 http://www.ncbi.nlm.nih.gov/gene/2339 NCBI-Mouse-GeneID:14272 http://www.ncbi.nlm.nih.gov/gene/14272 NCBI-Rat-GeneID:25318 http://www.ncbi.nlm.nih.gov/gene/25318 HOIP:HOIP_1000157 NCBI-Human-GeneID:55632 NCBI-Mouse-GeneID:217558 NCBI-Rat-GeneID:299002 G2e3 (mol) HOIP_1000157 NCBI-Human-GeneID:55632 http://www.ncbi.nlm.nih.gov/gene/55632 NCBI-Mouse-GeneID:217558 http://www.ncbi.nlm.nih.gov/gene/217558 NCBI-Rat-GeneID:299002 http://www.ncbi.nlm.nih.gov/gene/299002 HOIP:HOIP_1000158 NCBI-Human-GeneID:2539 NCBI-Rat-GeneID:24377 G6PD (mol) HOIP_1000158 NCBI-Human-GeneID:2539 http://www.ncbi.nlm.nih.gov/gene/2539 NCBI-Rat-GeneID:24377 http://www.ncbi.nlm.nih.gov/gene/24377 HOIP:HOIP_1000159 NCBI-Human-GeneID:23766 GABARAPL3 (mol) HOIP_1000159 NCBI-Human-GeneID:23766 http://www.ncbi.nlm.nih.gov/gene/23766 HOIP:HOIP_1000160 NCBI-Human-GeneID:4616 NCBI-Mouse-GeneID:17873 NCBI-Rat-GeneID:299626 GADD45B (mol) HOIP_1000160 NCBI-Human-GeneID:4616 http://www.ncbi.nlm.nih.gov/gene/4616 NCBI-Mouse-GeneID:17873 http://www.ncbi.nlm.nih.gov/gene/17873 NCBI-Rat-GeneID:299626 http://www.ncbi.nlm.nih.gov/gene/299626 HOIP:HOIP_1000161 NCBI-Human-GeneID:2619 NCBI-Mouse-GeneID:14451 NCBI-Rat-GeneID:683470 GAS1 (mol) HOIP_1000161 NCBI-Human-GeneID:2619 http://www.ncbi.nlm.nih.gov/gene/2619 NCBI-Mouse-GeneID:14451 http://www.ncbi.nlm.nih.gov/gene/14451 NCBI-Rat-GeneID:683470 http://www.ncbi.nlm.nih.gov/gene/683470 HOIP:HOIP_1000162 NCBI-Human-GeneID:9648 NCBI-Mouse-GeneID:70297 NCBI-Rat-GeneID:309798 GCC2 (mol) HOIP_1000162 NCBI-Human-GeneID:9648 http://www.ncbi.nlm.nih.gov/gene/9648 NCBI-Mouse-GeneID:70297 http://www.ncbi.nlm.nih.gov/gene/70297 NCBI-Rat-GeneID:309798 http://www.ncbi.nlm.nih.gov/gene/309798 HOIP:HOIP_1000163 NCBI-Human-GeneID:2729 NCBI-Mouse-GeneID:14629 NCBI-Rat-GeneID:25283 Glutamate-Cysteine Ligase Catalytic Subunit GCLC [canonical] (mol) HOIP_1000163 NCBI-Human-GeneID:2729 http://www.ncbi.nlm.nih.gov/gene/2729 NCBI-Mouse-GeneID:14629 http://www.ncbi.nlm.nih.gov/gene/14629 NCBI-Rat-GeneID:25283 http://www.ncbi.nlm.nih.gov/gene/25283 HOIP:HOIP_1000164 NCBI-Human-GeneID:9518 NCBI-Mouse-GeneID:23886 NCBI-Rat-GeneID:29455 GDF15 (mol) HOIP_1000164 NCBI-Human-GeneID:9518 http://www.ncbi.nlm.nih.gov/gene/9518 NCBI-Mouse-GeneID:23886 http://www.ncbi.nlm.nih.gov/gene/23886 NCBI-Rat-GeneID:29455 http://www.ncbi.nlm.nih.gov/gene/29455 HOIP:HOIP_1000165 NCBI-Human-GeneID:284161 NCBI-Mouse-GeneID:66569 NCBI-Rat-GeneID:303407 GDPD1 (mol) HOIP_1000165 NCBI-Human-GeneID:284161 http://www.ncbi.nlm.nih.gov/gene/284161 NCBI-Mouse-GeneID:66569 http://www.ncbi.nlm.nih.gov/gene/66569 NCBI-Rat-GeneID:303407 http://www.ncbi.nlm.nih.gov/gene/303407 HOIP:HOIP_1000166 NCBI-Human-GeneID:2673 NCBI-Mouse-GeneID:14583 NCBI-Rat-GeneID:297417 GFPT1 (mol) HOIP_1000166 NCBI-Human-GeneID:2673 http://www.ncbi.nlm.nih.gov/gene/2673 NCBI-Mouse-GeneID:14583 http://www.ncbi.nlm.nih.gov/gene/14583 NCBI-Rat-GeneID:297417 http://www.ncbi.nlm.nih.gov/gene/297417 HOIP:HOIP_1000167 NCBI-Human-GeneID:11010 NCBI-Mouse-GeneID:73690 NCBI-Rat-GeneID:299783 GLIPR1 (mol) HOIP_1000167 NCBI-Human-GeneID:11010 http://www.ncbi.nlm.nih.gov/gene/11010 NCBI-Mouse-GeneID:73690 http://www.ncbi.nlm.nih.gov/gene/73690 NCBI-Rat-GeneID:299783 http://www.ncbi.nlm.nih.gov/gene/299783 HOIP:HOIP_1000168 NCBI-Human-GeneID:10020 NCBI-Mouse-GeneID:50798 NCBI-Rat-GeneID:114711 GNE (mol) HOIP_1000168 NCBI-Human-GeneID:10020 http://www.ncbi.nlm.nih.gov/gene/10020 NCBI-Mouse-GeneID:50798 http://www.ncbi.nlm.nih.gov/gene/50798 NCBI-Rat-GeneID:114711 http://www.ncbi.nlm.nih.gov/gene/114711 HOIP:HOIP_1000169 NCBI-Human-GeneID:2863 NCBI-Mouse-GeneID:71111 NCBI-Rat-GeneID:288995 GPR39 (mol) HOIP_1000169 NCBI-Human-GeneID:2863 http://www.ncbi.nlm.nih.gov/gene/2863 NCBI-Mouse-GeneID:71111 http://www.ncbi.nlm.nih.gov/gene/71111 NCBI-Rat-GeneID:288995 http://www.ncbi.nlm.nih.gov/gene/288995 HOIP:HOIP_1000170 NCBI-Human-GeneID:2918 NCBI-Mouse-GeneID:14823 NCBI-Rat-GeneID:60590 GRM8 (mol) HOIP_1000170 NCBI-Human-GeneID:2918 http://www.ncbi.nlm.nih.gov/gene/2918 NCBI-Mouse-GeneID:14823 http://www.ncbi.nlm.nih.gov/gene/14823 NCBI-Rat-GeneID:60590 http://www.ncbi.nlm.nih.gov/gene/60590 HOIP:HOIP_1000171 NCBI-Human-GeneID:7184 NCBI-Mouse-GeneID:22027 NCBI-Rat-GeneID:362862 GRP94 HSP90B1 (mol) HOIP_1000171 NCBI-Human-GeneID:7184 http://www.ncbi.nlm.nih.gov/gene/7184 NCBI-Mouse-GeneID:22027 http://www.ncbi.nlm.nih.gov/gene/22027 NCBI-Rat-GeneID:362862 http://www.ncbi.nlm.nih.gov/gene/362862 HOIP:HOIP_1000173 NCBI-Human-GeneID:51512 NCBI-Mouse-GeneID:29870 NCBI-Rat-GeneID:300126 GTSE1 (mol) HOIP_1000173 NCBI-Human-GeneID:51512 http://www.ncbi.nlm.nih.gov/gene/51512 NCBI-Mouse-GeneID:29870 http://www.ncbi.nlm.nih.gov/gene/29870 NCBI-Rat-GeneID:300126 http://www.ncbi.nlm.nih.gov/gene/300126 HOIP:HOIP_1000174 NCBI-Human-GeneID:1647 NCBI-Mouse-GeneID:13197 NCBI-Rat-GeneID:25112 Gadd45a (mol) HOIP_1000174 NCBI-Human-GeneID:1647 http://www.ncbi.nlm.nih.gov/gene/1647 NCBI-Mouse-GeneID:13197 http://www.ncbi.nlm.nih.gov/gene/13197 NCBI-Rat-GeneID:25112 http://www.ncbi.nlm.nih.gov/gene/25112 HOIP:HOIP_1000177 Glutathione peroxidase (mol) HOIP_1000177 HOIP:HOIP_1000178 NCBI-Human-GeneID:2877 NCBI-Mouse-GeneID:14776 NCBI-Rat-GeneID:29326 Gpx2 (mol) HOIP_1000178 NCBI-Human-GeneID:2877 http://www.ncbi.nlm.nih.gov/gene/2877 NCBI-Mouse-GeneID:14776 http://www.ncbi.nlm.nih.gov/gene/14776 NCBI-Rat-GeneID:29326 http://www.ncbi.nlm.nih.gov/gene/29326 HOIP:HOIP_1000179 NCBI-Human-GeneID:2940 NCBI-Mouse-GeneID:14859 NCBI-Rat-GeneID:494500 GSTA3 (mol) HOIP_1000179 NCBI-Human-GeneID:2940 http://www.ncbi.nlm.nih.gov/gene/2940 NCBI-Mouse-GeneID:14859 http://www.ncbi.nlm.nih.gov/gene/14859 NCBI-Rat-GeneID:494500 http://www.ncbi.nlm.nih.gov/gene/494500 HOIP:HOIP_1000180 NCBI-Human-GeneID:2947 NCBI-Mouse-GeneID:14864 NCBI-Rat-GeneID:108348148 GSTM3 (mol) HOIP_1000180 NCBI-Human-GeneID:2947 http://www.ncbi.nlm.nih.gov/gene/2947 NCBI-Mouse-GeneID:14864 http://www.ncbi.nlm.nih.gov/gene/14864 NCBI-Rat-GeneID:108348148 http://www.ncbi.nlm.nih.gov/gene/108348148 HOIP:HOIP_1000181 NCBI-Human-GeneID:3021 NCBI-Mouse-GeneID:15081 NCBI-Rat-GeneID:117056 H3f3b (mol) HOIP_1000181 NCBI-Human-GeneID:3021 http://www.ncbi.nlm.nih.gov/gene/3021 NCBI-Mouse-GeneID:15081 http://www.ncbi.nlm.nih.gov/gene/15081 NCBI-Rat-GeneID:117056 http://www.ncbi.nlm.nih.gov/gene/117056 HOIP:HOIP_1000182 NCBI-Human-GeneID:3055 NCBI-Mouse-GeneID:15162 NCBI-Rat-GeneID:25734 HCK (mol) HOIP_1000182 NCBI-Human-GeneID:3055 http://www.ncbi.nlm.nih.gov/gene/3055 NCBI-Mouse-GeneID:15162 http://www.ncbi.nlm.nih.gov/gene/15162 NCBI-Rat-GeneID:25734 http://www.ncbi.nlm.nih.gov/gene/25734 HOIP:HOIP_1000183 HDGFRP3 (mol) HOIP_1000183 HOIP:HOIP_1000184 NCBI-Human-GeneID:9709 NCBI-Mouse-GeneID:64209 NCBI-Rat-GeneID:85430 HERPUD1 (mol) HOIP_1000184 NCBI-Human-GeneID:9709 http://www.ncbi.nlm.nih.gov/gene/9709 NCBI-Mouse-GeneID:64209 http://www.ncbi.nlm.nih.gov/gene/64209 NCBI-Rat-GeneID:85430 http://www.ncbi.nlm.nih.gov/gene/85430 HOIP:HOIP_1000185 NCBI-Human-GeneID:64344 NCBI-Mouse-GeneID:53417 NCBI-Rat-GeneID:64345 HIF3A (mol) HOIP_1000185 NCBI-Human-GeneID:64344 http://www.ncbi.nlm.nih.gov/gene/64344 NCBI-Mouse-GeneID:53417 http://www.ncbi.nlm.nih.gov/gene/53417 NCBI-Rat-GeneID:64345 http://www.ncbi.nlm.nih.gov/gene/64345 HOIP:HOIP_1000186 HLADPB2 (mol) HOIP_1000186 HOIP:HOIP_1000188 NCBI-Human-GeneID:3157 NCBI-Mouse-GeneID:208715 NCBI-Rat-GeneID:29637 HMGCS1 (mol) HOIP_1000188 NCBI-Human-GeneID:3157 http://www.ncbi.nlm.nih.gov/gene/3157 NCBI-Mouse-GeneID:208715 http://www.ncbi.nlm.nih.gov/gene/208715 NCBI-Rat-GeneID:29637 http://www.ncbi.nlm.nih.gov/gene/29637 HOIP:HOIP_1000189 NCBI-Human-GeneID:3158 NCBI-Mouse-GeneID:15360 NCBI-Rat-GeneID:24450 PMID:11479731 PMID:19710929 PMID:27816970 HMGCS2 (mol) HOIP_1000189 NCBI-Human-GeneID:3158 http://www.ncbi.nlm.nih.gov/gene/3158 NCBI-Mouse-GeneID:15360 http://www.ncbi.nlm.nih.gov/gene/15360 NCBI-Rat-GeneID:24450 http://www.ncbi.nlm.nih.gov/gene/24450 PMID:19710929 One known target involved in FA metabolism is HMG-CoA synthetase 2 (HMGCS2), the rate-limiting step in ketogenesis. Upon activation, SIRT3 deacetylates and activates HMGCS2 to increase ketone body synthesis The importance of this regulation in hepatic and whole-body lipid metabolism has not been characterized; however, absence of HMGCS2 causes hypoketotic hypoglycemia and fatty liver in humans fed low-carbohydrate diets, suggesting that this enzyme plays a major role in FA disposal and linking FA catabolism to gluconeogenesis. PMID:27816970 HMGCS2 enhances invasion and metastasis via direct interaction with PPARα to activate Src signaling in colorectal cancer and oral cancer. HOIP:HOIP_1000190 NCBI-Human-GeneID:6782 NCBI-Mouse-GeneID:110920 NCBI-Rat-GeneID:29734 HSPA13 (mol) HOIP_1000190 NCBI-Human-GeneID:6782 http://www.ncbi.nlm.nih.gov/gene/6782 NCBI-Mouse-GeneID:110920 http://www.ncbi.nlm.nih.gov/gene/110920 NCBI-Rat-GeneID:29734 http://www.ncbi.nlm.nih.gov/gene/29734 HOIP:HOIP_1000191 NCBI-Human-GeneID:10525 NCBI-Mouse-GeneID:12282 NCBI-Rat-GeneID:192235 GRP170 HSP12A HYOU1 (mol) HOIP_1000191 NCBI-Human-GeneID:10525 http://www.ncbi.nlm.nih.gov/gene/10525 NCBI-Mouse-GeneID:12282 http://www.ncbi.nlm.nih.gov/gene/12282 NCBI-Rat-GeneID:192235 http://www.ncbi.nlm.nih.gov/gene/192235 HOIP:HOIP_1000192 NCBI-Human-GeneID:26061 NCBI-Mouse-GeneID:56794 NCBI-Rat-GeneID:85255 Hacl1 (mol) HOIP_1000192 NCBI-Human-GeneID:26061 http://www.ncbi.nlm.nih.gov/gene/26061 NCBI-Mouse-GeneID:56794 http://www.ncbi.nlm.nih.gov/gene/56794 NCBI-Rat-GeneID:85255 http://www.ncbi.nlm.nih.gov/gene/85255 HOIP:HOIP_1000193 NCBI-Human-GeneID:3032 NCBI-Mouse-GeneID:231086 NCBI-Rat-GeneID:171155 Hadhb (mol) HOIP_1000193 NCBI-Human-GeneID:3032 http://www.ncbi.nlm.nih.gov/gene/3032 NCBI-Mouse-GeneID:231086 http://www.ncbi.nlm.nih.gov/gene/231086 NCBI-Rat-GeneID:171155 http://www.ncbi.nlm.nih.gov/gene/171155 HOIP:HOIP_1000194 NCBI-Rat-GeneID:680403 Hist1h2bcl1 (mol) HOIP_1000194 NCBI-Rat-GeneID:680403 http://www.ncbi.nlm.nih.gov/gene/680403 HOIP:HOIP_1000195 NCBI-Human-GeneID:8337 NCBI-Rat-GeneID:365877 Hist2h2aa3 (mol) HOIP_1000195 NCBI-Human-GeneID:8337 http://www.ncbi.nlm.nih.gov/gene/8337 NCBI-Rat-GeneID:365877 http://www.ncbi.nlm.nih.gov/gene/365877 HOIP:HOIP_1000196 NCBI-Human-GeneID:3162 NCBI-Mouse-GeneID:15368 NCBI-Rat-GeneID:24451 Hmox1 (mol) HOIP_1000196 NCBI-Human-GeneID:3162 http://www.ncbi.nlm.nih.gov/gene/3162 NCBI-Mouse-GeneID:15368 http://www.ncbi.nlm.nih.gov/gene/15368 NCBI-Rat-GeneID:24451 http://www.ncbi.nlm.nih.gov/gene/24451 HOIP:HOIP_1000197 NCBI-Human-GeneID:3182 NCBI-Mouse-GeneID:15384 NCBI-Rat-GeneID:83498 Hnrnpab (mol) HOIP_1000197 NCBI-Human-GeneID:3182 http://www.ncbi.nlm.nih.gov/gene/3182 NCBI-Mouse-GeneID:15384 http://www.ncbi.nlm.nih.gov/gene/15384 NCBI-Rat-GeneID:83498 http://www.ncbi.nlm.nih.gov/gene/83498 HOIP:HOIP_1000198 NCBI-Human-GeneID:84263 NCBI-Mouse-GeneID:72479 NCBI-Rat-GeneID:313200 Hsdl2 (mol) HOIP_1000198 NCBI-Human-GeneID:84263 http://www.ncbi.nlm.nih.gov/gene/84263 NCBI-Mouse-GeneID:72479 http://www.ncbi.nlm.nih.gov/gene/72479 NCBI-Rat-GeneID:313200 http://www.ncbi.nlm.nih.gov/gene/313200 HOIP:HOIP_1000199 NCBI-Human-GeneID:10553 NCBI-Mouse-GeneID:53415 NCBI-Rat-GeneID:292935 Htatip2 (mol) HOIP_1000199 NCBI-Human-GeneID:10553 http://www.ncbi.nlm.nih.gov/gene/10553 NCBI-Mouse-GeneID:53415 http://www.ncbi.nlm.nih.gov/gene/53415 NCBI-Rat-GeneID:292935 http://www.ncbi.nlm.nih.gov/gene/292935 HOIP:HOIP_1000202 NCBI-Human-GeneID:3560 NCBI-Mouse-GeneID:16185 NCBI-Rat-GeneID:25746 IL2RB (mol) HOIP_1000202 NCBI-Human-GeneID:3560 http://www.ncbi.nlm.nih.gov/gene/3560 NCBI-Mouse-GeneID:16185 http://www.ncbi.nlm.nih.gov/gene/16185 NCBI-Rat-GeneID:25746 http://www.ncbi.nlm.nih.gov/gene/25746 HOIP:HOIP_1000203 NCBI-Human-GeneID:83729 NCBI-Mouse-GeneID:16326 NCBI-Rat-GeneID:83711 INHBE (mol) HOIP_1000203 NCBI-Human-GeneID:83729 http://www.ncbi.nlm.nih.gov/gene/83729 NCBI-Mouse-GeneID:16326 http://www.ncbi.nlm.nih.gov/gene/16326 NCBI-Rat-GeneID:83711 http://www.ncbi.nlm.nih.gov/gene/83711 HOIP:HOIP_1000204 NCBI-Human-GeneID:387755 NCBI-Mouse-GeneID:233752 NCBI-Rat-GeneID:293166 INSC (mol) HOIP_1000204 NCBI-Human-GeneID:387755 http://www.ncbi.nlm.nih.gov/gene/387755 NCBI-Mouse-GeneID:233752 http://www.ncbi.nlm.nih.gov/gene/233752 NCBI-Rat-GeneID:293166 http://www.ncbi.nlm.nih.gov/gene/293166 HOIP:HOIP_1000205 NCBI-Human-GeneID:26512 NCBI-Mouse-GeneID:18130 NCBI-Rat-GeneID:361057 INTS6 (mol) HOIP_1000205 NCBI-Human-GeneID:26512 http://www.ncbi.nlm.nih.gov/gene/26512 NCBI-Mouse-GeneID:18130 http://www.ncbi.nlm.nih.gov/gene/18130 NCBI-Rat-GeneID:361057 http://www.ncbi.nlm.nih.gov/gene/361057 HOIP:HOIP_1000206 NCBI-Human-GeneID:3688 NCBI-Mouse-GeneID:16412 NCBI-Rat-GeneID:24511 ITGB1 (mol) HOIP_1000206 NCBI-Human-GeneID:3688 http://www.ncbi.nlm.nih.gov/gene/3688 NCBI-Mouse-GeneID:16412 http://www.ncbi.nlm.nih.gov/gene/16412 NCBI-Rat-GeneID:24511 http://www.ncbi.nlm.nih.gov/gene/24511 HOIP:HOIP_1000207 NCBI-Human-GeneID:8870 NCBI-Mouse-GeneID:15937 NCBI-Rat-GeneID:294235 Ier3 (mol) HOIP_1000207 NCBI-Human-GeneID:8870 http://www.ncbi.nlm.nih.gov/gene/8870 NCBI-Mouse-GeneID:15937 http://www.ncbi.nlm.nih.gov/gene/15937 NCBI-Rat-GeneID:294235 http://www.ncbi.nlm.nih.gov/gene/294235 HOIP:HOIP_1000208 NCBI-Human-GeneID:3484 NCBI-Mouse-GeneID:16006 NCBI-Rat-GeneID:25685 http://purl.obolibrary.org/obo/IMR_0002689 IGFBP1 (mol) HOIP_1000208 NCBI-Human-GeneID:3484 http://www.ncbi.nlm.nih.gov/gene/3484 NCBI-Mouse-GeneID:16006 http://www.ncbi.nlm.nih.gov/gene/16006 NCBI-Rat-GeneID:25685 http://www.ncbi.nlm.nih.gov/gene/25685 HOIP:HOIP_1000209 NCBI-Human-GeneID:51147 NCBI-Mouse-GeneID:28019 NCBI-Rat-GeneID:297597 Ing4 (mol) HOIP_1000209 NCBI-Human-GeneID:51147 http://www.ncbi.nlm.nih.gov/gene/51147 NCBI-Mouse-GeneID:28019 http://www.ncbi.nlm.nih.gov/gene/28019 NCBI-Rat-GeneID:297597 http://www.ncbi.nlm.nih.gov/gene/297597 HOIP:HOIP_1000210 NCBI-Human-GeneID:3638 NCBI-Mouse-GeneID:231070 NCBI-Rat-GeneID:64194 Insig1 (mol) HOIP_1000210 NCBI-Human-GeneID:3638 http://www.ncbi.nlm.nih.gov/gene/3638 NCBI-Mouse-GeneID:231070 http://www.ncbi.nlm.nih.gov/gene/231070 NCBI-Rat-GeneID:64194 http://www.ncbi.nlm.nih.gov/gene/64194 HOIP:HOIP_1000211 NCBI-Human-GeneID:51141 NCBI-Mouse-GeneID:72999 NCBI-Rat-GeneID:288985 Insig2 (mol) HOIP_1000211 NCBI-Human-GeneID:51141 http://www.ncbi.nlm.nih.gov/gene/51141 NCBI-Mouse-GeneID:72999 http://www.ncbi.nlm.nih.gov/gene/72999 NCBI-Rat-GeneID:288985 http://www.ncbi.nlm.nih.gov/gene/288985 HOIP:HOIP_1000213 NCBI-Human-GeneID:51477 NCBI-Mouse-GeneID:71780 NCBI-Rat-GeneID:290651 Isyna1 (mol) HOIP_1000213 NCBI-Human-GeneID:51477 http://www.ncbi.nlm.nih.gov/gene/51477 NCBI-Mouse-GeneID:71780 http://www.ncbi.nlm.nih.gov/gene/71780 NCBI-Rat-GeneID:290651 http://www.ncbi.nlm.nih.gov/gene/290651 HOIP:HOIP_1000214 NCBI-Human-GeneID:23210 NCBI-Mouse-GeneID:107817 NCBI-Rat-GeneID:360665 JMJD6 (mol) HOIP_1000214 NCBI-Human-GeneID:23210 http://www.ncbi.nlm.nih.gov/gene/23210 NCBI-Mouse-GeneID:107817 http://www.ncbi.nlm.nih.gov/gene/107817 NCBI-Rat-GeneID:360665 http://www.ncbi.nlm.nih.gov/gene/360665 HOIP:HOIP_1000215 NCBI-Human-GeneID:133746 NCBI-Mouse-GeneID:57748 NCBI-Rat-GeneID:683593 JMY (mol) HOIP_1000215 NCBI-Human-GeneID:133746 http://www.ncbi.nlm.nih.gov/gene/133746 NCBI-Mouse-GeneID:57748 http://www.ncbi.nlm.nih.gov/gene/57748 NCBI-Rat-GeneID:683593 http://www.ncbi.nlm.nih.gov/gene/683593 HOIP:HOIP_1000216 NCBI-Human-GeneID:5599 NCBI-Mouse-GeneID:26419 NCBI-Rat-GeneID:116554 MAPK8 (mol) HOIP_1000216 NCBI-Human-GeneID:5599 http://www.ncbi.nlm.nih.gov/gene/5599 NCBI-Mouse-GeneID:26419 http://www.ncbi.nlm.nih.gov/gene/26419 NCBI-Rat-GeneID:116554 http://www.ncbi.nlm.nih.gov/gene/116554 HOIP:HOIP_1000217 NCBI-Human-GeneID:3833 NCBI-Mouse-GeneID:100502766 NCBI-Rat-GeneID:294286 KIFC1 (mol) HOIP_1000217 NCBI-Human-GeneID:3833 http://www.ncbi.nlm.nih.gov/gene/3833 NCBI-Mouse-GeneID:100502766 http://www.ncbi.nlm.nih.gov/gene/100502766 NCBI-Rat-GeneID:294286 http://www.ncbi.nlm.nih.gov/gene/294286 HOIP:HOIP_1000218 NCBI-Human-GeneID:11014 NCBI-Mouse-GeneID:66913 NCBI-Rat-GeneID:304290 Kdelr2 (mol) HOIP_1000218 NCBI-Human-GeneID:11014 http://www.ncbi.nlm.nih.gov/gene/11014 NCBI-Mouse-GeneID:66913 http://www.ncbi.nlm.nih.gov/gene/66913 NCBI-Rat-GeneID:304290 http://www.ncbi.nlm.nih.gov/gene/304290 HOIP:HOIP_1000219 NCBI-Human-GeneID:1316 NCBI-Mouse-GeneID:23849 NCBI-Rat-GeneID:58954 Klf6 (mol) HOIP_1000219 NCBI-Human-GeneID:1316 http://www.ncbi.nlm.nih.gov/gene/1316 NCBI-Mouse-GeneID:23849 http://www.ncbi.nlm.nih.gov/gene/23849 NCBI-Rat-GeneID:58954 http://www.ncbi.nlm.nih.gov/gene/58954 HOIP:HOIP_1000220 NCBI-Human-GeneID:112849 NCBI-Mouse-GeneID:67217 NCBI-Rat-GeneID:314214 L3hypdh (mol) HOIP_1000220 NCBI-Human-GeneID:112849 http://www.ncbi.nlm.nih.gov/gene/112849 NCBI-Mouse-GeneID:67217 http://www.ncbi.nlm.nih.gov/gene/67217 NCBI-Rat-GeneID:314214 http://www.ncbi.nlm.nih.gov/gene/314214 HOIP:HOIP_1000221 NCBI-Human-GeneID:116842 NCBI-Mouse-GeneID:259301 NCBI-Rat-GeneID:497901 LEAP2 (mol) HOIP_1000221 NCBI-Human-GeneID:116842 http://www.ncbi.nlm.nih.gov/gene/116842 NCBI-Mouse-GeneID:259301 http://www.ncbi.nlm.nih.gov/gene/259301 NCBI-Rat-GeneID:497901 http://www.ncbi.nlm.nih.gov/gene/497901 HOIP:HOIP_1000222 NCBI-Human-GeneID:93273 NCBI-Mouse-GeneID:213409 NCBI-Rat-GeneID:100360142 LEMD1 (mol) HOIP_1000222 NCBI-Human-GeneID:93273 http://www.ncbi.nlm.nih.gov/gene/93273 NCBI-Mouse-GeneID:213409 http://www.ncbi.nlm.nih.gov/gene/213409 NCBI-Rat-GeneID:100360142 http://www.ncbi.nlm.nih.gov/gene/100360142 HOIP:HOIP_1000224 NCBI-Human-GeneID:150759 LINC00342 (mol) HOIP_1000224 NCBI-Human-GeneID:150759 http://www.ncbi.nlm.nih.gov/gene/150759 HOIP:HOIP_1000225 NCBI-Human-GeneID:64327 NCBI-Mouse-GeneID:56873 NCBI-Rat-GeneID:362295 LMBR1 (mol) HOIP_1000225 NCBI-Human-GeneID:64327 http://www.ncbi.nlm.nih.gov/gene/64327 NCBI-Mouse-GeneID:56873 http://www.ncbi.nlm.nih.gov/gene/56873 NCBI-Rat-GeneID:362295 http://www.ncbi.nlm.nih.gov/gene/362295 HOIP:HOIP_1000227 NCBI-Human-GeneID:2494 NCBI-Mouse-GeneID:26424 NCBI-Rat-GeneID:60349 NR5A2 (mol) HOIP_1000227 NCBI-Human-GeneID:2494 http://www.ncbi.nlm.nih.gov/gene/2494 NCBI-Mouse-GeneID:26424 http://www.ncbi.nlm.nih.gov/gene/26424 NCBI-Rat-GeneID:60349 http://www.ncbi.nlm.nih.gov/gene/60349 HOIP:HOIP_1000228 NCBI-Human-GeneID:4047 NCBI-Mouse-GeneID:16987 NCBI-Rat-GeneID:81681 LSS (mol) HOIP_1000228 NCBI-Human-GeneID:4047 http://www.ncbi.nlm.nih.gov/gene/4047 NCBI-Mouse-GeneID:16987 http://www.ncbi.nlm.nih.gov/gene/16987 NCBI-Rat-GeneID:81681 http://www.ncbi.nlm.nih.gov/gene/81681 HOIP:HOIP_1000229 NCBI-Human-GeneID:10542 NCBI-Mouse-GeneID:68576 NCBI-Rat-GeneID:295357 Lamtor5 (mol) HOIP_1000229 NCBI-Human-GeneID:10542 http://www.ncbi.nlm.nih.gov/gene/10542 NCBI-Mouse-GeneID:68576 http://www.ncbi.nlm.nih.gov/gene/68576 NCBI-Rat-GeneID:295357 http://www.ncbi.nlm.nih.gov/gene/295357 HOIP:HOIP_1000231 NCBI-Human-GeneID:9926 NCBI-Mouse-GeneID:226856 NCBI-Rat-GeneID:679692 Lpgat1 (mol) HOIP_1000231 NCBI-Human-GeneID:9926 http://www.ncbi.nlm.nih.gov/gene/9926 NCBI-Mouse-GeneID:226856 http://www.ncbi.nlm.nih.gov/gene/226856 NCBI-Rat-GeneID:679692 http://www.ncbi.nlm.nih.gov/gene/679692 HOIP:HOIP_1000232 NCBI-Human-GeneID:10586 NCBI-Mouse-GeneID:23937 NCBI-Rat-GeneID:680102 MAB21L2 (mol) HOIP_1000232 NCBI-Human-GeneID:10586 http://www.ncbi.nlm.nih.gov/gene/10586 NCBI-Mouse-GeneID:23937 http://www.ncbi.nlm.nih.gov/gene/23937 NCBI-Rat-GeneID:680102 http://www.ncbi.nlm.nih.gov/gene/680102 HOIP:HOIP_1000233 NCBI-Human-GeneID:7873 NCBI-Mouse-GeneID:74840 NCBI-Rat-GeneID:315989 MANF (mol) HOIP_1000233 NCBI-Human-GeneID:7873 http://www.ncbi.nlm.nih.gov/gene/7873 NCBI-Mouse-GeneID:74840 http://www.ncbi.nlm.nih.gov/gene/74840 NCBI-Rat-GeneID:315989 http://www.ncbi.nlm.nih.gov/gene/315989 HOIP:HOIP_1000234 NCBI-Human-GeneID:5608 NCBI-Mouse-GeneID:26399 NCBI-Rat-GeneID:114495 MAP2K6 (mol) HOIP_1000234 NCBI-Human-GeneID:5608 http://www.ncbi.nlm.nih.gov/gene/5608 NCBI-Mouse-GeneID:26399 http://www.ncbi.nlm.nih.gov/gene/26399 NCBI-Rat-GeneID:114495 http://www.ncbi.nlm.nih.gov/gene/114495 HOIP:HOIP_1000235 NCBI-Human-GeneID:9175 NCBI-Mouse-GeneID:71751 NCBI-Rat-GeneID:303823 MAP3K13 (mol) HOIP_1000235 NCBI-Human-GeneID:9175 http://www.ncbi.nlm.nih.gov/gene/9175 NCBI-Mouse-GeneID:71751 http://www.ncbi.nlm.nih.gov/gene/71751 NCBI-Rat-GeneID:303823 http://www.ncbi.nlm.nih.gov/gene/303823 HOIP:HOIP_1000236 NCBI-Human-GeneID:9439 NCBI-Mouse-GeneID:70208 NCBI-Rat-GeneID:309565 MED23 (mol) HOIP_1000236 NCBI-Human-GeneID:9439 http://www.ncbi.nlm.nih.gov/gene/9439 NCBI-Mouse-GeneID:70208 http://www.ncbi.nlm.nih.gov/gene/70208 NCBI-Rat-GeneID:309565 http://www.ncbi.nlm.nih.gov/gene/309565 HOIP:HOIP_1000238 NCBI-Human-GeneID:4313 NCBI-Mouse-GeneID:17390 NCBI-Rat-GeneID:81686 MMP2 (mol) HOIP_1000238 NCBI-Human-GeneID:4313 http://www.ncbi.nlm.nih.gov/gene/4313 NCBI-Mouse-GeneID:17390 http://www.ncbi.nlm.nih.gov/gene/17390 NCBI-Rat-GeneID:81686 http://www.ncbi.nlm.nih.gov/gene/81686 HOIP:HOIP_1000240 NCBI-Human-GeneID:4074 NCBI-Mouse-GeneID:17113 NCBI-Rat-GeneID:312689 M6PR (mol) HOIP_1000240 NCBI-Human-GeneID:4074 http://www.ncbi.nlm.nih.gov/gene/4074 NCBI-Mouse-GeneID:17113 http://www.ncbi.nlm.nih.gov/gene/17113 NCBI-Rat-GeneID:312689 http://www.ncbi.nlm.nih.gov/gene/312689 HOIP:HOIP_1000241 NCBI-Human-GeneID:2206 NCBI-Mouse-GeneID:14126 NCBI-Rat-GeneID:25316 MS4A2 (mol) HOIP_1000241 NCBI-Human-GeneID:2206 http://www.ncbi.nlm.nih.gov/gene/2206 NCBI-Mouse-GeneID:14126 http://www.ncbi.nlm.nih.gov/gene/14126 NCBI-Rat-GeneID:25316 http://www.ncbi.nlm.nih.gov/gene/25316 HOIP:HOIP_1000242 NCBI-Mouse-GeneID:666339 NCBI-Rat-GeneID:687030 MUC3 (mol) HOIP_1000242 NCBI-Mouse-GeneID:666339 http://www.ncbi.nlm.nih.gov/gene/666339 NCBI-Rat-GeneID:687030 http://www.ncbi.nlm.nih.gov/gene/687030 HOIP:HOIP_1000243 NCBI-Human-GeneID:4613 NCBI-Mouse-GeneID:18109 NCBI-Rat-GeneID:298894 MYCN (mol) HOIP_1000243 NCBI-Human-GeneID:4613 http://www.ncbi.nlm.nih.gov/gene/4613 NCBI-Mouse-GeneID:18109 http://www.ncbi.nlm.nih.gov/gene/18109 NCBI-Rat-GeneID:298894 http://www.ncbi.nlm.nih.gov/gene/298894 HOIP:HOIP_1000244 NCBI-Human-GeneID:4199 NCBI-Mouse-GeneID:17436 NCBI-Rat-GeneID:24552 Me1 (mol) HOIP_1000244 NCBI-Human-GeneID:4199 http://www.ncbi.nlm.nih.gov/gene/4199 NCBI-Mouse-GeneID:17436 http://www.ncbi.nlm.nih.gov/gene/17436 NCBI-Rat-GeneID:24552 http://www.ncbi.nlm.nih.gov/gene/24552 HOIP:HOIP_1000245 NCBI-Human-GeneID:11343 NCBI-Mouse-GeneID:23945 NCBI-Rat-GeneID:29254 Mgll (mol) HOIP_1000245 NCBI-Human-GeneID:11343 http://www.ncbi.nlm.nih.gov/gene/11343 NCBI-Mouse-GeneID:23945 http://www.ncbi.nlm.nih.gov/gene/23945 NCBI-Rat-GeneID:29254 http://www.ncbi.nlm.nih.gov/gene/29254 HOIP:HOIP_1000246 NCBI-Human-GeneID:4605 NCBI-Mouse-GeneID:17865 NCBI-Rat-GeneID:296344 Mybl2 (mol) HOIP_1000246 NCBI-Human-GeneID:4605 http://www.ncbi.nlm.nih.gov/gene/4605 NCBI-Mouse-GeneID:17865 http://www.ncbi.nlm.nih.gov/gene/17865 NCBI-Rat-GeneID:296344 http://www.ncbi.nlm.nih.gov/gene/296344 HOIP:HOIP_1000248 NCBI-Human-GeneID:4673 NCBI-Mouse-GeneID:53605 NCBI-Rat-GeneID:89825 NAP1L1 (mol) HOIP_1000248 NCBI-Human-GeneID:4673 http://www.ncbi.nlm.nih.gov/gene/4673 NCBI-Mouse-GeneID:53605 http://www.ncbi.nlm.nih.gov/gene/53605 NCBI-Rat-GeneID:89825 http://www.ncbi.nlm.nih.gov/gene/89825 HOIP:HOIP_1000249 NCBI-Human-GeneID:51594 NCBI-Mouse-GeneID:71169 NCBI-Rat-GeneID:690073 NBAS (mol) HOIP_1000249 NCBI-Human-GeneID:51594 http://www.ncbi.nlm.nih.gov/gene/51594 NCBI-Mouse-GeneID:71169 http://www.ncbi.nlm.nih.gov/gene/71169 NCBI-Rat-GeneID:690073 http://www.ncbi.nlm.nih.gov/gene/690073 HOIP:HOIP_1000250 NCBI-Human-GeneID:4747 NCBI-Mouse-GeneID:18039 NCBI-Rat-GeneID:83613 NEFL (mol) HOIP_1000250 NCBI-Human-GeneID:4747 http://www.ncbi.nlm.nih.gov/gene/4747 NCBI-Mouse-GeneID:18039 http://www.ncbi.nlm.nih.gov/gene/18039 NCBI-Rat-GeneID:83613 http://www.ncbi.nlm.nih.gov/gene/83613 HOIP:HOIP_1000252 NCBI-Human-GeneID:22861 NLRP1 (mol) HOIP_1000252 NCBI-Human-GeneID:22861 http://www.ncbi.nlm.nih.gov/gene/22861 HOIP:HOIP_1000253 NCBI-Human-GeneID:4830 NCBI-Mouse-GeneID:18102 NCBI-Rat-GeneID:191575 NME1 (mol) HOIP_1000253 NCBI-Human-GeneID:4830 http://www.ncbi.nlm.nih.gov/gene/4830 NCBI-Mouse-GeneID:18102 http://www.ncbi.nlm.nih.gov/gene/18102 NCBI-Rat-GeneID:191575 http://www.ncbi.nlm.nih.gov/gene/191575 HOIP:HOIP_1000254 NCBI-Human-GeneID:4925 NCBI-Mouse-GeneID:53322 NCBI-Rat-GeneID:59295 NUCB2 (mol) HOIP_1000254 NCBI-Human-GeneID:4925 http://www.ncbi.nlm.nih.gov/gene/4925 NCBI-Mouse-GeneID:53322 http://www.ncbi.nlm.nih.gov/gene/53322 NCBI-Rat-GeneID:59295 http://www.ncbi.nlm.nih.gov/gene/59295 HOIP:HOIP_1000255 NCBI-Human-GeneID:11163 NCBI-Mouse-GeneID:71207 NCBI-Rat-GeneID:94267 NUDT4 (mol) HOIP_1000255 NCBI-Human-GeneID:11163 http://www.ncbi.nlm.nih.gov/gene/11163 NCBI-Mouse-GeneID:71207 http://www.ncbi.nlm.nih.gov/gene/71207 NCBI-Rat-GeneID:94267 http://www.ncbi.nlm.nih.gov/gene/94267 HOIP:HOIP_1000256 NCBI-Human-GeneID:29078 NCBI-Mouse-GeneID:68493 NCBI-Rat-GeneID:362495 Ndufaf4 (mol) HOIP_1000256 NCBI-Human-GeneID:29078 http://www.ncbi.nlm.nih.gov/gene/29078 NCBI-Mouse-GeneID:68493 http://www.ncbi.nlm.nih.gov/gene/68493 NCBI-Rat-GeneID:362495 http://www.ncbi.nlm.nih.gov/gene/362495 HOIP:HOIP_1000259 NCBI-Human-GeneID:64332 NCBI-Mouse-GeneID:80859 NCBI-Rat-GeneID:304005 Nfkbiz (mol) HOIP_1000259 NCBI-Human-GeneID:64332 http://www.ncbi.nlm.nih.gov/gene/64332 NCBI-Mouse-GeneID:80859 http://www.ncbi.nlm.nih.gov/gene/80859 NCBI-Rat-GeneID:304005 http://www.ncbi.nlm.nih.gov/gene/304005 HOIP:HOIP_1000260 Nifib (mol) HOIP_1000260 HOIP:HOIP_1000261 NCBI-Human-GeneID:9221 NCBI-Mouse-GeneID:70769 NCBI-Rat-GeneID:64896 Nolc1 (mol) HOIP_1000261 NCBI-Human-GeneID:9221 http://www.ncbi.nlm.nih.gov/gene/9221 NCBI-Mouse-GeneID:70769 http://www.ncbi.nlm.nih.gov/gene/70769 NCBI-Rat-GeneID:64896 http://www.ncbi.nlm.nih.gov/gene/64896 HOIP:HOIP_1000262 NCBI-Human-GeneID:1728 NCBI-Mouse-GeneID:18104 NCBI-Rat-GeneID:24314 Nqo1 (mol) HOIP_1000262 NCBI-Human-GeneID:1728 http://www.ncbi.nlm.nih.gov/gene/1728 NCBI-Mouse-GeneID:18104 http://www.ncbi.nlm.nih.gov/gene/18104 NCBI-Rat-GeneID:24314 http://www.ncbi.nlm.nih.gov/gene/24314 HOIP:HOIP_1000263 NCBI-Human-GeneID:7376 NCBI-Mouse-GeneID:22260 NCBI-Rat-GeneID:58851 Nr1h2 (mol) HOIP_1000263 NCBI-Human-GeneID:7376 http://www.ncbi.nlm.nih.gov/gene/7376 NCBI-Mouse-GeneID:22260 http://www.ncbi.nlm.nih.gov/gene/22260 NCBI-Rat-GeneID:58851 http://www.ncbi.nlm.nih.gov/gene/58851 HOIP:HOIP_1000264 NCBI-Human-GeneID:3084 NCBI-Mouse-GeneID:211323 NCBI-Rat-GeneID:112400 Nrg1 (mol) HOIP_1000264 NCBI-Human-GeneID:3084 http://www.ncbi.nlm.nih.gov/gene/3084 NCBI-Mouse-GeneID:211323 http://www.ncbi.nlm.nih.gov/gene/211323 NCBI-Rat-GeneID:112400 http://www.ncbi.nlm.nih.gov/gene/112400 HOIP:HOIP_1000265 NCBI-Human-GeneID:55190 NCBI-Mouse-GeneID:58242 NCBI-Rat-GeneID:680248 Nudt11 (mol) HOIP_1000265 NCBI-Human-GeneID:55190 http://www.ncbi.nlm.nih.gov/gene/55190 NCBI-Mouse-GeneID:58242 http://www.ncbi.nlm.nih.gov/gene/58242 NCBI-Rat-GeneID:680248 http://www.ncbi.nlm.nih.gov/gene/680248 HOIP:HOIP_1000266 NCBI-Human-GeneID:11164 NCBI-Mouse-GeneID:53893 NCBI-Rat-GeneID:361274 Nudt5 (mol) HOIP_1000266 NCBI-Human-GeneID:11164 http://www.ncbi.nlm.nih.gov/gene/11164 NCBI-Mouse-GeneID:53893 http://www.ncbi.nlm.nih.gov/gene/53893 NCBI-Rat-GeneID:361274 http://www.ncbi.nlm.nih.gov/gene/361274 HOIP:HOIP_1000267 NCBI-Human-GeneID:283927 NCBI-Mouse-GeneID:67528 NCBI-Rat-GeneID:361413 Nudt7 (mol) HOIP_1000267 NCBI-Human-GeneID:283927 http://www.ncbi.nlm.nih.gov/gene/283927 NCBI-Mouse-GeneID:67528 http://www.ncbi.nlm.nih.gov/gene/67528 NCBI-Rat-GeneID:361413 http://www.ncbi.nlm.nih.gov/gene/361413 HOIP:HOIP_1000268 NCBI-Human-GeneID:9972 NCBI-Mouse-GeneID:218210 NCBI-Rat-GeneID:25281 Nup153 (mol) HOIP_1000268 NCBI-Human-GeneID:9972 http://www.ncbi.nlm.nih.gov/gene/9972 NCBI-Mouse-GeneID:218210 http://www.ncbi.nlm.nih.gov/gene/218210 NCBI-Rat-GeneID:25281 http://www.ncbi.nlm.nih.gov/gene/25281 HOIP:HOIP_1000269 NCBI-Human-GeneID:116150 NCBI-Mouse-GeneID:52014 NCBI-Rat-GeneID:294400 Nus1 (mol) HOIP_1000269 NCBI-Human-GeneID:116150 http://www.ncbi.nlm.nih.gov/gene/116150 NCBI-Mouse-GeneID:52014 http://www.ncbi.nlm.nih.gov/gene/52014 NCBI-Rat-GeneID:294400 http://www.ncbi.nlm.nih.gov/gene/294400 HOIP:HOIP_1000270 OATPs family HOIP_1000270 HOIP:HOIP_1000271 OCT family (mol) HOIP_1000271 HOIP:HOIP_1000272 NCBI-Human-GeneID:29948 NCBI-Mouse-GeneID:71839 NCBI-Rat-GeneID:171493 Osgin1 (mol) HOIP_1000272 NCBI-Human-GeneID:29948 http://www.ncbi.nlm.nih.gov/gene/29948 NCBI-Mouse-GeneID:71839 http://www.ncbi.nlm.nih.gov/gene/71839 NCBI-Rat-GeneID:171493 http://www.ncbi.nlm.nih.gov/gene/171493 HOIP:HOIP_1000273 NCBI-Human-GeneID:5101 NCBI-Mouse-GeneID:211712 NCBI-Rat-GeneID:306091 PCDH9 (mol) HOIP_1000273 NCBI-Human-GeneID:5101 http://www.ncbi.nlm.nih.gov/gene/5101 NCBI-Mouse-GeneID:211712 http://www.ncbi.nlm.nih.gov/gene/211712 NCBI-Rat-GeneID:306091 http://www.ncbi.nlm.nih.gov/gene/306091 HOIP:HOIP_1000274 NCBI-Human-GeneID:5106 NCBI-Mouse-GeneID:74551 NCBI-Rat-GeneID:361042 PCK2 (mol) HOIP_1000274 NCBI-Human-GeneID:5106 http://www.ncbi.nlm.nih.gov/gene/5106 NCBI-Mouse-GeneID:74551 http://www.ncbi.nlm.nih.gov/gene/74551 NCBI-Rat-GeneID:361042 http://www.ncbi.nlm.nih.gov/gene/361042 HOIP:HOIP_1000275 PDGF (mol) HOIP_1000275 HOIP:HOIP_1000276 NCBI-Human-GeneID:5034 NCBI-Mouse-GeneID:18453 NCBI-Rat-GeneID:25506 P4HB (mol) HOIP_1000276 NCBI-Human-GeneID:5034 http://www.ncbi.nlm.nih.gov/gene/5034 NCBI-Mouse-GeneID:18453 http://www.ncbi.nlm.nih.gov/gene/18453 NCBI-Rat-GeneID:25506 http://www.ncbi.nlm.nih.gov/gene/25506 HOIP:HOIP_1000277 NCBI-Human-GeneID:10611 NCBI-Mouse-GeneID:56376 NCBI-Rat-GeneID:64353 PDLIM5 (mol) HOIP_1000277 NCBI-Human-GeneID:10611 http://www.ncbi.nlm.nih.gov/gene/10611 NCBI-Mouse-GeneID:56376 http://www.ncbi.nlm.nih.gov/gene/56376 NCBI-Rat-GeneID:64353 http://www.ncbi.nlm.nih.gov/gene/64353 HOIP:HOIP_1000278 NCBI-Human-GeneID:8800 NCBI-Mouse-GeneID:18631 NCBI-Rat-GeneID:85249 PEX11a (mol) HOIP_1000278 NCBI-Human-GeneID:8800 http://www.ncbi.nlm.nih.gov/gene/8800 NCBI-Mouse-GeneID:18631 http://www.ncbi.nlm.nih.gov/gene/18631 NCBI-Rat-GeneID:85249 http://www.ncbi.nlm.nih.gov/gene/85249 HOIP:HOIP_1000279 NCBI-Human-GeneID:5308 NCBI-Mouse-GeneID:18741 NCBI-Rat-GeneID:54284 PITX2 (mol) HOIP_1000279 NCBI-Human-GeneID:5308 http://www.ncbi.nlm.nih.gov/gene/5308 NCBI-Mouse-GeneID:18741 http://www.ncbi.nlm.nih.gov/gene/18741 NCBI-Rat-GeneID:54284 http://www.ncbi.nlm.nih.gov/gene/54284 HOIP:HOIP_1000280 NCBI-Human-GeneID:112476 NCBI-Mouse-GeneID:69017 NCBI-Rat-GeneID:361651 PRRT2 (mol) HOIP_1000280 NCBI-Human-GeneID:112476 http://www.ncbi.nlm.nih.gov/gene/112476 NCBI-Mouse-GeneID:69017 http://www.ncbi.nlm.nih.gov/gene/69017 NCBI-Rat-GeneID:361651 http://www.ncbi.nlm.nih.gov/gene/361651 HOIP:HOIP_1000281 NCBI-Human-GeneID:23659 NCBI-Mouse-GeneID:192654 NCBI-Rat-GeneID:361401 PLA2G15 (mol) HOIP_1000281 NCBI-Human-GeneID:23659 http://www.ncbi.nlm.nih.gov/gene/23659 NCBI-Mouse-GeneID:192654 http://www.ncbi.nlm.nih.gov/gene/192654 NCBI-Rat-GeneID:361401 http://www.ncbi.nlm.nih.gov/gene/361401 HOIP:HOIP_1000282 NCBI-Mouse-GeneID:225845 NCBI-Rat-GeneID:24913 PLA2G16 (mol) HOIP_1000282 NCBI-Mouse-GeneID:225845 http://www.ncbi.nlm.nih.gov/gene/225845 NCBI-Rat-GeneID:24913 http://www.ncbi.nlm.nih.gov/gene/24913 HOIP:HOIP_1000283 NCBI-Human-GeneID:5322 NCBI-Mouse-GeneID:18784 NCBI-Rat-GeneID:29354 PLA2G5 (mol) HOIP_1000283 NCBI-Human-GeneID:5322 http://www.ncbi.nlm.nih.gov/gene/5322 NCBI-Mouse-GeneID:18784 http://www.ncbi.nlm.nih.gov/gene/18784 NCBI-Rat-GeneID:29354 http://www.ncbi.nlm.nih.gov/gene/29354 HOIP:HOIP_1000284 NCBI-Human-GeneID:151056 NCBI-Mouse-GeneID:665270 NCBI-Rat-GeneID:192259 PLB1 (mol) HOIP_1000284 NCBI-Human-GeneID:151056 http://www.ncbi.nlm.nih.gov/gene/151056 NCBI-Mouse-GeneID:665270 http://www.ncbi.nlm.nih.gov/gene/665270 NCBI-Rat-GeneID:192259 http://www.ncbi.nlm.nih.gov/gene/192259 HOIP:HOIP_1000285 NCBI-Human-GeneID:122618 NCBI-Mouse-GeneID:104759 NCBI-Rat-GeneID:362792 PLD4 (mol) HOIP_1000285 NCBI-Human-GeneID:122618 http://www.ncbi.nlm.nih.gov/gene/122618 NCBI-Mouse-GeneID:104759 http://www.ncbi.nlm.nih.gov/gene/104759 NCBI-Rat-GeneID:362792 http://www.ncbi.nlm.nih.gov/gene/362792 HOIP:HOIP_1000286 NCBI-Human-GeneID:123 NCBI-Mouse-GeneID:11520 NCBI-Rat-GeneID:298199 PLIN2 (mol) HOIP_1000286 NCBI-Human-GeneID:123 http://www.ncbi.nlm.nih.gov/gene/123 NCBI-Mouse-GeneID:11520 http://www.ncbi.nlm.nih.gov/gene/11520 NCBI-Rat-GeneID:298199 http://www.ncbi.nlm.nih.gov/gene/298199 HOIP:HOIP_1000287 NCBI-Human-GeneID:10769 NCBI-Mouse-GeneID:20620 NCBI-Rat-GeneID:83722 PLK2 (mol) HOIP_1000287 NCBI-Human-GeneID:10769 http://www.ncbi.nlm.nih.gov/gene/10769 NCBI-Mouse-GeneID:20620 http://www.ncbi.nlm.nih.gov/gene/20620 NCBI-Rat-GeneID:83722 http://www.ncbi.nlm.nih.gov/gene/83722 HOIP:HOIP_1000288 NCBI-Human-GeneID:5463 NCBI-Mouse-GeneID:19009 NCBI-Rat-GeneID:116545 POU6F1 (mol) HOIP_1000288 NCBI-Human-GeneID:5463 http://www.ncbi.nlm.nih.gov/gene/5463 NCBI-Mouse-GeneID:19009 http://www.ncbi.nlm.nih.gov/gene/19009 NCBI-Rat-GeneID:116545 http://www.ncbi.nlm.nih.gov/gene/116545 HOIP:HOIP_1000289 NCBI-Human-GeneID:22843 NCBI-Mouse-GeneID:320472 NCBI-Rat-GeneID:360593 PPM1E (mol) HOIP_1000289 NCBI-Human-GeneID:22843 http://www.ncbi.nlm.nih.gov/gene/22843 NCBI-Mouse-GeneID:320472 http://www.ncbi.nlm.nih.gov/gene/320472 NCBI-Rat-GeneID:360593 http://www.ncbi.nlm.nih.gov/gene/360593 HOIP:HOIP_1000290 NCBI-Human-GeneID:639 NCBI-Mouse-GeneID:12142 NCBI-Rat-GeneID:309871 PRDM1 (mol) HOIP_1000290 NCBI-Human-GeneID:639 http://www.ncbi.nlm.nih.gov/gene/639 NCBI-Mouse-GeneID:12142 http://www.ncbi.nlm.nih.gov/gene/12142 NCBI-Rat-GeneID:309871 http://www.ncbi.nlm.nih.gov/gene/309871 HOIP:HOIP_1000292 NCBI-Human-GeneID:5734 NCBI-Mouse-GeneID:19219 NCBI-Rat-GeneID:84023 PTGER4 (mol) HOIP_1000292 NCBI-Human-GeneID:5734 http://www.ncbi.nlm.nih.gov/gene/5734 NCBI-Mouse-GeneID:19219 http://www.ncbi.nlm.nih.gov/gene/19219 NCBI-Rat-GeneID:84023 http://www.ncbi.nlm.nih.gov/gene/84023 HOIP:HOIP_1000293 NCBI-Human-GeneID:5775 NCBI-Mouse-GeneID:19258 NCBI-Rat-GeneID:246116 PTPN4 (mol) HOIP_1000293 NCBI-Human-GeneID:5775 http://www.ncbi.nlm.nih.gov/gene/5775 NCBI-Mouse-GeneID:19258 http://www.ncbi.nlm.nih.gov/gene/19258 NCBI-Rat-GeneID:246116 http://www.ncbi.nlm.nih.gov/gene/246116 HOIP:HOIP_1000294 NCBI-Human-GeneID:53354 NCBI-Mouse-GeneID:75735 NCBI-Rat-GeneID:294088 Pank1 (mol) HOIP_1000294 NCBI-Human-GeneID:53354 http://www.ncbi.nlm.nih.gov/gene/53354 NCBI-Mouse-GeneID:75735 http://www.ncbi.nlm.nih.gov/gene/75735 NCBI-Rat-GeneID:294088 http://www.ncbi.nlm.nih.gov/gene/294088 HOIP:HOIP_1000295 NCBI-Human-GeneID:5095 NCBI-Mouse-GeneID:110821 NCBI-Rat-GeneID:687008 Pcca (mol) HOIP_1000295 NCBI-Human-GeneID:5095 http://www.ncbi.nlm.nih.gov/gene/5095 NCBI-Mouse-GeneID:110821 http://www.ncbi.nlm.nih.gov/gene/110821 NCBI-Rat-GeneID:687008 http://www.ncbi.nlm.nih.gov/gene/687008 HOIP:HOIP_1000296 NCBI-Human-GeneID:9159 NCBI-Mouse-GeneID:18554 NCBI-Rat-GeneID:29606 Pcsk7 (mol) HOIP_1000296 NCBI-Human-GeneID:9159 http://www.ncbi.nlm.nih.gov/gene/9159 NCBI-Mouse-GeneID:18554 http://www.ncbi.nlm.nih.gov/gene/18554 NCBI-Rat-GeneID:29606 http://www.ncbi.nlm.nih.gov/gene/29606 HOIP:HOIP_1000297 NCBI-Human-GeneID:5138 NCBI-Mouse-GeneID:207728 NCBI-Rat-GeneID:81743 Pde2A (mol) HOIP_1000297 NCBI-Human-GeneID:5138 http://www.ncbi.nlm.nih.gov/gene/5138 NCBI-Mouse-GeneID:207728 http://www.ncbi.nlm.nih.gov/gene/207728 NCBI-Rat-GeneID:81743 http://www.ncbi.nlm.nih.gov/gene/81743 HOIP:HOIP_1000298 NCBI-Human-GeneID:5166 NCBI-Mouse-GeneID:27273 NCBI-Rat-GeneID:89813 Pdk4 (mol) HOIP_1000298 NCBI-Human-GeneID:5166 http://www.ncbi.nlm.nih.gov/gene/5166 NCBI-Mouse-GeneID:27273 http://www.ncbi.nlm.nih.gov/gene/27273 NCBI-Rat-GeneID:89813 http://www.ncbi.nlm.nih.gov/gene/89813 HOIP:HOIP_1000300 NCBI-Human-GeneID:5824 NCBI-Mouse-GeneID:19298 NCBI-Rat-GeneID:289233 Pex19 (mol) HOIP_1000300 NCBI-Human-GeneID:5824 http://www.ncbi.nlm.nih.gov/gene/5824 NCBI-Mouse-GeneID:19298 http://www.ncbi.nlm.nih.gov/gene/19298 NCBI-Rat-GeneID:289233 http://www.ncbi.nlm.nih.gov/gene/289233 HOIP:HOIP_1000301 NCBI-Human-GeneID:10401 NCBI-Mouse-GeneID:229615 NCBI-Rat-GeneID:83614 Pias3 (mol) HOIP_1000301 NCBI-Human-GeneID:10401 http://www.ncbi.nlm.nih.gov/gene/10401 NCBI-Mouse-GeneID:229615 http://www.ncbi.nlm.nih.gov/gene/229615 NCBI-Rat-GeneID:83614 http://www.ncbi.nlm.nih.gov/gene/83614 HOIP:HOIP_1000302 NCBI-Human-GeneID:80235 NCBI-Mouse-GeneID:239827 NCBI-Rat-GeneID:303872 Pigz (mol) HOIP_1000302 NCBI-Human-GeneID:80235 http://www.ncbi.nlm.nih.gov/gene/80235 NCBI-Mouse-GeneID:239827 http://www.ncbi.nlm.nih.gov/gene/239827 NCBI-Rat-GeneID:303872 http://www.ncbi.nlm.nih.gov/gene/303872 HOIP:HOIP_1000303 NCBI-Human-GeneID:5288 NCBI-Mouse-GeneID:18705 NCBI-Rat-GeneID:116720 Pik3c2g (mol) HOIP_1000303 NCBI-Human-GeneID:5288 http://www.ncbi.nlm.nih.gov/gene/5288 NCBI-Mouse-GeneID:18705 http://www.ncbi.nlm.nih.gov/gene/18705 NCBI-Rat-GeneID:116720 http://www.ncbi.nlm.nih.gov/gene/116720 HOIP:HOIP_1000304 NCBI-Human-GeneID:8544 NCBI-Mouse-GeneID:69656 NCBI-Rat-GeneID:363465 Pir (mol) HOIP_1000304 NCBI-Human-GeneID:8544 http://www.ncbi.nlm.nih.gov/gene/8544 NCBI-Mouse-GeneID:69656 http://www.ncbi.nlm.nih.gov/gene/69656 NCBI-Rat-GeneID:363465 http://www.ncbi.nlm.nih.gov/gene/363465 HOIP:HOIP_1000305 NCBI-Human-GeneID:196463 NCBI-Mouse-GeneID:71772 NCBI-Rat-GeneID:246120 Plbd2 (mol) HOIP_1000305 NCBI-Human-GeneID:196463 http://www.ncbi.nlm.nih.gov/gene/196463 NCBI-Mouse-GeneID:71772 http://www.ncbi.nlm.nih.gov/gene/71772 NCBI-Rat-GeneID:246120 http://www.ncbi.nlm.nih.gov/gene/246120 HOIP:HOIP_1000306 NCBI-Human-GeneID:5350 NCBI-Mouse-GeneID:18821 NCBI-Rat-GeneID:64672 Pln (mol) HOIP_1000306 NCBI-Human-GeneID:5350 http://www.ncbi.nlm.nih.gov/gene/5350 NCBI-Mouse-GeneID:18821 http://www.ncbi.nlm.nih.gov/gene/18821 NCBI-Rat-GeneID:64672 http://www.ncbi.nlm.nih.gov/gene/64672 HOIP:HOIP_1000307 NCBI-Human-GeneID:5372 NCBI-Mouse-GeneID:29858 NCBI-Rat-GeneID:300089 Pmm1 (mol) HOIP_1000307 NCBI-Human-GeneID:5372 http://www.ncbi.nlm.nih.gov/gene/5372 NCBI-Mouse-GeneID:29858 http://www.ncbi.nlm.nih.gov/gene/29858 NCBI-Rat-GeneID:300089 http://www.ncbi.nlm.nih.gov/gene/300089 HOIP:HOIP_1000308 NCBI-Human-GeneID:55629 NCBI-Mouse-GeneID:52830 NCBI-Rat-GeneID:100125373 Pnrc2 (mol) HOIP_1000308 NCBI-Human-GeneID:55629 http://www.ncbi.nlm.nih.gov/gene/55629 NCBI-Mouse-GeneID:52830 http://www.ncbi.nlm.nih.gov/gene/52830 NCBI-Rat-GeneID:100125373 http://www.ncbi.nlm.nih.gov/gene/100125373 HOIP:HOIP_1000309 NCBI-Human-GeneID:5447 NCBI-Mouse-GeneID:18984 NCBI-Rat-GeneID:29441 Por (mol) HOIP_1000309 NCBI-Human-GeneID:5447 http://www.ncbi.nlm.nih.gov/gene/5447 NCBI-Mouse-GeneID:18984 http://www.ncbi.nlm.nih.gov/gene/18984 NCBI-Rat-GeneID:29441 http://www.ncbi.nlm.nih.gov/gene/29441 HOIP:HOIP_1000310 NCBI-Human-GeneID:5579 NCBI-Mouse-GeneID:18751 NCBI-Rat-GeneID:25023 Prkcb (mol) HOIP_1000310 NCBI-Human-GeneID:5579 http://www.ncbi.nlm.nih.gov/gene/5579 NCBI-Mouse-GeneID:18751 http://www.ncbi.nlm.nih.gov/gene/18751 NCBI-Rat-GeneID:25023 http://www.ncbi.nlm.nih.gov/gene/25023 HOIP:HOIP_1000311 NCBI-Human-GeneID:10419 NCBI-Mouse-GeneID:27374 NCBI-Rat-GeneID:364382 Prmt5 (mol) HOIP_1000311 NCBI-Human-GeneID:10419 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http://www.ncbi.nlm.nih.gov/gene/19650 NCBI-Rat-GeneID:680111 http://www.ncbi.nlm.nih.gov/gene/680111 HOIP:HOIP_1000316 NCBI-Human-GeneID:10741 NCBI-Mouse-GeneID:26450 NCBI-Rat-GeneID:29459 RBbp9 (mol) HOIP_1000316 NCBI-Human-GeneID:10741 http://www.ncbi.nlm.nih.gov/gene/10741 NCBI-Mouse-GeneID:26450 http://www.ncbi.nlm.nih.gov/gene/26450 NCBI-Rat-GeneID:29459 http://www.ncbi.nlm.nih.gov/gene/29459 HOIP:HOIP_1000317 NCBI-Human-GeneID:9400 NCBI-Mouse-GeneID:170472 NCBI-Rat-GeneID:287834 RECQL5 (mol) HOIP_1000317 NCBI-Human-GeneID:9400 http://www.ncbi.nlm.nih.gov/gene/9400 NCBI-Mouse-GeneID:170472 http://www.ncbi.nlm.nih.gov/gene/170472 NCBI-Rat-GeneID:287834 http://www.ncbi.nlm.nih.gov/gene/287834 HOIP:HOIP_1000318 NCBI-Human-GeneID:5991 NCBI-Mouse-GeneID:19726 NCBI-Rat-GeneID:361746 RFX3 (mol) HOIP_1000318 NCBI-Human-GeneID:5991 http://www.ncbi.nlm.nih.gov/gene/5991 NCBI-Mouse-GeneID:19726 http://www.ncbi.nlm.nih.gov/gene/19726 NCBI-Rat-GeneID:361746 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http://www.ncbi.nlm.nih.gov/gene/19363 NCBI-Rat-GeneID:500679 http://www.ncbi.nlm.nih.gov/gene/500679 HOIP:HOIP_1000323 NCBI-Human-GeneID:153020 NCBI-Mouse-GeneID:320292 NCBI-Rat-GeneID:100361238 Rasgef1b (mol) HOIP_1000323 NCBI-Human-GeneID:153020 http://www.ncbi.nlm.nih.gov/gene/153020 NCBI-Mouse-GeneID:320292 http://www.ncbi.nlm.nih.gov/gene/320292 NCBI-Rat-GeneID:100361238 http://www.ncbi.nlm.nih.gov/gene/100361238 HOIP:HOIP_1000324 NCBI-Human-GeneID:9939 NCBI-Mouse-GeneID:60365 NCBI-Rat-GeneID:295284 Rbm8a (mol) HOIP_1000324 NCBI-Human-GeneID:9939 http://www.ncbi.nlm.nih.gov/gene/9939 NCBI-Mouse-GeneID:60365 http://www.ncbi.nlm.nih.gov/gene/60365 NCBI-Rat-GeneID:295284 http://www.ncbi.nlm.nih.gov/gene/295284 HOIP:HOIP_1000325 NCBI-Human-GeneID:161253 NCBI-Mouse-GeneID:140743 NCBI-Rat-GeneID:64626 Rem2 (mol) HOIP_1000325 NCBI-Human-GeneID:161253 http://www.ncbi.nlm.nih.gov/gene/161253 NCBI-Mouse-GeneID:140743 http://www.ncbi.nlm.nih.gov/gene/140743 NCBI-Rat-GeneID:64626 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http://www.ncbi.nlm.nih.gov/gene/20219 NCBI-Rat-GeneID:29339 http://www.ncbi.nlm.nih.gov/gene/29339 HOIP:HOIP_1000332 NCBI-Human-GeneID:6341 NCBI-Mouse-GeneID:52892 NCBI-Rat-GeneID:497930 SCO1 (mol) HOIP_1000332 NCBI-Human-GeneID:6341 http://www.ncbi.nlm.nih.gov/gene/6341 NCBI-Mouse-GeneID:52892 http://www.ncbi.nlm.nih.gov/gene/52892 NCBI-Rat-GeneID:497930 http://www.ncbi.nlm.nih.gov/gene/497930 HOIP:HOIP_1000333 NCBI-Human-GeneID:23753 NCBI-Mouse-GeneID:64136 NCBI-Rat-GeneID:680945 SDF2L1 (mol) HOIP_1000333 NCBI-Human-GeneID:23753 http://www.ncbi.nlm.nih.gov/gene/23753 NCBI-Mouse-GeneID:64136 http://www.ncbi.nlm.nih.gov/gene/64136 NCBI-Rat-GeneID:680945 http://www.ncbi.nlm.nih.gov/gene/680945 HOIP:HOIP_1000334 NCBI-Human-GeneID:9871 NCBI-Mouse-GeneID:69608 NCBI-Rat-GeneID:310843 SEC24D (mol) HOIP_1000334 NCBI-Human-GeneID:9871 http://www.ncbi.nlm.nih.gov/gene/9871 NCBI-Mouse-GeneID:69608 http://www.ncbi.nlm.nih.gov/gene/69608 NCBI-Rat-GeneID:310843 http://www.ncbi.nlm.nih.gov/gene/310843 HOIP:HOIP_1000335 NCBI-Human-GeneID:10952 NCBI-Mouse-GeneID:66212 NCBI-Rat-GeneID:298068 SEC61B (mol) HOIP_1000335 NCBI-Human-GeneID:10952 http://www.ncbi.nlm.nih.gov/gene/10952 NCBI-Mouse-GeneID:66212 http://www.ncbi.nlm.nih.gov/gene/66212 NCBI-Rat-GeneID:298068 http://www.ncbi.nlm.nih.gov/gene/298068 HOIP:HOIP_1000336 NCBI-Human-GeneID:12 SERPINA3 (mol) HOIP_1000336 NCBI-Human-GeneID:12 http://www.ncbi.nlm.nih.gov/gene/12 HOIP:HOIP_1000337 NCBI-Human-GeneID:27244 NCBI-Mouse-GeneID:140742 NCBI-Rat-GeneID:294518 SESN1 (mol) HOIP_1000337 NCBI-Human-GeneID:27244 http://www.ncbi.nlm.nih.gov/gene/27244 NCBI-Mouse-GeneID:140742 http://www.ncbi.nlm.nih.gov/gene/140742 NCBI-Rat-GeneID:294518 http://www.ncbi.nlm.nih.gov/gene/294518 HOIP:HOIP_1000338 NCBI-Human-GeneID:6554 NCBI-Mouse-GeneID:20493 NCBI-Rat-GeneID:24777 SLC10A1 (mol) HOIP_1000338 NCBI-Human-GeneID:6554 http://www.ncbi.nlm.nih.gov/gene/6554 NCBI-Mouse-GeneID:20493 http://www.ncbi.nlm.nih.gov/gene/20493 NCBI-Rat-GeneID:24777 http://www.ncbi.nlm.nih.gov/gene/24777 HOIP:HOIP_1000339 NCBI-Human-GeneID:6506 NCBI-Mouse-GeneID:20511 NCBI-Rat-GeneID:29482 SLC1A2 (mol) HOIP_1000339 NCBI-Human-GeneID:6506 http://www.ncbi.nlm.nih.gov/gene/6506 NCBI-Mouse-GeneID:20511 http://www.ncbi.nlm.nih.gov/gene/20511 NCBI-Rat-GeneID:29482 http://www.ncbi.nlm.nih.gov/gene/29482 HOIP:HOIP_1000340 NCBI-Human-GeneID:291 NCBI-Mouse-GeneID:11739 NCBI-Rat-GeneID:85333 SLC25A4 (mol) HOIP_1000340 NCBI-Human-GeneID:291 http://www.ncbi.nlm.nih.gov/gene/291 NCBI-Mouse-GeneID:11739 http://www.ncbi.nlm.nih.gov/gene/11739 NCBI-Rat-GeneID:85333 http://www.ncbi.nlm.nih.gov/gene/85333 HOIP:HOIP_1000341 NCBI-Human-GeneID:3177 NCBI-Mouse-GeneID:13340 NCBI-Rat-GeneID:65194 SLC29A2 (mol) HOIP_1000341 NCBI-Human-GeneID:3177 http://www.ncbi.nlm.nih.gov/gene/3177 NCBI-Mouse-GeneID:13340 http://www.ncbi.nlm.nih.gov/gene/13340 NCBI-Rat-GeneID:65194 http://www.ncbi.nlm.nih.gov/gene/65194 HOIP:HOIP_1000342 NCBI-Human-GeneID:6515 NCBI-Mouse-GeneID:20527 NCBI-Rat-GeneID:25551 SLC2A3 (mol) HOIP_1000342 NCBI-Human-GeneID:6515 http://www.ncbi.nlm.nih.gov/gene/6515 NCBI-Mouse-GeneID:20527 http://www.ncbi.nlm.nih.gov/gene/20527 NCBI-Rat-GeneID:25551 http://www.ncbi.nlm.nih.gov/gene/25551 HOIP:HOIP_1000343 NCBI-Human-GeneID:80255 NCBI-Mouse-GeneID:74150 NCBI-Rat-GeneID:288993 SLC35F5 (mol) HOIP_1000343 NCBI-Human-GeneID:80255 http://www.ncbi.nlm.nih.gov/gene/80255 NCBI-Mouse-GeneID:74150 http://www.ncbi.nlm.nih.gov/gene/74150 NCBI-Rat-GeneID:288993 http://www.ncbi.nlm.nih.gov/gene/288993 HOIP:HOIP_1000344 NCBI-Human-GeneID:57153 NCBI-Mouse-GeneID:68682 NCBI-Rat-GeneID:363024 SLC44A2 (mol) HOIP_1000344 NCBI-Human-GeneID:57153 http://www.ncbi.nlm.nih.gov/gene/57153 NCBI-Mouse-GeneID:68682 http://www.ncbi.nlm.nih.gov/gene/68682 NCBI-Rat-GeneID:363024 http://www.ncbi.nlm.nih.gov/gene/363024 HOIP:HOIP_1000345 SMARCD3 (mol) HOIP_1000345 HOIP:HOIP_1000346 NCBI-Human-GeneID:6608 NCBI-Mouse-GeneID:319757 NCBI-Rat-GeneID:25273 SMO (mol) HOIP_1000346 NCBI-Human-GeneID:6608 http://www.ncbi.nlm.nih.gov/gene/6608 NCBI-Mouse-GeneID:319757 http://www.ncbi.nlm.nih.gov/gene/319757 NCBI-Rat-GeneID:25273 http://www.ncbi.nlm.nih.gov/gene/25273 HOIP:HOIP_1000347 NCBI-Human-GeneID:6609 NCBI-Mouse-GeneID:20597 NCBI-Rat-GeneID:308909 SMPD1 (mol) HOIP_1000347 NCBI-Human-GeneID:6609 http://www.ncbi.nlm.nih.gov/gene/6609 NCBI-Mouse-GeneID:20597 http://www.ncbi.nlm.nih.gov/gene/20597 NCBI-Rat-GeneID:308909 http://www.ncbi.nlm.nih.gov/gene/308909 HOIP:HOIP_1000348 NCBI-Human-GeneID:10924 NCBI-Mouse-GeneID:57319 NCBI-Rat-GeneID:294422 SMPDL3A (mol) HOIP_1000348 NCBI-Human-GeneID:10924 http://www.ncbi.nlm.nih.gov/gene/10924 NCBI-Mouse-GeneID:57319 http://www.ncbi.nlm.nih.gov/gene/57319 NCBI-Rat-GeneID:294422 http://www.ncbi.nlm.nih.gov/gene/294422 HOIP:HOIP_1000349 NCBI-Human-GeneID:10580 NCBI-Mouse-GeneID:20411 NCBI-Rat-GeneID:686098 SORBS1 (mol) HOIP_1000349 NCBI-Human-GeneID:10580 http://www.ncbi.nlm.nih.gov/gene/10580 NCBI-Mouse-GeneID:20411 http://www.ncbi.nlm.nih.gov/gene/20411 NCBI-Rat-GeneID:686098 http://www.ncbi.nlm.nih.gov/gene/686098 HOIP:HOIP_1000350 NCBI-Human-GeneID:9517 NCBI-Mouse-GeneID:20773 NCBI-Rat-GeneID:366697 SPTLC2 (mol) HOIP_1000350 NCBI-Human-GeneID:9517 http://www.ncbi.nlm.nih.gov/gene/9517 NCBI-Mouse-GeneID:20773 http://www.ncbi.nlm.nih.gov/gene/20773 NCBI-Rat-GeneID:366697 http://www.ncbi.nlm.nih.gov/gene/366697 HOIP:HOIP_1000351 NCBI-Human-GeneID:6733 NCBI-Mouse-GeneID:20817 NCBI-Rat-GeneID:296753 SRPK2 (mol) HOIP_1000351 NCBI-Human-GeneID:6733 http://www.ncbi.nlm.nih.gov/gene/6733 NCBI-Mouse-GeneID:20817 http://www.ncbi.nlm.nih.gov/gene/20817 NCBI-Rat-GeneID:296753 http://www.ncbi.nlm.nih.gov/gene/296753 HOIP:HOIP_1000352 NCBI-Human-GeneID:6426 NCBI-Mouse-GeneID:110809 NCBI-Rat-GeneID:689890 SRSF1 (mol) HOIP_1000352 NCBI-Human-GeneID:6426 http://www.ncbi.nlm.nih.gov/gene/6426 NCBI-Mouse-GeneID:110809 http://www.ncbi.nlm.nih.gov/gene/110809 NCBI-Rat-GeneID:689890 http://www.ncbi.nlm.nih.gov/gene/689890 HOIP:HOIP_1000353 NCBI-Human-GeneID:56910 NCBI-Mouse-GeneID:99138 NCBI-Rat-GeneID:296128 STARD7 (mol) HOIP_1000353 NCBI-Human-GeneID:56910 http://www.ncbi.nlm.nih.gov/gene/56910 NCBI-Mouse-GeneID:99138 http://www.ncbi.nlm.nih.gov/gene/99138 NCBI-Rat-GeneID:296128 http://www.ncbi.nlm.nih.gov/gene/296128 HOIP:HOIP_1000354 STF-083010 HOIP_1000354 HOIP:HOIP_1000355 NCBI-Human-GeneID:6794 NCBI-Mouse-GeneID:20869 NCBI-Rat-GeneID:314621 STK11 (mol) HOIP_1000355 NCBI-Human-GeneID:6794 http://www.ncbi.nlm.nih.gov/gene/6794 NCBI-Mouse-GeneID:20869 http://www.ncbi.nlm.nih.gov/gene/20869 NCBI-Rat-GeneID:314621 http://www.ncbi.nlm.nih.gov/gene/314621 HOIP:HOIP_1000356 NCBI-Human-GeneID:10273 NCBI-Mouse-GeneID:56424 NCBI-Rat-GeneID:287155 STUB1 (mol) HOIP_1000356 NCBI-Human-GeneID:10273 http://www.ncbi.nlm.nih.gov/gene/10273 NCBI-Mouse-GeneID:56424 http://www.ncbi.nlm.nih.gov/gene/56424 NCBI-Rat-GeneID:287155 http://www.ncbi.nlm.nih.gov/gene/287155 HOIP:HOIP_1000357 NCBI-Human-GeneID:9144 NCBI-Mouse-GeneID:20973 NCBI-Rat-GeneID:89815 SYNGR2 (mol) HOIP_1000357 NCBI-Human-GeneID:9144 http://www.ncbi.nlm.nih.gov/gene/9144 NCBI-Mouse-GeneID:20973 http://www.ncbi.nlm.nih.gov/gene/20973 NCBI-Rat-GeneID:89815 http://www.ncbi.nlm.nih.gov/gene/89815 HOIP:HOIP_1000358 NCBI-Human-GeneID:5777 NCBI-Mouse-GeneID:15170 NCBI-Rat-GeneID:116689 SHP1 PTPN6 (mol) HOIP_1000358 NCBI-Human-GeneID:5777 http://www.ncbi.nlm.nih.gov/gene/5777 NCBI-Mouse-GeneID:15170 http://www.ncbi.nlm.nih.gov/gene/15170 NCBI-Rat-GeneID:116689 http://www.ncbi.nlm.nih.gov/gene/116689 HOIP:HOIP_1000359 NCBI-Human-GeneID:8935 NCBI-Mouse-GeneID:54353 NCBI-Rat-GeneID:155183 Skap2 (mol) HOIP_1000359 NCBI-Human-GeneID:8935 http://www.ncbi.nlm.nih.gov/gene/8935 NCBI-Mouse-GeneID:54353 http://www.ncbi.nlm.nih.gov/gene/54353 NCBI-Rat-GeneID:155183 http://www.ncbi.nlm.nih.gov/gene/155183 HOIP:HOIP_1000360 NCBI-Human-GeneID:788 NCBI-Mouse-GeneID:57279 NCBI-Rat-GeneID:117035 Slc25a20 (mol) HOIP_1000360 NCBI-Human-GeneID:788 http://www.ncbi.nlm.nih.gov/gene/788 NCBI-Mouse-GeneID:57279 http://www.ncbi.nlm.nih.gov/gene/57279 NCBI-Rat-GeneID:117035 http://www.ncbi.nlm.nih.gov/gene/117035 HOIP:HOIP_1000361 NCBI-Human-GeneID:8884 NCBI-Mouse-GeneID:330064 NCBI-Rat-GeneID:170551 Slc5a6 (mol) HOIP_1000361 NCBI-Human-GeneID:8884 http://www.ncbi.nlm.nih.gov/gene/8884 NCBI-Mouse-GeneID:330064 http://www.ncbi.nlm.nih.gov/gene/330064 NCBI-Rat-GeneID:170551 http://www.ncbi.nlm.nih.gov/gene/170551 HOIP:HOIP_1000362 NCBI-Human-GeneID:6606 NCBI-Mouse-GeneID:20595 NCBI-Rat-GeneID:64301 Smn1 (mol) HOIP_1000362 NCBI-Human-GeneID:6606 http://www.ncbi.nlm.nih.gov/gene/6606 NCBI-Mouse-GeneID:20595 http://www.ncbi.nlm.nih.gov/gene/20595 NCBI-Rat-GeneID:64301 http://www.ncbi.nlm.nih.gov/gene/64301 HOIP:HOIP_1000364 Srnx1 (mol) HOIP_1000364 HOIP:HOIP_1000365 NCBI-Human-GeneID:140809 NCBI-Mouse-GeneID:76650 NCBI-Rat-GeneID:296271 Srxn1 (mol) HOIP_1000365 NCBI-Human-GeneID:140809 http://www.ncbi.nlm.nih.gov/gene/140809 NCBI-Mouse-GeneID:76650 http://www.ncbi.nlm.nih.gov/gene/76650 NCBI-Rat-GeneID:296271 http://www.ncbi.nlm.nih.gov/gene/296271 HOIP:HOIP_1000366 NCBI-Human-GeneID:6742 NCBI-Mouse-GeneID:381760 NCBI-Rat-GeneID:54304 Ssbp1 (mol) HOIP_1000366 NCBI-Human-GeneID:6742 http://www.ncbi.nlm.nih.gov/gene/6742 NCBI-Mouse-GeneID:381760 http://www.ncbi.nlm.nih.gov/gene/381760 NCBI-Rat-GeneID:54304 http://www.ncbi.nlm.nih.gov/gene/54304 HOIP:HOIP_1000367 NCBI-Human-GeneID:6747 NCBI-Mouse-GeneID:67437 NCBI-Rat-GeneID:81784 Ssr3 (mol) HOIP_1000367 NCBI-Human-GeneID:6747 http://www.ncbi.nlm.nih.gov/gene/6747 NCBI-Mouse-GeneID:67437 http://www.ncbi.nlm.nih.gov/gene/67437 NCBI-Rat-GeneID:81784 http://www.ncbi.nlm.nih.gov/gene/81784 HOIP:HOIP_1000368 NCBI-Human-GeneID:10923 NCBI-Mouse-GeneID:20024 NCBI-Rat-GeneID:192269 Sub1 (mol) HOIP_1000368 NCBI-Human-GeneID:10923 http://www.ncbi.nlm.nih.gov/gene/10923 NCBI-Mouse-GeneID:20024 http://www.ncbi.nlm.nih.gov/gene/20024 NCBI-Rat-GeneID:192269 http://www.ncbi.nlm.nih.gov/gene/192269 HOIP:HOIP_1000369 NCBI-Human-GeneID:6876 NCBI-Mouse-GeneID:21345 NCBI-Rat-GeneID:25123 TAGLN (mol) HOIP_1000369 NCBI-Human-GeneID:6876 http://www.ncbi.nlm.nih.gov/gene/6876 NCBI-Mouse-GeneID:21345 http://www.ncbi.nlm.nih.gov/gene/21345 NCBI-Rat-GeneID:25123 http://www.ncbi.nlm.nih.gov/gene/25123 HOIP:HOIP_1000370 TGF (mol) HOIP_1000370 HOIP:HOIP_1000372 NCBI-Human-GeneID:7057 NCBI-Mouse-GeneID:21825 NCBI-Rat-GeneID:445442 THBS1 (mol) HOIP_1000372 NCBI-Human-GeneID:7057 http://www.ncbi.nlm.nih.gov/gene/7057 NCBI-Mouse-GeneID:21825 http://www.ncbi.nlm.nih.gov/gene/21825 NCBI-Rat-GeneID:445442 http://www.ncbi.nlm.nih.gov/gene/445442 HOIP:HOIP_1000373 NCBI-Human-GeneID:7076 NCBI-Mouse-GeneID:21857 NCBI-Rat-GeneID:116510 TIMP1 (mol) HOIP_1000373 NCBI-Human-GeneID:7076 http://www.ncbi.nlm.nih.gov/gene/7076 NCBI-Mouse-GeneID:21857 http://www.ncbi.nlm.nih.gov/gene/21857 NCBI-Rat-GeneID:116510 http://www.ncbi.nlm.nih.gov/gene/116510 HOIP:HOIP_1000375 NCBI-Human-GeneID:3604 NCBI-Mouse-GeneID:21942 NCBI-Rat-GeneID:500590 TNFRSF9 (mol) HOIP_1000375 NCBI-Human-GeneID:3604 http://www.ncbi.nlm.nih.gov/gene/3604 NCBI-Mouse-GeneID:21942 http://www.ncbi.nlm.nih.gov/gene/21942 NCBI-Rat-GeneID:500590 http://www.ncbi.nlm.nih.gov/gene/500590 HOIP:HOIP_1000376 NCBI-Human-GeneID:94241 NCBI-Rat-GeneID:297822 TP53INP1 (mol) HOIP_1000376 NCBI-Human-GeneID:94241 http://www.ncbi.nlm.nih.gov/gene/94241 NCBI-Rat-GeneID:297822 http://www.ncbi.nlm.nih.gov/gene/297822 HOIP:HOIP_1000377 NCBI-Human-GeneID:29896 NCBI-Mouse-GeneID:101214 NCBI-Rat-GeneID:500116 TRA2A (mol) HOIP_1000377 NCBI-Human-GeneID:29896 http://www.ncbi.nlm.nih.gov/gene/29896 NCBI-Mouse-GeneID:101214 http://www.ncbi.nlm.nih.gov/gene/101214 NCBI-Rat-GeneID:500116 http://www.ncbi.nlm.nih.gov/gene/500116 HOIP:HOIP_1000378 NCBI-Human-GeneID:57761 NCBI-Mouse-GeneID:228775 NCBI-Rat-GeneID:246273 TRIB3 (mol) HOIP_1000378 NCBI-Human-GeneID:57761 http://www.ncbi.nlm.nih.gov/gene/57761 NCBI-Mouse-GeneID:228775 http://www.ncbi.nlm.nih.gov/gene/228775 NCBI-Rat-GeneID:246273 http://www.ncbi.nlm.nih.gov/gene/246273 HOIP:HOIP_1000379 NCBI-Human-GeneID:128553 NCBI-Mouse-GeneID:228911 NCBI-Rat-GeneID:100911757 TSHZ2 (mol) HOIP_1000379 NCBI-Human-GeneID:128553 http://www.ncbi.nlm.nih.gov/gene/128553 NCBI-Mouse-GeneID:228911 http://www.ncbi.nlm.nih.gov/gene/228911 NCBI-Rat-GeneID:100911757 http://www.ncbi.nlm.nih.gov/gene/100911757 HOIP:HOIP_1000380 NCBI-Human-GeneID:7291 NCBI-Mouse-GeneID:22160 NCBI-Rat-GeneID:85489 TWIST1 (mol) HOIP_1000380 NCBI-Human-GeneID:7291 http://www.ncbi.nlm.nih.gov/gene/7291 NCBI-Mouse-GeneID:22160 http://www.ncbi.nlm.nih.gov/gene/22160 NCBI-Rat-GeneID:85489 http://www.ncbi.nlm.nih.gov/gene/85489 HOIP:HOIP_1000381 NCBI-Human-GeneID:6880 NCBI-Mouse-GeneID:108143 NCBI-Rat-GeneID:373541 Taf9 (mol) HOIP_1000381 NCBI-Human-GeneID:6880 http://www.ncbi.nlm.nih.gov/gene/6880 NCBI-Mouse-GeneID:108143 http://www.ncbi.nlm.nih.gov/gene/108143 NCBI-Rat-GeneID:373541 http://www.ncbi.nlm.nih.gov/gene/373541 HOIP:HOIP_1000383 NCBI-Human-GeneID:51330 NCBI-Mouse-GeneID:27279 NCBI-Rat-GeneID:302965 Tnfrsf12a (mol) HOIP_1000383 NCBI-Human-GeneID:51330 http://www.ncbi.nlm.nih.gov/gene/51330 NCBI-Mouse-GeneID:27279 http://www.ncbi.nlm.nih.gov/gene/27279 NCBI-Rat-GeneID:302965 http://www.ncbi.nlm.nih.gov/gene/302965 HOIP:HOIP_1000384 NCBI-Human-GeneID:27242 NCBI-Mouse-GeneID:94185 NCBI-Rat-GeneID:316256 Tnfrsf21 (mol) HOIP_1000384 NCBI-Human-GeneID:27242 http://www.ncbi.nlm.nih.gov/gene/27242 NCBI-Mouse-GeneID:94185 http://www.ncbi.nlm.nih.gov/gene/94185 NCBI-Rat-GeneID:316256 http://www.ncbi.nlm.nih.gov/gene/316256 HOIP:HOIP_1000385 NCBI-Human-GeneID:9804 NCBI-Mouse-GeneID:67952 NCBI-Rat-GeneID:266601 Tomm20 (mol) HOIP_1000385 NCBI-Human-GeneID:9804 http://www.ncbi.nlm.nih.gov/gene/9804 NCBI-Mouse-GeneID:67952 http://www.ncbi.nlm.nih.gov/gene/67952 NCBI-Rat-GeneID:266601 http://www.ncbi.nlm.nih.gov/gene/266601 HOIP:HOIP_1000386 NCBI-Human-GeneID:163590 NCBI-Mouse-GeneID:240832 NCBI-Rat-GeneID:304881 Tor1aip2 (mol) HOIP_1000386 NCBI-Human-GeneID:163590 http://www.ncbi.nlm.nih.gov/gene/163590 NCBI-Mouse-GeneID:240832 http://www.ncbi.nlm.nih.gov/gene/240832 NCBI-Rat-GeneID:304881 http://www.ncbi.nlm.nih.gov/gene/304881 HOIP:HOIP_1000387 NCBI-Human-GeneID:1831 NCBI-Mouse-GeneID:14605 NCBI-Rat-GeneID:83514 Tsc22d3 (mol) HOIP_1000387 NCBI-Human-GeneID:1831 http://www.ncbi.nlm.nih.gov/gene/1831 NCBI-Mouse-GeneID:14605 http://www.ncbi.nlm.nih.gov/gene/14605 NCBI-Rat-GeneID:83514 http://www.ncbi.nlm.nih.gov/gene/83514 HOIP:HOIP_1000388 NCBI-Human-GeneID:10382 NCBI-Mouse-GeneID:22153 NCBI-Rat-GeneID:29213 TUBB4A (mol) HOIP_1000388 NCBI-Human-GeneID:10382 http://www.ncbi.nlm.nih.gov/gene/10382 NCBI-Mouse-GeneID:22153 http://www.ncbi.nlm.nih.gov/gene/22153 NCBI-Rat-GeneID:29213 http://www.ncbi.nlm.nih.gov/gene/29213 HOIP:HOIP_1000389 NCBI-Human-GeneID:7296 NCBI-Mouse-GeneID:50493 NCBI-Rat-GeneID:58819 Txnrd1 (mol) HOIP_1000389 NCBI-Human-GeneID:7296 http://www.ncbi.nlm.nih.gov/gene/7296 NCBI-Mouse-GeneID:50493 http://www.ncbi.nlm.nih.gov/gene/50493 NCBI-Rat-GeneID:58819 http://www.ncbi.nlm.nih.gov/gene/58819 HOIP:HOIP_1000390 Txrnd1 (mol) HOIP_1000390 HOIP:HOIP_1000391 NCBI-Human-GeneID:7298 NCBI-Mouse-GeneID:22171 NCBI-Rat-GeneID:29261 Tyms (mol) HOIP_1000391 NCBI-Human-GeneID:7298 http://www.ncbi.nlm.nih.gov/gene/7298 NCBI-Mouse-GeneID:22171 http://www.ncbi.nlm.nih.gov/gene/22171 NCBI-Rat-GeneID:29261 http://www.ncbi.nlm.nih.gov/gene/29261 HOIP:HOIP_1000393 NCBI-Human-GeneID:7352 NCBI-Mouse-GeneID:22229 NCBI-Rat-GeneID:25708 UCP3 (mol) HOIP_1000393 NCBI-Human-GeneID:7352 http://www.ncbi.nlm.nih.gov/gene/7352 NCBI-Mouse-GeneID:22229 http://www.ncbi.nlm.nih.gov/gene/22229 NCBI-Rat-GeneID:25708 http://www.ncbi.nlm.nih.gov/gene/25708 HOIP:HOIP_1000395 NCBI-Human-GeneID:54658 NCBI-Mouse-GeneID:394436 NCBI-Rat-GeneID:24861 UGT1a1 (mol) HOIP_1000395 NCBI-Human-GeneID:54658 http://www.ncbi.nlm.nih.gov/gene/54658 NCBI-Mouse-GeneID:394436 http://www.ncbi.nlm.nih.gov/gene/394436 NCBI-Rat-GeneID:24861 http://www.ncbi.nlm.nih.gov/gene/24861 HOIP:HOIP_1000397 NCBI-Mouse-GeneID:71773 NCBI-Rat-GeneID:286954 Ugt2b1 (mol) HOIP_1000397 NCBI-Mouse-GeneID:71773 http://www.ncbi.nlm.nih.gov/gene/71773 NCBI-Rat-GeneID:286954 http://www.ncbi.nlm.nih.gov/gene/286954 HOIP:HOIP_1000398 NCBI-Human-GeneID:7364 NCBI-Rat-GeneID:286989 Ugt2b7 (mol) HOIP_1000398 NCBI-Human-GeneID:7364 http://www.ncbi.nlm.nih.gov/gene/7364 NCBI-Rat-GeneID:286989 http://www.ncbi.nlm.nih.gov/gene/286989 HOIP:HOIP_1000401 A protein that is a translation product of the human VAV2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7410 NCBI-Mouse-GeneID:22325 NCBI-Rat-GeneID:296603 VAV2 guanine nucleotide exchange factor VAV2 HOIP_1000401 NCBI-Human-GeneID:7410 http://www.ncbi.nlm.nih.gov/gene/7410 NCBI-Mouse-GeneID:22325 http://www.ncbi.nlm.nih.gov/gene/22325 NCBI-Rat-GeneID:296603 http://www.ncbi.nlm.nih.gov/gene/296603 HOIP:HOIP_1000405 NCBI-Human-GeneID:7494 NCBI-Mouse-GeneID:22433 NCBI-Rat-GeneID:289754 XBP1 (mol) HOIP_1000405 NCBI-Human-GeneID:7494 http://www.ncbi.nlm.nih.gov/gene/7494 NCBI-Mouse-GeneID:22433 http://www.ncbi.nlm.nih.gov/gene/22433 NCBI-Rat-GeneID:289754 http://www.ncbi.nlm.nih.gov/gene/289754 HOIP:HOIP_1000406 NCBI-Human-GeneID:151126 ZNF385B (mol) HOIP_1000406 NCBI-Human-GeneID:151126 http://www.ncbi.nlm.nih.gov/gene/151126 HOIP:HOIP_1000414 caspase (mol) HOIP_1000414 HOIP:HOIP_1000415 NCBI-Human-GeneID:1052 NCBI-Mouse-GeneID:12609 NCBI-Rat-GeneID:25695 cebpd (mol) HOIP_1000415 NCBI-Human-GeneID:1052 http://www.ncbi.nlm.nih.gov/gene/1052 NCBI-Mouse-GeneID:12609 http://www.ncbi.nlm.nih.gov/gene/12609 NCBI-Rat-GeneID:25695 http://www.ncbi.nlm.nih.gov/gene/25695 HOIP:HOIP_1000418 An aminoquinoline that is quinoline which is substituted at position 4 by a [5-(diethylamino)pentan-2-yl]amino group at at position 7 by chlorine. It is used for the treatment of malaria, hepatic amoebiasis, lupus erythematosus, light-sensitive skin eruptions, and rheumatoid arthritis. C18H26ClN3 Wikipedia:Chloroquine CCN(CC)CCCC(C)Nc1ccnc2cc(Cl)ccc12 CAS:54-05-7 DrugBank:DB00608 LINCS:LSM-1901 MeSH:D002738 Patent:US2233970 N(4)-(7-chloroquinolin-4-yl)-N(1),N(1)-diethylpentane-1,4-diamine chloroquine HOIP_1000418 HOIP:HOIP_1000419 http://purl.bioontology.org/ontology/MESH/D019743 cxc family (mol) HOIP_1000419 HOIP:HOIP_1000421 NCBI-Human-GeneID:83939 NCBI-Mouse-GeneID:229317 NCBI-Rat-GeneID:502531 eIF2a (mol) HOIP_1000421 NCBI-Human-GeneID:83939 http://www.ncbi.nlm.nih.gov/gene/83939 NCBI-Mouse-GeneID:229317 http://www.ncbi.nlm.nih.gov/gene/229317 NCBI-Rat-GeneID:502531 http://www.ncbi.nlm.nih.gov/gene/502531 HOIP:HOIP_1000422 gentamicin (mol) HOIP_1000422 HOIP:HOIP_1000431 TIMP family HOIP_1000431 HOIP:HOIP_1000435 NCBI-Human-GeneID:811 NCBI-Mouse-GeneID:716910 NCBI-Rat-GeneID:64202 http://omim.org/entry/109091 calreticulin (mol) HOIP_1000435 NCBI-Human-GeneID:811 http://www.ncbi.nlm.nih.gov/gene/811 NCBI-Mouse-GeneID:716910 https://www.ncbi.nlm.nih.gov/gene/716910 NCBI-Rat-GeneID:64202 https://www.ncbi.nlm.nih.gov/gene/64202 HOIP:HOIP_1000442 fibrate HOIP_1000442 HOIP:HOIP_1000500 NCBI-Human-GeneID:123876 NCBI-Rat-GeneID:246263 ACSM2A (mol) HOIP_1000500 NCBI-Human-GeneID:123876 http://www.ncbi.nlm.nih.gov/gene/123876 NCBI-Rat-GeneID:246263 http://www.ncbi.nlm.nih.gov/gene/246263 HOIP:HOIP_1000501 NCBI-Human-GeneID:348158 ACSM2B (mol) HOIP_1000501 NCBI-Human-GeneID:348158 http://www.ncbi.nlm.nih.gov/gene/348158 HOIP:HOIP_1000502 NCBI-Human-GeneID:55109 NCBI-Mouse-GeneID:66549 NCBI-Rat-GeneID:310005 AGGF1 (mol) HOIP_1000502 NCBI-Human-GeneID:55109 http://www.ncbi.nlm.nih.gov/gene/55109 NCBI-Mouse-GeneID:66549 http://www.ncbi.nlm.nih.gov/gene/66549 NCBI-Rat-GeneID:310005 http://www.ncbi.nlm.nih.gov/gene/310005 HOIP:HOIP_1000503 NCBI-Human-GeneID:29028 NCBI-Mouse-GeneID:70472 NCBI-Rat-GeneID:314993 ATAD2 (mol) HOIP_1000503 NCBI-Human-GeneID:29028 http://www.ncbi.nlm.nih.gov/gene/29028 NCBI-Mouse-GeneID:70472 http://www.ncbi.nlm.nih.gov/gene/70472 NCBI-Rat-GeneID:314993 http://www.ncbi.nlm.nih.gov/gene/314993 HOIP:HOIP_1000504 NCBI-Human-GeneID:597 NCBI-Mouse-GeneID:12044 NCBI-Rat-GeneID:170929 BCL2A1 (mol) HOIP_1000504 NCBI-Human-GeneID:597 http://www.ncbi.nlm.nih.gov/gene/597 NCBI-Mouse-GeneID:12044 http://www.ncbi.nlm.nih.gov/gene/12044 NCBI-Rat-GeneID:170929 http://www.ncbi.nlm.nih.gov/gene/170929 HOIP:HOIP_1000506 NCBI-Human-GeneID:113130 NCBI-Mouse-GeneID:67849 NCBI-Rat-GeneID:684771 CDCA5 (mol) HOIP_1000506 NCBI-Human-GeneID:113130 http://www.ncbi.nlm.nih.gov/gene/113130 NCBI-Mouse-GeneID:67849 http://www.ncbi.nlm.nih.gov/gene/67849 NCBI-Rat-GeneID:684771 http://www.ncbi.nlm.nih.gov/gene/684771 HOIP:HOIP_1000508 NCBI-Human-GeneID:79789 NCBI-Mouse-GeneID:94040 NCBI-Rat-GeneID:299285 CLMN (mol) HOIP_1000508 NCBI-Human-GeneID:79789 http://www.ncbi.nlm.nih.gov/gene/79789 NCBI-Mouse-GeneID:94040 http://www.ncbi.nlm.nih.gov/gene/94040 NCBI-Rat-GeneID:299285 http://www.ncbi.nlm.nih.gov/gene/299285 HOIP:HOIP_1000509 NCBI-Human-GeneID:6372 NCBI-Rat-GeneID:60665 CXCL6 (mol) HOIP_1000509 NCBI-Human-GeneID:6372 http://www.ncbi.nlm.nih.gov/gene/6372 NCBI-Rat-GeneID:60665 http://www.ncbi.nlm.nih.gov/gene/60665 HOIP:HOIP_1000511 NCBI-Human-GeneID:1543 NCBI-Mouse-GeneID:13076 NCBI-Rat-GeneID:24296 CYP1A1 (mol) HOIP_1000511 NCBI-Human-GeneID:1543 http://www.ncbi.nlm.nih.gov/gene/1543 NCBI-Mouse-GeneID:13076 http://www.ncbi.nlm.nih.gov/gene/13076 NCBI-Rat-GeneID:24296 http://www.ncbi.nlm.nih.gov/gene/24296 HOIP:HOIP_1000512 NCBI-Human-GeneID:1544 NCBI-Mouse-GeneID:13077 NCBI-Rat-GeneID:24297 CYP1A2 (mol) HOIP_1000512 NCBI-Human-GeneID:1544 http://www.ncbi.nlm.nih.gov/gene/1544 NCBI-Mouse-GeneID:13077 http://www.ncbi.nlm.nih.gov/gene/13077 NCBI-Rat-GeneID:24297 http://www.ncbi.nlm.nih.gov/gene/24297 HOIP:HOIP_1000513 NCBI-Human-GeneID:1719 NCBI-Mouse-GeneID:13361 NCBI-Rat-GeneID:24312 DHFR (mol) HOIP_1000513 NCBI-Human-GeneID:1719 http://www.ncbi.nlm.nih.gov/gene/1719 NCBI-Mouse-GeneID:13361 http://www.ncbi.nlm.nih.gov/gene/13361 NCBI-Rat-GeneID:24312 http://www.ncbi.nlm.nih.gov/gene/24312 HOIP:HOIP_1000514 NCBI-Human-GeneID:1806 NCBI-Mouse-GeneID:99586 NCBI-Rat-GeneID:81656 DPYD (mol) HOIP_1000514 NCBI-Human-GeneID:1806 http://www.ncbi.nlm.nih.gov/gene/1806 NCBI-Mouse-GeneID:99586 http://www.ncbi.nlm.nih.gov/gene/99586 NCBI-Rat-GeneID:81656 http://www.ncbi.nlm.nih.gov/gene/81656 HOIP:HOIP_1000515 NCBI-Human-GeneID:2237 NCBI-Mouse-GeneID:14156 NCBI-Rat-GeneID:84490 FEN1 (mol) HOIP_1000515 NCBI-Human-GeneID:2237 http://www.ncbi.nlm.nih.gov/gene/2237 NCBI-Mouse-GeneID:14156 http://www.ncbi.nlm.nih.gov/gene/14156 NCBI-Rat-GeneID:84490 http://www.ncbi.nlm.nih.gov/gene/84490 HOIP:HOIP_1000516 NCBI-Human-GeneID:2674 NCBI-Mouse-GeneID:14585 NCBI-Rat-GeneID:25454 GFRA1 (mol) HOIP_1000516 NCBI-Human-GeneID:2674 http://www.ncbi.nlm.nih.gov/gene/2674 NCBI-Mouse-GeneID:14585 http://www.ncbi.nlm.nih.gov/gene/14585 NCBI-Rat-GeneID:25454 http://www.ncbi.nlm.nih.gov/gene/25454 HOIP:HOIP_1000517 NCBI-Human-GeneID:10243 NCBI-Mouse-GeneID:268566 NCBI-Rat-GeneID:64845 GPHN (mol) HOIP_1000517 NCBI-Human-GeneID:10243 http://www.ncbi.nlm.nih.gov/gene/10243 NCBI-Mouse-GeneID:268566 http://www.ncbi.nlm.nih.gov/gene/268566 NCBI-Rat-GeneID:64845 http://www.ncbi.nlm.nih.gov/gene/64845 HOIP:HOIP_1000518 NCBI-Human-GeneID:29923 NCBI-Mouse-GeneID:69573 NCBI-Rat-GeneID:100361568 HILPDA (mol) HOIP_1000518 NCBI-Human-GeneID:29923 http://www.ncbi.nlm.nih.gov/gene/29923 NCBI-Mouse-GeneID:69573 http://www.ncbi.nlm.nih.gov/gene/69573 NCBI-Rat-GeneID:100361568 http://www.ncbi.nlm.nih.gov/gene/100361568 HOIP:HOIP_1000519 NCBI-Human-GeneID:3161 NCBI-Mouse-GeneID:15366 NCBI-Rat-GeneID:25460 HMMR (mol) HOIP_1000519 NCBI-Human-GeneID:3161 http://www.ncbi.nlm.nih.gov/gene/3161 NCBI-Mouse-GeneID:15366 http://www.ncbi.nlm.nih.gov/gene/15366 NCBI-Rat-GeneID:25460 http://www.ncbi.nlm.nih.gov/gene/25460 HOIP:HOIP_1000520 NCBI-Human-GeneID:9768 KIAA0101 (mol) HOIP_1000520 NCBI-Human-GeneID:9768 http://www.ncbi.nlm.nih.gov/gene/9768 HOIP:HOIP_1000521 NCBI-Human-GeneID:283131 NCBI-Mouse-GeneID:66961 NEAT1 (mol) HOIP_1000521 NCBI-Human-GeneID:283131 http://www.ncbi.nlm.nih.gov/gene/283131 NCBI-Mouse-GeneID:66961 http://www.ncbi.nlm.nih.gov/gene/66961 HOIP:HOIP_1000522 NCBI-Human-GeneID:23594 NCBI-Mouse-GeneID:56452 NCBI-Rat-GeneID:291927 ORC6 (mol) HOIP_1000522 NCBI-Human-GeneID:23594 http://www.ncbi.nlm.nih.gov/gene/23594 NCBI-Mouse-GeneID:56452 http://www.ncbi.nlm.nih.gov/gene/56452 NCBI-Rat-GeneID:291927 http://www.ncbi.nlm.nih.gov/gene/291927 HOIP:HOIP_1000523 NCBI-Human-GeneID:64081 NCBI-Mouse-GeneID:68371 NCBI-Rat-GeneID:171564 PBLD (mol) HOIP_1000523 NCBI-Human-GeneID:64081 http://www.ncbi.nlm.nih.gov/gene/64081 NCBI-Mouse-GeneID:68371 http://www.ncbi.nlm.nih.gov/gene/68371 NCBI-Rat-GeneID:171564 http://www.ncbi.nlm.nih.gov/gene/171564 HOIP:HOIP_1000524 NCBI-Human-GeneID:5105 NCBI-Mouse-GeneID:18534 NCBI-Rat-GeneID:362282 PCK1 (mol) HOIP_1000524 NCBI-Human-GeneID:5105 http://www.ncbi.nlm.nih.gov/gene/5105 NCBI-Mouse-GeneID:18534 http://www.ncbi.nlm.nih.gov/gene/18534 NCBI-Rat-GeneID:362282 http://www.ncbi.nlm.nih.gov/gene/362282 HOIP:HOIP_1000525 NCBI-Human-GeneID:415116 NCBI-Mouse-GeneID:223775 NCBI-Rat-GeneID:64534 PIM3 (mol) HOIP_1000525 NCBI-Human-GeneID:415116 http://www.ncbi.nlm.nih.gov/gene/415116 NCBI-Mouse-GeneID:223775 http://www.ncbi.nlm.nih.gov/gene/223775 NCBI-Rat-GeneID:64534 http://www.ncbi.nlm.nih.gov/gene/64534 HOIP:HOIP_1000526 NCBI-Human-GeneID:5366 NCBI-Mouse-GeneID:58801 NCBI-Rat-GeneID:492821 PMAIP1 (mol) HOIP_1000526 NCBI-Human-GeneID:5366 http://www.ncbi.nlm.nih.gov/gene/5366 NCBI-Mouse-GeneID:58801 http://www.ncbi.nlm.nih.gov/gene/58801 NCBI-Rat-GeneID:492821 http://www.ncbi.nlm.nih.gov/gene/492821 HOIP:HOIP_1000527 NCBI-Human-GeneID:5789 NCBI-Mouse-GeneID:19266 NCBI-Rat-GeneID:313278 PTPRD (mol) HOIP_1000527 NCBI-Human-GeneID:5789 https://www.ncbi.nlm.nih.gov/gene/5789 NCBI-Mouse-GeneID:19266 https://www.ncbi.nlm.nih.gov/gene/19266 NCBI-Rat-GeneID:313278 https://www.ncbi.nlm.nih.gov/gene/313278 HOIP:HOIP_1000528 NCBI-Human-GeneID:10635 NCBI-Mouse-GeneID:19362 NCBI-Rat-GeneID:689055 RAD51AP1 (mol) HOIP_1000528 NCBI-Human-GeneID:10635 http://www.ncbi.nlm.nih.gov/gene/10635 NCBI-Mouse-GeneID:19362 http://www.ncbi.nlm.nih.gov/gene/19362 NCBI-Rat-GeneID:689055 http://www.ncbi.nlm.nih.gov/gene/689055 HOIP:HOIP_1000529 NCBI-Human-GeneID:83695 NCBI-Mouse-GeneID:72440 NCBI-Rat-GeneID:297627 RHNO1 (mol) HOIP_1000529 NCBI-Human-GeneID:83695 http://www.ncbi.nlm.nih.gov/gene/83695 NCBI-Mouse-GeneID:72440 http://www.ncbi.nlm.nih.gov/gene/72440 NCBI-Rat-GeneID:297627 http://www.ncbi.nlm.nih.gov/gene/297627 HOIP:HOIP_1000530 NCBI-Human-GeneID:6235 NCBI-Mouse-GeneID:20090 NCBI-Rat-GeneID:25348 RPS29 (mol) HOIP_1000530 NCBI-Human-GeneID:6235 http://www.ncbi.nlm.nih.gov/gene/6235 NCBI-Mouse-GeneID:20090 http://www.ncbi.nlm.nih.gov/gene/20090 NCBI-Rat-GeneID:25348 http://www.ncbi.nlm.nih.gov/gene/25348 HOIP:HOIP_1000531 NCBI-Human-GeneID:49855 NCBI-Mouse-GeneID:244891 NCBI-Rat-GeneID:117521 SCAPER (mol) HOIP_1000531 NCBI-Human-GeneID:49855 http://www.ncbi.nlm.nih.gov/gene/49855 NCBI-Mouse-GeneID:244891 http://www.ncbi.nlm.nih.gov/gene/244891 NCBI-Rat-GeneID:117521 http://www.ncbi.nlm.nih.gov/gene/117521 HOIP:HOIP_1000532 NCBI-Human-GeneID:6400 NCBI-Mouse-GeneID:20338 NCBI-Rat-GeneID:314352 SEL1L (mol) HOIP_1000532 NCBI-Human-GeneID:6400 http://www.ncbi.nlm.nih.gov/gene/6400 NCBI-Mouse-GeneID:20338 http://www.ncbi.nlm.nih.gov/gene/20338 NCBI-Rat-GeneID:314352 http://www.ncbi.nlm.nih.gov/gene/314352 HOIP:HOIP_1000533 NCBI-Human-GeneID:348235 NCBI-Mouse-GeneID:66140 NCBI-Rat-GeneID:287598 SKA2 (mol) HOIP_1000533 NCBI-Human-GeneID:348235 http://www.ncbi.nlm.nih.gov/gene/348235 NCBI-Mouse-GeneID:66140 http://www.ncbi.nlm.nih.gov/gene/66140 NCBI-Rat-GeneID:287598 http://www.ncbi.nlm.nih.gov/gene/287598 HOIP:HOIP_1000534 NCBI-Human-GeneID:55089 NCBI-Mouse-GeneID:69354 NCBI-Rat-GeneID:170573 SLC38A4 (mol) HOIP_1000534 NCBI-Human-GeneID:55089 http://www.ncbi.nlm.nih.gov/gene/55089 NCBI-Mouse-GeneID:69354 http://www.ncbi.nlm.nih.gov/gene/69354 NCBI-Rat-GeneID:170573 http://www.ncbi.nlm.nih.gov/gene/170573 HOIP:HOIP_1000535 NCBI-Human-GeneID:6519 NCBI-Mouse-GeneID:20532 NCBI-Rat-GeneID:29484 SLC3A1 (mol) HOIP_1000535 NCBI-Human-GeneID:6519 http://www.ncbi.nlm.nih.gov/gene/6519 NCBI-Mouse-GeneID:20532 http://www.ncbi.nlm.nih.gov/gene/20532 NCBI-Rat-GeneID:29484 http://www.ncbi.nlm.nih.gov/gene/29484 HOIP:HOIP_1000536 NCBI-Human-GeneID:55304 NCBI-Mouse-GeneID:228677 NCBI-Rat-GeneID:296188 SPTLC3 (mol) HOIP_1000536 NCBI-Human-GeneID:55304 http://www.ncbi.nlm.nih.gov/gene/55304 NCBI-Mouse-GeneID:228677 http://www.ncbi.nlm.nih.gov/gene/228677 NCBI-Rat-GeneID:296188 http://www.ncbi.nlm.nih.gov/gene/296188 HOIP:HOIP_1000537 NCBI-Human-GeneID:27286 NCBI-Mouse-GeneID:68792 NCBI-Rat-GeneID:317181 SRPX2 (mol) HOIP_1000537 NCBI-Human-GeneID:27286 http://www.ncbi.nlm.nih.gov/gene/27286 NCBI-Mouse-GeneID:68792 http://www.ncbi.nlm.nih.gov/gene/68792 NCBI-Rat-GeneID:317181 http://www.ncbi.nlm.nih.gov/gene/317181 HOIP:HOIP_1000538 NCBI-Human-GeneID:135932 NCBI-Mouse-GeneID:109218 NCBI-Rat-GeneID:680244 TMEM139 (mol) HOIP_1000538 NCBI-Human-GeneID:135932 http://www.ncbi.nlm.nih.gov/gene/135932 NCBI-Mouse-GeneID:109218 http://www.ncbi.nlm.nih.gov/gene/109218 NCBI-Rat-GeneID:680244 http://www.ncbi.nlm.nih.gov/gene/680244 HOIP:HOIP_1000539 NCBI-Human-GeneID:441027 NCBI-Mouse-GeneID:231503 NCBI-Rat-GeneID:360916 TMEM150C (mol) HOIP_1000539 NCBI-Human-GeneID:441027 http://www.ncbi.nlm.nih.gov/gene/441027 NCBI-Mouse-GeneID:231503 http://www.ncbi.nlm.nih.gov/gene/231503 NCBI-Rat-GeneID:360916 http://www.ncbi.nlm.nih.gov/gene/360916 HOIP:HOIP_1000540 NCBI-Human-GeneID:7112 NCBI-Mouse-GeneID:21917 NCBI-Rat-GeneID:25359 TMPO (mol) HOIP_1000540 NCBI-Human-GeneID:7112 http://www.ncbi.nlm.nih.gov/gene/7112 NCBI-Mouse-GeneID:21917 http://www.ncbi.nlm.nih.gov/gene/21917 NCBI-Rat-GeneID:25359 http://www.ncbi.nlm.nih.gov/gene/25359 HOIP:HOIP_1000541 NCBI-Human-GeneID:8743 NCBI-Mouse-GeneID:22035 NCBI-Rat-GeneID:246775 TNFSF10 (mol) HOIP_1000541 NCBI-Human-GeneID:8743 http://www.ncbi.nlm.nih.gov/gene/8743 NCBI-Mouse-GeneID:22035 http://www.ncbi.nlm.nih.gov/gene/22035 NCBI-Rat-GeneID:246775 http://www.ncbi.nlm.nih.gov/gene/246775 HOIP:HOIP_1000542 NCBI-Human-GeneID:84675 NCBI-Mouse-GeneID:381485 NCBI-Rat-GeneID:365751 TRIM55 (mol) HOIP_1000542 NCBI-Human-GeneID:84675 http://www.ncbi.nlm.nih.gov/gene/84675 NCBI-Mouse-GeneID:381485 http://www.ncbi.nlm.nih.gov/gene/381485 NCBI-Rat-GeneID:365751 http://www.ncbi.nlm.nih.gov/gene/365751 HOIP:HOIP_1000543 NCBI-Human-GeneID:25987 NCBI-Mouse-GeneID:244152 NCBI-Rat-GeneID:308843 TSKU (mol) HOIP_1000543 NCBI-Human-GeneID:25987 http://www.ncbi.nlm.nih.gov/gene/25987 NCBI-Mouse-GeneID:244152 http://www.ncbi.nlm.nih.gov/gene/244152 NCBI-Rat-GeneID:308843 http://www.ncbi.nlm.nih.gov/gene/308843 HOIP:HOIP_1000544 NCBI-Human-GeneID:22996 NCBI-Mouse-GeneID:230603 NCBI-Rat-GeneID:298366 TTC39A (mol) HOIP_1000544 NCBI-Human-GeneID:22996 http://www.ncbi.nlm.nih.gov/gene/22996 NCBI-Mouse-GeneID:230603 http://www.ncbi.nlm.nih.gov/gene/230603 NCBI-Rat-GeneID:298366 http://www.ncbi.nlm.nih.gov/gene/298366 HOIP:HOIP_1000545 NCBI-Human-GeneID:29089 NCBI-Mouse-GeneID:67196 NCBI-Rat-GeneID:360847 UBE2T (mol) HOIP_1000545 NCBI-Human-GeneID:29089 http://www.ncbi.nlm.nih.gov/gene/29089 NCBI-Mouse-GeneID:67196 http://www.ncbi.nlm.nih.gov/gene/67196 NCBI-Rat-GeneID:360847 http://www.ncbi.nlm.nih.gov/gene/360847 HOIP:HOIP_1000546 NCBI-Human-GeneID:79799 NCBI-Mouse-GeneID:72094 NCBI-Rat-GeneID:289533 UGT2A3 (mol) HOIP_1000546 NCBI-Human-GeneID:79799 http://www.ncbi.nlm.nih.gov/gene/79799 NCBI-Mouse-GeneID:72094 http://www.ncbi.nlm.nih.gov/gene/72094 NCBI-Rat-GeneID:289533 http://www.ncbi.nlm.nih.gov/gene/289533 HOIP:HOIP_1000547 NCBI-Human-GeneID:29128 NCBI-Mouse-GeneID:18140 NCBI-Rat-GeneID:316129 UHRF1 (mol) HOIP_1000547 NCBI-Human-GeneID:29128 http://www.ncbi.nlm.nih.gov/gene/29128 NCBI-Mouse-GeneID:18140 http://www.ncbi.nlm.nih.gov/gene/18140 NCBI-Rat-GeneID:316129 http://www.ncbi.nlm.nih.gov/gene/316129 BFO:0000001 Julius Caesar Verdi’s Requiem the Second World War your body mass index BFO 2 Reference: In all areas of empirical inquiry we encounter general terms of two sorts. First are general terms which refer to universals or types:animaltuberculosissurgical procedurediseaseSecond, are general terms used to refer to groups of entities which instantiate a given universal but do not correspond to the extension of any subuniversal of that universal because there is nothing intrinsic to the entities in question by virtue of which they – and only they – are counted as belonging to the given group. Examples are: animal purchased by the Emperortuberculosis diagnosed on a Wednesdaysurgical procedure performed on a patient from Stockholmperson identified as candidate for clinical trial #2056-555person who is signatory of Form 656-PPVpainting by Leonardo da VinciSuch terms, which represent what are called ‘specializations’ in [81 Entity doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. For example Werner Ceusters 'portions of reality' include 4 sorts, entities (as BFO construes them), universals, configurations, and relations. It is an open question as to whether entities as construed in BFO will at some point also include these other portions of reality. See, for example, 'How to track absolutely everything' at http://www.referent-tracking.com/_RTU/papers/CeustersICbookRevised.pdf An entity is anything that exists or has existed or will exist. (axiom label in BFO2 Reference: [001-001]) entity Entity doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. For example Werner Ceusters 'portions of reality' include 4 sorts, entities (as BFO construes them), universals, configurations, and relations. It is an open question as to whether entities as construed in BFO will at some point also include these other portions of reality. See, for example, 'How to track absolutely everything' at http://www.referent-tracking.com/_RTU/papers/CeustersICbookRevised.pdf per discussion with Barry Smith An entity is anything that exists or has existed or will exist. (axiom label in BFO2 Reference: [001-001]) BFO:0000002 BFO 2 Reference: Continuant entities are entities which can be sliced to yield parts only along the spatial dimension, yielding for example the parts of your table which we call its legs, its top, its nails. ‘My desk stretches from the window to the door. It has spatial parts, and can be sliced (in space) in two. With respect to time, however, a thing is a continuant.’ [60, p. 240 Continuant doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. For example, in an expansion involving bringing in some of Ceuster's other portions of reality, questions are raised as to whether universals are continuants A continuant is an entity that persists, endures, or continues to exist through time while maintaining its identity. (axiom label in BFO2 Reference: [008-002]) if b is a continuant and if, for some t, c has_continuant_part b at t, then c is a continuant. (axiom label in BFO2 Reference: [126-001]) if b is a continuant and if, for some t, cis continuant_part of b at t, then c is a continuant. (axiom label in BFO2 Reference: [009-002]) if b is a material entity, then there is some temporal interval (referred to below as a one-dimensional temporal region) during which b exists. (axiom label in BFO2 Reference: [011-002]) (forall (x y) (if (and (Continuant x) (exists (t) (continuantPartOfAt y x t))) (Continuant y))) // axiom label in BFO2 CLIF: [009-002] (forall (x y) (if (and (Continuant x) (exists (t) (hasContinuantPartOfAt y x t))) (Continuant y))) // axiom label in BFO2 CLIF: [126-001] (forall (x) (if (Continuant x) (Entity x))) // axiom label in BFO2 CLIF: [008-002] (forall (x) (if (Material Entity x) (exists (t) (and (TemporalRegion t) (existsAt x t))))) // axiom label in BFO2 CLIF: [011-002] continuant Continuant doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. For example, in an expansion involving bringing in some of Ceuster's other portions of reality, questions are raised as to whether universals are continuants A continuant is an entity that persists, endures, or continues to exist through time while maintaining its identity. (axiom label in BFO2 Reference: [008-002]) if b is a continuant and if, for some t, c has_continuant_part b at t, then c is a continuant. (axiom label in BFO2 Reference: [126-001]) if b is a continuant and if, for some t, cis continuant_part of b at t, then c is a continuant. (axiom label in BFO2 Reference: [009-002]) if b is a material entity, then there is some temporal interval (referred to below as a one-dimensional temporal region) during which b exists. (axiom label in BFO2 Reference: [011-002]) (forall (x y) (if (and (Continuant x) (exists (t) (continuantPartOfAt y x t))) (Continuant y))) // axiom label in BFO2 CLIF: [009-002] (forall (x y) (if (and (Continuant x) (exists (t) (hasContinuantPartOfAt y x t))) (Continuant y))) // axiom label in BFO2 CLIF: [126-001] (forall (x) (if (Continuant x) (Entity x))) // axiom label in BFO2 CLIF: [008-002] (forall (x) (if (Material Entity x) (exists (t) (and (TemporalRegion t) (existsAt x t))))) // axiom label in BFO2 CLIF: [011-002] BFO:0000003 BFO 2 Reference: every occurrent that is not a temporal or spatiotemporal region is s-dependent on some independent continuant that is not a spatial region BFO 2 Reference: s-dependence obtains between every process and its participants in the sense that, as a matter of necessity, this process could not have existed unless these or those participants existed also. A process may have a succession of participants at different phases of its unfolding. Thus there may be different players on the field at different times during the course of a football game; but the process which is the entire game s-depends_on all of these players nonetheless. Some temporal parts of this process will s-depend_on on only some of the players. Occurrent doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. An example would be the sum of a process and the process boundary of another process. Simons uses different terminology for relations of occurrents to regions: Denote the spatio-temporal location of a given occurrent e by 'spn[e]' and call this region its span. We may say an occurrent is at its span, in any larger region, and covers any smaller region. Now suppose we have fixed a frame of reference so that we can speak not merely of spatio-temporal but also of spatial regions (places) and temporal regions (times). The spread of an occurrent, (relative to a frame of reference) is the space it exactly occupies, and its spell is likewise the time it exactly occupies. We write 'spr[e]' and `spl[e]' respectively for the spread and spell of e, omitting mention of the frame. An occurrent is an entity that unfolds itself in time or it is the instantaneous boundary of such an entity (for example a beginning or an ending) or it is a temporal or spatiotemporal region which such an entity occupies_temporal_region or occupies_spatiotemporal_region. (axiom label in BFO2 Reference: [077-002]) Every occurrent occupies_spatiotemporal_region some spatiotemporal region. (axiom label in BFO2 Reference: [108-001]) b is an occurrent entity iff b is an entity that has temporal parts. (axiom label in BFO2 Reference: [079-001]) (forall (x) (if (Occurrent x) (exists (r) (and (SpatioTemporalRegion r) (occupiesSpatioTemporalRegion x r))))) // axiom label in BFO2 CLIF: [108-001] (forall (x) (iff (Occurrent x) (and (Entity x) (exists (y) (temporalPartOf y x))))) // axiom label in BFO2 CLIF: [079-001] occurrent Occurrent doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. An example would be the sum of a process and the process boundary of another process. per discussion with Barry Smith Simons uses different terminology for relations of occurrents to regions: Denote the spatio-temporal location of a given occurrent e by 'spn[e]' and call this region its span. We may say an occurrent is at its span, in any larger region, and covers any smaller region. Now suppose we have fixed a frame of reference so that we can speak not merely of spatio-temporal but also of spatial regions (places) and temporal regions (times). The spread of an occurrent, (relative to a frame of reference) is the space it exactly occupies, and its spell is likewise the time it exactly occupies. We write 'spr[e]' and `spl[e]' respectively for the spread and spell of e, omitting mention of the frame. An occurrent is an entity that unfolds itself in time or it is the instantaneous boundary of such an entity (for example a beginning or an ending) or it is a temporal or spatiotemporal region which such an entity occupies_temporal_region or occupies_spatiotemporal_region. (axiom label in BFO2 Reference: [077-002]) Every occurrent occupies_spatiotemporal_region some spatiotemporal region. (axiom label in BFO2 Reference: [108-001]) b is an occurrent entity iff b is an entity that has temporal parts. (axiom label in BFO2 Reference: [079-001]) (forall (x) (if (Occurrent x) (exists (r) (and (SpatioTemporalRegion r) (occupiesSpatioTemporalRegion x r))))) // axiom label in BFO2 CLIF: [108-001] (forall (x) (iff (Occurrent x) (and (Entity x) (exists (y) (temporalPartOf y x))))) // axiom label in BFO2 CLIF: [079-001] BFO:0000004 a chair a heart a leg a molecule a spatial region an atom an orchestra. an organism the bottom right portion of a human torso the interior of your mouth b is an independent continuant = Def. b is a continuant which is such that there is no c and no t such that b s-depends_on c at t. (axiom label in BFO2 Reference: [017-002]) For any independent continuant b and any time t there is some spatial region r such that b is located_in r at t. (axiom label in BFO2 Reference: [134-001]) For every independent continuant b and time t during the region of time spanned by its life, there are entities which s-depends_on b during t. (axiom label in BFO2 Reference: [018-002]) (forall (x t) (if (IndependentContinuant x) (exists (r) (and (SpatialRegion r) (locatedInAt x r t))))) // axiom label in BFO2 CLIF: [134-001] (forall (x t) (if (and (IndependentContinuant x) (existsAt x t)) (exists (y) (and (Entity y) (specificallyDependsOnAt y x t))))) // axiom label in BFO2 CLIF: [018-002] (iff (IndependentContinuant a) (and (Continuant a) (not (exists (b t) (specificallyDependsOnAt a b t))))) // axiom label in BFO2 CLIF: [017-002] independent continuant b is an independent continuant = Def. b is a continuant which is such that there is no c and no t such that b s-depends_on c at t. (axiom label in BFO2 Reference: [017-002]) For any independent continuant b and any time t there is some spatial region r such that b is located_in r at t. (axiom label in BFO2 Reference: [134-001]) For every independent continuant b and time t during the region of time spanned by its life, there are entities which s-depends_on b during t. (axiom label in BFO2 Reference: [018-002]) (forall (x t) (if (IndependentContinuant x) (exists (r) (and (SpatialRegion r) (locatedInAt x r t))))) // axiom label in BFO2 CLIF: [134-001] (forall (x t) (if (and (IndependentContinuant x) (existsAt x t)) (exists (y) (and (Entity y) (specificallyDependsOnAt y x t))))) // axiom label in BFO2 CLIF: [018-002] (iff (IndependentContinuant a) (and (Continuant a) (not (exists (b t) (specificallyDependsOnAt a b t))))) // axiom label in BFO2 CLIF: [017-002] BFO:0000006 BFO 2 Reference: Spatial regions do not participate in processes. Spatial region doesn't have a closure axiom because the subclasses don't exhaust all possibilites. An example would be the union of a spatial point and a spatial line that doesn't overlap the point, or two spatial lines that intersect at a single point. In both cases the resultant spatial region is neither 0-dimensional, 1-dimensional, 2-dimensional, or 3-dimensional. A spatial region is a continuant entity that is a continuant_part_of spaceR as defined relative to some frame R. (axiom label in BFO2 Reference: [035-001]) All continuant parts of spatial regions are spatial regions. (axiom label in BFO2 Reference: [036-001]) (forall (x y t) (if (and (SpatialRegion x) (continuantPartOfAt y x t)) (SpatialRegion y))) // axiom label in BFO2 CLIF: [036-001] (forall (x) (if (SpatialRegion x) (Continuant x))) // axiom label in BFO2 CLIF: [035-001] spatial region Spatial region doesn't have a closure axiom because the subclasses don't exhaust all possibilites. An example would be the union of a spatial point and a spatial line that doesn't overlap the point, or two spatial lines that intersect at a single point. In both cases the resultant spatial region is neither 0-dimensional, 1-dimensional, 2-dimensional, or 3-dimensional. per discussion with Barry Smith A spatial region is a continuant entity that is a continuant_part_of spaceR as defined relative to some frame R. (axiom label in BFO2 Reference: [035-001]) All continuant parts of spatial regions are spatial regions. (axiom label in BFO2 Reference: [036-001]) (forall (x y t) (if (and (SpatialRegion x) (continuantPartOfAt y x t)) (SpatialRegion y))) // axiom label in BFO2 CLIF: [036-001] (forall (x) (if (SpatialRegion x) (Continuant x))) // axiom label in BFO2 CLIF: [035-001] BFO:0000008 Temporal region doesn't have a closure axiom because the subclasses don't exhaust all possibilites. An example would be the mereological sum of a temporal instant and a temporal interval that doesn't overlap the instant. In this case the resultant temporal region is neither 0-dimensional nor 1-dimensional A temporal region is an occurrent entity that is part of time as defined relative to some reference frame. (axiom label in BFO2 Reference: [100-001]) All parts of temporal regions are temporal regions. (axiom label in BFO2 Reference: [101-001]) Every temporal region t is such that t occupies_temporal_region t. (axiom label in BFO2 Reference: [119-002]) (forall (r) (if (TemporalRegion r) (occupiesTemporalRegion r r))) // axiom label in BFO2 CLIF: [119-002] (forall (x y) (if (and (TemporalRegion x) (occurrentPartOf y x)) (TemporalRegion y))) // axiom label in BFO2 CLIF: [101-001] (forall (x) (if (TemporalRegion x) (Occurrent x))) // axiom label in BFO2 CLIF: [100-001] temporal region Temporal region doesn't have a closure axiom because the subclasses don't exhaust all possibilites. An example would be the mereological sum of a temporal instant and a temporal interval that doesn't overlap the instant. In this case the resultant temporal region is neither 0-dimensional nor 1-dimensional per discussion with Barry Smith A temporal region is an occurrent entity that is part of time as defined relative to some reference frame. (axiom label in BFO2 Reference: [100-001]) All parts of temporal regions are temporal regions. (axiom label in BFO2 Reference: [101-001]) Every temporal region t is such that t occupies_temporal_region t. (axiom label in BFO2 Reference: [119-002]) (forall (r) (if (TemporalRegion r) (occupiesTemporalRegion r r))) // axiom label in BFO2 CLIF: [119-002] (forall (x y) (if (and (TemporalRegion x) (occurrentPartOf y x)) (TemporalRegion y))) // axiom label in BFO2 CLIF: [101-001] (forall (x) (if (TemporalRegion x) (Occurrent x))) // axiom label in BFO2 CLIF: [100-001] BFO:0000009 an infinitely thin plane in space. the surface of a sphere-shaped part of space A two-dimensional spatial region is a spatial region that is of two dimensions. (axiom label in BFO2 Reference: [039-001]) A two-dimensional spatial region is a spatial region that is of two dimensions. (axiom label in BFO2 Reference: [039-001]) (forall (x) (if (TwoDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [039-001] two-dimensional spatial region A two-dimensional spatial region is a spatial region that is of two dimensions. (axiom label in BFO2 Reference: [039-001]) (forall (x) (if (TwoDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [039-001] BFO:0000011 the spatiotemporal region occupied by a human life the spatiotemporal region occupied by a process of cellular meiosis. the spatiotemporal region occupied by the development of a cancer tumor A spatiotemporal region is an occurrent entity that is part of spacetime. (axiom label in BFO2 Reference: [095-001]) All parts of spatiotemporal regions are spatiotemporal regions. (axiom label in BFO2 Reference: [096-001]) Each spatiotemporal region at any time t projects_onto some spatial region at t. (axiom label in BFO2 Reference: [099-001]) Each spatiotemporal region projects_onto some temporal region. (axiom label in BFO2 Reference: [098-001]) Every spatiotemporal region occupies_spatiotemporal_region itself. Every spatiotemporal region s is such that s occupies_spatiotemporal_region s. (axiom label in BFO2 Reference: [107-002]) (forall (r) (if (SpatioTemporalRegion r) (occupiesSpatioTemporalRegion r r))) // axiom label in BFO2 CLIF: [107-002] (forall (x t) (if (SpatioTemporalRegion x) (exists (y) (and (SpatialRegion y) (spatiallyProjectsOntoAt x y t))))) // axiom label in BFO2 CLIF: [099-001] (forall (x y) (if (and (SpatioTemporalRegion x) (occurrentPartOf y x)) (SpatioTemporalRegion y))) // axiom label in BFO2 CLIF: [096-001] (forall (x) (if (SpatioTemporalRegion x) (Occurrent x))) // axiom label in BFO2 CLIF: [095-001] (forall (x) (if (SpatioTemporalRegion x) (exists (y) (and (TemporalRegion y) (temporallyProjectsOnto x y))))) // axiom label in BFO2 CLIF: [098-001] spatiotemporal region A spatiotemporal region is an occurrent entity that is part of spacetime. (axiom label in BFO2 Reference: [095-001]) All parts of spatiotemporal regions are spatiotemporal regions. (axiom label in BFO2 Reference: [096-001]) Each spatiotemporal region at any time t projects_onto some spatial region at t. (axiom label in BFO2 Reference: [099-001]) Each spatiotemporal region projects_onto some temporal region. (axiom label in BFO2 Reference: [098-001]) Every spatiotemporal region s is such that s occupies_spatiotemporal_region s. (axiom label in BFO2 Reference: [107-002]) (forall (r) (if (SpatioTemporalRegion r) (occupiesSpatioTemporalRegion r r))) // axiom label in BFO2 CLIF: [107-002] (forall (x t) (if (SpatioTemporalRegion x) (exists (y) (and (SpatialRegion y) (spatiallyProjectsOntoAt x y t))))) // axiom label in BFO2 CLIF: [099-001] (forall (x y) (if (and (SpatioTemporalRegion x) (occurrentPartOf y x)) (SpatioTemporalRegion y))) // axiom label in BFO2 CLIF: [096-001] (forall (x) (if (SpatioTemporalRegion x) (Occurrent x))) // axiom label in BFO2 CLIF: [095-001] (forall (x) (if (SpatioTemporalRegion x) (exists (y) (and (TemporalRegion y) (temporallyProjectsOnto x y))))) // axiom label in BFO2 CLIF: [098-001] BFO:0000015 a process of cell-division, \ a beating of the heart a process of meiosis a process of sleeping the course of a disease the life of an organism your process of aging. p is a process = Def. p is an occurrent that has temporal proper parts and for some time t, p s-depends_on some material entity at t. (axiom label in BFO2 Reference: [083-003]) BFO 2 Reference: The realm of occurrents is less pervasively marked by the presence of natural units than is the case in the realm of independent continuants. Thus there is here no counterpart of ‘object’. In BFO 1.0 ‘process’ served as such a counterpart. In BFO 2.0 ‘process’ is, rather, the occurrent counterpart of ‘material entity’. Those natural – as contrasted with engineered, which here means: deliberately executed – units which do exist in the realm of occurrents are typically either parasitic on the existence of natural units on the continuant side, or they are fiat in nature. Thus we can count lives; we can count football games; we can count chemical reactions performed in experiments or in chemical manufacturing. We cannot count the processes taking place, for instance, in an episode of insect mating behavior.Even where natural units are identifiable, for example cycles in a cyclical process such as the beating of a heart or an organism’s sleep/wake cycle, the processes in question form a sequence with no discontinuities (temporal gaps) of the sort that we find for instance where billiard balls or zebrafish or planets are separated by clear spatial gaps. Lives of organisms are process units, but they too unfold in a continuous series from other, prior processes such as fertilization, and they unfold in turn in continuous series of post-life processes such as post-mortem decay. Clear examples of boundaries of processes are almost always of the fiat sort (midnight, a time of death as declared in an operating theater or on a death certificate, the initiation of a state of war) Superclass of unit process(primitive process) and senquence processes. It is dissective and has no unity, and hence it can change. It follows A-series of time. (iff (Process a) (and (Occurrent a) (exists (b) (properTemporalPartOf b a)) (exists (c t) (and (MaterialEntity c) (specificallyDependsOnAt a c t))))) // axiom label in BFO2 CLIF: [083-003] process p is a process = Def. p is an occurrent that has temporal proper parts and for some time t, p s-depends_on some material entity at t. (axiom label in BFO2 Reference: [083-003]) Superclass of unit process(primitive process) and senquence processes. It is dissective and has no unity, and hence it can change. It follows A-series of time. YAMATO ontology (iff (Process a) (and (Occurrent a) (exists (b) (properTemporalPartOf b a)) (exists (c t) (and (MaterialEntity c) (specificallyDependsOnAt a c t))))) // axiom label in BFO2 CLIF: [083-003] BFO:0000016 an atom of element X has the disposition to decay to an atom of element Y certain people have a predisposition to colon cancer children are innately disposed to categorize objects in certain ways. the cell wall is disposed to filter chemicals in endocytosis and exocytosis BFO 2 Reference: Dispositions exist along a strength continuum. Weaker forms of disposition are realized in only a fraction of triggering cases. These forms occur in a significant number of cases of a similar type. b is a disposition means: b is a realizable entity & b’s bearer is some material entity & b is such that if it ceases to exist, then its bearer is physically changed, & b’s realization occurs when and because this bearer is in some special physical circumstances, & this realization occurs in virtue of the bearer’s physical make-up. (axiom label in BFO2 Reference: [062-002]) b is a disposition means: b is a realizable entity & b’s bearer is some material entity & b is such that if it ceases to exist, then its bearer is physically changed, & b’s realization occurs when and because this bearer is in some special physical circumstances, & this realization occurs in virtue of the bearer’s physical make-up. (axiom label in BFO2 Reference: [062-002]) If b is a realizable entity then for all t at which b exists, b s-depends_on some material entity at t. (axiom label in BFO2 Reference: [063-002]) (forall (x t) (if (and (RealizableEntity x) (existsAt x t)) (exists (y) (and (MaterialEntity y) (specificallyDepends x y t))))) // axiom label in BFO2 CLIF: [063-002] (forall (x) (if (Disposition x) (and (RealizableEntity x) (exists (y) (and (MaterialEntity y) (bearerOfAt x y t)))))) // axiom label in BFO2 CLIF: [062-002] disposition b is a disposition means: b is a realizable entity & b’s bearer is some material entity & b is such that if it ceases to exist, then its bearer is physically changed, & b’s realization occurs when and because this bearer is in some special physical circumstances, & this realization occurs in virtue of the bearer’s physical make-up. (axiom label in BFO2 Reference: [062-002]) If b is a realizable entity then for all t at which b exists, b s-depends_on some material entity at t. (axiom label in BFO2 Reference: [063-002]) (forall (x t) (if (and (RealizableEntity x) (existsAt x t)) (exists (y) (and (MaterialEntity y) (specificallyDepends x y t))))) // axiom label in BFO2 CLIF: [063-002] (forall (x) (if (Disposition x) (and (RealizableEntity x) (exists (y) (and (MaterialEntity y) (bearerOfAt x y t)))))) // axiom label in BFO2 CLIF: [062-002] BFO:0000017 the disposition of this piece of metal to conduct electricity. the disposition of your blood to coagulate the function of your reproductive organs the role of being a doctor the role of this boundary to delineate where Utah and Colorado meet To say that b is a realizable entity is to say that b is a specifically dependent continuant that inheres in some independent continuant which is not a spatial region and is of a type instances of which are realized in processes of a correlated type. (axiom label in BFO2 Reference: [058-002]) All realizable dependent continuants have independent continuants that are not spatial regions as their bearers. (axiom label in BFO2 Reference: [060-002]) (forall (x t) (if (RealizableEntity x) (exists (y) (and (IndependentContinuant y) (not (SpatialRegion y)) (bearerOfAt y x t))))) // axiom label in BFO2 CLIF: [060-002] (forall (x) (if (RealizableEntity x) (and (SpecificallyDependentContinuant x) (exists (y) (and (IndependentContinuant y) (not (SpatialRegion y)) (inheresIn x y)))))) // axiom label in BFO2 CLIF: [058-002] realizable entity To say that b is a realizable entity is to say that b is a specifically dependent continuant that inheres in some independent continuant which is not a spatial region and is of a type instances of which are realized in processes of a correlated type. (axiom label in BFO2 Reference: [058-002]) All realizable dependent continuants have independent continuants that are not spatial regions as their bearers. (axiom label in BFO2 Reference: [060-002]) (forall (x t) (if (RealizableEntity x) (exists (y) (and (IndependentContinuant y) (not (SpatialRegion y)) (bearerOfAt y x t))))) // axiom label in BFO2 CLIF: [060-002] (forall (x) (if (RealizableEntity x) (and (SpecificallyDependentContinuant x) (exists (y) (and (IndependentContinuant y) (not (SpatialRegion y)) (inheresIn x y)))))) // axiom label in BFO2 CLIF: [058-002] BFO:0000018 A zero-dimensional spatial region is a point in space. (axiom label in BFO2 Reference: [037-001]) A zero-dimensional spatial region is a point in space. (axiom label in BFO2 Reference: [037-001]) (forall (x) (if (ZeroDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [037-001] zero-dimensional spatial region A zero-dimensional spatial region is a point in space. (axiom label in BFO2 Reference: [037-001]) (forall (x) (if (ZeroDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [037-001] BFO:0000019 the ambient temperature of this portion of air the color of a tomato the length of the circumference of your waist the mass of this piece of gold. the shape of your nose the shape of your nostril a quality is a specifically dependent continuant that, in contrast to roles and dispositions, does not require any further process in order to be realized. (axiom label in BFO2 Reference: [055-001]) If an entity is a quality at any time that it exists, then it is a quality at every time that it exists. (axiom label in BFO2 Reference: [105-001]) (forall (x) (if (Quality x) (SpecificallyDependentContinuant x))) // axiom label in BFO2 CLIF: [055-001] (forall (x) (if (exists (t) (and (existsAt x t) (Quality x))) (forall (t_1) (if (existsAt x t_1) (Quality x))))) // axiom label in BFO2 CLIF: [105-001] YAMATO:property quality a quality is a specifically dependent continuant that, in contrast to roles and dispositions, does not require any further process in order to be realized. (axiom label in BFO2 Reference: [055-001]) If an entity is a quality at any time that it exists, then it is a quality at every time that it exists. (axiom label in BFO2 Reference: [105-001]) (forall (x) (if (Quality x) (SpecificallyDependentContinuant x))) // axiom label in BFO2 CLIF: [055-001] (forall (x) (if (exists (t) (and (existsAt x t) (Quality x))) (forall (t_1) (if (existsAt x t_1) (Quality x))))) // axiom label in BFO2 CLIF: [105-001] BFO:0000020 Reciprocal specifically dependent continuants: the function of this key to open this lock and the mutually dependent disposition of this lock: to be opened by this key of one-sided specifically dependent continuants: the mass of this tomato of relational dependent continuants (multiple bearers): John’s love for Mary, the ownership relation between John and this statue, the relation of authority between John and his subordinates. the disposition of this fish to decay the function of this heart: to pump blood the mutual dependence of proton donors and acceptors in chemical reactions [79 the mutual dependence of the role predator and the role prey as played by two organisms in a given interaction the pink color of a medium rare piece of grilled filet mignon at its center the role of being a doctor the shape of this hole. the smell of this portion of mozzarella b is a specifically dependent continuant = Def. b is a continuant & there is some independent continuant c which is not a spatial region and which is such that b s-depends_on c at every time t during the course of b’s existence. (axiom label in BFO2 Reference: [050-003]) Specifically dependent continuant doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. We're not sure what else will develop here, but for example there are questions such as what are promises, obligation, etc. (iff (SpecificallyDependentContinuant a) (and (Continuant a) (forall (t) (if (existsAt a t) (exists (b) (and (IndependentContinuant b) (not (SpatialRegion b)) (specificallyDependsOnAt a b t))))))) // axiom label in BFO2 CLIF: [050-003] specifically dependent continuant b is a specifically dependent continuant = Def. b is a continuant & there is some independent continuant c which is not a spatial region and which is such that b s-depends_on c at every time t during the course of b’s existence. (axiom label in BFO2 Reference: [050-003]) Specifically dependent continuant doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. We're not sure what else will develop here, but for example there are questions such as what are promises, obligation, etc. per discussion with Barry Smith (iff (SpecificallyDependentContinuant a) (and (Continuant a) (forall (t) (if (existsAt a t) (exists (b) (and (IndependentContinuant b) (not (SpatialRegion b)) (specificallyDependsOnAt a b t))))))) // axiom label in BFO2 CLIF: [050-003] BFO:0000023 John’s role of husband to Mary is dependent on Mary’s role of wife to John, and both are dependent on the object aggregate comprising John and Mary as member parts joined together through the relational quality of being married. the priest role the role of a boundary to demarcate two neighboring administrative territories the role of a building in serving as a military target the role of a stone in marking a property boundary the role of subject in a clinical trial the student role BFO 2 Reference: One major family of examples of non-rigid universals involves roles, and ontologies developed for corresponding administrative purposes may consist entirely of representatives of entities of this sort. Thus ‘professor’, defined as follows,b instance_of professor at t =Def. there is some c, c instance_of professor role & c inheres_in b at t.denotes a non-rigid universal and so also do ‘nurse’, ‘student’, ‘colonel’, ‘taxpayer’, and so forth. (These terms are all, in the jargon of philosophy, phase sortals.) By using role terms in definitions, we can create a BFO conformant treatment of such entities drawing on the fact that, while an instance of professor may be simultaneously an instance of trade union member, no instance of the type professor role is also (at any time) an instance of the type trade union member role (any more than any instance of the type color is at any time an instance of the type length).If an ontology of employment positions should be defined in terms of roles following the above pattern, this enables the ontology to do justice to the fact that individuals instantiate the corresponding universals – professor, sergeant, nurse – only during certain phases in their lives. b is a role means: b is a realizable entity & b exists because there is some single bearer that is in some special physical, social, or institutional set of circumstances in which this bearer does not have to be& b is not such that, if it ceases to exist, then the physical make-up of the bearer is thereby changed. (axiom label in BFO2 Reference: [061-001]) b is a role means: b is a realizable entity & b exists because there is some single bearer that is in some special physical, social, or institutional set of circumstances in which this bearer does not have to be& b is not such that, if it ceases to exist, then the physical make-up of the bearer is thereby changed. (axiom label in BFO2 Reference: [061-001]) (forall (x) (if (Role x) (RealizableEntity x))) // axiom label in BFO2 CLIF: [061-001] role b is a role means: b is a realizable entity & b exists because there is some single bearer that is in some special physical, social, or institutional set of circumstances in which this bearer does not have to be& b is not such that, if it ceases to exist, then the physical make-up of the bearer is thereby changed. (axiom label in BFO2 Reference: [061-001]) (forall (x) (if (Role x) (RealizableEntity x))) // axiom label in BFO2 CLIF: [061-001] BFO:0000024 or with divisions drawn by cognitive subjects for practical reasons, such as the division of a cake (before slicing) into (what will become) slices (and thus member parts of an object aggregate). However, this does not mean that fiat object parts are dependent for their existence on divisions or delineations effected by cognitive subjects. If, for example, it is correct to conceive geological layers of the Earth as fiat object parts of the Earth, then even though these layers were first delineated in recent times, still existed long before such delineation and what holds of these layers (for example that the oldest layers are also the lowest layers) did not begin to hold because of our acts of delineation.Treatment of material entity in BFOExamples viewed by some as problematic cases for the trichotomy of fiat object part, object, and object aggregate include: a mussel on (and attached to) a rock, a slime mold, a pizza, a cloud, a galaxy, a railway train with engine and multiple carriages, a clonal stand of quaking aspen, a bacterial community (biofilm), a broken femur. Note that, as Aristotle already clearly recognized, such problematic cases – which lie at or near the penumbra of instances defined by the categories in question – need not invalidate these categories. The existence of grey objects does not prove that there are not objects which are black and objects which are white; the existence of mules does not prove that there are not objects which are donkeys and objects which are horses. It does, however, show that the examples in question need to be addressed carefully in order to show how they can be fitted into the proposed scheme, for example by recognizing additional subdivisions [29 the FMA:regional parts of an intact human body. the Western hemisphere of the Earth the division of the brain into regions the division of the planet into hemispheres the dorsal and ventral surfaces of the body the upper and lower lobes of the left lung BFO 2 Reference: Most examples of fiat object parts are associated with theoretically drawn divisions b is a fiat object part = Def. b is a material entity which is such that for all times t, if b exists at t then there is some object c such that b proper continuant_part of c at t and c is demarcated from the remainder of c by a two-dimensional continuant fiat boundary. (axiom label in BFO2 Reference: [027-004]) (forall (x) (if (FiatObjectPart x) (and (MaterialEntity x) (forall (t) (if (existsAt x t) (exists (y) (and (Object y) (properContinuantPartOfAt x y t)))))))) // axiom label in BFO2 CLIF: [027-004] fiat object part b is a fiat object part = Def. b is a material entity which is such that for all times t, if b exists at t then there is some object c such that b proper continuant_part of c at t and c is demarcated from the remainder of c by a two-dimensional continuant fiat boundary. (axiom label in BFO2 Reference: [027-004]) (forall (x) (if (FiatObjectPart x) (and (MaterialEntity x) (forall (t) (if (existsAt x t) (exists (y) (and (Object y) (properContinuantPartOfAt x y t)))))))) // axiom label in BFO2 CLIF: [027-004] BFO:0000026 an edge of a cube-shaped portion of space. A one-dimensional spatial region is a line or aggregate of lines stretching from one point in space to another. (axiom label in BFO2 Reference: [038-001]) A one-dimensional spatial region is a line or aggregate of lines stretching from one point in space to another. (axiom label in BFO2 Reference: [038-001]) (forall (x) (if (OneDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [038-001] one-dimensional spatial region A one-dimensional spatial region is a line or aggregate of lines stretching from one point in space to another. (axiom label in BFO2 Reference: [038-001]) (forall (x) (if (OneDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [038-001] BFO:0000027 a collection of cells in a blood biobank. a swarm of bees is an aggregate of members who are linked together through natural bonds a symphony orchestra an organization is an aggregate whose member parts have roles of specific types (for example in a jazz band, a chess club, a football team) defined by fiat: the aggregate of members of an organization defined through physical attachment: the aggregate of atoms in a lump of granite defined through physical containment: the aggregate of molecules of carbon dioxide in a sealed container defined via attributive delimitations such as: the patients in this hospital the aggregate of bearings in a constant velocity axle joint the aggregate of blood cells in your body the nitrogen atoms in the atmosphere the restaurants in Palo Alto your collection of Meissen ceramic plates. An entity a is an object aggregate if and only if there is a mutually exhaustive and pairwise disjoint partition of a into objects BFO 2 Reference: object aggregates may gain and lose parts while remaining numerically identical (one and the same individual) over time. This holds both for aggregates whose membership is determined naturally (the aggregate of cells in your body) and aggregates determined by fiat (a baseball team, a congressional committee). ISBN:978-3-938793-98-5pp124-158#Thomas Bittner and Barry Smith, 'A Theory of Granular Partitions', in K. Munn and B. Smith (eds.), Applied Ontology: An Introduction, Frankfurt/Lancaster: ontos, 2008, 125-158. b is an object aggregate means: b is a material entity consisting exactly of a plurality of objects as member_parts at all times at which b exists. (axiom label in BFO2 Reference: [025-004]) (forall (x) (if (ObjectAggregate x) (and (MaterialEntity x) (forall (t) (if (existsAt x t) (exists (y z) (and (Object y) (Object z) (memberPartOfAt y x t) (memberPartOfAt z x t) (not (= y z)))))) (not (exists (w t_1) (and (memberPartOfAt w x t_1) (not (Object w)))))))) // axiom label in BFO2 CLIF: [025-004] object aggregate An entity a is an object aggregate if and only if there is a mutually exhaustive and pairwise disjoint partition of a into objects An entity a is an object aggregate if and only if there is a mutually exhaustive and pairwise disjoint partition of a into objects ISBN:978-3-938793-98-5pp124-158#Thomas Bittner and Barry Smith, 'A Theory of Granular Partitions', in K. Munn and B. Smith (eds.), Applied Ontology: An Introduction, Frankfurt/Lancaster: ontos, 2008, 125-158. b is an object aggregate means: b is a material entity consisting exactly of a plurality of objects as member_parts at all times at which b exists. (axiom label in BFO2 Reference: [025-004]) (forall (x) (if (ObjectAggregate x) (and (MaterialEntity x) (forall (t) (if (existsAt x t) (exists (y z) (and (Object y) (Object z) (memberPartOfAt y x t) (memberPartOfAt z x t) (not (= y z)))))) (not (exists (w t_1) (and (memberPartOfAt w x t_1) (not (Object w)))))))) // axiom label in BFO2 CLIF: [025-004] BFO:0000028 a cube-shaped region of space a sphere-shaped region of space, A three-dimensional spatial region is a spatial region that is of three dimensions. (axiom label in BFO2 Reference: [040-001]) A three-dimensional spatial region is a spatial region that is of three dimensions. (axiom label in BFO2 Reference: [040-001]) (forall (x) (if (ThreeDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [040-001] three-dimensional spatial region A three-dimensional spatial region is a spatial region that is of three dimensions. (axiom label in BFO2 Reference: [040-001]) (forall (x) (if (ThreeDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [040-001] BFO:0000029 Manhattan Canyon) a hole in the interior of a portion of cheese a rabbit hole an air traffic control region defined in the airspace above an airport the Grand Canyon the Piazza San Marco the cockpit of an aircraft the hold of a ship the interior of a kangaroo pouch the interior of the trunk of your car the interior of your bedroom the interior of your office the interior of your refrigerator the lumen of your gut your left nostril (a fiat part – the opening – of your left nasal cavity) b is a site means: b is a three-dimensional immaterial entity that is (partially or wholly) bounded by a material entity or it is a three-dimensional immaterial part thereof. (axiom label in BFO2 Reference: [034-002]) (forall (x) (if (Site x) (ImmaterialEntity x))) // axiom label in BFO2 CLIF: [034-002] site b is a site means: b is a three-dimensional immaterial entity that is (partially or wholly) bounded by a material entity or it is a three-dimensional immaterial part thereof. (axiom label in BFO2 Reference: [034-002]) (forall (x) (if (Site x) (ImmaterialEntity x))) // axiom label in BFO2 CLIF: [034-002] BFO:0000030 atom cell cells and organisms engineered artifacts grain of sand molecule organelle organism planet solid portions of matter star BFO 2 Reference: BFO rests on the presupposition that at multiple micro-, meso- and macroscopic scales reality exhibits certain stable, spatially separated or separable material units, combined or combinable into aggregates of various sorts (for example organisms into what are called ‘populations’). Such units play a central role in almost all domains of natural science from particle physics to cosmology. Many scientific laws govern the units in question, employing general terms (such as ‘molecule’ or ‘planet’) referring to the types and subtypes of units, and also to the types and subtypes of the processes through which such units develop and interact. The division of reality into such natural units is at the heart of biological science, as also is the fact that these units may form higher-level units (as cells form multicellular organisms) and that they may also form aggregates of units, for example as cells form portions of tissue and organs form families, herds, breeds, species, and so on. At the same time, the division of certain portions of reality into engineered units (manufactured artifacts) is the basis of modern industrial technology, which rests on the distributed mass production of engineered parts through division of labor and on their assembly into larger, compound units such as cars and laptops. The division of portions of reality into units is one starting point for the phenomenon of counting. BFO 2 Reference: Each object is such that there are entities of which we can assert unproblematically that they lie in its interior, and other entities of which we can assert unproblematically that they lie in its exterior. This may not be so for entities lying at or near the boundary between the interior and exterior. This means that two objects – for example the two cells depicted in Figure 3 – may be such that there are material entities crossing their boundaries which belong determinately to neither cell. Something similar obtains in certain cases of conjoined twins (see below). BFO 2 Reference: To say that b is causally unified means: b is a material entity which is such that its material parts are tied together in such a way that, in environments typical for entities of the type in question,if c, a continuant part of b that is in the interior of b at t, is larger than a certain threshold size (which will be determined differently from case to case, depending on factors such as porosity of external cover) and is moved in space to be at t at a location on the exterior of the spatial region that had been occupied by b at t, then either b’s other parts will be moved in coordinated fashion or b will be damaged (be affected, for example, by breakage or tearing) in the interval between t and t.causal changes in one part of b can have consequences for other parts of b without the mediation of any entity that lies on the exterior of b. Material entities with no proper material parts would satisfy these conditions trivially. Candidate examples of types of causal unity for material entities of more complex sorts are as follows (this is not intended to be an exhaustive list):CU1: Causal unity via physical coveringHere the parts in the interior of the unified entity are combined together causally through a common membrane or other physical covering\. The latter points outwards toward and may serve a protective function in relation to what lies on the exterior of the entity [13, 47 BFO 2 Reference: an object is a maximal causally unified material entity BFO 2 Reference: ‘objects’ are sometimes referred to as ‘grains’ [74 b is an object means: b is a material entity which manifests causal unity of one or other of the types CUn listed above & is of a type (a material universal) instances of which are maximal relative to this criterion of causal unity. (axiom label in BFO2 Reference: [024-001]) object b is an object means: b is a material entity which manifests causal unity of one or other of the types CUn listed above & is of a type (a material universal) instances of which are maximal relative to this criterion of causal unity. (axiom label in BFO2 Reference: [024-001]) BFO:0000031 The entries in your database are patterns instantiated as quality instances in your hard drive. The database itself is an aggregate of such patterns. When you create the database you create a particular instance of the generically dependent continuant type database. Each entry in the database is an instance of the generically dependent continuant type IAO: information content entity. the pdf file on your laptop, the pdf file that is a copy thereof on my laptop the sequence of this protein molecule; the sequence that is a copy thereof in that protein molecule. b is a generically dependent continuant = Def. b is a continuant that g-depends_on one or more other entities. (axiom label in BFO2 Reference: [074-001]) (iff (GenericallyDependentContinuant a) (and (Continuant a) (exists (b t) (genericallyDependsOnAt a b t)))) // axiom label in BFO2 CLIF: [074-001] generically dependent continuant b is a generically dependent continuant = Def. b is a continuant that g-depends_on one or more other entities. (axiom label in BFO2 Reference: [074-001]) (iff (GenericallyDependentContinuant a) (and (Continuant a) (exists (b t) (genericallyDependsOnAt a b t)))) // axiom label in BFO2 CLIF: [074-001] BFO:0000034 the function of a hammer to drive in nails the function of a heart pacemaker to regulate the beating of a heart through electricity the function of amylase in saliva to break down starch into sugar BFO 2 Reference: In the past, we have distinguished two varieties of function, artifactual function and biological function. These are not asserted subtypes of BFO:function however, since the same function – for example: to pump, to transport – can exist both in artifacts and in biological entities. The asserted subtypes of function that would be needed in order to yield a separate monoheirarchy are not artifactual function, biological function, etc., but rather transporting function, pumping function, etc. A function is a disposition that exists in virtue of the bearer’s physical make-up and this physical make-up is something the bearer possesses because it came into being, either through evolution (in the case of natural biological entities) or through intentional design (in the case of artifacts), in order to realize processes of a certain sort. (axiom label in BFO2 Reference: [064-001]) (forall (x) (if (Function x) (Disposition x))) // axiom label in BFO2 CLIF: [064-001] function A function is a disposition that exists in virtue of the bearer’s physical make-up and this physical make-up is something the bearer possesses because it came into being, either through evolution (in the case of natural biological entities) or through intentional design (in the case of artifacts), in order to realize processes of a certain sort. (axiom label in BFO2 Reference: [064-001]) (forall (x) (if (Function x) (Disposition x))) // axiom label in BFO2 CLIF: [064-001] BFO:0000035 the boundary between the 2nd and 3rd year of your life. p is a process boundary =Def. p is a temporal part of a process & p has no proper temporal parts. (axiom label in BFO2 Reference: [084-001]) Every process boundary occupies_temporal_region a zero-dimensional temporal region. (axiom label in BFO2 Reference: [085-002]) (forall (x) (if (ProcessBoundary x) (exists (y) (and (ZeroDimensionalTemporalRegion y) (occupiesTemporalRegion x y))))) // axiom label in BFO2 CLIF: [085-002] (iff (ProcessBoundary a) (exists (p) (and (Process p) (temporalPartOf a p) (not (exists (b) (properTemporalPartOf b a)))))) // axiom label in BFO2 CLIF: [084-001] process boundary p is a process boundary =Def. p is a temporal part of a process & p has no proper temporal parts. (axiom label in BFO2 Reference: [084-001]) Every process boundary occupies_temporal_region a zero-dimensional temporal region. (axiom label in BFO2 Reference: [085-002]) (forall (x) (if (ProcessBoundary x) (exists (y) (and (ZeroDimensionalTemporalRegion y) (occupiesTemporalRegion x y))))) // axiom label in BFO2 CLIF: [085-002] (iff (ProcessBoundary a) (exists (p) (and (Process p) (temporalPartOf a p) (not (exists (b) (properTemporalPartOf b a)))))) // axiom label in BFO2 CLIF: [084-001] BFO:0000038 the temporal region during which a process occurs. BFO 2 Reference: A temporal interval is a special kind of one-dimensional temporal region, namely one that is self-connected (is without gaps or breaks). A one-dimensional temporal region is a temporal region that is extended. (axiom label in BFO2 Reference: [103-001]) A one-dimensional temporal region is a temporal region that is extended. (axiom label in BFO2 Reference: [103-001]) (forall (x) (if (OneDimensionalTemporalRegion x) (TemporalRegion x))) // axiom label in BFO2 CLIF: [103-001] one-dimensional temporal region A one-dimensional temporal region is a temporal region that is extended. (axiom label in BFO2 Reference: [103-001]) (forall (x) (if (OneDimensionalTemporalRegion x) (TemporalRegion x))) // axiom label in BFO2 CLIF: [103-001] BFO:0000040 material MaterialEntity material entity a flame a forest fire a human being a hurricane a photon a puff of smoke a sea wave a tornado an aggregate of human beings. an energy wave an epidemic the undetached arm of a human being An independent continuant that is spatially extended whose identity is independent of that of other entities and can be maintained through time. BFO 2 Reference: Material entities (continuants) can preserve their identity even while gaining and losing material parts. Continuants are contrasted with occurrents, which unfold themselves in successive temporal parts or phases [60 BFO 2 Reference: Material entities (continuants) can preserve their identity even while gaining and losing material parts. Continuants are contrasted with occurrents, which unfold themselves in successive temporal parts or phases [60 BFO 2 Reference: Object, Fiat Object Part and Object Aggregate are not intended to be exhaustive of Material Entity. Users are invited to propose new subcategories of Material Entity. BFO 2 Reference: Object, Fiat Object Part and Object Aggregate are not intended to be exhaustive of Material Entity. Users are invited to propose new subcategories of Material Entity. BFO 2 Reference: ‘Matter’ is intended to encompass both mass and energy (we will address the ontological treatment of portions of energy in a later version of BFO). A portion of matter is anything that includes elementary particles among its proper or improper parts: quarks and leptons, including electrons, as the smallest particles thus far discovered; baryons (including protons and neutrons) at a higher level of granularity; atoms and molecules at still higher levels, forming the cells, organs, organisms and other material entities studied by biologists, the portions of rock studied by geologists, the fossils studied by paleontologists, and so on.Material entities are three-dimensional entities (entities extended in three spatial dimensions), as contrasted with the processes in which they participate, which are four-dimensional entities (entities extended also along the dimension of time).According to the FMA, material entities may have immaterial entities as parts – including the entities identified below as sites; for example the interior (or ‘lumen’) of your small intestine is a part of your body. BFO 2.0 embodies a decision to follow the FMA here. BFO 2 Reference: ‘Matter’ is intended to encompass both mass and energy (we will address the ontological treatment of portions of energy in a later version of BFO). A portion of matter is anything that includes elementary particles among its proper or improper parts: quarks and leptons, including electrons, as the smallest particles thus far discovered; baryons (including protons and neutrons) at a higher level of granularity; atoms and molecules at still higher levels, forming the cells, organs, organisms and other material entities studied by biologists, the portions of rock studied by geologists, the fossils studied by paleontologists, and so on.Material entities are three-dimensional entities (entities extended in three spatial dimensions), as contrasted with the processes in which they participate, which are four-dimensional entities (entities extended also along the dimension of time).According to the FMA, material entities may have immaterial entities as parts – including the entities identified below as sites; for example the interior (or ‘lumen’) of your small intestine is a part of your body. BFO 2.0 embodies a decision to follow the FMA here. A material entity is an independent continuant that has some portion of matter as proper or improper continuant part. (axiom label in BFO2 Reference: [019-002]) A material entity is an independent continuant that has some portion of matter as proper or improper continuant part. (axiom label in BFO2 Reference: [019-002]) Every entity which has a material entity as continuant part is a material entity. (axiom label in BFO2 Reference: [020-002]) Every entity which has a material entity as continuant part is a material entity. (axiom label in BFO2 Reference: [020-002]) every entity of which a material entity is continuant part is also a material entity. (axiom label in BFO2 Reference: [021-002]) every entity of which a material entity is continuant part is also a material entity. (axiom label in BFO2 Reference: [021-002]) (forall (x) (if (MaterialEntity x) (IndependentContinuant x))) // axiom label in BFO2 CLIF: [019-002] (forall (x) (if (MaterialEntity x) (IndependentContinuant x))) // axiom label in BFO2 CLIF: [019-002] (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt x y t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [021-002] (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt x y t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [021-002] (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt y x t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [020-002] (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt y x t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [020-002] material entity A material entity is an independent continuant that has some portion of matter as proper or improper continuant part. (axiom label in BFO2 Reference: [019-002]) A material entity is an independent continuant that has some portion of matter as proper or improper continuant part. (axiom label in BFO2 Reference: [019-002]) Every entity which has a material entity as continuant part is a material entity. (axiom label in BFO2 Reference: [020-002]) Every entity which has a material entity as continuant part is a material entity. (axiom label in BFO2 Reference: [020-002]) every entity of which a material entity is continuant part is also a material entity. (axiom label in BFO2 Reference: [021-002]) every entity of which a material entity is continuant part is also a material entity. (axiom label in BFO2 Reference: [021-002]) (forall (x) (if (MaterialEntity x) (IndependentContinuant x))) // axiom label in BFO2 CLIF: [019-002] (forall (x) (if (MaterialEntity x) (IndependentContinuant x))) // axiom label in BFO2 CLIF: [019-002] (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt x y t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [021-002] (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt x y t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [021-002] (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt y x t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [020-002] (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt y x t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [020-002] BFO:0000140 b is a continuant fiat boundary = Def. b is an immaterial entity that is of zero, one or two dimensions and does not include a spatial region as part. (axiom label in BFO2 Reference: [029-001]) BFO 2 Reference: In BFO 1.1 the assumption was made that the external surface of a material entity such as a cell could be treated as if it were a boundary in the mathematical sense. The new document propounds the view that when we talk about external surfaces of material objects in this way then we are talking about something fiat. To be dealt with in a future version: fiat boundaries at different levels of granularity.More generally, the focus in discussion of boundaries in BFO 2.0 is now on fiat boundaries, which means: boundaries for which there is no assumption that they coincide with physical discontinuities. The ontology of boundaries becomes more closely allied with the ontology of regions. BFO 2 Reference: a continuant fiat boundary is a boundary of some material entity (for example: the plane separating the Northern and Southern hemispheres; the North Pole), or it is a boundary of some immaterial entity (for example of some portion of airspace). Three basic kinds of continuant fiat boundary can be distinguished (together with various combination kinds [29 Continuant fiat boundary doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. An example would be the mereological sum of two-dimensional continuant fiat boundary and a one dimensional continuant fiat boundary that doesn't overlap it. The situation is analogous to temporal and spatial regions. Every continuant fiat boundary is located at some spatial region at every time at which it exists (iff (ContinuantFiatBoundary a) (and (ImmaterialEntity a) (exists (b) (and (or (ZeroDimensionalSpatialRegion b) (OneDimensionalSpatialRegion b) (TwoDimensionalSpatialRegion b)) (forall (t) (locatedInAt a b t)))) (not (exists (c t) (and (SpatialRegion c) (continuantPartOfAt c a t)))))) // axiom label in BFO2 CLIF: [029-001] continuant fiat boundary b is a continuant fiat boundary = Def. b is an immaterial entity that is of zero, one or two dimensions and does not include a spatial region as part. (axiom label in BFO2 Reference: [029-001]) Continuant fiat boundary doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. An example would be the mereological sum of two-dimensional continuant fiat boundary and a one dimensional continuant fiat boundary that doesn't overlap it. The situation is analogous to temporal and spatial regions. (iff (ContinuantFiatBoundary a) (and (ImmaterialEntity a) (exists (b) (and (or (ZeroDimensionalSpatialRegion b) (OneDimensionalSpatialRegion b) (TwoDimensionalSpatialRegion b)) (forall (t) (locatedInAt a b t)))) (not (exists (c t) (and (SpatialRegion c) (continuantPartOfAt c a t)))))) // axiom label in BFO2 CLIF: [029-001] BFO:0000141 BFO 2 Reference: Immaterial entities are divided into two subgroups:boundaries and sites, which bound, or are demarcated in relation, to material entities, and which can thus change location, shape and size and as their material hosts move or change shape or size (for example: your nasal passage; the hold of a ship; the boundary of Wales (which moves with the rotation of the Earth) [38, 7, 10 immaterial entity BFO:0000142 The Equator all geopolitical boundaries all lines of latitude and longitude the line separating the outer surface of the mucosa of the lower lip from the outer surface of the skin of the chin. the median sulcus of your tongue a one-dimensional continuant fiat boundary is a continuous fiat line whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [032-001]) a one-dimensional continuant fiat boundary is a continuous fiat line whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [032-001]) (iff (OneDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (OneDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [032-001] one-dimensional continuant fiat boundary a one-dimensional continuant fiat boundary is a continuous fiat line whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [032-001]) (iff (OneDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (OneDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [032-001] BFO:0000144 On a somewhat higher level of complexity are what we shall call rate process profiles, which are the targets of selective abstraction focused not on determinate quality magnitudes plotted over time, but rather on certain ratios between these magnitudes and elapsed times. A speed process profile, for example, is represented by a graph plotting against time the ratio of distance covered per unit of time. Since rates may change, and since such changes, too, may have rates of change, we have to deal here with a hierarchy of process profile universals at successive levels One important sub-family of rate process profiles is illustrated by the beat or frequency profiles of cyclical processes, illustrated by the 60 beats per minute beating process of John’s heart, or the 120 beats per minute drumming process involved in one of John’s performances in a rock band, and so on. Each such process includes what we shall call a beat process profile instance as part, a subtype of rate process profile in which the salient ratio is not distance covered but rather number of beat cycles per unit of time. Each beat process profile instance instantiates the determinable universal beat process profile. But it also instantiates multiple more specialized universals at lower levels of generality, selected from rate process profilebeat process profileregular beat process profile3 bpm beat process profile4 bpm beat process profileirregular beat process profileincreasing beat process profileand so on.In the case of a regular beat process profile, a rate can be assigned in the simplest possible fashion by dividing the number of cycles by the length of the temporal region occupied by the beating process profile as a whole. Irregular process profiles of this sort, for example as identified in the clinic, or in the readings on an aircraft instrument panel, are often of diagnostic significance. The simplest type of process profiles are what we shall call ‘quality process profiles’, which are the process profiles which serve as the foci of the sort of selective abstraction that is involved when measurements are made of changes in single qualities, as illustrated, for example, by process profiles of mass, temperature, aortic pressure, and so on. b is a process_profile =Def. there is some process c such that b process_profile_of c (axiom label in BFO2 Reference: [093-002]) b process_profile_of c holds when b proper_occurrent_part_of c& there is some proper_occurrent_part d of c which has no parts in common with b & is mutually dependent on b& is such that b, c and d occupy the same temporal region (axiom label in BFO2 Reference: [094-005]) b process_profile_of c holds when b proper_occurrent_part_of c& there is some proper_occurrent_part d of c which has no parts in common with b & is mutually dependent on b& is such that b, c and d occupy the same temporal region (axiom label in BFO2 Reference: [094-005]) (forall (x y) (if (processProfileOf x y) (and (properContinuantPartOf x y) (exists (z t) (and (properOccurrentPartOf z y) (TemporalRegion t) (occupiesSpatioTemporalRegion x t) (occupiesSpatioTemporalRegion y t) (occupiesSpatioTemporalRegion z t) (not (exists (w) (and (occurrentPartOf w x) (occurrentPartOf w z))))))))) // axiom label in BFO2 CLIF: [094-005] (iff (ProcessProfile a) (exists (b) (and (Process b) (processProfileOf a b)))) // axiom label in BFO2 CLIF: [093-002] process profile b is a process_profile =Def. there is some process c such that b process_profile_of c (axiom label in BFO2 Reference: [093-002]) b process_profile_of c holds when b proper_occurrent_part_of c& there is some proper_occurrent_part d of c which has no parts in common with b & is mutually dependent on b& is such that b, c and d occupy the same temporal region (axiom label in BFO2 Reference: [094-005]) (forall (x y) (if (processProfileOf x y) (and (properContinuantPartOf x y) (exists (z t) (and (properOccurrentPartOf z y) (TemporalRegion t) (occupiesSpatioTemporalRegion x t) (occupiesSpatioTemporalRegion y t) (occupiesSpatioTemporalRegion z t) (not (exists (w) (and (occurrentPartOf w x) (occurrentPartOf w z))))))))) // axiom label in BFO2 CLIF: [094-005] (iff (ProcessProfile a) (exists (b) (and (Process b) (processProfileOf a b)))) // axiom label in BFO2 CLIF: [093-002] BFO:0000145 John’s role of husband to Mary is dependent on Mary’s role of wife to John, and both are dependent on the object aggregate comprising John and Mary as member parts joined together through the relational quality of being married. a marriage bond, an instance of love, an obligation between one person and another. b is a relational quality = Def. for some independent continuants c, d and for some time t: b quality_of c at t & b quality_of d at t. (axiom label in BFO2 Reference: [057-001]) (iff (RelationalQuality a) (exists (b c t) (and (IndependentContinuant b) (IndependentContinuant c) (qualityOfAt a b t) (qualityOfAt a c t)))) // axiom label in BFO2 CLIF: [057-001] relational quality b is a relational quality = Def. for some independent continuants c, d and for some time t: b quality_of c at t & b quality_of d at t. (axiom label in BFO2 Reference: [057-001]) (iff (RelationalQuality a) (exists (b c t) (and (IndependentContinuant b) (IndependentContinuant c) (qualityOfAt a b t) (qualityOfAt a c t)))) // axiom label in BFO2 CLIF: [057-001] BFO:0000146 a two-dimensional continuant fiat boundary (surface) is a self-connected fiat surface whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [033-001]) a two-dimensional continuant fiat boundary (surface) is a self-connected fiat surface whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [033-001]) (iff (TwoDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (TwoDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [033-001] two-dimensional continuant fiat boundary a two-dimensional continuant fiat boundary (surface) is a self-connected fiat surface whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [033-001]) (iff (TwoDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (TwoDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [033-001] BFO:0000147 the geographic North Pole the point of origin of some spatial coordinate system. the quadripoint where the boundaries of Colorado, Utah, New Mexico, and Arizona meet zero dimension continuant fiat boundaries are not spatial points. Considering the example 'the quadripoint where the boundaries of Colorado, Utah, New Mexico, and Arizona meet' : There are many frames in which that point is zooming through many points in space. Whereas, no matter what the frame, the quadripoint is always in the same relation to the boundaries of Colorado, Utah, New Mexico, and Arizona. a zero-dimensional continuant fiat boundary is a fiat point whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [031-001]) a zero-dimensional continuant fiat boundary is a fiat point whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [031-001]) (iff (ZeroDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (ZeroDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [031-001] zero-dimensional continuant fiat boundary zero dimension continuant fiat boundaries are not spatial points. Considering the example 'the quadripoint where the boundaries of Colorado, Utah, New Mexico, and Arizona meet' : There are many frames in which that point is zooming through many points in space. Whereas, no matter what the frame, the quadripoint is always in the same relation to the boundaries of Colorado, Utah, New Mexico, and Arizona. requested by Melanie Courtot a zero-dimensional continuant fiat boundary is a fiat point whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [031-001]) (iff (ZeroDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (ZeroDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [031-001] BFO:0000148 a temporal region that is occupied by a process boundary right now the moment at which a child is born the moment at which a finger is detached in an industrial accident the moment of death. temporal instant. A zero-dimensional temporal region is a temporal region that is without extent. (axiom label in BFO2 Reference: [102-001]) A zero-dimensional temporal region is a temporal region that is without extent. (axiom label in BFO2 Reference: [102-001]) (forall (x) (if (ZeroDimensionalTemporalRegion x) (TemporalRegion x))) // axiom label in BFO2 CLIF: [102-001] zero-dimensional temporal region A zero-dimensional temporal region is a temporal region that is without extent. (axiom label in BFO2 Reference: [102-001]) (forall (x) (if (ZeroDimensionalTemporalRegion x) (TemporalRegion x))) // axiom label in BFO2 CLIF: [102-001] The side of an organism that is left of the sagittal plane. The side of an organism that is left of the sagittal plane. left spatial BSPO:0000000 left side BSPO:0000000 The side of an organism that is left of the sagittal plane. BSPO:cjm upper spatial BSPO:0000001 Consider merging with superior side. upper side BSPO:0000001 lower spatial BSPO:0000002 Consider merging with inferior side. lower side BSPO:0000002 deep spatial BSPO:0000003 deep side BSPO:0000003 superficial spatial BSPO:0000004 superficial side BSPO:0000004 A 2D surface of an anatomical continuant. A 2D surface of an anatomical continuant. FMA:24137 surface spatial BSPO:0000005 to be merged into CARO anatomical surface BSPO:0000005 A 2D surface of an anatomical continuant. BSPO:cjm Fiat anatomical region extending a short distance from the boundary of an object inwards. Fiat anatomical region extending a short distance from the boundary of an object inwards. edge margin spatial BSPO:0000006 anatomical margin BSPO:0000006 Fiat anatomical region extending a short distance from the boundary of an object inwards. BSPO:cjm The side of an organism that is right of the sagittal plane. The side of an organism that is right of the sagittal plane. right spatial BSPO:0000007 right side BSPO:0000007 The side of an organism that is right of the sagittal plane. BSPO:cjm BSPO:wd Sagittal plane that divides a bilateral body into unequal left and right parts. Sagittal plane that divides a bilateral body into unequal left and right parts. parasagittal section spatial BSPO:0000008 parasagittal plane BSPO:0000008 Sagittal plane that divides a bilateral body into unequal left and right parts. BSPO:mah Sagittal plane that divides bilateral body into equal left and right parts. Sagittal plane that divides bilateral body into equal left and right parts. FMA:74563 median sagittal plane median sagittal plane midline plane midsagittal section spatial median plane BSPO:0000009 only in bilaterally symmetrical organisms midsagittal plane BSPO:0000009 Sagittal plane that divides bilateral body into equal left and right parts. BSPO:mah median sagittal plane FMA:74563 A straight line through space, intersecting an anatomical entity. A straight line through space, intersecting an anatomical entity. http://upload.wikimedia.org/wikipedia/commons/3/34/Anatomical_Directions_and_Axes.JPG spatial BSPO:0000010 Axis directions are defined in terms of axes. anatomical axis BSPO:0000010 A straight line through space, intersecting an anatomical entity. BSPO:cjm An anatomical axis determined by gravity. An anatomical axis determined by gravity. spatial superior-inferior axis BSPO:0000011 upper-lower axis BSPO:0000011 An anatomical axis determined by gravity. BSPO:cjm An axis that extends from an internal position to a more external position in the body or body part. An axis that extends from an internal position to a more external position in the body or body part. spatial BSPO:0000012 Muscles are frequently categorized as 'deep', 'intermediate', and 'superficial'. deep-superficial axis BSPO:0000012 An axis that extends from an internal position to a more external position in the body or body part. BSPO:PM An axis that extends through an organism from head end to opposite end of body or tail. An axis that extends through an organism from head end to opposite end of body or tail. A-P axis AP axis anteroposterior axis cephalocaudal axis cephalocaudal axis craniocaudal axis craniocaudal axis rostral/caudal rostral/caudal rostrocaudal axis rostrocaudal axis spatial longitudinal axis BSPO:0000013 In sponges, AP is used to indicate the direction of movement [in larval stage] (as it is in other metazoans that move, e.g., the basal bilaterians). [PM] anterior-posterior axis BSPO:0000013 An axis that extends through an organism from head end to opposite end of body or tail. BSPO:cjm cephalocaudal axis http://en.wikipedia.org/wiki/Anatomical_terms_of_location craniocaudal axis rostral/caudal rostrocaudal axis An axis that extends through an organism or organism part from the part of the organism or organism part attached to a substrate (basal) to the furthest from the attachment (apical). Note that the apical-basal axis is often used for organismal parts where there is attachment via a basal lamina or other structure. An axis that extends through an organism or organism part from the part of the organism or organism part attached to a substrate (basal) to the furthest from the attachment (apical). Note that the apical-basal axis is often used for organismal parts where there is attachment via a basal lamina or other structure. apical/basal spatial longitudinal axis BSPO:0000014 apical-basal axis relative to substrate BSPO:0000014 An axis that extends through an organism or organism part from the part of the organism or organism part attached to a substrate (basal) to the furthest from the attachment (apical). Note that the apical-basal axis is often used for organismal parts where there is attachment via a basal lamina or other structure. BSPO:mah An axis that extends from the point of attachment of a structure (proximal) to the point furthest away from the plane of attachment (distal). An axis that extends from the point of attachment of a structure (proximal) to the point furthest away from the plane of attachment (distal). proximal/distal proximodistal spatial BSPO:0000015 In some communities, proximal and distal are used when specifying the position of parts of elements that are contained within the body, such as gill arches or vertebral spines. In these cases, use of the classes medial-lateral axis or medial-external axis are more appropriate. proximal-distal axis BSPO:0000015 An axis that extends from the point of attachment of a structure (proximal) to the point furthest away from the plane of attachment (distal). BSPO:curators http://en.wikipedia.org/wiki/Anatomical_terms_of_location An axis that is approximately perpendicular to the anterior-posterior axis and that extends through the horizontal plane of the body. An axis that is approximately perpendicular to the anterior-posterior axis and that extends through the horizontal plane of the body. D-V axis DV axis dorsoventral axis anterior-posterior axis anterior-posterior axis spatial BSPO:0000016 dorsal-ventral axis BSPO:0000016 An axis that is approximately perpendicular to the anterior-posterior axis and that extends through the horizontal plane of the body. BSPO:curators anterior-posterior axis An axis that bisects an organism from left to right sides of body, through a sagittal plane. An axis that bisects an organism from left to right sides of body, through a sagittal plane. L-R axis LR axis R-L axis RL axis dextro-sinister axis left to right axis right to left axis right-left axis spatial BSPO:0000017 left-right axis BSPO:0000017 An axis that bisects an organism from left to right sides of body, through a sagittal plane. BSPO:cjm Anatomical plane that divides body into anterior and posterior parts. Anatomical plane that divides body into anterior and posterior parts. FMA:12247 axial plane axial section transverse section spatial cross-section BSPO:0000018 transverse plane BSPO:0000018 Anatomical plane that divides body into anterior and posterior parts. BSPO:mah Anatomical plane that divides bilateral body into dorsal and ventral parts. Anatomical plane that divides bilateral body into dorsal and ventral parts. FMA:52810 frontal plane horizontal anatomical plane horizontal anatomical plane horizontal section spatial coronal section frontal section BSPO:0000019 horizontal plane BSPO:0000019 Anatomical plane that divides bilateral body into dorsal and ventral parts. BSPO:mah horizontal anatomical plane FMA:52810 Anatomical gradient that is distributed along the upper-lower axis. Anatomical gradient that is distributed along the upper-lower axis. spatial BSPO:0000020 upper-lower gradient BSPO:0000020 Anatomical gradient that is distributed along the upper-lower axis. BSPO:wd Anatomical gradient that is distributed along the deep-superficial axis. Anatomical gradient that is distributed along the deep-superficial axis. spatial BSPO:0000021 deep-superficial gradient BSPO:0000021 Anatomical gradient that is distributed along the deep-superficial axis. BSPO:wd The side that is higher relative to the substrate. The side that is higher relative to the substrate. superior spatial cranial BSPO:0000022 superior side BSPO:0000022 The side that is higher relative to the substrate. BSPO:curators Anatomical gradient that is distributed along the apical-basal axis. Anatomical gradient that is distributed along the apical-basal axis. spatial BSPO:0000023 apical-basal gradient BSPO:0000023 Anatomical gradient that is distributed along the apical-basal axis. BSPO:wd Anatomical gradient that is distributed along the proximal-distal axis. Anatomical gradient that is distributed along the proximal-distal axis. spatial BSPO:0000024 proximal-distal gradient BSPO:0000024 Anatomical gradient that is distributed along the proximal-distal axis. BSPO:wd The side that is lower relative to the substrate. The side that is lower relative to the substrate. inferior spatial caudal BSPO:0000025 inferior side BSPO:0000025 The side that is lower relative to the substrate. BSPO:curators Anatomical region that overlaps the anterior and dorsal regions of a body or body part. Anatomical region that overlaps the anterior and dorsal regions of a body or body part. Melissa Haendel 2009-06-15T01:01:38Z anterodorsal region spatial BSPO:0000026 antero-dorsal region BSPO:0000026 Anatomical region that overlaps the anterior and dorsal regions of a body or body part. BSPO:wd Anatomical region that overlaps the anterior and ventral regions of a body or body part. Anatomical region that overlaps the anterior and ventral regions of a body or body part. Melissa Haendel 2009-06-15T01:04:59Z anteroventral region spatial BSPO:0000027 antero-ventral region BSPO:0000027 Anatomical region that overlaps the anterior and ventral regions of a body or body part. BSPO:wd Anatomical region that overlaps the posterior and lateral regions of the body or body part. Anatomical region that overlaps the posterior and lateral regions of the body or body part. Melissa Haendel 2009-06-15T01:06:01Z posterolateral region spatial BSPO:0000028 postero-lateral region BSPO:0000028 Anatomical region that overlaps the posterior and lateral regions of the body or body part. BSPO:wd Anatomical region that overlaps the anterior and lateral regions of a body or body part. Anatomical region that overlaps the anterior and lateral regions of a body or body part. Melissa Haendel 2009-06-15T01:07:18Z anterolateral region spatial BSPO:0000029 antero-lateral region BSPO:0000029 Anatomical region that overlaps the anterior and lateral regions of a body or body part. BSPO:wd Anatomical region that overlaps the posterior and dorsal regions of the body or body part. Anatomical region that overlaps the posterior and dorsal regions of the body or body part. Melissa Haendel 2009-06-15T01:08:13Z posterodorsal region spatial BSPO:0000030 postero-dorsal region BSPO:0000030 Anatomical region that overlaps the posterior and dorsal regions of the body or body part. BSPO:wd spatial BSPO:0000031 upper region BSPO:0000031 spatial BSPO:0000032 lower region BSPO:0000032 Anatomical region located deep within an organism or structure. Anatomical region located deep within an organism or structure. spatial BSPO:0000033 deep region BSPO:0000033 Anatomical region located deep within an organism or structure. BSPO:wd Anatomical region superficially located on the body or body part. Anatomical region superficially located on the body or body part. spatial BSPO:0000034 superficial region BSPO:0000034 Anatomical region superficially located on the body or body part. BSPO:wd Anatomical region that overlaps the posterior and ventral regions of a body or body part. Anatomical region that overlaps the posterior and ventral regions of a body or body part. Melissa Haendel 2009-06-15T01:08:38Z posteroventral region spatial BSPO:0000035 postero-ventral region BSPO:0000035 Anatomical region that overlaps the posterior and ventral regions of a body or body part. BSPO:wd Melissa Haendel 2009-06-16T08:49:03Z anterior-most anteriormost spatial BSPO:0000036 anterior-most region BSPO:0000036 Melissa Haendel 2009-06-16T08:49:50Z posterior-most posteriormost spatial BSPO:0000037 posterior-most region BSPO:0000037 Melissa Haendel 2009-06-16T08:50:26Z dorsal-most dorsalmost spatial BSPO:0000038 dorsal-most region BSPO:0000038 Melissa Haendel 2009-06-16T08:51:07Z ventral-most ventralmost spatial BSPO:0000039 ventral-most region BSPO:0000039 spatial BSPO:0000040 upper/lower compartment boundary BSPO:0000040 spatial BSPO:0000041 deep/superficial compartment boundary BSPO:0000041 Anatomical margin that is located on the antero-medial region of the body or body part. Anatomical margin that is located on the antero-medial region of the body or body part. Melissa Haendel 2009-09-10T08:49:57Z anteromedial margin spatial BSPO:0000042 antero-medial margin BSPO:0000042 Anatomical margin that is located on the antero-medial region of the body or body part. BSPO:wd spatial BSPO:0000043 apical/basal compartment boundary BSPO:0000043 spatial BSPO:0000044 proximal/distal compartment boundary BSPO:0000044 Anatomical margin that is located on the antero-lateral region of the body or body part. Anatomical margin that is located on the antero-lateral region of the body or body part. Melissa Haendel 2009-09-10T08:50:37Z anterolateral margin spatial BSPO:0000045 antero-lateral margin BSPO:0000045 Anatomical margin that is located on the antero-lateral region of the body or body part. BSPO:wd Anatomical margin that is located on the postero-medial region of the body or body part. Anatomical margin that is located on the postero-medial region of the body or body part. Melissa Haendel 2009-09-10T08:51:07Z posteromedial margin spatial BSPO:0000046 postero-medial margin BSPO:0000046 Anatomical margin that is located on the postero-medial region of the body or body part. BSPO:wd Anatomical margin that is located on the postero-lateral region of the body or body part. Anatomical margin that is located on the postero-lateral region of the body or body part. Melissa Haendel 2009-09-10T08:51:42Z posterolateral margin spatial BSPO:0000047 postero-lateral margin BSPO:0000047 Anatomical margin that is located on the postero-lateral region of the body or body part. BSPO:wd Anatomical margin that is located on the dorso-medial region of the body or body part. Anatomical margin that is located on the dorso-medial region of the body or body part. Melissa Haendel 2009-09-10T08:52:04Z dorso-medial margin spatial BSPO:0000048 dorso-medial margin BSPO:0000048 Anatomical margin that is located on the dorso-medial region of the body or body part. BSPO:wd Anatomical margin that is located on the ventro-medial region of the body or body part. Anatomical margin that is located on the ventro-medial region of the body or body part. Melissa Haendel 2009-09-10T08:52:48Z ventromedial margin spatial BSPO:0000049 ventro-medial margin BSPO:0000049 Anatomical margin that is located on the ventro-medial region of the body or body part. BSPO:wd Anatomical region that overlaps the anterior and medial regions of the body or body part. Anatomical region that overlaps the anterior and medial regions of the body or body part. Melissa Haendel 2009-09-10T08:55:32Z anteromedial region spatial BSPO:0000050 antero-medial region BSPO:0000050 Anatomical region that overlaps the anterior and medial regions of the body or body part. BSPO:wd Material anatomical entity defined by change in the value of some quantity per unit of distance across some spatial axis. Material anatomical entity defined by change in the value of some quantity per unit of distance across some spatial axis. FBql:00005254 spatial BSPO:0000051 anatomical gradient BSPO:0000051 Material anatomical entity defined by change in the value of some quantity per unit of distance across some spatial axis. BSPO:cjm Anatomical gradient that is distributed along the anterior-posterior axis. Anatomical gradient that is distributed along the anterior-posterior axis. FBcv:0000142 FBql:00005256 spatial BSPO:0000052 anterior-posterior gradient BSPO:0000052 Anatomical gradient that is distributed along the anterior-posterior axis. BSPO:wd Anatomical gradient that is distributed along the dorsal-ventral axis. Anatomical gradient that is distributed along the dorsal-ventral axis. FBcv:0000143 FBql:00005255 spatial BSPO:0000053 dorsal-ventral gradient BSPO:0000053 Anatomical gradient that is distributed along the dorsal-ventral axis. BSPO:wd An anatomical region bounded by a plane perpendicular to an axis through the middle. An anatomical region bounded by a plane perpendicular to an axis through the middle. FBql:00005841 spatial BSPO:0000054 anatomical side BSPO:0000054 An anatomical region bounded by a plane perpendicular to an axis through the middle. BSPO:cjm An anatomical region that is the entire part of an anatomical structure anterior to a transverse plane and bounded on one side by the same transverse plane. An anatomical region that is the entire part of an anatomical structure anterior to a transverse plane and bounded on one side by the same transverse plane. FBcv:0000053 FBql:00005848 anterior rostral spatial BSPO:0000055 anterior side BSPO:0000055 An anatomical region that is the entire part of an anatomical structure anterior to a transverse plane and bounded on one side by the same transverse plane. BSPO:RW An anatomical region that is the entire part of an anatomical structure posterior to a transverse plane and bounded on one side by the same transverse plane. An anatomical region that is the entire part of an anatomical structure posterior to a transverse plane and bounded on one side by the same transverse plane. FBcv:0000065 FBql:00005849 posterior caudal caudal spatial BSPO:0000056 posterior side BSPO:0000056 An anatomical region that is the entire part of an anatomical structure posterior to a transverse plane and bounded on one side by the same transverse plane. BSPO:RW BSPO:wd caudal Anatomical side that is located on the apical end of an organism or structure. Anatomical side that is located on the apical end of an organism or structure. FBcv:0000054 FBql:00005854 apical spatial BSPO:0000057 apical side BSPO:0000057 Anatomical side that is located on the apical end of an organism or structure. BSPO:wd Anatomical side that is located on the basal end of an organism or structure. Anatomical side that is located on the basal end of an organism or structure. FBcv:0000055 FBql:00005855 basal spatial BSPO:0000058 The part of the organism attached to a substrate. Axis of symmetry. basal side BSPO:0000058 Anatomical side that is located on the basal end of an organism or structure. BSPO:wd Anatomical side that is centrally located on an organism or structure. Anatomical side that is centrally located on an organism or structure. FBcv:0000056 FBql:00015851 central spatial BSPO:0000059 central is not an axis direction central side BSPO:0000059 Anatomical side that is centrally located on an organism or structure. BSPO:wd On the opposite side. On the opposite side. FBcv:0000057 FBql:00005851 contralateral spatial BSPO:0000060 inherited from flybase cv. not clear how this would be used. Suggest we obsolete, and use the corresponding relation. contralateral side BSPO:0000060 On the opposite side. BSPO:cjm FBcv:0000066 FBql:00005852 proximal spatial BSPO:0000061 proximal side BSPO:0000061 Anatomical side that is distally located on an organism or structure. Anatomical side that is distally located on an organism or structure. FBcv:0000058 FBql:00005853 distal spatial BSPO:0000062 distal side BSPO:0000062 Anatomical side that is distally located on an organism or structure. BSPO:wd An anatomical region that is the entire part of an anatomical structure dorsal to a horizontal plane and bounded on one side by the same transverse plane. An anatomical region that is the entire part of an anatomical structure dorsal to a horizontal plane and bounded on one side by the same transverse plane. FBcv:0000059 FBql:00005842 dorsal spatial BSPO:0000063 dorsal side BSPO:0000063 An anatomical region that is the entire part of an anatomical structure dorsal to a horizontal plane and bounded on one side by the same transverse plane. BSPO:wd Anatomical region that overlaps the posterior and medial regions of the body or body part. Anatomical region that overlaps the posterior and medial regions of the body or body part. Melissa Haendel 2009-09-10T08:56:39Z posteromedial region spatial BSPO:0000064 postero-medial region BSPO:0000064 Anatomical region that overlaps the posterior and medial regions of the body or body part. BSPO:wd On the same side On the same side FBcv:0000062 FBql:00005850 ipsilateral spatial BSPO:0000065 inherited from flybase cv. not clear how this would be used. Suggest we obsolete, and use the corresponding relation. ipsilateral side BSPO:0000065 On the same side BSPO:cjm FBcv:0000063 FBql:00005844 lateral spatial BSPO:0000066 lateral side BSPO:0000066 FBcv:0000064 FBql:00005847 medial spatial BSPO:0000067 a point in the centre of the organism (where the left-right axis intersects the midsagittal plane) medial side BSPO:0000067 An anatomical region that is the entire part of an anatomical structure ventral to a horizontal plane and bounded on one side by the same horizontal plane. An anatomical region that is the entire part of an anatomical structure ventral to a horizontal plane and bounded on one side by the same horizontal plane. FBcv:0000070 FBql:00005843 ventral spatial BSPO:0000068 ventral side BSPO:0000068 An anatomical region that is the entire part of an anatomical structure ventral to a horizontal plane and bounded on one side by the same horizontal plane. BSPO:RW BSPO:wd Anatomical region that overlaps the dorsal and medial regions of the body or body part. Anatomical region that overlaps the dorsal and medial regions of the body or body part. Melissa Haendel 2009-09-10T08:57:22Z dorsomedial region spatial BSPO:0000069 dorso-medial region BSPO:0000069 Anatomical region that overlaps the dorsal and medial regions of the body or body part. BSPO:wd A 3D region in space without well-defined compartmental boundaries; for example, the dorsal region of an ectoderm. A 3D region in space without well-defined compartmental boundaries; for example, the dorsal region of an ectoderm. FBql:00005841 spatial BSPO:0000070 to be merged into CARO anatomical region BSPO:0000070 A 3D region in space without well-defined compartmental boundaries; for example, the dorsal region of an ectoderm. BSPO:cjm Anatomical region anteriorly located on the body or body part. Anatomical region anteriorly located on the body or body part. FBql:00005848 spatial BSPO:0000071 anterior region BSPO:0000071 Anatomical region anteriorly located on the body or body part. BSPO:wd Anatomical region posteriorly located on the body or body part. Anatomical region posteriorly located on the body or body part. FBql:00005849 spatial BSPO:0000072 posterior region BSPO:0000072 Anatomical region posteriorly located on the body or body part. BSPO:wd Anatomical region located on the apical end on the body or body part. Anatomical region located on the apical end on the body or body part. FBql:00005854 spatial BSPO:0000073 apical region BSPO:0000073 Anatomical region located on the apical end on the body or body part. BSPO:wd Anatomical region located basally on the body or body part. Anatomical region located basally on the body or body part. FBql:00005855 spatial BSPO:0000074 basal region BSPO:0000074 Anatomical region located basally on the body or body part. BSPO:wd Anatomical region centrally located on the body or body part. Anatomical region centrally located on the body or body part. FBql:00015851 spatial BSPO:0000075 central region BSPO:0000075 Anatomical region centrally located on the body or body part. BSPO:wd FBql:00005851 spatial BSPO:0000076 inherited from flybase cv. not clear how this would be used contralateral region BSPO:0000076 Anatomical region proximally located on the body or body part. Anatomical region proximally located on the body or body part. FBql:00005852 spatial BSPO:0000077 proximal region BSPO:0000077 Anatomical region proximally located on the body or body part. BSPO:wd Anatomical region distally located on the body or body part. Anatomical region distally located on the body or body part. FBql:00005853 spatial BSPO:0000078 distal region BSPO:0000078 Anatomical region distally located on the body or body part. BSPO:wd Anatomical region dorsally located on the body or body part. Anatomical region dorsally located on the body or body part. FBql:00005842 spatial BSPO:0000079 dorsal region BSPO:0000079 Anatomical region dorsally located on the body or body part. BSPO:wd Anatomical region that overlaps the dorsal and lateral regions of a body or body part. Anatomical region that overlaps the dorsal and lateral regions of a body or body part. FBql:00005845 dorsolateral region spatial BSPO:0000080 dorso-lateral region BSPO:0000080 Anatomical region that overlaps the dorsal and lateral regions of a body or body part. BSPO:wd FBql:00005850 spatial BSPO:0000081 ipsilateral region BSPO:0000081 Anatomical region laterally located on the body or body part. Anatomical region laterally located on the body or body part. FBql:00005844 spatial BSPO:0000082 lateral region BSPO:0000082 Anatomical region laterally located on the body or body part. BSPO:wd Anatomical region medially located on the body or body part. Anatomical region medially located on the body or body part. FBql:00005847 spatial BSPO:0000083 medial region BSPO:0000083 Anatomical region medially located on the body or body part. BSPO:wd Anatomical region ventrally located on the body or body part. Anatomical region ventrally located on the body or body part. FBql:00005843 spatial BSPO:0000084 ventral region BSPO:0000084 Anatomical region ventrally located on the body or body part. BSPO:wd Anatomical region that overlaps the ventral and lateral regions of a body or body part. Anatomical region that overlaps the ventral and lateral regions of a body or body part. FBql:00005846 ventrolateral region spatial BSPO:0000085 This is an example of a composition of two axis positions. ventro-lateral region BSPO:0000085 Anatomical region that overlaps the ventral and lateral regions of a body or body part. BSPO:wd FBql:00005873 FMA:9647 spatial BSPO:0000086 to be merged into CARO anatomical compartment BSPO:0000086 FBcv:0000031 FBql:00005874 spatial BSPO:0000087 anterior compartment BSPO:0000087 FBcv:0000032 FBql:00005878 spatial BSPO:0000088 compartment boundary BSPO:0000088 FBcv:0000035 FBql:00005876 spatial BSPO:0000089 dorsal compartment BSPO:0000089 FBcv:0000036 FBql:00005875 spatial BSPO:0000090 posterior compartment BSPO:0000090 FBcv:0000037 FBql:00005877 spatial BSPO:0000091 ventral compartment BSPO:0000091 FBql:00005881 spatial BSPO:0000092 to be merged into CARO anatomical compartment boundary BSPO:0000092 FBcv:0000033 FBql:00005880 spatial BSPO:0000093 anterior/posterior compartment boundary BSPO:0000093 FBcv:0000034 FBql:00005879 spatial BSPO:0000094 dorsal/ventral compartment boundary BSPO:0000094 The region corresponding to the ventral region of the entity, towards the midline. The region corresponding to the ventral region of the entity, towards the midline. Melissa Haendel 2009-09-10T08:57:54Z medioventral region ventromedial region spatial BSPO:0000112 ventro-medial region BSPO:0000112 The region corresponding to the ventral region of the entity, towards the midline. BSPO:wd Anatomical region peripherally located on the body or body part. Anatomical region peripherally located on the body or body part. spatial BSPO:0000127 peripheral region BSPO:0000127 Anatomical region peripherally located on the body or body part. BSPO:wd spatial BSPO:0000128 axial region BSPO:0000128 spatial BSPO:0000129 peripheral side BSPO:0000129 spatial BSPO:0000130 axial side BSPO:0000130 An anatomical axis that extends from the side of the anatomical entity that is closer to an axis (adaxial) to the side that is further from the same axis (abaxial). An anatomical axis that extends from the side of the anatomical entity that is closer to an axis (adaxial) to the side that is further from the same axis (abaxial). wasila.dahdul 2013-07-02T11:20:29Z AA axis spatial dorsal-ventral axis BSPO:0000195 adaxial-abaxial axis BSPO:0000195 An anatomical axis that extends from the side of the anatomical entity that is closer to an axis (adaxial) to the side that is further from the same axis (abaxial). BSPO:RW An anatomical axis that extends from the center of the body outwards or externally. An anatomical axis that extends from the center of the body outwards or externally. wasila.dahdul 2013-07-02T11:21:42Z spatial proximal-distal axis BSPO:0000196 The medial-external axis could apply to a sphere-shaped body. medial-external axis BSPO:0000196 An anatomical axis that extends from the center of the body outwards or externally. BSPO:curators An anatomical axis that is perpendicular to an apical/basal axis or proximal/distal axis and extends from the center of an axis (shoot axis or root in the case of plants) to any point on the exterior of the axis. An anatomical axis that is perpendicular to an apical/basal axis or proximal/distal axis and extends from the center of an axis (shoot axis or root in the case of plants) to any point on the exterior of the axis. wasila.dahdul 2013-07-02T11:23:31Z M-R axis MR axis spatial BSPO:0000197 In plants, lateral growth (http://purl.obolibrary.org/obo/GO_0080190) run is along the medial/radial axis (from medial to radial) [RW]. Also applies to radially symmetrical animals such as sea urchins, cnidarians [PM] or applies to more-or-less cylindrical body parts in animals, like limbs. medial-radial axis BSPO:0000197 An anatomical axis that is perpendicular to an apical/basal axis or proximal/distal axis and extends from the center of an axis (shoot axis or root in the case of plants) to any point on the exterior of the axis. BSPO:curators An axis that extends from the oral opening to the furthest point in an organism that is directly opposite. An axis that extends from the oral opening to the furthest point in an organism that is directly opposite. wasila.dahdul 2013-07-02T11:29:33Z spatial BSPO:0000198 oral-aboral axis BSPO:0000198 An axis that extends from the oral opening to the furthest point in an organism that is directly opposite. BSPO:PM An axis that extends from the animal end of an egg or early embryo to the opposite, vegetal end. In animals with yolk-bearing eggs, the vegetal end is the yolk bearing pole. (pertains to animals only - both vertebrate and invertebrate embryos). An axis that extends from the animal end of an egg or early embryo to the opposite, vegetal end. In animals with yolk-bearing eggs, the vegetal end is the yolk bearing pole. (pertains to animals only - both vertebrate and invertebrate embryos). wasila.dahdul 2013-07-02T11:30:13Z A-V axis AV axis animal/vegetal axis spatial BSPO:0000199 animal-vegetal axis BSPO:0000199 An axis that extends from the animal end of an egg or early embryo to the opposite, vegetal end. In animals with yolk-bearing eggs, the vegetal end is the yolk bearing pole. (pertains to animals only - both vertebrate and invertebrate embryos). BSPO:PM An axis of a plant structure that is determined by the direction of apical growth, either by an apical meristem or an apical cell. Apical is toward the direction of apical growth: toward the tip of a growing shoot axis, root, thallus, or non-vascular leaf. Basal is away from the direction of apical growth: toward the root-shoot junction in the case of the primary root or stem, toward the primary root or stem for higher order roots or branches, toward the point of attachment for non-vascular leaves, and toward the original point of growth (as determined in the embryo) for thalli. An axis of a plant structure that is determined by the direction of apical growth, either by an apical meristem or an apical cell. Apical is toward the direction of apical growth: toward the tip of a growing shoot axis, root, thallus, or non-vascular leaf. Basal is away from the direction of apical growth: toward the root-shoot junction in the case of the primary root or stem, toward the primary root or stem for higher order roots or branches, toward the point of attachment for non-vascular leaves, and toward the original point of growth (as determined in the embryo) for thalli. spatial BSPO:0000200 Plant structures that do not grow from an apical meristem, such as vascular leaves or petals, should be described using the proximal-distal axis. The proximal-distal axis may also be used for branches or lateral roots, and, in those cases, is concordant with the apical-basal axis. apical-basal axis relative to direction of growth BSPO:0000200 An axis of a plant structure that is determined by the direction of apical growth, either by an apical meristem or an apical cell. Apical is toward the direction of apical growth: toward the tip of a growing shoot axis, root, thallus, or non-vascular leaf. Basal is away from the direction of apical growth: toward the root-shoot junction in the case of the primary root or stem, toward the primary root or stem for higher order roots or branches, toward the point of attachment for non-vascular leaves, and toward the original point of growth (as determined in the embryo) for thalli. BSPO:RW Anatomical plane that is perpendicular to a radial plane. Anatomical plane that is perpendicular to a radial plane. wasila.dahdul 2014-01-22T15:34:31Z spatial BSPO:0000201 Need to add logical definitions. tangential plane BSPO:0000201 Anatomical plane that is perpendicular to a radial plane. BSPO:wd Anatomical plane that follows the two dimensions specified by an apical-basal axis relative to direction of growth and a medial-lateral axis. Anatomical plane that follows the two dimensions specified by an apical-basal axis relative to direction of growth and a medial-lateral axis. wasila.dahdul 2014-01-22T15:34:02Z spatial BSPO:0000202 Need to add logical definitions. radial plane BSPO:0000202 Anatomical plane that follows the two dimensions specified by an apical-basal axis relative to direction of growth and a medial-lateral axis. BSPO:wd Anatomical surface that is located on the anterior side of the body or body part. Anatomical surface that is located on the anterior side of the body or body part. FBql:00005848 spatial BSPO:0000371 anterior surface BSPO:0000371 Anatomical surface that is located on the anterior side of the body or body part. BSPO:wd Anatomical surface that is located on the posterior side of the body or body part. Anatomical surface that is located on the posterior side of the body or body part. FBql:00005849 spatial BSPO:0000372 posterior surface BSPO:0000372 Anatomical surface that is located on the posterior side of the body or body part. BSPO:wd Anatomical surface that is located on the apical side of the body or body part. Anatomical surface that is located on the apical side of the body or body part. FBql:00005854 spatial BSPO:0000373 apical surface BSPO:0000373 Anatomical surface that is located on the apical side of the body or body part. BSPO:wd Anatomical surface that is located on the basal side of the body or body part. Anatomical surface that is located on the basal side of the body or body part. FBql:00005855 spatial BSPO:0000374 basal surface BSPO:0000374 Anatomical surface that is located on the basal side of the body or body part. BSPO:wd FBql:00005851 spatial BSPO:0000376 contralateral surface BSPO:0000376 Anatomical surface that is located on the proximal side of the body or body part. Anatomical surface that is located on the proximal side of the body or body part. FBql:00005852 spatial BSPO:0000377 proximal surface BSPO:0000377 Anatomical surface that is located on the proximal side of the body or body part. BSPO:wd Anatomical surface that is located on the distal side of the body or body part. Anatomical surface that is located on the distal side of the body or body part. FBql:00005853 spatial BSPO:0000378 distal surface BSPO:0000378 Anatomical surface that is located on the distal side of the body or body part. BSPO:wd Anatomical surface that located on the dorsal side of the body or body part. Anatomical surface that located on the dorsal side of the body or body part. FBql:00005842 spatial BSPO:0000379 dorsal surface BSPO:0000379 Anatomical surface that located on the dorsal side of the body or body part. BSPO:wd Anatomical surface that is located on the same side of an organism or structure. Anatomical surface that is located on the same side of an organism or structure. FBql:00005850 spatial BSPO:0000381 ipsilateral surface BSPO:0000381 Anatomical surface that is located on the same side of an organism or structure. BSPO:wd Anatomical surface that located on the lateral side of the body or body part. Anatomical surface that located on the lateral side of the body or body part. FBql:00005844 spatial BSPO:0000382 lateral surface BSPO:0000382 Anatomical surface that located on the lateral side of the body or body part. BSPO:wd Anatomical surface that located on the medial side of the body or body part. Anatomical surface that located on the medial side of the body or body part. FBql:00005847 spatial BSPO:0000383 medial surface BSPO:0000383 Anatomical surface that located on the medial side of the body or body part. BSPO:wd Anatomical surface that is located on the ventral side of the body or body part. Anatomical surface that is located on the ventral side of the body or body part. FBql:00005843 spatial BSPO:0000384 ventral surface BSPO:0000384 Anatomical surface that is located on the ventral side of the body or body part. BSPO:wd A flat 2D plane intersecting an anatomical continuant, dividing it into two adjacent portions. A flat 2D plane intersecting an anatomical continuant, dividing it into two adjacent portions. FMA:242982 anatomical cross-section anatomical section plane section spatial cross-section BSPO:0000400 These anatomical sections are applicable to most bilaterally symmetrical animals, but bipedal animals such as humans have more complex usage of these terms. For example, in post-embryonic humans a coronal plane is vertical and a transverse plane is horizontal, but for embryos and quadrupeds a coronal plane is horizontal and a transverse plane is vertical. anatomical plane BSPO:0000400 A flat 2D plane intersecting an anatomical continuant, dividing it into two adjacent portions. BSPO:cjm Anatomical plane that divides a bilateral body into left and right parts, not necessarily of even size. Anatomical plane that divides a bilateral body into left and right parts, not necessarily of even size. FMA:11361 left/right plane median plane sagittal section spatial BSPO:0000417 sagittal plane BSPO:0000417 Anatomical plane that divides a bilateral body into left and right parts, not necessarily of even size. BSPO:DOS BSPO:cjm BSPO:mah Anatomical margin that is located on the anterior side of a body or body part. Anatomical margin that is located on the anterior side of a body or body part. spatial BSPO:0000671 anterior margin BSPO:0000671 Anatomical margin that is located on the anterior side of a body or body part. BSPO:wd Anatomical margin that is located on the posterior side of the body or body part. Anatomical margin that is located on the posterior side of the body or body part. spatial BSPO:0000672 posterior margin BSPO:0000672 Anatomical margin that is located on the posterior side of the body or body part. BSPO:wd Anatomical margin that is located on the apical side of the body or body part. Anatomical margin that is located on the apical side of the body or body part. spatial BSPO:0000673 apical margin BSPO:0000673 Anatomical margin that is located on the apical side of the body or body part. BSPO:wd Anatomical margin that is located on the basal side of the body or body part. Anatomical margin that is located on the basal side of the body or body part. spatial BSPO:0000674 basal margin BSPO:0000674 Anatomical margin that is located on the basal side of the body or body part. BSPO:wd Anatomical margin that is located on the proximal region of the body or body part. Anatomical margin that is located on the proximal region of the body or body part. spatial BSPO:0000677 proximal margin BSPO:0000677 Anatomical margin that is located on the proximal region of the body or body part. BSPO:wd Anatomical margin that is located on the distal side of the body or body part. Anatomical margin that is located on the distal side of the body or body part. spatial BSPO:0000678 distal margin BSPO:0000678 Anatomical margin that is located on the distal side of the body or body part. BSPO:wd Anatomical margin that is located on the dorsal side of body or body part. Anatomical margin that is located on the dorsal side of body or body part. spatial BSPO:0000679 dorsal margin BSPO:0000679 Anatomical margin that is located on the dorsal side of body or body part. BSPO:wd Anatomical margin that is located on the dorso-lateral region of the body or body part. Anatomical margin that is located on the dorso-lateral region of the body or body part. dorsolateral margin spatial BSPO:0000680 dorso-lateral margin BSPO:0000680 Anatomical margin that is located on the dorso-lateral region of the body or body part. BSPO:wd Anatomical margin that is located on the lateral side of the body or body part. Anatomical margin that is located on the lateral side of the body or body part. spatial BSPO:0000682 lateral margin BSPO:0000682 Anatomical margin that is located on the lateral side of the body or body part. BSPO:wd Anatomical margin that is located on the medial side of the body or body part. Anatomical margin that is located on the medial side of the body or body part. spatial BSPO:0000683 medial margin BSPO:0000683 Anatomical margin that is located on the medial side of the body or body part. BSPO:wd Anatomical margin that is located on the ventral side of the body or body part. Anatomical margin that is located on the ventral side of the body or body part. spatial BSPO:0000684 ventral margin BSPO:0000684 Anatomical margin that is located on the ventral side of the body or body part. BSPO:wd Anatomical margin that is located on the ventro-lateral region of the body or body part. Anatomical margin that is located on the ventro-lateral region of the body or body part. ventrolateral margin spatial BSPO:0000685 This is an example of a composition of two axis positions ventro-lateral margin BSPO:0000685 Anatomical margin that is located on the ventro-lateral region of the body or body part. BSPO:wd Anatomical margin that is located on the antero-dorso region of the body or body part. Anatomical margin that is located on the antero-dorso region of the body or body part. anterodorsal margin spatial BSPO:0000686 antero-dorsal margin BSPO:0000686 Anatomical margin that is located on the antero-dorso region of the body or body part. BSPO:wd Anatomical margin that is located on the postero-dorsal region of the body or body part. Anatomical margin that is located on the postero-dorsal region of the body or body part. posterodorsal margin spatial BSPO:0000687 postero-dorsal margin BSPO:0000687 Anatomical margin that is located on the postero-dorsal region of the body or body part. BSPO:wd Anatomical margin that is located on the antero-ventral region of the body or body part. Anatomical margin that is located on the antero-ventral region of the body or body part. anteroventral margin spatial BSPO:0000688 antero-ventral margin BSPO:0000688 Anatomical margin that is located on the antero-ventral region of the body or body part. BSPO:wd Anatomical margin that is located on the postero-ventral region of the body or body part. Anatomical margin that is located on the postero-ventral region of the body or body part. posteroventral margin spatial BSPO:0000689 postero-ventral margin BSPO:0000689 Anatomical margin that is located on the postero-ventral region of the body or body part. BSPO:wd An axis that extends from the center of organism to one or other side. An axis that extends from the center of organism to one or other side. http://upload.wikimedia.org/wikipedia/commons/3/34/Anatomical_Directions_and_Axes.JPG M-L axis ML axis medio-lateral axis mediolateral axis spatial proximal-distal axis BSPO:0001001 Properly, the ML axis is a half axis; practically, its usage is less clumsy and less linguistically biased than "left-right". The terms may still be used relatively to describe locations along the LR axis. The gills are medial to the operculum, but lateral to the heart. medial-lateral axis BSPO:0001001 An axis that extends from the center of organism to one or other side. BSPO:cjm material anatomical entity An anatomical entity that has mass. An anatomical entity that has mass. UBERON:0000465 spatial CARO:0000006 material anatomical entity CARO:0000006 An anatomical entity that has mass. CC:DOS An anatomical entity that has no mass. An anatomical entity that has no mass. spatial CARO:0000007 immaterial anatomical entity CARO:0000007 An anatomical entity that has no mass. CC:DOS A one dimensional, immaterial anatomical entity. A one dimensional, immaterial anatomical entity. spatial CARO:0000008 anatomical line CARO:0000008 A one dimensional, immaterial anatomical entity. CC:DOS A non-material anatomical entity of two dimensions. Anatomical boundaries are contiguous structures. A non-material anatomical entity of two dimensions. Anatomical boundaries are contiguous structures. spatial CARO:0000010 anatomical boundary CARO:0000010 A non-material anatomical entity of two dimensions. Anatomical boundaries are contiguous structures. CC:DOS CHEBI:10023 A triazole-based antifungal agent used for the treatment of esophageal candidiasis, invasive pulmonary aspergillosis, and serious fungal infections caused by Scedosporium apiospermum and Fusarium spp. It is an inhibitor of cytochrome P450 2C9 (CYP2C9) and CYP3A4. Beilstein:7694998 CAS:137234-62-9 DrugBank:DB00582 Drug_Central:2846 LINCS:LSM-5244 PMID:12940129 PMID:22718362 PMID:23392902 PMID:23527908 PMID:23766489 PMID:24102553 (2R,3S)-2-(2,4-difluorophenyl)-3-(5-fluoropyrimidin-4-yl)-1-(1H-1,2,4-triazol-1-yl)butan-2-ol voriconazole (R-(R*,S*))-alpha-(2,4-difluorophenyl)-5-fluoro-beta-methyl-alpha-(1H-1,2,4-triazol-1-ylmethyl)-4-pyrimidineethanol (alphaR,betaS)-alpha-(2,4-difluorophenyl)-5-fluoro-beta-methyl-alpha(1H-1,2,4-triazol-1-ylmethyl)-4-pyrimidineethanol VCZ Vfend voriconazol voriconazole voriconazolum voriconazole Beilstein:7694998 Beilstein CAS:137234-62-9 ChemIDplus CAS:137234-62-9 DrugBank Drug_Central:2846 DrugCentral PMID:12940129 Europe PMC PMID:22718362 Europe PMC PMID:23392902 Europe PMC PMID:23527908 Europe PMC PMID:23766489 Europe PMC PMID:24102553 Europe PMC CHEBI:100241 A quinolone that is quinolin-4(1H)-one bearing cyclopropyl, carboxylic acid, fluoro and piperazin-1-yl substituents at positions 1, 3, 6 and 7, respectively. Beilstein:3568352 CAS:85721-33-1 DrugBank:DB00537 Drug_Central:659 LINCS:LSM-5226 PMID:10397494 PMID:10737746 Reaxys:3568352 1-cyclopropyl-6-fluoro-4-oxo-7-(piperazin-1-yl)-1,4-dihydroquinoline-3-carboxylic acid Ciprofloxacin ciprofloxacin 1-CYCLOPROPYL-6-FLUORO-4-OXO-7-PIPERAZIN-1-YL-1,4-DIHYDROQUINOLINE-3-CARBOXYLIC ACID 1-Cyclopropyl-6-fluoro-4-oxo-7-piperazin-1-yl-1,4-dihydro-quinoline-3-carboxylic acid 1-Cyclopropyl-6-fluoro-7-(4-methyl-piperazin-1-yl)-4-oxo-1,4-dihydro-quinoline-3-carboxylic acid 1-cyclopropyl-6-fluoro-1,4-dihydro-4-oxo-7-(1-piperazinyl)-3-quinolinecarboxylic acid 1-cyclopropyl-6-fluoro-4-oxo-7-(piperazin-1-yl)-1,4-dihydroquinoline-3-carboxylic acid 1-cyclopropyl-6-fluoro-4-oxo-7-piperazin-1-ylquinoline-3-carboxylic acid 1-cyclopropyl-6-fluoro-7-hexahydro-1-pyrazinyl-4-oxo-1,4-dihydro-3-quinolinecarboxylic acid ciprofloxacin ciprofloxacine ciprofloxacino ciprofloxacinum ciprofloxacin Beilstein:3568352 Beilstein CAS:85721-33-1 ChemIDplus Drug_Central:659 DrugCentral PMID:10397494 ChEMBL PMID:10737746 ChEMBL Reaxys:3568352 Reaxys CHEBI:10100 Beilstein:3641829 CAS:107753-78-6 DrugBank:DB00549 Drug_Central:2855 LINCS:LSM-5792 PMID:11888331 PMID:19331987 PMID:22159431 PMID:22614107 PMID:24258705 PMID:25798389 PMID:25834030 Reaxys:3641829 cyclopentyl 3-[2-methoxy-4-(2-methylphenylsulfonylcarbamoyl)benzyl]-1-methyl-1H-indol-5-ylcarbamate 4-(5-cyclopentyloxycarbonylamino-1-methyl-1H-indol-3-ylmethyl)-3-methoxy-N-o-tolylsulfonylbenzamide Accolate cyclopentyl 3-(2-methoxy-4-((o-tolylsulfonyl)carbamoyl)benzyl)-1-methylindole-5-carbamate zafirlukast zafirlukast Beilstein:3641829 Beilstein CAS:107753-78-6 ChemIDplus Drug_Central:2855 DrugCentral PMID:11888331 Europe PMC PMID:19331987 Europe PMC PMID:22159431 Europe PMC PMID:22614107 Europe PMC PMID:24258705 Europe PMC PMID:25798389 Europe PMC PMID:25834030 Europe PMC Reaxys:3641829 Reaxys CHEBI:10110 A pyrimidine 2',3'-dideoxyribonucleoside compound having a 3'-azido substituent and thymine as the nucleobase. C10H13N5O4 Cc1cn([C@H]2C[C@H](N=[N+]=[N-])[C@@H](CO)O2)c(=O)[nH]c1=O Beilstein:763034 CAS:30516-87-1 DrugBank:DB00495 Drug_Central:2861 LINCS:LSM-5806 PMID:19112024 PMID:26859826 PMID:29438107 PMID:9203666 Wikipedia:Zidovudine 3'-azido-3'-deoxythymidine AZT AZT Azidothymidine Retrovir Zidovudin Zidovudinum zidovudine zidovudine Beilstein:763034 Beilstein CAS:30516-87-1 ChemIDplus CAS:30516-87-1 DrugBank Drug_Central:2861 DrugCentral PMID:19112024 ChEMBL PMID:26859826 Europe PMC PMID:29438107 Europe PMC PMID:9203666 Europe PMC CHEBI:10112 A member of the class of 1-benzothiophenes that is 1-benzothiophene in which the hydrogen at position 2 is replaced by a 1-[carbamoyl(hydroxy)amino]ethyl group. A selective 5-lipoxygenase inhibitor, it inhibits the formation of leukotrienes LTB4, LTC4, LDT4, and LTE4. It is used for the management of chronic asthma. CAS:111406-87-2 DrugBank:DB00744 Drug_Central:2862 LINCS:LSM-5084 PMID:19309543 PMID:19645854 PMID:20204486 PMID:20436887 Reaxys:4869674 1-[1-(1-benzothien-2-yl)ethyl]-1-hydroxyurea Zileuton (+-)-1-(1-Benzo[b]thien-2-ylethyl)-1-hydroxyurea Leutrol N-(1-Benzo(b)thien-2-ylethyl)-N-hydroxyurea N-[1-(benzo[b]thiophen-2-yl)ethyl]-N-hydroxyurea Zyflo zileuton zileutonum zileuton CAS:111406-87-2 ChemIDplus Drug_Central:2862 DrugCentral PMID:19309543 Europe PMC PMID:19645854 Europe PMC PMID:20204486 Europe PMC PMID:20436887 Europe PMC Reaxys:4869674 Reaxys CHEBI:101278 A 5-[2-(dimethylamino)ethyl]-2-(4-methoxyphenyl)-4-oxo-2,3,4,5-tetrahydro-1,5-benzothiazepin-3-yl acetate in which both stereocentres have S configuration. A calcium-channel blocker and vasodilator, it is used as the hydrochloride in the management of angina pectoris and hypertension. Beilstein:3573079 CAS:42399-41-7 DrugBank:DB00343 Drug_Central:897 LINCS:LSM-2523 PMID:11937779 PMID:16651034 PMID:19167257 PMID:23687551 PMID:24261918 PMID:25122162 PMID:8369596 Reaxys:3573079 (2S,3S)-5-[2-(dimethylamino)ethyl]-2-(4-methoxyphenyl)-4-oxo-2,3,4,5-tetrahydro-1,5-benzothiazepin-3-yl acetate (+)-cis-5-[2-(dimethylamino)ethyl]-2,3-dihydro-3-hydroxy-2-(p-methoxyphenyl)-1,5-benzothiazepin-4(5H)-one acetate ester (2S,3S)-5-(2-(dimethylamino)ethyl)-2-(4-methoxyphenyl)-4-oxo-2,3,4,5-tetrahydrobenzo[b][1,4]thiazepin-3-yl acetate (2S-cis)-3-(acetyloxy)-5-[2-(dimethylamino)ethyl]-2,3-dihydro-2-(4-methoxyphenyl)-1,5-benzothiazepin-4(5H)-one Acetic acid (2S,3S)-5-(2-dimethylamino-ethyl)-2-(4-methoxy-phenyl)-4-oxo-2,3,4,5-tetrahydro-benzo[b][1,4]thiazepin-3-yl ester D-cis-diltiazem d-cis-diltiazem diltiazem diltiazemum diltiazem Beilstein:3573079 Beilstein CAS:42399-41-7 ChemIDplus CAS:42399-41-7 NIST Chemistry WebBook Drug_Central:897 DrugCentral PMID:11937779 Europe PMC PMID:16651034 Europe PMC PMID:19167257 Europe PMC PMID:23687551 Europe PMC PMID:24261918 Europe PMC PMID:25122162 Europe PMC PMID:8369596 Europe PMC Reaxys:3573079 Reaxys CHEBI:101381 0 C17H30N2O5 InChI=1S/C17H30N2O5/c1-6-23-17(22)14-13(24-14)16(21)19-12(9-11(4)5)15(20)18-8-7-10(2)3/h10-14H,6-9H2,1-5H3,(H,18,20)(H,19,21)/t12-,13-,14-/m0/s1 SRVFFFJZQVENJC-IHRRRGAJSA-N 342.431 342.21548 O1[C@@H]([C@H]1C(=O)N[C@@H](CC(C)C)C(=O)NCCC(C)C)C(=O)OCC CAS:88321-09-9 PMID:32142651 PMID:32221306 E-64d E64D Aloxistatin PMID:32142651 Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. PMID:32221306 To investigate whether cathepsins are required for SARS-CoV-2 entry, HEK 293/hACE2 cells were treated with either a broad inhibitor for cathepsin B, H, L, and calpain (E64D), cathepsin L inhibitor (SID 26681509), or cathepsin B inhibitor (CA-074). E64D treatment of 293/hACE2 cells reduced entry of SARS-CoV-2 S pseudovirions by 92.5%, indicating that at least one of cathepsins or calpain might be required for SARS-CoV-2 entry (Fig. 4a). CHEBI:111517 A dicarboxylic acid that is malonic acid in which both methylene hydrogens have been replaced by methyl groups. C5H8O4 O=C(O)C(C(O)=O)(C)C CAS:595-46-0 dimethyl malonate dimethylmalonic acid CHEBI:114785 A quinazoline compound having a (3-ethynylphenyl)amino group at the 4-position and two 2-methoxyethoxy groups at the 6- and 7-positions. CAS:183321-74-6 DrugBank:DB00530 Drug_Central:1045 LINCS:LSM-1097 PMID:12270171 PMID:14684309 PMID:15711537 PMID:16014882 PMID:16014883 PMID:16480284 PMID:17889528 PMID:17983745 PMID:29448920 PMID:29579331 PMID:29687154 PMID:30039303 PMID:30071517 PMID:30150014 PMID:30158288 Reaxys:8798958 N-(3-ethynylphenyl)-6,7-bis(2-methoxyethoxy)quinazolin-4-amine [6,7-bis(2-methoxy-ethoxy)quinazoline-4-yl]-(3-ethynylphenyl)amine [6,7-bis-(2-methoxy-ethoxy)-quinazolin-4-yl]-(3-ethynyl-phenyl)-amine erlotinib erlotinibum erlotinib CAS:183321-74-6 ChemIDplus CAS:183321-74-6 DrugBank Drug_Central:1045 DrugCentral PMID:12270171 ChEMBL PMID:14684309 ChEMBL PMID:15711537 ChEMBL PMID:16014882 Europe PMC PMID:16014883 Europe PMC PMID:16480284 ChEMBL PMID:17889528 ChEMBL PMID:17983745 ChEMBL PMID:29448920 Europe PMC PMID:29579331 Europe PMC PMID:29687154 Europe PMC PMID:30039303 Europe PMC PMID:30071517 Europe PMC PMID:30150014 Europe PMC PMID:30158288 Europe PMC Reaxys:8798958 Reaxys CHEBI:116225 An N-methylated tetrahydroisoquinoline carrying phenyl and amino substituents at positions C-4 and C-8, respectively. Beilstein:484561 CAS:24526-64-5 DrugBank:DB04821 Drug_Central:1958 LINCS:LSM-4388 PMID:1502708 PMID:24766210 PMID:7189402 Reaxys:484561 2-methyl-4-phenyl-1,2,3,4-tetrahydroisoquinolin-8-amine Nomifensine (+-)-Nomifensin (+-)-Nomifensine 2-Methyl-4-phenyl-1,2,3,4-tetrahydro-isoquinolin-8-ylamine 8-Amino-2-methyl-4-phenyl-1,2,3,4-tetrahydroisoquinoline D,L-nomifensine Nomifenison Nomifensin Nomiphensine R/S-nomifensine nomifensina nomifensine nomifensinum nomifensine Beilstein:484561 Beilstein CAS:24526-64-5 ChemIDplus CAS:24526-64-5 NIST Chemistry WebBook Drug_Central:1958 DrugCentral PMID:1502708 Europe PMC PMID:24766210 Europe PMC PMID:7189402 Europe PMC Reaxys:484561 Reaxys CHEBI:119486 1,4-Dihydro-2H-3,1-benzoxazin-2-one substituted at the 4 position by cyclopropylethynyl and trifluoromethyl groups (S configuration) and at the 6 position by chlorine. A non-nucleoside reverse transcriptase inhibitor with activity against HIV, it is used with other antiretrovirals for combination therapy of HIV infection. Beilstein:7387333 CAS:154598-52-4 DrugBank:DB00625 Drug_Central:989 LINCS:LSM-5526 PMID:10576692 PMID:10673109 PMID:25017682 Reaxys:7387333 (4S)-6-chloro-4-(cyclopropylethynyl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-2-one Efavirenz (-)-6-CHLORO-4-CYCLOPROPYLETHYNYL-4-TRIFLUOROMETHYL-1,4-DIHYDRO-2H-3,1-BENZOXAZIN-2-ONE (S)-6-chloro-4-(cyclopropylethynyl)-1,4-dihydro-4-(trifluoromethyl)-2H-3,1-benzoxazin-2-one (S)-6-chloro-4-cyclopropylethynyl-4-trifluoromethyl-1,4-dihydro-benzo[d][1,3]oxazin-2-one 6-chloro-4-(2-cyclopropyl-1-ethynyl)-4-trifluoromethyl-(4S)-1,4-dihydro-2H-benzo[d][1,3]oxazin-2-one efavirenz Beilstein:7387333 Beilstein CAS:154598-52-4 ChemIDplus Drug_Central:989 DrugCentral PMID:10576692 ChEMBL PMID:10673109 ChEMBL PMID:25017682 Europe PMC Reaxys:7387333 Reaxys CHEBI:127342 A secondary amino compound having methyl and 3-(2-methylphenoxy)-3-phenylpropan-1-yl substituents. Beilstein:4318684 CAS:83015-26-3 DrugBank:DB00289 Drug_Central:256 LINCS:LSM-2452 PMID:15338851 PMID:23048018 Reaxys:4318684 (3R)-N-methyl-3-(2-methylphenoxy)-3-phenylpropan-1-amine (-)-Tomoxetine Tomoxetina Tomoxetinum atomoxetine tomoxetine atomoxetine Beilstein:4318684 Beilstein CAS:83015-26-3 ChemIDplus Drug_Central:256 DrugCentral PMID:15338851 Europe PMC PMID:23048018 Europe PMC Reaxys:4318684 Reaxys CHEBI:132742 A member of the class of lysophosphatidic acids obtained by hydrolytic removal of one of the two acyl groups of any phosphatidic acid. A 'closed' class. MeSH:C032881 PMID:20118541 Lysophosphatidic acid (LPA) is a lipid mediator that is known to exhibit chemotactic activity toward a variety of cancer cells. However, its effect on the immune system has not been studied extensively. Another lipid mediator, sphingosine-1-phosphate (S1P), has been shown to influence lymphocyte recirculation by regulating lymphocyte egress from lymphoid organs. In this study, we found that LPA inhibits spontaneous migration of mouse splenic lymphocytes through a chemorepulsive effect. We also demonstrated that LPA inhibits chemokine CCL21-induced lymphocyte migration. This inhibitory effect on CCL21-induced migration was observed for both T and B cells. The involvement of a receptor, LPA(1), LPA(2) or LPA(3), in the inhibition of the CCL21-induced migration was confirmed with a synthetic agonist, oleyl thiophosphate. Considering that the signaling by CCL21 through cognate receptor CCR7 contributes to lymphocyte homing and dendritic cell trafficking to lymph nodes, LPA may play a role as a key regulator of these processes. The inhibitory effect of LPA is in remarkable contrast to the effect of S1P receptor signaling, which is known to potentiate lymphocyte chemotaxis involving CCR7. PMID:7768880 Lysophosphatidic acid, a multifunctional phospholipid messenger. Lysophosphatidic acid (LPA1(1); 1-acyl-glycerol-3-phosphate),is the simplest of all glycerophospholipids. While LPA has long been known as a precursor of phospholipid biosynthesis in both eukaryotic and prokaryotic cells, only recently has LPA emerged as an intercellular signaling molecule that is rapidly produced and released by activated cells, notably platelets, to influence target cells by acting on a specific cell-surface receptor. The list of biological responses to LPA is quite diverse, ranging from induction of cell proliferation to stimulation of neurite retraction. The mitogenic activities of LPA have been best studied in fibroblasts. As with peptide growth factors, induction of DNA synthesis by LPA requires its long term presence in the medium LPA, but not peptide growth factors, can mimic serum in inducing invasion of carcinoma and hepatoma cells into monolayers of mesothelial cells. The underlying mechanism is not clear but may well involve both increased cell adhesion and enhanced cell motility. Many mitogens activate the p85/p110 phosphatidylinositol (PI) 3-kinase in their target cells and so does LPA. LPA-induced PI 3-kinase activity has been found in 3T3 cells (Ref. 44; but see ref. 45 for conflicting data) and in megakaryoblastic cells. Whatever its precise link to the LPA receptor and physiological function, PI 3-kinase does not seem to be essential for mitogenic signaling, since microinjection of a neutralizing antibody does not affect LPA-induced DNA synthesis. LPA lysophosphatidic acid CHEBI:132933 A class of lipoproteins with a density between that of low-density and very-low-density lipoproteins. They are formed by the degradatiion of very-low-density lipoproteins. IDL intermediate-density lipoprotein CHEBI:132972 An agonist that binds to and activates farnesoid X receptors Wikipedia:Farnesoid_X_receptor BAR agonist FXR agonist bile acid receptor agonist farnesoid X receptor agonist CHEBI:132992 A drug that makes increases the sensitivity of tumour cells to radiation therapy. PMID:12520460 radiosensitiser radiosensitisers radiosensitising agent radiosensitising agents radiosensitizer radiosensitizers radiosensitizing agents radiosensitizing agent PMID:12520460 Europe PMC CHEBI:133190 A role played by the entity which inhibits the oxidation of any fatty acid. fatty acid oxidation inhibitor CHEBI:13389 Abbreviation for nicotinamide-adenine dinucleotide when its oxidation state is unknown or unspecified. It is used in metabolic pathways like glycolysis and citric acid cycle. Wikipedia:Nicotinamide_adenine_dinucleotide NAD CHEBI:134722 C5H4FN3O2 InChI=1S/C5H4FN3O2/c6-2-1-8-5(11)3(9-2)4(7)10/h1H,(H2,7,10)(H,8,11) ZCGNOVWYSGBHAU-UHFFFAOYSA-N N=1C(=CN=C(C1C(=O)N)O)F CAS:259793-96-9 Drug_Central:4887 T-705 avigan favipiravir CHEBI:134728 CAS:65-64-5 Drug_Central:4865 ICI-31397 actomol mebanazine hydrochloride mebanazine monohydrochloride mebanazine monooxalate mebanazine monosulfate mebanazine oxalate mebanazine sulfate mebanazine CAS:65-64-5 DrugCentral Drug_Central:4865 DrugCentral CHEBI:134762 CAS:4214-72-6 Drug_Central:1485 N-(Isopropylamino)-2-pyrimidine isaxonine CAS:4214-72-6 DrugCentral Drug_Central:1485 DrugCentral CHEBI:134891 CAS:547-44-4 Drug_Central:2496 sulfanilcarbamid sulfanilylurea sulfaurea sulphacarbamide sulphaurea urosulfan urosulfane sulfacarbamide CAS:547-44-4 DrugCentral Drug_Central:2496 DrugCentral CHEBI:134965 CAS:7175-09-9 Drug_Central:2662 5-Methyl-7-bromo-8-hydroxyquinoline tilbroquinol CAS:7175-09-9 DrugCentral Drug_Central:2662 DrugCentral CHEBI:135005 CAS:92623-85-3 Drug_Central:1808 (+/-)-Milnacipran midalcipran milnacipran HCl milnacipran hydrochloride milnacipran CAS:92623-85-3 DrugCentral Drug_Central:1808 DrugCentral CHEBI:135009 CAS:21721-92-6 Drug_Central:1946 altimol nitrefazole CAS:21721-92-6 DrugCentral Drug_Central:1946 DrugCentral CHEBI:135028 Pirprofen was a nonsteroidal anti-inflammatory drug (NSAID) that was brought to market by Ciba-Geigy in 1982 as a treatment for arthritis and pain. (by Wikipedia) C13H14ClNO2 ClC1=C(C=CC(=C1)C(C(O)=O)C)N2CC=CC2 CAS:31793-07-4 DrugBank:DB13722 Drug_Central:2213 Wikipedia:Pirprofen racemic pirprofen rengasil pirprofen CAS:31793-07-4 DrugCentral Drug_Central:2213 DrugCentral CHEBI:135273 CAS:5310-55-4 Drug_Central:3717 clomacran phosphate clomacran CAS:5310-55-4 DrugCentral Drug_Central:3717 DrugCentral CHEBI:135357 CAS:56775-88-3 Drug_Central:2863 cis-Zimelidine zimeldine hydrochloride hydrate zimelidine zimelidine HCl zimelidine dihydrochloride zimelidine dihydrochloride hydrate zimelidine dihydrochloride monohydrate zimelidine hydrochloride zimeldine CAS:56775-88-3 DrugCentral Drug_Central:2863 DrugCentral CHEBI:135358 CAS:125-13-3 Drug_Central:2038 oxyphenisatin phenolisatin veripaque oxyphenisatine CAS:125-13-3 DrugCentral Drug_Central:2038 DrugCentral CHEBI:135466 C19H17N5O2 InChI=1S/C19H17N5O2/c20-17(21)14-2-1-13-10-16(8-5-12(13)9-14)26-18(25)11-3-6-15(7-4-11)24-19(22)23/h1-10H,(H3,20,21)(H4,22,23,24) MQQNFDZXWVTQEH-UHFFFAOYSA-N C(=N)(N)C1=CC=2C(C=C1)=CC(=CC2)OC(=O)C3=CC=C(C=C3)NC(=N)N CAS:81525-10-2 Drug_Central:1867 PMID:32346093 ronastat nafamostat HOIP_0036114 PMID:32346093 Nafamostat mesylate and camostat mesylate are known inhibitors of TMPRSS2. CHEBI:135512 CAS:25803-14-9 Drug_Central:698 clometacine clometazin clomethacin duperan mindolic acid clometacin CAS:25803-14-9 DrugCentral Drug_Central:698 DrugCentral CHEBI:135632 0 C20H22N4O5 InChI=1S/C20H22N4O5/c1-24(2)17(25)12-28-18(26)11-13-3-9-16(10-4-13)29-19(27)14-5-7-15(8-6-14)23-20(21)22/h3-10H,11-12H2,1-2H3,(H4,21,22,23) XASIMHXSUQUHLV-UHFFFAOYSA-N 398.413 398.15903 C(OC1=CC=C(C=C1)CC(OCC(N(C)C)=O)=O)(=O)C2=CC=C(C=C2)NC(=N)N CAS:59721-28-7 Drug_Central:471 camostat CHEBI:135641 CAS:84-04-8 Drug_Central:2180 mornidine nausidol nometine pipamazine CAS:84-04-8 DrugCentral Drug_Central:2180 DrugCentral CHEBI:135649 C21H23Cl2N3O C(C(N(CCC)CCC)=O)C1=C(N=C2N1C=C(C=C2)Cl)C3=CC=C(C=C3)Cl CAS:82626-01-5 Drug_Central:134 Wikipedia:Alpidem Alpidem (Ananxyl) is an anxiolytic drug from the imidazopyridine family, related to the more well known sleeping medication zolpidem. (by Wikipedia) Ananxyl ananxyl alpidem CAS:82626-01-5 DrugCentral Drug_Central:134 DrugCentral CHEBI:135666 CAS:145733-36-4 Drug_Central:3839 ANA-756 ANA756 verdia tasosartan CAS:145733-36-4 DrugCentral Drug_Central:3839 DrugCentral CHEBI:135706 CAS:84845-75-0 Drug_Central:4002 niperotidine HCl niperotidine hydrochloride perultid piperonyl ranitidine HCl piperonyl ranitidine hydrochloride niperotidine CAS:84845-75-0 DrugCentral Drug_Central:4002 DrugCentral CHEBI:135774 CAS:100981-43-9 Drug_Central:979 FI-3542 ebrodin ulsanic ebrotidine CAS:100981-43-9 DrugCentral Drug_Central:979 DrugCentral CHEBI:135814 CAS:68-90-6 Drug_Central:321 cardivix dilafurane benziodarone CAS:68-90-6 DrugCentral Drug_Central:321 DrugCentral CHEBI:135829 CAS:146961-76-4 Drug_Central:102 alatrofloxacin mesilate alatrofloxacin mesylate alatrofloxacin CAS:146961-76-4 DrugCentral Drug_Central:102 DrugCentral CHEBI:137209 sn-glycero-3-phosphonocholine glycerophosphonocholine CHEBI:137736 Any psychotropic drug that induces anxiety or panic. Wikipedia:Anxiogenic panicogenic anxiogenic CHEBI:140921 Any pathway inhibitor that inhibits the Hedgehog signalling pathway. Hedgehog pathway inhibitor Hedgehog pathway inhibitors Hedgehog signaling pathway inhibitors Hedgehog signaling pathway inhibitor CHEBI:142468 A chloroalkane that is propane in which a hydrogen from each of two adjacent carbons has been replaced by chlorines. C3H6Cl2 CC(CCl)Cl 1,2-dichloropropane CHEBI:142593 A monounsaturated fatty aldehyde that is nonanal that has undergone dehydrogenation to introduce a double bond at any position in the aliphatic chain and in which a hydrogen at position 4 has been replaced by a hydroxy group. 4-hydroxynonenal CHEBI:144367 A member of the class of pyridines that is pyridine substituted by a 3-oxo-3-(pyridin-4-yl)prop-1-en-1-yl group at position 3. An inhibitor of PFKFB3 kinase, an enzyme with a key role in glycolysis. C13H10N2O InChI=1S/C13H10N2O/c16-13(12-5-8-14-9-6-12)4-3-11-2-1-7-15-10-11/h1-10H/b4-3+ UOWGYMNWMDNSTL-ONEGZZNKSA-N N=1C=C(C=CC1)/C=C/C(C2=CC=NC=C2)=O CAS:18550-98-6 PMID:32697943 (2E)-3-(pyridin-3-yl)-1-(pyridin-4-yl)prop-2-en-1-one 3PO PMID:32697943 To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). CHEBI:144387 An EC 2.7.1.* (phosphotransferases with an alcohol group as acceptor) inhibitor that interferes with the action of 6-phosphofructo-2-kinase (EC 2.7.1.105). EC 2.7.1.105 (6-phosphofructo-2-kinase) inhibitor CHEBI:145994 A carboxylic ester resulting from the formal condensation of the carboxy group of N-[(S)-{[(2R,3S,4R,5R)-5-(4-aminopyrrolo[2,1-f][1,2,4]triazin-7-yl)-5-cyano-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(phenoxy)phosphoryl]-L-alanine with the hydroxy group of 2-ethylbutan-1-ol. A broad-spectrum antiviral prodrug with potent in vitro antiviral activity against a diverse panel of RNA viruses such as Ebola virus, MERS-CoV and SARS-CoV. It is currently in Phase III clinical trials for the treatment of Covid-19 in adults. 0 C27H35N6O8P InChI=1S/C27H35N6O8P/c1-4-18(5-2)13-38-26(36)17(3)32-42(37,41-19-9-7-6-8-10-19)39-14-21-23(34)24(35)27(15-28,40-21)22-12-11-20-25(29)30-16-31-33(20)22/h6-12,16-18,21,23-24,34-35H,4-5,13-14H2,1-3H3,(H,32,37)(H2,29,30,31)/t17-,21+,23+,24+,27-,42-/m0/s1 RWWYLEGWBNMMLJ-YSOARWBDSA-N 602.585 602.22540 [C@]1(O[C@@H]([C@H]([C@H]1O)O)CO[P@@](N[C@H](C(OCC(CC)CC)=O)C)(OC=2C=CC=CC2)=O)(C#N)C=3N4N=CN=C(C4=CC3)N CAS:1809249-3 CAS:1809249-37-3 DrugBank:DB14761 DrugBank:DB:14761 PMCID:PMC5630887 PMID:26934220 PMID:28124907 PMID:28262699 PMID:28659436 PMID:29511076 PMID:30275474 PMID:30987343 PMID:31142680 PMID:31233808 PMID:31924756 PMID:32020029 PMID:32054787 PMID:32094225 PMID:32145386 PMID:32147516 PMID:32152082 PMID:32412710 PMID:32505227 PMID:32629875 Wikipedia:Remdesivir https://www.drugbank.ca/drugs/DB14761 2-ethylbutyl N-[(S)-{[(2R,3S,4R,5R)-5-(4-aminopyrrolo[2,1-f][1,2,4]triazin-7-yl)-5-cyano-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(phenoxy)phosphoryl]-L-alaninate (2S)-2-{(2R,3S,4R,5R)-[5-(4-Aminopyrrolo[2,1-f][1,2,4]triazin-7-yl)-5-cyano-3,4-dihydroxy-tetrahydro-furan-2-ylmethoxy]phenoxy-(S)-phosphorylamino}propionic acid 2-ethyl-butyl ester 2-ethylbutyl (2S)-2-{[(S)-{[(2R,3S,4R,5R)-5-(4-aminopyrrolo[2,1-f][1,2,4]triazin-7-yl)-5-cyano-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(phenoxy)phosphoryl]amino}propanoate GS 5734 GS-5734 GS5734 remdesivir remdesivirum remdesivir PMID:32505227 PMID:32505227 PMID:32412710 Data from a randomized, placebo-controlled trial involving more than 1000 patients with severe Covid-19 showed that the antiviral agent remdesivir reduced time to clinical recovery; the benefit appeared greatest in patients who were receiving supplemental oxygen but were not intubated. PMID:32505227 Remdesivir inhibits RNA dependent RNA polymerase(RdRp) by binding to RNA strands and preventing additional nucleotides from being added, thereby terminating RNA transcription. PMID:32629875 In addition, the antiviral drug, remdesivir, which has received Emergency Use Authorization for the treatment of hospitalized patients with suspected or laboratory-confirmed, severe COVID-19 could also be beneficial to reduce replication and release of infectious particles (NCT04292730). CHEBI:149553 Any antiviral agent which inhibits the activity of coronaviruses. anticoronaviral agent CHEBI:149836 Tetracycline in which the hydroxy group at position 5 and the methyl group at position 6 are replaced by hydrogen, and with a dimethylamino substituent and an (N-tert-butylglycyl)amino substituent at positions 7 and 9, respectively. A glycylcycline antibiotic, it has activity against a broad range of Gram-positive and Gram-negative bacteria, including tetracycline-resistant organisms. It is used for the intravenous treatment of complicated skin and skin structure infections caused by susceptible organisms. CAS:220620-09-7 DrugBank:DB00560 Drug_Central:2661 PMID:17194827 PMID:17210772 PMID:17220399 PMID:17307973 PMID:17353238 PMID:17353249 Reaxys:8379453 (4S,4aS,5aR,12aS)-9-[(N-tert-butylglycyl)amino]-4,7-bis(dimethylamino)-3,10,12,12a-tetrahydroxy-1,11-dioxo-1,4,4a,5,5a,6,11,12a-octahydrotetracene-2-carboxamide (4S,4aS,5aR,12aS)-9-(2-(tert-butylamino)acetamido)-4,7-bis(dimethylamino)-1,4,4a,5,5a,6,11,12a-octahydro-3,10,12,12a-tetrahydroxy-1,11-dioxo-2-naphthacenecarboxamide tigecycline CAS:220620-09-7 ChemIDplus Drug_Central:2661 DrugCentral PMID:17194827 ChEMBL PMID:17210772 ChEMBL PMID:17220399 ChEMBL PMID:17307973 ChEMBL PMID:17353238 ChEMBL PMID:17353249 ChEMBL Reaxys:8379453 Reaxys CHEBI:15343 The aldehyde formed from acetic acid by reduction of the carboxy group. It is the most abundant carcinogen in tobacco smoke. Wikipedia:Acetaldehyde acetaldehyde CHEBI:15422 An adenosine 5'-phosphate in which the 5'-phosphate is a triphosphate group. It is involved in the transportation of chemical energy during metabolic pathways. CAS:56-65-5 DrugBank:DB00171 adenosine 5'-triphosphate adenosine triphosphate ATP CHEBI:15551 Prostaglandin F2alpha in which the hydroxy group at position 9 has been oxidised to the corresponding ketone. Prostaglandin E2 is the most common and most biologically potent of mammalian prostaglandins. XEYBRNLFEZDVAW-ARSRFYASSA-N CCCCC[C@H](O)\C=C\[C@H]1[C@H](O)CC(=O)[C@@H]1C\C=C/CCCC(O)=O (5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dien-1-oic acid Prostaglandin E2 HOIP_0041673 CHEBI:15554 CCCCC[C@H](O)\C=C\[C@H]1[C@H]2C[C@H](OO2)[C@@H]1C\C=C/CCCC(O)=O Prostaglandin H2 CHEBI:15555 A member of the class of prostaglandins D that is prosta-5,13-dien-1-oic acid substituted by hydroxy groups at positions 9 and 15 and an oxo group at position 11 (the 5Z,9alpha,13E,15S- stereoisomer). Prostaglandin D2 CHEBI:156289 A tetrapeptide consisting of N-decanoyl-L-arginine, L-valine, L-lysine, and L-arginine joined in sequence by peptide linkages and in which the carboxy group at the C-terminus is substituted by a chloroacetyl group. It is a furin inhibitor that has antiviral activity against Chikungunya virus, Zika virus and Japanese encephalitis virus. 0 C34H66ClN11O5 InChI=1S/C34H66ClN11O5/c1-4-5-6-7-8-9-10-18-28(48)43-25(17-14-21-42-34(39)40)31(50)46-29(23(2)3)32(51)45-26(15-11-12-19-36)30(49)44-24(27(47)22-35)16-13-20-41-33(37)38/h23-26,29H,4-22,36H2,1-3H3,(H,43,48)(H,44,49)(H,45,51)(H,46,50)(H4,37,38,41)(H4,39,40,42)/t24-,25-,26-,29-/m0/s1 NHBJTTGFHCHQHS-VZTVMPNDSA-N 744.42 743.4937 CCCCCCCCCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)CCl CAS:150113-99-8 PMID:32362314 Decanoyl-RVKR-CMK decanoyl-L-Arg-L-Val-L-Lys-L-Arg-chloromethylketone PMID:32362314 Decanoyl-RVKR-CMK inhibited processing of MERS-S, which is known to depend on furin (Gierer et al., 2015; Millet and Whittaker, 2014), in a concentration-dependent manner and had no effect on SARS-S expression (Figure 2C), as expected. Processing of SARS-2-S was also inhibited, indicating that furin cleaves SARS-2-S at the S1/S2 site. CHEBI:156297 An EC 3.4.21.* (serine endopeptidase) inhibitor that interferes with the action of furin (EC 3.4.21.75). furin inhibitor EC 3.4.21.75 (furin)inhibitor CHEBI:15647 A leukotriene composed of (6Z,8E,10E,14Z)-icosatetraenoic acid having (5S)- and (12R)-hydroxy substituents. leukotriene B4 CHEBI:15846 The oxidised form of nicotinamide adenine dinucleotide found in all living cells. In metabolism, NAD(+) is involved in redox reactions, carrying electrons from one reaction to another. NAD(+) CHEBI:15866 A deoxyglucose that is D-glucose in which the hydroxy group at position 2 has been replaced by a hydrogen. It is an antimetabolite of glucose with antiviral activity, which acts by inhibiting the glycosylation of glycoproteins and glycolipids. Used as an antiherpes agent. C6H12O5 CAS:154-17-6 2-deoxy-D-glucose CHEBI:15956 biotin An organic heterobicyclic compound that consists of 2-oxohexahydro-1H-thieno[3,4-d]imidazole having a valeric acid substituent attached to the tetrahydrothiophene ring. The parent of the class of biotins. biotin CHEBI:15986 A nucleobase-containing molecular entity with a polymeric structure comprised of a linear sequence of 13 or more nucleotide residues. polynucleotide CHEBI:15996 CAS:86-01-1 DrugBank:DB04137 guanosine 5'-triphosphate GTP CHEBI:16038 A class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxy group of ethanolamine. DrugBank:DB04327 PtdEtn phosphatidylethanolamine CHEBI:16113 A cholestanoid consisting of cholestane having a double bond at the 5,6-position as well as a 3β-hydroxy group. C27H46O C1[C@@]2([C@]3(CC[C@]4([C@]([C@@]3(CC=C2C[C@H](C1)O)[H])(CC[C@@]4([C@H](C)CCCC(C)C)[H])[H])C)[H])C Wikipedia:cholesterol cholesterol CHEBI:16152 IMR:0001353 ISBN:0815340729 1-O-(3-sn-phosphatidyl)-1D-myo-inositol 3,4-bis(dihydrogen phosphate) 1-Phosphatidyl-1D-myo-inositol 3,4-bisphosphate PtsIns(3,4)P2 PtsIns-3,4-P2 1-Phosphatidyl-1D-myo-inositol 3,4-bisphosphate ISBN:0815340729 ISBN:0815340729 CHEBI:16236 A primary alcohol that is ethane in which one of the hydrogens is substituted by a hydroxy group. C2H6O CCO ethanol CHEBI:16247 A lipid containing phosphoric acid as a mono- or di-ester. The term encompasses phosphatidic acids and phosphoglycerides. C5H6O8PR3 phospholipid CHEBI:16325 A monohydroxy-5β-cholanic acid with aα-hydroxy substituent at position 3. It is a bile acid obtained from chenodeoxycholic acid by bacterial action. C24H40O3 [H][C@]12CC[C@]3([H])[C@]([H])(CC[C@]4(C)[C@]([H])(CC[C@@]34[H])[C@H](C)CCC(O)=O)[C@@]1(C)CC[C@@H](O)C2 lithocholic acid CHEBI:16335 A ribonucleoside composed of a molecule of adenine attached to a ribofuranose moiety via a beta-N(9)-glycosidic bond. A nucleoside that is composed of adenine and d-ribose. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter. DrugBank:DB00640 Adenine riboside Adenosine Ribofuranosyladenine adenosine A nucleoside that is composed of adenine and d-ribose. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter. MeSH:D000241 CHEBI:16337 A derivative of glycerol in which one hydroxy group, commonly but not necessarily primary, is esterified with phosphoric acid and the other two are esterified with fatty acids. phosphatidic acid CHEBI:16359 A bile acid that is 5β-cholan-24-oic acid bearing threeα-hydroxy substituents at position 3, 7 and 12. InChIKey:BHQCQFFYRZLCQQ-OELDTZBJSA-N cholic acid CHEBI:16393 A sphing-4-enine in which the double bond is trans. IMR:0100178 Sphingenine Sphingoid sphingosine CHEBI:16412 Liposaccharide natural compounds consisting of a trisaccharide repeating unit (two heptose units and octulosonic acid) with oligosaccharide side chains and 3-hydroxytetradecanoic acid units (they are a major constituent of the cell walls of Gram-negative bacteria). LPS Lipopolysaccharide (LPS) is a glycosylated lipid on the outer surface of Gram-negative bacteria acts as immunostimulants. Lipopolysaccharide (LPS) is a glycosylated lipid on the outer surface of Gram-negative bacteria acts as immunostimulants. liposaccharide Lipopolysaccharide (LPS) is a glycosylated lipid on the outer surface of Gram-negative bacteria acts as immunostimulants. ISBN:0815340729 CHEBI:16469 The 17beta-isomer of estradiol. 17β-Estradiol CHEBI:16474 NADPH is the reduced form of NADP+; used in anabolic reactions, such as lipid and nucleic acid synthesis, which require NADPH as a reducing agent. CHEBI:16474 Wikipedia:NADPH 2'-O-phosphonoadenosine 5'-{3-[1-(3-carbamoyl-1,4-dihydropyridin-1-yl)-1,4-anhydro-D-ribitol-5-yl] dihydrogen diphosphate} InChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1 NADP-reduced NADPH CHEBI:16480 A nitrogen oxide which is a free radical, each molecule of which consists of one nitrogen and one oxygen atom. Wikipedia:Endothelium-derived_relaxing_factor Wikipedia:Nitric_oxide nitric oxide Wikipedia:Endothelium-derived_relaxing_factor Endothelium produces NO which then diffuses to the vascular smooth muscle tissue, although there seems to be evidence that vasodilation may also be of neuronal origin, rather than endothelial. NO is produced by the enzyme nitric oxide synthase and it relaxes smooth muscle tissue by promoting the synthesis of cGMP. Wikipedia:Nitric_oxide Nitric oxide, known as an endothelium-derived relaxing factor (EDRF), is biosynthesized endogenously from L-arginine, oxygen, and NADPH by various nitric oxide synthase (NOS) enzymes. CHEBI:16602 A member of the class of chloroethenes that is ethene substituted by chloro groups at positions 1, 1 and 2. C2HCl3 ClC=C(Cl)Cl CAS:79-01-6 Wikipedia:Trichloroethylene 1,1,2-trichloroethene trichloroethylene CHEBI:16618 IMR:0001352 1-O-(3-sn-phosphatidyl)-1D-myo-inositol 3,4,5-tris(dihydrogen phosphate) 1-Phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate Phosphatidylinositol-3,4,5-trisphosphate 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate PIP3 PtsIns(3,4,5)P3 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate CHEBI:16646 Any member of the class of organooxygen compounds that is a polyhydroxy-aldehyde or -ketone or a lactol resulting from their intramolecular condensation (monosaccharides); substances derived from these by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom; and polymeric products arising by intermolecular acetal formation between two or more such molecules (disaccharides, polysaccharides and oligosaccharides). Carbohydrates contain only carbon, hydrogen and oxygen atoms; prior to any oxidation or reduction, most have the empirical formula Cm(H2O)n. Compounds obtained from carbohydrates by substitution, etc., are known as carbohydrate derivatives and may contain other elements. Cyclitols are generally not regarded as carbohydrates. carbohydrate CHEBI:16664 A carbamate ester that is methyl 1H-benzimidazol-2-ylcarbamate substituted by a propylsulfanyl group at position 5. It is commonly used in the treatment of parasitic worm infestations. Beilstein:752696 CAS:54965-21-8 DrugBank:DB00518 Drug_Central:103 LINCS:LSM-3782 PMID:22152396 PMID:24403707 PMID:24411094 Pesticides:albendazole Reaxys:752696 Albendazole albendazole methyl [5-(propylsulfanyl)-1H-benzimidazol-2-yl]carbamate (5-(propylthio)-1H-benzimidazol-2-yl)carbamic acid methyl ester 5-(propylthio)-2-carbomethoxyaminobenzimidazole Albenza Eskazole O-methyl N-(5-(propylthio)-2-benzimidazolyl)carbamate Proftril Valbazen Zentel albendazole Beilstein:752696 Beilstein CAS:54965-21-8 ChemIDplus Drug_Central:103 DrugCentral PMID:22152396 Europe PMC PMID:24403707 Europe PMC PMID:24411094 Europe PMC Pesticides:albendazole Alan Wood's Pesticides Reaxys:752696 Reaxys CHEBI:16670 Amide derived from two or more amino carboxylic acid molecules (the same or different) by formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another with formal loss of water. The term is usually applied to structures formed from alpha-amino acids, but it includes those derived from any amino carboxylic acid. X = OH, OR, NH2, NHR, etc. peptide CHEBI:166964 Family of globular proteins, the most common of which are the serum albumins. All the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. albumin type CHEBI:167176 A benzamide resulting from the formal condensation of the carboxy group of 5-amino-2-methylbenzoic acid with the amino group of (1R)-1-(naphthalen-1-yl)ethan-1-amine. It is a potent noncovalent inhibitor (IC50 = 600 nM) of severe acute respiratory syndrome-coronavirus papain-like protease (SARS-CoV PLpro). C20H20N2O CC1=C(C=C(C=C1)N)C(=O)NC(C)C2=CC=CC3=CC=CC=C32 PubChem CID: 24941262 http://ctdbase.org/detail.go?type=chem&acc=C000714108 5-Amino-2-Methyl-N-[(1r)-1-Naphthalen-1-Ylethyl]benzamide GRL-0617 HOIP_0040210 CHEBI:16749 A phosphatidylinositol in which the inositol moiety is the 1D-myo isomer and the phosphatidyl group is located at its position 1. C11H17O13P [C@@H]1([C@@H]([C@@H]([C@@H]([C@H]([C@@H]1O)O)O)O)OP(OC[C@@H](COC(*)=O)OC(=O)*)(=O)O)O PMID:28600633 1-O-(3-sn-phosphatidyl)-1D-myo-inositol 1-phosphatidyl-1D-myo-inositol CHEBI:16750 A purine nucleoside in which guanine is attached to ribofuranose via a beta-N(9)-glycosidic bond. guanosine CHEBI:16761 A purine ribonucleoside 5'-diphosphate having adenine as the nucleobase. A purine ribonucleoside 5'-diphosphate having adenine as the nucleobase. CAS:20398-34-9 Adenosine 5'-monophosphate AMP CHEBI:167893 A carbohydrazide that is L-tryptophan in which the amino and carboxy groups are substituted by tert-butoxycarbonyl and 2-({[2-(2-ethylanilino)-2-oxoethyl]sulfanyl}carbonyl)hydrazinyl groups, respectively. It is a potent and reversible inhibitor of human cathepsin L (IC50 = 56 nM). C27H33N5O5S InChI=1S/C27H33N5O5S/c1-5-17-10-6-8-12-20(17)29-23(33)16-38-26(36)32-31-24(34)22(30-25(35)37-27(2,3)4)14-18-15-28-21-13-9-7-11-19(18)21/h6-13,15,22,28H,5,14,16H2,1-4H3,(H,29,33)(H,30,35)(H,31,34)(H,32,36)/t22-/m0/s1 OTIWAYTTYNFEKL-QFIPXVFZSA-N CCC1=CC=CC=C1NC(=O)CSC(=O)NNC(=O)C(CC2=CNC3=CC=CC=C32)NC(=O)OC(C)(C)C PMID:32221306 PubChem CID:16725315 SID 26681509 HOIP_0040032 PMID:32221306 To investigate whether cathepsins are required for SARS-CoV-2 entry, HEK 293/hACE2 cells were treated with either a broad inhibitor for cathepsin B, H, L, and calpain (E64D), cathepsin L inhibitor (SID 26681509), or cathepsin B inhibitor (CA-074). While cathepsin B inhibitor treatment did not show any marked effect on virus entry, cathepsin L inhibition treatment decreased entry of SARS-CoV-2 S pseudovirions into 293/hACE2 by over 76% (Fig. 4a), suggesting that cathepsin L should be essential for priming of SARS-CoV-2 S protein in lysosome for entry into 293/hACE2 cells. CHEBI:16851 C11H19O19P3R2 [H][C@@](COC([*])=O)(COP(O)(=O)O[C@H]1[C@H](O)[C@@H](OP(O)(O)=O)[C@H](O)[C@@H](OP(O)(O)=O)[C@H]1O)OC([*])=O PMID:32221306 1,2-Diacyl-sn-glycero-3-phospho-(1'-myo-inositol-3',5'-bisphosphate) PI(3,5)P2 PtsIns(3,5)P2 PtsIns-3,5-P2 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate PMID:32221306 Phosphoinositides play many essential roles in endocytosis. Among them, one is phosphatidylinositol-3,5-bisphosphate (PI(3,5)P2), which regulates early endosome to late endosome dynamics. Two pore channel subtype 2 (TPC2) and TRPML1 in lysosome are two major downstream effectors of PI(3,5)P2. We confirmed this in this study, and further showed that blocking PIKfyve and TPC2 also strongly inhibited entry mediated by SARS-CoV-2 S protein, indicating that PI(3,5)P2 pathway might be considered as potential general drug target for CoV infection. CHEBI:16856 A tripeptide compound consisting of glutamic acid attached via its side chain to the N-terminus of cysteinylglycine. C10H17N3O6S N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)O)C(=O)O DrugBank:DB00143 Wikipedia:Glutathione Glutathione 5-L-Glutamyl-L-cysteinylglycine GSH Reduced glutathione L-gamma-glutamyl-L-cysteinylglycine CHEBI:16908 A coenzyme found in all living cells; consists of two nucleotides joined through their 5'-phosphate groups, with one nucleotide containing an adenine base and the other containing nicotinamide. DrugBank:DB00157 Wikipedia:Nicotinamide_adenine_dinucleotide NADH CHEBI:16914 A monohydroxybenzoic acid that is benzoic acid with a hydroxy group at the ortho position. It is obtained from the bark of the white willow and wintergreen leaves. C7H6O3 OC(=O)c1ccccc1O CAS:69-72-7 DrugBank:DB00936 Wikipedia:Salicylic_acid 2-hydroxybenzoic acid salicylic acid CHEBI:16961 Derivatives of phosphoglycerols which have only one of the alcohol groups of the glycerol backbone ester-linked with a fatty acid. lysophospholipids monoacylglycerol phosphates monoacylglycerophosphate monoacylglycerophosphates Lysophospholipid monoacylglycerol phosphate CHEBI:16990 A member of the class of biladienes that is a linear tetrapyrrole with the dipyrrole units being of both exovinyl and endovinyl type. A product of heme degradation, it is produced in the reticuloendothelial system by the reduction of biliverdin and transported to the liver as a complex with serum albumin. C33H36N4O6 CC1=C(C=C)\C(NC1=O)=C\c1[nH]c(Cc2[nH]c(\C=C3NC(=O)C(C=C)=C/3C)c(C)c2CCC(O)=O)c(CCC(O)=O)c1C Wikipedia:Bilirubin bilirubin CHEBI:16991 deoxyribonucleic acid High molecular weight, linear polymers, composed of nucleotides containing deoxyribose and linked by phosphodiester bonds; DNA contain the genetic information of organisms. DNA deoxyribonucleic acid CHEBI:17234 An aldohexose used as a source of energy and metabolic intermediate. PMID:32697943 glucose PMID:32697943 Glucose directly increased viral load, ACE2, and IL-1b expression in CoV-2-infected monocytes in a dose-dependent manner (Figures 1D–1F). CHEBI:17263 An estrogen that has formula C18H22O2. ATC:G03CA07 ATC:G03CC04 CASRN:53-16-7 DrugBank:DB00655 InChIKey:DNXHEGUUPJUMQT-CBZIJGRNSA-N estrone CHEBI:17268 An inositol having myo- configuration. Wikipedia:Inositol myo-inositol CHEBI:17347 An androstanoid having 17beta-hydroxy and 3-oxo groups, together with unsaturation at C-4-C-5.. Beilstein:1915399 Beilstein:3653705 CAS:58-22-0 DrugBank:DB00624 Drug_Central:2607 Gmelin:538843 LIPID_MAPS_instance:LMST02020002 PMID:10438974 PMID:11786693 PMID:18900503 PMID:24498482 Reaxys:1915399 17beta-hydroxyandrost-4-en-3-one TESTOSTERONE Testosterone testosterone 17beta-Hydroxy-4-androsten-3-one 17beta-hydroxy-4-androsten-3-one 4-androsten-17beta-ol-3-one Androderm Testosteron testosterona testosterone testosteronum testosterone Beilstein:1915399 Beilstein Beilstein:3653705 Beilstein CAS:58-22-0 ChemIDplus CAS:58-22-0 NIST Chemistry WebBook Drug_Central:2607 DrugCentral Gmelin:538843 Gmelin LIPID_MAPS_instance:LMST02020002 LIPID MAPS PMID:10438974 Europe PMC PMID:11786693 Europe PMC PMID:18900503 Europe PMC PMID:24498482 Europe PMC Reaxys:1915399 Reaxys CHEBI:17356 The parent of the class of 2-acetamidofluorenes, being an ortho-fused polycyclic arene that consists of 9H-fluorene bearing an acetamido substituent at position 2. It is a carcinogenic and mutagenic derivative of fluorene. C15H13NO C(=O)(NC=1C=C2C(C=3C(C2)=CC=CC3)=CC1)C CAS:53-96-3 Wikipedia:2-Acetylaminofluorene N-(9H-fluoren-2-yl)acetamide 2-AAF 2-Acetylaminofluorene 2-acetamidofluorene CHEBI:17361 A cytidine 5'-phosphate that has formula C9H14N3O8P. CMP CHEBI:17478 A compound RC(2O)H, in which a carbonyl group is bonded to one hydrogen atom and to one R group. aldehyde CHEBI:17517 A glycerophosphoglycerol that is glycerol in which the hydrogen of one of the primary hydroxy groups has been replaced by a phosphatidyl group. phosphatidylglycerol CHEBI:175901 A 2'-deoxycytidine having geminal fluoro substituents in the 2'-position. An inhibitor of ribonucleotide reductase, gemcitabine is used in the treatment of various carcinomas, particularly non-small cell lung cancer, pancreatic cancer, bladder cancer and breast cancer. Beilstein:5382060 CAS:95058-81-4 DrugBank:DB00441 Drug_Central:1283 LINCS:LSM-5333 PMID:11034044 PMID:11061612 PMID:11088063 PMID:11122828 PMID:11132538 PMID:11142482 PMID:11221019 PMID:11356111 PMID:11374818 PMID:11489002 PMID:11504793 PMID:11510027 PMID:11585734 PMID:11595724 PMID:11807603 PMID:11859947 PMID:11901308 PMID:12057041 PMID:12057046 PMID:12057157 PMID:12115355 PMID:12142097 PMID:12520460 PMID:12571808 PMID:12722678 PMID:12722691 PMID:12743987 PMID:12761494 PMID:12798170 PMID:12917815 PMID:12954073 PMID:14606642 PMID:14653877 PMID:14720338 PMID:15131028 PMID:15160243 PMID:15221904 PMID:15282439 PMID:15297392 PMID:15542781 PMID:15637766 PMID:15744590 PMID:16001951 PMID:16041610 PMID:16080557 PMID:16143373 PMID:16149285 PMID:16317298 PMID:16500746 PMID:16555971 PMID:16584929 PMID:16807461 PMID:16807463 PMID:16894289 PMID:16905983 PMID:17101674 PMID:17296311 PMID:17296587 PMID:17347561 PMID:17429628 PMID:17460420 PMID:17602464 PMID:17639396 PMID:17887663 PMID:17939651 PMID:17941128 PMID:17987263 PMID:18035967 PMID:18050344 PMID:18086345 PMID:18166944 PMID:18186604 PMID:18257544 PMID:18348652 PMID:18773046 PMID:18789834 PMID:18819792 PMID:18981552 PMID:19034448 PMID:19177022 PMID:19399788 PMID:19839926 PMID:19879060 PMID:22763439 PMID:28594276 PMID:28608357 PMID:28912244 Reaxys:5382060 2'-deoxy-2',2'-difluorocytidine 2',2'-Difluorodeoxycytidine 2'-Deoxy-2',2'-difluorocytidine 4-amino-1-((2R,4R,5R)-3,3-difluoro-4-hydroxy-5-(hydroxymethyl)-tetrahydrofuran-2-yl)pyrimidin-2(1H)-one gemcitabina gemcitabine gemcitabinum gemcitabine Beilstein:5382060 Beilstein CAS:95058-81-4 ChemIDplus CAS:95058-81-4 DrugBank Drug_Central:1283 DrugCentral PMID:11034044 Europe PMC PMID:11061612 Europe PMC PMID:11088063 Europe PMC PMID:11122828 Europe PMC PMID:11132538 Europe PMC PMID:11142482 Europe PMC PMID:11221019 Europe PMC PMID:11356111 ChEMBL PMID:11374818 Europe PMC PMID:11489002 Europe PMC PMID:11504793 Europe PMC PMID:11510027 Europe PMC PMID:11585734 Europe PMC PMID:11595724 Europe PMC PMID:11807603 Europe PMC PMID:11859947 Europe PMC PMID:11901308 Europe PMC PMID:12057041 Europe PMC PMID:12057046 Europe PMC PMID:12057157 Europe PMC PMID:12115355 Europe PMC PMID:12142097 Europe PMC PMID:12520460 Europe PMC PMID:12571808 Europe PMC PMID:12722678 Europe PMC PMID:12722691 Europe PMC PMID:12743987 Europe PMC PMID:12761494 Europe PMC PMID:12798170 Europe PMC PMID:12917815 Europe PMC PMID:12954073 Europe PMC PMID:14606642 Europe PMC PMID:14653877 Europe PMC PMID:14720338 Europe PMC PMID:15131028 Europe PMC PMID:15160243 Europe PMC PMID:15221904 Europe PMC PMID:15282439 Europe PMC PMID:15297392 Europe PMC PMID:15542781 Europe PMC PMID:15637766 Europe PMC PMID:15744590 Europe PMC PMID:16001951 Europe PMC PMID:16041610 Europe PMC PMID:16080557 Europe PMC PMID:16143373 Europe PMC PMID:16149285 Europe PMC PMID:16317298 Europe PMC PMID:16500746 Europe PMC PMID:16555971 Europe PMC PMID:16584929 Europe PMC PMID:16807461 Europe PMC PMID:16807463 Europe PMC PMID:16894289 Europe PMC PMID:16905983 Europe PMC PMID:17101674 ChEMBL PMID:17296311 Europe PMC PMID:17296587 Europe PMC PMID:17347561 Europe PMC PMID:17429628 Europe PMC PMID:17460420 Europe PMC PMID:17602464 ChEMBL PMID:17639396 Europe PMC PMID:17887663 ChEMBL PMID:17939651 ChEMBL PMID:17941128 Europe PMC PMID:17987263 Europe PMC PMID:18035967 Europe PMC PMID:18050344 Europe PMC PMID:18086345 Europe PMC PMID:18166944 Europe PMC PMID:18186604 ChEMBL PMID:18257544 ChEMBL PMID:18348652 Europe PMC PMID:18773046 Europe PMC PMID:18789834 Europe PMC PMID:18819792 Europe PMC PMID:18981552 Europe PMC PMID:19034448 Europe PMC PMID:19177022 Europe PMC PMID:19399788 Europe PMC PMID:19839926 Europe PMC PMID:19879060 Europe PMC PMID:22763439 Europe PMC PMID:28594276 Europe PMC PMID:28608357 Europe PMC PMID:28912244 Europe PMC Reaxys:5382060 Reaxys CHEBI:17677 cytidine 5'-(tetrahydrogen triphosphate) cytidine 5'-(tetrahydrogen triphosphate) CTP cytidine 5'-(tetrahydrogen triphosphate) IUPAC CHEBI:17747 A phthalate ester that is the bis(2-ethylhexyl) ester of benzene-1,2-dicarboxylic acid. C24H38O4 CCCCC(CC)COC(=O)c1ccccc1C(=O)OCC(CC)CCCC CAS:117-81-7 DEHP Diethylhexylphthalate bis(2-ethylhexyl) phthalate CHEBI:17761 Ceramides (N-acyl-sphingoid bases) are a major subclass of sphingoid base derivatives with an amide-linked fatty acid. The fatty acids are typically saturated or monounsaturated with chain lengths from 14 to 26 carbon atoms; the presence of a hydroxyl group on carbon 2 is fairly common. Ceramides are generally precursors of more complex sphingolipids. In the illustrated generalised structure, R(1) = OH, OX (where X = acyl, glycosyl, phosphate, phosphonate, etc.), or H. IMR:0100177 Cer N-acylated sphingoid ceramide CHEBI:17833 Gentamicin is a parenterally administered, broad spectrum aminoglycoside antibiotic typically used for moderate to severe gram negative infections. Despite its wide use, gentamicin has not been definitively linked to instances of clinically apparent liver injury. CAS:1403-66-3 DrugBank:DB00798 MeSH:D005839 Open TG-Gates compound_id=00147 https://livertox.nlm.nih.gov//Gentamicin.htm https://pubchem.ncbi.nlm.nih.gov/compound/3467 gentamicin CHEBI:17855 Any glyceride resulting from the condensation of all three hydroxy groups of glycerol (propane-1,2,3-triol) with fatty acids. C6H5O6R3 [*]C(=O)OCC(COC([*])=O)OC([*])=O PMID:2474544 Triacylglycerol triglyceride CHEBI:17907 An epoxide that is oxirane in which one of the hydrogens has been replaced by a phenyl group. C8H8O C1OC1c1ccccc1 CAS:96-09-3 Wikipedia:Styrene_oxide 2-phenyloxirane styrene-7,8-oxide styrene oxide CHEBI:17931 C15H13NO2 CC(=O)N(O)c1ccc-2c(Cc3ccccc-23)c1 CAS:53-95-2 N-(9H-fluoren-2-yl)-N-hydroxyacetamide N-OH-AAF N-hydroxy-2-acetylaminofluorene N-hydroxy-2-acetamidofluorene CHEBI:17984 A thioester that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of any carboxylic acid. C22H35N7O17P3SR CAS:9029-97-4 PMID:11264983 PMID:11524729 Acyl coenzyme A Acyl-CoA CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC([*])=O acyl-CoA CHEBI:18059 'Lipids' is a loosely defined term for substances of biological origin that are soluble in nonpolar solvents. They consist of saponifiable lipids, such as glycerides (fats and oils) and phospholipids, as well as nonsaponifiable lipids, principally steroids. Organic molecule that is insoluble in water but tends to dissolve in nonpolar organic solvent. Organic molecule that is insoluble in water but tends to dissolve in nonpolar organic solvent. lipid Organic molecule that is insoluble in water but tends to dissolve in nonpolar organic solvent. ISBN:0815340729 CHEBI:18154 A biomacromolecule consisting of large numbers of monosaccharide residues linked glycosidically. This term is commonly used only for those containing more than ten monosaccharide residues. Polysaccharide polysaccharides polysaccharide CHEBI:18179 Any phosphatidylinositol that is phosphorylated at one or more of the hydroxy groups of inositol. phosphoinositide CHEBI:18248 An iron group element atom that has atomic number 26. Fe [Fe] CAS:7439-89-6 DrugBank:DB01592 iron iron atom CHEBI:18295 A member of the class of imidazoles that is 1H-imidazole substituted at position C-4 by a 2-aminoethyl group. histamine CHEBI:18303 A class of aminophospholipids in which a phosphatidyl group is esterified to the hydroxy group of serine. DrugBank:DB00144 Ptd-L-Ser phosphatidylserine phosphatidyl-L-serine CHEBI:18320 The threo-diastereomer of 1,4-dimercaptobutane-2,3-diol. CAS:3483-12-3 DrugBank:DB04447 LINCS:LSM-36870 1,4-dithiothreitol CHEBI:18348 IMR:0200477 IMR:0001350 PI(4,5)P2 PIP2 Phosphatidylinositol-4,5-bisphosphate PtsIns-4,5-P2 PI(4,5)P2 is cleaved by phospholipase C-beta or gamma to generate IP3 and diacylglycerol. PI(4,5)P2 is cleaved by phospholipase C-beta or gamma to generate IP3 and diacylglycerol. 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate PI(4,5)P2 is cleaved by phospholipase C-beta or gamma to generate IP3 and diacylglycerol. ISBN:0815340729 CHEBI:18388 A trihydroxyflavone that is flavone substituted by hydroxy groups at positions 4', 5 and 7. It induces autophagy in leukaemia cells. C15H10O5 InChI=1S/C15H10O5/c16-9-3-1-8(2-4-9)13-7-12(19)15-11(18)5-10(17)6-14(15)20-13/h1-7,16-18H KZNIFHPLKGYRTM-UHFFFAOYSA-N HMDB:HMDB0002124 Wikipedia:Apigenin 5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one 5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one; 5,7,4'-Trihydroxyflavone spigenin apigenin CHEBI:18421 O2 [O][O-] dioxidanidyl superoxide CHEBI:20854 A mitochondrial respiratory-chain inhibitor that interferes with the action of ATP synthase. ATP synthase inhibitor CHEBI:22271 Any of a group of related and highly toxic secondary metabolites (mycotoxins) whose main structural feature is a fused coumarin-bis(dihydrofuran) ring system and which are produced by strains of the moulds Aspergillus flavus or A. parasiticus, together with further metabolites of these mycotoxins. aflatoxin CHEBI:22314 alkali metal atom CHEBI:22333 Highly reactive chemical that introduces alkyl radicals into biologically active molecules and thereby prevents their proper functioning. It could be used as an antineoplastic agent, but it might be very toxic, with carcinogenic, mutagenic, teratogenic, and immunosuppressant actions. It could also be used as a component of poison gases. alkylating agent CHEBI:22563 A monoatomic or polyatomic species having one or more elementary charges of the electron. anion CHEBI:22586 A role that opposes oxidation or inhibits reactions brought about by dioxygen or peroxides. A substance that opposes oxidation or inhibits reactions brought about by dioxygen or peroxides. antioxidants antioxydant antoxidant antioxidant CHEBI:22587 A substance that destroys or inhibits replication of viruses. anti-viral agent anti-viral agents antiviral antiviral agents antivirals antiviral agent CHEBI:22689 The most used of the bafilomycins, a family of toxic macrolide antibiotics derived from Streptomyces griseus. C35H58O9 InChI=1S/C35H58O9/c1-19(2)32-24(7)27(36)18-35(40,44-32)26(9)31(38)25(8)33-28(41-10)14-12-13-20(3)15-22(5)30(37)23(6)16-21(4)17-29(42-11)34(39)43-33/h12-14,16-17,19,22-28,30-33,36-38,40H,15,18H2,1-11H3/b14-12+,20-13+,21-16+,29-17-/t22-,23+,24-,25-,26-,27+,28-,30-,31+,32+,33+,35+/m0/s1 XDHNQDDQEHDUTM-JQWOJBOSSA-N CO[C@H]1\C=C\C=C(C)\C[C@H](C)[C@H](O)[C@H](C)\C=C(C)\C=C(OC)\C(=O)O[C@@H]1[C@@H](C)[C@@H](O)[C@H](C)[C@@]1(O)C[C@@H](O)[C@H](C)[C@H](O1)C(C)C CAS:88899-55-2 bafilomycin A1 CHEBI:22693 Members of the class of pyrimidones consisting of pyrimidine-2,4,6(1H,3H,5H)-trione (barbituric acid) and its derivatives. Largest group of the synthetic sedative/hypnotics, sharing a characteristic six-membered ring structure. barbiturates CHEBI:22695 A molecular entity having an available pair of electrons capable of forming a covalent bond with a hydron (Bronsted base) or with the vacant orbital of some other molecular entity (Lewis base). base CHEBI:22907 A glycopeptide produced by the bacterium Streptomyces verticillus. The term, 'bleomycin' refers to a family of structurally related compounds. When used as an anti-cancer agent, the chemotherapeutical forms are primarily bleomycin A2 and B2. DrugBank:DB00290 Wikipedia:Bleomycin bleomycin CHEBI:22984 CAS:7440-70-2 DrugBank:DB01373 calcium Ca calcium atom CHEBI:23018 An EC 4.2.1.* (hydro-lyases) inhibitor that interferes with the action of carbonic anhydrase (EC 4.2.1.1). Such compounds reduce the secretion of H(+) ions by the proximal kidney tubule. EC 4.2.1.1 (carbonic anhydrase) inhibitors EC 4.2.1.1 inhibitor EC 4.2.1.1 inhibitors anhydrase inhibitor anhydrase inhibitors carbonate anhydrase inhibitor carbonate anhydrase inhibitors carbonate dehydratase inhibitor carbonate dehydratase inhibitors carbonate hydro-lyase (carbon-dioxide-forming) inhibitor carbonate hydro-lyase (carbon-dioxide-forming) inhibitors carbonate hydro-lyase inhibitor carbonate hydro-lyase inhibitors carbonic acid anhydrase inhibitor carbonic acid anhydrase inhibitors carbonic anhydrase (EC 4.2.1.1) inhibitor carbonic anhydrase (EC 4.2.1.1) inhibitors carbonic anhydrase A inhibitor carbonic anhydrase A inhibitors carbonic anhydrase inhibitor carbonic anhydrase inhibitors carboxyanhydrase inhibitor carboxyanhydrase inhibitors EC 4.2.1.1 (carbonic anhydrase) inhibitor CHEBI:23092 A substance intended to sterilize any organism. chemosterilants chemosterilant CHEBI:23354 A low-molecular-weight, non-protein organic compound participating in enzymatic reactions as dissociable acceptor or donor of chemical groups or electrons. coenzyme CHEBI:23357 An organic molecule or ion (usually a metal ion) that is required by an enzyme for its activity. It may be attached either loosely (coenzyme) or tightly (prosthetic group). Wikipedia:Cofactor_(biochemistry) cofactor CHEBI:23367 Any constitutionally or isotopically distinct atom, molecule, ion, ion pair, radical, radical ion, complex, conformer etc., identifiable as a separately distinguishable entity. molecular entity CHEBI:233869 C12H11N3 C1=CC=C(C=C1)N=NC2=CC=C(C=C2)N CAS:60-09-3 Wikipedia:Aniline_Yellow 4-Aminoazobenzene 4-[(E)-phenyldiazenyl]aniline 4-phenyldiazenylaniline AAB 4-(phenylazo)aniline CHEBI:2376 A tetrasaccharide derivative consisting of a dideoxy-4-{[4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl C7 cyclitol moiety [called valienol (or valienamine)] linked via nitrogen to isomaltotriose. CAS:56180-94-0 DrugBank:DB00284 Drug_Central:39 LINCS:LSM-4345 PMID:11937512 PMID:18248270 PMID:25044702 PMID:8893066 PMID:9805641 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-D-glucopyranose Acarbose Glucobay Precose acarbosa acarbose acarbosum acarbose CAS:56180-94-0 ChemIDplus Drug_Central:39 DrugCentral PMID:11937512 Europe PMC PMID:18248270 Europe PMC PMID:25044702 Europe PMC PMID:8893066 Europe PMC PMID:9805641 Europe PMC CHEBI:23899 Any member of the group of signalling molecules arising from oxidation of the three C20 essential fatty acids (EFAs) icosapentaenoic acid (EPA), arachidonic acid (AA) and dihomo-gamma-linolenic acid (DGLA). IMR:0001381 eicosanoid icosanoid CHEBI:23924 A compound or agent that combines with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction. enzyme inhibitor enzyme inhibitors inhibidor enzimatico inhibidores enzimaticos inhibiteur enzymatique inhibiteurs enzymatiques enzyme inhibitor CHEBI:23965 A 3-hydroxy steroid that is estra-1,3,5(10)-triene substituted by hydroxy groups at positions 3 and 17. InChIKey=VOXZDWNPVJITMN-WKUFJEKOSA-N Wikipedia:Estradiol estradiol CHEBI:23995 A member of the class of N-nitrosoureas that is urea in which one of the nitrogens is substituted by ethyl and nitroso groups. C3H7N3O2 CCN(N=O)C(N)=O CAS:759-73-9 Wikipedia:ENU 1-ethyl-1-nitrosourea N-ethyl-N-nitrosourea CHEBI:240107 Amfenac in which the the hydrogen at the 4 position of the benzoyl group is substituted by bromine. It is used for the management of ocular pain and treatment of postoperative inflammation in patients who have undergone cataract extraction. It was withdrawn from the US market in 1998, following concerns over off-label abuse and hepatic failure. Beilstein:8335547 CAS:91714-94-2 DrugBank:DB00963 Drug_Central:401 LINCS:LSM-5585 [2-amino-3-(4-bromobenzoyl)phenyl]acetic acid 2-amino-3-(4-bromobenzoyl)benzeneacetic acid [2-Amino-3-(4-bromo-benzoyl)-phenyl]-acetic acid bromfenac bromfenaco bromfenacum bromfenac Beilstein:8335547 Beilstein CAS:91714-94-2 ChemIDplus Drug_Central:401 DrugCentral CHEBI:24127 A substance used to destroy fungal pests. fungicides fungicide CHEBI:24360 glycerophosphoglycerols CHEBI:24431 A chemical entity is a physical entity of interest in chemistry including molecular entities, parts thereof, and chemical substances. http://purl.obolibrary.org/obo/IMR_0000947 chemical compound chemical entity CHEBI:24432 A role played by the molecular entity or part thereof within a biological context. biological function biological role CHEBI:24621 Originally referring to an endogenous compound that is formed in specialized organ or group of cells and carried to another organ or group of cells, in the same organism, upon which it has a specific regulatory function, the term is now commonly used to include non-endogenous, semi-synthetic and fully synthetic analogues of such compounds. GO:0005180 endocrine hormones substance with hormone role: http://purl.bioontology.org/ontology/STY/T125 hormone CHEBI:24636 Nuclear particle of charge number +1, spin 1/2 and rest mass of 1.007276470(12) u. proton CHEBI:24783 Compounds having the structure RN=CR2 (R = H, hydrocarbyl). Thus analogues of aldehydes or ketones, having NR doubly bonded to carbon; aldimines have the structure RCH=NR, ketimines have the structure R'2C=NR (where R' is not H). Imines include azomethines and Schiff bases. Imine is used as a suffix in systematic nomenclature to denote the C=NH group excluding the carbon atom. CHEBI:24783 http://jglobal.jst.go.jp/en/detail?JGLOBAL_ID=200906016906308703 http://purl.jp/bio/4/id/200906016906308703 imine CHEBI:24839 inorganic salt CHEBI:24848 inositol CHEBI:24852 Strictly, a substance intended to kill members of the class Insecta. In common usage, any substance used for preventing, destroying, repelling or controlling insects. insecticides insecticide CHEBI:24870 A molecular entity having a net electric charge. ion CHEBI:2504 An aflatoxin having a tetrahydrocyclopenta[c]furo[3',2':4,5]furo[2,3-h]chromene skeleton with oxygen functionality at positions 1, 4 and 11. C17H12O6 [H][C@]12OC=C[C@@]1([H])c1c(O2)cc(OC)c2c3CCC(=O)c3c(=O)oc12 CAS:1162-65-8 (6aR,9aS)-4-methoxy-2,3,6a,9a-tetrahydrocyclopenta[c]furo[3',2':4,5]furo[2,3-h]chromene-1,11-dione aflatoxin B1 CHEBI:25212 Any intermediate or product resulting from metabolism. The term 'metabolite' subsumes the classes commonly known as primary and secondary metabolites. metabolite metabolites primary metabolites secondary metabolites metabolite CHEBI:25355 A role played by the entity that inhibits the mitochondrial respiratory-chain. mitochondrial electron transport chain inhibitors mitochondrial respiratory-chain inhibitor CHEBI:25367 Any polyatomic entity that is an electrically neutral entity consisting of more than one atom. molecule CHEBI:25435 An agent that increases the frequency of mutations above the normal background level, usually by interacting directly with DNA and causing it damage, including base substitution. Wikipedia:Mutagen mutagene mutagenes mutagenic agent mutageno mutagenos mutagens mutagen CHEBI:25442 Poisonous substance produced by fungi. mycotoxin CHEBI:254496 A tetraphene having methyl substituents at the 7- and 12-positions. It is a potent carcinogen and is present in tobacco smoke. C20H16 Cc1c2ccccc2c(C)c2c1ccc1ccccc21 CAS:57-97-6 7,12-dimethylbenz(a)anthracene 7,12-dimethylbenzo[a]anthracene 7,12-dimethyltetraphene CHEBI:25491 A substance used to destroy pests of the phylum Nematoda (roundworms). nematicides nematocide nematocides nematicide CHEBI:25512 An endogenous compound that is used to transmit information across the synapse between a neuron and another cell. IMR:0000967 (obsolete) neurotransmitter CHEBI:25555 N nitrogen atom CHEBI:25675 Any of the 26-membered ring macrolides produced by Streptomyces species that can be toxic to other organisms through their ability to inhibit mitochondrial membrane-bound ATP synthases. PMID:32697943 oligomycin PMID:32697943 We used 2-DG to inhibit glucose flux and oligomycin to inhibit ATP synthase (Fig- ure 2A). In contrast, oligomycin treatment led to an increase in the viral load, ACE2 and IL- 1b expression, and TNF-a, IL-6, a, b, and l IFN expression in monocytes (Figures 2E–2G and S3B). CHEBI:25710 An organophosphorus compound is formally a compound containing at least one carbon-phosphorus bond, but the term is often extended to include esters and thioesters. organophosphorus compound CHEBI:25805 Inchikey:QVGXLLKOCUKJST-UHFFFAOYSA-N oxygen oxygen atom CHEBI:25806 oxygen molecular entity CHEBI:25935 HO2 [H]O[O] (HO2)(.) hydroperoxyl CHEBI:25944 Strictly, a substance intended to kill pests. In common usage, any substance used for controlling, preventing, or destroying animal, microbiological or plant pests. pesticide Pestizid Pestizide pesticides pesticide CHEBI:2618 0 C10H17N InChI=1S/C10H17N/c11-10-4-7-1-8(5-10)3-9(2-7)6-10/h7-9H,1-6,11H2 DKNWSYNQZKUICI-UHFFFAOYSA-N 151.2487 151.1361 NC12CC3CC(CC(C3)C1)C2 CAS:768-94-5 PMID:32361028 amantadine PMID:32361028 One of the top significant results shown to downregulate the expression of the CTSL gene is amantadine (10uM). Amantadine in addition to downregulating CTSL appears to further disrupt lysosomal pathway, CHEBI:26216 CAS:7440-09-7 DrugBank:DB01345 potassium potassium atom CHEBI:26347 The family of natural prostaglandins and prostaglandin-like compounds. prostanoid CHEBI:26519 A molecular entity possessing an unpaired electron. free radical radical CHEBI:26523 Molecules or ions formed by the incomplete one-electron reduction of oxygen. They contribute to the microbicidal activity of phagocytes, regulation of signal transduction and gene expression, and the oxidative damage to biopolymers. Wikipedia:Reactive_oxygen_species reactive oxygen species CHEBI:26607 Any fatty acid containing no carbon to carbon multiple bonds. Known to produce adverse biological effects when ingested to excess. saturated fatty acid CHEBI:2663 A member of the class of 1-benzofurans that is 1-benzofuran substituted by a butyl group at position 2 and a 4-[2-(diethylamino)ethoxy]-3,5-diiodobenzoyl group at position 3. It is a cardiovascular drug used for the treatment of cardiac dysrhythmias. C25H29I2NO3 CCCCc1oc2ccccc2c1C(=O)c1cc(I)c(OCCN(CC)CC)c(I)c1 Beilstein:1271711 CAS:1951-25-3 ChemicalBook:CB5310616 DrugBank:DB01118 Drug_Central:176 LINCS:LSM-2379 Open TG-Gates compound_id=00033 PMID:10188629 PMID:16479044 PMID:18368867 (2-butyl-1-benzofuran-3-yl){4-[2-(diethylamino)ethoxy]-3,5-diiodophenyl}methanone Amiodarone 2-Butyl-3-(3,5-diiodo-4-(2-diethylaminoethoxy)benzoyl)benzofuran 2-Butyl-3-benzofuranyl 4-(2-(diethylamino)ethoxy)-3,5-diiodophenyl ketone 2-n-Butyl-3',5'-diiodo-4'-N-diethylaminoethoxy-3-benzoylbenzofuran amiodarona amiodaronum amiodarone Beilstein:1271711 Beilstein CAS:1951-25-3 ChemIDplus ChemicalBook:CB5310616 https://www.chemicalbook.com/ChemicalProductProperty_EN_CB5310616 Drug_Central:176 DrugCentral PMID:10188629 Europe PMC PMID:16479044 Europe PMC PMID:18368867 Europe PMC CHEBI:2666 An organic tricyclic compound that is 10,11-dihydro-5H-dibenzo[a,d][7]annulene substituted by a 3-(dimethylamino)propylidene group at position 5. C20H23N CN(C)CCC=C1c2ccccc2CCc2ccccc12 CAS:50-48-6 DrugBank:DB00321 LINCS:LSM-3190 MeSH:D000639 Patent:WO2011089289 Wikipedia:Amitriptyline 3-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-ylidene)-N,N-dimethylpropan-1-amine amitriptyline CHEBI:26708 sodium atom CHEBI:26739 Sphingolipids are a complex family of compounds that share a common structural feature, a sphingoid base backbone. sphingolipid CHEBI:26806 A dicarboxylic acid anion obtained by deprotonation of at least one of the carboxy groups of succinic acid. PMID:32697943 succinate anion succinic acid anion succinate PMID:32697943 It is known that succinate accumulation drives HIF-1a stabilization (Tannahill et al., 2013). We used cell-permeable diethyl succinate and observed that succinate boosted CoV-2 viral load (Fig- ure S4F). CHEBI:26833 CAS:7704-34-9 sulfur sulfur atom CHEBI:26995 A class of oxygenated oxane derivatives, originally derived from prostaglandin precursors in platelets, that stimulate aggregation of platelets and constriction of blood vessels. IMR:0100020 TX thromboxane CHEBI:27026 Poisonous substance produced by a biological organism such as a microbe, animal or plant. Wikipedia:Toxin toxin CHEBI:27136 A chemical compound containing three hydroxy groups. triol CHEBI:27226 An oxopurine that is the final oxidation product of purine metabolism. uric acid CHEBI:27385 A chlorocarbon that is methane in which all the hydrogens have been replaced by chloro groups. CCl4 ClC(Cl)(Cl)Cl CAS:56-23-5 LINCS:LSM-37019 Wikipedia:Carbon_Tetrachloride CCl4 Carbon tetrachloride tetrachloromethane CHEBI:27594 CAS:7440-44-0 Inchikey:OKTJSMMVPCPJKN-UHFFFAOYSA-N carbon carbon atom CHEBI:27690 Beilstein:212994 CAS:59-66-5 DrugBank:DB00819 Drug_Central:56 Gmelin:365421 LINCS:LSM-5543 Acetazolamide N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)acetamide 2-acetylamino-1,3,4-thiadiazole-5-sulfonamide 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE 5-acetylamino-1,3,4-thiadiazole-2-sulfonamide Defiltran Diacarb Diamox Diluran Glaupax N-[5-(aminosulfonyl)-1,3,4-thiadiazol-2-yl]acetamide N-[5-(aminosulfonyl)-1,3,5-thiadiazol-2-yl]acetamide acetazolamida acetazolamide acetazolamidum acetazolamide Beilstein:212994 Beilstein CAS:59-66-5 ChemIDplus CAS:59-66-5 NIST Chemistry WebBook Drug_Central:56 DrugCentral Gmelin:365421 Gmelin CHEBI:27779 An oxaspiro compound produced by Penicillium griseofulvum. It is used by mouth as an antifungal drug for infections involving the scalp, hair, nails and skin that do not respond to topical treatment. Beilstein:95226 CAS:126-07-8 DrugBank:DB00400 Drug_Central:1331 LINCS:LSM-5259 LIPID_MAPS_instance:LMPK13060001 PMID:14407521 PMID:15078340 PMID:16922553 PMID:23111828 PMID:25476923 PMID:3277037 Reaxys:95226 (2S,6'R)-7-chloro-2',4,6-trimethoxy-6'-methyl-3H,4'H-spiro[1-benzofuran-2,1'-cyclohex[2]ene]-3,4'-dione Griseofulvin (+)-griseofulvin Curling factor Fulcin Fulvicin Grifulvin Grisactin Grisovin Grysio Lamoryl Likuden Poncyl Spirofulvin Sporostatin amudane griseofulvin griseofulvina griseofulvine griseofulvinum griseofulvin Beilstein:95226 Beilstein CAS:126-07-8 ChemIDplus CAS:126-07-8 NIST Chemistry WebBook Drug_Central:1331 DrugCentral LIPID_MAPS_instance:LMPK13060001 LIPID MAPS PMID:14407521 Europe PMC PMID:15078340 Europe PMC PMID:16922553 Europe PMC PMID:23111828 Europe PMC PMID:25476923 Europe PMC PMID:3277037 Europe PMC Reaxys:95226 Reaxys CHEBI:27902 A broad-spectrum polyketide antibiotic produced by the Streptomyces genus of actinobacteria. C22H24N2O8 [H][C@@]12C[C@@]3([H])C(C(=O)c4c(O)cccc4[C@@]3(C)O)=C(O)[C@]1(O)C(=O)C(C(N)=O)=C(O)[C@H]2N(C)C CAS:60-54-8 DrugBank:DB00759 Wikipedia:Tetracycline (4S,4aS,5aS,6S,12aS)-4-(dimethylamino)-3,6,10,12,12a-pentahydroxy-6-methyl-1,11-dioxo-1,4,4a,5,5a,6,11,12a-octahydrotetracene-2-carboxamide tetracycline CHEBI:28077 A member of the class of rifamycins that is a a semisynthetic antibiotic derived from Amycolatopsis rifamycinica (previously known as Amycolatopsis mediterranei and Streptomyces mediterranei) CO[C@H]1\C=C\O[C@@]2(C)Oc3c(C)c(O)c4c(O)c(NC(=O)\C(C)=C/C=C/[C@H](C)[C@H](O)[C@@H](C)[C@@H](O)[C@@H](C)[C@H](OC(C)=O)[C@@H]1C)c(\C=N\N1CCN(C)CC1)c(O)c4c3C2=O CASRN:13292-46-1 DrugBank:DB01045 Wikipedia:Rifampicin rifampicin CHEBI:28087 A polydisperse, highly branched glucan composed of chains of D-glucopyranose residues in alpha(1->4) glycosidic linkage, joined together by alpha(1->6) glycosidic linkages. A small number of alpha(1->3) glycosidic linkages and some cumulative alpha(1->6) links also may occur. The branches in glycogen typically contain 8 to 12 glucose residues. CAS:9005-79-2 glycogen CHEBI:28201 A member of the class of rotenones that consists of 1,2,12,12a-tetrahydrochromeno[3,4-b]furo[2,3-h]chromen-6(6aH)-one substituted at position 2 by a prop-1-en-2-yl group and at positions 8 and 9 by methoxy groups (the 2R,6aS,12aS-isomer). A non-systemic insecticide, it is the principal insecticidal constituent of derris (the dried rhizome and root of Derris elliptica). C23H22O6 [H][C@@]1(Cc2c(O1)ccc1C(=O)[C@@]3([H])c4cc(OC)c(OC)cc4OC[C@@]3([H])Oc21)C(C)=C CAS:83-79-4 PMID:32697943 rotenone PMID:32697943 CoV-2-infected monocytes treated with rotenone have reduced viral replication (Figure 3O). CHEBI:28241 A benzylisoquinoline alkaloid that is isoquinoline substituted by methoxy groups at positions 6 and 7 and a 3,4-dimethoxybenzyl group at position 1. It has been isolated from Papaver somniferum. CAS:58-74-2 DrugBank:DB01113 Drug_Central:2056 LINCS:LSM-2338 PMID:11971205 PMID:24414229 Reaxys:312930 1-(3,4-dimethoxybenzyl)-6,7-dimethoxyisoquinoline papaverine CAS:58-74-2 ChemIDplus CAS:58-74-2 NIST Chemistry WebBook Drug_Central:2056 DrugCentral PMID:11971205 Europe PMC PMID:24414229 Europe PMC Reaxys:312930 Reaxys CHEBI:28304 A highly sulfated linear glycosaminoglycan comprising complex patterns of uronic acid-(1->4)-D-glucosamine repeating subunits. Used as an injectable anticoagulant, it has the highest negative charge density of any known biological molecule. (C26H40N2O36S5)n CAS:9005-49-6 PMID:33332362 enoxaparin heparin PMID:33332362 All hospitalized patients received pharmacological antithrombotic prophylaxis or therapy in contrast to none of the outpatients. As antithrombotic drug, UFH was administered in all but 2 patients (6%) who received LMWH. 2 (6%) patients were switched from UFH to argatroban when a heparin-induced thrombocytopenia was suspected CHEBI:28494 A phosphatidylglycerol composed of two molecules of phosphatidic acid covalently linked to a molecule of glycerol. Wikipedia:cardiolipin cardiolipin CHEBI:28499 A tetrahydroxyflavone in which the four hydroxy groups are located at positions 3, 5, 7 and 4'. Acting as an antioxidant by reducing oxidative stress, it is currently under consideration as a possible cancer treatment. C15H10O6 InChI=1S/C15H10O6/c16-8-3-1-7(2-4-8)15-14(20)13(19)12-10(18)5-9(17)6-11(12)21-15/h1-6,16-18,20H IYRMWMYZSQPJKC-UHFFFAOYSA-N DrugBank:DB01852 KNApSAcK:C00004565 Wikipedia:kaempferol 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one kaempferol CHEBI:28509 A monohaloethene that is ethene in which one of the hydrogens has been replaced by a chloro group. C2H3Cl ClC=C CAS:75-01-4 Wikipedia:Chloroethene Vinyl chloride クロロエチレン 塩化ビニル chloroethene CHEBI:28619 CHEBI:28680 A pyrimidine nucleoside in which cytosine is attached to D-arabinofuranose via a beta-N(1)-glycosidic bond. Used mainly in the treatment of leukaemia, especially acute non-lymphoblastic leukaemia, cytarabine is an antimetabolite antineoplastic agent that inhibits the synthesis of DNA. It also has antiviral and immunosuppressant properties. Beilstein:89175 CAS:147-94-4 DrugBank:DB00987 Drug_Central:770 LINCS:LSM-5470 PMID:15492802 Reaxys:89175 4-amino-1-beta-D-arabinofuranosylpyrimidin-2(1H)-one Cytarabine 1-beta-D-Arabinofuranosylcytosine 4-Amino-1-beta-D-arabinofuranosyl-2(1H)-pyrimidinone Arabinoside C Cytosine arabinoside Cytosine-1-beta-D-arabinofuranoside ara-C arabinocytosine citarabina cytarabine cytarabinum cytosine-beta-D-arabinofuranoside cytarabine Beilstein:89175 Beilstein CAS:147-94-4 ChemIDplus Drug_Central:770 DrugCentral PMID:15492802 Europe PMC Reaxys:89175 Reaxys CHEBI:28757 A ketohexose that is an isomer of glucose. fructose CHEBI:28765 Any member of the phosphoinositide family of compounds, of which seven occur naturally. phosphatidylinositol phosphate CHEBI:28794 A chromenone having the keto group located at the 2-position. C=1C=CC=C2C1C=CC(=O)O2 DrugBank:DB04665 PMID:28166217 Wikipedia:Coumarin coumarin CHEBI:28815 A linear polysaccharide in which the backbone consists of a variably sulfated repeating disaccharide unit. heparan sulfate CHEBI:28834 A bile acid that is 5β-cholan-24-oic acid substituted by hydroxy groups at positions 3 and 12 respectively. InChIKey:KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid CHEBI:28874 Any glycerophosphoinositol having one phosphatidyl group esterified to one of the hydroxy groups of inositol. IMR:0001651 PI phosphatidylinositol CHEBI:28877 C14H8O3 Oc1cccc2C(=O)c3ccccc3C(=O)c12 CAS:129-43-1 1-hydroxyanthracene-9,10-dione 1-hydroxyanthraquinone CHEBI:28901 A methanesulfonate ester that is butane-1,4-diol in which the hydrogens of the hydroxy groups are replaced by methanesulfonyl groups. An alkylating antineoplastic agent, it is used for the treatment of chronic myeloid leukemia (although it has been largely replaced by newer drugs). It is also used as an insect sterilant. Beilstein:1791786 CAS:55-98-1 DrugBank:DB01008 Drug_Central:438 LINCS:LSM-5388 PMID:10523796 PMID:19361744 PMID:19611402 Reaxys:1791786 Busulfan butane-1,4-diyl dimethanesulfonate 1,4-Bis(methanesulfonoxy)butane 1,4-Butanediol dimethanesulfonate 1,4-Dimesyloxybutane 1,4-Dimethanesulfonoxybutane Bisulfex Leucosulfan Mablin Mielucin Misulban Mitostan Myeloleukon Myleran Tetramethylene bis(methanesulfonate) busulfan busulfano busulfanum busulfan Beilstein:1791786 Beilstein CAS:55-98-1 ChemIDplus Drug_Central:438 DrugCentral PMID:10523796 Europe PMC PMID:19361744 Europe PMC PMID:19611402 Europe PMC Reaxys:1791786 Reaxys CHEBI:28939 An N-acetyl-L-amino acid that is the N-acetylated derivative of the natural amino acid L-cysteine. C5H9NO3S CC(=O)N[C@@H](CS)C(O)=O CAS:616-91-1 PMID:32697943 N-acetylcysteine N-acetyl-L-cysteine HOIP_0040152 PMID:32697943 Treatment of CoV-2-infected monocytes with antioxidants, such as mitoquinol (MitoQ) or thiol reductant N-acetyl cystein (NAC), was sufficient to inhibit viral replication and CoV-2-induced HIF-1a stabilization and expression of ACE2 and IL-1b (Figures 3K–3N). These antioxidants also prevented the upregulation of TNF-a; IL-6; IFN a, b, and l; and HIF-1a target genes (Figure S4H). CHEBI:29132 A ketoimine that has formula C8H7NO2. CHEBI:29132 http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-76397 N-(4-oxocyclohexa-2,5-dien-1-ylidene)acetamide N-(4-oxocyclohexa-2,5-dien-1-ylidene)acetamide InChI=1S/C8H7NO2/c1-6(10)9-7-2-4-8(11)5-3-7/h2-5H,1H3 NAPQI N-acetyl-1,4-benzoquinone imine N-(4-oxocyclohexa-2,5-dien-1-ylidene)acetamide IUPAC NAME CHEBI:29191 HO [O][H] hydroxyl CHEBI:2948 A thiopurine that is 6-mercaptopurine in which the mercapto hydrogen is replaced by a 1-methyl-4-nitroimidazol-5-yl group. It is a prodrug for mercaptopurine and is used as an immunosuppressant, prescribed for the treatment of inflammatory conditions and after organ transplantation and also for treatment of Crohn's didease and MS. CAS:446-86-6 DrugBank:DB00993 Drug_Central:269 PMID:11064448 PMID:15199672 PMID:15476481 PMID:15628319 PMID:15973722 PMID:16344342 PMID:16397313 PMID:16764353 PMID:16954801 PMID:17381669 PMID:17970886 PMID:18008354 PMID:18336531 PMID:19243907 PMID:20080917 PMID:25248004 PMID:25314066 PMID:25440430 PMID:25443086 PMID:25581826 PMID:25641386 PMID:28166217 PMID:8738760 PMID:9273463 PMID:9345422 Reaxys:1225351 6-[(1-methyl-4-nitro-1H-imidazol-5-yl)sulfanyl]-7H-purine 6-((1-Methyl-4-nitro-1H-imidazol-5-yl)thio)-1H-purine 6-(1'-Methyl-4'-nitro-5'-imidazolyl)-mercaptopurine Imuran (TN) azathioprine CAS:446-86-6 ChemIDplus Drug_Central:269 DrugCentral PMID:11064448 Europe PMC PMID:15199672 Europe PMC PMID:15476481 Europe PMC PMID:15628319 Europe PMC PMID:15973722 Europe PMC PMID:16344342 Europe PMC PMID:16397313 Europe PMC PMID:16764353 Europe PMC PMID:16954801 Europe PMC PMID:17381669 Europe PMC PMID:17970886 Europe PMC PMID:18008354 Europe PMC PMID:18336531 Europe PMC PMID:19243907 Europe PMC PMID:20080917 Europe PMC PMID:25248004 Europe PMC PMID:25314066 Europe PMC PMID:25440430 Europe PMC PMID:25443086 Europe PMC PMID:25581826 Europe PMC PMID:25641386 Europe PMC PMID:28166217 Europe PMC PMID:8738760 Europe PMC PMID:9273463 Europe PMC PMID:9345422 Europe PMC Reaxys:1225351 Reaxys CHEBI:2955 macrolide antibiotic useful for the treatment of bacterial infections. C38H72N2O12 CC[C@H]1OC(=O)[C@H](C)[C@@H](O[C@H]2C[C@@](C)(OC)[C@@H](O)[C@H](C)O2)[C@H](C)[C@@H](O[C@@H]2O[C@H](C)C[C@@H]([C@H]2O)N(C)C)[C@](C)(O)C[C@@H](C)CN(C)[C@H](C)[C@@H](O)[C@]1(C)O PMID:32307653 azithromycin PMID:32307653 The most interesting finding of this study was that all patients treated with hydroxychloroquine and azithromycin had negative PCR results in nasopharyngeal samples, i.e., 100% of patients treated with both drugs were virologically cured compared to 57.1% of subjects treated with hydroxychloroquine only, and 12.5% of untreated individuals. Studies suggest beneficial effects of azithromycin in reducing viral load of hospitalized patients, possibly interfering with ligand/CD147 receptor interactions; however, its possible effects on SARS-CoV-2 invasion has not yet been evaluated. CHEBI:29688 CAS:191114-48-4 Drug_Central:2581 TELITHROMYCIN Telithromycin (3aS,4R,7S,9R,10R,11R,13R,15R,15aR)-4-ethyl-11-methoxy-3a,7,9,11,13,15-hexamethyl-2,6,8,14-tetraoxo-1-[4-(4-pyridin-3-yl-1H-imidazol-1-yl)butyl]tetradecahydro-2H-oxacyclotetradecino[4,3-d][1,3]oxazol-10-yl 3,4,6-trideoxy-3-(dimethylamino)-beta-D-xylo-hexopyranoside HMR 3647 HMR-3647 HMR3647 RU 66647 RU-66647 RU66647 telithromycin Drug_Central:2581 DrugCentral CHEBI:29699 A mixture of antiviral nucleoside antibiotics produced by Streptomyces lysosuperificus. It contains at least 10 homologues comprising uracil, N-acetylglucosamine, an 11-carbon aminodialdose called tunicamine, and a fatty acid linked to the amino group of the tunicamine. The homologues vary in the composition of the fatty acid moiety. CAS:11089-65-9 Open TG-Gates compound_id:00A02 Wikipedia:Tunicamycin tunicamycin CHEBI:3023 1-Benzofuran substituted at C-2 and C-3 by an ethyl group and a 3,5-dibromo-4-hydroxybenzoyl group respectively. An inhibitor of CYP2C9, it is used as an anti-gout medication. Beilstein:273668 CAS:3562-84-3 Drug_Central:318 LINCS:LSM-2239 PMID:18636784 PMID:26693855 PMID:26792818 PMID:27391386 PMID:28131653 PMID:28166217 PMID:28202260 PMID:7661033 (3,5-dibromo-4-hydroxyphenyl)(2-ethyl-1-benzofuran-3-yl)methanone Benzbromarone 2-ethyl-3-(3,5-dibrom-4-hydroxybenzoyl)benzofuran 3,5-dibromo-4-hydroxyphenyl-2-ethyl-3-benzofuranyl ketone Uroleap (TN) benzbromarone Beilstein:273668 Beilstein CAS:3562-84-3 ChemIDplus Drug_Central:318 DrugCentral PMID:18636784 Europe PMC PMID:26693855 Europe PMC PMID:26792818 Europe PMC PMID:27391386 Europe PMC PMID:28131653 Europe PMC PMID:28166217 Europe PMC PMID:28202260 Europe PMC PMID:7661033 Europe PMC CHEBI:30725 C17H12O7 [H][C@@]12Oc3cc(OC)c4c5CCC(=O)c5c(=O)oc4c3[C@]1([H])[C@@]1([H])O[C@@]1([H])O2 CAS:42583-46-0 6aS,7aS,8aR,8bR)-4-methoxy-2,3,6a,7a,8a,8b-hexahydrocyclopenta[c]oxireno[4',5']furo[3',2':4,5]furo[2,3-h]chromene-1,10-dione aflatoxin B1 exo-8,9-epoxide CHEBI:30737 CCl3 Cl[C](Cl)Cl trichloromethyl(.) CHEBI:30879 A compound in which a hydroxy group, -OH, is attached to a saturated carbon atom. HOR O[*] alcohol CHEBI:3090 A racemate comprising of equal amounts of (R)-bicalutamide and (S)-bicalutamide. It is an oral non-steroidal antiandrogen used in the treatment of prostate cancer and hirsutism. Beilstein:5364666 CAS:90357-06-5 DrugBank:DB01128 Drug_Central:367 LINCS:LSM-1437 PMID:11915584 PMID:12015321 PMID:12017896 PMID:12421104 PMID:12959312 PMID:15509184 PMID:17313204 PMID:18062751 PMID:19194583 PMID:23527766 PMID:30784326 PMID:31099426 Reaxys:5364666 rac-N-[4-cyano-3-(trifluoromethyl)phenyl]-3-[(4-fluorophenyl)sulfonyl]-2-hydroxy-2-methylpropanamide (+-)-bicalutamide (RS)-4'-cyano-alpha',alpha',alpha',-trifluoro-3-(4-fluorophenylsulphonyl)-2-hydroxy-2-methylpropiono-m-toluidide (RS)-bicalutamide Bicadex Bical Bicalox Bicamide Bicatlon Bicusan Binabic Bypro Calumid Calutide Calutol Casodex Cosudex ICI 176,334 ICI 176334 ICI-176334 Kalumid Ormandyl bicalutamida bicalutamide bicalutamidum racemic bicalutamide bicalutamide Beilstein:5364666 Beilstein CAS:90357-06-5 ChemIDplus CAS:90357-06-5 NIST Chemistry WebBook Drug_Central:367 DrugCentral PMID:11915584 Europe PMC PMID:12015321 Europe PMC PMID:12017896 Europe PMC PMID:12421104 Europe PMC PMID:12959312 Europe PMC PMID:15509184 Europe PMC PMID:17313204 Europe PMC PMID:18062751 Europe PMC PMID:19194583 Europe PMC PMID:23527766 Europe PMC PMID:30784326 Europe PMC PMID:31099426 Europe PMC Reaxys:5364666 Reaxys CHEBI:30956 A monocarboxylic acid that is acetic acid in which all three methyl hydrogens are substituted by chlorine. C2HCl3O2 OC(=O)C(Cl)(Cl)Cl CAS:76-03-9 trichloroacetic acid CHEBI:31183 An aromatic ether in which the ether oxygen links an allyl group to the 4-position of (3-chlorophenyl)acetic acid.A non-steroidal anti-inflammatory drug, it was withdrawn from the UK market in 1979 due to concerns with its association with vasculitis and rash. CAS:22131-79-9 Drug_Central:107 PMID:18796 PMID:19205 PMID:21068 PMID:236805 PMID:237493 PMID:241593 PMID:241595 PMID:241596 PMID:241597 PMID:241598 PMID:241600 PMID:241601 PMID:241602 PMID:241603 PMID:24426 PMID:4279126 PMID:509935 PMID:6103793 PMID:6106453 PMID:6109575 PMID:6120697 PMID:6141199 PMID:7853459 PMID:7905004 Reaxys:2116510 [3-chloro-4-(prop-2-en-1-yloxy)phenyl]acetic acid (4-Allyloxy-3-chlorphenyl)essigsaeure 3-Chloro-4-(2-propenyloxy)benzeneacetic acid [4-(allyloxy)-3-chlorophenyl]acetic acid alclofenac alclofenaco alclofenacum alclofenac CAS:22131-79-9 ChemIDplus Drug_Central:107 DrugCentral PMID:18796 Europe PMC PMID:19205 Europe PMC PMID:21068 Europe PMC PMID:236805 Europe PMC PMID:237493 Europe PMC PMID:241593 Europe PMC PMID:241595 Europe PMC PMID:241596 Europe PMC PMID:241597 Europe PMC PMID:241598 Europe PMC PMID:241600 Europe PMC PMID:241601 Europe PMC PMID:241602 Europe PMC PMID:241603 Europe PMC PMID:24426 Europe PMC PMID:4279126 Europe PMC PMID:509935 Europe PMC PMID:6103793 Europe PMC PMID:6106453 Europe PMC PMID:6109575 Europe PMC PMID:6120697 Europe PMC PMID:6141199 Europe PMC PMID:7853459 Europe PMC PMID:7905004 Europe PMC Reaxys:2116510 Reaxys CHEBI:31206 0 ClH4N InChI=1S/ClH.H3N/h1H;1H3 NLXLAEXVIDQMFP-UHFFFAOYSA-N 53.4912 53.00323 [Cl-].[H][N+]([H])([H])[H] CAS:12125-02-9 PMID:32142651 Ammonium chloride HOIP_00040002 PMID:32142651 In order to determine whether SARS-CoV-2 can use CatB/L for cell entry, we initially employed ammonium chloride, which elevates endosomal pH and thereby blocks CatB/L activity. Ammonium chloride treatment strongly inhibited SARS-2-S- and SARS-S-driven entry into TMPRSS2 293T cells (Figure S3 A), suggesting CatB/L dependence. CHEBI:31257 A monocarboxylic acid that is glycolic acid in which the hydrogen attached to the 2-hydroxy group is replaced by a 1-benzyl-1H-indazol-3-yl group. Although it has anti-inflammatory, antinecrotic, choleretic and antilipidaemic properties and has been used for the treatment of various inflammatory skin disorders, its principal effect is to inhibit the denaturation of proteins. Its lysine salt is used in the management of cataracts. CAS:20187-55-7 Drug_Central:303 PMID:1809299 PMID:2190795 PMID:3176111 PMID:3508133 PMID:3817034 PMID:4099158 PMID:4389308 PMID:5746786 PMID:8483582 PMID:8736488 Reaxys:893958 [(1-benzyl-1H-indazol-3-yl)oxy]acetic acid BRN 0893958 EINECS 243-569-2 Iwazac UNII-G4AG71204O bendazac bendazaco bendazacum bendazolic acid bendazac CAS:20187-55-7 ChemIDplus Drug_Central:303 DrugCentral PMID:1809299 Europe PMC PMID:2190795 Europe PMC PMID:3176111 Europe PMC PMID:3508133 Europe PMC PMID:3817034 Europe PMC PMID:4099158 Europe PMC PMID:4389308 Europe PMC PMID:5746786 Europe PMC PMID:8483582 Europe PMC PMID:8736488 Europe PMC Reaxys:893958 Reaxys CHEBI:31446 CAS:2624-43-3 Drug_Central:753 Cyclofenil cyclofenyl cyclopenil cyclophenil cyclophenyl fertodur ondogyne Cyclofenil Drug_Central:753 DrugCentral CHEBI:31596 A 1,3-thiazolemonocarboxylic acid that is 4-methyl-1,3-thiazole-5-carboxylic acid which is substituted by a 3-cyano-4-(2-methylpropoxy)phenyl group at position 2. It is an orally-active, potent, and selective xanthine oxidase inhibitor used for the treatment of chronic hyperuricaemia in patients with gout. CAS:144060-53-7 DrugBank:DB04854 Drug_Central:1137 LINCS:LSM-3064 PMID:25724536 PMID:30844048 PMID:30919894 PMID:31267805 PMID:31332638 PMID:31335677 PMID:31378626 PMID:31447893 PMID:31449565 PMID:31499267 PMID:31531831 PMID:31560952 2-[3-cyano-4-(2-methylpropoxy)phenyl]-4-methyl-1,3-thiazole-5-carboxylic acid 2-(3-cyano-4-isobutoxyphenyl)-4-methyl-1,3-thiazole-5-carboxylic acid Adenuric Donifoxate Febuday Feburic Goturic Goutex TEI 6720 TEI-6720 TMX 67 TMX-67 Uloric Zurig febuxostat febuxostatum febuxostat CAS:144060-53-7 ChemIDplus Drug_Central:1137 DrugCentral PMID:25724536 Europe PMC PMID:30844048 Europe PMC PMID:30919894 Europe PMC PMID:31267805 Europe PMC PMID:31332638 Europe PMC PMID:31335677 Europe PMC PMID:31378626 Europe PMC PMID:31447893 Europe PMC PMID:31449565 Europe PMC PMID:31499267 Europe PMC PMID:31531831 Europe PMC PMID:31560952 Europe PMC CHEBI:31624 fluorescein (lactone form) A xanthene dye that is highly fluorescent, detectable even when present in minute quantities. Used forensically to detect traces of blood, in analytical chemistry as an indicator in silver nitrate titrations and in microscopy. fluorescein (lactone form) CHEBI:3165 A linear nonapeptide messenger belonging to the kinin group of proteins, with amino acid sequence RPPGFSPFR. Enzymatically produced from kallidin in the blood, it is a powerful vasodilator that causes smooth muscle contraction, and may mediate inflammation. MeSH:D001920 bradykinin CHEBI:31653 A carboxylic ester that is 2,3-dihydroxypropyl anthranilate in which the amino group is substituted by a 7-chloroquinolin-4-yl group. A non-steroidal anti-inflammatory drug, glafenine and its hydrochloride salt were used for the relief of all types of pain, but high incidence of anaphylactic reactions resulted in their withdrawal from the market. Beilstein:497124 CAS:3820-67-5 Drug_Central:1297 LINCS:LSM-4419 PMID:19567678 PMID:2210868 Reaxys:497124 2,3-dihydroxypropyl 2-[(7-chloroquinolin-4-yl)amino]benzoate 2,3-Dihydroxypropyl N-(7-chloro-4-quinolyl) anthranilate 4-((2-Carboxyphenyl)amino)-7-chloroquinoline alpha-monoglyceride 4-(2'-beta,gamma-Dihydroxypropoxycarbonylphenylamino)-7-chloroquinoline Glafenin Glaphenin Glaphenine Glicafan Glifan Glifanan Glycerylaminophenaquine glafenina glafenine glafeninum glafenine Beilstein:497124 Beilstein CAS:3820-67-5 ChemIDplus CAS:3820-67-5 NIST Chemistry WebBook Drug_Central:1297 DrugCentral PMID:19567678 Europe PMC PMID:2210868 Europe PMC Reaxys:497124 Reaxys CHEBI:31781 A dicarboxylic acid amide in which a parent structure of amphetamine is substituted on nitrogen by a (2,6-dimethylphenoxy)acetyl group and on the carbon alpha to nitrogen by a (1S,3S)-1-hydroxy-3-{[(2S)-3-methyl-2-(2-oxotetrahydropyrimidin-1(2H)-yl)butanoyl]amino}-4-phenylbutyl group. An antiretroviral of the protease inhibitor class. It is used against HIV infections as a fixed-dose combination with another protease inhibitor, ritonavir. C37H48N4O5 CC(C)[C@H](N1CCCNC1=O)C(=O)N[C@H](C[C@H](O)[C@H](Cc1ccccc1)NC(=O)COc1c(C)cccc1C)Cc1ccccc1 CAS:192725-17-0 DrugBank:DB01601 LINCS:LSM-6027 MeSH:D061466 PMID:19447225 PMID:19732776 (2S)-N-[(2S,4S,5S)-5-{[(2,6-dimethylphenoxy)acetyl]amino}-4-hydroxy-1,6-diphenylhexan-2-yl]-3-methyl-2-(2-oxotetrahydropyrimidin-1(2H)-yl)butanamide lopinavir PMID:19447225 HIV protease inhibitor lopinavir-induced TNF-alpha and IL-6 expression is coupled to the unfolded protein response and ERK signaling pathways in macrophages. PMID:19732776 HIV protease inhibitors induce endoplasmic reticulum stress and disrupt barrier integrity in intestinal epithelial cells. CHEBI:3179 The simplest member of the class of bromobenzenes, that is benzene in which a single hydrogen has been substituted by a bromine. A liquid at room temperature (m.p. -30degreeC; b.p.760 156degreeC), it is used as a solvent, particularly for large-scale crystallisations, and for the introduction of phenyl groups in organic synthesis. C6H5Br Brc1ccccc1 CAS:108-86-1 MetaCyc:BROMOBENZENE PMID:10996478 PMID:24318069 Reaxys:1236661 Wikipedia:Bromobenzene bromobenzene CHEBI:31941 A platinum coordination entity that is a commonly used chemothrepeutic drug for treatment of colorectal cancer. CAS:61825-94-3 CAS:63121-00-6 DrugBank:DB00526 Gmelin:1046012 Gmelin:28892 LINCS:LSM-6352 PMID:11300320 PMID:14755010 PMID:15477639 PMID:17347561 PMID:18440088 PMID:19138416 PMID:19735649 PMID:27756654 PMID:28186109 PMID:28398406 PMID:28415810 PMID:28499428 PMID:28505615 PMID:28624791 PMID:28642473 PMID:28654098 PMID:28695397 PMID:28762171 PMID:28777427 PMID:28800641 PMID:28811232 PMID:28812173 PMID:28837658 PMID:28876454 PMID:28881354 PMID:28881481 PMID:28884286 PMID:28894576 PMID:28924870 PMID:28938919 Reaxys:15700099 (SP-4-2)[(1R,2R)-cyclohexane-1,2-diamine-kappa(2)N,N'][ethanedioato(2-)-kappa(2)O(1),O(2)]platinum Oxaliplatin (SP-4-2-(1R-trans))-(1,2-cyclohexanediamine-N,N')(ethanedioato(2-)-O,O')platinum Eloxatin oxalato(1,2-diaminocyclohexane)platinum(II) oxaliplatin oxaliplatine oxaliplatino oxaliplatinum oxaliplatin CAS:63121-00-6 ChemIDplus Gmelin:1046012 Gmelin Gmelin:28892 Gmelin PMID:11300320 Europe PMC PMID:14755010 Europe PMC PMID:15477639 Europe PMC PMID:17347561 Europe PMC PMID:18440088 Europe PMC PMID:19138416 Europe PMC PMID:19735649 Europe PMC PMID:27756654 Europe PMC PMID:28186109 Europe PMC PMID:28398406 Europe PMC PMID:28415810 Europe PMC PMID:28499428 Europe PMC PMID:28505615 Europe PMC PMID:28624791 Europe PMC PMID:28642473 Europe PMC PMID:28654098 Europe PMC PMID:28695397 Europe PMC PMID:28762171 Europe PMC PMID:28777427 Europe PMC PMID:28800641 Europe PMC PMID:28811232 Europe PMC PMID:28812173 Europe PMC PMID:28837658 Europe PMC PMID:28876454 Europe PMC PMID:28881354 Europe PMC PMID:28881481 Europe PMC PMID:28884286 Europe PMC PMID:28894576 Europe PMC PMID:28924870 Europe PMC PMID:28938919 Europe PMC Reaxys:15700099 Reaxys CHEBI:3216 A morphinane alkaloid that is 7,8-dihydromorphine 6-O-methyl ether in which positions 6 and 14 are joined by a -CH2CH2- bridge, one of the hydrogens of the N-methyl group is substituted by cyclopropyl, and a hydrogen at position 7 is substituted by a 2-hydroxy-3,3-dimethylbutan-2-yl group. C29H41NO4 [H][C@@]1(C[C@]23CC[C@]1(OC)[C@@H]1Oc4c(O)ccc5C[C@H]2N(CC[C@@]31c45)CC1CC1)[C@](C)(O)C(C)(C)C CAS:52485-79-7 DrugBank:DB00921 Wikipedia:Buprenorphine (5alpha,6beta,14beta,18R)-17-(cyclopropylmethyl)-18-[(2S)-2-hydroxy-3,3-dimethylbutan-2-yl]-6-methoxy-18,19-dihydro-4,5-epoxy-6,14-ethenomorphinan-3-ol buprenorphine CHEBI:32246 CAS:150683-30-0 Drug_Central:4110 Tolvaptan OPC 41061 OPC-41061 jinarc samsca Tolvaptan Drug_Central:4110 DrugCentral CHEBI:32499 A carbocyclic fatty acid that is 5-aminoheptanoic acid in which one of the hydrogens attached to the nitrogen is replaced by a 10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl group. A tricyclic antidepressant, it was never approved in the US and was withdrawn from the French market in 1999 due to concerns over abuse, dependence and severe acne. C22H27NO2 OC(=O)CCCCCCNC1c2ccccc2CCc2ccccc12 Beilstein:2170218 CAS:57574-09-1 DrugBank:DB04836 Drug_Central:161 PMID:2131927 PMID:2141246 PMID:2698268 PMID:7609861 PMID:9347390 Reaxys:2170218 Wikipedia:Amineptine 7-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-ylamino)heptanoic acid Amineptin Survector amineptine amineptino amineptinum amineptine Beilstein:2170218 Beilstein CAS:57574-09-1 ChemIDplus CAS:57574-09-1 NIST Chemistry WebBook Drug_Central:161 DrugCentral PMID:2131927 Europe PMC PMID:2141246 Europe PMC PMID:2698268 Europe PMC PMID:7609861 Europe PMC PMID:9347390 Europe PMC Reaxys:2170218 Reaxys CHEBI:32509 C14H14ClN3O2S Cc1cccc(Nc2cc(Cl)nc(SCC(O)=O)n2)c1C Cc1cccc(Nc2cc(Cl)nc(SCC(O)=O)n2)c1C CAS:50892-23-4 LINCS:LSM-2015 PubChem:17396608 Wikipedia:Pirinixic_Acid ({4-chloro-6-[(2,3-dimethylphenyl)amino]pyrimidin-2-yl}sulfanyl)acetic acid WY14643 pirinixic acid CHEBI:32957 Any monoacylglycerol phosphate obtained by hydrolytic removal of one of the two acyl groups of any phosphatidic acid or derivatives therein. lysophosphatidic acids CHEBI:33184 A fatty acyl-CoA that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of any long-chain (C13 to C22) fatty acid. C22H35N7O17P3SR CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC([*])=O PMID:10224157 PMID:14516204 PMID:16357361 PMID:17652214 LCFA-coenzyme A long-chain fatty acyl-CoA CHEBI:33231 A substance that kills or slows the growth of Mycobacterium tuberculosis and is used in the treatment of tuberculosis. antitubercular antitubercular agents antitubercular drug antitubercular drugs tuberculostatic agent antitubercular agent CHEBI:33250 A chemical entity constituting the smallest component of an element having the chemical properties of the element. atom CHEBI:33280 chemical messenger molecular messenger CHEBI:33281 A substance that kills or slows the growth of microorganisms, including bacteria, viruses, fungi and protozoans. PMID:12964249 PMID:22117953 PMID:22439833 PMID:22849268 PMID:22849276 PMID:22958833 Antibiotika Antibiotikum antibiotic antibiotics antibiotique antimicrobial antimicrobial agents antimicrobials microbicide microbicides antimicrobial agent PMID:12964249 Europe PMC PMID:22117953 Europe PMC PMID:22439833 Europe PMC PMID:22849268 Europe PMC PMID:22849276 Europe PMC PMID:22958833 Europe PMC CHEBI:33282 A substance (or active part thereof) that kills or slows the growth of bacteria. A substance that kills or slows the growth of bacteria. antibacterial agents antibacterials bactericide bactericides antibacterial agent CHEBI:33290 Any material that can be ingested by an organism. food role CHEBI:33521 metal atom CHEBI:33694 A macromolecule formed by a living organism. biomacromolecule CHEBI:33696 nucleic acid A macromolecule made up of nucleotide units and hydrolysable into certain pyrimidine or purine bases (usually adenine, cytosine, guanine, thymine, uracil), D-ribose or 2-deoxy-D-ribose and phosphoric acid. nucleic acid CHEBI:33697 ribonucleic acid High molecular weight, linear polymers, composed of nucleotides containing ribose and linked by phosphodiester bonds; RNA is central to the synthesis of proteins. RNA ribonucleic acid CHEBI:33709 A carboxylic acid containing one or more amino groups. Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. amino acid Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. MeSH:D000596 CHEBI:33838 An N-glycosyl compound that has both a nucleobase, normally adenine, guanine, xanthine, thymine, cytosine or uracil, and either a ribose or deoxyribose as functional parents. nucleoside CHEBI:33839 macromolecule A macromolecule is a molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass. polymer macromolecule CHEBI:3387 A dibenzoazepine that is 5H-dibenzo[b,f]azepine carrying a carbamoyl substituent at the azepine nitrogen, used as an anticonvulsant. Beilstein:1246090 CAS:298-46-4 DrugBank:DB00564 Drug_Central:489 LINCS:LSM-3610 PMID:10411478 PMID:11071486 PMID:11129121 PMID:11240598 PMID:11475584 PMID:11595204 PMID:11888243 PMID:11891095 PMID:12073283 PMID:12228880 PMID:12475188 PMID:12749779 PMID:12799799 PMID:12957643 PMID:14160216 PMID:14572037 PMID:14581052 PMID:14713026 PMID:14723323 PMID:15165631 PMID:15557493 PMID:15665743 PMID:15683742 PMID:15739418 PMID:15820347 PMID:15850602 PMID:16033627 PMID:16150575 PMID:16245817 PMID:16380297 PMID:16394456 PMID:16437428 PMID:16538175 PMID:16562645 PMID:16616830 PMID:16990009 PMID:17027750 PMID:17028629 PMID:17207414 PMID:17582711 PMID:17873967 PMID:17949959 PMID:18163657 PMID:18415623 PMID:18637155 PMID:18652684 PMID:18656520 PMID:18969759 PMID:19135617 PMID:19473818 PMID:19741433 PMID:19921623 PMID:22322005 PMID:27967303 PMID:7602118 Reaxys:1246090 5H-dibenzo[b,f]azepine-5-carboxamide 5-Carbamoyl-5H-dibenz(b,f)azepine 5-Carbamoyl-5H-dibenzo(b,f)azepine 5-Carbamyl-5H-dibenzo(b,f)azepine 5-carbamoyl-5H-dibenz[b,f]azepine 5H-Dibenz(b,f)azepine-5-carboxamide Carbamazepen Carnexiv carbamazepina carbamazepine carbamazepinum carbamazepine Beilstein:1246090 Beilstein CAS:298-46-4 ChemIDplus CAS:298-46-4 NIST Chemistry WebBook Drug_Central:489 DrugCentral PMID:10411478 ChEMBL PMID:11071486 Europe PMC PMID:11129121 Europe PMC PMID:11240598 Europe PMC PMID:11475584 Europe PMC PMID:11595204 Europe PMC PMID:11888243 Europe PMC PMID:11891095 Europe PMC PMID:12073283 Europe PMC PMID:12228880 Europe PMC PMID:12475188 Europe PMC PMID:12749779 Europe PMC PMID:12799799 Europe PMC PMID:12957643 Europe PMC PMID:14160216 Europe PMC PMID:14572037 Europe PMC PMID:14581052 Europe PMC PMID:14713026 Europe PMC PMID:14723323 Europe PMC PMID:15165631 Europe PMC PMID:15557493 Europe PMC PMID:15665743 Europe PMC PMID:15683742 Europe PMC PMID:15739418 Europe PMC PMID:15820347 Europe PMC PMID:15850602 Europe PMC PMID:16033627 Europe PMC PMID:16150575 Europe PMC PMID:16245817 Europe PMC PMID:16380297 Europe PMC PMID:16394456 Europe PMC PMID:16437428 Europe PMC PMID:16538175 Europe PMC PMID:16562645 Europe PMC PMID:16616830 Europe PMC PMID:16990009 Europe PMC PMID:17027750 Europe PMC PMID:17028629 Europe PMC PMID:17207414 Europe PMC PMID:17582711 Europe PMC PMID:17873967 Europe PMC PMID:17949959 Europe PMC PMID:18163657 Europe PMC PMID:18415623 Europe PMC PMID:18637155 Europe PMC PMID:18652684 Europe PMC PMID:18656520 Europe PMC PMID:18969759 Europe PMC PMID:19135617 Europe PMC PMID:19473818 Europe PMC PMID:19741433 Europe PMC PMID:19921623 Europe PMC PMID:22322005 Europe PMC PMID:27967303 Europe PMC PMID:7602118 Europe PMC Reaxys:1246090 Reaxys CHEBI:34559 CAS:1477-19-6 Drug_Central:317 Benzarone 2-Ethyl-3-(4-hydroxybenzoyl)benzofuran benzaron benzarone Drug_Central:317 DrugCentral CHEBI:34873 A nitrosamine that is N-ethylethanamine substituted by a nitroso group at the N-atom. C4H10N2O CCN(CC)N=O CAS:55-18-5 N-ethyl-N-nitrosoethanamine DEN Diethylnitrosamine N-nitrosodiethylamine CHEBI:35221 A substance which is structurally similar to a metabolite but which competes with it or replaces it, and so prevents or reduces its normal utilization. antimetabolite antimetabolites antimetabolite CHEBI:35222 A substance role that diminishes the rate of a chemical reaction. inhibitor inhibidor inhibiteur inhibitors inhibitor CHEBI:35223 A substance that increases the rate of a reaction without modifying the overall standard Gibbs energy change in the reaction. catalyst CHEBI:35337 Any drug that enhances the activity of the central nervous system. central nervous system stimulant CNS stimulant analeptic analeptic agent analeptic drug analeptics central stimulant central nervous system stimulant CHEBI:35341 Any of naturally occurring compounds and synthetic analogues, based on the cyclopenta[a]phenanthrene carbon skeleton, partially or completely hydrogenated; there are usually methyl groups at C-10 and C-13, and often an alkyl group at C-17. By extension, one or more bond scissions, ring expansions and/or ring contractions of the skeleton may have occurred. Natural steroids are derived biogenetically from triterpenoids. SMILES: C12C(C3C(C(CC3)*)(C)CC1)CCC4C2(CCCC4)C steroids steroid CHEBI:35381 Parent monosaccharides are polyhydroxy aldehydes H[CH(OH)]nC(=O)H or polyhydroxy ketones H-[CHOH]n-C(=O)[CHOH]m-H with three or more carbon atoms. The generic term 'monosaccharide' (as opposed to oligosaccharide or polysaccharide) denotes a single unit, without glycosidic connection to other such units. It includes aldoses, dialdoses, aldoketoses, ketoses and diketoses, as well as deoxy sugars, provided that the parent compound has a (potential) carbonyl group. Monosaccharide monosaccharide monosaccharides monosaccharide CHEBI:35441 A substance used in the prophylaxis or therapy of infectious diseases. anti-infective agents anti-infective drugs antiinfective agents antiinfective drug antiinfective agent CHEBI:35442 A substance used to treat or prevent parasitic infections. antiparasitic drugs antiparasitics parasiticides antiparasitic agent CHEBI:35443 Substance intended to kill parasitic worms (helminths). anthelminthic anthelminthics anthelmintic anthelmintics antihelminth antihelmintico vermifuge anthelminthic drug CHEBI:35444 A substance used in the treatment or control of nematode infestations. antinematodal agent antinematodal drugs antinematodals antinematodal drug CHEBI:35469 Antidepressants are mood-stimulating drugs used primarily in the treatment of affective disorders and related conditions. antidepressant drugs antidepressants thymoanaleptics thymoleptic drugs thymoleptics antidepressant CHEBI:35470 A class of drugs producing both physiological and psychological effects through a variety of mechanisms involving the central nervous system. CNS agent CNS drugs central nervous system agents central nervous system drug CHEBI:35471 A loosely defined grouping of drugs that have effects on psychological function. Wikipedia:Psychotropic_drug psychoactive agent psychoactive drugs psychopharmaceuticals psychotropic drugs psychotropic drug CHEBI:35472 A substance that reduces or suppresses inflammation. anti-inflammatory drugs antiinflammatory agent antiinflammatory drug antiinflammatory drugs anti-inflammatory drug CHEBI:35473 A traditional grouping of drugs said to have a soothing or calming effect on mood, thought or behaviour. ataractics tranquilising drug tranquilizing drugs tranquillising agent tranquillizing agents tranquilizing drug CHEBI:35474 Anxiolytic drugs are agents that alleviate anxiety, tension, and anxiety disorders, promote sedation, and have a calming effect without affecting clarity of consciousness or neurologic conditions. anti-anxiety agents anti-anxiety drugs anxiolytic agents anxiolytics minor tranquilisers minor tranquilizers minor tranquilizing agents anxiolytic drug CHEBI:35475 An anti-inflammatory drug that is not a steroid. In addition to anti-inflammatory actions, non-steroidal anti-inflammatory drugs have analgesic, antipyretic, and platelet-inhibitory actions. They act by blocking the synthesis of prostaglandins by inhibiting cyclooxygenase, which converts arachidonic acid to cyclic endoperoxides, precursors of prostaglandins. Wikipedia:Non-steroidal_anti-inflammatory_drug NSAID NSAIDs non-steroidal anti-inflammatory agent non-steroidal anti-inflammatory drugs non-steroidal anti-inflammatory drug CHEBI:35476 Antipsychotic drugs are agents that control agitated psychotic behaviour, alleviate acute psychotic states, reduce psychotic symptoms, and exert a quieting effect. Neuroleptikum antipsychotic agents antipsychotic drug antipsychotic drugs antipsychotics antipsychotiques grosser Tranquilizer major tranquilizers major tranquilizing agents neuroleptic neuroleptic agents neuroleptics neuroleptique neuroleptiques antipsychotic agent CHEBI:35477 Antimanic drugs are agents used to treat bipolar disorders or mania associated with other affective disorders. antimanic agent antimanic drugs antimanics antimanic drug CHEBI:35480 An agent capable of relieving pain without the loss of consciousness or without producing anaesthesia. In addition, analgesic is a role played by a compound which is exhibited by a capability to cause a reduction of pain symptoms. analgesic CHEBI:35481 A drug that has principally analgesic, antipyretic and anti-inflammatory actions. Non-narcotic analgesics do not bind to opioid receptors. non-narcotic analgesic CHEBI:35487 An EC 1.2.1.* (oxidoreductase acting on donor aldehyde/oxo group with NAD(+) or NADP(+) as acceptor) inhibitor that interferes with the action of aldehyde dehydrogenase (NAD(+)), EC 1.2.1.3. CoA-independent aldehyde dehydrogenase inhibitor CoA-independent aldehyde dehydrogenase inhibitors EC 1.2.1.3 (aldehyde dehydrogenase (NAD(+))) inhibitor EC 1.2.1.3 (aldehyde dehydrogenase (NAD(+))) inhibitors EC 1.2.1.3 [aldehyde dehydrogenase (NAD(+))] inhibitors EC 1.2.1.3 inhibitor EC 1.2.1.3 inhibitors NAD-aldehyde dehydrogenase inhibitor NAD-aldehyde dehydrogenase inhibitors NAD-dependent 4-hydroxynonenal dehydrogenase inhibitor NAD-dependent 4-hydroxynonenal dehydrogenase inhibitors NAD-dependent aldehyde dehydrogenase inhibitor NAD-dependent aldehyde dehydrogenase inhibitors NAD-linked aldehyde dehydrogenase inhibitor NAD-linked aldehyde dehydrogenase inhibitors aldehyde dehydrogenase (NAD(+)) (EC 1.2.1.3) inhibitor aldehyde dehydrogenase (NAD(+)) (EC 1.2.1.3) inhibitors aldehyde dehydrogenase (NAD(+)) inhibitor aldehyde dehydrogenase (NAD(+)) inhibitors aldehyde dehydrogenase (NAD) inhibitor aldehyde dehydrogenase (NAD) inhibitors aldehyde dehydrogenase inhibitor aldehyde dehydrogenase inhibitors m-methylbenzaldehyde dehydrogenase inhibitor m-methylbenzaldehyde dehydrogenase inhibitors propionaldehyde dehydrogenase inhibitor propionaldehyde dehydrogenase inhibitors EC 1.2.1.3 [aldehyde dehydrogenase (NAD(+))] inhibitor CHEBI:35488 A loosely defined group of drugs that tend to reduce the activity of the central nervous system. CNS depressants central nervous system depressants central nervous system depressant CHEBI:35493 A drug that prevents or reduces fever by lowering the body temperature from a raised state. An antipyretic will not affect the normal body temperature if one does not have fever. Antipyretics cause the hypothalamus to override an interleukin-induced increase in temperature. The body will then work to lower the temperature and the result is a reduction in fever. anti-pyretic antipyretic CHEBI:35497 A compound which inhibits or antagonises the biosynthesis or actions of androgens. antiandrogen androgen antagonist CHEBI:35498 An agent that promotes the excretion of urine through its effects on kidney function. diuretics diuretic CHEBI:35526 A drug which lowers the blood glucose level. antidiabetic antihyperglycemic antihyperglycemic agent antihyperglycemic agents antihyperglycemic drug antihyperglycemic drugs antihyperglycemics hypoglycemic agents hypoglycemic drug hypoglycemic drugs hypoglycemic agent CHEBI:35530 An agent that binds to but does not activate beta-adrenergic receptors thereby blocking the actions of endogenous or exogenous beta-adrenergic agonists. beta-Adrenergic antagonists are used for treatment of hypertension, cardiac arrhythmias, angina pectoris, glaucoma, migraine headaches and anxiety. beta-adrenergic antagonists beta-adrenergic blocker beta-adrenergic blockers beta-adrenergic receptor blockaders beta-adrenoceptor antagonists beta-blocker beta-blockers beta-adrenergic antagonist CHEBI:35544 A compound or agent that combines with cyclooxygenases (EC 1.14.99.1) and thereby prevents its substrate-enzyme combination with arachidonic acid and the formation of icosanoids, prostaglandins, and thromboxanes. (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate,hydrogen-donor:oxygen oxidoreductase inhibitor (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate,hydrogen-donor:oxygen oxidoreductase inhibitors (PG)H synthase inhibitor (PG)H synthase inhibitors COX inhibitor EC 1.14.99.1 (cyclooxygenase) inhibitor EC 1.14.99.1 (cyclooxygenase) inhibitors EC 1.14.99.1 (prostaglandin-endoperoxide synthase) inhibitors EC 1.14.99.1 inhibitor EC 1.14.99.1 inhibitors PG synthetase inhibitor PG synthetase inhibitors cyclooxygenase (EC 1.14.99.1) inhibitor cyclooxygenase (EC 1.14.99.1) inhibitors cyclooxygenase inhibitor cyclooxygenase inhibitors fatty acid cyclooxygenase inhibitor fatty acid cyclooxygenase inhibitors prostaglandin G/H synthase inhibitor prostaglandin G/H synthase inhibitors prostaglandin endoperoxide synthetase inhibitor prostaglandin endoperoxide synthetase inhibitors prostaglandin synthase inhibitor prostaglandin synthase inhibitors prostaglandin synthetase inhibitor prostaglandin synthetase inhibitors EC 1.14.99.1 (prostaglandin-endoperoxide synthase) inhibitor CHEBI:35553 Perhexiline (Pexsig) is a prophylactic antianginal agent used primarily in Australia and New Zealand. Perhexiline is thought to act by inhibiting mitochondrial carnitine palmitoyltransferase-1. (by Wikipedia) C19H35N C1CCC(CC1)C(CC1CCCCN1)C1CCCCC1 Beilstein:4979856 CAS:6621-47-2 DrugBank:DB01074 Drug_Central:2106 LINCS:LSM-4353 Wikipedia:Perhexiline 2-(2,2-dicyclohexylethyl)piperidine Perhexiline Perhexilene perhexiline Beilstein:4979856 Beilstein CAS:6621-47-2 ChemIDplus CAS:6621-47-2 NIST Chemistry WebBook Drug_Central:2106 DrugCentral CHEBI:35554 A drug that affects the rate or intensity of cardiac contraction, blood vessel diameter or blood volume. cardiovascular agent cardiovascular drugs cardiovascular drug CHEBI:35569 An agent that selectively binds to and activates alpha-adrenergic receptors. alpha-adrenergic agonists alpha-adrenergic receptor agonist alpha-adrenoceptor agonists alpha-adrenergic agonist CHEBI:35572 C9H14O CC(C)=CC(=O)C=C(C)C CAS:504-20-1 2,6-dimethylhepta-2,5-dien-4-one phorone CHEBI:35610 A substance that inhibits or prevents the proliferation of neoplasms. anticancer agent anticancer agents antineoplastic antineoplastic agents cytostatic antineoplastic agent CHEBI:35620 A drug used to cause dilation of the blood vessels. vasodilator vasodilator agents vasodilator agent CHEBI:35623 A drug used to prevent seizures or reduce their severity. Antiepileptika Antiepileptikum Antikonvulsiva Antikonvulsivum anti-convulsant anti-convulsants anti-convulsive agent anti-convulsive agents anticonvulsants anticonvulsive agent anticonvulsive agents antiepileptic antiepileptics antiepileptique antiepileptiques anticonvulsant CHEBI:35634 An EC 1.17.3.* (oxidoreductase acting on CH or CH2 with oxygen as acceptor) inhibitor that interferes with the action of xanthine oxidase (EC 1.17.3.2). EC 1.17.3.2 (xanthine oxidase) inhibitors EC 1.17.3.2 inhibitor EC 1.17.3.2 inhibitors Schardinger enzyme inhibitor Schardinger enzyme inhibitors hypoxanthine oxidase inhibitor hypoxanthine oxidase inhibitors hypoxanthine-xanthine oxidase inhibitor hypoxanthine-xanthine oxidase inhibitors hypoxanthine:oxygen oxidoreductase inhibitor hypoxanthine:oxygen oxidoreductase inhibitors xanthine oxidase (EC 1.17.3.2) inhibitor xanthine oxidase (EC 1.17.3.2) inhibitors xanthine oxidase inhibitor xanthine oxidase inhibitors xanthine oxidoreductase inhibitor xanthine oxidoreductase inhibitors xanthine:O2 oxidoreductase inhibitor xanthine:O2 oxidoreductase inhibitors xanthine:oxygen oxidoreductase inhibitor xanthine:oxygen oxidoreductase inhibitors xanthine:xanthine oxidase inhibitor xanthine:xanthine oxidase inhibitors EC 1.17.3.2 (xanthine oxidase) inhibitor CHEBI:35640 Adrenergic uptake inhibitors are drugs that block the transport of adrenergic transmitters into axon terminals or into storage vesicles within terminals. The tricyclic antidepressants and amphetamines are among the therapeutically important drugs that may act via inhibition of adrenergic transport. Many of these drugs also block transport of serotonin. ARI NERI NRI adrenergic reuptake inhibitor adrenergic reuptake inhibitors adrenergic uptake inhibitors norepinephrine reuptake inhibitor norepinephrine reuptake inhibitors adrenergic uptake inhibitor CHEBI:35660 An inhibitor of HIV protease, an enzyme required for production of proteins needed for viral assembly. Wikipedia:Protease_inhibitor_(pharmacology) HIV protease inhibitors HIV protease inhibitor CHEBI:35674 Any drug used in the treatment of acute or chronic vascular hypertension regardless of pharmacological mechanism. antihypertensive antihypertensive agents antihypertensive drug antihypertensive drugs antihypertensive agent CHEBI:35679 A substance used to treat hyperlipidemia (an excess of lipids in the blood). antihyperlipemic antihyperlipemics antihyperlipidemic antihyperlipidemic agent antihyperlipidemic agents antihyperlipidemic drug antihyperlipidemic drugs antihyperlipidemics antilipemic antilipemic drugs antilipemics hypolipidemic agent hypolipidemic agents antilipemic drug CHEBI:35703 A xenobiotic (Greek, xenos "foreign"; bios "life") is a compound that is foreign to a living organism. Principal xenobiotics include: drugs, carcinogens and various compounds that have been introduced into the environment by artificial means. Wikipedia:Xenobiotic Xenobiotic xenobiotic xenobiotics xenobiotics xenobiotic compounds xenobiotic xenobiotics IUPAC CHEBI:35705 An agent that suppresses immune function by one of several mechanisms of action. Classical cytotoxic immunosuppressants act by inhibiting DNA synthesis. Others may act through activation of T-cells or by inhibiting the activation of helper cells. In addition, an immunosuppressive agent is a role played by a compound which is exhibited by a capability to diminish the extent and/or voracity of an immune response. immunosuppressant immunosuppressive agents inmunosupresor immunosuppressive agent CHEBI:35717 A central nervous system depressant used to induce drowsiness or sleep or to reduce psychological excitement or anxiety. hypnotics hypnotics and sedatives sedative drug sedatives sedatives and hypnotics sedative CHEBI:35718 An antimicrobial agent that destroys fungi by suppressing their ability to grow or reproduce. antifungal antifungal agents antifungal drug antifungal drugs antifungals antifungal agent CHEBI:35741 Any member of the group of lipids containing a common glycerol backbone to which at least one fatty acid-derived group is attached. IMR:0001382 glycerolipid CHEBI:35766 glycerophosphoserine CHEBI:35786 http://purl.obolibrary.org/obo/IMR_0001383 sphingophospholipid phosphosphingolipid CHEBI:35816 A substance that suppresses Mycobacterium leprae, ameliorates the clinical manifestations of leprosy, and/or reduces the incidence and severity of leprous reactions. leprostatic leprostatic agent leprostatic drugs leprostatic drug CHEBI:35820 Any antimicrobial drug which is used to treat or prevent protozoal infections. antiprotozoal agent antiprotozoal agents antiprotozoal drugs antiprotozoal drug CHEBI:35821 A substance used to lower plasma cholesterol levels. anticholesteremic drug CHEBI:35841 A gout suppressant that acts directly on the renal tubule to increase the excretion of uric acid, thus reducing its concentrations in plasma. uricosuric agent uricosuric drugs uricosuric drug CHEBI:35842 A drug used to treat rheumatoid arthritis. anti-rheumatic drugs antirheumatic agent antirheumatic drugs antirheumatic drug CHEBI:35845 A drug that increases uric acid excretion by the kidney (uricosuric drug), decreases uric acid production (antihyperuricemic), or alleviates the pain and inflammation of acute attacks of gout. gout suppressants gout suppressant CHEBI:35846 A drug used for its effect on the kidneys' regulation of body fluid composition and volume. renal agents renal agent CHEBI:35856 A compound or agent that combines with lipoxygenase and thereby prevents its substrate-enzyme combination with arachidonic acid and the formation of the icosanoid products hydroxyicosatetraenoic acid and various leukotrienes. lipooxygenase inhibitor lipoxygenase inhibitors lipoxygenase inhibitor CHEBI:35942 A substance used for its pharmacological action on any aspect of neurotransmitter systems. Neurotransmitter agents include agonists, antagonists, degradation inhibitors, uptake inhibitors, depleters, precursors, and modulators of receptor function. neurotransmitter agents neurotransmitter agent CHEBI:36043 A drug used to treat or prevent microbial infections. antimicrobial drugs antimicrobial drug CHEBI:36044 A substance used in the prophylaxis or therapy of virus diseases. anti-viral drug anti-virus drug antiviral drugs antiviral drug CHEBI:36047 A drug used to treat or prevent bacterial infections. Wikipedia:Antibacterial antibacterial drugs antibacterial drug CHEBI:36080 An amino acid chain that is produced de novo by ribosome-mediated translation of a genetically-encoded mRNA. http://purl.obolibrary.org/obo/PR_000000001 protein CHEBI:3619 A 1,3-thiazine that is 1,3-thiazinan-4-one S,S-dioxide in which a hydrogen at position 2 is substituted by a 4-chlorophenyl group and the hydrogen attached to the nitrogen is substituted by methyl. A non-benzodiazepine muscle relaxant, it was used in the management of anxiety and in the treatment of muscle spasms until being discontinued worldwide by its manufacturer in 1996, due to rare but serious cutaneous reactions. Beilstein:23033 CAS:80-77-3 DrugBank:DB01178 Drug_Central:603 LINCS:LSM-4356 PMID:10191862 PMID:10412893 PMID:10798243 PMID:15897685 PMID:29438107 PMID:3449070 PMID:3720548 PMID:3768082 PMID:6403110 PMID:7104168 PMID:7758315 PMID:9770210 Reaxys:23033 2-(4-chlorophenyl)-3-methyl-1,3-thiazinan-4-one 1,1-dioxide (+-)-chlormezanone 2-(p-chlorophenyl)tetrahydro-3-methyl-4H-1,3-thiazin-4-one 1,1-dioxide 2-(p-chlorphenyl)-3-methyl-1,3-perhydrothiazin-4-on-1,1-dioxide chlormethazanone chlormezanona chlormezanone chlormezanonum chlormezanone Beilstein:23033 Beilstein CAS:80-77-3 ChemIDplus Drug_Central:603 DrugCentral PMID:10191862 Europe PMC PMID:10412893 Europe PMC PMID:10798243 Europe PMC PMID:15897685 Europe PMC PMID:29438107 Europe PMC PMID:3449070 Europe PMC PMID:3720548 Europe PMC PMID:3768082 Europe PMC PMID:6403110 Europe PMC PMID:7104168 Europe PMC PMID:7758315 Europe PMC PMID:9770210 Europe PMC Reaxys:23033 Reaxys CHEBI:36314 glycerophosphoethanolamine CHEBI:36315 Any glycerophospholipid having the polar alcohol inositol esterified to the phosphate group at the sn-3 position of the glycerol backbone. PMID:14706866 glycerophosphoinositols glycerophosphoinositol CHEBI:36335 A drug used to treat or prevent infections caused by protozoal organisms belonging to the suborder Trypanosomatida. antitrypanosomal agent antitrypanosomal agents antitrypanosomal drug antitrypanosomal drugs trypanocidal drugs trypanocide trypanosomicidal agents trypanocidal drug CHEBI:36357 Any molecular entity consisting of more than one atom. polyatomic entity CHEBI:36386 An organochlorine compound comprising acetic acid carrying two chloro substituents at the 2-position. It occurs in nature in seaweed, Asparagopsis taxiformis. C2H2Cl2O2 OC(=O)C(Cl)Cl CAS:79-43-6 Wikipedia:Dichloroacetic_acid dichloroacetic acid CHEBI:36413 A compound which stimulates anabolism and inhibits catabolism. Anabolic agents stimulate the development of muscle mass, strength, and power. anabolic agent CHEBI:3647 A substituted phenothiazine in which the ring nitrogen at position 10 is attached to C-3 of an N,N-dimethylpropanamine moiety. C17H19ClN2S CN(C)CCCN1c2ccccc2Sc2ccc(Cl)cc12 CAS:50-53-3 DrugBank:DB00477 LINCS:LSM-4017 3-(2-chloro-10H-phenothiazin-10-yl)-N,N-dimethylpropan-1-amine chlorpromazine CHEBI:3655 A member of the class of 1,3-benzoxazoles that is 1,3-benzoxazol-2-ol in which the hydrogen atom at position 5 is substituted by chlorine. A centrally acting muscle relaxant with sedative properties, it is used for the symptomatic treatment of painful muscle spasm. Beilstein:638882 CAS:95-25-0 DrugBank:DB00356 Drug_Central:626 LINCS:LSM-6011 PMID:10640318 PMID:11727787 PMID:12437348 PMID:16763012 PMID:16859676 PMID:17621748 PMID:21195386 PMID:23975871 PMID:24210069 PMID:25815637 PMID:6631711 Reaxys:638882 5-chloro-1,3-benzoxazol-2-ol CHLORZOXAZONE Chlorzoxazone 2-hydroxy-5-chlorobenzoxazole 5-chloro-2(3H)-benzoxazolone 5-chloro-2-benzoxazolinone 5-chloro-2-benzoxazolol 5-chloro-2-benzoxazolone 5-chloro-2-hydroxybenzoxazole 5-chlorobenzoxazolidone 5-chlorobenzoxazolin-2-one chlorzoxane chlorzoxazona chlorzoxazone chlorzoxazonum chlorzoxazone Beilstein:638882 Beilstein CAS:95-25-0 ChemIDplus CAS:95-25-0 NIST Chemistry WebBook Drug_Central:626 DrugCentral PMID:10640318 Europe PMC PMID:11727787 Europe PMC PMID:12437348 Europe PMC PMID:16763012 Europe PMC PMID:16859676 Europe PMC PMID:17621748 Europe PMC PMID:21195386 Europe PMC PMID:23975871 Europe PMC PMID:24210069 Europe PMC PMID:25815637 Europe PMC PMID:6631711 Europe PMC Reaxys:638882 Reaxys CHEBI:36710 An agent that promotes the production and release of interferons. interferon inducer CHEBI:36711 phosphoethanolamine CHEBI:367163 An N,N-disubstituted benzenesulfonamide bearing an unsubstituted amino group at the 4-position, used for the treatment of HIV infection. A second-generation HIV protease inhibitor, darunavir was designed to form robust interactions with the protease enzyme from many strains of HIV, including those from treatment-experienced patients with multiple resistance mutations to other protease inhibitors. Beilstein:7960555 CAS:206361-99-1 DrugBank:DB01264 Drug_Central:4143 PMID:15771427 PMID:16480273 PMID:25017682 Reaxys:7960555 (3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-yl [(2S,3R)-4-{[(4-aminophenyl)sulfonyl](2-methylpropyl)amino}-3-hydroxy-1-phenylbutan-2-yl]carbamate Darunavir (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE (3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-yl N-((1S,2R)-1-benzyl-2-hydroxy-3-(N(1)-isobutylsulfanilamido)propyl)carbamate (3R,3aS,6aR)-tetrahydro-2H-furo[2,3-b]furan-3-yl (2S,3R)-4-(4-amino-N-isobutylphenylsulfonamido)-3-hydroxy-1-phenylbutan-2-ylcarbamate (3R,3aS,6aR)-tetrahydro-2H-furo[2,3-b]furan-3-yl (2S,3R)-4-(4-amino-N-neopentylphenylsulfonamido)-3-hydroxy-1-phenylbutan-2-ylcarbamate N-((1S,2R)-3-(((4-aminophenyl)sulfonyl)(2-methylpropyl)amino)-2-hydroxy-1-benzylpropyl)((1S,2R,5R)-4,6-dioxabicyclo(3.3.0)oct-2-yloxy)carboxamide TMC114 [(S)-3-[(4-Amino-benzenesulfonyl)-isobutyl-amino]-2-hydroxy-1-((R)-phenylmethyl)-propyl]-carbamic acid (3R,3aS,6aR)-(hexahydro-furo[2,3-b]furan-3-yl) ester darunavir darunavirum {(1S,2R)-3-[(4-Amino-benzenesulfonyl)-isobutyl-amino]-1-benzyl-2-hydroxy-propyl}-carbamic acid (3R,3aS,6aR)-(hexahydro-furo[2,3-b]furan-3-yl) ester darunavir Beilstein:7960555 Beilstein CAS:206361-99-1 ChemIDplus Drug_Central:4143 DrugCentral PMID:15771427 ChEMBL PMID:16480273 ChEMBL PMID:25017682 Europe PMC Reaxys:7960555 Reaxys CHEBI:36796 Beilstein:8842375 CAS:116539-58-3 PMID:20825390 N-methyl-3-(naphthalen-1-yloxy)-3-(2-thienyl)propan-1-amine N-methyl-3-(1-naphthyloxy)-3-(2-thienyl)propan-1-amine duloxetine Beilstein:8842375 Beilstein CAS:116539-58-3 ChemIDplus PMID:20825390 Europe PMC CHEBI:36976 A nucleotide is a nucleoside phosphate resulting from the condensation of the 3 or 5 hydroxy group of a nucleoside with phosphoric acid. A nucleotide consists of a nitrogen-containing base, a five-carbon sugar, and one or more phosphate groups. Nucleotides can carry chemical energy (e.g. ATP), form coenzymes (e.g. CoA), be used as specific signaling molecules (e.g. cAMP) in the cell. Nucleotides are the subunits of the nucleic acids. IMR:0001349 nucleotide A nucleotide consists of a nitrogen-containing base, a five-carbon sugar, and one or more phosphate groups. Nucleotides can carry chemical energy (e.g. ATP), form coenzymes (e.g. CoA), be used as specific signaling molecules (e.g. cAMP) in the cell. Nucleotides are the subunits of the nucleic acids. ISBN:0815340729 CHEBI:37153 Any EC 3.1.3.* (phosphoric monoester hydrolase) inhibitor that interferes with the action of phosphoprotein phosphatase (EC 3.1.3.16). 3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase inhibitor 3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase inhibitors Aspergillus awamori acid protein phosphatase inhibitor Aspergillus awamori acid protein phosphatase inhibitors BCKDH phosphatase inhibitor BCKDH phosphatase inhibitors EC 3.1.3.16 (protein serine/threonine phosphatase) inhibitors EC 3.1.3.16 inhibitor EC 3.1.3.16 inhibitors HMG-CoA reductase phosphatase inhibitor HMG-CoA reductase phosphatase inhibitors branched-chain alpha-keto acid dehydrogenase phosphatase inhibitor branched-chain alpha-keto acid dehydrogenase phosphatase inhibitors calcineurin inhibitor calcineurin inhibitors casein phosphatase inhibitor casein phosphatase inhibitors phosphatase 2A inhibitor phosphatase 2A inhibitors phosphatase 2B inhibitor phosphatase 2B inhibitors phosphatase C-II inhibitor phosphatase C-II inhibitors phosphatase H-II inhibitor phosphatase H-II inhibitors phosphatase I inhibitor phosphatase I inhibitors phosphatase IB inhibitor phosphatase IB inhibitors phosphatase II inhibitor phosphatase II inhibitors phosphatase III inhibitor phosphatase III inhibitors phosphatase IV inhibitor phosphatase IV inhibitors phosphatase SP inhibitor phosphatase SP inhibitors phosphoprotein phosphatase (EC 3.1.3.16) inhibitor phosphoprotein phosphatase (EC 3.1.3.16) inhibitors phosphoprotein phosphatase inhibitor phosphoprotein phosphatase inhibitors phosphoprotein phosphohydrolase inhibitor phosphoprotein phosphohydrolase inhibitors phosphopyruvate dehydrogenase phosphatase inhibitor phosphopyruvate dehydrogenase phosphatase inhibitors phosphospectrin phosphatase inhibitor phosphospectrin phosphatase inhibitors polycation modulated (PCM-) phosphatase inhibitor polycation modulated (PCM-) phosphatase inhibitors protein D phosphatase inhibitor protein D phosphatase inhibitors protein phosphatase inhibitor protein phosphatase inhibitors protein phosphatase-1 inhibitor protein phosphatase-1 inhibitors protein phosphatase-2A inhibitor protein phosphatase-2A inhibitors protein phosphatase-2B inhibitor protein phosphatase-2B inhibitors protein phosphatase-2C inhibitor protein phosphatase-2C inhibitors protein serine/threonine phosphatase (EC 3.1.3.16) inhibitors protein serine/threonine phosphatase inhibitor protein serine/threonine phosphatase inhibitors serine/threonine specific protein phosphatase inhibitor serine/threonine specific protein phosphatase inhibitors EC 3.1.3.16 (phosphoprotein phosphatase) inhibitor CHEBI:3732 The 6-O-methyl ether of erythromycin A, clarithromycin is a macrolide antibiotic used in the treatment of respiratory-tract, skin and soft-tissue infections. It is also used to eradicate Helicobacter pylori in the treatment of peptic ulcer disease. It prevents bacteria from growing by interfering with their protein synthesis. Beilstein:3581974 CAS:81103-11-9 DrugBank:DB01211 Drug_Central:668 LINCS:LSM-5606 LIPID_MAPS_instance:LMPK04000014 PMID:16387493 Reaxys:3581974 CLARITHROMYCIN Clarithromycin O(6)-methylerythromycin 6-O-methylerythromycin 6-O-methylerythromycin A CLA clarithromycin clarithromycina clarithromycine clarithromycinum clarithromycin Beilstein:3581974 Beilstein CAS:81103-11-9 ChemIDplus Drug_Central:668 DrugCentral LIPID_MAPS_instance:LMPK04000014 LIPID MAPS PMID:16387493 ChEMBL Reaxys:3581974 Reaxys CHEBI:37328 phosphatidylinositol bisphosphate CHEBI:3750 The ethyl ester of clofibric acid. C12H15ClO3 CCOC(=O)C(C)(C)Oc1ccc(Cl)cc1 LINCS:LSM-2996 Open TG-Gates compound_id:00006 Wikipedia:Clofibrate ethyl 2-(4-chlorophenoxy)-2-methylpropanoate clofibrate CHEBI:37527 An acid is a molecular entity capable of donating a hydron (Bronsted acid) or capable of forming a covalent bond with an electron pair (Lewis acid). acid CHEBI:37550 A phosphosphingolipid that consists of sphingosine having a phospho group attached at position 1 Sphingolipid mediators, such as sphingosine 1-phosphate (S1P), ceramide, and sphingosine are derived by the enzymatic breakdown of sphingomyelin, an abundant membrane phospholipid. S1P is an evolutionarily conserved bioactive lipid mediator with potent effects on multiple organ systems. Sphingolipid mediators, such as sphingosine 1-phosphate (S1P), ceramide, and sphingosine are derived by the enzymatic breakdown of sphingomyelin, an abundant membrane phospholipid. S1P is an evolutionarily conserved bioactive lipid mediator with potent effects on multiple organ systems. IMR:0100179 S1P sphingosine-1-phosphate Sphingolipid mediators, such as sphingosine 1-phosphate (S1P), ceramide, and sphingosine are derived by the enzymatic breakdown of sphingomyelin, an abundant membrane phospholipid. S1P is an evolutionarily conserved bioactive lipid mediator with potent effects on multiple organ systems. PMID:15059942 CHEBI:37554 An acyl-CoA that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of any fatty acid. C22H35N7O17P3SR CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC([*])=O PMID:11524729 PMID:20442897 PMID:2079609 fatty acyl-CoA CHEBI:3766 A benzodiazepine that is 5H-dibenzo[b,e][1,4]diazepine substituted by a chloro group at position 8 and a 4-methylpiperazin-1-yl group at position 11. It is a second generation antipsychotic used in the treatment of psychiatric disorders like schizophrenia. Beilstein:0764984 CAS:5786-21-0 DrugBank:DB00363 Drug_Central:722 PMID:18690109 PMID:18766167 PMID:20825390 PMID:24219174 Reaxys:764984 8-chloro-11-(4-methylpiperazin-1-yl)-5H-dibenzo[b,e][1,4]diazepine Clozapine Clozapin clozapina clozapine clozapinum clozapine Beilstein:0764984 Beilstein CAS:5786-21-0 ChemIDplus Drug_Central:722 DrugCentral PMID:18690109 Europe PMC PMID:18766167 Europe PMC PMID:20825390 Europe PMC PMID:24219174 Europe PMC Reaxys:764984 Reaxys CHEBI:37670 A compound which inhibits or antagonizes the biosynthesis or actions of proteases (endopeptidases). protease inhibitors protease inhibitor CHEBI:37699 An EC 2.7.* (P-containing group transferase) inhibitor that interferes with the action of protein kinases. protein kinase inhibitors protein kinase inhibitor CHEBI:37700 An EC 2.7.11.* (protein-serine/threonine kinase) inhibitor that interferes with the action of protein kinase C (EC 2.7.11.13). ATP:protein phosphotransferase (diacylglycerol-dependent) inhibitor ATP:protein phosphotransferase (diacylglycerol-dependent) inhibitors EC 2.7.11.13 (protein kinase C) inhibitors EC 2.7.11.13 inhibitor EC 2.7.11.13 inhibitors PKC inhibitor PKC inhibitors PKCalpha inhibitor PKCalpha inhibitors PKCbeta inhibitor PKCbeta inhibitors PKCdelta inhibitor PKCdelta inhibitors PKCepsilon inhibitor PKCepsilon inhibitors PKCgamma inhibitor PKCgamma inhibitors PKCzeta inhibitor PKCzeta inhibitors PKN3 inhibitor PKN3 inhibitors Pkc1p inhibitor Pkc1p inhibitors STK24 inhibitor STK24 inhibitors cPKC inhibitor cPKC inhibitors cPKCalpha inhibitor cPKCalpha inhibitors cPKCbeta inhibitor cPKCbeta inhibitors cPKCgamma inhibitor cPKCgamma inhibitors calcium-dependent protein kinase C inhibitor calcium-dependent protein kinase C inhibitors calcium-independent protein kinase C inhibitor calcium-independent protein kinase C inhibitors calcium/phospholipid dependent protein kinase inhibitor calcium/phospholipid dependent protein kinase inhibitors nPKC inhibitor nPKC inhibitors nPKCdelta inhibitor nPKCdelta inhibitors nPKCepsilon inhibitor nPKCepsilon inhibitors nPKCeta inhibitor nPKCeta inhibitors nPKCtheta inhibitor nPKCtheta inhibitors protein kinase C (EC 2.7.11.13) inhibitor protein kinase C (EC 2.7.11.13) inhibitors protein kinase C inhibitor protein kinase C inhibitors protein kinase Cepsilon inhibitor protein kinase Cepsilon inhibitors EC 2.7.11.13 (protein kinase C) inhibitor CHEBI:37733 An EC 3.1.1.* (carboxylic ester hydrolase) inhibitor that interferes with the action of cholinesterase (EC 3.1.1.8). BChE inhibitor BChE inhibitors BtChoEase inhibitor BtChoEase inhibitors EC 3.1.1.8 (cholinesterase) inhibitors EC 3.1.1.8 inhibitor EC 3.1.1.8 inhibitors anticholineesterase inhibitor anticholineesterase inhibitors anticholinesterase anticholinesterases benzoylcholinesterase inhibitor benzoylcholinesterase inhibitors butyrylcholine esterase inhibitor butyrylcholine esterase inhibitors butyrylcholinesterase inhibitor butyrylcholinesterase inhibitors choline esterase II (unspecific) inhibitor choline esterase II (unspecific) inhibitors choline esterase inhibitor choline esterase inhibitors cholinesterase (EC 3.1.1.8) inhibitor cholinesterase (EC 3.1.1.8) inhibitors cholinesterase inhibitor non-specific cholinesterase inhibitor non-specific cholinesterase inhibitors propionylcholinesterase inhibitor propionylcholinesterase inhibitors pseudocholinesterase inhibitor pseudocholinesterase inhibitors EC 3.1.1.8 (cholinesterase) inhibitor CHEBI:37734 phosphoric ester CHEBI:37739 Any glycerolipid having a phosphate group ester-linked to a terminal carbon of the glycerol backbone. Any glycerolipid having a phosphate group ester-linked to a terminal carbon of the glycerol backbone. PMID:17393491 http://purl.obolibrary.org/obo/IMR_0001384 phosphatide phosphoglyceride glycerophospholipid Any glycerolipid having a phosphate group ester-linked to a terminal carbon of the glycerol backbone. CHEBI:37739 CHEBI:37845 A hormone that specifically regulates growth. CAS:9002-72-6 growth hormone CHEBI:37886 An agent that selectively binds to and activates adrenergic receptors. adrenergic agonists adrenergic receptor agonist adrenoceptor agonists adrenomimetic adrenomimetics adrenergic agonist CHEBI:37887 An agent that binds to but does not activate adrenergic receptors thereby blocking the actions of endogenous or exogenous adrenergic agonists. adrenergic antagonists adrenergic blockaders adrenergic blocker adrenergic blockers adrenergic receptor blockaders adrenoceptor antagonists adrenergic antagonist CHEBI:37890 An agent that binds to but does not activate alpha-adrenergic receptors thereby blocking the actions of endogenous or exogenous alpha-adrenergic agonists. alpha-Adrenergic antagonists are used in the treatment of hypertension, vasospasm, peripheral vascular disease, shock, and pheochromocytoma. alpha-adrenergic antagonists alpha-adrenergic blocker alpha-adrenergic blockers alpha-adrenergic receptor blockaders alpha-adrenoceptor antagonists alpha-adrenergic antagonist CHEBI:37924 A heavily substituted carbohydrazide that is an antiretroviral drug of the protease inhibitor (PI) class used to treat infection of human immunodeficiency virus (HIV). COC(=O)N[C@H](C(=O)N[C@@H](Cc1ccccc1)[C@@H](O)CN(Cc1ccc(cc1)-c1ccccn1)NC(=O)[C@@H](NC(=O)OC)C(C)(C)C)C(C)(C)C CAS:198904-31-3 DrugBank:DB01072 Wikipedia:Atazanavir dimethyl (3S,8S,9S,12S)-9-benzyl-3,12-di-tert-butyl-8-hydroxy-4,11-dioxo-6-[4-(2-pyridyl)benzyl]-2,5,6,10,13-pentaazatetradecanedioate atazanavir CHEBI:37956 Histamine antagonists are the drugs that bind to but do not activate histamine receptors, thereby blocking the actions of histamine or histamine agonists. PMID:22035879 antihistamine antihistamines antihistaminico antihistaminics histamine receptor blocker histamine receptor blockers histamine antagonist PMID:22035879 Europe PMC CHEBI:37957 Drugs used for their actions on histaminergic systems. histamine agents histamine drugs histaminergic agent histaminergic agents histaminergic drugs histaminergic drug CHEBI:37962 Any agent that acts on an adrenergic receptor or affects the life cycle of an adrenergic transmitter. adrenergic agents adrenergic drug adrenergic drugs adrenergic neuron agents adrenergics adrenergic agent CHEBI:37972 phosphorus-32 atom The radioactive isotope of phosphorus with relative atomic mass 31.973907 and half-life of 14.26 days. phosphorus-32 atom CHEBI:37973 phosphorus-33 atom The radioactive isotope of phosphorus with relative atomic mass 32.971725, half-life of 25.34 days and nuclear spin (1)/2. phosphorus-33 atom CHEBI:37987 Cy3 dye Cy3 dye CHEBI:37989 Cy5 dye Cy5 dye CHEBI:38068 A drug used in the treatment of malaria. Antimalarials are usually classified on the basis of their action against Plasmodia at different stages in their life cycle in the human. antimalarials antimalarial CHEBI:38070 A drug used for the treatment or prevention of cardiac arrhythmias. Anti-arrhythmia drugs may affect the polarisation-repolarisation phase of the action potential, its excitability or refractoriness, or impulse conduction or membrane responsiveness within cardiac fibres. antiarrhythmic agent anti-arrhythmia drug CHEBI:38147 A drug that has a strengthening effect on the heart or that can increase cardiac output. cardiotonic drug CHEBI:3815 collagen CHEBI:38157 iron chelating agents iron chelators iron chelator CHEBI:38161 A ligand with two or more separate binding sites that can bind to a single metallic central atom, forming a chelate. Chelating agent Metal chelator chelating agents chelators complexon chelator CHEBI:38213 A hydrochloride that is the monohydrochloride salt of methapyrilene. C14H19N3S.ClH C14H20ClN3S Cl.CN(C)CCN(Cc1cccs1)c1ccccn1 CAS:135-23-9 DrugBank:DB04819 N,N-dimethyl-N'-pyridin-2-yl-N'-[(thiophen-2-yl)methyl]ethane-1,2-diamine hydrochloride Methapyrilene hydrochloride CHEBI:38214 A member of the class of phhenylureas that is urea in which one of the nitrogens is substituted by a p-chlorophenyl group while the other is substituted by two methyl groups. C9H11ClN2O CN(C)C(=O)Nc1ccc(Cl)cc1 CAS:150-68-5 3-(4-chlorophenyl)-1,1-dimethylurea Monuron CHEBI:38215 One of a class of drugs that acts by selective inhibition of calcium influx through cell membranes or on the release and binding of calcium in intracellular pools. calcium channel antagonist calcium channel antagonists calcium channel blockers calcium channel blocker CHEBI:38221 A diester that results from the condensation of the 1-carboxy groups of two molecules of propane-1,2,3-tricarboxylic acid with hydroxy groups at positions 14 and 15 of (2S,3S,5R,10R,12S,14S,15R,16R)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol. C34H59NO15 CCCC[C@H]([C@H]([C@H](C[C@H](C[C@@H](CCCC[C@H](C[C@@H]([C@H](C)N)O)O)O)C)OC(C[C@@H](CC(=O)O)C(=O)O)=O)OC(=O)C[C@@H](CC(O)=O)C(=O)O)C CAS:116355-83-0 (2R,2'R)-2,2'-{[(5R,6R,7S,9S,11R,16R,18S,19S)-19-amino-11,16,18-trihydroxy-5,9-dimethylicosane-6,7-diyl]bis[oxy(2-oxoethane-2,1-diyl)]}dibutanedioic acid fumonisin B1 CHEBI:38234 Any inhibitor of a DNA polymerase. DNA polymerase inhibitor CHEBI:38323 Any drug used for its actions on cholinergic systems. Included here are agonists and antagonists, drugs that affect the life cycle of acetylcholine, and drugs that affect the survival of cholinergic neurons. cholinergic agent cholinergic drugs cholinomimetic cholinergic drug CHEBI:38462 An EC 3.1.1.* (carboxylic ester hydrolase) inhibitor that interferes with the action of enzyme acetylcholinesterase (EC 3.1.1.7), which helps breaking down of acetylcholine into choline and acetic acid. EC 3.1.1.7 (acetylcholinesterase) inhibitor role acetylcholinesterase inhibitor role CHEBI:38496 A role played by the entity that inhibits the electron-transport chain electron-transport chain inhibitor CHEBI:38497 A role played by the entity that inhibits the respiratory-chain. respiratory-chain inhibitor CHEBI:38503 A respiratory-chain inhibitor that interferes with the action of the the enzyme NADH:ubiquinone reductase (H(+)-translocating), EC 1.6.5.3. DPNH-coenzyme Q reductase inhibitor DPNH-ubiquinone reductase inhibitor EC 1.6.5.3 (NADH:ubiquinone reductase (H(+)-translocating)) inhibitor EC 1.6.5.3 (NADH:ubiquinone reductase (H(+)-translocating)) inhibitors EC 1.6.5.3 [NADH:ubiquinone reductase (H(+)-translocating)] inhibitors EC 1.6.5.3 inhibitor EC 1.6.5.3 inhibitors NADH coenzyme Q1 reductase inhibitor NADH coenzyme Q1 reductase inhibitors NADH dehydrogenase (ubiquinone) inhibitor NADH dehydrogenase (ubiquinone) inhibitors NADH-CoQ oxidoreductase inhibitor NADH-CoQ oxidoreductase inhibitors NADH-CoQ reductase inhibitor NADH-CoQ reductase inhibitors NADH-Q6 oxidoreductase inhibitor NADH-coenzyme Q oxidoreductase inhibitors NADH-coenzyme Q reductase inhibitor NADH-coenzyme Q reductase inhibitors NADH-ubiquinone oxidoreductase inhibitor NADH-ubiquinone oxidoreductase inhibitors NADH-ubiquinone reductase inhibitor NADH-ubiquinone reductase inhibitors NADH-ubiquinone-1 reductase inhibitor NADH-ubiquinone-1 reductase inhibitors NADH2 dehydrogenase (ubiquinone) inhibitor NADH:ubiquinone oxidoreductase complex inhibitor NADH:ubiquinone oxidoreductase inhibitor NADH:ubiquinone oxidoreductase inhibitors NADH:ubiquinone reductase (H(+)-translocating) inhibitor NADH:ubiquinone reductase (H(+)-translocating) inhibitors NADH:ubiquinone reductase (H+-translocating) inhibitor NADH:ubiquinone reductase inhibitor coenzyme Q reductase complex 1 dehydrogenase inhibitor complex I (NADH:Q1 oxidoreductase) inhibitors complex I (electron transport chain) inhibitors complex I (mitochondrial electron transport) inhibitors dihydronicotinamide adenine dinucleotide-coenzyme Q reductase inhibitor electron transfer complex I inhibitor electron transfer complex I inhibitors mitochondrial electron transport complex 1 inhibitor mitochondrial electron transport complex I inhibitor mitochondrial electron transport complex I inhibitors reduced nicotinamide adenine dinucleotide-coenzyme Q reductase inhibitor reduced nicotinamide adenine dinucleotide-coenzyme Q reductase inhibitors type 1 dehydrogenase inhibitor type 1 dehydrogenase inhibitors ubiquinone reductase inhibitor ubiquinone reductase inhibitors EC 1.6.5.3 [NADH:ubiquinone reductase (H(+)-translocating)] inhibitor CHEBI:38632 Any agent that affects the transport of molecular entities across a biological membrane. membrane transport modulators membrane transport modulator CHEBI:38633 An agent that inhibits sodium influx through cell membranes. Na channel blocker sodium channel blockers sodium channel blocker CHEBI:38637 Any protein kinase inhibitor that interferes with the action of tyrosine kinase. TKI inhibitor TKI inhibitors protein tyrosine kinase inhibitor protein tyrosine kinase inhibitors tyrosine kinase inhibitors tyrphostin tyrphostins tyrosine kinase inhibitor CHEBI:38807 Agents that increase calcium influx into calcium channels of excitable tissues. calcium channel activator calcium channel agonist CHEBI:38808 A membrane transport modulator that is able to regulate intracellular calcium levels. calcium channel modulators calcium channel modulator CHEBI:38809 RyR modulator ryanodine receptor modulator CHEBI:38940 CAS:557795-19-4 DrugBank:DB01268 Drug_Central:2544 PMID:12531805 PMID:16845442 PMID:16916320 PMID:17327610 PMID:17962201 PMID:18971320 PMID:19830602 PMID:20406969 PMID:21792888 PMID:24188025 PMID:24393200 PMID:24402960 PMID:24403097 PMID:24521256 N-[2-(diethylamino)ethyl]-5-[(Z)-(5-fluoro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide Sunitinib SU-11248 Sutent sunitinib sunitinibum sunitinib CAS:557795-19-4 ChemIDplus Drug_Central:2544 DrugCentral PMID:12531805 Europe PMC PMID:16845442 Europe PMC PMID:16916320 Europe PMC PMID:17327610 Europe PMC PMID:17962201 Europe PMC PMID:18971320 Europe PMC PMID:19830602 Europe PMC PMID:20406969 Europe PMC PMID:21792888 Europe PMC PMID:24188025 Europe PMC PMID:24393200 Europe PMC PMID:24402960 Europe PMC PMID:24403097 Europe PMC PMID:24521256 Europe PMC CHEBI:39000 sodium channel modulators sodium channel modulator CHEBI:39025 A class of lipoproteins of small size (4-13 nm) and dense (greater than 1.063 g/ml) particles. They are synthesized in the liver without a lipid core, accumulate cholesterol esters from peripheral tissues and transport them to the liver for re-utilization or elimination from the body (the reverse cholesterol transport). HDL high-density lipoprotein CHEBI:39026 A class of lipoproteins of small size (18-25 nm) and low density (1.019-1.063 g/ml) particles with a core composed mainly of cholesterol esters and smaller amounts of triglycerides. The surface monolayer consists mostly of phospholipids, a single copy of apolipoprotein B-100, and free cholesterol molecules. The main function of LDL is to transport cholesterol and cholesterol esters from the liver. Excessive levels are associated with cardiovascular disease. LDL Wikipedia:Low-density_lipoprotein low-density lipoprotein CHEBI:39027 A class of lipoproteins of large size (30-80 nm), very low density (0.93-1.006 g/ml) particles with a core composed mainly of triglycerides and a surface monolayer of phospholipids and cholesterol into which are imbedded the apolipoproteins B, E, and C. VLDL facilitate the transport of endogenously made triglycerides to extrahepatic tissues. VLDL very-low-density lipoproteins very-low-density lipoprotein CHEBI:39098 The active insecticidal constituents of Chrysanthemum cinerariifolium flowers. CAS:8003-34-7 pyrethrins CHEBI:39123 calcium cation CHEBI:39124 A calcium cation that has formula Ca. Ca(2+) Ca++ Ca2+ calcium(2+) calcium ion CHEBI:39548 A dihydroxy monocarboxylic acid that is a member of the drug class known as statins, used primarily for lowering blood cholesterol and for preventing cardiovascular diseases. Beilstein:8373630 CAS:134523-00-5 DrugBank:DB01076 Drug_Central:257 LINCS:LSM-5771 PMID:11693468 PMID:15012735 PMID:18720283 Reaxys:8373630 (3R,5R)-7-[3-(anilinocarbonyl)-5-(4-fluorophenyl)-4-phenyl-2-(propan-2-yl)-1H-pyrrol-1-yl]-3,5-dihydroxyheptanoic acid Atorvastatin (R-(R*,R*))-2-(4-Fluorophenyl)-beta,delta-dihydroxy-5-(1-methylethyl)-3-phenyl-4-((phenylamino)carbonyl)-1H-pyrrole-1-heptanoic acid 7-[2-(4-FLUORO-PHENYL)-5-ISOPROPYL-3-PHENYL-4-PHENYLCARBAMOYL-PYRROL-1-YL]-3,5-DIHYDROXY-HEPTANOIC ACID Atorlip atorvastatin atorvastatina atorvastatine atorvastatinum atorvastatin Beilstein:8373630 Beilstein CAS:134523-00-5 ChemIDplus Drug_Central:257 DrugCentral PMID:11693468 Europe PMC PMID:15012735 Europe PMC PMID:18720283 Europe PMC Reaxys:8373630 Reaxys CHEBI:39669 An organofluorine compound comprising salicylic acid having a 2,4-difluorophenyl group at the 5-position. CAS:22494-42-4 DrugBank:DB00861 Drug_Central:880 LINCS:LSM-2490 PMID:23144359 PMID:23416065 PMID:28166217 Reaxys:2654431 2',4'-difluoro-4-hydroxy-[1,1'-biphenyl]-3-carboxylic acid Diflunisal 2',4'-difluoro-4-hydroxy-3-biphenylcarboxylic acid 2-(hydroxy)-5-(2,4-difluorophenyl)benzoic acid 5-(2,4-difluorophenyl)salicylic acid Dolobid diflunisal CAS:22494-42-4 ChemIDplus CAS:22494-42-4 NIST Chemistry WebBook Drug_Central:880 DrugCentral PMID:23144359 Europe PMC PMID:23416065 Europe PMC PMID:28166217 Europe PMC Reaxys:2654431 Reaxys CHEBI:39867 A branched-chain saturated fatty acid that comprises of a propyl substituent on a pentanoic acid stem. C8H16O2 CCCC(CCC)C(O)=O Beilstein:1750447 CAS:99-66-1 DrugBank:DB00313 Drug_Central:2803 LINCS:LSM-4620 LIPID_MAPS_instance:LMFA01020291 PMID:11716839 PMID:12475192 PMID:15124690 PMID:15560954 PMID:15578701 PMID:16496131 PMID:16621443 PMID:16759735 PMID:17156483 PMID:17273758 PMID:19280426 PMID:19318486 PMID:23792104 PMID:23810771 PMID:23949302 PMID:24135375 PMID:24200999 PMID:24348849 PMID:8558327 PMID:8681902 Reaxys:1750447 Wikipedia:Valproic_Acid 2-propylpentanoic acid VALPROIC ACID 2-PROPYL-PENTANOIC ACID 2-n-propyl-n-valeric acid 2-propylpentanoic acid 2-propylvaleric acid 4-heptanecarboxylic acid DPA Depakene Di-n-propylessigsaeure VPA Valproinsaeure acide valproique acido valproico acidum valproicum di-n-propylacetic acid dipropylacetic acid n-DPA valproic acid valproic acid Beilstein:1750447 ChemIDplus CAS:99-66-1 ChemIDplus CAS:99-66-1 NIST Chemistry WebBook Drug_Central:2803 DrugCentral LIPID_MAPS_instance:LMFA01020291 LIPID MAPS PMID:11716839 Europe PMC PMID:12475192 Europe PMC PMID:15124690 Europe PMC PMID:15560954 Europe PMC PMID:15578701 Europe PMC PMID:16496131 Europe PMC PMID:16621443 Europe PMC PMID:16759735 Europe PMC PMID:17156483 Europe PMC PMID:17273758 Europe PMC PMID:19280426 Europe PMC PMID:19318486 Europe PMC PMID:23792104 Europe PMC PMID:23810771 Europe PMC PMID:23949302 Europe PMC PMID:24135375 Europe PMC PMID:24200999 Europe PMC PMID:24348849 Europe PMC PMID:8558327 Europe PMC PMID:8681902 Europe PMC Reaxys:1750447 Reaxys CHEBI:40279 A bicyclic structure comprising a pyrazole ring fused to a hydroxy-substituted pyrimidine ring. Beilstein:608611 CAS:315-30-0 DrugBank:DB00437 Drug_Central:124 LINCS:LSM-5919 PMID:11333159 PMID:16650385 PMID:24395556 PMID:24590210 PMID:24591375 PMID:7602118 Reaxys:608611 1H-pyrazolo[3,4-d]pyrimidin-4-ol Allopurinol 1,5-Dihydro-4H-pyrazolo(3,4-d)pyrimidin-4-one 1,5-Dihydro-4H-pyrazolo(3,4-d)pyrimidine-4-one 1H-Pyrazolo(3,4-d)pyrimidin-4-ol 4'-Hydroxypyrazolol(3,4-d)pyrimidine 4-HPP 4-Hydroxy-1H-pyrazolo(3,4-d)pyrimidine 4-Hydroxy-3,4-pyrazolopyrimidine 4-Hydroxypyrazolo(3,4-d)pyrimidine 4-Hydroxypyrazolopyrimidine 4-Hydroxypyrazolyl(3,4-d)pyrimidine 4H-Pyrazolo(3,4-d)pyrimidin-4-one AL-100 Allopurinolum Alopurinol Zyloprim (TN) allopurinol Beilstein:608611 Beilstein CAS:315-30-0 ChemIDplus CAS:315-30-0 NIST Chemistry WebBook Drug_Central:124 DrugCentral PMID:11333159 Europe PMC PMID:16650385 Europe PMC PMID:24395556 Europe PMC PMID:24590210 Europe PMC PMID:24591375 Europe PMC PMID:7602118 Europe PMC Reaxys:608611 Reaxys CHEBI:4031 A cyclic nonribosomal peptide of eleven amino acids; an immunosuppressant drug widely used in post-allogeneic organ transplant to reduce the activity of the patient's immune system, and therefore the risk of organ rejection. Also causes reversible inhibition of immunocompetent lymphocytes in the G0- and G1-phase of the cell cycle. C62H111N11O12 CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O)C(C)C DrugBank:DB00091 LINCS:LSM-1703 30-ethyl-33-[(4E)-1-hydroxy-2-methylhex-4-en-1-yl]-1,4,7,10,12,15,19,25,28-nonamethyl-6,9,18,24-tetrakis(2-methylpropyl)-3,21-bis(propan-2-yl)-1,4,7,10,13,16,19,22,25,28,31-undecaazacyclotritriacontane-2,5,8,11,14,17,20,23,26,29,32-undecone cyclosporin A CHEBI:41774 Tamoxifen, sold under the brand name Nolvadex among others, is a medication that is used to prevent breast cancer in women and treat breast cancer in women and men. (by Wikipedia) C26H29NO CC\C(c1ccccc1)=C(/c1ccccc1)c1ccc(OCCN(C)C)cc1 Beilstein:2062020 CAS:10540-29-1 DrugBank:DB00675 Drug_Central:2561 PMID:12612646 PMID:14681337 PMID:14709804 PMID:18348622 PMID:7688593 2-{4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy}-N,N-dimethylethanamine Tamoxifen (Z)-2-(4-(1,2-Diphenyl-1-butenyl)phenoxy)-N,N-dimethylethanamine (Z)-2-(para-(1,2-Diphenyl-1-butenyl)phenoxy)-N,N-dimethylamine 1-p-beta-Dimethylaminoethoxyphenyl-trans-1,2-diphenylbut-1-ene 1-para-beta-Dimethylaminoethoxyphenyl-trans-1,2-diphenylbut-1-ene Apo-Tamox Crisafeno Diemon tamoxifen tamoxifene tamoxifeno tamoxifenum trans-Tamoxifen tamoxifen Beilstein:2062020 Beilstein CAS:10540-29-1 ChemIDplus Drug_Central:2561 DrugCentral PMID:14681337 Europe PMC PMID:14709804 Europe PMC PMID:18348622 Europe PMC PMID:7688593 Europe PMC CHEBI:41879 A fluorinated steroid that is 9-fluoropregna-1,4-diene substituted by hydroxy groups at positions 11, 17 and 21, a methyl group at position 16 and oxo groups at positions 3 and 20. It is a synthetic member of the class of glucocorticoids. 0 C22H29FO5 InChI=1S/C22H29FO5/c1-12-8-16-15-5-4-13-9-14(25)6-7-19(13,2)21(15,23)17(26)10-20(16,3)22(12,28)18(27)11-24/h6-7,9,12,15-17,24,26,28H,4-5,8,10-11H2,1-3H3/t12-,15+,16+,17+,19+,20+,21+,22+/m1/s1 UREBDLICKHMUKA-CXSFZGCWSA-N 392.46106 392.19990 [H][C@@]12C[C@@H](C)[C@](O)(C(=O)CO)[C@@]1(C)C[C@H](O)[C@@]1(F)[C@@]2([H])CCC2=CC(=O)C=C[C@]12C Beilstein:2066652 CAS:50-02-2 DrugBank:DB01234 Drug_Central:824 HMDB:HMDB0015364 PMID:11508649 PMID:18272184 PMID:18524938 PMID:32412710 Patent:DE1113690 Patent:GB869511 Patent:US3007923 Reaxys:2066652 VSDB:1769 Wikipedia:Dexamethasone 9-fluoro-11beta,17,21-trihydroxy-16alpha-methylpregna-1,4-diene-3,20-dione Dexamethasone dexamethasone 1-Dehydro-16alpha-methyl-9alpha-fluorohydrocortisone 16alpha-Methyl-9alpha-fluoro-1-dehydrocortisol 9alpha-Fluoro-16alpha-methylprednisolone Decadron dexametasona dexamethasone dexamethasonum dexamethasone HOIP_0040473 PMID:32412710 A large, randomized clinical trial involving more than 6400 hospitalized patients with Covid-19 showed that dexamethasone significantly reduced 30-day mortality (17% reduction); benefit was limited to patients who required oxygen supplementation and appeared greater in patients receiving mechanical ventilation. CHEBI:42098 digoxigenin A hydroxy steroid that consists of 5beta-cardanolide having a double bond at the 20(22)-position as well as hydroxy groups at the 3beta-, 12beta- and 14beta-positions. It has been isolated from the plant species of the genus Digitalis. digoxigenin CHEBI:421707 A 2,6-diaminopurine that is (1S)-cyclopent-2-en-1-ylmethanol in which the pro-R hydrogen at the 4-position is substituted by a 2-amino-6-(cyclopropylamino)-9H-purin-9-yl group. A nucleoside analogue reverse transcriptase inhibitor (NRTI) with antiretroviral activity against HIV, it is used (particularly as the sulfate) with other antiretrovirals in combination therapy of HIV infection. Beilstein:7493116 CAS:136470-78-5 DrugBank:DB01048 Drug_Central:34 PMID:11678376 PMID:11806176 PMID:12781181 PMID:15887959 PMID:16458506 PMID:16539393 PMID:16759112 PMID:17172311 PMID:17870541 PMID:18029175 PMID:18549801 PMID:24751900 PMID:25017682 PMID:25674793 PMID:26024233 Reaxys:7493116 Abacavir {(1S,4R)-4-[2-amino-6-(cyclopropylamino)-9H-purin-9-yl]cyclopent-2-en-1-yl}methanol ABC abacavir {(1S-cis)-4-[2-amino-6-(cyclopropylamino)-9H-purin-9-yl]cyclopent-2-en-1-yl}methanol abacavir Beilstein:7493116 Beilstein CAS:136470-78-5 ChemIDplus Drug_Central:34 DrugCentral PMID:11678376 Europe PMC PMID:11806176 Europe PMC PMID:12781181 ChEMBL PMID:15887959 ChEMBL PMID:16458506 ChEMBL PMID:16539393 ChEMBL PMID:16759112 ChEMBL PMID:17172311 ChEMBL PMID:17870541 ChEMBL PMID:18029175 ChEMBL PMID:18549801 Europe PMC PMID:24751900 Europe PMC PMID:25017682 Europe PMC PMID:25674793 Europe PMC PMID:26024233 Europe PMC Reaxys:7493116 Reaxys CHEBI:42355 An erythromycin that consists of erythronolide A having 2,6-dideoxy-3-C-methyl-3-O-methyl-α-L-ribo-hexopyranosyl and 3,4,6-trideoxy-3-(dimethylamino)-β-D-xylo-hexopyranosyl residues attahced at positions 4 and 6 respectively. C37H67NO13 CC[C@H]1OC(=O)[C@H](C)[C@@H](O[C@H]2C[C@@](C)(OC)[C@@H](O)[C@H](C)O2)[C@H](C)[C@@H](O[C@@H]2O[C@H](C)C[C@@H]([C@H]2O)N(C)C)[C@](C)(O)C[C@@H](C)C(=O)[C@H](C)[C@@H](O)[C@]1(C)O DrugBank:DB00199 Wikipedia:Erythromycin erythromycin A CHEBI:4305 A monocarboxylic acid amide that is 1H-imidazole-4-carboxamide which is substituted at position 5 by a 3,3-dimethyltriaz-1-en-1-yl group. It is used for the treatment of metastatic malignant melanoma, and in combination with other drugs for the treatment of Hodgkin's disease and soft-tissue sarcoma. Beilstein:521487 CAS:4342-03-4 DrugBank:DB00851 Drug_Central:773 PMID:10751609 PMID:11318431 PMID:12195827 PMID:15010317 PMID:20082117 PMID:21471822 PMID:21654834 PMID:23029050 PMID:23318786 PMID:26940170 PMID:28096700 PMID:28250333 PMID:28387914 PMID:28419676 PMID:29076951 PMID:29184162 PMID:29287706 PMID:29296081 PMID:29305638 PMID:29344241 Reaxys:521487 5-(3,3-dimethyltriaz-1-en-1-yl)-1H-imidazole-4-carboxamide 4-(3,3-dimethyl-1-triazeno)imidazole-5-carboxamide 4-(5)-(3,3-dimethyl-1-triazeno)imidazole-5(4)-carboxamide 4-(dimethyltriazeno)imidazole-5-carboxamide 5-(3,3-Dimethyl-1-triazeno)imidazole-4-carboxamide 5-(3,3-dimethyl-1-triazeno)imidazole-4-carboxamide 5-(3,3-dimethyltriazeno)imidazole-4-carboxamide 5-(dimethyltriazeno)imidazole-4-carboxamide DIC DTIC Di-me-triazenoimidazolecarboxamide Dtic-Dome (TN) HSDB 3219 ICDMT Imidazole-4-carboxamide, 5-(3,3-dimethyl-1-triazeno)- NCI-C04717 NSC 45388 NSC-45388 dacarbazina dacarbazine dacarbazinum deticene dacarbazine Beilstein:521487 Beilstein CAS:4342-03-4 ChemIDplus CAS:4342-03-4 NIST Chemistry WebBook Drug_Central:773 DrugCentral PMID:10751609 Europe PMC PMID:11318431 Europe PMC PMID:12195827 Europe PMC PMID:15010317 Europe PMC PMID:20082117 Europe PMC PMID:21471822 Europe PMC PMID:21654834 Europe PMC PMID:23029050 Europe PMC PMID:23318786 Europe PMC PMID:26940170 Europe PMC PMID:28096700 Europe PMC PMID:28250333 Europe PMC PMID:28387914 Europe PMC PMID:28419676 Europe PMC PMID:29076951 Europe PMC PMID:29184162 Europe PMC PMID:29287706 Europe PMC PMID:29296081 Europe PMC PMID:29305638 Europe PMC PMID:29344241 Europe PMC Reaxys:521487 Reaxys CHEBI:4315 Beilstein:4851114 CAS:17230-88-5 DrugBank:DB01406 Drug_Central:779 PMID:17929794 PMID:18834112 [1,2]oxazolo[4',5':2,3]-17alpha-pregn-4-en-20-yn-17-ol Cyclomen Danocrine danazol danazolum danazol Beilstein:4851114 Beilstein CAS:17230-88-5 ChemIDplus Drug_Central:779 DrugCentral PMID:17929794 ChEMBL PMID:18834112 ChEMBL CHEBI:4317 The hydrazone resulting from the formal condensation of 5-(4-nitrophenyl)furfural with 1-aminohydantoin. Beilstein:705189 CAS:7261-97-4 DrugBank:DB01219 LINCS:LSM-3823 1-({[5-(4-nitrophenyl)furan-2-yl]methylidene}amino)imidazolidine-2,4-dione Dantrolene 1-((5-(p-nitrophenyl)furfurylidene)amino)hydantoin dantrolene dantroleno dantrolenum dantrolene Beilstein:705189 Beilstein CAS:7261-97-4 ChemIDplus CHEBI:44032 CAS:150378-17-9 DrugBank:DB00224 Drug_Central:1437 LINCS:LSM-5471 (2S)-1-[(2S,4R)-4-benzyl-2-hydroxy-5-{[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino}-5-oxopentyl]-N-tert-butyl-4-(pyridin-3-ylmethyl)piperazine-2-carboxamide 2-benzyl-5-[(2S)-2-(tert-butylcarbamoyl)-4-(pyridin-3-ylmethyl)piperazin-1-yl]-2,3,5-trideoxy-N-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-D-erythro-pentonamide Indinavir (1(1S,2R),5(S))-2,3,5-Trideoxy-N-(2,3-dihydro-2-hydroxy-1H-inden-1-yl)-5-(2-(((1,1-dimethylethyl)amino)carbonyl)-4-(3-pyridinylmethyl)-1-piperazinyl)-2-(phenylmethyl)-D-erythro-Pentonamide indinavir CAS:150378-17-9 ChemIDplus Drug_Central:1437 DrugCentral CHEBI:44185 Beilstein:70669 CAS:59-05-2 DrugBank:DB00563 Drug_Central:1751 LINCS:LSM-5690 METHOTREXATE Methotrexate N-(4-{[(2,4-diaminopteridin-6-yl)methyl](methyl)amino}benzoyl)-L-glutamic acid 4-amino-10-methylfolic acid 4-amino-N(10)-methylpteroylglutamic acid Emtexate Ledertrexate MTX N-[4-[[(2,4-diamino-6-pteridinyl)methyl]methylamino]benzoyl]-L-glutamic acid Rheumatrex Trexall methotrexate methotrexatum metotrexato methotrexate Beilstein:70669 Beilstein CAS:59-05-2 ChemIDplus CAS:59-05-2 NIST Chemistry WebBook Drug_Central:1751 DrugCentral CHEBI:4439 A mucopolysaccharide consisting of repeating beta-(1->4)-linked L-iduronyl-(beta1->3)-N-acetyl-D-galactosamine units. Dermatan Dermatan L-iduronate dermatan CHEBI:44423 A member of the class of ureas that is urea in which one of the hydrogens is replaced by a hydroxy group. An antineoplastic used in the treatment of chronic myeloid leukaemia as well as for sickle-cell disease. Beilstein:1741548 CAS:127-07-1 DrugBank:DB01005 Drug_Central:1399 Gmelin:130423 PMID:11285159 PMID:11298103 PMID:11364534 PMID:11365149 PMID:11391710 PMID:12107454 PMID:14988684 PMID:15772364 PMID:15994344 PMID:16356682 PMID:22983419 PMID:23318979 PMID:23643402 PMID:23696560 PMID:9271088 Reaxys:1741548 Hydroxyurea N-hydroxyurea hydroxyurea Hydroxycarbamid Hydroxycarbamide Hydroxyharnstoff N-HYDROXYUREA N-carbamoylhydroxylamine carbamohydroxamic acid carbamohydroximic acid carbamoyl oxime carbamyl hydroxamate hidroxicarbamida hydrea hydroxycarbamide hydroxycarbamidum oxyurea hydroxyurea Beilstein:1741548 ChemIDplus CAS:127-07-1 ChemIDplus Drug_Central:1399 DrugCentral Gmelin:130423 Gmelin PMID:11285159 Europe PMC PMID:11298103 Europe PMC PMID:11364534 Europe PMC PMID:11365149 Europe PMC PMID:11391710 Europe PMC PMID:12107454 Europe PMC PMID:14988684 Europe PMC PMID:15772364 Europe PMC PMID:15994344 Europe PMC PMID:16356682 Europe PMC PMID:22983419 Europe PMC PMID:23318979 Europe PMC PMID:23643402 Europe PMC PMID:23696560 Europe PMC PMID:9271088 Europe PMC Reaxys:1741548 Reaxys CHEBI:44445 An aromatic ether having phenyl and 2-methylsulfonamido-5-nitrophenyl as the two aryl groups. C13H12N2O5S CS(=O)(=O)Nc1ccc(cc1Oc1ccccc1)[N+]([O-])=O Beilstein:2421175 CAS:51803-78-2 DrugBank:DB04743 Drug_Central:1935 LINCS:LSM-3718 PMID:18426087 Reaxys:2421175 N-(4-nitro-2-phenoxyphenyl)methanesulfonamide Nimesulide 4'-nitro-2'-phenoxymethanesulfonanilide 4-NITRO-2-PHENOXYMETHANESULFONANILIDE nimesulide Beilstein:2421175 Beilstein CAS:51803-78-2 ChemIDplus Drug_Central:1935 DrugCentral PMID:18426087 Europe PMC Reaxys:2421175 Reaxys CHEBI:45304 CAS:61379-65-5 DrugBank:DB01201 (7S,9E,11S,12R,13S,14R,15R,16R,17S,18S,19E,21Z)-26-{(E)-[(4-cyclopentylpiperazin-1-yl)imino]methyl}-2,15,17,27,29-pentahydroxy-11-methoxy-3,7,12,14,16,18,22-heptamethyl-6,23-dioxo-8,30-dioxa-24-azatetracyclo[23.3.1.1(4,7).0(5,28)]triaconta-1(28),1(29),2,4,9,19,21,25,27-nonaen-13-yl acetate Rifapentine 3-(((4-Cyclopentyl-1-piperazinyl)imino)methyl)rifamycin Cyclopentylrifampicin Priftin (TN) rifapentine CAS:61379-65-5 ChemIDplus CHEBI:45409 An L-valine derivative that is an antiretroviral drug from the protease inhibitor class used to treat HIV infection and AIDS, it is often used as a fixed-dose combination with another protease inhibitor, lopinavir. Also used in combination with dasabuvir sodium hydrate, ombitasvir and paritaprevir (under the trade name Viekira Pak) for treatment of chronic hepatitis C virus genotype 1 infection as well as cirrhosis of the liver. C37H48N6O5S2 CC(C)[C@H](NC(=O)N(C)Cc1csc(n1)C(C)C)C(=O)N[C@H](C[C@H](O)[C@H](Cc1ccccc1)NC(=O)OCc1cncs1)Cc1ccccc1 CAS:155213-67-5 Drug_Central:2391 LINCS:LSM-5623 PMID:11363086 PMID:11363184 PMID:11363300 PMID:11363329 PMID:11363397 PMID:11363517 PMID:11996889 PMID:24202050 PMID:27993242 PMID:32505227 PMID:32690910 PMID:8568292 PMID:9140265 PMID:9278209 PMID:9585800 Reaxys:768009 N-[(2S,4S,5S)-4-hydroxy-1,6-diphenyl-5-{[(1,3-thiazol-5-ylmethoxy)carbonyl]amino}hexan-2-yl]-N(2)-(methyl{[2-(propan-2-yl)-1,3-thiazol-4-yl]methyl}carbamoyl)-L-valinamide ritonavir CAS:155213-67-5 ChemIDplus Drug_Central:2391 DrugCentral PMID:11363086 Europe PMC PMID:11363184 Europe PMC PMID:11363300 Europe PMC PMID:11363329 Europe PMC PMID:11363397 Europe PMC PMID:11363517 Europe PMC PMID:11996889 Europe PMC PMID:24202050 Europe PMC PMID:32505227 Nine existing HIV protease inhibitors (nelfinavir, lopinavir, ritonavir, saquinavir, atazanavir, tipranavir, amprenavir, darunavir, and indinavir) were evaluated for their antiviral activity in Vero cells infected with SARS-CoV-2 (Yamamoto et al., 2020), and nelfinavir was the most potent at inhibiting viral replication. PMID:32690910 Lopinavir–ritonavir is a fixed- dose drug combination used for the prevention and treatment of HIV infection and works by inhibiting protease activity. lopinavir–ritonavir should be used with caution in patients with COVID-19 because this drug combination might interact with common cardiovascular drugs that are metabolized by cytochrome P450 3A4, including antiarrhythmic agents, antiplatelet drugs and anticoagulants. PMID:8568292 Europe PMC PMID:9140265 Europe PMC PMID:9278209 Europe PMC PMID:9585800 Europe PMC Reaxys:768009 Reaxys CHEBI:45783 A benzamide obtained by formal condensation of the carboxy group of 4-[(4-methylpiperazin-1-yl)methyl]benzoic acid with the primary aromatic amino group of 4-methyl-N(3)-[4-(pyridin-3-yl)pyrimidin-2-yl]benzene-1,3-diamine. Used (as its mesylate salt) for treatment of chronic myelogenous leukemia and gastrointestinal stromal tumours. 0 C29H31N7O InChI=1S/C29H31N7O/c1-21-5-10-25(18-27(21)34-29-31-13-11-26(33-29)24-4-3-12-30-19-24)32-28(37)23-8-6-22(7-9-23)20-36-16-14-35(2)15-17-36/h3-13,18-19H,14-17,20H2,1-2H3,(H,32,37)(H,31,33,34) KTUFNOKKBVMGRW-UHFFFAOYSA-N 493.60270 493.25901 CN1CCN(Cc2ccc(cc2)C(=O)Nc2ccc(C)c(Nc3nccc(n3)-c3cccnc3)c2)CC1 Beilstein:7671333 CAS:152459-95-5 DrugBank:DB00619 Drug_Central:1423 HMDB:HMDB0014757 LINCS:LSM-1023 PDBeChem:STI PMID:14660054 PMID:14715630 PMID:15073101 PMID:15170967 PMID:15722647 PMID:15794712 PMID:15966213 PMID:16122278 PMID:16826359 PMID:16983347 PMID:17190842 PMID:17410337 PMID:17457302 PMID:17717205 PMID:18193246 PMID:18216472 PMID:18337118 PMID:18344535 PMID:18376233 PMID:18407734 PMID:18420270 PMID:18423008 PMID:18548219 PMID:18623899 PMID:18780518 PMID:18809244 PMID:19020005 PMID:19052981 PMID:19077095 PMID:19097599 PMID:19182535 PMID:19242505 PMID:19415889 PMID:19527930 PMID:19591692 PMID:19693287 PMID:19749465 PMID:19810774 PMID:19853594 PMID:19920908 PMID:22891806 PMID:23075630 PMID:23183914 PMID:23313020 PMID:23394269 PMID:23480638 PMID:23503753 PMID:23536338 PMID:23574742 PMID:23580311 PMID:23587588 Patent:EP564409 Patent:US5521184 Reaxys:7671333 Wikipedia:Imatinib 4-[(4-methylpiperazin-1-yl)methyl]-N-{4-methyl-3-[(4-pyridin-3-ylpyrimidin-2-yl)amino]phenyl}benzamide 4-(4-METHYL-PIPERAZIN-1-YLMETHYL)-N-[4-METHYL-3-(4-PYRIDIN-3-YL-PYRIMIDIN-2-YLAMINO)-PHENYL]-BENZAMIDE STI 571 alpha-(4-methyl-1-piperazinyl)-3'-((4-(3-pyridyl)-2-pyrimidinyl)amino)-p-toluidide imatinib imatinib Beilstein:7671333 Beilstein CAS:152459-95-5 ChemIDplus Drug_Central:1423 DrugCentral PMID:14660054 Europe PMC PMID:14715630 Europe PMC PMID:15073101 Europe PMC PMID:15170967 Europe PMC PMID:15722647 Europe PMC PMID:15794712 Europe PMC PMID:15966213 Europe PMC PMID:16122278 Europe PMC PMID:16826359 Europe PMC PMID:16983347 Europe PMC PMID:17190842 Europe PMC PMID:17410337 Europe PMC PMID:17457302 Europe PMC PMID:17717205 Europe PMC PMID:18193246 Europe PMC PMID:18216472 Europe PMC PMID:18337118 Europe PMC PMID:18344535 Europe PMC PMID:18376233 Europe PMC PMID:18407734 Europe PMC PMID:18420270 Europe PMC PMID:18423008 Europe PMC PMID:18548219 Europe PMC PMID:18623899 Europe PMC PMID:18780518 Europe PMC PMID:18809244 Europe PMC PMID:19020005 Europe PMC PMID:19052981 Europe PMC PMID:19077095 Europe PMC PMID:19097599 Europe PMC PMID:19182535 Europe PMC PMID:19242505 Europe PMC PMID:19415889 Europe PMC PMID:19527930 Europe PMC PMID:19591692 Europe PMC PMID:19693287 Europe PMC PMID:19749465 Europe PMC PMID:19810774 Europe PMC PMID:19853594 Europe PMC PMID:19920908 Europe PMC PMID:22891806 Europe PMC PMID:23075630 Europe PMC PMID:23183914 Europe PMC PMID:23313020 Europe PMC PMID:23394269 Europe PMC PMID:23480638 Europe PMC PMID:23503753 Europe PMC PMID:23536338 Europe PMC PMID:23574742 Europe PMC PMID:23580311 Europe PMC PMID:23587588 Europe PMC Reaxys:7671333 Reaxys CHEBI:45979 A member of the class of benzimidazoles carrying a 1,3-thiazol-4-yl substituent at position 2. A mainly post-harvest fungicide used to control a wide range of diseases including Aspergillus, Botrytis, Cladosporium and Fusarium. Beilstein:611403 CAS:148-79-8 DrugBank:DB00730 Drug_Central:2621 LINCS:LSM-3741 PMID:11226373 PMID:13900465 PMID:23790859 PMID:9009055 Pesticides:thiabendazole Reaxys:611403 2-(1,3-thiazol-4-yl)-1H-benzimidazole Thiabendazole 2-(1,3-THIAZOL-4-YL)-1H-BENZIMIDAZOLE 2-(1,3-thiazol-4-yl)benzimidazole 2-(4-thiazolyl)-1H-benzimidazole 2-(thiazol-4-yl)benzimidazole 4-(2-benzimidazolyl)thiazole Equizole MK 360 Mintezol TBZ Thibenzole Tiabendazole thiabendazole Beilstein:611403 Beilstein CAS:148-79-8 ChemIDplus CAS:148-79-8 NIST Chemistry WebBook Drug_Central:2621 DrugCentral PMID:11226373 Europe PMC PMID:13900465 Europe PMC PMID:23790859 Europe PMC PMID:9009055 Europe PMC Pesticides:thiabendazole Alan Wood's Pesticides Reaxys:611403 Reaxys CHEBI:45980 A member of the class of acridines that is 1,2,3,4-tetrahydroacridine substituted by an amino group at position 9. It is used in the treatment of Alzheimer's disease. C13H14N2 Nc1c2CCCCc2nc2ccccc12 CAS:321-64-2 DrugBank:DB00382 Wikipedia:Tacrine 1,2,3,4-tetrahydroacridin-9-amine tacrine CHEBI:46081 A member of the class of triazoles that is propan-2-ol substituted at position 1 and 3 by 1H-1,2,4-triazol-1-yl groups and at position 2 by a 2,4-difluorophenyl group. It is an antifungal drug used for the treatment of mucosal candidiasis and for systemic infections including systemic candidiasis, coccidioidomycosis, and cryptococcosis. Beilstein:4269710 CAS:86386-73-4 DrugBank:DB00196 Drug_Central:1187 LINCS:LSM-2106 PMID:11366931 PMID:16822276 PMID:23171950 PMID:23793863 Reaxys:7311650 2-(2,4-difluorophenyl)-1,3-bis-(1H-1,2,4-triazol-1-yl)propan-2-ol fluconazole 2,4-difluoro-alpha,alpha-bis(1H-1,2,4-triazol-1-ylmethyl)benzyl alcohol 2-(2,4-DIFLUOROPHENYL)-1,3-DI(1H-1,2,4-TRIAZOL-1-YL)PROPAN-2-OL Biozole Diflucan Elazor Triflucan fluconazol fluconazole fluconazolum fluconazole Beilstein:4269710 Beilstein CAS:86386-73-4 ChemIDplus Drug_Central:1187 DrugCentral PMID:11366931 Europe PMC PMID:16822276 Europe PMC PMID:23171950 Europe PMC PMID:23793863 Europe PMC Reaxys:7311650 Reaxys CHEBI:46195 A member of the class of phenols that is 4-aminophenol in which one of the hydrogens attached to the amino group has been replaced by an acetyl group. C8H9NO2 CC(=O)Nc1ccc(O)cc1 CAS:103-90-2 DrugBank:DB00316 Wikipedia:Acetaminophen Wikipedia:Paracetamol N-(4-hydroxyphenyl)acetamide APAP Acetaminophen paracetamol CHEBI:4659 An organic disulfide that results from the formal oxidative dimerisation of N,N-diethyldithiocarbamic acid. A multi-enzyme inhibitor that is used in alcohol aversion therapy and also exhibits anticancer properties. An organic disulfide that results from the formal oxidative dimerisation of N,N-diethyldithiocarbamic acid. A multi-enzyme inhibitor that is used in alcohol aversion therapy and also exhibits anticancer properties. C10H20N2S4 S(SC(N(CC)CC)=S)C(N(CC)CC)=S CAS:97-77-8 DrugBank:DB00822 Drug_Central:928 LINCS:LSM-5467 PMID:10841824 PMID:11005259 PMID:11716515 PMID:14978246 PMID:15325261 PMID:15709459 PMID:16426571 PMID:16661923 PMID:16666414 PMID:16880974 PMID:17079463 PMID:17579916 PMID:17667894 PMID:18579431 PMID:19720750 PMID:19782464 PMID:19787200 PMID:21471244 PMID:24496638 PMID:25133664 PMID:25445071 PMID:25464072 PMID:25476326 PMID:25495604 PMID:25557293 PMID:25565438 PMID:25657800 PMID:25777347 PMID:26033731 PMID:26224731 PMID:26235918 PMID:26239994 PMID:26314552 PMID:26517513 PMID:26550292 PMID:8442800 PMID:8572926 Reaxys:1712560 Wikipedia:Disulfiram 1,1',1'',1'''-[disulfanediylbis(carbonothioylnitrilo)]tetraethane Disulfiram 1,1'-dithiobis(N,N-diethylthioformamide) Antabuse N,N,N',N'-tetraethylthiuram disulfide Tetraethylthiuram disulfide bis(diethylthiocarbamoyl) disulfide tetraethylthioperoxydicarbonic diamide tetraethylthiuram disulfide tetraethylthiuram disulphide disulfiram CAS:97-77-8 ChemIDplus CAS:97-77-8 NIST Chemistry WebBook Drug_Central:928 DrugCentral PMID:10841824 Europe PMC PMID:11005259 Europe PMC PMID:11716515 Europe PMC PMID:14978246 Europe PMC PMID:15325261 Europe PMC PMID:15709459 Europe PMC PMID:16426571 Europe PMC PMID:16661923 Europe PMC PMID:16666414 Europe PMC PMID:16880974 Europe PMC PMID:17079463 Europe PMC PMID:17579916 Europe PMC PMID:17667894 Europe PMC PMID:18579431 Europe PMC PMID:19720750 Europe PMC PMID:19782464 Europe PMC PMID:19787200 Europe PMC PMID:21471244 Europe PMC PMID:24496638 Europe PMC PMID:25133664 Europe PMC PMID:25445071 Europe PMC PMID:25464072 Europe PMC PMID:25476326 Europe PMC PMID:25495604 Europe PMC PMID:25557293 Europe PMC PMID:25565438 Europe PMC PMID:25657800 Europe PMC PMID:25777347 Europe PMC PMID:26033731 Europe PMC PMID:26224731 Europe PMC PMID:26235918 Europe PMC PMID:26239994 Europe PMC PMID:26314552 Europe PMC PMID:26517513 Europe PMC PMID:26550292 Europe PMC PMID:8442800 Europe PMC PMID:8572926 Europe PMC Reaxys:1712560 Reaxys CHEBI:46787 A liquid that can dissolve other substances (solutes) without any change in their chemical composition. Wikipedia:Solvent solvent CHEBI:4705 double-stranded DNA double-stranded DNA CHEBI:47381 A monocarboxylic acid consisting of phenylacetic acid having a (2,6-dichlorophenyl)amino group at the 2-position. C14H11Cl2NO2 C1(Cl)=CC=CC(=C1NC2=CC=CC=C2CC(=O)O)Cl ATC:D11AX18 ATC:M01AB05 ATC:M02AA15 ATC:S01BC03 Beilstein:2146636 CAS:15307-86-5 DrugBank:DB00586 Drug_Central:865 LINCS:LSM-2160 PMID:11322639 PMID:1502708 PMID:23777257 PMID:27967303 PMID:7838674 Reaxys:2146636 Wikipedia:Diclofenac 2-[(2,6-dichlorophenyl)amino]benzeneacetic acid Diclofenac {2-[(2,6-dichlorophenyl)amino]phenyl}acetic acid 2-((2,6-dichlorophenyl)amino)benzeneacetic acid [2-(2,6-dichloroanilino)phenyl]acetic acid diclofenac diclofenac acid diclofenaco diclofenacum diclofenamic acid diclofenac Beilstein:2146636 Beilstein CAS:15307-86-5 ChemIDplus CAS:15307-86-5 NIST Chemistry WebBook Drug_Central:865 DrugCentral PMID:11322639 Europe PMC PMID:1502708 Europe PMC PMID:23777257 Europe PMC PMID:27967303 Europe PMC PMID:7838674 Europe PMC Reaxys:2146636 Reaxys CHEBI:474180 A semisynthetic cyclic hexapeptide echinocandin antibiotic which exerts its effect by inhibiting the synthesis of 1,3-beta-D-glucan, an integral component of the fungal cell wall. Beilstein:8471798 CAS:162808-62-0 DrugBank:DB00520 Drug_Central:2977 PMID:24270605 (10R,12S)-N-{(2R,6S,9S,11R,12S,14aS,15S,20S,23S,25aS)-12-[(2-aminoethyl)amino]-20-[(1R)-3-amino-1-hydroxypropyl]-23-[(1S,2S)-1,2-dihydroxy-2-(4-hydroxyphenyl)ethyl]-2,11,15-trihydroxy-6-[(1R)-1-hydroxyethyl]-5,8,14,19,22,25-hexaoxotetracosahydro-1H-dipyrrolo[2,1-c:2',1'-l][1,4,7,10,13,16]hexaazacyclohenicosin-9-yl}-10,12-dimethyltetradecanamide Caspofungin (4R,5S)-5-((2-aminoethyl)amino)-N(2)-(10,12-dimethyltetradecanoyl)-4-hydroxy-L-ornithyl-L-threonyl-trans-4-hydroxy-L-prolyl-(S)-4-hydroxy-4-(p-hydroxyphenyl)-L-threonyl-threo-3-hydroxy-L-ornithyl-trans-3-hydroxy-L-proline cyclic (6-1)-peptide 1-[(4R,5S)-5-[(2-aminoethyl)amino]-N(2)-(10,12-dimethyl-1-oxotetradecyl)-4-hydroxy-L-ornithine]-5-[(3R)-3-hydroxy-L-ornithine]-pneumocandin B0 caspofungin caspofungin Beilstein:8471798 Beilstein CAS:162808-62-0 ChemIDplus Drug_Central:2977 DrugCentral PMID:24270605 Europe PMC CHEBI:47499 Imipramine is a tricyclic antidepressant that continues to be widely used in the therapy of depression. Imipramine can cause mild and transient serum enzyme elevations and is rare cause of clinically apparent acute cholestatic liver injury. C19H24N2 CN(C)CCCN1c2ccccc2CCc2ccccc12 DrugBank:DB00458 Open TG-Gates compound_id:00069 Wikipedia:Imipramine https://livertox.nlm.nih.gov//Imipramine.htm imipramine CHEBI:47519 A racemate consisting of equimolar amounts of (2R,4S)- and (2S,4R)-ketoconazole. Beilstein:4303081 CAS:65277-42-1 DrugBank:DB01026 Gmelin:1713206 Open TG-Gates compound_id=00047 rac-1-acetyl-4-(4-{[(2R,4S)-2-(2,4-dichlorophenyl)-2-(1H-imidazol-1-ylmethyl)-1,3-dioxolan-4-yl]methoxy}phenyl)piperazine (+-)-cis-1-acetyl-4-(p-((2-(2,4-dichlorophenyl)-2-(imidazol-1-ylmethyl)-1,3-dioxolan-4-yl)methoxy)phenyl)piperazine Fungarest Fungoral Ketoderm Ketoisdin Nizoral Panfungol Xolegel cis-1-acetyl-4-(4-((2-(2,4-dichlorophenyl)-2-(1H-imidazol-1-ylmethyl)-1,3-dioxolan-4-yl)methoxy)phenyl)piperazine ketoconazol ketoconazole ketoconazolum ketoconazole Beilstein:4303081 ChemIDplus CAS:65277-42-1 ChemIDplus Gmelin:1713206 Gmelin CHEBI:47780 A dibenzoazepine that is 10,11-dihydro-5H-dibenzo[b,f]azepine which is substituted by chlorine at position 3 and in which the hydrogen attached to the nitrogen is replaced by a 3-(dimethylamino)propyl group. One of the more sedating tricyclic antidepressants, it is used as the hydrochloride salt for the treatment of depression as well as obsessive-compulsive disorder and phobias. C19H23ClN2 Beilstein:1323477 CAS:303-49-1 CN(C)CCCN1c2ccccc2CCc2ccc(Cl)cc12 DrugBank:DB01242 Drug_Central:701 LINCS:LSM-3171 Open TG-Gates compound_id:00121 PMID:12007764 PMID:12084414 PMID:16085036 PMID:17471183 PMID:19747949 PMID:19810911 Patent:US3467650 Reaxys:1323477 3-(3-chloro-10,11-dihydro-5H-dibenzo[b,f]azepin-5-yl)-N,N-dimethylpropan-1-amine Clomipramine 3-(3-CHLORO-5H-DIBENZO[B,F]AZEPIN-5-YL)-N,N-DIMETHYLPROPAN-1-AMINE 3-(3-chloro-10,11-dihydro-5H-dibenzo[b,f]azepin-5-yl)-N,N-dimethyl-1-propanamine 3-chloroimipramine G 34586 chlorimipramine monochlorimipramine clomipramine Beilstein:1323477 ChemIDplus CAS:303-49-1 ChemIDplus CAS:303-49-1 NIST Chemistry WebBook Drug_Central:701 DrugCentral PMID:12007764 Europe PMC PMID:12084414 Europe PMC PMID:16085036 Europe PMC PMID:17471183 Europe PMC PMID:19747949 Europe PMC PMID:19810911 Europe PMC Reaxys:1323477 Reaxys CHEBI:47868 A chemical compound that can be excited by light of a specific wavelength and subsequently transfer energy to a chosen reactant. This is commonly molecular oxygen within a cancer tissue, which is converted to (highly rective) singlet state oxygen. This rapidly reacts with any nearby biomolecules, ultimately killing the cancer cells. photosensitising agent photosensitizing agent CHEBI:48001 A compound, usually an anti-bacterial agent or a toxin, which inhibits the synthesis of a protein. protein synthesis antagonist protein synthesis antagonists protein synthesis inhibitors protein synthesis inhibitor CHEBI:48278 serotonergic agents serotonergic drugs serotonin drugs serotonergic drug CHEBI:48279 Drugs that bind to but do not activate serotonin receptors, thereby blocking the actions of serotonin or serotonergic agonists. 5-HT antagonists 5-hydroxytryptamine antagonists antiserotonergic agents serotonin antagonists serotonin blockaders serotonergic antagonist CHEBI:48406 An EC 2.1.1.* (methyltransferase) inhibitor that interferes with the action of catechol O-methyltransferase (EC 2.1.1.6). COMT inhibitor COMT inhibitors EC 2.1.1.6 (catechol O-methyltransferase) inhibitors EC 2.1.1.6 inhibitor EC 2.1.1.6 inhibitors S-adenosyl-L-methionine:catechol O-methyltransferase inhibitor S-adenosyl-L-methionine:catechol O-methyltransferase inhibitors catechol O-methyltransferase (EC 2.1.1.6) inhibitor catechol O-methyltransferase (EC 2.1.1.6) inhibitors catechol O-methyltransferase inhibitor catechol O-methyltransferase inhibitors catechol methyltransferase inhibitor catechol methyltransferase inhibitors catecholamine O-methyltransferase inhibitor catecholamine O-methyltransferase inhibitors EC 2.1.1.6 (catechol O-methyltransferase) inhibitor CHEBI:48407 A drug used in the treatment of Parkinson's disease. Wikipedia:Antiparkinson antiparkinson agent antiparkinson drug CHEBI:48422 An agent and endogenous substances that antagonize or inhibit the development of new blood vessels. angiogenesis antagonist angiostatic agents anti-angiogenic agent angiogenesis inhibitor CHEBI:4846 C40H71NO14.C12H26O4S CCCCCCCCCCCCOS(O)(=O)=O.CC[C@H]1OC(=O)[C@H](C)[C@@H](O[C@H]2C[C@@](C)(OC)[C@@H](O)[C@H](C)O2)[C@H](C)[C@@H](O[C@@H]2O[C@H](C)C[C@@H]([C@H]2OC(=O)CC)N(C)C)[C@](C)(O)C[C@@H](C)C(=O)[C@H](C)[C@@H](O)[C@]1(C)O erythromycin estolate CHEBI:48539 Any drug that acts on an alpha-adrenergic receptor. alpha-adrenergic drugs alpha-adrenergic drug CHEBI:48540 Any of the drugs that act on beta-adrenergic receptors. beta-adrenergic drugs beta-adrenergic drug CHEBI:48549 Beilstein:4208277 CAS:82964-04-3 DrugBank:DB02383 Drug_Central:2704 N-{[6-methoxy-5-(trifluoromethyl)naphthalen-1-yl]carbonothioyl}-N-methylglycine TOLRESTAT Tolrestat Alredase N-((6-methoxy-5-(trifluoromethyl)-1-naphthalenyl)thioxomethyl)-N-methylglycine N-{[6-methoxy-5-(trifluoromethyl)-1-naphthyl]carbonothioyl}-N-methylglycine tolrestat tolrestatum tolrestat Beilstein:4208277 Beilstein CAS:82964-04-3 ChemIDplus Drug_Central:2704 DrugCentral CHEBI:48550 An EC 1.1.1.* (oxidoreductase acting on donor CH-OH group, NAD(+) or NADP(+) acceptor) inhibitor that interferes with the action of aldehyde reductase (EC 1.1.1.21). ALR2 inhibitor ALR2 inhibitors EC 1.1.1.21 (aldehyde reductase) inhibitors EC 1.1.1.21 inhibitor EC 1.1.1.21 inhibitors NADPH-aldopentose reductase inhibitor NADPH-aldopentose reductase inhibitors NADPH-aldose reductase inhibitor NADPH-aldose reductase inhibitors aldehyde reductase (EC 1.1.1.21) inhibitor aldehyde reductase (EC 1.1.1.21) inhibitors aldehyde reductase inhibitor aldehyde reductase inhibitors alditol:NAD(P)(+) 1-oxidoreductase inhibitor alditol:NAD(P)(+) 1-oxidoreductase inhibitors alditol:NADP oxidoreductase inhibitor alditol:NADP oxidoreductase inhibitors alditol:NADP(+) 1-oxidoreductase inhibitor alditol:NADP(+) 1-oxidoreductase inhibitors aldose reductase inhibitor aldose reductase inhibitors polyol dehydrogenase (NADP(+)) inhibitor polyol dehydrogenase (NADP(+)) inhibitors EC 1.1.1.21 (aldehyde reductase) inhibitor CHEBI:48560 A drug used for its effects on dopamine receptors, on the life cycle of dopamine, or on the survival of dopaminergic neurons. dopamine agent dopamine agents dopamine drug dopamine drugs dopaminergic agents dopaminergic agent CHEBI:48561 A drug that binds to but does not activate dopamine receptors, thereby blocking the actions of dopamine or exogenous agonists. dopamine antagonist dopamine blocker dopamine receptor antagonist dopaminergic antagonists dopaminergic antagonist CHEBI:48578 A role played by a substance that can react readily with, and thereby eliminate, radicals. free radical scavenger free radical scavengers free-radical scavenger radical scavenger CHEBI:48676 A drug that affects the function of fibrin in blood coagulation. fibrin modulating agent fibrin modulating agents fibrin modulating drugs fibrin modulating drug CHEBI:4868 A carbamate ester obtained by the formal condensation of the hydroxy group of 17beta-estradiol with the carboxy group of bis(2-chloroethyl)carbamic acid. Beilstein:5637599 CAS:2998-57-4 DrugBank:DB01196 Drug_Central:1065 LIPID_MAPS_instance:LMST02010038 PMID:11131983 PMID:15762353 PMID:7638085 Reaxys:5637599 (17beta)-17-hydroxyestra-1(10),2,4-trien-3-yl bis(2-chloroethyl)carbamate Estramustine 17beta-Estradiol 3-(bis(2-chloroethyl)carbamate) Estradiol 3-(N,N-bis(2-chloroethyl)carbamate) estramustina estramustine estramustinum estramustine Beilstein:5637599 Beilstein CAS:2998-57-4 ChemIDplus Drug_Central:1065 DrugCentral LIPID_MAPS_instance:LMST02010038 LIPID MAPS PMID:11131983 Europe PMC PMID:15762353 Europe PMC PMID:7638085 Europe PMC Reaxys:5637599 Reaxys CHEBI:48705 Substance which binds to cell receptors normally responding to naturally occurring substances and which produces a response of its own. agonist agonista agoniste agonists agonist CHEBI:48706 Substance that attaches to and blocks cell receptors that normally bind naturally occurring substances. antagonist antagonista antagoniste antagonists antagonist CHEBI:48720 A synthetic derivative of L-arginine with antithrombotic activity. Argatroban is a univalent and direct inhibitor of fibrin-bound thrombin. This agent reversibly binds to the thrombin active site thereby preventing the thrombin-dependent reactions, which include conversion of fibrinogen to fibrin; the activation of factors V, VIII and XI; the activation of protein C; and platelet aggregation. Argatroban is highly selective for thrombin and is able to inhibit the action of both free and clot-associated thrombin. As a result, stabilization of blood clots and coagulation is inhibited. (https://www.ebi.ac.uk/ols/ontologies/ncit/terms?iri=http%3A%2F%2Fpurl.obolibrary.org%2Fobo%2FNCIT_C28833) PMID:33332362 argatroban PMID:33332362 All hospitalized patients received pharmacological antithrombotic prophylaxis or therapy in contrast to none of the outpatients. As antithrombotic drug, UFH was administered in all but 2 patients (6%) who received LMWH. 2 (6%) patients were switched from UFH to argatroban when a heparin-induced thrombocytopenia was suspected CHEBI:4877 An ethylenediamine derivative that is ethane-1,2-diamine in which one hydrogen attached to each of the nitrogens is sutstituted by a 1-hydroxybutan-2-yl group (S,S-configuration). It is a bacteriostatic antimycobacterial drug, effective against Mycobacterium tuberculosis and some other mycobacteria. It is used (as the dihydrochloride salt) in combination with other antituberculous drugs in the treatment of pulmonary and extrapulmonary tuberculosis; resistant strains of M. tuberculosis are readily produced if ethambutol is used alone. Beilstein:6312870 CAS:74-55-5 DrugBank:DB00330 Drug_Central:1073 PMID:10649975 PMID:10891117 PMID:10966749 PMID:12182855 PMID:14695841 PMID:14698152 PMID:15225698 PMID:16005211 PMID:16759086 PMID:16870429 PMID:17210775 PMID:17239593 PMID:17276683 PMID:17315960 PMID:17331717 PMID:17562368 PMID:17851083 PMID:17888665 PMID:19524332 PMID:19648006 PMID:3934384 Reaxys:6312870 (2S,2'S)-2,2'-(ethane-1,2-diyldiimino)dibutan-1-ol Ethambutol (+)-2,2'-(ethylenediimino)di-1-butanol (+)-N,N'-bis(1-(hydroxymethyl)propyl)ethylenediamine (+)-S,S-ethambutol (+)-ethambutol (2S,7S)-2,7-diethyl-3,6-diazaoctane-1,8-diol (S,S)-ethambutol EMB S,S-Ethambutol etambutol ethambutol ethambutolum ethambutol Beilstein:6312870 Beilstein CAS:74-55-5 ChemIDplus Drug_Central:1073 DrugCentral PMID:10649975 ChEMBL PMID:10891117 ChEMBL PMID:10966749 ChEMBL PMID:12182855 ChEMBL PMID:14695841 ChEMBL PMID:14698152 ChEMBL PMID:15225698 ChEMBL PMID:16005211 ChEMBL PMID:16759086 ChEMBL PMID:16870429 ChEMBL PMID:17210775 ChEMBL PMID:17239593 ChEMBL PMID:17276683 ChEMBL PMID:17315960 ChEMBL PMID:17331717 ChEMBL PMID:17562368 ChEMBL PMID:17851083 ChEMBL PMID:17888665 ChEMBL PMID:19524332 ChEMBL PMID:19648006 ChEMBL PMID:3934384 ChEMBL Reaxys:6312870 Reaxys CHEBI:4885 A thiocarboxamide that is pyridine-4-carbothioamide substituted by an ethyl group at position 2. A prodrug that undergoes metabolic activation by conversion to the corresponding S-oxide. C8H10N2S CCc1cc(ccn1)C(N)=S CAS:536-33-4 DrugBank:DB00609 Wikipedia:Ethionamide 2-ethylpyridine-4-carbothioamide ethionamide CHEBI:48873 Any drug that binds to but does not activate cholinergic receptors, thereby blocking the actions of acetylcholine or cholinergic agonists. Anticholinergika Anticholinergikum acetylcholine antagonists acetylcholine receptor antagonist agent anticholinergique agente anticolinergico agentes anticolinergicos anticholinergic agents anticholinergics anticholinergiques anticolinergicos cholinergic-blocking agents cholinergic antagonist CHEBI:48876 A drug that binds to but does not activate muscarinic cholinergic receptors, thereby blocking the actions of endogenous acetylcholine or exogenous agonists. Antimuskarinika Antimuskarinikum agente antimuscarinico agentes antimuscarinicos agents antimuscariniques antimuscarinic agents antimuscarinicos muscarinic acetylcholine receptor antagonist muscarinic antagonists muscarinic antagonist CHEBI:48887 Metabolites of bile acids, four-ringed steroid acids formed along the cholesterol degradation pathway. bile acid metabolite CHEBI:48923 Any of several wide-spectrum macrolide antibiotics obtained from actinomycete Saccharopolyspora erythraea (formerly known as Streptomyces erythraeus). DrugBank:DB00199 eritromicina erthromycin erythromycine erythromycin CHEBI:49 C38H42N2O6 InChI=1S/C38H42N2O6/c1-39-15-13-25-20-32(42-4)34-22-28(25)29(39)17-23-7-10-27(11-8-23)45-33-19-24(9-12-31(33)41-3)18-30-36-26(14-16-40(30)2)21-35(43-5)37(44-6)38(36)46-34/h7-12,19-22,29-30H,13-18H2,1-6H3/t29-,30-/m0/s1 WVTKBKWTSCPRNU-KYJUHHDHSA-N COc1ccc2C[C@@H]3N(C)CCc4cc(OC)c(OC)c(Oc5cc6[C@H](Cc7ccc(Oc1c2)cc7)N(C)CCc6cc5OC)c34 CAS:518-34-3 PMID:32221306 tetrandrine (+)-Tetrandrine PMID:32221306 While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect (Supplementary Fig. 1), indicating that TPC2, not TRPML1, is important for SARS-CoV-2 entry. CHEBI:49005 A member of the class of triazoles, deferasirox is 1,2,4-triazole substituted by a 4-carboxyphenyl group at position 1 and by 2-hydroxyphenyl groups at positions 3 and 5. An orally active iron chelator, it is used to manage chronic iron overload in patients receiving long-term blood transfusions. Beilstein:8442898 CAS:201530-41-8 DrugBank:DB01609 Drug_Central:3128 Reaxys:8442898 4-[3,5-bis(2-hydroxyphenyl)-1H-1,2,4-triazol-1-yl]benzoic acid Exjade ICL 670 ICL 670A deferasirox deferasiroxum deferasirox Beilstein:8442898 Beilstein CAS:201530-41-8 ChemIDplus Drug_Central:3128 DrugCentral Reaxys:8442898 Reaxys CHEBI:49020 A chemical substance which inhibits the function of the endocrine glands, the biosynthesis of their secreted hormones, or the action of hormones upon their specific sites. hormone antagonists hormone antagonist CHEBI:490877 A purine 2',3'-dideoxyribonucleoside that is inosine in which the hydroxy groups at both the 2' and the 3' positions on the sugar moiety have been replaced by hydrogen. An antiviral drug, it is used as a medication to treat HIV/AIDS. C10H12N4O3 OC[C@@H]1CC[C@@H](O1)n1cnc2c1nc[nH]c2=O Beilstein:3619529 CAS:69655-05-6 DrugBank:DB00900 Drug_Central:869 LINCS:LSM-6017 PMID:10386939 PMID:1619614 PMID:17046264 PMID:18549801 PMID:29438107 Reaxys:3619529 Wikipedia:Didanosine 2',3'-dideoxyinosine Didanosine ddI 2,3-dideoxyinosine 9-((2R,5S)-5-(hydroxymethyl)-tetrahydrofuran-2-yl)-1H-purin-6(9H)-one 9-((2R,5S)-5-Hydroxymethyl-tetrahydro-furan-2-yl)-1,9-dihydro-purin-6-one 9-((2S,5R)-5-Hydroxymethyl-tetrahydro-furan-2-yl)-9H-purin-6-ol 9-[(2R,5S)-5-(hydroxymethyl)tetrahydrofuran-2-yl]-1,9-dihydro-6H-purin-6-one DDI ddI ddIno didanosina didanosine didanosinum dideoxyinosine didanosine Beilstein:3619529 Beilstein CAS:69655-05-6 ChemIDplus Drug_Central:869 DrugCentral PMID:10386939 ChEMBL PMID:1619614 ChEMBL PMID:17046264 ChEMBL PMID:18549801 Europe PMC PMID:29438107 Europe PMC Reaxys:3619529 Reaxys CHEBI:4909 A monocarboxylic acid that is acetic acid in which one of the methyl hydrogens is substituted by a 1,8-diethyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl moiety. A preferential inhibitor of cyclo-oxygenase 2 and non-steroidal anti-inflammatory, it is used for the treatment of rheumatoid arthritis and osteoarthritis, and for the alleviation of postoperative pain. Administered as the racemate, only the (S)-enantiomer is active. CAS:41340-25-4 DrugBank:DB00749 Drug_Central:1103 LINCS:LSM-1781 PMID:15369391 PMID:2527995 PMID:28166217 PMID:2970548 (1,8-diethyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl)acetic acid ETODOLAC (+-)-1,8-diethyl-1,3,4,9-tetrahydropyrano(3,4-b)indole-1-acetic acid (1,8-Diethyl-1,3,4,9-tetrahydro-pyrano[3,4-b]indol-1-yl)-acetic acid 1,3,4,9-tetrahydro-1,8-diethylpyrano(3,4-b)indole-1-acetic acid 1,8-diethyl-1,3,4,9-tetrahydropyrano(3,4-b)indole-1-acetic acid 1,8-diethyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-ylacetic acid ETODOLIC ACID etodolac etodolaco etodolacum etodolac CAS:41340-25-4 ChemIDplus Drug_Central:1103 DrugCentral PMID:15369391 ChEMBL PMID:2527995 ChEMBL PMID:28166217 Europe PMC PMID:2970548 ChEMBL CHEBI:49103 Any human metabolite produced by metabolism of drugs in humans. drug metabolites drug metabolite CHEBI:49159 A drug designed to prevent leukotriene synthesis or activity by blocking binding at the receptor level. LTRA leukotriene antagonists leukotriene receptor antagonist leukotriene receptor antagonists leukotriene antagonist CHEBI:49167 A drug used to treat asthma. anti-asthmatic agent anti-asthmatic agents anti-asthmatic drugs anti-asthmatic drug CHEBI:49201 One of various classes of drugs with different action mechanisms used to treat or ameliorate peptic ulcer or irritation of the gastrointestinal tract. anti-ulcer agent anti-ulcer drug CHEBI:49323 A chemical substance that prevents or reduces the probability of conception. contraceptive agent contraceptive drugs contraceptive drug CHEBI:49324 A chemical substance or agent with contraceptive activity in females. female contraceptive agent female contraceptive drugs female contraceptive drug CHEBI:4953 A 17-oxo steroid that is androsta-1,4-diene-3,17-dione in which the hydrogens at position 6 are replaced by a double bond to a methylene group. A selective inhibitor of the aromatase (oestrogen synthase) system, it is used in the treatment of advanced breast cancer. CAS:107868-30-4 DrugBank:DB00990 Drug_Central:1122 PMID:10882163 Reaxys:6609645 6-methylideneandrosta-1,4-diene-3,17-dione Exemestane 6-methyleneandrosta-1,4-diene-3,17-dione exemestane exemestano exemestanum exemestane CAS:107868-30-4 ChemIDplus Drug_Central:1122 DrugCentral PMID:10882163 Europe PMC Reaxys:6609645 Reaxys CHEBI:49603 Beilstein:10502247 CAS:231277-92-2 DrugBank:DB01259 Drug_Central:1548 LINCS:LSM-1051 N-[3-chloro-4-(3-fluorobenzyloxy)phenyl]-6-[5-({[2-(methanesulfonyl)ethyl]amino}methyl)furan-2-yl]quinazolin-4-amine GW 572016 N-(3-chloro-4-((3-fluorophenyl)methoxy)phenyl)-6-(5-(((2-(methylsulfonyl)ethyl)amino)methyl)-2-furanyl)-4-quinazolinamine N-{3-CHLORO-4-[(3-FLUOROBENZYL)OXY]PHENYL}-6-[5-({[2-(METHYLSULFONYL)ETHYL]AMINO}METHYL)-2-FURYL]-4-QUINAZOLINAMINE Tykerb lapatinib Beilstein:10502247 Beilstein CAS:231277-92-2 ChemIDplus Drug_Central:1548 DrugCentral CHEBI:49637 Inchikey:YZCKVEUIGOORGS-UHFFFAOYSA-N hydrogen hydrogen atom CHEBI:49668 A member of the class of quinazolines that is quinazoline which is substituted by a (3-chloro-4-fluorophenyl)nitrilo group, 3-(morpholin-4-yl)propoxy group and a methoxy group at positions 4,6 and 7, respectively. An EGFR kinase inhibitor used for the treatment of non-small cell lung cancer. CAS:184475-35-2 DrugBank:DB00317 Drug_Central:1282 LINCS:LSM-1098 PMID:14981586 PMID:15068398 PMID:20573926 PMID:20949670 PMID:27396387 PMID:28968167 PMID:29332330 PMID:29493460 PMID:29579334 PMID:29668619 PMID:30068310 PMID:30069771 PMID:30214852 Reaxys:8949523 N-(3-chloro-4-fluorophenyl)-7-methoxy-6-(3-morpholin-4-ylpropoxy)quinazolin-4-amine 4-(3'-chloro-4'-fluoroanilino)-7-methoxy-6-(3-morpholinopropoxy)quinazoline Iressa Irressat N-(3-chloro-4-fluorophenyl)-7-methoxy-6-(3-(4-morpholinyl)propoxy)-4-quinazolinamine ZD 1839 ZD-1839 ZD1839 gefitinib gefitinibum gefitinib CAS:184475-35-2 ChemIDplus Drug_Central:1282 DrugCentral PMID:14981586 Europe PMC PMID:15068398 Europe PMC PMID:20573926 Europe PMC PMID:20949670 Europe PMC PMID:27396387 Europe PMC PMID:28968167 Europe PMC PMID:29332330 Europe PMC PMID:29493460 Europe PMC PMID:29579334 Europe PMC PMID:29668619 Europe PMC PMID:30068310 Europe PMC PMID:30069771 Europe PMC PMID:30214852 Europe PMC Reaxys:8949523 Reaxys CHEBI:4995 The bis(carbamate ester) of 2-phenylpropane-1,3-diol. An anticonvulsant, it is used in the treatment of epilepsy. CAS:25451-15-4 DrugBank:DB00949 Drug_Central:1140 LINCS:LSM-4232 PMID:12825948 PMID:12873507 PMID:18311896 Reaxys:3345236 2-phenylpropane-1,3-diyl dicarbamate Felbamate 2-phenyl-1,3-propanediol dicarbamate Carbamic acid 3-carbamoyloxy-2-phenyl-propyl ester carbamic acid 2-phenyltrimethylene ester felbamate felbamato felbamatum felbamate CAS:25451-15-4 ChemIDplus CAS:25451-15-4 NIST Chemistry WebBook Drug_Central:1140 DrugCentral PMID:12825948 ChEMBL PMID:12873507 ChEMBL PMID:18311896 ChEMBL Reaxys:3345236 Reaxys CHEBI:5001 A chlorobenzophenone that is (4-chlorophenyl)(phenyl)methanone substituted by a [2-methyl-1-oxo-1-(propan-2-yloxy)propan-2-yl]oxy group at position 1 on the phenyl ring. CC(C)OC(=O)C(C)(C)Oc1ccc(cc1)C(=O)c1ccc(Cl)cc1 LINCS:LSM-3107 propan-2-yl 2-[4-(4-chlorobenzoyl)phenoxy]-2-methylpropanoate fenofibrate CHEBI:5004 A monocarboxylic acid that is propanoic acid in which one of the hydrogens at position 2 is substituted by a 3-phenoxyphenyl group. A non-steroidal anti-inflammatory drug, the dihydrate form of the calcium salt is used for the management of mild to moderate pain and for the relief of pain and inflammation associated with disorders such as arthritis. It is pharmacologically similar to aspirin, but causes less gastrointestinal bleeding. CAS:31879-05-7 DrugBank:DB00573 Drug_Central:1154 PMID:21328296 PMID:21342694 PMID:25554116 PMID:28166217 PMID:30168706 PMID:4616811 Reaxys:2118687 2-(3-phenoxyphenyl)propanoic acid FENOPROFEN Fenoprofen (+-)-2-(3-phenoxyphenyl)propionic acid (+-)-m-phenoxyhydratropic acid 2-(3-phenoxyphenyl)propionic acid 2-(m-phenoxyphenyl)propionic acid alpha-(m-phenoxyphenyl)propionic acid alpha-methyl-3-phenoxybenzeneacetic acid fenoprofen fenoprofene fenoprofeno fenoprofenum fenoprofen CAS:31879-05-7 ChemIDplus CAS:31879-05-7 NIST Chemistry WebBook Drug_Central:1154 DrugCentral PMID:21328296 Europe PMC PMID:21342694 Europe PMC PMID:25554116 Europe PMC PMID:28166217 Europe PMC PMID:30168706 Europe PMC PMID:4616811 Europe PMC Reaxys:2118687 Reaxys CHEBI:50112 Any hormone that is responsible for controlling sexual characteristics and reproductive function. Geschlechtshormon Geschlechtshormone Sexualhormon Sexualhormone hormone sexuelle hormones sexuelles sex hormones sex hormone CHEBI:50113 A sex hormone that stimulates or controls the development and maintenance of masculine characteristics in vertebrates by binding to androgen receptors. Androgen Androgene androgene androgenes androgeno androgenos androgens androgen CHEBI:50114 A hormone that stimulates or controls the development and maintenance of female sex characteristics in mammals by binding to oestrogen receptors. The oestrogens are named for their importance in the oestrous cycle. The oestrogens that occur naturally in the body, notably estrone, estradiol, estriol, and estetrol are steroids. Other compounds with oestrogenic activity are produced by plants (phytoestrogens) and fungi (mycoestrogens); synthetic compounds with oestrogenic activity are known as xenoestrogens. Wikipedia:Estrogen estrogen CHEBI:50122 CN(CCOc1ccc(CC2SC(=O)NC2=O)cc1)c1ccccn1 CAS:122320-73-4 DrugBank:DB00412 Wikipedia:Rosiglitazone 5-(4-{2-[methyl(pyridin-2-yl)amino]ethoxy}benzyl)-1,3-thiazolidine-2,4-dione LINCS:LSM-1949 rosiglitazone CHEBI:50172 A retinoid that consists of 3,7-dimethylnona-2,4,6,8-tetraenoic acid having a 4-methoxy-2,3,6-trimethylphenyl group attached at position 9. CAS:54757-46-9 LINCS:LSM-5713 Reaxys:15057225 9-(4-methoxy-2,3,6-trimethylphenyl)-3,7-dimethylnona-2,4,6,8-tetraenoic acid acitretin CAS:54757-46-9 ChemIDplus Reaxys:15057225 Reaxys CHEBI:50176 A drug that softens, separates, and causes desquamation of the cornified epithelium or horny layer of skin. Keratolytic drugs are used to expose mycelia of infecting fungi or to treat corns, warts, and certain other skin diseases. desquamating agent keratolytic agent keratolytic drugs skin-peeling agent keratolytic drug CHEBI:50177 A drug used to treat or prevent skin disorders or for the routine care of skin. dermatologic agent dermatologic drugs dermatological agent dermatologic drug CHEBI:50183 An enzyme inhibitor that interferes with the activity of cytochrome P450 involved in catalysis of organic substances. P450 inhibitors cytochrome P450 inhibitor cytochrome P450 inhibitors P450 inhibitor CHEBI:50184 A compound which inhibits the movement of an ion across an energy-transducing cell membrane. ion transport inhibitor CHEBI:50185 Any pathway inhibitor that inhibits the synthesis of fatty acids. fatty acid synthesis inhibitor CHEBI:50248 Drug that acts on blood and blood-forming organs and those that affect the hemostatic system. hematologic agents hematologic agent CHEBI:50249 An agent that prevents blood clotting. anticoagulante anticoagulants anticoagulant CHEBI:50266 A compound that, on administration, must undergo chemical conversion by metabolic processes before becoming the pharmacologically active drug for which it is a prodrug. PMID:23993918 PMID:23998799 PMID:24329110 PMID:24628402 PMID:24709544 PMID:25144792 PMID:25157234 PMID:25269430 PMID:25391982 PMID:25591121 PMID:25620096 PMID:25795057 PMID:26028253 PMID:26184144 PMID:28070577 PMID:28215138 PMID:28219047 PMID:28259775 PMID:28319647 PMID:28329729 PMID:28334528 Prodrugs prodrug PMID:23993918 Europe PMC PMID:23998799 Europe PMC PMID:24329110 Europe PMC PMID:24628402 Europe PMC PMID:24709544 Europe PMC PMID:25144792 Europe PMC PMID:25157234 Europe PMC PMID:25269430 Europe PMC PMID:25391982 Europe PMC PMID:25591121 Europe PMC PMID:25620096 Europe PMC PMID:25795057 Europe PMC PMID:26028253 Europe PMC PMID:26184144 Europe PMC PMID:28070577 Europe PMC PMID:28215138 Europe PMC PMID:28219047 Europe PMC PMID:28259775 Europe PMC PMID:28319647 Europe PMC PMID:28329729 Europe PMC PMID:28334528 Europe PMC CHEBI:50267 Synthetic or natural substance which is given to prevent a disease or disorder or are used in the process of treating a disease or injury due to a poisonous agent. chemoprotectant chemoprotectants chemoprotective agent chemoprotective agents protective agents protective agent CHEBI:50276 A topoisomerase inhibitor that inhibits the bacterial enzymes of the DNA topoisomerases, Type I class (EC 5.99.1.2) that catalyze ATP-independent breakage of one of the two strands of DNA, passage of the unbroken strand through the break, and rejoining of the broken strand. These bacterial enzymes reduce the topological stress in the DNA structure by relaxing negatively, but not positively, supercoiled DNA. DNA topoisomerase inhibitor DNA topoisomerase inhibitors EC 5.99.1.2 (DNA topoisomerase) inhibitors EC 5.99.1.2 (topoisomerase I) inhibitor EC 5.99.1.2 (topoisomerase I) inhibitors EC 5.99.1.2 inhibitor EC 5.99.1.2 inhibitors topoisomerase I (EC 5.99.1.2) inhibitor topoisomerase I (EC 5.99.1.2) inhibitors topoisomerase I inhibitor topoisomerase I inhibitors type I DNA topoisomerase inhibitor type I DNA topoisomerase inhibitors EC 5.99.1.2 (DNA topoisomerase) inhibitor CHEBI:50427 A drug or agent which antagonizes or impairs any mechanism leading to blood platelet aggregation, whether during the phases of activation and shape change or following the dense-granule release reaction and stimulation of the prostaglandin-thromboxane system. platelet aggregation inhibitors platelet aggregation inhibitor CHEBI:50469 An EC 3.1.1.* (carboxylic ester hydrolase) inhibitor that interferes with the action of phospholipase A2 (EC 3.1.1.4). EC 3.1.1.4 (phospholipase A2) inhibitor phospholipase A2 inhibitor CHEBI:50502 An EC 2.5.1.* (non-methyl-alkyl or aryl transferase) inhibitor that interferes with the action of dihydropteroate synthase (EC 2.5.1.15), an enzyme that catalyzes the formation of dihydropteroate from p-aminobenzoic acid and dihydropteridine-hydroxymethyl-pyrophosphate. (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase inhibitor (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase inhibitors 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase inhibitor 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase inhibitors 7,8-dihydropteroate synthase inhibitor 7,8-dihydropteroate synthase inhibitors 7,8-dihydropteroate synthetase inhibitor 7,8-dihydropteroate synthetase inhibitors 7,8-dihydropteroic acid synthetase inhibitor 7,8-dihydropteroic acid synthetase inhibitors DHPS inhibitor DHPS inhibitors EC 2.5.1.15 (dihydropteroate synthase) inhibitors EC 2.5.1.15 inhibitor EC 2.5.1.15 inhibitors dihydropteroate diphosphorylase inhibitor dihydropteroate diphosphorylase inhibitors dihydropteroate pyrophosphorylase inhibitor dihydropteroate pyrophosphorylase inhibitors dihydropteroate synthase (EC 2.5.1.15) inhibitor dihydropteroate synthase (EC 2.5.1.15) inhibitors dihydropteroate synthase inhibitor dihydropteroate synthase inhibitors dihydropteroate synthetase inhibitor dihydropteroate synthetase inhibitors dihydropteroic synthetase inhibitor dihydropteroic synthetase inhibitors EC 2.5.1.15 (dihydropteroate synthase) inhibitor CHEBI:50510 potassium channel modulator CHEBI:50514 Drug used to cause constriction of the blood vessels. vasoconstrictor agent CHEBI:50627 An EC 3.2.1.* (glycosidase) inhibitor that interferes with the action of alpha-amylase (EC 3.2.1.1). 1,4-alpha-D-glucan glucanohydrolase inhibitor 1,4-alpha-D-glucan glucanohydrolase inhibitors 4-alpha-D-glucan glucanohydrolase inhibitor 4-alpha-D-glucan glucanohydrolase inhibitors EC 3.2.1.1 (alpha-amylase) inhibitors EC 3.2.1.1 inhibitor EC 3.2.1.1 inhibitors Taka-amylase A inhibitor Taka-amylase A inhibitors alpha-amylase (EC 3.2.1.1) inhibitor alpha-amylase (EC 3.2.1.1) inhibitors alpha-amylase inhibitor alpha-amylase inhibitors endoamylase inhibitor endoamylase inhibitors glycogenase inhibitor glycogenase inhibitors EC 3.2.1.1 (alpha-amylase) inhibitor CHEBI:50629 A cyclooxygenase inhibitor that interferes with the action of cyclooxygenase 2. COX-2 inhibitor COX-2 inhibitors PGHS-2 inhibitor PGHS-2 inhibitors cyclo-oxygenase 2 inhibitor cyclo-oxygenase 2 inhibitors cyclo-oxygenase-2 inhibitor cyclo-oxygenase-2 inhibitors cyclooxygenase 2 inhibitors cyclooxygenase-2 inhibitor cyclooxygenase-2 inhibitors prostaglandin H synthase-2 inhibitor prostaglandin H synthase-2 inhibitors prostaglandin-endoperoxide synthase 2 inhibitor prostaglandin-endoperoxide synthase 2 inhibitors cyclooxygenase 2 inhibitor CHEBI:50630 A cyclooxygenase inhibitor that interferes with the action of cyclooxygenase 1. COX-1 inhibitor COX-1 inhibitors PTGS1 inhibitor PTGS1 inhibitors cyclo-oxygenase 1 inhibitor cyclo-oxygenase 1 inhibitors cyclooxygenase 1 inhibitors cyclooxygenase-1 inhibitor cyclooxygenase-1 inhibitors prostaglandin G/H synthase 1 inhibitor prostaglandin G/H synthase 1 inhibitors prostaglandin H2 synthase 1 inhibitor prostaglandin H2 synthase 1 inhibitors prostaglandin-endoperoxide synthase 1 inhibitor prostaglandin-endoperoxide synthase 1 inhibitors cyclooxygenase 1 inhibitor CHEBI:50646 An agent that inhibits bone resorption and/or favor bone mineralization and bone regeneration. Used to heal bone fractures and to treat bone diseases such as osteopenia and osteoporosis. anti-osteopenia agent anti-osteopenia agents anti-osteopenia drug anti-osteopenia drugs anti-osteoporosis agent anti-osteoporosis agents anti-osteoporosis drug anti-osteoporosis drugs anti-osteoporotic anti-osteoporotic agent anti-osteoporotic agents anti-osteoporotic drug anti-osteoporotic drugs anti-osteoporotics antiosteoporotic antiosteoporotics bone density conservation agents bone density conservation drug bone density conservation drugs bone density conservation agent CHEBI:50671 A drug used to treat hyperthyroidism by reducing the excessive production of thyroid hormones. antithyroid agent antithyroid agents antithyroid drugs antithyroid drug CHEBI:50673 A member of the class of imidazoles that it imidazole-2-thione in which a methyl group replaces the hydrogen which is attached to a nitrogen. Beilstein:108646 CAS:60-56-0 DrugBank:DB00763 Drug_Central:1745 LINCS:LSM-5646 PMID:17438883 PMID:24443787 PMID:7454742 PMID:9172960 Reaxys:108646 1-methyl-1,3-dihydro-2H-imidazole-2-thione Methimazole 1-METHYL-1,3-DIHYDRO-2H-IMIDAZOLE-2-THIONE 1-Methylimidazole-2(3H)-thione Danantizol Favistan Strumazol Tapazole Thacapzol USAF el-30 thiamazol thiamazole thiamazolum tiamazol methimazole Beilstein:108646 Beilstein CAS:60-56-0 ChemIDplus CAS:60-56-0 NIST Chemistry WebBook Drug_Central:1745 DrugCentral PMID:17438883 Europe PMC PMID:24443787 Europe PMC PMID:7454742 Europe PMC PMID:9172960 Europe PMC Reaxys:108646 Reaxys CHEBI:50683 An EC 1.5.1.* (oxidoreductase acting on donor CH-NH group, NAD(+) or NADP(+) as acceptor) inhibitor that interferes with the action of dihydrofolate reductase (EC 1.5.1.3). 7,8-dihydrofolate reductase inhibitor 7,8-dihydrofolate reductase inhibitors DHFR inhibitor DHFR inhibitors EC 1.5.1.3 (dihydrofolate reductase) inhibitors EC 1.5.1.3 inhibitor EC 1.5.1.3 inhibitors NADPH-dihydrofolate reductase inhibitor NADPH-dihydrofolate reductase inhibitors dihydrofolate reductase (EC 1.5.1.3) inhibitor dihydrofolate reductase (EC 1.5.1.3) inhibitors dihydrofolate reductase inhibitor dihydrofolate reductase inhibitors dihydrofolic acid reductase inhibitor dihydrofolic acid reductase inhibitors dihydrofolic reductase inhibitor dihydrofolic reductase inhibitors folic acid reductase inhibitor folic acid reductase inhibitors folic reductase inhibitor folic reductase inhibitors tetrahydrofolate dehydrogenase inhibitor tetrahydrofolate dehydrogenase inhibitors EC 1.5.1.3 (dihydrofolate reductase) inhibitor CHEBI:50689 A substance used either in the prevention or facilitation of pregnancy. reproductive control agent reproductive control drugs reproductive control drug CHEBI:50691 A chemical substance that interrupts pregnancy after implantation. abortifacient agent abortifacient agents abortifacient drug abortifacient drugs abortifacients abortifacient CHEBI:50694 A tetracycline analogue having a dimethylamino group at position 7 and lacking the methyl and hydroxy groups at position 5. Beilstein:3077644 CAS:10118-90-8 DrugBank:DB01017 Drug_Central:1813 LIPID_MAPS_instance:LMPK07000002 PMID:28709717 PMID:31630007 PMID:31719236 PMID:31733348 Reaxys:3077644 (4S,4aS,5aR,12aS)-4,7-bis(dimethylamino)-3,10,12,12a-tetrahydroxy-1,11-dioxo-1,4,4a,5,5a,6,11,12a-octahydrotetracene-2-carboxamide Minocycline (4S,4AS,5AR,12AS)-4,7-BIS(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE 7-Dimethylamino-6-demethyl-6-deoxytetracycline minociclina minociclinum minocycline minomycin minocycline Beilstein:3077644 Beilstein CAS:10118-90-8 ChemIDplus Drug_Central:1813 DrugCentral LIPID_MAPS_instance:LMPK07000002 LIPID MAPS PMID:28709717 Europe PMC PMID:31630007 Europe PMC PMID:31719236 Europe PMC PMID:31733348 Europe PMC Reaxys:3077644 Reaxys CHEBI:50739 A substance that possess antiestrogenic actions but can also produce estrogenic effects as well. It acts as complete or partial agonist or as antagonist. It can be either steroidal or nonsteroidal in structure. estrogen receptor modulator CHEBI:50743 C24H29ClO4 [H][C@@]12C[C@]1([H])[C@@]1(C)C(=CC2=O)C(Cl)=C[C@@]2([H])[C@]3([H])CC[C@](OC(C)=O)(C(C)=O)[C@@]3(C)CC[C@]12[H] CAS:427-51-0 Wikipedia:Cyproterone_Acetate 6-chloro-3,20-dioxo-1beta,2beta-dihydro-3'H-cyclopropa[1,2]pregna-4,6-dien-17-yl acetate CPA cyproterone acetate CHEBI:50745 A compound that interacts with progesterone receptors in target tissues to bring about effects similar to those of progesterone. gestagen gestagens progestagen progestagens progestogens progestogen CHEBI:50748 A drug used to treat psoriasis. antipsoriatic agent antipsoriatic drug antipsoriatic CHEBI:50750 A topoisomerase inhibitor that inhibits DNA topoisomerase (ATP-hydrolysing), EC 5.99.1.3 (also known as topoisomerase II and as DNA gyrase), which catalyses ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. DNA gyrase inhibitor DNA gyrase inhibitors DNA topoisomerase (ATP-hydrolysing) (EC 5.99.1.3) inhibitor DNA topoisomerase (ATP-hydrolysing) (EC 5.99.1.3) inhibitors DNA topoisomerase (ATP-hydrolysing) inhibitor DNA topoisomerase (ATP-hydrolysing) inhibitors DNA topoisomerase II inhibitor DNA topoisomerase II inhibitors EC 5.99.1.3 (DNA topoisomerase (ATP-hydrolysing)) inhibitor EC 5.99.1.3 (DNA topoisomerase (ATP-hydrolysing)) inhibitors EC 5.99.1.3 [DNA topoisomerase (ATP-hydrolysing)] inhibitors EC 5.99.1.3 inhibitor EC 5.99.1.3 inhibitors inhibitor of type II topoisomerase inhibitors of type II topoisomerase topoisomerase II inhibitor topoisomerase II inhibitors topoisomerase-II inhibitor topoisomerase-II inhibitors type II DNA topoisomerase inhibitor type II DNA topoisomerase inhibitors EC 5.99.1.3 [DNA topoisomerase (ATP-hydrolysing)] inhibitor CHEBI:50751 A drug which acts to reduce estrogenic activity in the body, either by reducing the amount of estrogen or by reducing the activity of whatever estrogen is present. anti-estrogenic agent anti-estrogenic drug anti-oestrogen anti-oestrogenic agent anti-oestrogenic drug antiestrogen antiestrogenic agent antiestrogenic drug antioestrogen antioestrogenic agent antioestrogenic drug anti-estrogen CHEBI:50777 Beilstein:4237530 CAS:54048-10-1 DrugBank:DB00294 Drug_Central:1110 17alpha-ethynyl-17beta-hydroxy-11-methylidene-18a-homo-estr-4-en-3-one 3-Ketodesogestrel 3-Oxodesogestrel Implanon etonogestrel etonogestrelum etonogestrel Beilstein:4237530 Beilstein CAS:54048-10-1 ChemIDplus Drug_Central:1110 DrugCentral CHEBI:50790 An EC 1.14.14.* (oxidoreductase acting on paired donors, incorporating of 1 atom of oxygen, with reduced flavin or flavoprotein as one donor) inhibitor which interferes with the action of aromatase (EC 1.14.14.14) and so reduces production of estrogenic steroid hormones. EC 1.14.14.14 (aromatase) inhibitors EC 1.14.14.14 inhibitor EC 1.14.14.14 inhibitors aromatase (EC 1.14.14.14) inhibitor aromatase (EC 1.14.14.14) inhibitors aromatase inhibitor aromatase inhibitors estrogen synthase inhibitor estrogen synthase inhibitors estrogen synthetase inhibitor estrogen synthetase inhibitors oestrogen synthase inhibitor oestrogen synthase inhibitors oestrogen synthetase inhibitor oestrogen synthetase inhibitors EC 1.14.14.14 (aromatase) inhibitor CHEBI:50792 An antagonist at the estrogen receptor. estrogen receptor antagonists estrogen receptor antagonist CHEBI:50803 A nanosized spherical or capsule-shaped structure. nanoparticle http://purl.obolibrary.org/obo/CHEBI_50803 CHEBI:50837 A compound which inhibits or antagonises the biosynthesis or actions of estrogens. oestrogen antagonist estrogen antagonist CHEBI:50846 Biologically active substance whose activity affects or plays a role in the functioning of the immune system. Biomodulator Immune factor Immunologic factor Immunological factor immunomodulators immunomodulator CHEBI:50857 A drug used to treat allergic reactions. anti-allergic drug anti-allergic agent CHEBI:50858 A natural or synthetic analogue of the hormones secreted by the adrenal gland. PMID:32919977 corticoides corticosteroid PMID:32919977 Corticosteroids have widespread inhibitory effects on the immune system and are efficacious in managing acute inflammatory processes. The identification of respiratory support as a predictor of dexamethasone efficacy has provided insights into the disease stages of COVID-19. CHEBI:50859 CAS:153559-49-0 DrugBank:DB00307 Drug_Central:361 4-[1-(3,5,5,8,8-pentamethyl-5,6,7,8-tetrahydronaphthalen-2-yl)vinyl]benzoic acid bexarotene bexaroteno bexarotenum p-(1-(5,6,7,8-Tetrahydro-3,5,5,8,8-pentamethyl-2-naphthyl)vinyl)benzoic acid bexarotene CAS:153559-49-0 ChemIDplus Drug_Central:361 DrugCentral CHEBI:50860 Any molecular entity that contains carbon. organic compounds organic entity organic molecular entity CHEBI:50864 An agent which overcomes insulin resistance by activation of the peroxisome proliferator activated receptor gamma (PPAR-gamma). insulin-sensitizing drug CHEBI:50902 A role played by a chemical compound to induce direct or indirect DNA damage. Such damage can potentially lead to the formation of a malignant tumour, but DNA damage does not lead inevitably to the creation of cancerous cells. Wikipedia:Genotoxicity genotoxic agent genotoxic agents genotoxins genotoxin CHEBI:50903 A role played by a chemical compound which is known to induce a process of carcinogenesis by corrupting normal cellular pathways, leading to the acquistion of tumoral capabilities. agente carcinogeno cancerigene cancerogene carcinogen carcinogene carcinogenic agents carcinogeno carcinogens carcinogenic agent CHEBI:50904 A chemical compound which causes the onset of an allergic reaction by interacting with any of the molecular pathways involved in an allergy. A chemical compound, or part thereof, which causes the onset of an allergic reaction by interacting with any of the molecular pathways involved in an allergy. Wikipedia:Allergen alergeno allergene allergenic agent allergen CHEBI:50905 A role played by a chemical compound in biological systems with adverse consequences in embryo developments, leading to birth defects, embryo death or altered development, growth retardation and functional defect. agent teratogene teratogen teratogeno teratogenic agent CHEBI:50908 A role played by a chemical compound exihibiting itself through the ability to induce damage to the liver in animals. A role played by an entity exihibiting itself through the ability to induce damage to the liver in animals. agente hepatotoxico hepatotoxic agents hepatotoxicant hepatotoxicants hepatotoxin hepatotoxins hepatoxic agent hepatoxicant hepatotoxic agent CHEBI:50912 A role played by aan entity exihibiting itself through the ability to induce damage to the heart and cardiomyocytes. cardiotoxic agent CHEBI:50916 An EC 2.7.* (P-containing group transferase) inhibitor that interferes with the action of lipid kinases. lipid kinase inhibitor CHEBI:50924 A member of the class of phenylureas that is urea in which one of the nitrogens is substituted by a 4-chloro-3-trifluorophenyl group while the other is substituted by a phenyl group which, in turn, is substituted at the para position by a [2-(methylcarbamoyl)pyridin-4-yl]oxy group. CAS:284461-73-0 DrugBank:DB00398 Drug_Central:2459 LINCS:LSM-1008 4-[4-({[4-chloro-3-(trifluoromethyl)phenyl]carbamoyl}amino)phenoxy]-N-methylpyridine-2-carboxamide 4-(4-((((4-Chloro-3-(trifluoromethyl)phenyl)amino)carbonyl)amino)phenoxy)-N-methyl-2-pyridinecarboxamide N-(4-Chloro-3-(trifluoromethyl)phenyl)-N'-(4-(2-(N-methylcarbamoyl)-4-pyridyloxy)phenyl)urea sorafenib sorafenibum sorafenib CAS:284461-73-0 ChemIDplus Drug_Central:2459 DrugCentral CHEBI:50925 An EC 2.7.11.* (protein-serine/threonine kinase) inhibitor that interferes with the action of non-specific serine/threonine protein kinase (EC 2.7.11.1), a kinase enzyme involved in phosphorylation of hydroxy group of serine or threonine. A-kinase inhibitor A-kinase inhibitors AP50 kinase inhibitor AP50 kinase inhibitors ATP-protein transphosphorylase inhibitor ATP-protein transphosphorylase inhibitors ATP:protein phosphotransferase (non-specific) inhibitor ATP:protein phosphotransferase (non-specific) inhibitors BR serine/threonine-protein kinase 2 inhibitor BR serine/threonine-protein kinase 2 inhibitors CK-2 inhibitor CK-2 inhibitors CKI inhibitor CKI inhibitors CKII inhibitor CKII inhibitors EC 2.7.11.1 (non-specific serine/threonine protein kinase) inhibitors EC 2.7.11.1 inhibitor EC 2.7.11.1 inhibitors HIPK2 inhibitor HIPK2 inhibitors Hpr kinase inhibitor Hpr kinase inhibitors M phase-specific cdc2 kinase inhibitor M phase-specific cdc2 kinase inhibitors MKNK2 inhibitor MKNK2 inhibitors PAK-1 inhibitor PAK-1 inhibitors PAK1 inhibitor PAK1 inhibitors PKA inhibitor PKA inhibitors Prp4 protein kinase inhibitor Prp4 protein kinase inhibitors Raf kinase inhibitor Raf kinase inhibitors Raf-1 inhibitor Raf-1 inhibitors STK32 inhibitor STK32 inhibitors T-antigen kinase inhibitor T-antigen kinase inhibitors WEE1Hu inhibitor WEE1Hu inhibitors Wee 1-like kinase inhibitor Wee 1-like kinase inhibitors Wee-kinase inhibitor Wee-kinase inhibitors betaIIPKC inhibitor betaIIPKC inhibitors cAMP-dependent protein kinase A inhibitor cAMP-dependent protein kinase A inhibitors cAMP-dependent protein kinase inhibitor cAMP-dependent protein kinase inhibitors cGMP-dependent protein kinase inhibitor cGMP-dependent protein kinase inhibitors calcium-dependent protein kinase C inhibitor calcium-dependent protein kinase C inhibitors calcium/phospholipid-dependent protein kinase inhibitor calcium/phospholipid-dependent protein kinase inhibitors casein kinase (phosphorylating) inhibitor casein kinase (phosphorylating) inhibitors casein kinase 2 inhibitor casein kinase 2 inhibitors casein kinase I inhibitor casein kinase I inhibitors casein kinase II inhibitor casein kinase II inhibitors casein kinase inhibitor casein kinase inhibitors cyclic AMP-dependent protein kinase A inhibitor cyclic AMP-dependent protein kinase A inhibitors cyclic AMP-dependent protein kinase inhibitor cyclic AMP-dependent protein kinase inhibitors cyclic monophosphate-dependent protein kinase inhibitor cyclic monophosphate-dependent protein kinase inhibitors cyclic nucleotide-dependent protein kinase inhibitor cyclic nucleotide-dependent protein kinase inhibitors cyclin-dependent kinase inhibitor cyclin-dependent kinase inhibitors dsk1 inhibitor dsk1 inhibitors epsilon PKC inhibitor epsilon PKC inhibitors glycogen synthase a kinase inhibitor glycogen synthase a kinase inhibitors glycogen synthase kinase inhibitor glycogen synthase kinase inhibitors hydroxyalkyl-protein kinase inhibitor hydroxyalkyl-protein kinase inhibitors mitogen-activated S6 kinase inhibitor mitogen-activated S6 kinase inhibitors non-specific serine/threonine protein kinase (EC 2.7.11.1) inhibitor non-specific serine/threonine protein kinase (EC 2.7.11.1) inhibitors non-specific serine/threonine protein kinase inhibitor non-specific serine/threonine protein kinase inhibitors p21 activated kinase-1 inhibitor p21 activated kinase-1 inhibitors p82 kinase inhibitor p82 kinase inhibitors phosphorylase b kinase kinase inhibitor phosphorylase b kinase kinase inhibitors protein glutamyl kinase inhibitor protein glutamyl kinase inhibitors protein kinase (phosphorylating) inhibitor protein kinase (phosphorylating) inhibitors protein kinase A inhibitor protein kinase A inhibitors protein kinase CK2 inhibitor protein kinase CK2 inhibitors protein kinase p58 inhibitor protein kinase p58 inhibitors protein phosphokinase inhibitor protein phosphokinase inhibitors protein serine kinase inhibitor protein serine kinase inhibitors protein serine-threonine kinase inhibitor protein serine-threonine kinase inhibitors protein-aspartyl kinase inhibitor protein-aspartyl kinase inhibitors protein-cysteine kinase inhibitor protein-cysteine kinase inhibitors protein-serine kinase inhibitor protein-serine kinase inhibitors protein-serine/threonine kinase inhibitors ribosomal S6 protein kinase inhibitor ribosomal S6 protein kinase inhibitors ribosomal protein S6 kinase II inhibitor ribosomal protein S6 kinase II inhibitors serine kinase inhibitor serine kinase inhibitors serine protein kinase inhibitor serine protein kinase inhibitors serine(threonine) protein kinase inhibitor serine(threonine) protein kinase inhibitors serine-specific protein kinase inhibitor serine-specific protein kinase inhibitors serine/threonine protein kinase inhibitor serine/threonine protein kinase inhibitors threonine-specific protein kinase inhibitor threonine-specific protein kinase inhibitors twitchin kinase inhibitor twitchin kinase inhibitors type-2 casein kinase inhibitor type-2 casein kinase inhibitors EC 2.7.11.1 (non-specific serine/threonine protein kinase) inhibitor CHEBI:50926 An agent that modulates the physiologic angiogenesis process. This is accomplished by endogenous angiogenic proteins and a variety of other chemicals and pharmaceutical agents. angiogenesis modulating agent CHEBI:50949 A compound that specifically inhibits the reuptake of serotonin in the brain. This increases the serotonin concentration in the synaptic cleft which then activates serotonin receptors to a greater extent. SSRI serotonin reuptake inhibitor serotonin uptake inhibitor CHEBI:51006 A fatty acyl-CoA that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of any unsaturated fatty acid. PMID:13152086 unsaturated fatty acyl-CoA CHEBI:51039 A dopaminergic agent that blocks the transport of dopamine into axon terminals or into storage vesicles within terminals. Most of the adrenergic uptake inhibitors also inhibit dopamine uptake. DARI DRI dopamine reuptake inhibitor dopamine reuptake inhibitors dopamine uptake inhibitors dopamine uptake inhibitor CHEBI:51061 A drug that modulates the function of the endocrine glands, the biosynthesis of their secreted hormones, or the action of hormones upon their specific sites. hormone receptor modulators hormone receptor modulator CHEBI:51086 A role played by the molecular entity or part thereof within a chemical context. chemical role CHEBI:5120 Beilstein:2008796 CAS:76-43-7 DrugBank:DB01185 Drug_Central:1210 LIPID_MAPS_instance:LMST02020025 9-fluoro-11beta,17beta-dihydroxy-17alpha-methylandrost-4-en-3-one 11beta,17beta-Dihydroxy-9alpha-fluoro-17alpha-methyl-4-androster-3-one 17alpha-Methyl-9alpha-fluoro-11beta-hydroxytesterone 9-Fluoro-11beta,17beta-dihydroxy-17-methylandrost-4-en-3-one 9alpha-Fluoro-11beta-hydroxy-17-methyltestosterone Testosterone, 9-fluoro-11beta-hydroxy-17-methyl- fluoximesterona fluoxymesterone fluoxymesteronum fluoxymesterone Beilstein:2008796 Beilstein CAS:76-43-7 ChemIDplus Drug_Central:1210 DrugCentral LIPID_MAPS_instance:LMST02020025 LIPID MAPS CHEBI:5132 Beilstein:2157663 CAS:13311-84-7 DrugBank:DB00499 Drug_Central:1223 LINCS:LSM-2621 2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]propanamide Flutamide 4'-nitro-3'-trifluoromethylisobutyranilide Eulexin Niftolide alpha,alpha,alpha-trifluoro-2-methyl-4'-nitro-m-propionotoluidide flutamida flutamide flutamidum niftolid flutamide Beilstein:2157663 ChemIDplus CAS:13311-84-7 ChemIDplus Drug_Central:1223 DrugCentral CHEBI:51371 A drug used to produce muscle relaxation (excepting neuromuscular blocking agents). Its primary clinical and therapeutic use is the treatment of muscle spasm and immobility associated with strains, sprains, and injuries of the back and, to a lesser degree, injuries to the neck. Also used for the treatment of a variety of clinical conditions that have in common only the presence of skeletal muscle hyperactivity, for example, the muscle spasms that can occur in multiple sclerosis. muscle relaxants muscle relaxant CHEBI:51372 A drug used for its actions on skeletal muscle. neuromuscular agent CHEBI:51374 A substance, such as agonists, antagonists, degradation or uptake inhibitors, depleters, precursors, and modulators of receptor function, used for its pharmacological actions on GABAergic systems. GABA agent CHEBI:51450 COc1ccccc1Oc1c(NS(=O)(=O)c2ccc(cc2)C(C)(C)C)nc(nc1OCCO)-c1ncccn1 ATC:C02KX01 CAS:147536-97-8 DrugBank:DB00559 Drug_Central:392 LINCS:LSM-5825 Wikipedia:Bosentan 4-tert-butyl-N-[6-(2-hydroxyethoxy)-5-(2-methoxyphenoxy)-2,2'-bipyrimidin-4-yl]benzenesulfonamide 4-(1,1-Dimethylethyl)-N-(6-(2-hydroxyethoxy)-5-(2-methoxyphenoxy)-(2,2'-bipyrimidin)-4-yl) benzenesulfornamide bosentan bosentanum p-tert-Butyl-N-(6-(2-hydroxyethoxy)-5-(o-methoxyphenoxy)-2-(2-pyrimidinyl)-4-pyrimidinyl)benzenesulfonamide bosentan CAS:147536-97-8 ChemIDplus Drug_Central:392 DrugCentral CHEBI:51451 A hormone antagonist that blocks endothelin receptors. ERA endothelin receptor antagonist CHEBI:5165 CAS:93390-81-9 Drug_Central:1247 Fosphenytoin cerebyx fosphenytoin sodium fosphenytoin sodium hydrate Fosphenytoin Drug_Central:1247 DrugCentral CHEBI:51756 Alexa Fluor 532 Alexa Fluor 532 CHEBI:51760 Alexa Fluor 546 Alexa Fluor 546 CHEBI:52206 A biological role played by the molecular entity or part thereof within a biochemical context. biochemical role CHEBI:52208 biophysical role CHEBI:52209 A role played by the molecular entity or part thereof which causes the development of a pathological process. etiopathogenetic agent etiopathogenetic role aetiopathogenetic role CHEBI:52210 A biological role which describes how a drug interacts within a biological system and how the interactions affect its medicinal properties. pharmacological role CHEBI:52214 Any molecule or ion capable of binding to a central metal atom to form coordination complexes. ligands ligand CHEBI:52217 Any substance introduced into a living organism with therapeutic or diagnostic purpose. farmaco medicament pharmaceuticals pharmaceutical CHEBI:52290 A chemical substance that encourages a cell to commence cell division, triggering mitosis. mitogens mitogen CHEBI:52424 An EC 3.2.* (glycosylase) inhibitor that interferes with the action of any glycosidase (i.e. enzymes hydrolysing O- and S-glycosyl compounds, EC 3.2.1.*). EC 3.2.1.* (glycosidase) inhibitors EC 3.2.1.* inhibitor EC 3.2.1.* inhibitors glycosidase (EC 3.2.1.*) inhibitor glycosidase (EC 3.2.1.*) inhibitors glycosidase inhibitor glycosidase inhibitors glycoside hydrolase inhibitors EC 3.2.1.* (glycosidase) inhibitor CHEBI:52450 A 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine betaine which has octadecyl as the alkyl group. PAF is a potent phospholipid activator and mediator of many leukocyte functions, including platelet aggregation, inflammation, and anaphylaxis. 2-O-acetyl-1-O-octadecyl-sn-glycero-3-phosphocholine CHEBI:52629 An inhibitor of ribonuclease H (EC 3.1.26.13), an enzyme required for specific hydrolysis of the RNA strand of an RNA/DNA hybrid. EC 3.1.26.13 (retroviral ribonuclease H) inhibitors EC 3.1.26.13 inhibitor EC 3.1.26.13 inhibitors HIV RNase H inhibitor HIV RNase H inhibitors HIV-1 RNase H inhibitor HIV-1 RNase H inhibitors HIV-1 ribonuclease H inhibitor HIV-1 ribonuclease H inhibitors RT/RNase H inhibitor RT/RNase H inhibitors retroviral reverse transcriptase RNaseH inhibitor retroviral reverse transcriptase RNaseH inhibitors retroviral ribonuclease H (EC 3.1.26.13) inhibitor retroviral ribonuclease H (EC 3.1.26.13) inhibitors retroviral ribonuclease H inhibitor EC 3.1.26.13 (retroviral ribonuclease H) inhibitor CHEBI:52673 Alexa Fluor 555 A fluorescent dye of absorption wavelength 555 nm and emission wavelength 565 nm, derived from a 3,6-diaminoxanthene-4,5-disulfate. Alexa Fluor 555 CHEBI:52717 L-Phenylalaninamide substituted at the amide nitrogen by a 1-(dihydroxyboranyl)-3-methylbutyl group and at N(alpha) by a pyrazin-2-ylcarbonyl group. It is a dipeptidyl boronic acid that reversibly inhibits the 26S proteasome. C19H25BN4O4 CC(C)C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)c1cnccn1)B(O)O CAS:179324-69-7 DrugBank:DB00188 Drug_Central:391 LINCS:LSM-6281 PMID:18484921 PMID:18980173 PMID:21504411 PMID:21865767 Reaxys:8723817 Wikipedia:Bortezomib N-[(1R)-1-(dihydroxyboranyl)-3-methylbutyl]-N(alpha)-(pyrazin-2-ylcarbonyl)-L-phenylalaninamide [(1R)-3-methyl-1-({(2S)-3-phenyl-2-[(pyrazin-2-ylcarbonyl)amino]propanoyl}amino)butyl]boronic acid N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE PS 341 PS-341 Velcade bortezomib bortezomib CAS:179324-69-7 ChemIDplus Drug_Central:391 DrugCentral PMID:18484921 Europe PMC PMID:18980173 Europe PMC PMID:21504411 Europe PMC PMID:21865767 Europe PMC Reaxys:8723817 Reaxys CHEBI:52726 A drug that blocks the action of proteasomes, cellular complexes that break down proteins. proteasome inhibitors proteasome inhibitor CHEBI:5296 C15H22O3 Cc1ccc(C)c(OCCCC(C)(C)C(O)=O)c1 Beilstein:1881200 CAS:25812-30-0 DrugBank:DB01241 Drug_Central:1285 LINCS:LSM-2227 Wikipedia:Gemfibrozil 5-(2,5-dimethylphenoxy)-2,2-dimethylpentanoic acid Gemfibrozil 2,2-Dimethyl-5-(2,5-dimethylphenoxy)valeriansaeure 2,2-Dimethyl-5-(2,5-xylyloxy)valeriansaeure 2,2-Dimethyl-5-(2,5-xylyloxy)valeric acid Gemfibrozilo Lopid gemfibrozil gemfibrozilum gemfibrozil Beilstein:1881200 Beilstein CAS:25812-30-0 ChemIDplus Drug_Central:1285 DrugCentral CHEBI:53559 A topoisomerase inhibitor that inhibits DNA topoisomerase IV, which catalyses ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. topoisomerase IV inhibitors topoisomerase IV inhibitor CHEBI:53756 An entity which inhibits the activity of HIV-1 reverse transcriptase. HIV-1 reverse transcriptase inhibitors reverse transcriptase inhibitor reverse transcriptase inhibitors HIV-1 reverse transcriptase inhibitor CHEBI:53784 A drug that suppresses spasms. These are usually caused by smooth muscle contraction, especially in tubular organs. The effect is to prevent spasms of the stomach, intestine or urinary bladder. antispasmodics antispasmodic drug CHEBI:5441 An urea that has formula C23H28ClN3O5S. CASRN:10238-21-8 DrugBank:DB01016 InChIKeyZ:NNLBTZKUZBEKO-UHFFFAOYSA-N Wikipedia:Glyburide glibenclamide glyburide CHEBI:55324 A drug used for its effects on the gastrointestinal system, e.g. controlling gastric acidity, regulating gastrointestinal motility and water flow, and improving digestion. gastrointestinal agent gastrointestinal agents gastrointestinal drugs gastrointestinal drug CHEBI:55438 An angiotensin compound consisting of the linear heptapeptide sequence L-Asp-L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro. 0 C41H62N12O11 InChI=1S/C41H62N12O11/c1-5-22(4)33(38(61)50-29(17-24-19-45-20-47-24)39(62)53-15-7-9-30(53)40(63)64)52-36(59)28(16-23-10-12-25(54)13-11-23)49-37(60)32(21(2)3)51-35(58)27(8-6-14-46-41(43)44)48-34(57)26(42)18-31(55)56/h10-13,19-22,26-30,32-33,54H,5-9,14-18,42H2,1-4H3,(H,45,47)(H,48,57)(H,49,60)(H,50,61)(H,51,58)(H,52,59)(H,55,56)(H,63,64)(H4,43,44,46)/t22-,26-,27-,28-,29-,30-,32-,33-/m0/s1 PVHLMTREZMEJCG-GDTLVBQBSA-N 899.00480 898.46610 CC[C@H](C)[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C(=O)N[C@@H](Cc1cnc[nH]1)C(=O)N1CCC[C@H]1C(O)=O Beilstein:8753045 CAS:39386-80-6 CAS:51833-78-4 L-alpha-aspartyl-L-arginyl-L-valyl-L-tyrosyl-L-isoleucyl-L-histidyl-L-proline 8-Des-phe-angiotensin II Angiotensin (1-7) Angiotensin I (1-7) Angiotensin II (1-7) Angiotensin II (1-7) heptapeptide Ile(5)-angiotensin II (1-7) CHEBI:566274 A dialdehyde that is propane substituted by two oxo groups at the terminal carbon atoms respectively. A biomarker of oxidative damage to lipids caused by smoking, it exists in vivo mainly in the enol form. malondialdehyde CHEBI:575568 A naphthoquinone compound having a 4-(4-chlorophenyl)cyclohexyl group at the 2-position and a hydroxy substituent at the 3-position. Beilstein:8076827 CAS:95233-18-4 DrugBank:DB01117 Drug_Central:258 PMID:10658902 PMID:11956677 PMID:12791689 PMID:14727190 PMID:15044733 PMID:15718226 PMID:21735454 PMID:23292347 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxy-1,4-naphthoquinone 2-(trans-4-(p-Chlorophenyl)cyclohexyl)-3-hydroxy-1,4-naphthoquinone Acuvel Mepron Wellvone atovaquone atovaquone Beilstein:8076827 Beilstein CAS:95233-18-4 ChemIDplus CAS:95233-18-4 DrugBank Drug_Central:258 DrugCentral PMID:10658902 Europe PMC PMID:11956677 Europe PMC PMID:12791689 Europe PMC PMID:14727190 Europe PMC PMID:15044733 Europe PMC PMID:15718226 Europe PMC PMID:21735454 Europe PMC PMID:23292347 Europe PMC CHEBI:5801 An aminoquinoline that is chloroquine in which one of the N-ethyl groups is hydroxylated at position 2. An antimalarial with properties similar to chloroquine that acts against erythrocytic forms of malarial parasites, it is mainly used as the sulfate salt for the treatment of lupus erythematosus, rheumatoid arthritis, and light-sensitive skin eruptions. C18H26ClN3O CCN(CCO)CCCC(C)Nc1ccnc2cc(Cl)ccc12 PMID:32307653 PMID:33691216 hydroxychloroquine PMID:32307653 The open-label non-randomized clinical trial of Gautret and co-workers suggested hydroxychloroquine and azithromycin for COVID-19 therapy. In this trial, twenty-six cases were treated daily with 600 mg of hydroxychloroquine (six patients were lost during the monitoring) and presented a significant decrease in viral load after six days compared to untreated controls. The most interesting finding of this study was that all patients treated with hydroxychloroquine and azithromycin had negative PCR results in nasopharyngeal samples, i.e., 100% of patients treated with both drugs were virologically cured compared to 57.1% of subjects treated with hydroxychloroquine only, and 12.5% of untreated individuals. PMID:33691216 Chloroquine and hydroxychloroquine interfere with virus entry (by blocking the terminal glycosylation of ACE-2), and inhibit the post-entry mechanism through alkalinisation of the endosome pH (Vincent et al., 2005). They also inhibit the biosynthesis of sialic acid (Vincent et al., 2005). Growing evidence alleviates the potential use of hydroxychoroquine as an effective therapy in the treatment of COVID-19 patients. Multiple clinical trials have demonstrated that hydroxychoroquine is of no value when used in moderate doses as either a pre- or post-exposure prophylaxis (Barnabas et al., 2020; Boulware et al., 2020; Rajasingham et al., 2020). In addition, many retrospective observational studies deny its value in COVID-19 treatment (Geleris et al., 2020; Magagnoli et al., 2020; Rosenberg et al., 2020) and also in some prospective clinical trials (Cavalcanti et al., 2020; Horby et al., 2020). However, more than 100 clinical trials conducted on the efficacy of chloroquine and hydroxychloroquine are still ongoing (Chen et al., 2020); thus, it may be too early to determine conclusively the value of such drugs. CHEBI:58363 A monocarboxylic acid anion arising from deprotonation of the carboxy group of oxamic acid. -1 C2H2NO3 NC(=O)C([O-])=O PMID:32697943 oxamate PMID:32697943 Finally, to evaluate the importance of aerobic glycolysis for CoV-2 infection, we blocked lactate dehydrogenase A (LDH-A) activity with oxamate. This also completely abrogated viral replication and reduced ACE2 and IL-1b expression in CoV-2-infected cells (Figures 2K and S3F). CHEBI:5855 A monocarboxylic acid that is propionic acid in which one of the hydrogens at position 2 is substituted by a 4-(2-methylpropyl)phenyl group. C13H18O2 CC(C)Cc1ccc(cc1)C(C)C(O)=O CAS:15687-27-1 DrugBank:DB01050 2-[4-(2-methylpropyl)phenyl]propanoic acid ibuprofen CHEBI:59132 Any substance that stimulates an immune response in the body, such as through antibody production or by presentation to a T-cell receptor after binding to a major histocompability complex (MHC). antigen CHEBI:5924 Any EC 3.4.* (hydrolases acting on peptide bond) inhibitor that inhibits the activity of a serine endopeptidase (EC 3.4.21.*). EC 3.4.21.* (serine endopeptidase) inhibitors EC 3.4.21.* inhibitor EC 3.4.21.* inhibitors inhibitor of serine endopeptidase (EC 3.4.21.*) inhibitor of serine endopeptidase (EC 3.4.21.*)s serine endopeptidase inhibitor serine endopeptidase inhibitors EC 3.4.21.* (serine endopeptidase) inhibitor CHEBI:59285 An EC 1.14.13.* (oxidoreductase acting on paired donors, incorporating 1 atom of oxygen, with NADH or NADPH as one donor) inhibitor that interferes with the action of squalene monooxygenase (EC 1.14.13.132). EC 1.14.13.132 (squalene monooxygenase) inhibitors squalene 2,3-oxidocyclase inhibitor squalene 2,3-oxidocyclase inhibitors squalene epoxidase inhibitor squalene epoxidase inhibitors squalene hydroxylase inhibitor squalene hydroxylase inhibitors squalene monooxygenase (EC 1.14.13.132) inhibitor squalene monooxygenase (EC 1.14.13.132) inhibitors squalene monooxygenase inhibitor squalene monooxygenase inhibitors squalene oxydocyclase inhibitor squalene oxydocyclase inhibitors squalene-2,3-epoxidase inhibitor squalene-2,3-epoxidase inhibitors squalene-2,3-epoxide cyclase inhibitor squalene-2,3-epoxide cyclase inhibitors EC 1.14.13.132 (squalene monooxygenase) inhibitor CHEBI:5937 CAS:76543-88-9 Interferon alfa-2a Interferon alpha-2A Interferon alfa-2a CHEBI:5938 CAS:145155-23-3 Interferon beta-1b Interferon beta-1b CHEBI:59517 Any substance that inhibits the synthesis of DNA. DNA synthesis inhibitors DNA synthesis inhibitor CHEBI:5958 CAS:54-92-2 Drug_Central:1480 LINCS:LSM-5940 Iproniazid euphozid iprazid iprazide iproniazid phosphate iproniazide iproniazide phosphate marsilid Iproniazid Drug_Central:1480 DrugCentral CHEBI:59739 A reagent that forms a bond to its reaction partner (the nucleophile) by accepting both bonding electrons from that reaction partner. electrophile electrophiles electrophilic reagents electrophilic reagent CHEBI:59740 A reagent that forms a bond to its reaction partner (the electrophile) by donating both bonding electrons. nucleophile nucleophilic reagent CHEBI:59826 A synthetic progestogen. progestins progestin CHEBI:59886 A drug which interferes with the binding, fusion and entry of an HIV virion to a human cell. By blocking this step in HIV's replication cycle, such agents slow the progression from HIV infection to AIDS. PMID:22470838 HIV entry inhibitor HIV entry inhibitors HIV fusion inhibitors HIV fusion inhibitor PMID:22470838 Europe PMC CHEBI:59897 A DNA polymerase inhibitor that interferes with the activity of reverse transcriptase, EC 2.7.7.49, a viral DNA polymerase enzyme that retroviruses need in order to reproduce. DNA nucleotidyltransferase (RNA-directed) inhibitor DNA nucleotidyltransferase (RNA-directed) inhibitors EC 2.7.7.49 (RNA-directed DNA polymerase) inhibitors EC 2.7.7.49 inhibitor EC 2.7.7.49 inhibitors RNA revertase inhibitor RNA revertase inhibitors RNA-dependent DNA polymerase inhibitor RNA-dependent DNA polymerase inhibitors RNA-dependent deoxyribonucleate nucleotidyltransferase inhibitor RNA-dependent deoxyribonucleate nucleotidyltransferase inhibitors RNA-directed DNA polymerase (EC 2.7.7.49) inhibitor RNA-directed DNA polymerase (EC 2.7.7.49) inhibitors RNA-directed DNA polymerase inhibitor RNA-directed DNA polymerase inhibitors RNA-instructed DNA polymerase inhibitor RNA-instructed DNA polymerase inhibitors RT inhibitor RT inhibitors deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (RNA-directed) inhibitor deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (RNA-directed) inhibitors reverse transcriptase inhibitor reverse transcriptase inhibitors revertase inhibitor revertase inhibitors telomerase inhibitor telomerase inhibitors EC 2.7.7.49 (RNA-directed DNA polymerase) inhibitor CHEBI:59999 A chemical substance is a portion of matter of constant composition, composed of molecular entities of the same type or of different types. chemical substance CHEBI:600520 A cyclic hexapeptide echinocandin antibiotic which exerts its effect by inhibiting the synthesis of 1,3-beta-D-glucan, an integral component of the fungal cell wall. It is used as the sodium salt for the treatment of invasive candidiasis, and of aspergillosis in patients who are intolerant of other therapy. Beilstein:9610508 CAS:235114-32-6 DrugBank:DB01141 PMID:17194830 PMID:17307974 PMID:17325217 PMID:17325225 PMID:17420211 PMID:17785512 5-[(1S,2S)-2-{(2R,6S,9S,11R,12R,14aS,15S,16S,20S,23S,25aS)-20-[(1R)-3-amino-1-hydroxy-3-oxopropyl]-2,11,12,15-tetrahydroxy-6-[(1R)-1-hydroxyethyl]-16-methyl-5,8,14,19,22,25-hexaoxo-9-[(4-{5-[4-(pentyloxy)phenyl]isoxazol-3-yl}benzoyl)amino]tetracosahydro-1H-dipyrrolo[2,1-c:2',1'-l][1,4,7,10,13,16]hexaazacyclohenicosin-23-yl}-1,2-dihydroxyethyl]-2-hydroxyphenyl hydrogen sulfate 5.1:6-anhydro{(4R,5R)-4,5-dihydroxy-N(2)-(4-{5-[4-(pentyloxy)phenyl]isoxazol-3-yl}benzoyl)-L-ornithyl-L-threonyl-(4R)-4-hydroxy-L-prolyl-(4S)-4-hydroxy-4-[4-hydroxy-3-(sulfooxy)phenyl]-L-threonyl-(3R)-3-hydroxy-L-glutaminyl-(3S,4S)-3-hydroxy-4-methyl-L-proline} Mycamine micafungin micafungin Beilstein:9610508 Beilstein CAS:235114-32-6 ChemIDplus PMID:17194830 ChEMBL PMID:17307974 ChEMBL PMID:17325217 ChEMBL PMID:17325225 ChEMBL PMID:17420211 ChEMBL PMID:17785512 ChEMBL CHEBI:60169 A derivative of phosphatidylinositol in which the inositol ring is phosphorylated at three unspecified positions. phosphatidylinositol trisphosphate CHEBI:60258 A hydrolase inhibitor that interferes with the action of any hydrolase acting on peptide bonds (peptidase), EC 3.4.*.*). EC 3.4.* (hydrolase acting on peptide bond) inhibitor EC 3.4.* (hydrolase acting on peptide bonds) inhibitors EC 3.4.* (hydrolases acting on peptide bond) inhibitors EC 3.4.* (peptidase) inhibitor EC 3.4.* (peptidase) inhibitors EC 3.4.* inhibitor EC 3.4.* inhibitors inhibitor of hydrolases acting on peptide bond (EC 3.4.*) inhibitors of hydrolases acting on peptide bond (EC 3.4.*) peptidase inhibitors protease inhibitor protease inhibitors EC 3.4.* (hydrolases acting on peptide bond) inhibitor CHEBI:6030 A carbohydrazide obtained by formal condensation between pyridine-4-carboxylic acid and hydrazine. C6H7N3O NNC(=O)c1ccncc1 CAS:54-85-3 DrugBank:DB00951 LINCS:LSM-6682 pyridine-4-carbohydrazide isoniazide CHEBI:6067 A retinoic acid that is all-trans-retinoic acid in which the double bond which is alpha,beta- to the carboxy group is isomerised to Z configuration. A synthetic retinoid, it is used for the treatment of severe cases of acne and other skin diseases. Beilstein:1885770 CAS:4759-48-2 DrugBank:DB00982 Drug_Central:1508 LIPID_MAPS_instance:LMPR01090021 PMID:11606947 PMID:11866680 PMID:15304471 PMID:18077132 PMID:18788179 PMID:19568610 PMID:20482692 PMID:23676507 PMID:9807973 Reaxys:1885770 (2Z,4E6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)nona-2,4,6,8-tetraenoic acid (7E,9E,11E,13Z)-retinoic acid 13-RA 13-cis-Vitamin A acid 13-cis-retinoic acid Accutane Amnesteem Claravis Neovitamin A acid cis-RA isotretinoin isotretinoina isotretinoine isotretinoino isotretinoinum isotretinoin Beilstein:1885770 Beilstein CAS:4759-48-2 ChemIDplus Drug_Central:1508 DrugCentral LIPID_MAPS_instance:LMPR01090021 LIPID MAPS PMID:11606947 Europe PMC PMID:11866680 Europe PMC PMID:15304471 Europe PMC PMID:18077132 Europe PMC PMID:18788179 Europe PMC PMID:19568610 Europe PMC PMID:20482692 Europe PMC PMID:23676507 Europe PMC PMID:9807973 Europe PMC Reaxys:1885770 Reaxys CHEBI:6076 An N-arylpiperazine that is cis-ketoconazole in which the imidazol-1-yl group is replaced by a 1,2,4-triazol-1-yl group and in which the actyl group attached to the piperazine moiety is replaced by a p-[(+-)1-sec-butyl-5-oxo-1,5-dihydro-4H-1,2,4-triazol-4-yl]phenyl group. A potent P-glycoprotein and CYP3A4 inhibitor, it is used as an antifungal drug for the treatment of various fungal infections, including aspergillosis, blastomycosis, candidiasis, chromoblastomycosis, coccidioidomycosis, cryptococcosis, histoplasmosis, and sporotrichosis. CAS:84625-61-6 DrugBank:DB01167 PMID:11219548 PMID:11403818 PMID:11422002 PMID:15521894 PMID:19025521 PMID:20400651 PMID:25326091 2-(butan-2-yl)-4-{4-[4-(4-{[(2R,4S)-2-(2,4-dichlorophenyl)-2-(1H-1,2,4-triazol-1-ylmethyl)-1,3-dioxolan-4-yl]methoxy}phenyl)piperazin-1-yl]phenyl}-2,4-dihydro-3H-1,2,4-triazol-3-one Itraconazole itraconazole Itrizole (TN) Oriconazole Sporanox (TN) itraconazole CAS:84625-61-6 ChemIDplus PMID:11219548 Europe PMC PMID:11403818 Europe PMC PMID:11422002 Europe PMC PMID:15521894 Europe PMC PMID:19025521 Europe PMC PMID:20400651 Europe PMC PMID:25326091 Europe PMC CHEBI:6078 A mixture consisting of >= 90% 22,23-dihydroavermectin B1a (R = Me) and <= 10% 22,23-dihydroavermectin B1b (R = H). A semi-synthetic derivative of abamectin, it is used as a broad-spectrum antiparasite medication, particularly against worms (except tapeworms), although it is also effective against most mites and some lice. https://www.drugbank.ca/drugs/DB00602 0 C47H71O14R 860.060 859.48438 [H][C@@]12C\C=C(C)\[C@@H](O[C@H]3C[C@H](OC)[C@@H](O[C@H]4C[C@H](OC)[C@@H](O)[C@H](C)O4)[C@H](C)O3)[C@@H](C)\C=C\C=C3/CO[C@]4([H])[C@H](O)C(C)=C[C@@]([H])(C(=O)O[C@@H](C1)C[C@]1(CC[C@H](C)[C@]([H])(O1)[C@@H](C)C[*])O2)[C@]34O CAS:70288-86-7 ChemIDplus:70288-86-7 CiteXplore:15078277 CiteXplore:18718154 CiteXplore:21824728 CiteXplore:21831526 CiteXplore:22039801 CiteXplore:22047763 DrugBank:DB00602 HMDB:HMDB0014740 PMID:15078277 PMID:18718154 PMID:21824728 PMID:21831526 PMID:22039784 PMID:22039801 PMID:22047763 Patent:US4199569 Wikipedia:Ivermectin Ivermax Ivomec Mectizan Noromectin Privermectin Sklice Stromectol Vetrimec Zimecterin ivermectine ivermectino ivermectinum ivermectin CHEBI:60798 Any substance which inhibits the action of receptors for excitatory amino acids. EAA receptor antagonist EAA receptor antagonists excitatory amino acid antagonists excitatory amino acid receptor antagonist excitatory amino acid receptor antagonists excitatory amino acid antagonist CHEBI:60815 A lysophosphatidic acid having the unusual property of a phosphodiester moiety linked to positions sn-1 and sn1' of glycerol; and two additional fatty acids esterified to the glycerol head group. BMP is a negatively charged phospholipid found almost exclusively in late endosomes/lysosomes. BMP content is higher in alveolar macrophages (18% of total phospholipids) than in other cell types. BMP is a structural isomer of phosphatidylglycerol (PG) and is synthesized through a series of acylation and deacylation steps involving a transacylase. BMP its unusual sn-1;sn-1′ structural configuration (based on the phosphate-linked glycerol carbon), which is not observed in other phospholipids. This unusual configuration is thought to play a role in the resistance of BMP to many phospholipases, and its stability in late endosomes/lysosomes. BMP stimulates the degradation of glycosphingolipids in coordination with lipid binding proteins (saposins) in lysosomes. PMID:25795792 BMP LBPA bis(monoacylglycerol) hydrogen phosphate lysobisphosphatidic acid PMID:22960355 CHEBI:60832 Any substance that interacts with tubulin to inhibit or promote polymerisation of microtubules. tubulin modulators tubulin modulator CHEBI:61015 A poison that interferes with the function of the kidneys. nephrotoxins nephrotoxin CHEBI:61115 An EC 3.5.1.* (non-peptide linear amide C-N hydrolase) inhibitor that interferes with the function of histone deacetylase (EC 3.5.1.98). EC 3.5.1.98 (histone deacetylase) inhibitors EC 3.5.1.98 inhibitor EC 3.5.1.98 inhibitors HDAC inhibitor HDAC inhibitors HDACi HDACis HDI HDIs histone amidohydrolase inhibitor histone amidohydrolase inhibitors histone deacetylase (EC 3.5.1.98) inhibitor histone deacetylase (EC 3.5.1.98) inhibitors histone deacetylase inhibitor histone deacetylase inhibitors EC 3.5.1.98 (histone deacetylase) inhibitor CHEBI:61697 Any organic molecular entity derived from a fatty acid. FA derivative fatty acid derivative CHEBI:61910 A fatty acyl-CoA in which the fatty acyl group has a chain length greater than C22. VLCFA-CoA very long-chain fatty acyl-CoA CHEBI:61951 Any substance that interacts with tubulin to inhibit polymerisation of microtubules. PMID:17099073 microtubule destabilising agent microtubule destabilising agents microtubule destabilising role microtubule destabilizing role microtubule-destabilising agents microtubule-destabilizing agent microtubule-destabilizing agents microtubule-destabilising agent PMID:17099073 Europe PMC CHEBI:62434 An EC 2.7.10.* (protein-tyrosine kinase) inhibitor that interferes with the action of receptor protein-tyrosine kinase (EC 2.7.10.1). AATK inhibitor AATYK inhibitor AATYK2 inhibitor AATYK3 inhibitor ACH inhibitor ALK inhibitor ALK inhibitors ARK inhibitor ATP:[protein]-L-tyrosine O-phosphotransferase (receptor-type) inhibitor ATP:[protein]-L-tyrosine O-phosphotransferase (receptor-type) inhibitors AXL inhibitor BRT inhibitor Bek inhibitor Bfgfr inhibitor Bsk inhibitor C-FMS inhibitor CAK inhibitor CCK4 inhibitor CD115 inhibitor CD135 inhibitor CDw135 inhibitor CFD1 inhibitor CKIT inhibitor CSF1R inhibitor Cek1 inhibitor Cek10 inhibitor Cek11 inhibitor Cek2 inhibitor Cek3 inhibitor Cek5 inhibitor Cek6 inhibitor Cek7 inhibitor DAlk inhibitor DDR1 inhibitor DDR2 inhibitor DKFZp434C1418 inhibitor DRT inhibitor DTK inhibitor Dek inhibitor Drosophila Eph kinase inhibitor EC 2.7.10.1 (receptor protein-tyrosine kinase) inhibitors EC 2.7.10.1 inhibitor EC 2.7.10.1 inhibitors ECK inhibitor EDDR1 inhibitor EGFR inhibitor EPH inhibitor EPHA1 inhibitor EPHA2 inhibitor EPHA6 inhibitor EPHA7 inhibitor EPHA8 inhibitor EPHB1 inhibitor EPHB2 inhibitor EPHB3 inhibitor EPHB4 inhibitor EPHT inhibitor EPHT2 inhibitor EPHT3 inhibitor EPHX inhibitor ERBB inhibitor ERBB1 inhibitor ERBB2 inhibitor ERBB3 inhibitor ERBB4 inhibitor ERK inhibitor Ebk inhibitor Eek inhibitor Ehk2 inhibitor Ehk3 inhibitor Elk inhibitor EphB5 inhibitor Eyk inhibitor FGFR1 inhibitor FGFR2 inhibitor FGFR3 inhibitor FGFR4 inhibitor FLG inhibitor FLK1 inhibitor FLK2 inhibitor FLT1 inhibitor FLT2 inhibitor FLT3 inhibitor FLT4 inhibitor FMS inhibitor Fv2 inhibitor HBGFR inhibitor HEK11 inhibitor HEK2 inhibitor HEK3 inhibitor HEK5 inhibitor HEK6 inhibitor HEP inhibitor HER2 inhibitor HER3 inhibitor HER4 inhibitor HGFR inhibitor HSCR1 inhibitor HTK inhibitor IGF1R inhibitor INSR inhibitor INSRR inhibitor IR inhibitor IRR inhibitor JTK12 inhibitor JTK13 inhibitor JTK14 inhibitor JWS inhibitor K-SAM inhibitor KDR inhibitor KGFR inhibitor KIA0641 inhibitor KIAA1079 inhibitor KIAA1459 inhibitor KIT inhibitor KLG inhibitor Kil inhibitor Kin15 inhibitor Kin16 inhibitor LTK inhibitor MCF3 inhibitor MEN2A/B inhibitor MER inhibitor MERTK inhibitor MEhk1 inhibitor MST1R inhibitor MTC1 inhibitor MUSK inhibitor Mdk1 inhibitor Mdk2 inhibitor Mdk5 inhibitor Mep inhibitor Mlk1 inhibitor Mlk2 inhibitor Mrk inhibitor Myk1 inhibitor N-SAM inhibitor NEP inhibitor NET inhibitor NGL inhibitor NOK inhibitor NTRK1 inhibitor NTRK2 inhibitor NTRK3 inhibitor NTRK4 inhibitor NTRKR1 inhibitor NTRKR2 inhibitor NTRKR3 inhibitor NYK inhibitor Neu inhibitor Nsk2 inhibitor Nuk inhibitor PCL inhibitor PDGFR inhibitor PDGFRA inhibitor PDGFRB inhibitor PHB6 inhibitor PTK inhibitor PTK3 inhibitor PTK7 inhibitor RET inhibitor RON inhibitor ROR1 inhibitor ROR2 inhibitor ROS1 inhibitor RSE inhibitor RTK inhibitor RYK inhibitor SEA inhibitor SKY inhibitor STK inhibitor STK1 inhibitor Sek2 inhibitor Sek3 inhibitor Sek4 inhibitor Sfr inhibitor TEK inhibitor TIE inhibitor TIE1 inhibitor TIE2 inhibitor TIF inhibitor TKT inhibitor TRK inhibitor TRKA inhibitor TRKB inhibitor TRKC inhibitor TRKE inhibitor TYK1 inhibitor TYRO10 inhibitor TYRO3 inhibitor TYRO7 inhibitor Tyro11 inhibitor Tyro5 inhibitor Tyro6 inhibitor UFO inhibitor VEGFR1 inhibitor VEGFR2 inhibitor VEGFR3 inhibitor Vik inhibitor YK1 inhibitor Yrk inhibitor anaplastic lymphoma kinase inhibitor anaplastic lymphoma kinase inhibitors ephrin-B3 receptor tyrosine kinase inhibitor insulin receptor protein-tyrosine kinase inhibitor neurite outgrowth regulating kinase inhibitor nork inhibitor novel oncogene with kinase-domain inhibitor receptor protein tyrosine kinase inhibitor receptor protein-tyrosine kinase (EC 2.7.10.1) inhibitor receptor protein-tyrosine kinase (EC 2.7.10.1) inhibitors receptor protein-tyrosine kinase inhibitor receptor protein-tyrosine kinase inhibitors EC 2.7.10.1 (receptor protein-tyrosine kinase) inhibitor CHEBI:62872 An EC 1.2.3.* (oxidoreductase acting on donor aldehyde/oxo group with oxygen as acceptor) inhibitor which interferes with the action of aldehyde oxidase (EC 1.2.3.1). EC 1.2.3.1 (aldehyde oxidase) inhibitors EC 1.2.3.1 inhibitor EC 1.2.3.1 inhibitors aldehyde oxidase (EC 1.2.3.1) inhibitor aldehyde oxidase (EC 1.2.3.1) inhibitors aldehyde oxidase inhibitor aldehyde oxidase inhibitors aldehyde:oxygen oxidoreductase inhibitor aldehyde:oxygen oxidoreductase inhibitors quinoline oxidase inhibitor quinoline oxidase inhibitors retinal oxidase inhibitor retinal oxidase inhibitors retinoic acid synthase inhibitor retinoic acid synthase inhibitors EC 1.2.3.1 (aldehyde oxidase) inhibitor CHEBI:63090 An EC 2.4.2.* (pentosyltransferase) inhibitor that interferes with the action of purine nucleoside phosphorylase (EC 2.4.2.1). EC 2.4.2.1 (purine-nucleoside phosphorylase) inhibitors EC 2.4.2.1 inhibitor EC 2.4.2.1 inhibitors PNPase inhibitor PNPase inhibitors PUNPI inhibitor PUNPI inhibitors PUNPII inhibitor PUNPII inhibitors inosine phosphorylase inhibitor inosine phosphorylase inhibitors inosine-guanosine phosphorylase inhibitor inosine-guanosine phosphorylase inhibitors nucleotide phosphatase inhibitor nucleotide phosphatase inhibitors purine deoxynucleoside phosphorylase inhibitor purine deoxynucleoside phosphorylase inhibitors purine deoxyribonucleoside phosphorylase inhibitor purine deoxyribonucleoside phosphorylase inhibitors purine nucleoside phosphorylase inhibitor purine nucleoside phosphorylase inhibitors purine ribonucleoside phosphorylase inhibitor purine ribonucleoside phosphorylase inhibitors purine-nucleoside phosphorylase (EC 2.4.2.1) inhibitor purine-nucleoside phosphorylase (EC 2.4.2.1) inhibitors purine-nucleoside phosphorylase inhibitor purine-nucleoside phosphorylase inhibitors purine-nucleoside:phosphate ribosyltransferase inhibitor purine-nucleoside:phosphate ribosyltransferase inhibitors EC 2.4.2.1 (purine-nucleoside phosphorylase) inhibitor CHEBI:63247 The element or compound in a reduction-oxidation (redox) reaction that donates an electron to another species. Wikipedia:Reducing_agent reducer reductant reducing agent CHEBI:63248 A substance that removes electrons from another reactant in a redox reaction. oxidant oxidiser oxidizer oxidising agent CHEBI:6343 A secondary amino compound formally derived from ammonia by replacing two of the hydrogens by 2-(3-carbamoyl-4-hydroxyphenyl)-2-hydroxyethyl and 4-phenylbutan-2-yl groups. It is an adrenergic antagonist used to treat high blood pressure. Beilstein:2948416 CAS:36894-69-6 DrugBank:DB00598 Drug_Central:1531 LINCS:LSM-1282 PMID:21908132 PMID:22300487 PMID:22528277 PMID:23055089 PMID:28166217 Reaxys:2948416 2-hydroxy-5-{1-hydroxy-2-[(1-methyl-3-phenylpropyl)amino]ethyl}benzamide Labetalol 3-Carboxamido-4-hydroxy-alpha-((1-methyl-3-phenylpropylamino)methyl)benzyl alcohol 5-(1-Hydroxy-2-(1-methyl-3-phenylpropylamino)ethyl)salicylamide kabetalol labetalol labetalolum labetalol Beilstein:2948416 Beilstein CAS:36894-69-6 ChemIDplus Drug_Central:1531 DrugCentral PMID:21908132 Europe PMC PMID:22300487 Europe PMC PMID:22528277 Europe PMC PMID:23055089 Europe PMC PMID:28166217 Europe PMC Reaxys:2948416 Reaxys CHEBI:63581 A nucleoside analogue obtained by formal dehydration across positions 2 and 3 of thymidine. An inhibitor of HIV-1 reverse transcriptase C10H12N2O4 Cc1cn([C@@H]2O[C@H](CO)C=C2)c(=O)[nH]c1=O CAS:3056-17-5 DrugBank:DB00649 Drug_Central:2478 LINCS:LSM-5983 Reaxys:618327 Wikipedia:Stavudine 1-[(2R,5S)-5-(hydroxymethyl)-2,5-dihydrofuran-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione Stavudine d4T 1-(2,3-Dideoxy-beta-D-glycero-pent-2-enofuranosyl)thymine 2',3'-Didehydro-3'-deoxythimidine 3'-Deoxy-2'-thymidinene STV Sanilvudine d4T estavudina stavudine stavudinum stavudine CAS:3056-17-5 ChemIDplus Drug_Central:2478 DrugCentral Reaxys:618327 Reaxys CHEBI:63589 An aminopyrimidine that consists of 2,6-diaminopyrimidine bearing a bromo substituent at position 5, a 4-cyano-2,6-dimethylphenoxy substituent at position 4 and having a 4-cyanophenyl substituent attached to the 2-amino group. NNRTI of HIV-1, binds directly to RT and blocks RNA-dependent and DNA-dependent DNA polymerase activities CAS:269055-15-4 DrugBank:DB06414 PMID:21114458 PMID:21142266 PMID:21173188 PMID:21189339 PMID:21383098 PMID:21464253 PMID:21557669 PMID:21600016 PMID:21637112 PMID:21881478 PMID:22011983 PMID:22089378 PMID:22190606 PMID:25017682 Reaxys:8945855 4-({6-amino-5-bromo-2-[(4-cyanophenyl)amino]pyrimidin-4-yl}oxy)-3,5-dimethylbenzonitrile etravirine etravirine CAS:269055-15-4 ChemIDplus PMID:21114458 Europe PMC PMID:21142266 Europe PMC PMID:21173188 Europe PMC PMID:21189339 Europe PMC PMID:21383098 Europe PMC PMID:21464253 Europe PMC PMID:21557669 Europe PMC PMID:21600016 Europe PMC PMID:21637112 Europe PMC PMID:21881478 Europe PMC PMID:22011983 Europe PMC PMID:22089378 Europe PMC PMID:22190606 Europe PMC PMID:25017682 Europe PMC Reaxys:8945855 Reaxys CHEBI:63598 An optically active form of ofloxacin having (S)-configuration; an inhibitor of bacterial topoisomerase IV and DNA gyrase CAS:100986-85-4 DrugBank:DB01137 Drug_Central:1569 LINCS:LSM-5270 PMID:21075586 PMID:21965436 PMID:21974858 PMID:22088660 PMID:22221614 Reaxys:5385660 (3S)-9-fluoro-3-methyl-10-(4-methylpiperazin-1-yl)-7-oxo-2,3-dihydro-7H-[1,4]oxazino[2,3,4-ij]quinoline-6-carboxylic acid (-)-Ofloxacin (3S)-(-)-9-fluoro-3-methyl-10-(4-methyl-1-piperazinyl)-7-oxo-2,3-dihydro-7H-pyrido[1,2,3-de][1,4]benzoxazine-6-carboxylic acid (S)-(-)-9-fluoro-3-methyl-10-(4-methyl-1-piperazinyl)-7-oxo-2,3-dihydro-7H-pyrido[1,2,3-de][1,4]benzooxazine-6-carboxylic acid (S)-9-Fluoro-2,3-dihydro-3-methyl-10-(4-methyl-1-piperazinyl)-7-oxo-7H-pyrido(1,2,3-de)-1,4-benzoxazine-6-carboxylic acid (S)-Ofloxacin L-Ofloxacin Ofloxacin S-(-)-form levofloxacin levofloxacine levofloxacino levofloxacinum levofloxacin CAS:100986-85-4 ChemIDplus Drug_Central:1569 DrugCentral PMID:21075586 Europe PMC PMID:21965436 Europe PMC PMID:21974858 Europe PMC PMID:22088660 Europe PMC PMID:22221614 Europe PMC Reaxys:5385660 Reaxys CHEBI:63608 A monocarboxylic acid amide obtained by formal condensation of the carboxy group of 4,4-difluorocyclohexanecarboxylic acid and the primary amino group of (1S)-3-[(3-exo)-3-(3-isopropyl-5-methyl-4H-1,2,4-triazol-4-yl)-8-azabicyclo[3.2.1]oct-8-yl]-1-phenylpropylamine. An antiretroviral drug, it prevents the interaction of HIV-1 gp120 and chemokine receptor 5 (CCR5) necessary for CCR5-tropic HIV-1 to enter cells. CAS:376348-65-1 DrugBank:DB04835 PMID:21134404 PMID:21383098 PMID:21393136 PMID:21505306 PMID:21595497 PMID:21692669 PMID:21987241 PMID:22017448 PMID:22034870 PMID:22064539 PMID:22090117 PMID:22118500 PMID:22174038 PMID:22236118 PMID:22247337 PMID:24419064 PMID:24651825 PMID:24652492 PMID:25017682 Reaxys:10131963 4,4-difluoro-N-{(1S)-3-[(3-exo)-3-(3-isopropyl-5-methyl-4H-1,2,4-triazol-4-yl)-8-azabicyclo[3.2.1]oct-8-yl]-1-phenylpropyl}cyclohexanecarboxamide maraviroc maravirocum maraviroc CAS:376348-65-1 ChemIDplus PMID:21134404 Europe PMC PMID:21383098 Europe PMC PMID:21393136 Europe PMC PMID:21505306 Europe PMC PMID:21595497 Europe PMC PMID:21692669 Europe PMC PMID:21987241 Europe PMC PMID:22017448 Europe PMC PMID:22034870 Europe PMC PMID:22064539 Europe PMC PMID:22090117 Europe PMC PMID:22118500 Europe PMC PMID:22174038 Europe PMC PMID:22236118 Europe PMC PMID:22247337 Europe PMC PMID:24419064 Europe PMC PMID:24651825 Europe PMC PMID:24652492 Europe PMC PMID:25017682 Europe PMC Reaxys:10131963 Reaxys CHEBI:63613 A dipyridodiazepine that is 5,11-dihydro-6H-dipyrido[3,2-b:2',3'-e][1,4]diazepine which is substituted by methyl, oxo, and cyclopropyl groups at positions 4, 6, and 11, respectively. A non-nucleoside reverse transcriptase inhibitor with activity against HIV-1, it is used in combination with other antiretrovirals for the treatment of HIV infection. CAS:129618-40-2 DrugBank:DB00238 LINCS:LSM-5336 PMID:1712395 PMID:25017682 PMID:28782122 PMID:28786740 PMID:28819312 PMID:28827836 PMID:28835669 Reaxys:4757598 11-cyclopropyl-4-methyl-5,11-dihydro-6H-dipyrido[3,2-b:2',3'-e][1,4]diazepin-6-one Nevirapine 11-cyclopropyl-5,11-dihydro-4-methyl-6H-dipyrido(3,2-b:2',3'-e)(1,4)diazepin-6-one NEV NVP Viramune nevirapine nevirapine CAS:129618-40-2 ChemIDplus PMID:1712395 Europe PMC PMID:25017682 Europe PMC PMID:28782122 Europe PMC PMID:28786740 Europe PMC PMID:28819312 Europe PMC PMID:28827836 Europe PMC PMID:28835669 Europe PMC Reaxys:4757598 Reaxys CHEBI:63628 A pyridine-2-sulfonamide substituted at C-5 by a trifluoromethyl group and at the sulfonamide nitrogen by a dihydropyrone-containing m-tolyl substituent. It is an HIV-1 protease inhibitor. CAS:174484-41-4 DrugBank:DB00932 PMID:17620375 PMID:20368406 PMID:21041916 PMID:21571982 PMID:21576452 PMID:21825300 PMID:21871444 PMID:22007990 PMID:22096044 PMID:22258921 PMID:25017682 Reaxys:7698323 N-(3-{(1R)-1-[(6R)-4-hydroxy-2-oxo-6-(2-phenylethyl)-6-propyl-5,6-dihydro-2H-pyran-3-yl]propyl}phenyl)-5-(trifluoromethyl)pyridine-2-sulfonamide 3'-((1R)-1-((6R)-5,6-Dihydro-4-hydroxy-2-oxo-6-phenethyl-6-propyl-2H-pyran-3-yl)propyl)-5-(trifluoromethyl)-2-pyridinesulfonanilide tipranavir tipranavir CAS:174484-41-4 ChemIDplus PMID:17620375 Europe PMC PMID:20368406 Europe PMC PMID:21041916 Europe PMC PMID:21571982 Europe PMC PMID:21576452 Europe PMC PMID:21825300 Europe PMC PMID:21871444 Europe PMC PMID:22007990 Europe PMC PMID:22096044 Europe PMC PMID:22258921 Europe PMC PMID:25017682 Europe PMC Reaxys:7698323 Reaxys CHEBI:63629 2,1,3-Benzothiadiazole substituted at C-4 by a Delta(1)-imidazolin-2-ylamino group and at C-4 by a chloro group. It is an agonist at alpha2-adrenergic receptor sites. Beilstein:618691 CAS:51322-75-9 DrugBank:DB00697 Drug_Central:2683 LINCS:LSM-5242 PMID:21317414 PMID:21733633 PMID:21982341 PMID:22196407 PMID:22223284 Reaxys:618691 5-chloro-N-(4,5-dihydro-1H-imidazol-2-yl)-2,1,3-benzothiadiazol-4-amine Tizanidine 5-Chloro-4-(2-imidazolin-2-ylamino)-2,1,3-benzothiadiazole tizanidina tizanidine tizanidinum tizanidine Beilstein:618691 ChemIDplus CAS:51322-75-9 ChemIDplus Drug_Central:2683 DrugCentral PMID:21317414 Europe PMC PMID:21733633 Europe PMC PMID:21982341 Europe PMC PMID:22196407 Europe PMC PMID:22223284 Europe PMC Reaxys:618691 Reaxys CHEBI:63630 Benzophenone substituted on one of the phenyl rings at C-3 and C-4 by hydroxy groups and at C-5 by a nitro group, and on the other phenyl ring by a methyl group at C-4. It is an inhibitor of catechol O-methyltransferase. DrugBank:DB00323 Drug_Central:2697 LINCS:LSM-5282 PMID:20381177 PMID:20502133 PMID:21521027 PMID:22136163 Reaxys:8151577 (3,4-dihydroxy-5-nitrophenyl)(4-methylphenyl)methanone 3,4-Dihydroxy-4'-methyl-5-nitrobenzophenone 3,4-dihydroxy-4'-methyl-5-nitrobenzophenone 3,4-dihydroxy-5-nitro-4'-methylbenzophenone 4'-methyl-3,4-dihydroxy-5-nitrobenzophenone tolcapone tolcapone Drug_Central:2697 DrugCentral PMID:20381177 Europe PMC PMID:20502133 Europe PMC PMID:21521027 Europe PMC PMID:22136163 Europe PMC Reaxys:8151577 Reaxys CHEBI:6367 A member of the class of 1,2,4-triazines in which the triazene skeleton is substituted by amino groups at positions 3 and 5, and by a 2,3-dichlorophenyl group at position 6. CAS:84057-84-1 DrugBank:DB00555 Drug_Central:1540 LINCS:LSM-4104 PMID:20825390 PMID:21242744 Reaxys:7589268 6-(2,3-dichlorophenyl)-1,2,4-triazine-3,5-diamine 3,5-diamino-6-(2,3-dichlorophenyl)-1,2,4-triazine Lamictal lamotrigina lamotrigine lamotriginum lamotrigine CAS:84057-84-1 ChemIDplus CAS:84057-84-1 NIST Chemistry WebBook Drug_Central:1540 DrugCentral PMID:20825390 Europe PMC PMID:21242744 Europe PMC Reaxys:7589268 Reaxys CHEBI:63673 An antogonist that blocks chemokine receptor 5 (CCR5). CCR-5 antagonist CCR-5 antagonists CCR5 antagonist CCR5 antagonists chemokine receptor 5 antagonists chemokine receptor 5 antagonist CHEBI:63726 Any compound that can be used for the treatment of neurodegenerative disorders. neuroprotectant neuroprotectants neuroprotective agents neuroprotective agent CHEBI:63924 C18H23NO6 [H][C@@]12[C@H]3CCN1CC=C2COC(=O)[C@@](O)(CO)C(=C)C\C(=C\C)C(=O)O3 A macrolide that is 13,19-didehydrosenecionan bearing two additional hydroxy substituents at positions 12 and 18 as well as two additional oxo groups at positions 11 and 16. CAS:23246-96-0 (15Z)-12,18-dihydroxy-13,19-didehydrosenecionan-11,16-dione riddelliine CHEBI:63951 An agonist at the estrogen receptor. estrogen receptor agonist CHEBI:64018 An agonist that selectively binds to and activates a protein kinase C receptor protein kinase C agonists protein kinase C agonist CHEBI:6402 A monocarboxylic acid amide obtained by formal condensation of the carboxy group of 5-methyl-1,2-oxazole-4-carboxylic acid with the anilino group of 4-(trifluoromethyl)aniline. The prodrug of teriflunomide. Beilstein:4323174 CAS:75706-12-6 DrugBank:DB01097 Drug_Central:1552 LINCS:LSM-3771 PMID:10515382 PMID:10702725 PMID:10890256 PMID:11043056 PMID:11053058 PMID:11067959 PMID:11271257 PMID:11333342 PMID:11340750 PMID:11391470 PMID:11475244 PMID:11522581 PMID:11707749 PMID:11718154 PMID:11876141 PMID:11884931 PMID:11994686 PMID:12017890 PMID:12074690 PMID:12833393 PMID:14622739 PMID:15030575 PMID:15127968 PMID:15127974 PMID:15188371 PMID:15214907 PMID:15385935 PMID:15489872 PMID:15537652 PMID:15652966 PMID:15665760 PMID:15789891 PMID:15899055 PMID:15934905 PMID:16106593 PMID:16142756 PMID:16202258 PMID:16284916 PMID:16638062 PMID:16638420 PMID:16645972 PMID:16688677 PMID:16769661 PMID:16778342 PMID:17366662 PMID:17604599 PMID:17646975 PMID:17854740 PMID:18034546 PMID:18173611 PMID:18413415 PMID:18496682 PMID:18663553 PMID:18688040 PMID:19169882 PMID:19190124 PMID:19344337 PMID:19581389 PMID:19715969 PMID:19751817 PMID:19770782 PMID:7496341 PMID:7676489 PMID:8610393 PMID:9075844 PMID:9123314 PMID:9625011 PMID:9777697 Reaxys:4323174 5-methyl-N-[4-(trifluoromethyl)phenyl]-1,2-oxazole-4-carboxamide Leflunomide 5-Methyl-N-(4-(trifluoromethyl)phenyl)-4-isoxazolecarboxamide 5-Methylisoxazole-4-carboxylic acid (4-trifluoromethyl)anilide Arava alpha,alpha,alpha-Trifluoro-5-methyl-4-isoxazolecarboxy-p-toluidide leflunomida leflunomide leflunomidum leflunomide Beilstein:4323174 Beilstein CAS:75706-12-6 ChemIDplus Drug_Central:1552 DrugCentral PMID:10515382 Europe PMC PMID:10702725 Europe PMC PMID:10890256 Europe PMC PMID:11043056 Europe PMC PMID:11053058 Europe PMC PMID:11067959 Europe PMC PMID:11271257 Europe PMC PMID:11333342 Europe PMC PMID:11340750 Europe PMC PMID:11391470 Europe PMC PMID:11475244 Europe PMC PMID:11522581 Europe PMC PMID:11707749 Europe PMC PMID:11718154 Europe PMC PMID:11876141 Europe PMC PMID:11884931 Europe PMC PMID:11994686 Europe PMC PMID:12017890 Europe PMC PMID:12074690 Europe PMC PMID:12833393 Europe PMC PMID:14622739 Europe PMC PMID:15030575 Europe PMC PMID:15127968 Europe PMC PMID:15127974 Europe PMC PMID:15188371 Europe PMC PMID:15214907 Europe PMC PMID:15385935 Europe PMC PMID:15489872 Europe PMC PMID:15537652 Europe PMC PMID:15652966 Europe PMC PMID:15665760 Europe PMC PMID:15789891 Europe PMC PMID:15899055 Europe PMC PMID:15934905 Europe PMC PMID:16106593 Europe PMC PMID:16142756 Europe PMC PMID:16202258 Europe PMC PMID:16284916 Europe PMC PMID:16638062 Europe PMC PMID:16638420 Europe PMC PMID:16645972 Europe PMC PMID:16688677 Europe PMC PMID:16769661 Europe PMC PMID:16778342 Europe PMC PMID:17366662 Europe PMC PMID:17604599 Europe PMC PMID:17646975 Europe PMC PMID:17854740 Europe PMC PMID:18034546 Europe PMC PMID:18173611 Europe PMC PMID:18413415 Europe PMC PMID:18496682 Europe PMC PMID:18663553 Europe PMC PMID:18688040 Europe PMC PMID:19169882 Europe PMC PMID:19190124 Europe PMC PMID:19344337 Europe PMC PMID:19581389 Europe PMC PMID:19715969 Europe PMC PMID:19751817 Europe PMC PMID:19770782 Europe PMC PMID:7496341 Europe PMC PMID:7676489 Europe PMC PMID:8610393 Europe PMC PMID:9075844 Europe PMC PMID:9123314 Europe PMC PMID:9625011 Europe PMC PMID:9777697 Europe PMC Reaxys:4323174 Reaxys CHEBI:64106 An agonist that selectively binds to and activates a protein kinase receptor. protein kinase agonists protein kinase agonist CHEBI:64152 Any protease inhibitor that restricts the action of a cysteine protease. cysteine protease inhibitors cysteine proteinase inhibitor cysteine proteinase inhibitors システインプロテアーゼ 阻害ロール CHEBI:64297 Any chemical substance produced during the conversion of a reactant to a product. Wikipedia:Reaction_intermediate reaction intermediate CHEBI:64355 An N-arylpiperazine that consists of piperazine carrying two 4-substituted phenyl groups at positions 1 and 4. A triazole antifungal drug. CAS:171228-49-2 DrugBank:DB01263 Drug_Central:3483 PMID:21762211 PMID:21967490 PMID:22058198 PMID:22176629 PMID:22215361 PMID:22215487 PMID:22286158 PMID:22290952 PMID:22303909 PMID:22324990 PMID:22330929 PMID:22380765 PMID:22391464 PMID:22391534 PMID:22427614 Reaxys:8379448 2,5-anhydro-1,3,4-trideoxy-2-(2,4-difluorophenyl)-4-({4-[4-(4-{1-[(2S,3S)-2-hydroxypentan-3-yl]-5-oxo-1,5-dihydro-4H-1,2,4-triazol-4-yl}phenyl)piperazin-1-yl]phenoxy}methyl)-1-(1H-1,2,4-triazol-1-yl)-D-threo-pentitol Noxafil SCH56592 Sch 56592 Schering 56592 posaconazole posaconazole CAS:171228-49-2 ChemIDplus Drug_Central:3483 DrugCentral PMID:21762211 Europe PMC PMID:21967490 Europe PMC PMID:22058198 Europe PMC PMID:22176629 Europe PMC PMID:22215361 Europe PMC PMID:22215487 Europe PMC PMID:22286158 Europe PMC PMID:22290952 Europe PMC PMID:22303909 Europe PMC PMID:22324990 Europe PMC PMID:22330929 Europe PMC PMID:22380765 Europe PMC PMID:22391464 Europe PMC PMID:22391534 Europe PMC PMID:22427614 Europe PMC Reaxys:8379448 Reaxys CHEBI:64370 A neurotransmitter transporter modulator that activates glutamate transporters. excitatory amino-acid transporter activator excitatory amino-acid transporter activators glutamate transporter activators glutamate transporter activator CHEBI:64371 A membrane transport modulator that affects the transport of neurotransmitters. neurotransmitter transporter modulators neurotransmitter transporter modulator CHEBI:64482 A glycerophosphocholine that is glycero-3-phosphocholine bearing two acyl substituents at positions 1 and 2. phosphatidylcholine CHEBI:64583 Any of a class of phospholipids in which the amino group of a sphingoid base is in amide linkage with one of several fatty acids, while the terminal hydroxy group of the sphingoid base is esterified to phosphorylcholine. Ceramide phosphocholine sphingomyelin CHEBI:64909 Any substance that causes disturbance to organisms by chemical reaction or other activity on the molecular scale, when a sufficient quantity is absorbed by the organism. Wikipedia:Poison poisonous agent poisonous agents poisonous substance poisonous substances poisons toxic agent toxic agents toxic substance toxic substances poison CHEBI:64911 Any compound that inhibits cell division (mitosis). antimitotics mitosis inhibitor mitosis inhibitors mitotic inhibitor mitotic inhibitors antimitotic CHEBI:64912 A drug used to treat or prevent infections caused by Mycobacteria, a genus of actinobacteria. Aerobic and nonmotile, members of the genus include the pathogens responsible for causing tuberculosis and leprosy. antimycobacterial agent antimycobacterial agents antimycobacterial drugs antimycobacterials antimycobacterium antimycobacterial drug CHEBI:64915 An antiparasitic drug which is effective against Apicomplexan parasites in the genus Plasmodium. The genus contains over 200 species and includes those responsible for malaria. antiplasmodial agent antiplasmodial agents antiplasmodial drugs antiplasmodium agent antiplasmodium agents antiplasmodium drug antiplasmodium drugs antiplasmodial drug CHEBI:64926 Any protease inhibitor that restricts the action of a serine protease. serine protease inhibitors serine proteinase inhibitor serine proteinase inhibitors serine protease inhibitor CHEBI:64932 A cysteine protease inhibitor which inhibits cathepsin B (EC 3.4.22.1). cathepsin B inhibitor CHEBI:64946 An antiviral agent that destroys or inhibits the replication of the human immunodeficiency virus. anti-AIDS agent anti-AIDS agents anti-HIV agents anti-HIV agent CHEBI:64947 An anti-HIV agent that destroys or inhibits the replication of HIV-1, the more infective and more virulent of the two types of HIV virus. anti-HIV-1 agents anti-HTLV-III agent anti-HTLV-III agents anti-LAV agent anti-LAV agents anti-HIV-1 agent CHEBI:6495 A clathrate complex consisting of a lipid enwrapped in a protein host without covalent binding in such a way that the complex has a hydrophilic outer surface consisting of all the protein and the polar ends of any phospholipids. lipoprotein CHEBI:64964 A lipoxygenase inhibitor that interferes with the action of arachidonate 5-lipoxygenase (EC 1.13.11.34). 5-LOX inhibitor 5-LOX inhibitors 5-lipoxygenase inhibitor 5-lipoxygenase inhibitors 5delta-lipoxygenase inhibitor 5delta-lipoxygenase inhibitors C-5-lipoxygenase inhibitor C-5-lipoxygenase inhibitors EC 1.13.11.34 (arachidonate 5-lipoxygenase) inhibitors EC 1.13.11.34 inhibitor EC 1.13.11.34 inhibitors LTA synthase inhibitor LTA synthase inhibitors arachidonate 5-lipoxygenase (EC 1.13.11.34) inhibitor arachidonate 5-lipoxygenase (EC 1.13.11.34) inhibitors arachidonate 5-lipoxygenase inhibitor arachidonate 5-lipoxygenase inhibitors arachidonic 5-lipoxygenase inhibitor arachidonic 5-lipoxygenase inhibitors arachidonic acid 5-lipoxygenase inhibitor arachidonic acid 5-lipoxygenase inhibitors delta(5)-lipoxygenase inhibitor delta(5)-lipoxygenase inhibitors leukotriene A4 synthase inhibitor leukotriene A4 synthase inhibitors leukotriene-A4 synthase inhibitor leukotriene-A4 synthase inhibitors EC 1.13.11.34 (arachidonate 5-lipoxygenase) inhibitor CHEBI:65001 Any EC 3.1.1.* (carboxylic ester hydrolase) inhibitor that inhibits the action of triacylglycerol lipase (EC 3.1.1.3). EC 3.1.1.3 (triacylglycerol lipase) inhibitors EC 3.1.1.3 inhibitor EC 3.1.1.3 inhibitors GEH inhibitor GEH inhibitors PPL inhibitor PPL inhibitors Tween hydrolase inhibitor Tween hydrolase inhibitors Tweenase inhibitor Tweenase inhibitors Tweenesterase inhibitor Tweenesterase inhibitors butyrinase inhibitor butyrinase inhibitors cacordase inhibitor cacordase inhibitors capalase L inhibitor capalase L inhibitors glycerol ester hydrolase inhibitor glycerol ester hydrolase inhibitors glycerol-ester hydrolase inhibitor glycerol-ester hydrolase inhibitors heparin releasable hepatic lipase inhibitor heparin releasable hepatic lipase inhibitors hepatic lipase inhibitor hepatic lipase inhibitors hepatic monoacylglycerol acyltransferase inhibitor hepatic monoacylglycerol acyltransferase inhibitors lipase inhibitor lipase inhibitors lipazin inhibitor lipazin inhibitors liver lipase inhibitor liver lipase inhibitors pancreatic lipase inhibitor pancreatic lipase inhibitors pancreatic triacylglycerol lipase inhibitor pancreatic triacylglycerol lipase inhibitors post-heparin plasma protamine-resistant lipase inhibitor post-heparin plasma protamine-resistant lipase inhibitors salt-resistant post-heparin lipase inhibitor salt-resistant post-heparin lipase inhibitors steapsin inhibitor steapsin inhibitors triacetinase inhibitor triacetinase inhibitors triacylglycerol ester hydrolase inhibitor triacylglycerol ester hydrolase inhibitors triacylglycerol lipase (EC 3.1.1.3) inhibitor triacylglycerol lipase (EC 3.1.1.3) inhibitors triacylglycerol lipase inhibitor triacylglycerol lipase inhibitors tributyrase inhibitor tributyrase inhibitors tributyrin esterase inhibitor tributyrin esterase inhibitors tributyrinase inhibitor tributyrinase inhibitors triglyceridase inhibitor triglyceridase inhibitors triglyceride hydrolase inhibitor triglyceride hydrolase inhibitors triglyceride lipase inhibitor triglyceride lipase inhibitors triolein hydrolase inhibitor triolein hydrolase inhibitors tween-hydrolysing esterase inhibitor tween-hydrolyzing esterase inhibitors EC 3.1.1.3 (triacylglycerol lipase) inhibitor CHEBI:65023 Any compound that has anti-asthmatic effects. anti-asthmatic agents antiasthmatic agent antiasthmatic agents anti-asthmatic agent CHEBI:65172 A member of the class of azetidines that is melagatran in which the carboxylic acid group has been converted to the corresponding ethyl ester and in which the amidine group has been converted into the corresponding amidoxime. A prodrug for melagatran, ximelagatran was the first orally available direct thrombin inhibitor to be brought to market as an anticoagulant, but was withdrawn in 2006 following reports of it causing liver damage. CAS:192939-46-1 DrugBank:DB04898 Drug_Central:2852 PMID:12846595 PMID:15487959 PMID:16084146 PMID:16106594 PMID:16123912 PMID:16511607 PMID:16767816 PMID:17319469 PMID:17636192 PMID:19028773 PMID:20020269 PMID:28338626 Reaxys:14559655 ethyl N-{(1R)-1-cyclohexyl-2-[(2S)-2-{[4-(N'-hydroxycarbamimidoyl)benzyl]carbamoyl}azetidin-1-yl]-2-oxoethyl}glycinate Exanta Exarta H 376-95 H 376/95 H 37695 ethyl 2-[[(1R)-1-cyclohexyl-2- [(2S)-2-[[4-(N'-hydroxycarbamimidoyl) phenyl]methylcarbamoyl]azetidin-1-yl]- 2-oxo-ethyl]amino]acetate ximelagatran ximelagatran (oxime form) ximelagatranum ximelagatran CAS:192939-46-1 ChemIDplus DrugBank:DB04898 SUBMITTER Drug_Central:2852 DrugCentral PMID:12846595 Europe PMC PMID:15487959 Europe PMC PMID:16084146 Europe PMC PMID:16106594 Europe PMC PMID:16123912 Europe PMC PMID:16511607 Europe PMC PMID:16767816 Europe PMC PMID:17319469 Europe PMC PMID:17636192 Europe PMC PMID:19028773 Europe PMC PMID:20020269 Europe PMC PMID:28338626 Europe PMC Reaxys:14559655 Reaxys CHEBI:65191 Antipsychotic drugs which can have different modes of action but which tend to be less likely than first generation antipsychotics to cause extrapyramidal motor control disabilities such as body rigidity or Parkinson's disease-type movements. Antipsychotic drugs which can have different modes of action but which tend to be less likely than first generation antipsychotics to cause extrapyramidal motor control disabilities such as body rigidity or Parkinson's disease-type movements. atypical antipsychotic atypical antipsychotic agent atypical antipsychotic agents atypical antipsychotic drug atypical antipsychotic drugs atypical antipsychotics second generation antipsychotic agent second generation antipsychotic agents second generation antipsychotic drug second generation antipsychotic drugs second generation antipsychotics second generation antipsychotic CHEBI:65207 An antagonist at the vascular endothelial growth factor receptor. VEGF receptor inhibitor VEGF receptor inhibitors VEGFR inhibitor VEGFR inhibitors vascular endothelial growth factor receptor antagonists vascular endothelial growth factor receptor inhibitor vascular endothelial growth factor receptor inhibitors vascular endothelial growth factor receptor antagonist CHEBI:65232 An EC 3.4.21.* (serine endopeptidase) inhibitor that interferes with the action of thrombin (EC 3.4.21.5). E thrombin inhibitor E thrombin inhibitors EC 3.4.21.5 (thrombin) inhibitors EC 3.4.21.5 inhibitor EC 3.4.21.5 inhibitors activated blood-coagulation factor II inhibitor activated blood-coagulation factor II inhibitors beta-thrombin inhibitor beta-thrombin inhibitors blood-coagulation factor IIa inhibitor blood-coagulation factor IIa inhibitors factor IIa inhibitor factor IIa inhibitors fibrinogenase inhibitor fibrinogenase inhibitors gamma-thrombin inhibitor gamma-thrombin inhibitors thrombase inhibitor thrombase inhibitors thrombin (EC 3.4.21.5) inhibitor thrombin (EC 3.4.21.5) inhibitors thrombin inhibitor thrombin inhibitors thrombin-C inhibitor thrombin-C inhibitors thrombofort inhibitor thrombofort inhibitors tropostasin inhibitor tropostasin inhibitors EC 3.4.21.5 (thrombin) inhibitor CHEBI:65259 A compound that inhibits the action of gamma-aminobutyric acid. GABA antagonists gamma-aminobutyric acid receptor antagonist gamma-aminobutyric acid receptor antagonists GABA antagonist CHEBI:66919 A pyrazole substituted at position 1 by a 2-cyano-1-cyclopentylethyl group and at position 3 by a pyrrolo[2,3-d]pyrimidin-4-yl group. Used as the phosphate salt for the treatment of patients with intermediate or high-risk myelofibrosis, including primary myelofibrosis, post-polycythemia vera myelofibrosis and post-essential thrombocythemia myelofibrosis. C17H18N6 InChI=1S/C17H18N6/c18-7-5-15(12-3-1-2-4-12)23-10-13(9-22-23)16-14-6-8-19-17(14)21-11-20-16/h6,8-12,15H,1-5H2,(H,19,20,21)/t15-/m1/s1 N#CC[C@H](C1CCCC1)n1cc(cn1)-c1ncnc2[nH]ccc12 CAS:941678-49-5 ruxolitinib CHEBI:66956 Any compound which can be used to treat or alleviate the symptoms of dyskinesia. antidyskinesia agents antidyskinesia drug antidyskinesia drugs antidyskinetic agent antidyskinetic agents antidyskinetic drug antidyskinetic drugs antidyskinesia agent CHEBI:66987 radiation protective agent CHEBI:66991 Any compound which inhibits the postganglionic functioning of the sympathetic nervous system (SNS). sympatholytic sympatholytic agents sympatholytic drug sympatholytic drugs sympatholytics sympatholytic agent CHEBI:66993 Any compound used to suppress premature labour and immature birth by suppressing uterine contractions. anti-contraction drug anti-contraction drugs anti-contraction medication anti-contraction medications labour repressant labour repressants tocolytic tocolytic agents tocolytic drug tocolytic drugs tocolytics tocolytic agent CHEBI:67079 Any compound that has anti-inflammatory effects. anti-inflammatory agent CHEBI:67105 A chemosterilant intended to sterilize insects. insect chemosterilant insect chemosterilants insect sterilants insect sterilant CHEBI:67114 A ryanodine receptor modulator which activates the receptor. Ryanodine receptors (RyRs) act as selective ion channels, modulating the release of calcium. Activating the receptors causes the release of calcium, so depleting internal calcium and ultimately preventing further muscle contraction. Wikipedia:Ryanodine_receptor RyR activator RyR agonists ryanodine receptor agonist CHEBI:6717 An aminobenzoic acid that is anthranilic acid in which one of the hydrogens attached to the nitrogen is replaced by a 2,3-dimethylphenyl group. Although classed as a non-steroidal anti-inflammatory drug, its anti-inflammatory properties are considered to be minor. It is used to relieve mild to moderate pain, including headaches, dental pain, osteoarthritis and rheumatoid arthritis. CAS:61-68-7 DrugBank:DB00784 Drug_Central:1663 LINCS:LSM-4085 PMID:14001132 PMID:17330662 PMID:22275128 PMID:22369458 PMID:23402341 PMID:23494912 PMID:23656341 PMID:2684858 PMID:28166217 PMID:3304401 PMID:4212650 PMID:425903 PMID:4916242 PMID:5286553 PMID:577447 PMID:6155061 Reaxys:2216243 2-[(2,3-dimethylphenyl)amino]benzoic acid CI-473 CN 35355 CN-35355 INF 3355 INF-3355 Mefenaminsaeure N-(2,3-xylyl)-2-aminobenzoic acid N-2,3-xylylanthranilic acid Ponstel acide mefenamique acido mefenamico acidum mefenamicum mefenamic acid mefenamic acid CAS:61-68-7 ChemIDplus CAS:61-68-7 NIST Chemistry WebBook Drug_Central:1663 DrugCentral PMID:14001132 Europe PMC PMID:17330662 Europe PMC PMID:22275128 Europe PMC PMID:22369458 Europe PMC PMID:23402341 Europe PMC PMID:23494912 Europe PMC PMID:23656341 Europe PMC PMID:2684858 Europe PMC PMID:28166217 Europe PMC PMID:3304401 Europe PMC PMID:4212650 Europe PMC PMID:425903 Europe PMC PMID:4916242 Europe PMC PMID:5286553 Europe PMC PMID:577447 Europe PMC PMID:6155061 Europe PMC Reaxys:2216243 Reaxys CHEBI:67199 An antogonist that interferes with the action of activator protein 1 (AP-1). AP-1 antagonist CHEBI:67208 A ribonucleic acid with two complementary strands, similar to the DNA found in all cells. double stranded ribonucleic acid dsRNA double-stranded RNA CHEBI:67239 An EC 3.2.1.* (glycosidase) inhibitor that interferes with the action of alpha-glucosidase (EC 3.2.1.20). EC 3.2.1.20 (alpha-glucosidase) inhibitors EC 3.2.1.20 inhibitor EC 3.2.1.20 inhibitors alpha-1,4-glucosidase inhibitor alpha-1,4-glucosidase inhibitors alpha-D-glucosidase inhibitor alpha-D-glucosidase inhibitors alpha-glucopyranosidase inhibitor alpha-glucopyranosidase inhibitors alpha-glucosidase (EC 3.2.1.20) inhibitor alpha-glucosidase (EC 3.2.1.20) inhibitors alpha-glucosidase inhibitor alpha-glucosidase inhibitors alpha-glucoside hydrolase inhibitor alpha-glucoside hydrolase inhibitors glucoinvertase inhibitor glucoinvertase inhibitors glucosidoinvertase inhibitor glucosidoinvertase inhibitors glucosidosucrase inhibitor glucosidosucrase inhibitors maltase inhibitor maltase inhibitors maltase-glucoamylase inhibitor maltase-glucoamylase inhibitors EC 3.2.1.20 (alpha-glucosidase) inhibitor CHEBI:6741 A benzothiazine that is piroxicam in which the pyridin-2-yl group is replaced by a 5-methyl-1,3-thiazol-2-yl group. A non-steroidal anti-inflammatory drug and selective inhibitor of COX-2, it is used particularly for the management of rheumatoid arthritis. CN1C(C(=O)Nc2ncc(C)s2)=C(O)c2ccccc2S1(=O)=O DrugBank:DB00814 http://jglobal.jst.go.jp/en/redirect?Nikkaji_No=J22.773K 4-hydroxy-2-methyl-N-(5-methyl-1,3-thiazol-2-yl)-2H-1,2-benzothiazine-3-carboxamide 1,1-dioxide MLX meloxicam CHEBI:6801 A member of the class of guanidines that is biguanide the carrying two methyl substituents at position 1. CN(C)C(=N)NC(N)=N InChI=1S/C4H11N5/c1-9(2)4(7)8-3(5)6/h1-2H3,(H5,5,6,7,8) XZWYZXLIPXDOLR-UHFFFAOYSA-N metformin CHEBI:681569 A purine nucleoside analogue consisting of a 6-amino-2-chloropurin-9-yl group attached to the 1beta position of 2'-deoxy-2'-fluoro-D-arabinofuranose. It is metabolized intracellularly to the active 5'-triphosphate metabolite, which inhibits DNA synthesisis and so stops the growth of cancer cells. Clofarabine is used as an antimetabolite antineoplastic agent in the treatment of relapsed or refractory acute lymphoblastic leukaemia. Beilstein:4882539 CAS:123318-82-1 DrugBank:DB00631 PMID:19929004 2-chloro-9-(2-deoxy-2-fluoro-beta-D-arabinofuranosyl)-9H-purin-6-amine clofarabine (2R,3R,4S,5R)-5-(6-amino-2-chloropurin-9-yl)-4-fluoro-2-(hydroxymethyl)oxolan-3-ol 2-chloro-9-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)adenine 2-chloro-9-(2-deoxy-2-fluoro-beta-D-arabinofuranosyl)adenine CAFdA Cl-F-Ara-A clofarabina clofarabine clofarabinum clofarabine Beilstein:4882539 Beilstein CAS:123318-82-1 ChemIDplus PMID:19929004 ChEMBL CHEBI:68494 Any substance that inhibits the process of apoptosis (programmed cell death) in multi-celled organisms. Type I cell-death inhibitor apoptosis inhibitor CHEBI:68495 Any substance that induces the process of apoptosis (programmed cell death) in multi-celled organisms. Type I cell-death inducer Type I cell-death inducers Type I programmed cell-death inducer Type I programmed cell-death inducers apoptosis inducers apoptosis inducer CHEBI:68508 A maleate ester resulting from the formal condensation of both carboxy groups of maleic acid with ethanol. A colourless liquid at room temperature (m.p. -10degreeC) with boiling point 220degreeC at 1 atm., it is commonly used as a dienophile for Diels-Alder-type cycloaddition reactions in organic synthesis. C8H12O4 CCOC(=O)C=C/C(=O)OCC CAS:141-05-9 PMID:1471155 PMID:1609410 PMID:3341033 diethyl (2Z)-but-2-enedioate diethyl malate CHEBI:68509 A compound which causes a reduction in the levels of glutathione in cells. glutathione depletion agent role glutathione depleting agent CHEBI:68542 An EC 1.3.98.* (oxidoreductase acting on CH-CH group of donors, with other, known, acceptors) inhibitor that interferes with the action of dihydroorotate oxidase (fumarate), EC 1.3.98.1 (formerly EC 1.3.3.1). (S)-dihydroorotate:fumarate oxidoreductase inhibitor (S)-dihydroorotate:fumarate oxidoreductase inhibitors DHODH inhibitor DHODH inhibitors EC 1.3.3.1 inhibitor EC 1.3.3.1 inhibitors EC 1.3.98.1 (dihydroorotate oxidase (fumarate)) inhibitor EC 1.3.98.1 (dihydroorotate oxidase (fumarate)) inhibitors EC 1.3.98.1 [dihydroorotate oxidase (fumarate)] inhibitors EC 1.3.98.1 inhibitor EC 1.3.98.1 inhibitors dihydroorotate dehydrogenase inhibitor dihydroorotate dehydrogenase inhibitors dihydroorotate oxidase (fumarate) (EC 1.3.98.1) inhibitor dihydroorotate oxidase (fumarate) (EC 1.3.98.1) inhibitors dihydroorotate oxidase (fumarate) inhibitor dihydroorotate oxidase (fumarate) inhibitors EC 1.3.98.1 [dihydroorotate oxidase (fumarate)] inhibitor CHEBI:68543 A pathway inhibitor that inhibits the synthesis of pyrimidine. pyrimidine synthesis inhibitors pyrimidine synthesis inhibitor CHEBI:68563 An antagonist at the P2Y12 receptor ADP receptor subtype P2Y12 antagonist ADP receptor subtype P2Y12 antagonists P2Y12 receptor antagonists purinergic receptor subtype P2Y12 antagonist purinergic receptor subtype P2Y12 antagonists P2Y12 receptor antagonist CHEBI:6916 An aromatic ether which is 2,6-dimethylphenyl ether of 2-aminopropan-1-ol. CAS:31828-71-4 DrugBank:DB00379 Drug_Central:1794 LINCS:LSM-1700 PMID:10883344 PMID:11009230 Reaxys:2092205 1-(2,6-dimethylphenoxy)propan-2-amine Mexiletine (+-)-1-(2,6-dimethylphenoxy)propan-2-amine (2RS)-1-(2,6-dimethylphenoxy)-2-aminopropane 1-(2',6'-dimethylphenoxy)-2-aminopropane 1-(2,6-dimethylphenoxy)-2-propanamine 1-methyl-2-(2,6-xylyloxy)ethanamine mexiletina mexiletine mexiletinum mexiletine CAS:31828-71-4 ChemIDplus CAS:31828-71-4 NIST Chemistry WebBook Drug_Central:1794 DrugCentral PMID:10883344 Europe PMC PMID:11009230 Europe PMC Reaxys:2092205 Reaxys CHEBI:70727 An EC 5.99.1.* (miscellaneous isomerase) inhibitor that interferes with the action of any of the topoisomerases (enzymes that regulate the overwinding or underwinding of DNA). topoisomerase inhibitors topoisomerase inhibitor CHEBI:70782 A PPAR modulator which activates the peroxisome proliferator-activated receptor-alpha. PPAR-alpha agonist peroxisome proliferator-activated receptor-alpha agonist PPARalpha agonist CHEBI:70821 An EC 3.4.22.* (cysteine endopeptidase) inhibitor which interferes with the action of cathepsin L (EC 3.4.22.15). cathepsin L inhibitor cathepsin L (EC 3.4.22.15) inhibitor CHEBI:71219 A pyrimidine that is 5-(pyrimidin-2-yl}amino-2-methylbenzenesulfonamide substituted at position 4 by a (2,3-dimethylindazol-6-yl)(methyl)amino group. Used as its hydrochloride salt for treatment of kidney cancer. CAS:444731-52-6 Drug_Central:4118 LINCS:LSM-1114 PMID:21394443 PMID:21766486 PMID:21811833 PMID:22112314 PMID:22190407 PMID:22233389 PMID:22341567 PMID:22359392 PMID:22595799 PMID:22679111 PMID:22688250 PMID:22716487 PMID:22733110 PMID:22733795 PMID:22759480 PMID:22766517 PMID:22830347 PMID:22861374 PMID:22917595 PMID:22984765 PMID:23054212 PMID:23064954 PMID:23072642 PMID:23088634 PMID:23135778 Reaxys:11646488 5-({4-[(2,3-dimethyl-2H-indazol-6-yl)(methyl)amino]pyrimidin-2-yl}amino)-2-methylbenzenesulfonamide GW 78603 GW786034 pazopanib pazopanibum pazopanib CAS:444731-52-6 ChemIDplus Drug_Central:4118 DrugCentral PMID:21394443 Europe PMC PMID:21766486 Europe PMC PMID:21811833 Europe PMC PMID:22112314 Europe PMC PMID:22190407 Europe PMC PMID:22233389 Europe PMC PMID:22341567 Europe PMC PMID:22359392 Europe PMC PMID:22595799 Europe PMC PMID:22679111 Europe PMC PMID:22688250 Europe PMC PMID:22716487 Europe PMC PMID:22733110 Europe PMC PMID:22733795 Europe PMC PMID:22759480 Europe PMC PMID:22766517 Europe PMC PMID:22830347 Europe PMC PMID:22861374 Europe PMC PMID:22917595 Europe PMC PMID:22984765 Europe PMC PMID:23054212 Europe PMC PMID:23064954 Europe PMC PMID:23072642 Europe PMC PMID:23088634 Europe PMC PMID:23135778 Europe PMC Reaxys:11646488 Reaxys CHEBI:71300 An enzyme inhibitor that inhibits the action of a transferase (EC 2.*) EC 2 inhibitor EC 2 inhibitors EC 2.* (transferase) inhibitors EC 2.* inhibitor EC 2.* inhibitors transferase inhibitor transferase inhibitors EC 2.* (transferase) inhibitor CHEBI:71415 An imidazolidine-2,4-dione that is hydantoin substituted at position 1 by a [(5-nitro-2-furyl)methylene]amino group. An antibiotic that damages bacterial DNA. CAS:67-20-9 DrugBank:DB00698 Drug_Central:1949 PMID:21567157 PMID:22240115 PMID:22252772 PMID:22252808 PMID:22285235 PMID:22332195 PMID:22508296 PMID:22535452 PMID:22552451 PMID:22722224 PMID:22779302 PMID:22787489 PMID:22836745 PMID:22857139 PMID:22869929 PMID:22876623 PMID:22923965 PMID:22929632 PMID:22977056 PMID:23016316 PMID:23109011 PMID:23113731 PMID:23114172 Reaxys:8132135 1-{[(5-nitro-2-furyl)methylene]amino}imidazolidine-2,4-dione 1-((5-Nitrofurfurylidene)amino)hydantoin 1-(5-Nitro-2-furfurylidenamino)hydantoin 1-(5-Nitro-2-furfurylideneamino)hydantoin 1-[(5-Nitrofurfurylidene)amino]hydantoin 5-Nitrofurantoin N-(5-Nitrofurfurylidene)-1-aminohydantoin nitrofurantoin nitrofurantoina nitrofurantoine nitrofurantoinum nitrofurantoin CAS:67-20-9 ChemIDplus CAS:67-20-9 NIST Chemistry WebBook Drug_Central:1949 DrugCentral PMID:21567157 Europe PMC PMID:22240115 Europe PMC PMID:22252772 Europe PMC PMID:22252808 Europe PMC PMID:22285235 Europe PMC PMID:22332195 Europe PMC PMID:22508296 Europe PMC PMID:22535452 Europe PMC PMID:22552451 Europe PMC PMID:22722224 Europe PMC PMID:22779302 Europe PMC PMID:22787489 Europe PMC PMID:22836745 Europe PMC PMID:22857139 Europe PMC PMID:22869929 Europe PMC PMID:22876623 Europe PMC PMID:22923965 Europe PMC PMID:22929632 Europe PMC PMID:22977056 Europe PMC PMID:23016316 Europe PMC PMID:23109011 Europe PMC PMID:23113731 Europe PMC PMID:23114172 Europe PMC Reaxys:8132135 Reaxys CHEBI:71476 An EC 2.3.1.* (acyltransferase transferring other than amino-acyl group) inhibitor that interferes with the action of fatty acid synthase (EC 2.3.1.85), a multi-enzyme protein involved in fatty acid synthesis. (FAS) inhibitors EC 2.3.1.85 (fatty acid synthase) inhibitors EC 2.3.1.85 inhibitor EC 2.3.1.85 inhibitors acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing and thioester-hydrolysing) inhibitor acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing and thioester-hydrolysing) inhibitors fatty acid synthase (EC 2.3.1.85) inhibitor fatty acid synthase (EC 2.3.1.85) inhibitors fatty acid synthase inhibitor fatty acid synthase inhibitors EC 2.3.1.85 (fatty acid synthase) inhibitor CHEBI:71554 A PPAR modulator which activates the peroxisome proliferator-activated receptor-gamma. PPAR-gamma agonist peroxisome proliferator-activated receptor-gamma agonist PPARgamma agonist CHEBI:72695 Any molecule that consists of at least one carbon atom as part of the electrically neutral entity. organic compound organic molecule CHEBI:72768 An agonist that binds to and activates aryl hydrocarbon receptors (AhRs). AHR agonist aryl hydrocarbon receptor agonist CHEBI:73044 An amino acid that is phenylacetic acid which is substituted at position 2 by the nitrogen of 2-chloro-6-fluoroaniline and at position 5 by a methyl group. A highly selective cyclooxygenase 2 inhibitor, it was briefly used for the treatment of osteoarthritis, but was withdrawn due to concersns of hepatotoxicity. CAS:220991-20-8 DrugBank:DB01283 Drug_Central:1618 PMID:14965322 PMID:15311562 PMID:15456339 PMID:17380211 PMID:19800190 PMID:21688392 PMID:22069133 PMID:22142375 PMID:22621454 PMID:22732767 Reaxys:9784107 {2-[(2-chloro-6-fluorophenyl)amino]-5-methylphenyl}acetic acid 2-((2-chloro-6-fluorophenyl)amino)-5-methylbenzeneacetic acid COX 189 COX-189 COX189 Prexige lumiracoxib lumiracoxibum lumiracoxib CAS:220991-20-8 ChemIDplus Drug_Central:1618 DrugCentral PMID:14965322 Europe PMC PMID:15311562 Europe PMC PMID:15456339 Europe PMC PMID:17380211 Europe PMC PMID:19800190 Europe PMC PMID:21688392 Europe PMC PMID:22069133 Europe PMC PMID:22142375 Europe PMC PMID:22621454 Europe PMC PMID:22732767 Europe PMC Reaxys:9784107 Reaxys CHEBI:73216 Any hydrolase inhibitor that interferes with the action of a hydrolase which acts on acid anhydrides (EC 3.6.*.*). EC 3.6 inhibitor EC 3.6 inhibitors EC 3.6.* (hydrolases acting on acid anhydrides) inhibitors EC 3.6.* inhibitor EC 3.6.* inhibitors EC 3.6.*.* inhibitor EC 3.6.*.* inhibitors acid anhydride hydrolase inhibitor acid anhydride hydrolase inhibitors inhibitor of hydrolase acting on acid anhydride (EC 3.6.*) inhibitors of hydrolase acting on acid anhydride (EC 3.6.*) EC 3.6.* (hydrolases acting on acid anhydrides) inhibitor CHEBI:73240 An inhibitor of NF-kappaB (nuclear factor kappa-light-chain-enhancer of activated B cells), a protein complex involved in the transcription of DNA. NF-kappaB inhibitors nuclear factor kappa-light-chain-enhancer of activated B cells inhibitor nuclear factor kappa-light-chain-enhancer of activated B cells inhibitors NF-kappaB inhibitor CHEBI:73693 A carbonyl compound produced as a water-soluble byproduct when fatty acids are broken down for energy in the liver. There are three endogenous ketone bodies: acetone, acetoacetic acid, and (R)-3-hydroxybutyric acid; others may be produced as a result of the metabolism of synthetic triglycerides. ketone body CHEBI:73913 An antimetabolite that impairs the action of folic acids antifolates folic acid antagonist folic acid antagonists antifolate CHEBI:74213 An EC 1.17.* (oxidoreductase acting on CH or CH2) inhibitor that inhibits the action of ribonucleoside-diphosphate reductase (EC 1.17.4.1). 2'-deoxyribonucleoside-diphosphate:thioredoxin-disulfide 2'-oxidoreductase inhibitor 2'-deoxyribonucleoside-diphosphate:thioredoxin-disulfide 2'-oxidoreductase inhibitors ADP reductase inhibitor ADP reductase inhibitors CDP reductase inhibitor CDP reductase inhibitors EC 1.17.4.1 (ribonucleoside-diphosphate reductase) inhibitors EC 1.17.4.1 inhibitor EC 1.17.4.1 inhibitors RR inhibitor RR inhibitors UDP reductase inhibitor UDP reductase inhibitors nucleoside diphosphate reductase inhibitor nucleoside diphosphate reductase inhibitors ribonucleoside diphosphate reductase inhibitor ribonucleoside diphosphate reductase inhibitors ribonucleoside-diphosphate reductase (EC 1.17.4.1) inhibitor ribonucleoside-diphosphate reductase (EC 1.17.4.1) inhibitors ribonucleoside-diphosphate reductase inhibitor ribonucleoside-diphosphate reductase inhibitors ribonucleotide diphosphate reductase inhibitor ribonucleotide diphosphate reductase inhibitors ribonucleotide reductase inhibitor ribonucleotide reductase inhibitors EC 1.17.4.1 (ribonucleoside-diphosphate reductase) inhibitor CHEBI:74440 An antagonist at the epidermal growth factor receptor. EGFR antagonoist EGFR antagonoists EGFR inhibitor EGFR inhibitors epidermal growth factor receptor antagonists epidermal growth factor receptor inhibitor epidermal growth factor receptor inhibitors epidermal growth factor receptor antagonist CHEBI:74518 Any substance which is used to reduce or control weight. anti-obesity agents anti-obestic agent anti-obestic agents anti-obesity agent CHEBI:7466 A 3-oxo Delta(4)-steroid that is estr-4-en-3-one substituted by a beta-hydroxy group at position 17. Beilstein:2055849 Beilstein:4690380 CAS:434-22-0 DrugBank:DB00984 Drug_Central:1879 Gmelin:1228044 PMID:11888015 PMID:19055689 PMID:20020363 PMID:24405322 Reaxys:2055849 17beta-hydroxyestr-4-en-3-one Nandrolone (17beta)-17-hydroxyestr-4-en-3-one 17beta-hydroxy-19-nor-4-androsten-3-one 17beta-hydroxy-4-estren-3-one 17beta-hydroxyestr-4-en-3-one 19-Norandrostenolone 19-Nortestosterone 4-estren-17beta-ol-3-one nandrolone Beilstein:2055849 Beilstein Beilstein:4690380 Beilstein CAS:434-22-0 ChemIDplus Drug_Central:1879 DrugCentral Gmelin:1228044 Gmelin PMID:11888015 Europe PMC PMID:19055689 Europe PMC PMID:20020363 Europe PMC PMID:24405322 Europe PMC Reaxys:2055849 Reaxys CHEBI:7494 Beilstein:4728403 CAS:83366-66-9 DrugBank:DB01149 Drug_Central:1890 LINCS:LSM-4031 2-{3-[4-(3-chlorophenyl)piperazin-1-yl]propyl}-5-ethyl-4-(2-phenoxyethyl)-2,4-dihydro-3H-1,2,4-triazol-3-one Nefazodone nefazodone 1-(3-(4-(m-Chlorophenyl)-1-piperazinyl)propyl)-3-ethyl-4-(2-phenoxyethyl)-delta2-1,2,4-triazolin-5-one nefazodona nefazodone nefazodonum nefazodone Beilstein:4728403 Beilstein CAS:83366-66-9 ChemIDplus Drug_Central:1890 DrugCentral CHEBI:7496 An aryl sulfide that is used (as its mesylate salt) for treatment of HIV and also exhibits some anticancer properties. C32H45N3O4S Cc1c(O)cccc1C(=O)N[C@@H](CSc1ccccc1)[C@H](O)CN1C[C@H]2CCCC[C@H]2C[C@H]1C(=O)NC(C)(C)C nelfinavir CHEBI:75142 A tripeptide that is L-leucyl-L-leucyl-L-leucine in which the C-terminal carboxy group has been reduced to the corresponding aldehyde and the N-terminal amino group is protected as its benzyloxycarbonyl derivative. C26H41N3O5 PubChem:462382 C([C@H](CC(C)C)NC([C@H](CC(C)C)NC([C@H](CC(C)C)NC(=O)OCC1=CC=CC=C1)=O)=O)(=O)[H] Wikipedia:MG132 MG-132 N-benzyloxycarbonyl-L-leucyl-L-leucyl-L-leucinal CHEBI:75596 An enzyme inhibitor that inhibits the action of an isomerase (EC 5.*.*.*). EC 5.* (isomerase) inhibitors EC 5.* inhibitor EC 5.* inhibitors EC 5.*.*.* inhibitor EC 5.*.*.* inhibitors isomerase (EC 5.*) inhibitor isomerase (EC 5.*) inhibitors isomerase inhibitor isomerase inhibitors EC 5.* (isomerase) inhibitor CHEBI:7573 Nilutamide, sold under the brand names Nilandron and Anandron, is a nonsteroidal antiandrogen (NSAA) which is used in the treatment of prostate cancer. (by Wikipedia) C12H10F3N3O4 CC1(C)NC(=O)N(C1=O)c1ccc(c(c1)C(F)(F)F)[N+]([O-])=O Beilstein:841906 CAS:63612-50-0 DrugBank:DB00665 Drug_Central:1933 LINCS:LSM-2513 Wikipedia:Nilutamide 5,5-dimethyl-3-[4-nitro-3-(trifluoromethyl)phenyl]imidazolidine-2,4-dione Nilutamide 5,5-Dimethyl-3-(alpha,alpha,alpha-trifluoro-4-nitro-m-tolyl)hydantoin Nilandron nilutamida nilutamide nilutamidum nilutamide Beilstein:841906 Beilstein CAS:63612-50-0 ChemIDplus Drug_Central:1933 DrugCentral CHEBI:75763 Any metabolite produced during a metabolic reaction in eukaryotes, the taxon that include members of the fungi, plantae and animalia kingdoms. eukaryotic metabolites eukaryotic metabolite CHEBI:75767 Any eukaryotic metabolite produced during a metabolic reaction in animals that include diverse creatures from sponges, insects to mammals. animal metabolites animal metabolite CHEBI:75768 Any animal metabolite produced during a metabolic reaction in mammals. mammalian metabolites mammalian metabolite CHEBI:75771 Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus). Mus musculus metabolite Mus musculus metabolites mouse metabolites mouse metabolite CHEBI:75787 Any metabolite produced during a metabolic reaction in prokaryotes, the taxon that include members of domains such as the bacteria and archaea. prokaryotic metabolites prokaryotic metabolite CHEBI:76114 A monocarboxylic acid that is propionic acid substituted at position 2 by a 2-(4-chlorophenyl)-1,3-benzoxazol-5-yl group. It was used as a non-steroidal anti-inflammatory drug until 1982 when it was withdrawn from the market due to adverse side-effects including liver necrosis, photosensitivity, and carcinogenicity in animals. CAS:51234-28-7 DrugBank:DB04812 Drug_Central:311 PMID:19439485 PMID:19773537 PMID:21128314 PMID:22514582 PMID:23250699 PMID:2413686 PMID:2833969 PMID:2947294 PMID:3981515 PMID:6407402 PMID:6526401 PMID:6645654 PMID:6813936 PMID:6993669 PMID:6993670 PMID:6993671 PMID:6993672 PMID:7044799 PMID:7044801 PMID:7084283 PMID:7084287 PMID:7221526 Reaxys:1085080 2-[2-(4-chlorophenyl)-1,3-benzoxazol-5-yl]propanoic acid (+-)-benoxaprofen (1)-2-(4-Chlorophenyl)benzoxazole-5-propionic acid 2-(4-Chlorophenyl)-alpha-methyl-5-benzoxazoleacetic acid 2-(4-chlorophenyl)-alpha-methyl-5-benzoxazoleacetic acid 2-(p-chlorophenyl)-alpha-methyl-5-benzoxazoleacetic acid DL-benoxaprofen Lilly 90459 benoxaprofen benoxaprofene benoxaprofeno benoxaprofenum benoxaprofen CAS:51234-28-7 ChemIDplus CAS:51234-28-7 NIST Chemistry WebBook Drug_Central:311 DrugCentral PMID:19439485 Europe PMC PMID:19773537 Europe PMC PMID:21128314 Europe PMC PMID:22514582 Europe PMC PMID:23250699 Europe PMC PMID:2413686 Europe PMC PMID:2833969 Europe PMC PMID:2947294 Europe PMC PMID:3981515 Europe PMC PMID:6407402 Europe PMC PMID:6526401 Europe PMC PMID:6645654 Europe PMC PMID:6813936 Europe PMC PMID:6993669 Europe PMC PMID:6993670 Europe PMC PMID:6993671 Europe PMC PMID:6993672 Europe PMC PMID:7044799 Europe PMC PMID:7044801 Europe PMC PMID:7084283 Europe PMC PMID:7084287 Europe PMC PMID:7221526 Europe PMC Reaxys:1085080 Reaxys CHEBI:76133 An organic heterotricyclic compound that is 2H,5H-[1,3]oxazino[5,6-c][1,2]benzothiazine-2,4(3H)-dione 6,6-dioxide substituted at positions 3 and 5 by pyridin-2-yl and methyl groups respectively. A prodrug of piroxicam, it is used for the relief of pain and inflammation in musculoskeletal disorders such as rheumatoid arthritis and osteoarthritis. CAS:90101-16-9 Drug_Central:970 PMID:12093490 PMID:1365484 PMID:1365486 PMID:1365487 PMID:1365489 PMID:1365490 PMID:1365491 PMID:1487550 PMID:1507922 PMID:1507923 PMID:1507924 PMID:1545609 PMID:23656309 PMID:2778095 PMID:3110512 PMID:3221746 PMID:3278945 PMID:3489870 PMID:3762266 PMID:8489815 PMID:8492964 PMID:8616003 PMID:8656732 PMID:8983932 Reaxys:6006252 5-methyl-3-(pyridin-2-yl)-2H,5H-[1,3]oxazino[5,6-c][1,2]benzothiazine-2,4(3H)-dione 6,6-dioxide droxicam droxicamum droxicam CAS:90101-16-9 ChemIDplus Drug_Central:970 DrugCentral PMID:12093490 Europe PMC PMID:1365484 Europe PMC PMID:1365486 Europe PMC PMID:1365487 Europe PMC PMID:1365489 Europe PMC PMID:1365490 Europe PMC PMID:1365491 Europe PMC PMID:1487550 Europe PMC PMID:1507922 Europe PMC PMID:1507923 Europe PMC PMID:1507924 Europe PMC PMID:1545609 Europe PMC PMID:23656309 Europe PMC PMID:2778095 Europe PMC PMID:3110512 Europe PMC PMID:3221746 Europe PMC PMID:3278945 Europe PMC PMID:3489870 Europe PMC PMID:3762266 Europe PMC PMID:8489815 Europe PMC PMID:8492964 Europe PMC PMID:8616003 Europe PMC PMID:8656732 Europe PMC PMID:8983932 Europe PMC Reaxys:6006252 Reaxys CHEBI:76158 A monocarboxylic acid that is acetic acid in which one of the methyl hydrogens is replaced by a 4-isobutylphenyl group. Although it was shown to be effective in treatment of rheumatoid arthritis, the clinical use of ibufenac was discontinued due to hepatotoxic side-effects. CAS:1553-60-2 Drug_Central:3293 PMID:1479559 PMID:16456879 PMID:21128314 PMID:2585272 PMID:3215965 PMID:5329891 PMID:5657238 PMID:5748163 PMID:5752436 PMID:5807207 PMID:687781 PMID:7587932 PMID:9061203 Reaxys:2046683 (4-isobutylphenyl)acetic acid [4-(2-methylpropyl)phenyl]acetic acid (p-Isobutylphenyl)acetic acid 4-(2-Methylpropyl)benzeneacetic acid 4-Isobutylphenylacetic acid Dytransin Ibunac ibufenac ibufenaco ibufenacum ibufenac CAS:1553-60-2 ChemIDplus Drug_Central:3293 DrugCentral PMID:1479559 Europe PMC PMID:16456879 Europe PMC PMID:21128314 Europe PMC PMID:2585272 Europe PMC PMID:3215965 Europe PMC PMID:5329891 Europe PMC PMID:5657238 Europe PMC PMID:5748163 Europe PMC PMID:5752436 Europe PMC PMID:5807207 Europe PMC PMID:687781 Europe PMC PMID:7587932 Europe PMC PMID:9061203 Europe PMC Reaxys:2046683 Reaxys CHEBI:76206 Any metabolite produced by metabolism of a xenobiotic compound. xenobiotic metabolites xenobiotic metabolite CHEBI:7640 An organic tricyclic compound that is 10,11-dihydro-5H-dibenzo[a,d][7]annulene substituted by a 3-(methylamino)propylidene group at position 5. It is an active metabolite of amitriptyline. Beilstein:2216786 CAS:72-69-5 DrugBank:DB00540 Drug_Central:1971 LINCS:LSM-4039 PMID:10379421 PMID:14561440 PMID:17071817 PMID:23280809 PMID:24037379 PMID:24368464 PMID:25224004 PMID:25480462 PMID:25569864 PMID:25592638 PMID:25683584 PMID:25707462 PMID:25749306 PMID:26086857 PMID:26453560 Reaxys:2216786 3-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-ylidene)-N-methylpropan-1-amine Nortriptyline 10,11-dihydro-N-methyl-5H-dibenzo[a,d]cycloheptene-Delta(5,gamma)-propylamine 3-(10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5-ylidene)-N-methyl-1-propanamine Ateben Avantyl Aventyl Noritren Psychostyl Sensaval demethylamitriptyline desmethylamitriptyline nortriptylina nortriptyline nortriptylinum nortriptyline Beilstein:2216786 ChemIDplus CAS:72-69-5 ChemIDplus CAS:72-69-5 NIST Chemistry WebBook Drug_Central:1971 DrugCentral PMID:10379421 Europe PMC PMID:14561440 Europe PMC PMID:17071817 Europe PMC PMID:23280809 Europe PMC PMID:24037379 Europe PMC PMID:24368464 Europe PMC PMID:25224004 Europe PMC PMID:25480462 Europe PMC PMID:25569864 Europe PMC PMID:25592638 Europe PMC PMID:25683584 Europe PMC PMID:25707462 Europe PMC PMID:25749306 Europe PMC PMID:26086857 Europe PMC PMID:26453560 Europe PMC Reaxys:2216786 Reaxys CHEBI:76603 A bridged organochlorine compound resulting from the Diels-Alder reaction of hexachlorocyclopentadiene with maleic anhydride followed by hydrolysis of the resulting anhydride. A chemical intermediate used in the preparation of fire-retardant polyester resins and plasticisers. C9H4Cl6O4 OC(=O)C1C(C(O)=O)C2(Cl)C(Cl)=C(Cl)C1(Cl)C2(Cl)Cl CAS:115-28-6 1,4,5,6,7,7-hexachlorobicyclo[2.2.1]hept-5-ene-2,3-dicarboxylic acid Chlorendic Acid CHEBI:76612 A member of the class of acrylamides that is (3R)-3-[4-amino-3-(4-phenoxyphenyl)pyrazolo[3,4-d]pyrimidin-1-yl]piperidine in which the piperidine nitrogen is replaced by an acryloyl group. A selective and covalent inhibitor of the enzyme Bruton's tyrosine kinase, it is used for treatment of B-cell malignancies. C25H24N6O2 InChI=1S/C25H24N6O2/c1-2-21(32)30-14-6-7-18(15-30)31-25-22(24(26)27-16-28-25)23(29-31)17-10-12-20(13-11-17)33-19-8-4-3-5-9-19/h2-5,8-13,16,18H,1,6-7,14-15H2,(H2,26,27,28)/t18-/m1/s1 Nc1ncnc2n(nc(-c3ccc(Oc4ccccc4)cc3)c12)[C@@H]1CCCN(C1)C(=O)C=C CAS:936563-96-1 PMID:33328281 ibrutinib PMID:33328281 Many patients with COVID-19 are suffering with high risk of thrombotic complications, with 20% of severely ill patients affected by venous thromboembolism. This has a critical impact on the prognosis of the disease. BTK inhibitors, specifically ibrutinib, are associated with reduced venous thrombosis and arterial thrombosis. CHEBI:76617 An EC 2.7.10.* (protein-tyrosine kinase) inhibitor that specifically blocks the action of non-specific protein-tyrosine kinase (EC 2.7.10.2). BTK inhibitors JAK1/JAK2 inhibitors EC 2.7.10.2 (non-specific protein-tyrosine kinase) inhibitor CHEBI:76655 A transferase inhibitor inhibiting the action of transferase of a one-carbon-containing group (EC 2.1.*.*). C1-transferase (EC 2.1.*) inhibitor C1-transferase (EC 2.1.*) inhibitors C1-transferase inhibitor C1-transferase inhibitors EC 2.1.* (C1-transferase) inhibitors EC 2.1.* inhibitor EC 2.1.* inhibitors one-carbon-containing group transferase inhibitor one-carbon-containing group transferase inhibitors EC 2.1.* (C1-transferase) inhibitor CHEBI:76661 A transferase inhibitor that interferes with the action of an acyltransferase (EC 2.3.*.*). EC 2.3.* (acyltransferase) inhibitors EC 2.3.* inhibitor EC 2.3.* inhibitors acyltransferase inhibitor acyltransferase inhibitors EC 2.3.* (acyltransferase) inhibitor CHEBI:76662 A transferase inhibitor inhibiting the action of a glycosyltransferase (EC 2.4.*.*). EC 2.4.* (glycosyltransferase) inhibitors EC 2.4.* inhibitor EC 2.4.* inhibitors glycosyltransferase (EC 2.4.*) inhibitor glycosyltransferase (EC 2.4.*) inhibitors glycosyltransferase inhibitor glycosyltransferase inhibitors EC 2.4.* (glycosyltransferase) inhibitor CHEBI:76663 A transferase inhibitor that inhibits the transfer of an alkyl (other than methyl) or aryl group (EC 2.5.1.*). EC 2.5.1.* (non-methyl-alkyl or aryl transferase) inhibitors EC 2.5.1.* inhibitor EC 2.5.1.* inhibitors alkyl/aryl (non-methyl) transferase inhibitor alkyl/aryl (non-methyl) transferase inhibitors non-methyl alkyl/aryl transferase (EC 2.5.1.*) inhibitor non-methyl alkyl/aryl transferase (EC 2.5.1.*) inhibitors non-methyl alkyl/aryl transferase inhibitor non-methyl alkyl/aryl transferase inhibitors non-methyl-alkyl or aryl transferase inhibitor non-methyl-alkyl or aryl transferase inhibitors EC 2.5.1.* (non-methyl-alkyl or aryl transferase) inhibitor CHEBI:76668 A transferase inhibitor that inhibits the action of a phosphorus-containing group transferase (EC 2.7.*.*). EC 2.7.* (P-containing group transferase) inhibitors EC 2.7.* (phosphorus-containing group transferase) inhibitor EC 2.7.* (phosphorus-containing group transferase) inhibitors EC 2.7.* inhibitor EC 2.7.* inhibitors phosphorus-containing group transferase (EC 2.7.*) inhibitor phosphorus-containing group transferase (EC 2.7.*) inhibitors phosphorus-containing group transferase inhibitor phosphorus-containing group transferase inhibitors EC 2.7.* (P-containing group transferase) inhibitor CHEBI:76697 An isomerase inhibitor that interferes with the action of any member of the group of 'other isomerases' (EC 5.99.*.*). EC 5.99.* (miscellaneous isomerases) inhibitor EC 5.99.* (miscellaneous isomerases) inhibitors EC 5.99.* (other isomerase) inhibitor EC 5.99.* (other isomerase) inhibitors EC 5.99.* (other isomerases) inhibitors EC 5.99.* inhibitor EC 5.99.* inhibitors EC 5.99.* (other isomerases) inhibitor CHEBI:76710 An enzyme inhibitor which interferes with the action of a lyase (EC 4.*.*.*). Lyases are enzymes cleaving C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation. EC 4.* (lyase) inhibitors EC 4.* inhibitor EC 4.* inhibitors EC 4.*.*.* inhibitor EC 4.*.*.* inhibitors lyase (EC 4.*) inhibitor lyase (EC 4.*) inhibitorS lyase inhibitor lyase inhibitors EC 4.* (lyase) inhibitor CHEBI:76712 A lyase inhibitor which inhibits the action of a C-O lyase (EC 4.2.*.*). C-O lyase (EC 4.2.*) inhibitor C-O lyase (EC 4.2.*) inhibitors C-O lyase inhibitor C-O lyase inhibitors EC 4.2.* (C-O lyase) inhibitors EC 4.2.* inhibitor EC 4.2.* inhibitors EC 4.2.* (C-O lyase) inhibitor CHEBI:76725 An enzyme inhibitor which interferes with the action of an oxidoreductase (EC 1.*.*.*). EC 1.* (oxidoreductase) inhibitors EC 1.* inhibitor EC 1.* inhibitors oxidoreductase (EC 1.*) inhibitor oxidoreductase (EC 1.*) inhibitors oxidoreductase inhibitor oxidoreductase inhibitors EC 1.* (oxidoreductase) inhibitor CHEBI:76726 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on the CH-OH group of donors (EC 1.1.*.*). EC 1.1.* (oxidoreductase acting on donor CH-OH group) inhibitors EC 1.1.* inhibitor EC 1.1.* inhibitors inhibitor of oxidoreductase acting on CH-OH group of donor inhibitor of oxidoreductase acting on CH-OH group of donors inhibitors of oxidoreductase acting on CH-OH group of donor inhibitors of oxidoreductase acting on CH-OH group of donors oxidoreductase acting on donor CH-OH group (EC 1.1.*) inhibitor oxidoreductase acting on donor CH-OH group (EC 1.1.*) inhibitors oxidoreductase acting on donor CH-OH group inhibitor oxidoreductase acting on donor CH-OH group inhibitors EC 1.1.* (oxidoreductase acting on donor CH-OH group) inhibitor CHEBI:76727 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on the aldehyde or oxo group of donors (EC 1.2.*.*). EC 1.2.* (oxidoreductase acting on donor aldehyde or oxo group) inhibitor EC 1.2.* (oxidoreductase acting on donor aldehyde or oxo group) inhibitors EC 1.2.* (oxidoreductase acting on donor aldehyde/oxo group) inhibitors EC 1.2.* inhibitor EC 1.2.* inhibitors inhibitor of oxidoreductase acting on aldehyde or oxo group of donor inhibitor of oxidoreductase acting on aldehyde or oxo group of donors inhibitor of oxidoreductase acting on aldehyde/oxo group of donor inhibitor of oxidoreductase acting on aldehyde/oxo group of donors inhibitors of oxidoreductase acting on aldehyde or oxo group of donor inhibitors of oxidoreductase acting on aldehyde or oxo group of donors inhibitors of oxidoreductase acting on aldehyde/oxo group of donor inhibitors of oxidoreductase acting on aldehyde/oxo group of donors oxidoreductase acting on donor aldehyde or oxo group (EC 1.2.*) inhibitor oxidoreductase acting on donor aldehyde or oxo group (EC 1.2.*) inhibitors oxidoreductase acting on donor aldehyde or oxo group inhibitor oxidoreductase acting on donor aldehyde or oxo group inhibitors oxidoreductase acting on donor aldehyde/oxo group (EC 1.2.*) inhibitor oxidoreductase acting on donor aldehyde/oxo group (EC 1.2.*) inhibitors oxidoreductase acting on donor aldehyde/oxo group inhibitor oxidoreductase acting on donor aldehyde/oxo group inhibitors EC 1.2.* (oxidoreductase acting on donor aldehyde/oxo group) inhibitor CHEBI:76729 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on the CH-CH group of donors (EC 1.3.*.*). EC 1.3.* (oxidoreductase acting on donor CH-CH group) inhibitors EC 1.3.* inhibitor EC 1.3.* inhibitors inhibitor of oxidoreductase acting on CH-CH group of donor inhibitor of oxidoreductase acting on CH-CH group of donors inhibitors of oxidoreductase acting on CH-CH group of donor inhibitors of oxidoreductase acting on CH-CH group of donors oxidoreductase acting on donor CH-CH group (EC 1.3.*) inhibitor oxidoreductase acting on donor CH-CH group (EC 1.3.*) inhibitors oxidoreductase acting on donor CH-CH group inhibitor oxidoreductase acting on donor CH-CH group inhibitors EC 1.3.* (oxidoreductase acting on donor CH-CH group) inhibitor CHEBI:76731 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on the CH-NH group of donors (EC 1.5.*.*). EC 1.5.* (oxidoreductase acting on donor CH-NH group) inhibitors EC 1.5.* inhibitor EC 1.5.* inhibitors inhibitor of oxidoreductase acting on CH-NH group of donor inhibitor of oxidoreductase acting on CH-NH group of donors inhibitors of oxidoreductase acting on CH-NH group of donor inhibitors of oxidoreductase acting on CH-NH group of donors oxidoreductase acting on donor CH-NH group (EC 1.5.*) inhibitor oxidoreductase acting on donor CH-NH group (EC 1.5.*) inhibitors EC 1.5.* (oxidoreductase acting on donor CH-NH group) inhibitor CHEBI:76733 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on NADH or NADPH (EC 1.6.*.*). EC 1.6.* (oxidoreductase acting on NADH or NADPH) inhibitors inhibitor of oxidoreductase acting on NADH or NADPH inhibitor of oxidoreductase acting on NADH or NADPH (EC 1.6.*) inhibitors of oxidoreductase acting on NADH or NADPH inhibitors of oxidoreductase acting on NADH or NADPH (EC 1.6.*) oxidoreductase acting on NADH or NADPH (EC 1.6.*) inhibitor oxidoreductase acting on NADH or NADPH (EC 1.6.*) inhibitors oxidoreductase acting on NADH or NADPH inhibitor oxidoreductase acting on NADH or NADPH inhibitors EC 1.6.* (oxidoreductase acting on NADH or NADPH) inhibitor CHEBI:76735 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase of class EC 1.8.*.* (acting on a sulfur group of donors). EC 1.8.* (oxidoreductase acting on sulfur group of donors) inhibitors EC 1.8.* inhibitor EC 1.8.* inhibitors oxidoreductase acting on a sulfur group of donors (EC 1.8.*) inhibitor oxidoreductase acting on a sulfur group of donors (EC 1.8.*) inhibitors EC 1.8.* (oxidoreductase acting on sulfur group of donors) inhibitor CHEBI:76737 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on diphenols and related substances as donors (EC 1.10.*.*). EC 1.10.* (oxidoreductase acting on diphenols and related substances as donors) inhibitors EC 1.10.* (oxidoreductases acting on diphenols and related substances as donors) inhibitor EC 1.10.* (oxidoreductases acting on diphenols and related substances as donors) inhibitors EC 1.10.* inhibitor EC 1.10.* inhibitors inhibitor of an oxidoreductase acting on diphenols and related substances as donor inhibitor of an oxidoreductase acting on diphenols and related substances as donor (EC 1.10.*) inhibitor of an oxidoreductase acting on diphenols and related substances as donors inhibitors of an oxidoreductase acting on diphenols and related substances as donor inhibitors of an oxidoreductase acting on diphenols and related substances as donor (EC 1.10.*) inhibitors of an oxidoreductase acting on diphenols and related substances as donors EC 1.10.* (oxidoreductase acting on diphenols and related substances as donors) inhibitor CHEBI:76740 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on single donors with incorporation of molecular oxygen (oxygenases), EC 1.13.*.*. EC 1.13.* [oxidoreductase acting on single donors with incorporation of molecular oxygen (oxygenases)] inhibitors EC 1.13.* inhibitor EC 1.13.* inhibitors oxidoreductase acting on single donors with incorporation of molecular oxygen (oxygenases) (EC 1.13.*) inhibitor oxidoreductase acting on single donors with incorporation of molecular oxygen (oxygenases) (EC 1.13.*) inhibitors oxidoreductase acting on single donors with incorporation of molecular oxygen (oxygenases) inhibitor oxidoreductase acting on single donors with incorporation of molecular oxygen (oxygenases) inhibitors EC 1.13.* [oxidoreductase acting on single donors with incorporation of molecular oxygen (oxygenases)] inhibitor CHEBI:76741 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on hydrogen as donors (EC 1.14.*.*). EC 1.14.* (oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen) inhibitors EC 1.14.* inhibitor EC 1.14.* inhibitors inhibitor of oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen (EC 1.14.*) inhibitor of oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (EC 1.14.*) inhibitors of oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen (EC 1.14.*) inhibitors of oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (EC 1.14.*) oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen (EC 1.14.*) inhibitor oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen (EC 1.14.*) inhibitors oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen inhibitor oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen inhibitors EC 1.14.* (oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen) inhibitor CHEBI:76744 An oxidoreductase inhibitor which interferes with the action of an oxidoreductase acting on CH or CH2 (EC 1.17.*.*). EC 1.17.* (oxidoreductase acting on CH or CH2) inhibitors EC 1.17.* inhibitor EC 1.17.* inhibitors oxidoreductase acting on CH or CH2 (EC 1.17.*) inhibitor oxidoreductase acting on CH or CH2 (EC 1.17.*) inhibitors oxidoreductase acting on CH or CH2 inhibitor oxidoreductase acting on CH or CH2 inhibitors EC 1.17.* (oxidoreductase acting on CH or CH2) inhibitor CHEBI:76759 Any enzyme inhibitor that interferes with the action of a hydrolase (EC 3.*.*.*). EC 3.* (hydrolase) inhibitor EC 3.* (hydrolase) inhibitors EC 3.* inhibitor EC 3.* inhibitors EC 3.*.*.* inhibitor EC 3.*.*.* inhibitors hydrolase (EC 3.*) inhibitor hydrolase (EC 3.*) inhibitors hydrolase inhibitor hydrolase inhibitors Wikipedia:Hydrolase EC 3.* (hydrolase) inhibitor CHEBI:76760 A hydrolase inhibitor that interferes with the action of any ester hydrolase (EC 3.1.*.*). EC 3.1.* (ester hydrolase) inhibitors EC 3.1.* inhibitor EC 3.1.* inhibitors ester hydrolase (EC 3.1.*) inhibitor ester hydrolase (EC 3.1.*) inhibitors ester hydrolase inhibitor ester hydrolase inhibitors EC 3.1.* (ester hydrolase) inhibitor CHEBI:76761 A hydrolase inhibitor that interferes with the action of any glycosylase (EC 3.2.*.*). EC 3.2.* (glycosylase) inhibitors EC 3.2.* inhibitor EC 3.2.* inhibitors glycosylase (EC 3.2.*) inhibitor glycosylase (EC 3.2.*) inhibitors glycosylase inhibitor glycosylase inhibitors EC 3.2.* (glycosylase) inhibitor CHEBI:76764 Any hydrolase inhibitor that interferes with the action of a hydrolase acting on C-N bonds, other than peptide bonds (EC 3.5.*.*). EC 3.5.* (hydrolase acting on non-peptide C-N bond) inhibitor EC 3.5.* (hydrolase acting on non-peptide C-N bond) inhibitors EC 3.5.* (hydrolases acting on C-N bonds, other than peptide bonds) inhibitor EC 3.5.* (hydrolases acting on C-N bonds, other than peptide bonds) inhibitors EC 3.5.* (hydrolases acting on non-peptide C-N bonds) inhibitors EC 3.5.* inhibitor EC 3.5.* inhibitors EC 3.5.* (hydrolases acting on non-peptide C-N bonds) inhibitor CHEBI:76773 An EC 3.1.* (ester hydrolase) inhibitor that interferes with the action of a carboxylic ester hydrolase (EC 3.1.1.*). EC 3.1.1.* (carboxylic ester hydrolase) inhibitors EC 3.1.1.* inhibitor EC 3.1.1.* inhibitors carboxylic ester hydrolase (EC 3.1.1.*) inhibitor carboxylic ester hydrolase (EC 3.1.1.*) inhibitors EC 3.1.1.* (carboxylic ester hydrolase) inhibitor CHEBI:76775 An EC 3.1.* (ester hydrolase) inhibitor that interferes with the action of any phosphoric monoester hydrolase (EC 3.1.3.*). EC 3.1.3.* (phosphoric monoester hydrolase) inhibitors EC 3.1.3.* inhibitor EC 3.1.3.* inhibitors inhibitor of phosphoric monoester hydrolase inhibitor of phosphoric monoester hydrolase (EC 3.1.3.*) inhibitors of phosphoric monoester hydrolase inhibitors of phosphoric monoester hydrolase (EC 3.1.3.*) phosphoric monoester hydrolase (EC 3.1.3.*) inhibitor phosphoric monoester hydrolase (EC 3.1.3.*) inhibitors phosphoric monoester hydrolase inhibitor phosphoric monoester hydrolase inhibitors EC 3.1.3.* (phosphoric monoester hydrolase) inhibitor CHEBI:76779 Any EC 3.4.21.* (serine endopeptidase) inhibitor that interferes with the action of prolyl oligopeptidase (EC 3.4.21.26). EC 3.4.21.26 (prolyl oligopeptidase) inhibitors EC 3.4.21.26 inhibitor EC 3.4.21.26 inhibitors endoprolylpeptidase inhibitor endoprolylpeptidase inhibitors post-proline cleaving enzyme inhibitor post-proline cleaving enzyme inhibitors post-proline endopeptidase inhibitor post-proline endopeptidase inhibitors proline endopeptidase inhibitor proline endopeptidase inhibitors proline-specific endopeptidase inhibitor proline-specific endopeptidase inhibitors prolyl endopeptidase inhibitor prolyl endopeptidase inhibitors prolyl oligopeptidase (EC 3.4.21.26) inhibitor prolyl oligopeptidase (EC 3.4.21.26) inhibitors prolyl oligopeptidase inhibitor EC 3.4.21.26 (prolyl oligopeptidase) inhibitor CHEBI:76785 An EC 3.1.* (ester hydrolase) inhibitor that interferes with the action of any endoribonuclease producing 5'-phosphomonoesters (EC 3.1.26.*). EC 3.1.26.* (endoribonucleases producing 5'-phosphomonoesters) inhibitors EC 3.1.26.* inhibitor EC 3.1.26.* inhibitors endoribonuclease producing 5'-phosphomonoesters (EC 3.1.26.*) inhibitor endoribonuclease producing 5'-phosphomonoesters (EC 3.1.26.*) inhibitors endoribonuclease producing 5'-phosphomonoesters inhibitor endoribonuclease producing 5'-phosphomonoesters inhibitors EC 3.1.26.* (endoribonucleases producing 5'-phosphomonoesters) inhibitor CHEBI:76790 An EC 2.4.* (glycosyltransferase) inhibitor that interferes with the action of any pentosyltransferase (EC 2.4.2.*). EC 2.4.2.* (pentosyltransferase) inhibitors EC 2.4.2.* inhibitor EC 2.4.2.* inhibitors pentosyltransferase (EC 2.4.2.*) inhibitor pentosyltransferase (EC 2.4.2.*) inhibitors pentosyltransferase inhibitor pentosyltransferase inhibitors EC 2.4.2.* (pentosyltransferase) inhibitor CHEBI:76797 An EC 2.5.1.* (non-methyl-alkyl or aryl transferase) inhibitor that interferes with the action of a glutathione transferase (EC 2.5.1.18). EC 2.5.1.18 (glutathione transferase) inhibitors EC 2.5.1.18 inhibitor EC 2.5.1.18 inhibitors RX:glutathione R-transferase inhibitor RX:glutathione R-transferase inhibitors S-(hydroxyalkyl)glutathione lyase inhibitor S-(hydroxyalkyl)glutathione lyase inhibitors glutathione S-alkyl transferase inhibitor glutathione S-alkyl transferase inhibitors glutathione S-alkyltransferase inhibitor glutathione S-alkyltransferase inhibitors glutathione S-aralkyltransferase inhibitor glutathione S-aralkyltransferase inhibitors glutathione S-aryltransferase inhibitor glutathione S-aryltransferase inhibitors glutathione S-transferase inhibitor glutathione S-transferase inhibitors glutathione transferase (EC 2.5.1.18) inhibitor glutathione transferase (EC 2.5.1.18) inhibitors glutathione transferase inhibitor glutathione transferase inhibitors EC 2.5.1.18 (glutathione transferase) inhibitor CHEBI:76807 An EC 3.5.* (hydrolases acting on non-peptide C-N bonds) inhibitor that interferes with the action of any non-peptide linear amide C-N hydrolase (EC 3.5.1.*). EC 3.5.1.* (non-peptide linear amide C-N hydrolase) inhibitors EC 3.5.1.* inhibitor EC 3.5.1.* inhibitors non-peptide linear amide C-N hydrolase (EC 3.5.1.*) inhibitor non-peptide linear amide C-N hydrolase (EC 3.5.1.*) inhibitors EC 3.5.1.* (non-peptide linear amide C-N hydrolase) inhibitor CHEBI:76811 An EC 3.1.4.* (phosphoric diester hydrolase) inhibitor that interferes with the action of sphingomyelin phosphodiesterase (EC 3.1.4.12). EC 3.1.4.12 (sphingomyelin phosphodiesterase) inhibitor sphingomyelin phosphodiesterase inhibitor sphingomyelin phosphodiesterase inhibitor role CHEBI:76812 An EC 2.7.* (P-containing group transferase) inhibitor that interferes with the action of any protein-serine/threonine kinase (EC 2.7.11.*). EC 2.7.11.* (protein-serine/threonine kinase) inhibitors EC 2.7.11.* inhibitor EC 2.7.11.* inhibitors protein-serine/threonine kinase (EC 2.7.11.*) inhibitor protein-serine/threonine kinase (EC 2.7.11.*) inhibitors protein-serine/threonine kinase inhibitor protein-serine/threonine kinase inhibitors EC 2.7.11.* (protein-serine/threonine kinase) inhibitor CHEBI:76815 An EC 2.7.* (P-containing group transferase) inhibitor that interferes with the action of any nucleotidyltransferase (EC 2.7.7.*). EC 2.7.7.* (nucleotidyltransferase) inhibitors inhibitor of nucleotidyltransferases inhibitor of nucleotidyltransferases (EC 2.7.7.*) inhibitors of nucleotidyltransferases inhibitors of nucleotidyltransferases (EC 2.7.7.*) nucleotidyltransferase (EC 2.7.7.*) inhibitor nucleotidyltransferase (EC 2.7.7.*) inhibitors nucleotidyltransferase inhibitor nucleotidyltransferase inhibitors EC 2.7.7.* (nucleotidyltransferase) inhibitor CHEBI:76817 An EC 2.7.* (P-containing group transferase) inhibitor that interferes with the action of any protein-tyrosine kinase (EC 2.7.10.*). EC 2.7.10.* (protein-tyrosine kinase) inhibitors EC 2.7.10.* inhibitor EC 2.7.10.* inhibitors protein-tyrosine kinase (EC 2.7.10.*) inhibitor protein-tyrosine kinase (EC 2.7.10.*) inhibitors protein-tyrosine kinase inhibitor protein-tyrosine kinase inhibitors EC 2.7.10.* (protein-tyrosine kinase) inhibitor CHEBI:76830 An EC 5.99.* (other isomerases) inhibitor that interferes with the activity of any enzyme in the EC 5.99.1.* class. EC 5.99.1.* (miscellaneous isomerase) inhibitors EC 5.99.1.* inhibitor EC 5.99.1.* inhibitors EC 5.99.1.* (miscellaneous isomerase) inhibitor CHEBI:76834 An EC 2.5.* (transferase) inhibitor that inhibits the action of any transferase that transfers an alkyl (other than methyl) or aryl group (EC 2.5.*). EC 2.5.* (non-methyl-alkyl or aryl transferase) inhibitors EC 2.5.* inhibitor EC 2.5.* inhibitors non-methyl-alkyl or aryl transferase (EC 2.5.*) inhibitor non-methyl-alkyl or aryl transferase (EC 2.5.*) inhibitors EC 2.5.* (non-methyl-alkyl or aryl transferase) inhibitor CHEBI:76835 An EC 1.1.* (oxidoreductase acting on donor CH-OH group) inhibitor that uses NAD(+) or NADP(+) as acceptor (EC 1.1.1.*). EC 1.1.1.* (oxidoreductase acting on donor CH-OH group, NAD(+) or NADP(+)acceptor) inhibitors EC 1.1.1.* inhibitor EC 1.1.1.* inhibitors oxidoreductase acting on donor CH-OH group, NAD(+) or NADP(+) acceptor (EC 1.1.1.*) inhibitor oxidoreductase acting on donor CH-OH group, NAD(+) or NADP(+) acceptor (EC 1.1.1.*) inhibitors EC 1.1.1.* (oxidoreductase acting on donor CH-OH group, NAD(+) or NADP(+) acceptor) inhibitor CHEBI:76837 An EC 1.13.* [oxidoreductase acting on single donors with incorporation of molecular oxygen (oxygenases)] inhibitor that inhibits the action of any oxidoreductase incorporating 2 atoms of oxygen (EC 1.13.11.*). EC 1.13.11.* (oxidoreductase acting on single donors and incorporating 2 O atoms) inhibitors EC 1.13.11.* (oxidoreductase acting on single donors and incorporating 2 atoms of oxygen) inhibitor EC 1.13.11.* (oxidoreductase acting on single donors and incorporating 2 atoms of oxygen) inhibitors EC 1.13.11.* inhibitor EC 1.13.11.* inhibitors oxidoreductase acting on single donors and incorporating 2 atoms of oxygen (EC 1.13.11.*) inhibitor oxidoreductase acting on single donors and incorporating 2 atoms of oxygen (EC 1.13.11.*) inhibitors EC 1.13.11.* (oxidoreductase acting on single donors and incorporating 2 O atoms) inhibitor CHEBI:76838 An EC 1.14.* (oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen) inhibitor that interferes with the action of any such enzyme incorporating one atom of oxygen and using reduced flavin or flavoprotein as donor (EC 1.14.14.*). EC 1.14.14.* (oxidoreductase acting on paired donors, incorporating of 1 atom of oxygen, with reduced flavin or flavoprotein as one donor) inhibitors EC 1.14.14.* (oxidoreductase acting on paired donors, with incorporation of 1 atom of oxygen, with reduced flavin or flavoprotein as one donor) inhibitor EC 1.14.14.* (oxidoreductase acting on paired donors, with incorporation of 1 atom of oxygen, with reduced flavin or flavoprotein as one donor) inhibitors EC 1.14.14.* inhibitor EC 1.14.14.* inhibitors oxidoreductase acting on paired donors, with incorporation of 1 atom of oxygen, with reduced flavin or flavoprotein as one donor (EC 1.14.14.*) inhibitor oxidoreductase acting on paired donors, with incorporation of 1 atom of oxygen, with reduced flavin or flavoprotein as one donor (EC 1.14.14.*) inhibitors EC 1.14.14.* (oxidoreductase acting on paired donors, incorporating of 1 atom of oxygen, with reduced flavin or flavoprotein as one donor) inhibitor CHEBI:76840 An EC 1.14.* (oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen) inhibitor that interferes with the action of any enzyme in the EC 1.14.99.* (miscellaneous) category. EC 1.14.99.* (miscellaneous oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen) inhibitors EC 1.14.99.* inhibitor EC 1.14.99.* inhibitors miscellaneous oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen (EC 1.14.99.*) inhibitor miscellaneous oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen (EC 1.14.99.*) inhibitors EC 1.14.99.* (miscellaneous oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen) inhibitor CHEBI:76841 An EC 1.14.* (oxidoreductase acting on paired donors, with incorporation or reduction of molecular oxygen) inhibitor that interferes with the action of any such enzyme incorporating one atom of oxygen and using NADH or NADPH as one donor (EC 1.14.13.*). EC 1.14.13.* (oxidoreductase acting on paired donors, incorporating 1 atom of oxygen, with NADH or NADPH as one donor) inhibitors EC 1.14.13.* inhibitor EC 1.14.13.* inhibitors oxidoreductase acting on paired donors, incorporating 1 atom of oxygen, with NADH or NADPH as one donor (EC 1.14.13.*) inhibitor oxidoreductase acting on paired donors, incorporating 1 atom of oxygen, with NADH or NADPH as one donor (EC 1.14.13.*) inhibitors EC 1.14.13.* (oxidoreductase acting on paired donors, incorporating 1 atom of oxygen, with NADH or NADPH as one donor) inhibitor CHEBI:76848 An EC 1.17.* (oxidoreductase acting on CH or CH2) inhibitor that interferes with the activity of any such enzyme that uses a disulfide as acceptor (EC 1.17.4.*). EC 1.17.4.* (oxidoreductase acting on CH or CH2 with a disulfide as acceptor) inhibitors EC 1.17.4.* inhibitor EC 1.17.4.* inhibitors oxidoreductase acting on CH or CH2 with a disulfide as acceptor (EC 1.17.4.*) inhibitor oxidoreductase acting on CH or CH2 with a disulfide as acceptor (EC 1.17.4.*) inhibitors EC 1.17.4.* (oxidoreductase acting on CH or CH2 with a disulfide as acceptor) inhibitor CHEBI:76850 An EC 1.17.* (oxidoreductase acting on CH or CH2) inhibitor that interferes with the function of any such enzyme that uses oxygen as acceptor (EC 1.17.3.*). EC 1.17.3.* (oxidoreductase acting on CH or CH2 with oxygen as acceptor) inhibitors EC 1.17.3.* inhibitor EC 1.17.3.* inhibitors oxidoreductase acting on CH or CH2 with oxygen as acceptor (EC 1.17.3.*) inhibitor oxidoreductase acting on CH or CH2 with oxygen as acceptor (EC 1.17.3.*) inhibitors EC 1.17.3.* (oxidoreductase acting on CH or CH2 with oxygen as acceptor) inhibitor CHEBI:76852 An EC 1.2.* (oxidoreductase acting on donor aldehyde/oxo group) inhibitor that interferes with the action of any such enzyme using NAD(+) or NADP(+) as acceptor (EC 1.2.1.*). EC 1.2.1.* (oxidoreductase acting on donor aldehyde/oxo group with NAD(+) or NADP(+) as acceptor) inhibitors EC 1.2.1.* inhibitor EC 1.2.1.* inhibitors oxidoreductase acting on donor aldehyde/oxo group with NAD(+) or NADP(+) as acceptor (EC 1.2.1.*) inhibitor oxidoreductase acting on donor aldehyde/oxo group with NAD(+) or NADP(+) as acceptor (EC 1.2.1.*) inhibitors EC 1.2.1.* (oxidoreductase acting on donor aldehyde/oxo group with NAD(+) or NADP(+) as acceptor) inhibitor CHEBI:76853 An EC 1.2.* (oxidoreductase acting on donor aldehyde/oxo group) inhibitor that interferes with the action of any such enzyme using oxygen as acceptor (EC 1.2.3.*). EC 1.2.3.* (oxidoreductase acting on donor aldehyde/oxo group with oxygen as acceptor) inhibitors EC 1.2.3.* inhibitor EC 1.2.3.* inhibitors oxidoreductase acting on donor aldehyde/oxo group with oxygen as acceptor (EC 1.2.3.*) inhibitor oxidoreductase acting on donor aldehyde/oxo group with oxygen as acceptor (EC 1.2.3.*) inhibitors EC 1.2.3.* (oxidoreductase acting on donor aldehyde/oxo group with oxygen as acceptor) inhibitor CHEBI:76858 An EC 1.3.* (oxidoreductase acting on donor CH-CH group) inhibitor that interferes with the function of any such enzyme in the EC 1.3.98.* (with other, known, acceptors) category. EC 1.3.98.* (oxidoreductase acting on CH-CH group of donors, with other, known, acceptors) inhibitor EC 1.3.98.* (oxidoreductase acting on CH-CH group of donors, with other, known, acceptors) inhibitors EC 1.3.98.* (oxidoreductase acting on donor CH-CH group, with other, known, acceptors) inhibitors EC 1.3.98.* inhibitor EC 1.3.98.* inhibitors oxidoreductase acting on CH-CH group of donors, with other, known, acceptors (EC 1.3.98.*) inhibitor oxidoreductase acting on CH-CH group of donors, with other, known, acceptors (EC 1.3.98.*) inhibitors EC 1.3.98.* (oxidoreductase acting on donor CH-CH group, with other, known, acceptors) inhibitor CHEBI:76863 An EC 1.5.* (oxidoreductase acting on donor CH-NH group) inhibitor that interferes with the action of any such enzyme using NAD(+) or NADP(+) as acceptor (EC 1.5.1.*). EC 1.5.1.* (oxidoreductase acting on donor CH-NH group, NAD(+) or NADP(+) as acceptor) inhibitors EC 1.5.1.* inhibitor EC 1.5.1.* inhibitors oxidoreductase acting on donor CH-NH group, NAD(+) or NADP(+) as acceptor (EC 1.5.1.*) inhibitor oxidoreductase acting on donor CH-NH group, NAD(+) or NADP(+) as acceptor (EC 1.5.1.*) inhibitors EC 1.5.1.* (oxidoreductase acting on donor CH-NH group, NAD(+) or NADP(+) as acceptor) inhibitor CHEBI:76866 An EC 1.6.* (oxidoreductase acting on NADH or NADPH) inhibitor that interferes with the action of any such enzyme using a quinone or similar as acceptor (EC 1.6.5.*). EC 1.6.5.* (oxidoreductase acting on NADH or NADPH with a quinone or similar as acceptor) inhibitors EC 1.6.5.* inhibitor EC 1.6.5.* inhibitors oxidoreductase acting on NADH or NADPH with a quinone or similar as acceptor (EC 1.6.5.*) inhibitor oxidoreductase acting on NADH or NADPH with a quinone or similar as acceptor (EC 1.6.5.*) inhibitors EC 1.6.5.* (oxidoreductase acting on NADH or NADPH with a quinone or similar as acceptor) inhibitor CHEBI:76869 An EC 1.8.* (oxidoreductase acting on sulfur group of donors) inhibitor that interferes with the action of any such enzyme using NAD(+) or NADP(+) as acceptor (EC 1.8.1.*). EC 1.8.1.* (oxidoreductase acting on sulfur group of donors, NAD(+) or NADP(+) as acceptor) inhibitors EC 1.8.1.* inhibitor EC 1.8.1.* inhibitors oxidoreductase acting on sulfur group of donors, NAD(+) or NADP(+) as acceptor (EC 1.8.1.*) inhibitor oxidoreductase acting on sulfur group of donors, NAD(+) or NADP(+) as acceptor (EC 1.8.1.*) inhibitors EC 1.8.1.* (oxidoreductase acting on sulfur group of donors, NAD(+) or NADP(+) as acceptor) inhibitor CHEBI:76871 An EC 2.1.* (C1-transferase) inhibitor that interferes with the action of any methyltransferase (EC 2.1.1.*). EC 2.1.1.* (methyltransferase) inhibitor EC 2.1.1.* (methyltransferase) inhibitors EC 2.1.1.* (methyltransferases) inhibitors EC 2.1.1.* inhibitor EC 2.1.1.* inhibitors methyltransferase (EC 2.1.1.*) inhibitor methyltransferase (EC 2.1.1.*) inhibitors EC 2.1.1.* (methyltransferases) inhibitor CHEBI:76878 An EC 2.3.* (acyltransferase) inhibitor that inhibits the action of any acyltransferase transferring groups other than amino-acyl groups (EC 2.3.1.*). EC 2.3.1.* (acyltransferase transferring other than amino-acyl group) inhibitors EC 2.3.1.* inhibitor EC 2.3.1.* inhibitors acyltransferase transferring other than amino-acyl group EC 2.3.1.* inhibitor acyltransferase transferring other than amino-acyl group EC 2.3.1.* inhibitors EC 2.3.1.* (acyltransferase transferring other than amino-acyl group) inhibitor CHEBI:76881 An EC 2.7.* (P-containing group transferase) inhibitor that interferes with the action of any phosphotransferase with an alcohol group as acceptor (EC 2.7.1.*). EC 2.7.1.* (phosphotransferases with an alcohol group as acceptor) inhibitor CHEBI:76895 An EC 3.6.* (hydrolases acting on acid anhydrides) inhibitor that interferes with the action of any such enzyme that catalyses transmembrane movement of substances (EC 3.6.3.*). EC 3.6.3.* (acid anhydride hydrolase catalysing transmembrane movement of substances) inhibitors EC 3.6.3.* inhibitor EC 3.6.3.* inhibitors acid anhydride hydrolase catalysing transmembrane movement of substances (EC 3.6.3.*) inhibitor acid anhydride hydrolase catalysing transmembrane movement of substances (EC 3.6.3.*) inhibitors EC 3.6.3.* (acid anhydride hydrolase catalysing transmembrane movement of substances) inhibitor CHEBI:76898 An EC 1.14.14.* (oxidoreductase acting on paired donors, incorporating of 1 atom of oxygen, with reduced flavin or flavoprotein as one donor) inhibitor that interferes with the action of an unspecified monooxygenase (EC 1.14.14.1). EC 1.14.14.1 (unspecific monooxygenase) inhibitors EC 1.14.14.1 inhibitor EC 1.14.14.1 inhibitors aryl hydrocarbon hydroxylase inhibitor aryl hydrocarbon hydroxylase inhibitors aryl-4-monooxygenase inhibitor aryl-4-monooxygenase inhibitors flavoprotein monooxygenase inhibitor flavoprotein monooxygenase inhibitors flavoprotein-linked monooxygenase inhibitor flavoprotein-linked monooxygenase inhibitors microsomal P-450 inhibitor microsomal P-450 inhibitors microsomal monooxygenase inhibitor microsomal monooxygenase inhibitors substrate,reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidising) inhibitor substrate,reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidising) inhibitors unspecific monooxygenase (EC 1.14.14.1) inhibitor unspecific monooxygenase (EC 1.14.14.1) inhibitors unspecific monooxygenase inhibitor unspecific monooxygenase inhibitors xenobiotic monooxygenase inhibitor xenobiotic monooxygenase inhibitors EC 1.14.14.1 (unspecific monooxygenase) inhibitor CHEBI:76907 An EC 4.2.* (C-O lyase) inhibitor that interferes with the action of any hydro-lyase (EC 4.2.1.*). EC 4.2.1.* (hydro-lyase) inhibitor EC 4.2.1.* (hydro-lyase) inhibitors EC 4.2.1.* (hydro-lyases) inhibitors EC 4.2.1.* inhibitor EC 4.2.1.* inhibitors hydro-lyase (EC 4.2.1.*) inhibitor hydro-lyase (EC 4.2.1.*) inhibitors EC 4.2.1.* (hydro-lyases) inhibitor CHEBI:76932 An enzyme inhibitor that interferes with one or more steps in a metabolic pathway. An enzyme inhibitor that interferes with one or more steps in a signaling or metabolic pathway. metabolic pathway inhibitor metabolic pathway inhibitors pathway inhibitors pathway inhibitor CHEBI:76946 Any eukaryotic metabolite produced during a metabolic reaction in fungi, the kingdom that includes microorganisms such as the yeasts and moulds. fungal metabolites fungal metabolite CHEBI:76964 Any fungal metabolite produced during a metabolic reaction in Penicillium. Penicillium metabolites Penicillium metabolite CHEBI:76967 Any human metabolite produced by metabolism of a xenobiotic compound in humans. human xenobiotic metabolites human xenobiotic metabolite CHEBI:76969 Any prokaryotic metabolite produced during a metabolic reaction in bacteria. bacterial metabolite CHEBI:76971 Any bacterial metabolite produced during a metabolic reaction in Escherichia coli. E.coli metabolite E.coli metabolites Escherichia coli metabolites Escherichia coli metabolite CHEBI:76998 An antagonist that binds to and inactivates aryl hydrocarbon receptors (AhRs). AhR antagonist AhR receptor antagonist aryl hydrocarbon receptor antagonist CHEBI:77102 An EC 1.3.* (oxidoreductase acting on donor CH-CH group) inhibitor that interferes with the action of any such enzyme using a quinone or related compound as acceptor (EC 1.3.5.*). EC 1.3.5.* (oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor) inhibitors EC 1.3.5.* inhibitor EC 1.3.5.* inhibitors inhibitor of oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor inhibitor of oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor (EC 1.3.5.*) inhibitors of oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor inhibitors of oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor (EC 1.3.5.*) oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor (EC 1.3.5.*) inhibitor oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor (EC 1.3.5.*) inhibitors EC 1.3.5.* (oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor) inhibitor CHEBI:77103 An EC 1.3.5.* (oxidoreductase acting on CH-CH of donor with a quinone or related compound as acceptor) inhibitor that interferes with the action of dihydroorotate dehydrogenase (quinone), EC 1.3.5.2. (S)-dihydroorotate:(acceptor) oxidoreductase inhibitor (S)-dihydroorotate:(acceptor) oxidoreductase inhibitors (S)-dihydroorotate:acceptor oxidoreductase inhibitor (S)-dihydroorotate:acceptor oxidoreductase inhibitors (S)-dihydroorotate:quinone oxidoreductase inhibitor (S)-dihydroorotate:quinone oxidoreductase inhibitors DHOD inhibitor DHOD inhibitors DHODH inhibitor DHODH inhibitors DHOdehase inhibitor DHOdehase inhibitors EC 1.3.5.2 (dihydroorotate dehydrogenase (quinone)) inhibitor EC 1.3.5.2 (dihydroorotate dehydrogenase (quinone)) inhibitors EC 1.3.5.2 [dihydroorotate dehydrogenase (quinone)] inhibitors EC 1.3.5.2 inhibitor EC 1.3.5.2 inhibitors dihydroorotate:ubiquinone oxidoreductase inhibitor dihydroorotate:ubiquinone oxidoreductase inhibitors EC 1.3.5.2 [dihydroorotate dehydrogenase (quinone)] inhibitor CHEBI:77105 An EC 1.10.* (oxidoreductase acting on diphenols and related substances as donors) inhibitor that interferes with the action of any such enzyme using a cytochrome as acceptor (EC 1.10.2.*). EC 1.10.2.* (oxidoreductase acting on diphenols and related substances as donors with a cytochrome as acceptor) inhibitors EC 1.10.2.* inhibitor EC 1.10.2.* inhibitors inhibitor of an oxidoreductase acting on diphenols and related substances as donors with a cytochrome as acceptor (EC 1.10.2.*) inhibitors of an oxidoreductase acting on diphenols and related substances as donors with a cytochrome as acceptor (EC 1.10.2.*) oxidoreductase acting on diphenols and related substances as donors with a cytochrome as acceptor (EC 1.10.2.*) inhibitor oxidoreductase acting on diphenols and related substances as donors with a cytochrome as acceptor (EC 1.10.2.*) inhibitors EC 1.10.2.* (oxidoreductase acting on diphenols and related substances as donors with a cytochrome as acceptor) inhibitor CHEBI:77106 An EC 1.10.2.* (oxidoreductase acting on diphenols and related substances as donors with a cytochrome as acceptor) inhibitor that interferes with the action of quinol--cytochrome-c reductase (EC 1.10.2.2). EC 1.10.2.2 (quinol--cytochrome-c reductase) inhibitors EC 1.10.2.2 inhibitor EC 1.10.2.2 inhibitors inhibitor of quinol--cytochrome-c reductase (EC 1.10.2.2) inhibitors of quinol--cytochrome-c reductase (EC 1.10.2.2) quinol--cytochrome-c reductase (EC 1.10.2.2) inhibitor quinol--cytochrome-c reductase (EC 1.10.2.2) inhibitors EC 1.10.2.2 (quinol--cytochrome-c reductase) inhibitor CHEBI:77113 An EC 2.7.11.* (protein-serine/threonine kinase) inhibitor that interferes with the action of IkappaB kinase (EC 2.7.11.10). Wikipedia:IkappaB_kinase EC 2.7.11.10 (IkappaB kinase) inhibitor ATP:[IkappaB protein] phosphotransferase inhibitor IKK inhibitor IkappaB kinase inhibitor IkappaB kinase inhibitor CHEBI:77326 An agonist that selectively binds to and activates androstane receptors. Wikipedia:Constitutive_androstane_receptor CAR agonist constitutive androstane receptor agonist androstane receptor agonist CHEBI:77402 An EC 1.8.1.* (oxidoreductase acting on sulfur group of donors, NAD+ or NADP+ as acceptor) inhibitor that interferes with the action of trypanothione-disulfide reductase (EC 1.8.1.12). EC 1.8.1.12 (trypanothione-disulfide reductase) inhibitors EC 1.8.1.12 inhibitor EC 1.8.1.12 inhibitors N(1),N(8)-bis(glutathionyl)spermidine reductase inhibitor N(1),N(8)-bis(glutathionyl)spermidine reductase inhibitors NADPH2:trypanothione oxidoreductase inhibitor NADPH2:trypanothione oxidoreductase inhibitors NADPH:trypanothione oxidoreductase inhibitor NADPH:trypanothione oxidoreductase inhibitors trypanothione reductase inhibitor trypanothione reductase inhibitors trypanothione-disulfide reductase (EC 1.8.1.12) inhibitor trypanothione-disulfide reductase (EC 1.8.1.12) inhibitors trypanothione:NADP(+) oxidoreductase inhibitor trypanothione:NADP(+) oxidoreductase inhibitors EC 1.8.1.12 (trypanothione-disulfide reductase) inhibitor CHEBI:7772 A racemate comprising equimolar amounts of (R)- and (S)-omeprazole. Beilstein:3628192 CAS:73590-58-6 DrugBank:DB00338 PMID:11060758 PMID:11208500 PMID:11210716 PMID:11304936 PMID:11321383 PMID:11395292 PMID:11404722 PMID:11459434 PMID:11568514 PMID:11700946 PMID:11774962 PMID:11807212 PMID:11851112 PMID:11903739 PMID:11962536 PMID:12072663 PMID:12135028 PMID:12235248 PMID:12495367 PMID:12683615 PMID:13680386 PMID:14616415 PMID:14708212 PMID:14725575 PMID:15004262 PMID:15125696 PMID:15586641 PMID:15598025 PMID:15684503 PMID:15707461 PMID:15774534 PMID:16080278 PMID:16129922 PMID:16259581 PMID:16276979 PMID:16380990 PMID:16386527 PMID:16397810 PMID:16440530 PMID:16998872 PMID:17049542 PMID:17384694 PMID:17532167 PMID:18294333 PMID:18366242 PMID:18416943 PMID:18448060 PMID:18498918 PMID:18520598 PMID:18571645 PMID:18616070 PMID:18793272 PMID:18818790 PMID:19150046 PMID:19166730 PMID:19176055 PMID:19236757 PMID:19327607 PMID:19383986 PMID:19434360 PMID:19470853 PMID:19517893 PMID:19746659 PMID:19796313 PMID:19801857 PMID:19937171 Patent:EP5129 Patent:US4255431 Patent:US5693818 Reaxys:3628192 VSDB:1827 Wikipedia:Omeprazole rac-5-methoxy-2-{[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]sulfinyl}-1H-benzimidazole 5-methoxy-2-{[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]sulfinyl}-1H-benzimidazole Antra Audazol Belmazol Ceprandal Danlox Desec Elgam Emeproton Gasec Gastrimut Indurgan Inhibitron Losec OMEP OMP OMZ Olit Omapren Omebeta Prazidec Procelac Sanamidol Ulceral Ulcesep Ultop omeprazol omeprazole omeprazolum omeprazole CHEBI:77731 A role played by the entity that activates p53. p53 activator CHEBI:77746 Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens). H. sapiens metabolite H. sapiens metabolites Homo sapiens metabolite Homo sapiens metabolites human metabolite CHEBI:77748 An EC 3.6.3.* (acid anhydride hydrolase catalysing transmembrane movement of substances) inhibitor that interferes with the action of xenobiotic-transporting ATPase (EC 3.6.3.44). ATP phosphohydrolase (steroid-exporting) inhibitor ATP phosphohydrolase (steroid-exporting) inhibitors ATP phosphohydrolase (xenobiotic-exporting) inhibitor ATP phosphohydrolase (xenobiotic-exporting) inhibitors EC 3.6.3.44 (xenobiotic-transporting ATPase) inhibitors EC 3.6.3.44 inhibitor EC 3.6.3.44 inhibitors MDR protein inhibitor MDR protein inhibitors P-glycoprotein inhibitor P-glycoprotein inhibitors PDR protein inhibitor PDR protein inhibitors multidrug-resistance protein inhibitor multidrug-resistance protein inhibitors pleiotropic-drug-resistance protein inhibitor pleiotropic-drug-resistance protein inhibitors steroid-transporting ATPase inhibitor steroid-transporting ATPase inhibitors xenobiotic-transporting ATPase (EC 3.6.3.44) inhibitor xenobiotic-transporting ATPase (EC 3.6.3.44) inhibitors xenobiotic-transporting ATPase inhibitor xenobiotic-transporting ATPase inhibitors EC 3.6.3.44 (xenobiotic-transporting ATPase) inhibitor CHEBI:7798 A cyclohexenecarboxylate ester that is the ethyl ester of oseltamivir acid. An antiviral prodrug (it is hydrolysed to the active free carboxylic acid in the liver), it is used to slow the spread of influenza. 0 C16H28N2O4 InChI=1S/C16H28N2O4/c1-5-12(6-2)22-14-9-11(16(20)21-7-3)8-13(17)15(14)18-10(4)19/h9,12-15H,5-8,17H2,1-4H3,(H,18,19)/t13-,14+,15+/m0/s1 VSZGPKBBMSAYNT-RRFJBIMHSA-N 312.40450 312.20491 CCOC(=O)C1=C[C@@H](OC(CC)CC)[C@H](NC(C)=O)[C@@H](N)C1 Beilstein:8003908 CAS:196618-13-0 DrugBank:DB00198 Drug_Central:2001 HMDB:HMDB0014343 PMID:11075941 PMID:11270942 PMID:11825310 PMID:17912363 PMID:18559644 PMID:18936828 PMID:19355841 PMID:19439487 PMID:19557131 PMID:19884755 Patent:US5763483 Reaxys:8003908 Wikipedia:Oseltamivir Oseltamivir ethyl (3R,4R,5S)-4-acetamido-5-amino-3-(pentan-3-yloxy)cyclohex-1-ene-1-carboxylate (-)-oseltamivir 1-Cyclohexene-1-carboxylic acid, 4-(acetylamino)-5-amino-3-(1-ethylpropoxy)-, ethyl ester, (3R-(3alpha,4beta,5alpha))- Agucort Ethyl (3R,4R,5S)-4-acetamido-5-amino-3-(1-ethylpropoxy)-1-cyclohexene-1-carboxylate GS-4104 HSDB 7433 Tamiflu oseltamivir oseltamivirum oseltamivir CHEBI:7820 Beilstein:5480667 DrugBank:DB00621 Drug_Central:2011 17beta-hydroxy-17alpha-methyl-2-oxa-5alpha-androstan-3-one Oxandrolone oxandrolona oxandrolone oxandrolonum oxandrolone Beilstein:5480667 Beilstein Drug_Central:2011 DrugCentral CHEBI:78298 Any minor or unwanted substance introduced into the environment that can have undesired effects. environmental contaminants environmental contaminant CHEBI:78444 Any EC 3.1.1.* (carboxylic ester hydrolase) inhibitor that inhibits the action of carboxylesterase (EC 3.1.1.1 ). Alpha-carboxylesterase inhibitor Alpha-carboxylesterase inhibitors Beta-esterase inhibitor Beta-esterase inhibitors EC 3.1.1.1 (carboxylesterase) inhibitors ali-esterase inhibitor ali-esterase inhibitors butyrate esterase inhibitor butyrate esterase inhibitors butyryl esterase inhibitor butyryl esterase inhibitors carboxyl ester hydrolase inhibitor carboxyl ester hydrolase inhibitors carboxylate esterase inhibitor carboxylate esterase inhibitors carboxylesterase inhibitor carboxylesterase inhibitors carboxylic acid esterase inhibitor carboxylic acid esterase inhibitors carboxylic esterase inhibitor carboxylic esterase inhibitors carboxylic-ester hydrolase inhibitor carboxylic-ester hydrolase inhibitors cocaine esterase inhibitor cocaine esterase inhibitors esterase A inhibitor esterase A inhibitors esterase B inhibitor esterase B inhibitors esterase D inhibitor esterase D inhibitors methylbutyrase inhibitor methylbutyrase inhibitors methylbutyrate esterase inhibitor methylbutyrate esterase inhibitors monobutyrase inhibitor monobutyrase inhibitors nonspecific carboxylesterase inhibitor nonspecific carboxylesterase inhibitors procaine esterase inhibitor procaine esterase inhibitors propionyl esterase inhibitor propionyl esterase inhibitors serine esterase inhibitor serine esterase inhibitors triacetin esterase inhibitor triacetin esterase inhibitors vitamin A esterase inhibitor vitamin A esterase inhibitors EC 3.1.1.1 (carboxylesterase) inhibitor CHEBI:7864 A 3-oxo-5alpha- steroid that is 4,5alpha-dihydrotestosterone which is substituted by a hydroxymethylidene group at position 2 and by a methyl group at the 17alpha position. A synthetic androgen, it was mainly used for the treatment of anaemias until being replaced by treatments with fewer side effects. CAS:434-07-1 PMID:11071398 PMID:1125426 PMID:11440282 PMID:21860526 Reaxys:2623806 17beta-hydroxy-2-(hydroxymethylidene)-17-methyl-5alpha-androstan-3-one (5alpha,17beta)-17-hydroxy-2-(hydroxymethylidene)-17-methylandrostan-3-one 17alpha-methyl-2-hydroxymethylene-17-hydroxy-5alpha-androstan-3-one 17beta-hydroxy-2-(hydroxymethylene)-17-methyl-5alpha-androstan-3-one 2-hydroxymethylene-17alpha-methyl-17beta-hydroxy-5alpha-androstan-3-one 2-hydroxymethylene-17alpha-methyl-5alpha-androstan-17beta-ol-3-one 2-hydroxymethylene-17alpha-methyldihydrotestosterone 4,5alpha-dihydro-2-hydroxymethylene-17alpha-methyltestosterone Adroyd Anadrol-50 Anapolon Nastenon Pardroyd Plenastril Protanabol Synasteron oximetolona oxymetholone oxymetholonum oxymetholone CAS:434-07-1 ChemIDplus CAS:434-07-1 NIST Chemistry WebBook PMID:11071398 Europe PMC PMID:1125426 Europe PMC PMID:11440282 Europe PMC PMID:21860526 Europe PMC Reaxys:2623806 Reaxys CHEBI:791 A steroid glucosiduronic acid that consists of 17β-estradiol having a beta-glucuronyl residue attached at position 17 via a glycosidic linkage. InChIKey:MTKNDAQYHASLID-QXYWQCSFSA-N Nikkaji:J386.923G http://purl.bioontology.org/ontology/MESH/C025483 Estradiol-17beta-glucuronide 17β-estradiol 17-glucosiduronic acid CHEBI:7953 A member of the class of 1,3-oxazoles that is 1,3-oxazol-4(5H)-one which is substituted by an amino group at position 2 and by a phenyl group at position 5. A central nervous system stimulant, it was used to treat hyperactivity disorders in children, but withdrawn from use following reports of serious hepatotoxicity. CAS:2152-34-3 DrugBank:DB01230 Drug_Central:2075 LINCS:LSM-5159 PMID:11216184 PMID:2210262 PMID:2303976 PMID:2388127 PMID:4021028 PMID:641739 PMID:772696 Reaxys:151559 2-amino-5-phenyl-1,3-oxazol-4(5H)-one 2-Amino-5-phenyl-4(5H)-oxazolone 2-imino-4-keto-5-phenyltetrahydrooxazole 2-imino-5-phenyl-4-oxazolidinone 5-phenyl-2-imino-4-oxazolidinone 5-phenyl-2-imino-4-oxooxazolidine 5-phenylisohydantion Azoxodon Betanamin Cylert Dantromin Deltamine Hyton Myamin Nitan Notair pemolina pemoline pemolinum pheniminooxazolidinone phenylisohydantoin phenylpseudohydantoin pemoline CAS:2152-34-3 ChemIDplus CAS:2152-34-3 NIST Chemistry WebBook Drug_Central:2075 DrugCentral PMID:11216184 Europe PMC PMID:2210262 Europe PMC PMID:2303976 Europe PMC PMID:2388127 Europe PMC PMID:4021028 Europe PMC PMID:641739 Europe PMC PMID:772696 Europe PMC Reaxys:151559 Reaxys CHEBI:8069 A member of the class of barbiturates, the structure of which is that of barbituric acid substituted at C-5 by ethyl and phenyl groups. C12H12N2O3 CCC1(C(=O)NC(=O)NC1=O)c1ccccc1 CAS:50-06-6 CHEBI:8069 DrugBank:DB01174 Open TG-Gates compound_id=00004 https://livertox.nlm.nih.gov//Phenobarbital.htm phenobarbital CHEBI:8107 A imidazolidine-2,4-dione that consists of hydantoin bearing two phenyl substituents at position 5. Beilstein:384532 CAS:57-41-0 DrugBank:DB00252 Drug_Central:2152 LINCS:LSM-5663 PMID:10698828 PMID:12952753 PMID:15246836 PMID:15744730 PMID:16303054 PMID:7105825 PMID:7602118 PMID:9186244 Reaxys:384532 5,5-diphenylimidazolidine-2,4-dione 5,5-Diphenyl-imidazolidine-2,4-dione 5,5-diphenylimidazolidine-2,4-dione 5,5-diphenyltetrahydro-1H-2,4-imidazoledione DILANTIN PHENTYTOIN fenitoina phenytoin phenytoine phenytoinum phenytoin Beilstein:384532 Beilstein CAS:57-41-0 ChemIDplus Drug_Central:2152 DrugCentral PMID:10698828 Europe PMC PMID:12952753 Europe PMC PMID:15246836 Europe PMC PMID:15744730 Europe PMC PMID:16303054 Europe PMC PMID:7105825 Europe PMC PMID:7602118 Europe PMC PMID:9186244 Europe PMC Reaxys:384532 Reaxys CHEBI:82824 An EC 3.4.22.* (cysteine endopeptidase) inhibitor that interferes with the action of any calpain. calpain inhibitor CHEBI:83039 An animal metabolite produced by arthropods such as crabs, lobsters, crayfish, shrimps and krill. crustacean metabolites crustacean metabolite CHEBI:83056 A Daphnia metabolite produced by the species Daphnia magna. Daphnia magna metabolites Daphnia magna metabolite CHEBI:83057 A crustacean metabolite produced by the genus of small planktonic arthropods, Daphnia Daphnia metabolites Daphnia metabolite CHEBI:83317 Any compound that inhibits the biosynthesis of any sterol. sterol biosynthesis inhibitors sterol biosynthesis inhibitor CHEBI:83612 Any hepatotoxic agent capable of inducing liver steatosis or fatty liver disease. hepatic steatosis inducing drugs hepatic steatosis inducing agent CHEBI:85010 A hydrazine in which each nitrogen atom is substituted, one by a 3'-carboxy-2-hydroxy[1,1'-biphenyl]-3-yl group and the other by a 1-(3,4-dimethylphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene group. A small molecule agonist of the c-mpl (TpoR) receptor (the physiological target of the hormone thrombopoietin), it has been developed as a medication for conditions that lead to thrombocytopenia (abnormally low platelet counts). CAS:496775-61-2 Drug_Central:4399 PMID:24433306 PMID:25063763 PMID:25170628 PMID:25400215 PMID:25578417 PMID:25700916 3'-{(2Z)-2-[1-(3,4-dimethylphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]hydrazinyl}-2'-hydroxy[1,1'-biphenyl]-3-carboxylic acid 3'-{(2Z)-2-[1-(3,4-dimethylphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]hydrazino}-2'-hydroxybiphenyl-3-carboxylic acid eltrombopag CAS:496775-61-2 ChemIDplus Drug_Central:4399 DrugCentral PMID:24433306 Europe PMC PMID:25063763 Europe PMC PMID:25170628 Europe PMC PMID:25400215 Europe PMC PMID:25578417 Europe PMC PMID:25700916 Europe PMC CHEBI:85012 An agonist that selectively binds to and activates the thrombopoietin receptor [myeloproliferative leukemia protein or CD110 (Cluster of Differentiation 110)]. TPO receptor agonist TPO receptor agonists thrombopoietin receptor agonists thrombopoietin receptor agonist CHEBI:86327 Any antifungal agent used to prevent or treat fungal infections in humans or animals. Wikipedia:Antifungal antifungal drug CHEBI:86328 Any substance used in acriculture, horticulture, forestry, etc. for its fungicidal properties. agrichemical fungicide agrichemical fungicides agrochemical fungicide agrochemical fungicides anti-fungal agrichemical anti-fungal agrichemicals anti-fungal agrochemical anti-fungal agrochemicals antifungal agrichemical antifungal agrichemicals antifungal agrochemicals antifungal agrochemical CHEBI:88188 Any drug which causes the onset of an allergic reaction. allergenic drug drug allergen CHEBI:88230 Any compound that inhibits the process of autophagy (the self-digestion of one or more components of a cell through the action of enzymes originating within the same cell). PMID:24830781 PMID:25727221 PMID:25793774 PMID:25896709 Wikipedia:Autophagy autophagocytosis inhibitor autophagy inhibitor CHEBI:8863 CAS:1744-22-5 Drug_Central:2382 LINCS:LSM-2471 Riluzole 6-Trifluoromethoxybenzothiazol-2-ylamine RP-54274 RP54274 rilutek rilutor riluzole HCl riluzole hydrochloride Riluzole Drug_Central:2382 DrugCentral CHEBI:90233 A 1-monoglyceride resulting from the condensation of the carboxy group of prostaglandin F2alpha with the 1-hydroxy group of glycerol. prostaglandin F2alpha 1-glyceryl ester CHEBI:90454 A glycerophosphoglycerol resulting from partial hydrolysis of a phosphatidylglycerol, which removes one of the fatty acid groups. The structure is depicted in the image where R1 = acyl, R2 = H or where R1 = H, R2 = acyl. monoacylglycerophosphoglycerol lysophosphatidylglycerol CHEBI:90710 A drug that acts as an antagonist, agonist, reverse agonist, or in some other fashion when interacting with cellular receptors. receptor modulators receptor modulator CHEBI:91079 An antagonist at purinergic P2 receptors P2 antagonist P2 antagonists non-selective P2 purinergic antagonist non-selective P2 purinergic antagonists purinergic receptor P2 antagonists purinergic receptor P2 antagonist CHEBI:9334 An azobenzene consisting of diphenyldiazene having a carboxy substituent at the 4-position, a hydroxy substituent at the 3-position and a 2-pyridylaminosulphonyl substituent at the 4'-position. Beilstein:356241 Beilstein:8132868 CAS:599-79-1 DrugBank:DB00795 Gmelin:2666050 PMID:11362329 PMID:11485124 PMID:11587223 PMID:14981898 PMID:15248210 PMID:16322111 PMID:17386570 PMID:2434548 PMID:7720170 Reaxys:8132868 2-hydroxy-5-{[4-(pyridin-2-ylsulfamoyl)phenyl]diazenyl}benzoic acid Sulfasalazine 2-Hydroxy-5-((4-((2-pyridinylamino)sulfonyl)phenyl)azo)benzoic acid 2-Hydroxy-5-[4-(pyridin-2-ylsulfamoyl)-phenylazo]-benzoic acid 4-(Pyridyl-2-amidosulfonyl)-3'-carboxy-4'-hydroxyazobenzene 5-((p-(2-Pyridylsulfamoyl)phenyl)azo)salicylic acid 5-(4-(2-Pyridylsulfamoyl)phenylazo)-2-hydroxybenzoic acid 5-(p-(2-Pyridylsulfamyl)phenylazo)salicylic acid Azulfidine Salazosulfapiridina Salazosulfapyridine Salazosulfapyridinum Salicylazosulfapyridine Sulfasalazina Sulfasalazinum sulfasalazine sulfasalazine Beilstein:356241 Beilstein Beilstein:8132868 Beilstein CAS:599-79-1 ChemIDplus Gmelin:2666050 Gmelin PMID:11362329 Europe PMC PMID:11485124 Europe PMC PMID:11587223 Europe PMC PMID:14981898 Europe PMC PMID:15248210 Europe PMC PMID:16322111 Europe PMC PMID:17386570 Europe PMC PMID:2434548 Europe PMC PMID:7720170 Europe PMC Reaxys:8132868 Reaxys CHEBI:9337 A 1,3-thiazole compound having a 4-aminobenzenesulfonamido group at the 2-position. Beilstein:226178 CAS:72-14-0 DrugBank:DB06147 Drug_Central:2527 Gmelin:218965 LINCS:LSM-5327 PMID:11431418 PMID:7486915 Reaxys:226178 4-amino-N-1,3-thiazol-2-ylbenzenesulfonamide 2-(Sulfanilylamino)thiazole 2-(p-Aminobenzenesulfonamido)thiazole 2-(p-Aminobenzenesulphonamido)thiazole 2-Sulfanilamidothiazol 2-Sulfanilamidothiazole 2-Sulfonamidothiazole 4-Amino-N-2-thiazolylbenzenesulfonamide N(1)-2-Thiazolylsulfanilamide Sulfanilamidothiazole Sulfatiazol Sulphathiazole sulfathiazol sulfathiazole sulfathiazolum sulfthiazole sulfathiazole Beilstein:226178 Beilstein CAS:72-14-0 ChemIDplus CAS:72-14-0 NIST Chemistry WebBook Drug_Central:2527 DrugCentral Gmelin:218965 Gmelin PMID:11431418 Europe PMC PMID:7486915 Europe PMC Reaxys:226178 Reaxys CHEBI:9352 A monocarboxylic acid that is 1-benzylidene-1H-indene which is substituted at positions 2, 3, and 5 by methyl, carboxymethyl, and fluorine respectively, and in which the phenyl group of the benzylidene moiety is substituted at the para position by a methylsulfinyl group. It is a prodrug for the corresponding sulfide, a non-steroidal anti-inflammatory drug, used particularly in the treatment of acute and chronic inflammatory conditions. CC1=C(CC(O)=O)c2cc(F)ccc2C\1=C/c1ccc(cc1)S(C)=O ATC:M01AB02 Beilstein:2951842 CAS:38194-50-2 DrugBank:DB00605 Drug_Central:2534 PMID:11569947 PMID:11927004 PMID:12406542 PMID:15020200 PMID:15123337 PMID:19884509 PMID:23689354 PMID:23804703 Reaxys:2951842 Wikipedia:Sulindac Sulindac {(1Z)-5-fluoro-2-methyl-1-[4-(methylsulfinyl)benzylidene]-1H-inden-3-yl}acetic acid (Z)-5-Fluoro-2-methyl-1-((p-(methylsulfinyl)phenyl)methylene)-1H-indene-3-acetic acid Clinoril Sulindacum cis-5-Fluoro-2-methyl-1-((4-(methylsulfinyl)phenyl)methylene)-1H-indene-3-acetic acid cis-5-Fluoro-2-methyl-1-((p-methylsulfinyl)benzylidene)indene-3-acetic acid sulindac sulindaco sulindac Beilstein:2951842 Beilstein CAS:38194-50-2 ChemIDplus CAS:38194-50-2 NIST Chemistry WebBook Drug_Central:2534 DrugCentral PMID:11569947 Europe PMC PMID:11927004 Europe PMC PMID:12406542 Europe PMC PMID:15020200 Europe PMC PMID:15123337 Europe PMC PMID:19884509 Europe PMC PMID:23689354 Europe PMC PMID:23804703 Europe PMC Reaxys:2951842 Reaxys CHEBI:9448 A tertiary amine that is N-methyl-1-naphthalenemethylamine in which the amino hydrogen is replaced by a 3-(tertbutylethynyl)allyl group. An antifungal agent administered orally (generally as the hydrochloride salt) for the treatment of skin and nail infections. CAS:91161-71-6 DrugBank:DB00857 Drug_Central:2597 PMID:23750489 PMID:23802806 PMID:23841559 PMID:23895037 PMID:24126579 PMID:24352873 PMID:24389279 PMID:24410098 PMID:24447130 PMID:24452843 PMID:24477462 PMID:24490976 PMID:24497012 PMID:24533442 PMID:24563892 PMID:24576265 PMID:24581620 PMID:24588014 Reaxys:4256376 (2E)-N,6,6-trimethyl-N-(1-naphthylmethyl)hept-2-en-4-yn-1-amine terbinafine (E)-N-(6,6-Dimethyl-2-hepten-4-ynyl)-N-methyl-1-naphthalene methanamine (E)-N-(6,6-Dimethyl-2-hepten-4-ynyl)-N-methyl-1-naphthalenemethylamine terbinafina terbinafine terbinafinum terbinafine CAS:91161-71-6 ChemIDplus Drug_Central:2597 DrugCentral PMID:23750489 Europe PMC PMID:23802806 Europe PMC PMID:23841559 Europe PMC PMID:23895037 Europe PMC PMID:24126579 Europe PMC PMID:24352873 Europe PMC PMID:24389279 Europe PMC PMID:24410098 Europe PMC PMID:24447130 Europe PMC PMID:24452843 Europe PMC PMID:24477462 Europe PMC PMID:24490976 Europe PMC PMID:24497012 Europe PMC PMID:24533442 Europe PMC PMID:24563892 Europe PMC PMID:24576265 Europe PMC PMID:24581620 Europe PMC PMID:24588014 Europe PMC Reaxys:4256376 Reaxys CHEBI:94686 A carboxylic ester resulting from the formal condensation of the carboxy group of N-formyl-L-leucine with the hydroxy group of (3S,4S)-3-hexyl-4-[(2S)-2-hydroxytridecyl]oxetan-2-one. A pancreatic lipase inhibitor, it is used as an anti-obesity drug. CAS:96829-58-2 Drug_Central:1996 LINCS:LSM-5724 PMID:27793869 PMID:28097013 PMID:28191026 PMID:28260907 PMID:28387458 PMID:28559211 PMID:28588183 PMID:28624425 Reaxys:3658031 (2S)-1-[(2S,3S)-3-hexyl-4-oxooxetan-2-yl]tridecan-2-yl N-formyl-L-leucinate (-)-tetrahydrolipostatin (2S)-2-formamido-4-methylpentanoic acid [(2S)-1-[(2S,3S)-3-hexyl-4-oxo-2-oxetanyl]tridecan-2-yl] ester Alli N-formyl-L-leucine (1S)-1-{[(2S,3S)-3-hexyl-4-oxo-2-oxetanyl]methyl}dodecyl ester Ro-18-0647 Xenical orlipastat orlistat orlistatum orlistat CAS:96829-58-2 ChemIDplus CAS:96829-58-2 DrugCentral Drug_Central:1996 DrugCentral PMID:27793869 Europe PMC PMID:28097013 Europe PMC PMID:28191026 Europe PMC PMID:28260907 Europe PMC PMID:28387458 Europe PMC PMID:28559211 Europe PMC PMID:28588183 Europe PMC PMID:28624425 Europe PMC Reaxys:3658031 Reaxys CHEBI:9516 An organic heterotricyclic compound that is a hexa-oxygenated 6,7-guaianolide isolated fron the roots of Thapsia garganica L., Apiaceae. A potent skin irritant, it is used in traditional medicine as a counter-irritant. Thapsigargin inhibits Ca(2+)-transporting ATPase mediated uptake of calcium ions into sarcoplasmic reticulum and is used in experimentation examining the impacts of increasing cytosolic calcium concentrations. C34H50O12 [H][C@@]1(OC(=O)C(\C)=C/C)[C@@H](OC(=O)CCCCCCC)[C@@]2([H])C(=C1C)[C@]1([H])OC(=O)[C@@](C)(O)[C@@]1(O)[C@H](C[C@]2(C)OC(C)=O)OC(=O)CCC CAS:67526-95-8 (3S,3aR,4S,6S,6aR,7S,8S,9bS)-6-(acetyloxy)-4-(butanoyloxy)-3,3a-dihydroxy-3,6,9-trimethyl-8-{[(2Z)-2-methylbut-2-enoyl]oxy}-2-oxo-2,3,3a,4,5,6,6a,7,8,9b-decahydroazuleno[4,5-b]furan-7-yl octanoate thapsigargin CHEBI:9588 A thienopyridine that is 4,5,6,7-tetrahydrothieno[3,2-c]pyridine in which the hydrogen attached to the nitrogen is replaced by an o-chlorobenzyl group. CAS:55142-85-3 DrugBank:DB00208 Drug_Central:2657 LINCS:LSM-1986 PMID:19180126 Reaxys:1216802 5-(2-chlorobenzyl)-4,5,6,7-tetrahydrothieno[3,2-c]pyridine ticlopidina ticlopidine ticlopidinum ticlopidine CAS:55142-85-3 ChemIDplus Drug_Central:2657 DrugCentral PMID:19180126 Europe PMC Reaxys:1216802 Reaxys CHEBI:9727 CAS:127-48-0 Drug_Central:2751 LINCS:LSM-5345 Trimethadione Tridione (TN) tridione trimetadione trimetin Trimethadione CAS:127-48-0 DrugCentral Drug_Central:2751 DrugCentral CHEBI:9753 A chromane that has formula C24H27NO5S. Troglitazone is an antidiabetic and anti-inflammatory drug, and a member of the drug class of the thiazolidinediones. It was prescribed for people with diabetes mellitus type 2. (by Wikipedia) C24H27NO5S Cc1c(C)c2OC(C)(CCc2c(C)c1O)COc1ccc(CC2SC(=O)NC2=O)cc1 Wikipedia:Troglitazone ATC:A10BG01 Beilstein:4338399 CAS:97322-87-7 DrugBank:DB00197 Drug_Central:2767 LINCS:LSM-4890 5-{4-[(6-hydroxy-2,5,7,8-tetramethyl-3,4-dihydro-2H-chromen-2-yl)methoxy]benzyl}-1,3-thiazolidine-2,4-dione Troglitazone (+-)-all-rac-5-(p-((6-Hydroxy-2,5,7,8-tetramethyl-2-chromanyl)methoxy)benzyl)-2,4-thiazolidinedione 5-(4-(6-Hydroxy-2,5,7,8-tetramethylchroman-2-ylmethoxy)benzyl)thiazolidine-2,4-dione Rezulin (TN) Romglizone troglitazona troglitazone troglitazonum troglitazone Beilstein:4338399 Beilstein CAS:97322-87-7 ChemIDplus Drug_Central:2767 DrugCentral CHEBI:9763 A 1,8-naphthyridine derivative that is 4-oxo-1,4-dihydro-1,8-naphthyridine-3-carboxylic acid bearing additional 2,4-difluorophenyl, fluoro and 6-amino-3-azabicyclo[3.1.0]hex-3-yl substituents at positions 1, 6 and 7 respectively. A broad-spectrum antibiotic that was withdrawn from the market due to risk of liver failure. CAS:147059-72-1 DrugBank:DB00685 Drug_Central:2777 PMID:20022474 PMID:20462743 PMID:20538741 PMID:20655887 PMID:21151465 PMID:22305082 PMID:23727874 PMID:24097668 PMID:24525298 Reaxys:8172628 7-[(1R,5S,6s)-6-amino-3-azabicyclo[3.1.0]hex-3-yl]-1-(2,4-difluorophenyl)-6-fluoro-4-oxo-1,4-dihydro-1,8-naphthyridine-3-carboxylic acid trovafloxacin trovafloxacine trovafloxacino trovafloxacinum trovafloxacin CAS:147059-72-1 ChemIDplus Drug_Central:2777 DrugCentral PMID:20022474 Europe PMC PMID:20462743 Europe PMC PMID:20538741 Europe PMC PMID:20655887 Europe PMC PMID:21151465 Europe PMC PMID:22305082 Europe PMC PMID:23727874 Europe PMC PMID:24097668 Europe PMC PMID:24525298 Europe PMC Reaxys:8172628 Reaxys CHEBI:9907 A bile acid found in the bile of bears (Ursidae) as a conjugate with taurine. Used therapeutically, it prevents the synthesis and absorption of cholesterol and can lead to the dissolution of gallstones. InChIKey:RUDATBOHQWOJDD-UZVSRGJWSA-N ursodeoxycholic acid Any type of microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelengths. These specimens are called fluorophores. Any type of microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelengths. These specimens are called fluorophores. fluorescence imaging aasay fluorescence microscopic imaging aasay FIX:0000123 FM fluorescence imaging fluorescence microscopic imaging CHMO:0000087 fluorescence microscopy fluorescence microscopy assay CHMO:0000087 Any type of microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelengths. These specimens are called fluorophores. https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a laser spot of specific wavelength over its surface. FLSM LSM laser scanning fluorescence microscopy laser scanning microscopy CHMO:0000088 fluorescence laser scanning microscopy CHMO:0000088 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a laser spot of specific wavelength over its surface. FIX:0000380 https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a gas (Ar or Kr) laser spot of specific wavelength over its surface and using a spatial pinhole to eliminate out-of-focus fluorescence. CLSM LSCM confocal fluorescence imaging confocal fluorescence microscopy confocal laser scanning fluorescence microscopy confocal-laser scanning microscopy fluorescence confocal microscopy fluorescence confocal scanning laser microscopy scanning confocal fluorescence microscopy CHMO:0000089 confocal laser scanning microscopy CHMO:0000089 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a gas (Ar or Kr) laser spot of specific wavelength over its surface and using a spatial pinhole to eliminate out-of-focus fluorescence. https://doi.org/10.1039/b807581f Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a solid-state (Ti sapphire) laser spot of specific wavelength over its surface to produce multi-photon fluorescence (i.e. the fluorophore simultaneously absorbs multiple photons of typically one half to one third of the energy required for single-photon excitation). FIX:0000383 MPLSM multi photon laser scanning microscopy multiphoton laser scanning microscopy CHMO:0000090 multi-photon laser scanning microscopy CHMO:0000090 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a solid-state (Ti sapphire) laser spot of specific wavelength over its surface to produce multi-photon fluorescence (i.e. the fluorophore simultaneously absorbs multiple photons of typically one half to one third of the energy required for single-photon excitation). https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelengths and the spatial distribution of mean fluorescence lifetimes (usually on the ns scale) is mapped within the microscopic images. FLIM fluorescence-lifetime imaging microscopy CHMO:0000091 fluorescence lifetime imaging microscopy CHMO:0000091 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelengths and the spatial distribution of mean fluorescence lifetimes (usually on the ns scale) is mapped within the microscopic images. https://doi.org/10.1007/b102213 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with radiation in the infra-red region (2.5–16 &#x3bc;m). IR fluorescence microscopy infra-red fluorescence microscopy CHMO:0000092 infrared fluorescence microscopy CHMO:0000092 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with radiation in the infra-red region (2.5–16 &#x3bc;m). https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with radiation in the near infra-red region (0.8–2.5 &#x3bc;m). NIRF microscopy NIRFM near infra-red fluorescence microscopy near-infrared fluorescence microscopy CHMO:0000093 near-infrared fluorescence microscopy CHMO:0000093 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with radiation in the near infra-red region (0.8–2.5 &#x3bc;m). https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen (a fluorophore) can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelength. The light is totally internally reflected to generate an evanescent wave at the glass microscope slide-water interface. The evanescent wave selectively illuminates and excites fluorophores in a restricted region of the specimen allowing fluorophores on the surface to be imaged (normally the fluorescence of surface fluorophores is overwhelmed by background fluorescence). TIRF microscopy TIRFM CHMO:0000094 total internal reflection fluorescence microscopy CHMO:0000094 Microscopy where the specimen (a fluorophore) can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelength. The light is totally internally reflected to generate an evanescent wave at the glass microscope slide-water interface. The evanescent wave selectively illuminates and excites fluorophores in a restricted region of the specimen allowing fluorophores on the surface to be imaged (normally the fluorescence of surface fluorophores is overwhelmed by background fluorescence). https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with radiation in the ultra-violet region (4–380 nm). UV fluorescence microscopy UVF microscopy UVFM ultra-violet fluorescence microscopy ultraviolet fluorescence microscopy CHMO:0000095 ultraviolet fluorescence microscopy CHMO:0000095 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with radiation in the ultra-violet region (4–380 nm). ISBN:0632034335 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with radiation in the visible region (380–750 nm). CHMO:0000096 visible fluorescence microscopy CHMO:0000096 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with radiation in the visible region (380–750 nm). https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen is illuminated with visible light and a system of lenses is used to produce an image. FIX:0000113 OM light microscopy CHMO:0000102 optical microscopy CHMO:0000102 Microscopy where the specimen is illuminated with visible light and a system of lenses is used to produce an image. https://orcid.org/0000-0002-0640-0422 Microscopy where visible light coming from the specimen is collected and guided through a pinhole before it is detected. The pinhole allows only light from the focal point to pass to the detector, reducing background interference. CHMO:0000103 confocal microscopy CHMO:0000103 Microscopy where visible light coming from the specimen is collected and guided through a pinhole before it is detected. The pinhole allows only light from the focal point to pass to the detector, reducing background interference. ISBN:978-3-540-74597-6 Microscopy where the specimen is illuminated with light transmitted from a source on the opposite side of the specimen from the objective. bright field microscopy bright-field optical microscopy transmitted light microscopy transmitted-light microscopy CHMO:0000104 bright-field microscopy CHMO:0000104 Microscopy where the specimen is illuminated with light transmitted from a source on the opposite side of the specimen from the objective. https://orcid.org/0000-0002-0640-0422 Microscopy where two specimens can be compared by illuminating them with visible light using two identical sets of microscope lenses which are linked by an optical bridge. CHMO:0000105 comparison light microscopy CHMO:0000105 Microscopy where two specimens can be compared by illuminating them with visible light using two identical sets of microscope lenses which are linked by an optical bridge. ISBN:0-85404-539-2 Microscopy where the specimen is illuminated with visible light split into two beams, which then interfere to produce fringes whose spacing is proportional to the height of the specimen. IOM OIM interference optical microscopy CHMO:0000106 optical interference microscopy CHMO:0000106 Microscopy where the specimen is illuminated with visible light split into two beams, which then interfere to produce fringes whose spacing is proportional to the height of the specimen. https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen is illuminated with polarised visible light split into two beams, which then interfere to produce fringes whose spacing is proportional to the height of the specimen. DIC DIC microscopy NIC NIC microscopy Nomarski interference contrast microscopy Nomarski microscopy CHMO:0000107 differential interference contrast microscopy CHMO:0000107 Microscopy where the specimen is illuminated with polarised visible light split into two beams, which then interfere to produce fringes whose spacing is proportional to the height of the specimen. https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen is illuminated with short-coherence length visible light split into two beams, which then interfere to produce fringes whose spacing is proportional to the height of the specimen. CHMO:0000108 low coherence interference microscopy CHMO:0000108 Microscopy where the specimen is illuminated with short-coherence length visible light split into two beams, which then interfere to produce fringes whose spacing is proportional to the height of the specimen. ISBN:0824742524 Microscopy where the surface of the specimen is illuminated with short-coherence length visible light split into two beams, which then interfere to produce fringes whose spacing is proportional to the profile of the specimen. CPM coherence-probe microscopy phase correlation microscopy CHMO:0000109 coherence probe microscopy CHMO:0000109 Microscopy where the surface of the specimen is illuminated with short-coherence length visible light split into two beams, which then interfere to produce fringes whose spacing is proportional to the profile of the specimen. ISBN:0824742524 Microscopy where a transparent specimen is illuminated with visible light and small phase shifts in the light passing through the specimen are used to produce an image. PCM phase-contrast microscopy CHMO:0000110 phase contrast microscopy CHMO:0000110 Microscopy where a transparent specimen is illuminated with visible light and small phase shifts in the light passing through the specimen are used to produce an image. https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen placed between two orthogonal polarising filters and illuminated with visible light. PLM POM optical polarisation microscopy optical polarising microscopy optical polarization microscopy polarised light microscopy polarised optical microscopy polarized light microscopy polarized light optical microscopy polarized optical microscopy polarizing light microscopy polarizing optical microscopy CHMO:0000111 polarising light microscopy CHMO:0000111 Microscopy where the specimen placed between two orthogonal polarising filters and illuminated with visible light. https://orcid.org/0000-0002-0640-0422 Microscopy which uses a probe to scan the surface of the specimen and measure some form of interaction between surface and probe. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the probe-surface interaction as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. SPM scanning-probe microscopy CHMO:0000112 scanning probe microscopy CHMO:0000112 Microscopy which uses a probe to scan the surface of the specimen and measure some form of interaction between surface and probe. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the probe-surface interaction as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. FIX:0000121 ISBN:1-86094-199-0 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. AFM SFM atomic force imaging atomic-force microscopy scanning force microscopy CHMO:0000113 atomic force microscopy CHMO:0000113 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. FIX:0000114 https://orcid.org/0000-0002-0640-0422 Microscopy where an electric field is applied to a sharp spike (known as a 'tip') which is mounted on the end of a cantilever. The tip scans the surface of a piezoelectric specimen and the distortion of the electric field by the specimen is measured as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. piezo-force microscopy PFM CHMO:0000114 piezoresponse force microscopy CHMO:0000114 Microscopy where an electric field is applied to a sharp spike (known as a 'tip') which is mounted on the end of a cantilever. The tip scans the surface of a piezoelectric specimen and the distortion of the electric field by the specimen is measured as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://doi.org/10.1007/s10853-005-7244-2 PFM Microscopy which uses a sharp magnetic spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of a magnetic specimen. An image of the surface is obtained by mechanically moving the tip in a raster scan of the specimen, line by line, and recording the magnetic force experienced by it as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. MFM magnetic-force microscopy CHMO:0000115 magnetic force microscopy CHMO:0000115 Microscopy which uses a sharp magnetic spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of a magnetic specimen. An image of the surface is obtained by mechanically moving the tip in a raster scan of the specimen, line by line, and recording the magnetic force experienced by it as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. FIX:0000118 ISBN:1-86094-199-0 Microscopy where optical tweezers are used to trap a small fluorescent latex bead which is then scanned across biological specimens in aqueous solution. An image of the surface is obtained by mechanically moving the bead in a raster scan of the specimen, line by line, and recording the fluorescence intensity as a function of position. A feedback loop is used to maintain a fixed relationship between the bead and surface during scanning. PFM photonic-force microscopy CHMO:0000116 photonic force microscopy CHMO:0000116 Microscopy where optical tweezers are used to trap a small fluorescent latex bead which is then scanned across biological specimens in aqueous solution. An image of the surface is obtained by mechanically moving the bead in a raster scan of the specimen, line by line, and recording the fluorescence intensity as a function of position. A feedback loop is used to maintain a fixed relationship between the bead and surface during scanning. https://doi.org/10.1006/jsbi.1997.3881 Microscopy which uses a small electrode to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the electrostatic capacitance of the surface as a function of position. A feedback loop is used to maintain a fixed relationship between the electrode and surface during scanning. SCAM scanning-capacitance microscopy CHMO:0000117 scanning capacitance microscopy CHMO:0000117 Microscopy which uses a small electrode to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the electrostatic capacitance of the surface as a function of position. A feedback loop is used to maintain a fixed relationship between the electrode and surface during scanning. https://orcid.org/0000-0002-0640-0422 Any type of microscopy where a probe is positioned very close to the surface of the specimen (in the near-field). An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the probe-surface interaction as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. near-field scanning microscopy CHMO:0000118 scanning near-field microscopy CHMO:0000118 Any type of microscopy where a probe is positioned very close to the surface of the specimen (in the near-field). An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the probe-surface interaction as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen is illuminated with a near-field of photons. An image of the surface is obtained by mechanically moving an optical fibre probe in a raster scan over the specimen, line by line, and detecting any photons which tunnel from the specimen to the probe as a function of position. A feedback loop is used to maintain a fixed relationship between the optical fibre probe and surface during scanning. PSTM photon scanning tunneling microscopy photon-scanning tunneling microscopy photon-scanning tunnelling microscopy CHMO:0000119 photon scanning tunnelling microscopy CHMO:0000119 Microscopy where the specimen is illuminated with a near-field of photons. An image of the surface is obtained by mechanically moving an optical fibre probe in a raster scan over the specimen, line by line, and detecting any photons which tunnel from the specimen to the probe as a function of position. A feedback loop is used to maintain a fixed relationship between the optical fibre probe and surface during scanning. USPatent:5018865 Microscopy where a probe consisting of a laser transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen. The tip is coated with metal (to prevent light from escaping from the sides) and near-field (or evanescent field) light is emitted through a small opening or 'aperture' (50–100 nm in diameter) at the apex of the probe. An image is produced by scanning the probe over the specimen and detecting the disturbance of the near-field as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. NSOM SNOM aperture NSOM aperture SNOM aperture scanning near-field optical microscopy aperture-NSOM aperture-SNOM near-field scanning optical microscopy CHMO:0000120 scanning near-field optical microscopy CHMO:0000120 Microscopy where a probe consisting of a laser transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen. The tip is coated with metal (to prevent light from escaping from the sides) and near-field (or evanescent field) light is emitted through a small opening or 'aperture' (50–100 nm in diameter) at the apex of the probe. An image is produced by scanning the probe over the specimen and detecting the disturbance of the near-field as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. FIX:0000385 ISBN:1-86094-199-0 Microscopy where a probe consisting of a laser of a specific wavelength transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen. The tip is coated with metal (to prevent light from escaping from the sides) and near-field (or evanescent field) light is emitted through a small opening or 'aperture' (50–100 nm in diameter) at the apex of the probe. An image is produced by scanning the probe over the specimen and detecting the fluorescence intensity from fluorophores on the surface of the specimen as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. CHMO:0000121 fluorescence scanning near-field optical microscopy CHMO:0000121 Microscopy where a probe consisting of a laser of a specific wavelength transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen. The tip is coated with metal (to prevent light from escaping from the sides) and near-field (or evanescent field) light is emitted through a small opening or 'aperture' (50–100 nm in diameter) at the apex of the probe. An image is produced by scanning the probe over the specimen and detecting the fluorescence intensity from fluorophores on the surface of the specimen as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://orcid.org/0000-0002-0640-0422 Microscopy where a probe consisting of an infrared laser transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen. The tip is coated with metal (to prevent light from escaping from the sides) and near-field (or evanescent field) infrared radiation is emitted through a small opening or 'aperture' (50–100 nm in diameter) at the apex of the probe. An image is produced by scanning the probe over the specimen and detecting the disturbance of the infrared near-field as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. IR-NSOM IR-SNOM SNFIM SNIM SNIM imaging infra-red near-field scanning optical microscopy infra-red scanning near-field optical microscopy infrared near-field scanning optical microscopy CHMO:0000122 infrared scanning near-field optical microscopy CHMO:0000122 Microscopy where a probe consisting of an infrared laser transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen. The tip is coated with metal (to prevent light from escaping from the sides) and near-field (or evanescent field) infrared radiation is emitted through a small opening or 'aperture' (50–100 nm in diameter) at the apex of the probe. An image is produced by scanning the probe over the specimen and detecting the disturbance of the infrared near-field as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://doi.org/10.1016/j.jallcom.2005.02.057 Microscopy where a probe consisting of a microwave radiation source transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen. The tip is coated with metal (to prevent light from escaping from the sides) and near-field (or evanescent field) microwave radiation is emitted through a small opening or 'aperture' (50-100 nm in diameter) at the apex of the probe. An image is produced by scanning the probe over the specimen and detecting the disturbance of the microwave near-field as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. NSMM SNMM microwave near-field scanning microscopy near-field scanning microwave microscopy CHMO:0000123 microwave scanning near-field microscopy CHMO:0000123 Microscopy where a probe consisting of a microwave radiation source transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen. The tip is coated with metal (to prevent light from escaping from the sides) and near-field (or evanescent field) microwave radiation is emitted through a small opening or 'aperture' (50-100 nm in diameter) at the apex of the probe. An image is produced by scanning the probe over the specimen and detecting the disturbance of the microwave near-field as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://orcid.org/0000-0002-0640-0422 Microscopy where a laser spot is focused on a solid sharp metallic probe producing a confined light field very close to (<10 nm from) the surface of the specimen. An image is produced by scanning the probe over the specimen and detecting the scattering of the incident light by the probe as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. aNSOM aSNOM apertureless scanning near-field optical microscopy scattering type apertureless near-field scanning optical microscopy scattering type apertureless scanning near-field optical microscopy scattering type near-field scanning optical microscopy scattering type scanning near-field optical microscopy CHMO:0000124 apertureless near-field scanning optical microscopy CHMO:0000124 Microscopy where a laser spot is focused on a solid sharp metallic probe producing a confined light field very close to (<10 nm from) the surface of the specimen. An image is produced by scanning the probe over the specimen and detecting the scattering of the incident light by the probe as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://doi.org/10.1039/b815925d Microscopy where a thermocouple probe is positioned very close to the surface of the specimen (in the near-field). An image of the surface is obtained by mechanically moving the thermocouple probe in a raster scan of the specimen, line by line, and recording the surface–probe heat transfer as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. NSThM SNThM near-field scanning thermal microscopy CHMO:0000126 scanning near-field thermal microscopy CHMO:0000126 Microscopy where a thermocouple probe is positioned very close to the surface of the specimen (in the near-field). An image of the surface is obtained by mechanically moving the thermocouple probe in a raster scan of the specimen, line by line, and recording the surface–probe heat transfer as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://orcid.org/0000-0002-0640-0422 Microscopy where an electrode probe is positioned very close to the surface of the specimen (in the near-field). The surface is mechanically scanned by the electrode in a raster scan and the height required by a feedback loop in order to maintain a constant electrical conductance between the electrode and the specimen is recorded as a function of position. SECM scanning-electrochemical microscopy CHMO:0000127 scanning electrochemical microscopy CHMO:0000127 Microscopy where an electrode probe is positioned very close to the surface of the specimen (in the near-field). The surface is mechanically scanned by the electrode in a raster scan and the height required by a feedback loop in order to maintain a constant electrical conductance between the electrode and the specimen is recorded as a function of position. ISBN:1-86094-199-0 Microscopy where a probe consisting of a glass nano- or micro- pipette filled with electrolyte is positioned very close to (in the near-field of) a specimen which is held in an oppositely charge electrolyte. An image of the surface is obtained by mechanically moving the pipette in a raster scan of the specimen, line by line, and recording the ion conductance as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. SICM scanning-ion conductance microscopy CHMO:0000128 scanning ion conductance microscopy CHMO:0000128 Microscopy where a probe consisting of a glass nano- or micro- pipette filled with electrolyte is positioned very close to (in the near-field of) a specimen which is held in an oppositely charge electrolyte. An image of the surface is obtained by mechanically moving the pipette in a raster scan of the specimen, line by line, and recording the ion conductance as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. ISBN:1-86094-199-0 Microscopy where a probe vibrating at its resonant frequency is scanned over the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the resonant frequency (or the amplitude of vibration) of the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. SPAM scanning acoustic microscopy SAM CHMO:0000129 scanning probe acoustic microscopy CHMO:0000129 Microscopy where a probe vibrating at its resonant frequency is scanned over the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the resonant frequency (or the amplitude of vibration) of the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://doi.org/10.1007/s10853-005-7244-2 SAM Microscopy where a probe vibrating at its resonant frequency is positioned very close to the surface of the specimen (in the near-field). An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the resonant frequency (or amplitude of vibration) of the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. NSAM SNAM near-field scanning acoustic microscopy CHMO:0000130 scanning near-field acoustic microscopy CHMO:0000130 Microscopy where a probe vibrating at its resonant frequency is positioned very close to the surface of the specimen (in the near-field). An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the resonant frequency (or amplitude of vibration) of the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://doi.org/10.1007/BF00694423 Microscopy where an Wollaston wire probe is scanned over the surface of the specimen and the height required by a feedback loop in order to maintain a constant temperature between the probe and the specimen is recorded as a function of position. SThM scanning-thermal microscopy CHMO:0000131 scanning thermal microscopy CHMO:0000131 Microscopy where an Wollaston wire probe is scanned over the surface of the specimen and the height required by a feedback loop in order to maintain a constant temperature between the probe and the specimen is recorded as a function of position. ISBN:1-86094-199-0 Microscopy which uses a sharp conducting probe (or 'tip') held very close (1 nm) to the surface of the specimen. A bias voltage is applied between the tip and specimen which causes a tunnelling current to flow. An image is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the tunnelling current as a function of position. FIX:0000112 STM scanning tunneling electron microscopy scanning tunnelling electron microscopy scanning-tunneling electron microscopy scanning-tunnelling microscopy CHMO:0000132 scanning tunnelling microscopy CHMO:0000132 Microscopy which uses a sharp conducting probe (or 'tip') held very close (1 nm) to the surface of the specimen. A bias voltage is applied between the tip and specimen which causes a tunnelling current to flow. An image is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the tunnelling current as a function of position. ISBN:1-86094-199-0 Microscopy where an excitation laser and a probe laser are focused onto a specimen forming a refractive index distribution which results in a concave excitation beam. The strength of this lens is proportional to the sample concentration and is detected by a change in transmittance in the probe beam. TLM thermal-lens microscopy CHMO:0000133 thermal lens microscopy CHMO:0000133 Microscopy where an excitation laser and a probe laser are focused onto a specimen forming a refractive index distribution which results in a concave excitation beam. The strength of this lens is proportional to the sample concentration and is detected by a change in transmittance in the probe beam. https://doi.org/10.1021/ac05196u Thermal lens microscopy where the excitation laser is an ultraviolet laser. UV-TLM ultra-violet thermal-lens microscopy ultraviolet thermal lens microscopy ultraviolet thermal-lens microscopy CHMO:0000134 ultra-violet thermal lens microscopy CHMO:0000134 Thermal lens microscopy where the excitation laser is an ultraviolet laser. https://doi.org/10.1021/ac05196u Microscopy which uses a microparticle (usually made of silica) mounted on the end of a cantilever to scan the surface of a colloidal specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force between the two colloidal surfaces as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. colloid force microscopy colloidal probe AFM CHMO:0000764 colloidal probe atomic force microscopy CHMO:0000764 Microscopy which uses a microparticle (usually made of silica) mounted on the end of a cantilever to scan the surface of a colloidal specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force between the two colloidal surfaces as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://doi.org/10.1006/jcis.2001.8075 Microscopy where fluorophores in the specimen can be made to fluoresce (emit energy as visible light) by absorption of two or more photons. multi-photon excitation microscopy multi-photon fluorescence imaging multi-photon fluorescence microscopy multiphoton excitation microscopy multiphoton fluorescence imaging multiphoton fluorescence microscopy CHMO:0000771 multiphoton fluorescence microscopy CHMO:0000771 Microscopy where fluorophores in the specimen can be made to fluoresce (emit energy as visible light) by absorption of two or more photons. https://orcid.org/0000-0002-0640-0422 Microscopy where fluorophores in the specimen can be made to fluoresce (emit energy as visible light) by the near-simultaneous absorption of two photons. two photon excitation microscopy two photon fluorescence imaging two-photon excitation imaging two-photon fluorescence imaging two-photon fluorescence microscopy CHMO:0000772 two photon fluorescence microscopy CHMO:0000772 Microscopy where fluorophores in the specimen can be made to fluoresce (emit energy as visible light) by the near-simultaneous absorption of two photons. https://orcid.org/0000-0002-0640-0422 Conductive AFM is used for collecting simultaneous topography imaging and current imaging. Specifically, standard conductive AFM operates in contact AFM mode. Variations in surface conductivity can be distinguished using this mode. Conductive AFM operates in contact AFM mode by using a conductive AFM tip. The contact tip is scanned in contact with the sample surface. Just like contact AFM, the feedback loop uses the DC cantilever deflection signal to maintain a constant force between the tip and the sample to generate the topography image. At the same time, a DC bias is applied to the tip. The sample is held at ground potential. C-AFM CAFM conductive AFM CHMO:0000874 conductive atomic force microscopy CHMO:0000874 Conductive AFM is used for collecting simultaneous topography imaging and current imaging. Specifically, standard conductive AFM operates in contact AFM mode. Variations in surface conductivity can be distinguished using this mode. Conductive AFM operates in contact AFM mode by using a conductive AFM tip. The contact tip is scanned in contact with the sample surface. Just like contact AFM, the feedback loop uses the DC cantilever deflection signal to maintain a constant force between the tip and the sample to generate the topography image. At the same time, a DC bias is applied to the tip. The sample is held at ground potential. http://www.mcc.uiuc.edu/summerschool/2002/Chang%20Liu/Liu_files/ChangLiu5.pdf Microscopy where an electric field is applied to a sharp spike (known as a 'tip') which is mounted on the end of a cantilever. The tip scans the surface of a piezoelectric specimen and the distortion of the electric field by the specimen is measured as components from three directions (one vertical and two lateral). A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. VPFM vector PFM CHMO:0000940 vector piezoresponse force microscopy CHMO:0000940 Microscopy where an electric field is applied to a sharp spike (known as a 'tip') which is mounted on the end of a cantilever. The tip scans the surface of a piezoelectric specimen and the distortion of the electric field by the specimen is measured as components from three directions (one vertical and two lateral). A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0002-0640-0422 A piece of apparatus which is used to produce an enlarged image of a specimen by scanning a finely focused (<10 nm diameter) electron beam with an acceleration voltage of 50–150 kV across the specimen under vacuum and measuring the interaction of the electrons with the specimen. SEM CHMO:0000941 scanning electron microscope CHMO:0000941 A piece of apparatus which is used to produce an enlarged image of a specimen by scanning a finely focused (<10 nm diameter) electron beam with an acceleration voltage of 50–150 kV across the specimen under vacuum and measuring the interaction of the electrons with the specimen. https://doi.org/10.1351/goldbook.S05484 A piece of apparatus which is used to produce an enlarged image of a specimen by scanning a finely focused (<10 nm diameter) electron beam produced by thermionic emission heating (field emission) with an acceleration voltage of 50–150 kV across the specimen under vacuum and measuring interaction of the electrons with the specimen. field emission scanning electron microscope FE-SEM FEG-SEM field emission SEM field-emission SEM CHMO:0000942 field-emission scanning electron microscope CHMO:0000942 A piece of apparatus which is used to produce an enlarged image of a specimen by scanning a finely focused (<10 nm diameter) electron beam produced by thermionic emission heating (field emission) with an acceleration voltage of 50–150 kV across the specimen under vacuum and measuring interaction of the electrons with the specimen. https://orcid.org/0000-0002-0640-0422 A microscope which uses a probe to scan the surface of the specimen, mechanically moving the probe in a raster scan of the specimen, line by line, and recording the probe-surface interaction as a function of position, producing an image of the surface. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. SPM CHMO:0000943 scanning probe microscope CHMO:0000943 A microscope which uses a probe to scan the surface of the specimen, mechanically moving the probe in a raster scan of the specimen, line by line, and recording the probe-surface interaction as a function of position, producing an image of the surface. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. CHMO:0000112 CHMO:0000951 CHMO:0000952 A microscope which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. AFM CHMO:0000954 atomic force microscope CHMO:0000954 A microscope which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. CHMO:0000113 Microscopy in which the same object (e.g., a cell) is imaged at regular time intervals over several hours. CHMO:0001074 time-lapse microscopy CHMO:0001074 Microscopy in which the same object (e.g., a cell) is imaged at regular time intervals over several hours. https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) and the specimen is imaged at regular time intervals over several hours. time-lapse fluorescence imaging CHMO:0001084 time-lapse fluorescence microscopy CHMO:0001084 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) and the specimen is imaged at regular time intervals over several hours. https://orcid.org/0000-0002-0640-0422 A microscope that uses an excitation source to produce light which is passed through an excitation filter, reflects off the surface of a dichroic mirror onto the specimen which fluoresces, producing light that passes through an emission filter to select only the required wavelengths onto the collector lens. CHMO:0001095 fluorescence microscope CHMO:0001095 A microscope that uses an excitation source to produce light which is passed through an excitation filter, reflects off the surface of a dichroic mirror onto the specimen which fluoresces, producing light that passes through an emission filter to select only the required wavelengths onto the collector lens. http://www.microscopyu.com/articles/fluorescence/fluorescenceintro.html A fluorescence microscope where the light source is mounted above (epi) the specimen and the excitation light passes through the microscope objective lens on its way toward the specimen. epifluorescent microscope CHMO:0001096 epifluorescence microscope CHMO:0001096 A fluorescence microscope where the light source is mounted above (epi) the specimen and the excitation light passes through the microscope objective lens on its way toward the specimen. http://www.microscopyu.com/articles/fluorescence/fluorescenceintro.html https://orcid.org/0000-0001-5985-7429 CHMO:0001098 A piece of apparatus which is used to produce an enlarged image of an electron transparent specimen using a finely focused (<10 nm diameter) electron beam with an acceleration voltage of 50–150 kV under vacuum. The energies and intensities of the transmitted electrons are measured. TEM transmission EM CHMO:0001099 transmission electron microscope CHMO:0001099 A piece of apparatus which is used to produce an enlarged image of an electron transparent specimen using a finely focused (<10 nm diameter) electron beam with an acceleration voltage of 50–150 kV under vacuum. The energies and intensities of the transmitted electrons are measured. https://orcid.org/0000-0002-0640-0422 A piece of apparatus which is used to produce an enlarged image of an electron transparent specimen using a finely focused (<10 nm diameter) electron beam (produced by thermionic emission heating) with an acceleration voltage of 50–150 kV under vacuum. The energies and intensities of the transmitted electrons are measured. TEM-FEG field emission transmission electron microscope field-emission-gun transmission electron microscope FEG-TEM FEGTEM field-emission TEM CHMO:0001100 field-emission transmission electron microscope CHMO:0001100 A piece of apparatus which is used to produce an enlarged image of an electron transparent specimen using a finely focused (<10 nm diameter) electron beam (produced by thermionic emission heating) with an acceleration voltage of 50–150 kV under vacuum. The energies and intensities of the transmitted electrons are measured. https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen is illuminated with light transmitted from a source on the opposite side of the specimen from the objective, and image resolution (which is normally limited by diffraction) is enhanced by processing the images with image restoration algorithms. super resolution bright field microscopy super resolution bright field optical microscopy super-resolution bright-field optical microscopy CHMO:0001112 super-resolution bright-field microscopy CHMO:0001112 Microscopy where the specimen is illuminated with light transmitted from a source on the opposite side of the specimen from the objective, and image resolution (which is normally limited by diffraction) is enhanced by processing the images with image restoration algorithms. https://orcid.org/0000-0002-0640-0422 A piece of apparatus, consisting of an optical microscope coupled to a reflecting magnifying mirror system, which is used to collect spatially resolved infrared spectra of the surface of a specimen. https://orcid.org/0000-0001-5985-7429 2009-05-26T12:36:47Z IR microscope CHMO:0001813 infrared microscope CHMO:0001813 A piece of apparatus, consisting of an optical microscope coupled to a reflecting magnifying mirror system, which is used to collect spatially resolved infrared spectra of the surface of a specimen. ISBN:2884490736 A piece of apparatus, consisting of a laser beam (<10 μm diameter), a monochromator and a detector coupled to an optical microscope, which is used to measure Raman spectra. https://orcid.org/0000-0001-5985-7429 2009-05-26T01:03:35Z CHMO:0001236 Raman microspectrometer CHMO:0001814 Raman microscope CHMO:0001814 A piece of apparatus, consisting of a laser beam (<10 μm diameter), a monochromator and a detector coupled to an optical microscope, which is used to measure Raman spectra. https://orcid.org/0000-0002-0640-0422 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates, intermittently touching or tapping the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2009-06-02T10:51:10Z AC-mode AFM AFM tapping-mode DFM DSFM dynamic force AFM dynamic scanning force microscopy intermittant contact AFM intermittant contact atomic force microscopy intermittant-contact AFM intermittant-contact atomic force microscopy tapping mode AFM tapping mode atomic force microscopy tapping-mode AFM CHMO:0001896 dynamic force microscopy CHMO:0001896 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates, intermittently touching or tapping the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. ISBN:1-86094-199-0 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the frictional force experienced by the tip as a function of position (the 'twist' of the tip). A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2009-06-02T10:58:31Z LFM lateral force AFM lateral-force AFM lateral-force microscopy CHMO:0001897 lateral force microscopy CHMO:0001897 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the frictional force experienced by the tip as a function of position (the 'twist' of the tip). A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. FIX:0000115 ISBN:1-86094-199-0 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates in the 'attractive' force region, i.e. avoiding sample contact. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2009-06-02T11:02:43Z DFM-AR DFMAR DSFM-AR DSFMA DSFMAR NC-AFM NC-SFM attractive dynamic scanning force microscopy dynamic AFM dynamic force microscopy in attractive regime dynamic mode AFM dynamic scanning force microscopy in attractive regime dynamic-mode AFM non-contact mode AFM noncontact atomic force microscopy noncontact mode AFM noncontact mode scanning force microscopy noncontact scanning force microscopy CHMO:0001898 non-contact mode atomic force microscopy CHMO:0001898 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates in the 'attractive' force region, i.e. avoiding sample contact. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. FIX:0000117 https://doi.org/10.1016/j.eurpolymj.2008.05.019 https://doi.org/10.1039/b817510a Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates parallel to the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2009-06-04T04:31:08Z SMFM ShFM dynamic shear force microscopy shear force AFM shear force atomic force microscopy shear force modulation microscopy shear force modulation mode AFM shear force modulation mode atomic force microscopy shear-force AFM shear-force atomic force microscopy shear-force controlled AFM shear-force microscopy CHMO:0001923 shear force microscopy CHMO:0001923 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates parallel to the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://doi.org/10.1063/1.106940 A type of optical microscopy which is used to monitor Brownian fluctuations in the separation between a single microscopic sphere and a flat plate in aqueous media. The sphere is levitated above the plate by colloidal forces such as double-layer or steric repulsion. Changes in elevation as small as 1 nm can be detected by measuring the light scattered by a single sphere when illuminated by an evanescent wave. https://orcid.org/0000-0001-5985-7429 2009-06-04T04:46:13Z TIRM CHMO:0001925 total internal reflection microscopy CHMO:0001925 A type of optical microscopy which is used to monitor Brownian fluctuations in the separation between a single microscopic sphere and a flat plate in aqueous media. The sphere is levitated above the plate by colloidal forces such as double-layer or steric repulsion. Changes in elevation as small as 1 nm can be detected by measuring the light scattered by a single sphere when illuminated by an evanescent wave. https://doi.org/10.1021/ie010377t A piece of apparatus, consisting of a flow cell, a laser and a detector, which detects the fluorescence and light scattering of individual particles (e.g. cells). https://orcid.org/0000-0001-5985-7429 2009-06-11T02:20:37Z CHMO:0001957 flow cytometer CHMO:0001957 A piece of apparatus, consisting of a flow cell, a laser and a detector, which detects the fluorescence and light scattering of individual particles (e.g. cells). https://orcid.org/0000-0002-0640-0422 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates, intermittently touching or tapping the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the resonant frequency of the tip and the surface during scanning, which is performed under ultra-high vacuum conditions. https://orcid.org/0000-0001-5985-7429 2009-07-06T02:26:05Z FM-AFM frequency modulation AFM frequency modulation atomic force microscopy frequency-modulation AFM CHMO:0002116 frequency-modulation atomic force microscopy CHMO:0002116 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates, intermittently touching or tapping the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the resonant frequency of the tip and the surface during scanning, which is performed under ultra-high vacuum conditions. https://orcid.org/0000-0002-0640-0422 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen that is immersed in a liquid cell. The tip oscillates, intermittently touching or tapping the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2009-07-06T02:30:09Z liquid AFM solution atomic force microscopy solution-state AFM solution-state atomic force microscopy CHMO:0002117 liquid atomic force microscopy CHMO:0002117 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen that is immersed in a liquid cell. The tip oscillates, intermittently touching or tapping the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0002-0640-0422 Microscopy where the sample is illuminated with visible light that is not collected by the objective lens. Only the light scattered by the specimen is collected by the lens, producing an image of a light specimen on a black background. https://orcid.org/0000-0001-5985-7429 2009-07-16T02:28:55Z dark-field optical microscopy darkfield microscopy darkfield optical microscopy CHMO:0002177 dark-field microscopy CHMO:0002177 Microscopy where the sample is illuminated with visible light that is not collected by the objective lens. Only the light scattered by the specimen is collected by the lens, producing an image of a light specimen on a black background. https://orcid.org/0000-0002-0640-0422 A piece of apparatus, consisting of an eyepiece, an objective lens, object turret, stage, condenser and light source, which collects electromagnetic radiation in the visible range. In an inverted microscope the light source and condenser are mounted above the stage, while the objective lens and turret are mounted below the stage. https://orcid.org/0000-0001-5985-7429 2009-07-17T04:06:13Z inverted optical microscope CHMO:0002180 inverted microscope CHMO:0002180 A piece of apparatus, consisting of an eyepiece, an objective lens, object turret, stage, condenser and light source, which collects electromagnetic radiation in the visible range. In an inverted microscope the light source and condenser are mounted above the stage, while the objective lens and turret are mounted below the stage. https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelengths. In epifluorescence microscopy light is transmitted through the objective lens onto the specimen, eliminating the need to filter out unwanted light directly from the source. https://orcid.org/0000-0001-5985-7429 2009-07-21T10:34:34Z CHMO:0002194 epifluorescence microscopy CHMO:0002194 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by illuminating it with light of specific wavelengths. In epifluorescence microscopy light is transmitted through the objective lens onto the specimen, eliminating the need to filter out unwanted light directly from the source. https://orcid.org/0000-0002-0640-0422 A piece of apparatus, consisting of an eyepiece, an objective lens, a condenser lens, stage, and light source, which collects electromagnetic radiation in the visible range. An opaque disc is placed underneath the condenser lens, so that only light that is scattered by objects on the slide can reach the eye. https://orcid.org/0000-0001-5985-7429 2009-07-31T01:56:03Z dark field microscope dark field optical microscope dark-field optical microscope CHMO:0002236 dark-field microscope CHMO:0002236 A piece of apparatus, consisting of an eyepiece, an objective lens, a condenser lens, stage, and light source, which collects electromagnetic radiation in the visible range. An opaque disc is placed underneath the condenser lens, so that only light that is scattered by objects on the slide can reach the eye. https://orcid.org/0000-0002-0640-0422 A piece of apparatus which is used to produce an enlarged image of an electron- transparent specimen using a finely focused (<10 nm diameter) electron beam with an acceleration voltage of 50-150 kV under vacuum. X-rays emerging from the sample (as a result of electron bombardment) pass through a slit, then a grating disperses them by diffraction according to their wavelength. Finally, X-ray energy (which is characteristic of atomic number) is converted to voltage pulses or 'counts' by a detector. https://orcid.org/0000-0001-5985-7429 2009-07-31T04:13:12Z TEM/EDX transmission electron microscope equipped with an energy dispersive X-ray analyzer transmission electron microscope with an energy dispersive X-ray analyzer CHMO:0002237 transmission electron microscope with an energy dispersive X-ray analyser CHMO:0002237 A piece of apparatus which is used to produce an enlarged image of an electron- transparent specimen using a finely focused (<10 nm diameter) electron beam with an acceleration voltage of 50-150 kV under vacuum. X-rays emerging from the sample (as a result of electron bombardment) pass through a slit, then a grating disperses them by diffraction according to their wavelength. Finally, X-ray energy (which is characteristic of atomic number) is converted to voltage pulses or 'counts' by a detector. https://orcid.org/0000-0002-0640-0422 Microscopy where a metal-coated AFM tip is positioned very close to the surface of the specimen (in the near-field) and an image of the surface is obtained by mechanically moving the tip in a raster scan of the specimen, line by line, and recording the change in the polarisation of incident light when it is reflected from a surface as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://orcid.org/0000-0001-5985-7429 2009-08-21T01:12:23Z SNEM CHMO:0002285 scanning near-field ellipsometric microscopy CHMO:0002285 Microscopy where a metal-coated AFM tip is positioned very close to the surface of the specimen (in the near-field) and an image of the surface is obtained by mechanically moving the tip in a raster scan of the specimen, line by line, and recording the change in the polarisation of incident light when it is reflected from a surface as a function of position. A feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://doi.org/10.1039/b9nr00156e A piece of apparatus which is used to produce an enlarged image of an electron transparent specimen using several finely focused (<10 nm diameter) electron beams with an acceleration voltage of 50–150 kV under vacuum. The amplitude of the interference of the transmitted electron waves is then measured and the phase contrast is used to produce an image. https://orcid.org/0000-0001-5985-7429 2009-09-01T01:32:33Z high resolution transmission electron microscope HRTEM high-resolution (HR) TEM CHMO:0002323 high-resolution transmission electron microscope CHMO:0002323 A piece of apparatus which is used to produce an enlarged image of an electron transparent specimen using several finely focused (<10 nm diameter) electron beams with an acceleration voltage of 50–150 kV under vacuum. The amplitude of the interference of the transmitted electron waves is then measured and the phase contrast is used to produce an image. https://orcid.org/0000-0002-0640-0422 Microscopy that determines the specimen's shape and distance away from a nearby, usually flat, reflective surface from the interference pattern produced by light reflecting from both the object and the surface. A microscope objective focusses a laser on the fluorescent specimen, and the same objective collects fluorescence. The interference between the fluorescence directly emitted by the specimen and the fluorescence reflected by the surface is observed by measuring the intensity of fluorescence passing through a confocal pinhole. https://orcid.org/0000-0001-5985-7429 2009-09-22T05:31:44Z RIC microscopy RICM reflection interference contrast (RIC) microscopy reflection interference contrast (RIC-) microscopy CHMO:0002437 reflection interference contrast microscopy CHMO:0002437 Microscopy that determines the specimen's shape and distance away from a nearby, usually flat, reflective surface from the interference pattern produced by light reflecting from both the object and the surface. A microscope objective focusses a laser on the fluorescent specimen, and the same objective collects fluorescence. The interference between the fluorescence directly emitted by the specimen and the fluorescence reflected by the surface is observed by measuring the intensity of fluorescence passing through a confocal pinhole. https://doi.org/10.1039/b9nr00156e A piece of apparatus which is used to produce an enlarged image of a specimen by scanning a finely focused (<10 nm diameter) electron beam produced by applying a high voltage to a tungsten crystal (cold-field emission) with an acceleration voltage of 50–150 kV across the specimen under vacuum and measuring interaction of the electrons with the specimen. https://orcid.org/0000-0001-5985-7429 2009-09-23T04:27:09Z cold field emission RELATED cold field emission scanning electron microscope cold-field-emission RELATED cold-field-gun scanning electron microscope CFE-SEM CFG-SEM CHMO:0002454 cold-field-emission scanning electron microscope CHMO:0002454 A piece of apparatus which is used to produce an enlarged image of a specimen by scanning a finely focused (<10 nm diameter) electron beam produced by applying a high voltage to a tungsten crystal (cold-field emission) with an acceleration voltage of 50–150 kV across the specimen under vacuum and measuring interaction of the electrons with the specimen. https://orcid.org/0000-0002-0640-0422 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The conducting tip forms a capacitor with the surface, over which it is scanned laterally at a constant separation, in order to map the change in work function of the surface. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2009-09-23T06:01:55Z KFM KPFM Kelvin force microscopy Kelvin probe microscopy SSPM scanning surface potential microscopy CHMO:0002457 Kelvin probe force microscopy CHMO:0002457 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The conducting tip forms a capacitor with the surface, over which it is scanned laterally at a constant separation, in order to map the change in work function of the surface. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. FIX:0000120 https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a solid-state (Ti sapphire) laser spot of specific wavelength over its surface to produce multi-photon fluorescence (i.e. the fluorophore simultaneously absorbs two photons, each one half of the energy required for single-photon excitation). https://orcid.org/0000-0001-5985-7429 2009-10-09T01:19:49Z two photon LSM two photon laser scanning microscopy two-photon LSM CHMO:0002519 two-photon laser scanning microscopy CHMO:0002519 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a solid-state (Ti sapphire) laser spot of specific wavelength over its surface to produce multi-photon fluorescence (i.e. the fluorophore simultaneously absorbs two photons, each one half of the energy required for single-photon excitation). FIX:0000382 https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a solid-state (Ti sapphire) laser spot of specific wavelength over its surface to produce single-photon fluorescence. https://orcid.org/0000-0001-5985-7429 2009-10-09T01:22:48Z single photon LSM single photon laser scanning microscopy single-photon LSM CHMO:0002520 single-photon laser scanning microscopy CHMO:0002520 Microscopy where the specimen can be made to fluoresce (emit energy as visible light) by scanning a solid-state (Ti sapphire) laser spot of specific wavelength over its surface to produce single-photon fluorescence. FIX:0000381 https://orcid.org/0000-0002-0640-0422 Microscopy where the specimen placed between two orthogonal polarising filters and illuminated with visible light transmitted from a source on the opposite side of the specimen from the objective. https://orcid.org/0000-0001-5985-7429 2009-10-13T11:54:50Z TPLM TPOM transmitted optical polarising microscopy transmitted polarised light microscopy transmitted polarised optical microscopy transmitted polarized light microscopy transmitted polarized light optical microscopy transmitted polarized optical microscopy transmitted polarized-light optical microscopy transmitted polarizing light microscopy transmitted polarizing optical microscopy CHMO:0002526 transmitted polarising light microscopy CHMO:0002526 Microscopy where the specimen placed between two orthogonal polarising filters and illuminated with visible light transmitted from a source on the opposite side of the specimen from the objective. https://orcid.org/0000-0002-0640-0422 A piece of apparatus, consisting of an eyepiece, an objective lens, object turret, stage, orthogonal polarising filters and light source, which collects electromagnetic radiation in the visible range. https://orcid.org/0000-0001-5985-7429 2009-10-13T01:32:14Z polarised light microscope polarised-light microscope polarising light microscope polarized light microscope polarized-light microscope polarizing light microscope polarizing microscope CHMO:0002527 polarising microscope CHMO:0002527 A piece of apparatus, consisting of an eyepiece, an objective lens, object turret, stage, orthogonal polarising filters and light source, which collects electromagnetic radiation in the visible range. https://orcid.org/0000-0002-0640-0422 A piece of apparatus, consisting of an eyepiece, an objective lens, object turret, stage, orthogonal polarising filters and light source, which collects electromagnetic radiation in the visible range. The specimen is illuminated with visible light transmitted from a source on the opposite side of the specimen from the objective. https://orcid.org/0000-0001-5985-7429 2009-10-13T01:35:03Z polarized transmitted light microscope transmitted light polarising microscope transmitting polarizing light microscope transmitting polarizing microscope CHMO:0002528 transmitting polarising microscope CHMO:0002528 A piece of apparatus, consisting of an eyepiece, an objective lens, object turret, stage, orthogonal polarising filters and light source, which collects electromagnetic radiation in the visible range. The specimen is illuminated with visible light transmitted from a source on the opposite side of the specimen from the objective. https://orcid.org/0000-0002-0640-0422 A piece of apparatus, consisting of an eyepiece, an objective lens, a condenser lens, stage, and light source, which collects electromagnetic radiation in the visible range. The specimen is illuminated with visible light transmitted from a source on the opposite side of the specimen from the objective. https://orcid.org/0000-0001-5985-7429 2009-10-13T01:39:29Z bright-field optical microscope transmitted light microscope transmitted-light microscope CHMO:0002529 bright-field microscope CHMO:0002529 A piece of apparatus, consisting of an eyepiece, an objective lens, a condenser lens, stage, and light source, which collects electromagnetic radiation in the visible range. The specimen is illuminated with visible light transmitted from a source on the opposite side of the specimen from the objective. https://orcid.org/0000-0002-0640-0422 Microscopy where a laser is scanned over the surface of the specimen and the photocurrent is recorded as a function of position. https://orcid.org/0000-0001-5985-7429 2009-10-23T02:41:41Z SPCM CHMO:0002553 scanning photocurrent microscopy CHMO:0002553 Microscopy where a laser is scanned over the surface of the specimen and the photocurrent is recorded as a function of position. arxiv:0707.3176 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates, intermittently touching or tapping the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between oscillation amplitude or phase of the tip and the surface during scanning, which is performed under ultra-high vacuum conditions. https://orcid.org/0000-0001-5985-7429 2009-11-14T02:48:25Z AM-AFM amplitude modulation AFM amplitude modulation atomic force microscopy amplitude-modulation AFM CHMO:0002600 amplitude-modulation atomic force microscopy CHMO:0002600 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. The tip oscillates, intermittently touching or tapping the surface. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the force experienced by the tip as a function of position. A feedback loop is used to maintain a fixed relationship between oscillation amplitude or phase of the tip and the surface during scanning, which is performed under ultra-high vacuum conditions. https://orcid.org/0000-0002-0640-0422 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. A bias voltage is applied between the tip and sample, forming a capacitor with the sample surface, over which it is scanned laterally at a constant separation. The electrostatic force (measured as the change in resonant frequency of the cantilever) is probed as a function of position by changing the applied voltage. https://orcid.org/0000-0001-5985-7429 2009-12-09T05:35:47Z EFM electric force microscopy CHMO:0002638 electrostatic force microscopy CHMO:0002638 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. A bias voltage is applied between the tip and sample, forming a capacitor with the sample surface, over which it is scanned laterally at a constant separation. The electrostatic force (measured as the change in resonant frequency of the cantilever) is probed as a function of position by changing the applied voltage. FIX:0000119 https://doi.org/10.1039/b9nr00256a A transmission electron microscope where the electron beam is scanned across an electron-transparent specimen under vacuum and the intensities of the transmitted electrons are measured. batchelorc 2009-12-24T12:55:29Z STEM CHMO:0002649 scanning transmission electron microscope CHMO:0002649 A transmission electron microscope where the electron beam is scanned across an electron-transparent specimen under vacuum and the intensities of the transmitted electrons are measured. https://orcid.org/0000-0001-5985-7429 STEM A piece of apparatus which is used to produce an enlarged image of a specimen by scanning a finely focused (<10 nm diameter) electron beam with an acceleration voltage of 50–150 kV across the specimen in a gaseous environment and measuring interaction of the electrons with the specimen. https://orcid.org/0000-0001-5985-7429 2010-01-05T01:19:22Z E-SEM ESEM environmental SEM CHMO:0002656 environmental scanning electron microscope CHMO:0002656 A piece of apparatus which is used to produce an enlarged image of a specimen by scanning a finely focused (<10 nm diameter) electron beam with an acceleration voltage of 50–150 kV across the specimen in a gaseous environment and measuring interaction of the electrons with the specimen. https://orcid.org/0000-0002-0640-0422 Microscopy which uses a chemically functionalised sharp spike (e.g. with thiols) mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the chemical interactions between the tip and surface (e.g. gold) as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2010-01-09T10:47:31Z CFM CHMO:0002660 chemical force microscopy CHMO:0002660 Microscopy which uses a chemically functionalised sharp spike (e.g. with thiols) mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the chemical interactions between the tip and surface (e.g. gold) as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://doi.org/10.1039/b9nr00279k Microscopy where a probe consisting of a laser transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen and focused to a diffraction-limited spot size. A vibrating metallic AFM cantilever tip periodically and locally modifies the electromagnetic field distribution of the excitation laser. An image is produced by scanning the probe over the specimen and detecting the scattered light from the tip as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://orcid.org/0000-0001-5985-7429 2010-01-09T10:52:58Z s-SNOM sSNOM scattering SNOM scattering near-field microscopy scattering-type SNOM scattering-type near-field microscopy scattering-type near-field optical microscopy SNIM CHMO:0002662 scattering near-field optical microscopy CHMO:0002662 Microscopy where a probe consisting of a laser transmitted through a tapered optical fibre is positioned very close to (<10 nm from) the surface of the specimen and focused to a diffraction-limited spot size. A vibrating metallic AFM cantilever tip periodically and locally modifies the electromagnetic field distribution of the excitation laser. An image is produced by scanning the probe over the specimen and detecting the scattered light from the tip as a function of position. A force feedback loop is used to maintain a fixed relationship between the probe and surface during scanning. https://doi.org/10.1039/b9nr00279k SNIM Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the deflection of the tip, which is in contact with the specimen surface, as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2010-01-11T11:45:17Z contact AFM contact mode AFM contact-mode AFM contact-mode atomic force microscopy static AFM static mode AFM static mode atomic force microscopy static-mode AFM static-mode atomic force microscopy CHMO:0002669 contact mode atomic force microscopy CHMO:0002669 Microscopy which uses a sharp spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. An image of the surface is obtained by mechanically moving the probe in a raster scan of the specimen, line by line, and recording the deflection of the tip, which is in contact with the specimen surface, as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. FIX:0000116 https://orcid.org/0000-0002-0640-0422 Microscopy which uses a sharp conductive spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. A two-dimensional map of the carrier concentration profile (resistance) of the semiconducting specimen is obtained by applying a DC bias between the probe and specimen and mechanically moving the probe in a raster scan line-by-line, and recording the current as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0001-5985-7429 2010-01-11T11:46:21Z SSRM CHMO:0002670 scanning spreading resistance microscopy CHMO:0002670 Microscopy which uses a sharp conductive spike (known as a 'tip') mounted on the end of a cantilever to scan the surface of the specimen. A two-dimensional map of the carrier concentration profile (resistance) of the semiconducting specimen is obtained by applying a DC bias between the probe and specimen and mechanically moving the probe in a raster scan line-by-line, and recording the current as a function of position. A feedback loop is used to maintain a fixed relationship between the tip and surface during scanning. https://orcid.org/0000-0002-0640-0422 Microscopy where a very low concentration of fluorescent subunits in a polymer or peptide reveals the assembly dynamics, movement and turnover of assemblies throughout the image. Hils 2010-07-24T10:27:44Z fluorescent speckle microscopy FSM CHMO:0002703 fluorescence speckle microscopy CHMO:0002703 Microscopy where a very low concentration of fluorescent subunits in a polymer or peptide reveals the assembly dynamics, movement and turnover of assemblies throughout the image. https://doi.org/10.1529/biophysj.106.091116 Microscopy which uses a cantilever tipped with a ferromagnetic (iron cobalt) particle to directly detect a modulated spin gradient force between sample spins and the tip to scan the surface of a magnetic specimen. As the ferromagnetic tip moves close to the sample, the nuclear spins become attracted to it and generate a small force on the cantilever. The spins are then repeatedly flipped, causing the cantilever to gently sway back and forth in a synchronous motion. That displacement is measured with an interferometer to create a series of 2D images of the sample. Hils 2010-07-25T04:51:05Z MRFM CHMO:0002713 magnetic resonance force microscopy CHMO:0002713 Microscopy which uses a cantilever tipped with a ferromagnetic (iron cobalt) particle to directly detect a modulated spin gradient force between sample spins and the tip to scan the surface of a magnetic specimen. As the ferromagnetic tip moves close to the sample, the nuclear spins become attracted to it and generate a small force on the cantilever. The spins are then repeatedly flipped, causing the cantilever to gently sway back and forth in a synchronous motion. That displacement is measured with an interferometer to create a series of 2D images of the sample. FIX:0000125 A piece of apparatus that is used to measure a physical quantity. CHMO:0002793 sensor CHMO:0002793 A piece of apparatus that is used to measure a physical quantity. https://orcid.org/0000-0001-5985-7429 CHMO:0002894 CHMO:0002895 CIDO:0000085 A coronavirus-host interaction by which the virus enters the host cell viral entry into host cell [coronavirus infectious disease] Precious HoIP ID: HOIP_0037006 coronaviral entry to cell CIDO:0000088 A coronavirus-host interaction by which the SARS-CoV-2 virus enters the host cell PMID:32155444 PMID:32221306 PMID:32404436 PMID:32416769 PMID:32629875 PMID:33077917 PMID:33123165 viral entry into host cell [COVID-19] Following S protein binding in its prefusion state, the S1 subunit is cleaved and permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. Previous HoIP ID: HOIP_0037063 SARS-CoV-2 entry to host cell PMID:32155444 As a result, SARS-CoV-2 SB opening is expected to be necessary for interacting with ACE2 at the host cell surface and initiating the conformational changes leading to cleavage of the S2' site, membrane fusion and viral entry (Gui et al., 2017; Kirchdoerfer et al., 2018; Millet and Whittaker, 2014; Pallesen et al., 2017; Park et al., 2016; Song et al., 2018; Walls et al., 2019; Yuan et al., 2017). PMID:32221306 Here, using SARS-CoV-2 S protein pseudovirus system, we confirm that human angiotensin converting enzyme 2 (hACE2) is the receptor for SARS-CoV-2, find that SARS-CoV-2 enters 293/hACE2 cells mainly through endocytosis, that PIKfyve, TPC2, and cathepsin L are critical for entry, and that SARS-CoV-2 S protein is less stable than SARS-CoV S. While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect (Supplementary Fig. 1), indicating that TPC2, not TRPML1, is important for SARS-CoV-2 entry. PMID:32404436 Following receptor engagement, SARS-CoV-2 S is processed by a plasma membrane-associated type II transmembrane serine protease, TMPRSS2, prior to membrane fusion which is essential to release the viral contents into the host cell cytosol (3, 6). PMID:32416769 Furthermore, virus particles were reported to be present in renal endothelial cells, indicating viraemia as a possible cause of endothelial damage in the kidney and a probable contributor to AKI. PMID:32629875 In COVID-19, adding to the blood clotting risk from increased IL-6, SARS-CoV-2 can infect, replicate and induce endothelial cell death, compromising the continuity of the luminal vascular surface; a perturbed endothelium can actively participate in pro-coagulant reactions. Since SARS-CoV-2 can infect the epithelial cells on the luminal side of the small intestine and the virus has been detected in stools and rectal swabs, gastrointestinal symptoms are potentially attributable to viral infection and replication in the intestine. PMID:33077917 SARS-CoV-2 has also been found in proximal tubular cells, which exhibit high levels of ACE2 in the apical brush border. CIDO:0000187 the binding between the SARS-CoV-2 S protein and the ACE2 in a human cell https://pubmed.ncbi.nlm.nih.gov/32142651/ PMID:32075877 PMID:32142651 PMID:32155444 PMID:32221306 PMID:32225175 PMID:32307653 PMID:32361028 PMID:32404436 PMID:32629875 PMID:33077917 host cell surface receptor binding [COVID-19] SARS-CoV-2 S binding to human ACE2 HOIP_0037058 PMID:32075877 We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. 2019-nCoV makes use of a densely glycosylated spike (S) protein to gain entry into host cells. The S protein is a trimeric class I fusion protein that exists in a metastable prefusion conformation that undergoes a substantial structural rearrangement to fuse the viral membrane with the host cell membrane. This process is triggered when the S1 subunit binds to a host cell receptor. Receptor binding destabilizes the prefusion trimer, resulting in shedding of the S1 subunit and transition of the S2 subunit to a stable postfusion conformation. PMID:32142651 Finally, authentic SARS-CoV-2 infected BHK-21 cells transfected to express ACE2 cells but not parental BHK-21 cells with high efficiency (Figure 3C), indicating that SARS-2-S, like SARS-S, uses ACE2 for cellular entry. Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. PMID:32155444 We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS- CoV-2 among humans. PMID:32221306 Of note, SARS-CoV-2, but not SARS-CoV, S proteins induced syncytia formation on 293/hACE2 cells even in the absence of trypsin (Fig. 4c), suggesting that SARS-CoV-2 S proteins could be triggered upon the receptor binding without exogenous protease priming or activation. PMID:32225175 SARS-CoV-2 and SARS-CoV recognize the same receptor - human ACE2 (hACE2). PMID:32307653 SARS-CoV-2 invades host cells via two receptors: angiotensin-converting enzyme 2 (ACE2) and CD147 (also known as Basigin or EMMPRIN) (Fig. 1). Spike protein (SP) from virus binds to ACE2 or CD147 on the host cell, mediating viral invasion and dissemination of virus among other cells PMID:32361028 SARS-Cov-2 entry into a cell is dependent upon binding of the viral spike (S) protein to cellular receptor and on cleavage of the spike protein by the host cell proteases such as Cathepsin L and Cathepsin B. PMID:32404436 The attachment of SARS-CoV-2 to the target cell is initiated by interactions between the spike glycoprotein (S) and its cognate receptor, angiotensin converting enzyme 2 (ACE2) (2–5). Following receptor engagement, SARS-CoV-2 S is processed by a plasma membrane-associated type II transmembrane serine protease, TMPRSS2, prior to membrane fusion which is essential to release the viral contents into the host cell cytosol (3, 6). PMID:32629875 Also, as a consequence of SARS-CoV-2 receptor binding and entry into any cells, cell surface ACE2 is reduced in association with increased angiotensin II, which confers a pro-inflammatory, pro-coagulant and pro-apoptotic phenotype to endothelial cells. PMID:32629875 Angiotensin converting enzyme 2 (ACE2), the receptor for SARS-CoV-2 and other coronaviruses, is a transmembrane protein expressed by lung alveolar epithelial cells, enterocytes, and vascular endothelial cells, whose physiologic role is to induce the maturation of angiotensin I to generate angiotensin 1-7, a peptide hormone that controls vasoconstriction and blood pressure. A consequence of SARS-CoV-2 infection is that ACE2 function is disrupted and this disruption contributes to the pathogenesis to COVID-19. ACE2 belongs to the family of angiotensin-converting enzymes, which are essential regulators of blood pressure, cardiac function, and fluid balance. PMID:33077917 ACE2 internalization following SARS-CoV-2 infection could induce an imbalance in the renin–angiotensin–aldosterone system, with increased Ang II signalling leading to pro-inflammatory and profibrotic processes in the kidney. CIDO:0000202 A coronavirus process that involves in the release of the assemblied virion from the host cell viral release from host cell [coronavirus infectious disease] Previous HoIP ID:HOIP_0037068 coronavirus shedding CIDO:0000284 vial life cycle is the collection of the multiple steps involved in the virus processes occurring inside cells viral life cycle stage CIDO:0000285 coronavirus life cycle stage CIDO:0000287 SARS-CoV-2 release out of cell viral release from host cell [COVID-19] ウイルス排出 Previous HoIP ID:HOIP_0037020 SARS-CoV-2 shedding CLO:0000001 cell line cell cell line cell 细胞系细胞 A cultured cell that is part of a cell line - a stable and homogeneous population of cells with a common biological origin and propagation history in culture A cultured cell that is part of a cell line - a stable and homogeneous population of cells with a common biological origin and propagation history in culture 一个培养细胞，它是一个细胞株（一个稳定的，同质的细胞群，具有共同的生物学起源和增殖史）的一部分 一个培养细胞，它是一个细胞株（一个稳定的，同质的细胞群，具有共同的生物学起源和增殖史）的一部分 cell line cell cell line cell 细胞系细胞 'derives from' is transitive, so even cell line cells created through modification of an existing cell line cell have derived_from some initial primary cultured cell that existed at some point in time. CLO:0000019 immortal cell line cell immortal cell line cell 永生细胞系细胞 A cell line cell that is expected to be capable of an unlimited number of divisions, and is thus able to support indefinite propagation in vitro as part of an immortal cell line. A cell line cell that is expected to be capable of an unlimited number of divisions, and is thus able to support indefinite propagation in vitro as part of an immortal cell line. 预期能够进行无限次分裂的细胞系细胞，作为永生细胞系一部分，能够支持体外无限增殖。 immortal cell line cell immortal cell line cell 永生细胞系细胞 CLO:0000031 cell line 细胞系 A cultured cell population that represents a genetically stable and homogenous population of cultured cells that shares a common propagation history (i.e. has been successively passaged together in culture). A cultured cell population that represents a genetically stable and homogenous population of cultured cells that shares a common propagation history (i.e. has been successively passaged together in culture). 一个培养细胞群体，其代表具有共同增殖历史（即已经在培养中一起连续传代）的遗传稳定且同质的培养细胞群体。 培养的细胞群体代表具有共同繁殖历史（即已经在培养中一起连续传代）的遗传稳定且同质的培养细胞群体。 cell line 细胞系 CLO:0001601 A549 cell CLO:0003704 HepG2 cell Hep G2 cell CLO:0004283 HT-29 cell CLO:0009828 immortal cell line A cell line that is expected to be capable of indefinite propagation in an vitro culture. immortal cell line CLO:0054404 HuH-7 derived cell line cell CL:0000000 A material entity of anatomical origin (part of or deriving from an organism) that has as its parts a maximally connected cell compartment surrounded by a plasma membrane. http://purl.bioontology.org/ontology/STY/T025 The definition of cell is intended to represent all cells, and thus a cell is defined as a material entity and not an anatomical structure, which implies that it is part of an organism (or the entirety of one). cell CL:0000001 primary cultured cell primary cultured cell A cultured cell that is freshly isolated from a organismal source, or derives in culture from such a cell prior to the culture being passaged. A cultured cell that is freshly isolated from a organismal source, or derives in culture from such a cell prior to the culture being passaged. primary cultured cell primary cultured cell CL:0000010 cultured cell cultured cell A cell in vitro that is or has been maintained or propagated as part of a cell culture. A cell in vitro that is or has been maintained or propagated as part of a cell culture. cultured cell cultured cell CL:0000019 A mature male germ cell that develops from a spermatid. FBbt:00004954 FMA:67338 WBbt:0006798 sperm CL:0000023 A female germ cell that has entered meiosis. [database_cross_reference: GOC:tfm][database_cross_reference: ISBN:0721662544] Annotations oocyte CL:0000025 A female gamete where meiosis has progressed to metaphase II and is able to participate in fertilization. mature oocyte ovum egg cell CL:0000034 A relatively undifferentiated cell that retains the ability to divide and proliferate throughout life to provide progenitor cells that can differentiate into specialized cells. stem cell CL:0000039 A cell that is within the developmental lineage of gametes and is able to pass along its genetic material to offspring. germ line cell CL:0000056 A cell that is commited to differentiating into a muscle cell. Embryonic myoblasts develop from the mesoderm. They undergo proliferation, migrate to their various sites, and then differentiate into the appropriate form of myocytes. Myoblasts also occur as transient populations of cells in muscles undergoing repair. myoblast CL:0000057 A connective tissue cell which secretes an extracellular matrix rich in collagen and other macromolecules. Flattened and irregular in outline with branching processes; appear fusiform or spindle-shaped. BTO:0000452 FMA:63877 fibroblast CL:0000064 A cell that has a filiform extrusion of the cell surface. ciliated cell CL:0000066 epithelial cell A cell that is usually found in a two-dimensional sheet with a free surface. The cell has a cytoskeleton that allows for tight cell to cell contact and for cell polarity where apical part is directed towards the lumen and the basal part to the basal lamina. epithelial cell CL:0000067 An epithelial cell that has a cilia. ciliated epithelial cell CL:0000071 An endothelial cell that lines the vasculature. vascular endothelial cells blood vessel endothelial cell CL:0000082 An epithelial cell of the lung. epithelial cell of lung CL:0000083 An epithelial cell of the pancreas. epithelial cell of pancreas CL:0000084 T cell A type of lymphocyte whose defining characteristic is the expression of a T cell receptor complex. T cell CL:0000091 A tissue-resident macrophage of the reticuloendothelial system found on the luminal surface of the hepatic sinusoids involved in erythrocyte clearance. Markers include F4/80+, CD11b-low, CD68-positive, sialoadhesin-positive, CD163/SRCR-positive. Irregular, with long processes including lamellipodia extending into the sinusoid lumen, have flattened nucleus with cytoplasm containing characteristic invaginations of the plasma membrane (vermiform bodies); lie within the sinusoid lumen attached to the endothelial surface; derived from the bone marrow, form a major part of the body's mononuclear phagocyte system. Markers: Mouse: F4/80+, CD11b-low, CD68+, sialoadhesin+, CD163/SRCR+; role or process: immune, antigen-presentation, clearance of senescent erythrocytes, iron metabolism. Kupffer cells are also reportedly C3aR-positive, CD14-low, CD54-positive, CD88-positive, and CD284-positive. They are also capable of producing IL-1, IL-6, TNF-alpha, nitric oxide, PGD2, PGE2, PGF2alpha, and TXA2. Kupffer cell CL:0000094 A leukocyte with abundant granules in the cytoplasm. A leukocyte with abundant granules in the cytoplasm. granulocyte A leukocyte with abundant granules in the cytoplasm. MESH:D006098 CL:0000097 A cell that is found in almost all tissues containing numerous basophilic granules and capable of releasing large amounts of histamine and heparin upon activation. Progenitors leave bone marrow and mature in connective and mucosal tissue. Mature mast cells are found in all tissues, except the bloodstream. Their phenotype is CD117-high, CD123-negative, CD193-positive, CD200R3-positive, and FceRI-high. Stem-cell factor (KIT-ligand; SCF) is the main controlling signal of their survival and development. BTO:0000830 FMA:66784 mast cell CL:0000113 A vertebrate phagocyte with a single nucleus. mononuclear phagocyte CL:0000115 An endothelial cell comprises the outermost layer or lining of anatomical structures and can be squamous or cuboidal. In mammals, endothelial cell has vimentin filaments and is derived from the mesoderm. endothelial cell CL:0000134 A connective tissue cell that normally gives rise to other cells that are organized as three-dimensional masses. In humans, this cell type is CD73-positive, CD90-positive, CD105-positive, CD45-negative, CD34-negative, and MHCII-negative. They may further differentiate into osteoblasts, adipocytes, myocytes, neurons, or chondroblasts in vitro. Originally described as residing in the bone marrow, this cell type is now known to reside in many, if not all, adult organs. mesenchymal stem cells CL:0000136 A fat-storing cell found mostly in the abdominal cavity and subcutaneous tissue of mammals. Fat is usually stored in the form of triglycerides. BTO:0000443 CALOHA:TS-0012 FMA:63880 adipocyte adipose cell fat cell CL:0000151 A cell that specializes in controlled release of one or more substances. BTO:0003659 FMA:86916 secretory cell CL:0000160 A cell of the epithelial lining that produce and secrete mucins. goblet cell CL:0000168 insulin secreting cell is a secretory cell and is capable of some insulin secretion BTO:0000783 insulin secreting cell CL:0000169 Pancreatic beta cells are also reportedly CD284-positive. Upon activation, they upregulate their CD14 expression. A cell that secretes insulin and is located towards the center of the islets of Langerhans. FMA:70586 ncithesaurus:Beta_Cell type B pancreatic cell CL:0000182 The main structural component of the liver. They are specialized epithelial cells that are organized into interconnected plates called lobules. Majority of cell population of liver, polygonal in shape, arranged in plates or trabeculae between sinusoids; may have single nucleus or binucleated. hepatocyte CL:0000186 An animal cell that has characteristics of both a fibroblast cell and a smooth muscle cell. myofibroblast cell CL:0000192 A non-striated, elongated, spindle-shaped cell found lining the digestive tract, uterus, and blood vessels. They develop from specialized myoblasts (smooth muscle myoblast). smooth muscle cell CL:0000232 erythrocyte A red blood cell. In mammals, mature erythrocytes are biconcave disks containing hemoglobin whose function is to transport oxygen. erythrocyte CL:0000233 A non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation. Platelets are reportedly CCR1-positive, CCR2-negative, CCR3-positive, CCR4-positive, CCR5-negative, CCR6-negative, CCR7-negative, CCR8-negative, CCR9-negative, CCR10-negative, CD16-positive, CD23-positive, CD32-positive, CD40-positive, CD41-positive CD42-positive, CD61-positive, CD62P-positive, CD64-positive, CD89-positive, CD102-positive, CD147-positive (activated platelets), CD154-positive (activated platelets), CD162-positive, CD209, CD282-positive, CD284-positive, CD289-positive, CD181-negative, CD182-negative, CD183-negative, CD184-positive, CLEC2-positive, GPVI-positive, JAMC-positive, PAR1-positive, PAR2-negative, PAR3-positive, PAR4-positive, TSP1-positive, and TXA2R-positive. Platelets can reportedly produce CCL2, CCL3, CCL5, CCL7, CCL17, CD40L, CXCL1, CXCL4, CXCL4L1, CXCL5, CXCL7, CXCL8, CXCL12, EGF, factor V, factor VII, factor XI, factor XIII, bFGF, histamine, IGF-1, IL-1beta, PAI-1, PDGF, plasminogen, protein S, serotonin, TGF-beta, TFPI, VEGF, and vWF. A non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation. platelet CL:0000234 Any cell capable of ingesting particulate matter via phagocytosis. Any cell capable of ingesting particulate matter via phagocytosis. phagocyte Any cell capable of ingesting particulate matter via phagocytosis. ISBN:0721601464 CL:0000235 A mononuclear phagocyte present in variety of tissues, typically differentiated from monocytes, capable of phagocytosing a variety of extracellular particulate material, including immune complexes, microorganisms, and dead cells. histiocyte Morphology: Diameter 30_M-80 _M, abundant cytoplasm, low N/C ratio, eccentric nucleus. Irregular shape with pseudopods, highly adhesive. Contain vacuoles and phagosomes, may contain azurophilic granules; markers: Mouse &amp; Human: CD68, in most cases CD11b. Mouse: in most cases F4/80+; role or process: immune, antigen presentation, &amp; tissue remodelling; lineage: hematopoietic, myeloid. macrophage CL:0000236 B cell A lymphocyte of B lineage with the phenotype CD19-positive, CD20-positive, and capable of B cell mediated immunity. B cell CL:0000312 An epidermal cell which synthesizes keratin and undergoes a characteristic change as it moves upward from the basal layers of the epidermis to the cornified (horny) layer of the skin. Successive stages of differentiation of the keratinocytes forming the epidermal layers are basal cell, spinous or prickle cell, and the granular cell. keratinocyte CL:0000322 An epithelial cell that lines the peripheral gas exchange region of the lungs of air-breathing vertebrates. pneumocyte CL:0000448 Fat cells with light coloration and few mitochondria. They contain a scant ring of cytoplasm surrounding a single large lipid droplet or vacuole. CALOHA:TS-1119 FMA:83434 white fat cell CL:0000449 A cell from the thermogenic form of adipose tissue found in many species, particularly in newborns and hibernating mammals, but also in lesser amounts in adults of other mammals including humans. Brown fat is capable of rapid liberation of energy and seems to be important in the maintenance of body temperature immediately after birth and upon waking from hibernation. CALOHA:TS-0099 FMA:83435 brown adipocyte brown adipose cell brown fat cell CL:0000451 dendritic cell A cell of hematopoietic origin, typically resident in particular tissues, specialized in the uptake, processing, and transport of antigens to lymph nodes for the purpose of stimulating an immune response via T cell activation. These cells are lineage negative (CD3-negative, CD19-negative, CD34-negative, and CD56-negative). dendritic cell CL:0000492 A CD4-positive, alpha-beta T cell that cooperates with other lymphocytes via direct contact or cytokine release to initiate a variety of immune functions. CD4-positive helper T cell CL:0000540 The basic cellular unit of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the nervous system. neuron CL:0000542 A lymphocyte is a leukocyte commonly found in the blood and lymph that has the characteristics of a large nucleus, a neutral staining cytoplasm, and prominent heterochromatin. lymphocyte CL:0000545 A CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive, CXCR3-positive, CCR6-negative, and is capable of producing interferon-gamma. T-helper 1 cell CL:0000546 A CD4-positive, alpha-beta T cell that has the phenotype GATA-3-positive, CXCR3-negative, CCR6-negative, and is capable of producing interleukin-4. T-helper 2 cell CL:0000576 Myeloid mononuclear recirculating leukocyte that can act as a precursor of tissue macrophages, osteoclasts and some populations of tissue dendritic cells. BTO:0000876 FMA:62864 monocyte CL:0000578 experimentally modified cell in vitro experimentally modified cell in vitro A cell in vitro that has undergone physical changes as a consequence of a deliberate and specific experimental procedure. A cell in vitro that has undergone physical changes as a consequence of a deliberate and specific experimental procedure. experimentally modified cell in vitro experimentally modified cell in vitro CL:0000584 An epithelial cell that has its apical plasma membrane folded into microvilli to provide ample surface for the absorption of nutrients from the intestinal lumen. enterocyte CL:0000586 The reproductive cell in multicellular organisms. [database_cross_reference: MESH:A05.360.490] WBbt:0006796 germ cell CL:0000623 A lymphocyte that can spontaneously kill a variety of target cells without prior antigenic activation via germline encoded activation receptors and also regulate immune responses via cytokine release and direct contact with other cells. natural killer cell ISBN:0815341504 ISBN:0815341504 ISBN:0815341504 ISBN:0815341504 ISBN:0815341504 ISBN:0815341504 CL:0000624 A mature alpha-beta T cell that expresses an alpha-beta T cell receptor and the CD4 coreceptor. CD4-positive, alpha-beta T cell CL:0000625 A T cell expressing an alpha-beta T cell receptor and the CD8 coreceptor. CD8-positive, alpha-beta T cell CL:0000632 A cell that is found in the perisinusoidal space of the liver that is capable of multiple roles including storage of retinol, presentation of antigen to T cells (including CD1d-restricted NKT cells), and upon activation, production of extracellular matrix components that can contribute to liver fibrosis. This activated state has a myofibroblast-like phenotype, though it's not clear in the literature if this is terminally differentiated. This cell type comprises approximately 8-15% of total cells in the liver. Ito cell hepatic perisinusoidal cell perisinusoidal cell hepatic stellate cell CL:0000650 A cell type that encapsulates the capillaries and venules in the kidney. This cell secretes mesangial matrix that provides the structural support for the capillaries. mesangial cell CL:0000675 A mature sexual reproductive cell of the female germline. female gamete CL:0000738 An achromatic cell of the myeloid or lymphoid lineages capable of ameboid movement, found in blood or other tissue. leucocyte white blood cell leukocyte CL:0000767 Any of the immature or mature forms of a granular leukocyte that in its mature form has an irregularly shaped, pale-staining nucleus that is partially constricted into two lobes, and with cytoplasm that contains coarse, bluish-black granules of variable size. Basophils contain vasoactive amines such as histamine and serotonin, which are released on appropriate stimulation. A basophil is CD123-positive, CD193-positive, CD203c-positive, and FceRIa-positive. Any of the immature or mature forms of a granular leukocyte that in its mature form has an irregularly shaped, pale-staining nucleus that is partially constricted into two lobes, and with cytoplasm that contains coarse, bluish-black granules of variable size. Basophils contain vasoactive amines such as histamine and serotonin, which are released on appropriate stimulation. A basophil is CD123-positive, CD193-positive, CD203c-positive, and FceRIa-positive. basophil Any of the immature or mature forms of a granular leukocyte that in its mature form has an irregularly shaped, pale-staining nucleus that is partially constricted into two lobes, and with cytoplasm that contains coarse, bluish-black granules of variable size. Basophils contain vasoactive amines such as histamine and serotonin, which are released on appropriate stimulation. A basophil is CD123-positive, CD193-positive, CD203c-positive, and FceRIa-positive. PMCID:PMC2626675 PMID:11927641 PMID:19741522 PMID:9933081 CL:0000771 Any of the immature or mature forms of a granular leukocyte with a nucleus that usually has two lobes connected by one or more slender threads of chromatin, and cytoplasm containing coarse, round granules that are uniform in size and which can be stained by the dye eosin. Eosinophils are CD9-positive, CD191-positive, and CD193-positive. Any of the immature or mature forms of a granular leukocyte with a nucleus that usually has two lobes connected by one or more slender threads of chromatin, and cytoplasm containing coarse, round granules that are uniform in size and which can be stained by the dye eosin. Eosinophils are CD9-positive, CD191-positive, and CD193-positive. eosinophil Any of the immature or mature forms of a granular leukocyte with a nucleus that usually has two lobes connected by one or more slender threads of chromatin, and cytoplasm containing coarse, round granules that are uniform in size and which can be stained by the dye eosin. Eosinophils are CD9-positive, CD191-positive, and CD193-positive. ISBN:0721601464 PMCID:PMC2626675 PMID:10914487 PMID:1662676 CL:0000775 Any of the immature or mature forms of a granular leukocyte that in its mature form has a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. Any of the immature or mature forms of a granular leukocyte that in its mature form has a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. BTO:0000130 CALOHA:TS-0688 FMA:62860 neutrocyte neutrophil leucocyte neutrophil leukocyte neutrophilic leucocyte neutrophilic leukocyte neutrophil Any of the immature or mature forms of a granular leukocyte that in its mature form has a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. ISBN:0721601464 CL:0000786 plasma cell A terminally differentiated, post-mitotic, antibody secreting cell of the B cell lineage with the phenotype CD138-positive, surface immunonoglobulin-negative, and MHC Class II-negative. Plasma cells are oval or round with extensive rough endoplasmic reticulum, a well-developed Golgi apparatus, and a round nucleus having a characteristic cartwheel heterochromatin pattern and are devoted to producing large amounts of immunoglobulin. http://purl.jp/bio/10/lsd/term/J089510 plasma cell CL:0000789 alpha-beta T cell A T cell that expresses an alpha-beta T cell receptor complex. alpha-beta T cell CL:0000794 A CD8-positive, alpha-beta T cell that is capable of killing target cells in an antigen specific manner with the phenotype perforin-positive and granzyme B-positive. CD8-positive, alpha-beta cytotoxic T cell CL:0000813 A long-lived, antigen-experienced T cell that has acquired a memory phenotype including distinct surface markers and the ability to differentiate into an effector T cell upon antigen reexposure. memory T cell CL:0000814 A mature alpha-beta T cell of a distinct lineage that bears natural killer markers and a T cell receptor specific for a limited set of ligands. NK T cells have activation and regulatory roles particularly early in an immune response. mature NK T cell CL:0000842 mononuclear cell A leukocyte with a single non-segmented nucleus in the mature form. BTO:0000878 CALOHA:TS-0768 FMA:86713 mononuclear cell CL:0000863 An elicited macrophage that is recruited into the tissues in response to injury and infection as part of an inflammatory response, expresses high levels of pro-inflammatory cytokines, ROS and NO, and shows potent microbicidal activity. M1 macrophage Markers: Express: TNFa, IL1b, IL6, iNOS, NADPH-oxidase; produce: reactive oxygen species, nitric oxide; role or process: immune, inflammation (inflammatory response). inflammatory macrophage CL:0000864 A macrophage constitutively resident in a particular tissue under non-inflammatory conditions, and capable of phagocytosing a variety of extracellular particulate material, including immune complexes, microorganisms, and dead cells. tissue-resident macrophage CL:0000891 A type of cell containing lipids in small vacuoles and typically seen in atherolosclerotic lesions, as well as other conditions. foam cell CL:0000899 CD4-positive, alpha-beta T cell with the phenotype RORgamma-t-positive, CXCR3-negative, CCR6-positive, and capable of producing IL-17. T-helper 17 cell CL:0000901 CD4-positive alpha-beta T cell with regulatory function that produces IL-10. Tr1 cell CL:0000910 A mature T cell that differentiated and acquired cytotoxic function with the phenotype perforin-positive and granzyme-B positive. cytotoxic T cell CL:0000912 A effector T cell that provides help in the form of secreted cytokines to other immune cells. helper T cell CL:0000988 A cell of a hematopoietic lineage. BTO:0000574 CALOHA:TS-2017 FMA:70366 FMA:83598 haematopoietic cell haemopoietic cell hemopoietic cell hematopoietic cell CL:0001042 CD4-positive, alpha-beta T cell that produces IL-22. T-helper 22 cell CL:0002038 A CD4-positive, CXCR5-positive, CCR7-negative alpha-beta T cell located in follicles of secondary lymph nodes that expresses is BCL6-high, ICOS-high and PD1-high, and stimulates follicular B cells to undergo class-switching and antibody production. T follicular helper cell CL:0002062 A type I pneumocyte is a flattened, branched pneumocyte that covers more than 98% of the alveolar surface. This large cell has thin (50-100 nm) cytoplasmic extensions to form the air-blood barrier essential for normal gas exchange type I pneumocyte CL:0002063 A type II pneumocyte is a pneumocyte that modulates the fluid surrounding the alveolar epithelium by secreting and recycling surfactants. This cell type also contributes to tissue repair and can differentiate after injury into a type I pneumocyte. Thicker than squamous alveolar cells, have a rounded apical surface that projects above the level of surrounding epithelium. The free surface is covered by short microvilli. type II pneumocyte CL:0002188 An endothelial cell found in the glomerulus of the kidney. This cell is flattened, highly fenestrated, and plays a vital role in the formation of glomerular ultrafiltrate. glomerular endothelial cell CL:0002320 A cell of the supporting or framework tissue of the body, arising chiefly from the embryonic mesoderm and including adipose tissue, cartilage, and bone. CALOHA:TS-2096 FMA:63875 connective tissue cell CL:0002368 An endo-epithelial cell of the respiratory tract. respiratory epithelial cell CL:0002371 A cell of an organism that does not pass on its genetic material to the organism's offspring (i.e. a non-germ line cell). somatic cell CL:0002480 A goblet cell located in the nasal epithelium. nasal mucosa goblet cell CL:0002563 An epithelial cell of the intestine. intestinal epithelial cell CL:0008019 A non-polarised cell precursor cell that is part of some mesenchyme, is associated with the cell matrix but is not connected to other cells and is capable of migration. mesenchymal cell CL:0009002 Any cell participating in the inflammatory response to a foreign substance, e.g. neutrophil, macrophage. inflammatory cell CL:0010003 An epithelial cell that is part_of a alveolus of lung. epithelial cell of alveolus of lung CL:0010017 A zygote in a plant or an animal. zygote CL:1000488 An epithelial cell that is part of the bile duct. Cholangiocytes contribute to bile secretion via net release of bicarbonate and water. They are cuboidal epithelium in the small interlobular bile ducts, but become columnar and mucus secreting in larger bile ducts approaching the porta hepatis and the extrahepatic ducts. cholangiocyte CL:1000494 An epithelial cell that is part of a nephron tubule. renal tubular epithelial cells nephron tubule epithelial cell CL:1000507 renal tubular cells kidney tubule cell CL:2000001 A leukocyte with a single non-segmented nucleus in the mature form found in the circulatory pool of blood. peripheral blood mononuclear cell CL:2000063 Any fibroblast that is part of a female gonad. ovarian fibroblast CL:2000094 Any epithelial cell of viscerocranial mucosa that is part of a nasal cavity respiratory epithelium. nasal cavity respiratory epithelium epithelial cell of viscerocranial mucosa DOID:0040099 A vasculitis with purpuric ulcers. livedoid vasculitis A pulmonary fibrosis that is characterized by scarring of the lung. EFO:0000768 GARD:8609 ICD10CM:J84.112 ICD9CM:516.31 MESH:D054990 NCI:C35716 OMIM:178500 SNOMEDCT_US_2023_03_01:28168000 UMLS_CUI:C1800706 FIBROCYSTIC PULMONARY DYSPLASIA IDIOPATHIC PULMONARY FIBROSIS, FAMILIAL cryptogenic fibrosing alveolitis disease_ontology DOID:0050156 OMIM mapping confirmed by DO. [SN]. idiopathic pulmonary fibrosis DOID:0050156 A pulmonary fibrosis that is characterized by scarring of the lung. url:https://www.pulmonaryfibrosis.org/life-with-pf/about-ipf DOID:0050700 A heart disease and a myopathy that is characterized by deterioration of the function of the heart muscle. cardiomyopathy A vascular disease that is located_in an artery. lschriml 2014-02-12T03:08:35Z disease_ontology DOID:0050828 artery disease DOID:0050828 A vascular disease that is located_in an artery. url:http://en.wikipedia.org/wiki/Artery#Pathology A glomerulonephritis that is characterized by hardening of the glomerulus in the kidney. A glomerulonephritis that is characterized by hardening of the glomerulus in the kidney. lschriml 2014-04-15T03:40:31Z disease_ontology DOID:0050851 glomerulosclerosis DOID:0050851 A glomerulonephritis that is characterized by hardening of the glomerulus in the kidney. url:http://en.wikipedia.org/wiki/Glomerulosclerosis DOID:0050855 A kidney disease that is characterized by progressive detrimental connective tissue deposition of the kidney parenchyma leading to deterioration of renal function. renal fibrosis DOID:0060903 A vascular disease caused by the formation of a blood clot inside a blood vessel, obstructing the flow of blood through the circulatory system. thrombosis DOID:0070111 A Niemann-Pick disease characterized by onset in infancy and involvement of neurological tissues that has_material_basis_in an autosomal recessive mutation of SMPD1 on chromosome 11p15.4. ICD10CM:E75.2 OMIM:257200 Niemann-Pick disease type A DOID:0070112 A Niemann-Pick disease characterized by visceral involvement only and survival into adulthood that has_material_basis_in an autosomal recessive mutation of SMPD1 on chromosome 11p15.4. ICD10CM:E75.2 OMIM:607616 Niemann-Pick disease type B DOID:0070113 A Niemann-Pick disease that has_material_basis_in an autosomal recessive mutation of NPC1 on chromosome 18q11.2. ICD10CM:E75.2 OMIM:257220 NPC1 Niemann-Pick disease type C1 DOID:0070114 A Niemann-Pick disease that has_material_basis_in an autosomal recessive mutation of NPC2 on chromosome 14q24.3. ICD10CM:E75.2 OMIM:607625 NPC2 Niemann-Pick disease type C2 DOID:0080208 A steatotic liver disease characterized by at least one of five cardiometabolic risk factors (adjusted for age, sex and ethnicity), alcohol consumption below 140g/week (female) or 210g/week (male), and no other discernible cause. The five cardiometabolic risk factors are:\n(1) Body mass index ≥ 25 kg/m2 (adult), 23 kg/m2 (adult Asian), or 85th percentile (pediatric); waist circumference > 94 cm (adult male), 80 cm (adult female), or 95th percentile (pediatric); or ethnicity adjusted equivalents.\n(2) Fasting serum glucose ≥ 5.6 mmol/L, 2-hr post-load glucose levels ≥ 7.8 mmol/L, glycated hemoglobin (HbA1c) ≥ 5.7% (39 mmol/L), type 2 diabetes, treatment for type 2 diabetes, previously diagnosed or treated type 2 diabetes (pediatric only), or serum glucose ≥ 11.1 mmol/L (pediatric only).\n(3) Blood pressure ≥ lower of 130/85 mmHg or 95th percentile (age < 13 years), or 130/85 mmHg (age ≥ 13 years); or specific hypertensive drug treatment.\n(4) Plasma triglycerides ≥ 1.15 mmol/L (age < 10 years) or 1.70 mmol/L (age ≥ 10 years); or lipid lowering treatment.\n(5) Plasma high-density lipoprotein cholesterol ≤ 1.0 mmol/L (adult male, pediatric) or 1.3 mmol/L (adult female); or lipid lowering treatment. https://pubmed.ncbi.nlm.nih.gov/37364816/ MAFLD MASLD NAFLD non-alcoholic fatty liver disease metabolic dysfunction-associated steatotic liver disease DOID:0080599 A viral infectious disease that has_material_basis_in Coronavirus. Coronavirus infectious disease DOID:0080600 A Coronavirus infection that is characterized by fever, cough and shortness of breath and that has_material_basis_in SARS-CoV-2. A viral infectious disease that has_material_basis_in Coronavirus. PMID:32007143 PMID:32007145 https://www.cdc.gov/coronavirus/2019-ncov/about/index.htm https://www.who.int/emergencies/diseases/novel-coronavirus-2019 COVID-19 DOID:0080642 A Coronavirus infection that is characterized by severe respiratory illness, including fever, cough, and shortness of breath and that has_material_basis_in MERS-CoV. PMID:23891402 https://www.cdc.gov/coronavirus/mers/index.html MERS Middle East respiratory syndrom DOID:0080711 A Coronavirus infectious disease that is characterized by a patient aged less than 21 years with fever, laboratory evidence of inflammation, and evidence of clinically severe illness requiring hospitalization, with multisystem organ involvement (cardiovascular, dermatologic, gastrointestinal, hematologic, neurologic, renal, or respiratory) who tested positive for SARS-CoV-2 or had exposure to COVID-19. multisystem inflammatory syndrome in children DOID:10273 A cardiovascular system disease that involves the heart's electrical conduction system. heart block heart conduction disease DOID:11247 Defibrination syndrome Diffuse or disseminated intravascular coagulation disseminated intravascular coagulation DOID:11394 A respiratory failure that results from diffuse injury to the endothelium of the lung (as in sepsis, chest trauma, massive blood transfusion, aspiration of the gastric contents, or pneumonia) and is characterized by pulmonary edema with an abnormally high amount of protein in the edematous fluid and by difficult rapid breathing and hypoxemia. ARDS Non-cardiogenic pulmonary edema adult RDS adult respiratory distress syndrome Shock lung acute respiratory distress syndrome DOID:11396 A respiratory failure that is characterized by the accumulation of fluid in the lung tissues causing disturbance of the gas exchange that may lead to respiratory failure. pulmonary edema DOID:11840 Coronary vasospasm refers to when a coronary artery suddenly undergoes either complete or sub-total temporary occlusion. (Wikipedia:Coronary vasospasm) Coronary Vasospasm Coronary artery spasm coronary artery vasospasm In general, it is thought that an abnormality within a coronary artery causes it to become hyperreactive to vasoconstrictor stimuli. DOID:12842 An autoimmune disease of peripheral nervous system that causes body's immune system to attack part of the peripheral nervous system. Guillain-Barre syndrome DOID:13378 A lymphadenitis characterized by swelling of cervical lymph nodes in infants and young children and inflammation of medium-sized blood vessels located_in body, has_symptom fever, has_symptom congestion of ocular conjunctivae, has_symptom reddening of lips, has_symptom reddening of oral cavity, has_symptom protuberance of tongue papillae and has_symptom edema of extremities. Kawasaki disease DOID:14504 A sphingoliidosis characterized by the accumulation of the lipid sphingomyelin in lysosomes in cells. Sphingomyelinase Deficiency Disease lipoid histiocytosis (classical phosphatide) sphingomyelin lipidosis Niemann-Pick disease An eye disease that is characterized by an unstable or a sustained increase in the intraocular pressure which the eye cannot withstand without damage to its structure or impairment of its function. EFO:0000516 ICD10CM:H40 ICD9CM:365 MESH:D005901 NCI:C26782 SNOMEDCT_US_2023_03_01:155120009 UMLS_CUI:C0017601 disease_ontology DOID:1686 glaucoma DOID:1686 An eye disease that is characterized by an unstable or a sustained increase in the intraocular pressure which the eye cannot withstand without damage to its structure or impairment of its function. url:https://en.wikipedia.org/wiki/Glaucoma url:https://www.aao.org/eye-health/diseases/what-is-glaucoma A disease of anatomical entity that is located_in kidney, ureter, bladder and urethra. DOID:579 NCI:C27599 UMLS_CUI:C1335051 Non-neoplastic urinary tract disease urinary tract disease disease_ontology DOID:18 urinary system disease DOID:18 A disease of anatomical entity that is located_in kidney, ureter, bladder and urethra. url:http://en.wikipedia.org/wiki/Urinary_system DOID:1837 A metabolic acidosis that is characterized by the shift of acid-base status of the body toward the acid side accompanied by the accumulation of ketone bodies in body tissues and fluids, resulting from uncontrolled diabetes mellitus. diabetic ketoacidosis EFO:0003914 ICD10CM:I70 ICD9CM:440 MESH:D050197 NCI:C35768 SNOMEDCT_US_2023_03_01:155414001 UMLS_CUI:C0004153 disease_ontology DOID:1936 atherosclerosis MESH:D050197 DOID:1936 DOID:2237 Hepatitis is inflammation of the liver tissue. (https://en.wikipedia.org/wiki/Hepatitis) acute hepatitis chronic hepatitis hepatitis DOID:224 A brain ischemia that is characterized by ischemia of brief duration and without resultant tissue death. transient ischemic attack DOID:225 A disease characterized by a group of signs and symptoms that occur together and characterize a particular abnormality. MESH:D013577 NCI:C28193 Syndrome ICD10CM:I70 ICD9CM:440 MESH:D050197 NCI:C34403 NCI:C35768 SNOMEDCT_US_2023_03_01:155414001 SNOMEDCT_US_2023_03_01:39468009 UMLS_CUI:C0004153 UMLS_CUI:C3665365 Cardiovascular arteriosclerosis disease_ontology DOID:2348 arteriosclerotic cardiovascular disease DOID:2348 An artery disease that is characterized by a thickening and hardening of arterial walls in the arteries. An artery disease that is characterized by a thickening and hardening of arterial walls in the arteries. ICD10CM:I70 MESH:D001161 NCI:C34398 SNOMEDCT_US_2023_03_01:195251000 UMLS_CUI:C0003850 Arteriosclerotic vascular disease disease_ontology DOID:2349 arteriosclerosis DOID:2349 An artery disease that is characterized by a thickening and hardening of arterial walls in the arteries. url:http://en.wikipedia.org/wiki/Arteriosclerosis DOID:2945 A Coronavirus infection that results_in infection located_in respiratory tract, has_material_basis_in SARS coronavirus (SARS-CoV), which is transmitted_by droplet spread of respiratory secretions, transmitted_by ingestion of contaminated food, or transmitted_by fomites. The infection has_symptom fever, has_symptom headache, has_symptom body aches, has_symptom dry cough, and has_symptom hypoxia. ICD10CM:J12.81 SARS severe acute respiratory syndrome DOID:3454 A cerebrovascular disease that is characterized by tissue necrosis located_in the brain, resulting from inadequate blood flow through the brain. brain infarct cerebral infarction brain infarction An interstitial lung disease that is characterized by destruction, scarring, and thickening of the interstitial lung tissues and progressive pulmonary function loss in a restrictive pattern, has_symptom progressive shortness of breath, fatigue, and chronic cough, possibly has_material_basis_in exposure to certain chemicals, autoimmune conditions, and radiation. An interstitial lung disease that is characterized by destruction, scarring, and thickening of the interstitial lung tissues and progressive pulmonary function loss in a restrictive pattern, has_symptom progressive shortness of breath, fatigue, and chronic cough, possibly has_material_basis_in exposure to certain chemicals, autoimmune conditions, and radiation. MESH:D011658 NCI:C26869 SNOMEDCT_US_2023_03_01:155613001 UMLS_CUI:C0034069 Fibrosis of lung disease_ontology DOID:3770 pulmonary fibrosis pulmonary fibrosis DOID:3770 An interstitial lung disease that is characterized by destruction, scarring, and thickening of the interstitial lung tissues and progressive pulmonary function loss in a restrictive pattern, has_symptom progressive shortness of breath, fatigue, and chronic cough, possibly has_material_basis_in exposure to certain chemicals, autoimmune conditions, and radiation. url:https://www.sciencedirect.com/science/article/pii/S0954611106004331 DOID:4 A disease is a disposition (i) to undergo pathological processes that (ii) exists in an organism because of one or more disorders in that organism. MESH:D004194 NCI:C2991 SNOMEDCT_US_2016_03_01:64572001 UMLS_CUI:C0012634 disease DOID:4724 A brain disease that is characterized by excess accumulation of fluid in the intracellular and/or extracellular spaces of the brain, has_symptom nausea, has_symptom vomiting, has_symptom blurred vision, has_symptom seizure, has_symptom coma. brain edema DOID:5214 demyelinating polyneuropathy DOID:552 A lung disease that involves lung parenchyma or alveolar inflammation and abnormal alveolar filling with fluid (consolidation and exudation). It results from a variety of causes including infection with bacteria, viruses, fungi or parasites, and chemical or physical injury to the lungs. It is accompanied by fever, chills, cough, and difficulty in breathing. pneumonia (disease) A urinary system disease that is located_in the kidney. DOID:11705 EFO:0003086 ICD10CM:N08 MESH:D007674 NCI:C3149 SNOMEDCT_US_2023_03_01:266612003 UMLS_CUI:C0022658 impaired renal function disease nephropathy disease_ontology DOID:557 kidney disease DOID:557 A urinary system disease that is located_in the kidney. url:http://www.nlm.nih.gov/medlineplus/kidneydiseases.html DOID:576 A kidney disease that is characterized by the presence of excess proteins in the urine. proteinuria DOID:5844 A coronary artery disease characterized by myocardial cell death (myocardial necrosis) due to prolonged ischaemia. myocardial infarction DOID:614 lymphopenia is a subtype of decreasing quantity: A process that changes the amount of lymphocytes to be lower. A leukopenia that is the condition of having an abnormally low level of lymphocytes in the blood. lymphocytopenia lymphopenia DOID:615 Leukopenia is a subtype of decreasing quantity: A process that changes the amount of leukocytes to be lower. A leukocyte disorder that is characterized by a decrease in the number of white blood cells (leukocytes) found in the blood, which places individuals at increased risk of infection. leucopenia DOID:6195 A conjunctival disease characterized by an inflammation of the conjunctiva, the outermost layer of the eye and the inner surface of the eyelids. conjunctivitis DOID:820 An extrinsic cardiomyopathy that is characterized as an inflammation of the heart muscle. myocarditis An arthritis that has_material_basis_in worn out cartilage located_in joint. EFO:0002506 ICD9CM:715.3 UMLS_CUI:C0157946 Osteoarthrosis and allied disorder degenerative arthritis degenerative joint disease hypertrophic arthritis osteoarthrosis disease_ontology DOID:8398 Xref MGI. osteoarthritis MESH:D010003 DOID:8398 An arthritis that has_material_basis_in worn out cartilage located_in joint. url:http://en.wikipedia.org/wiki/Osteoarthritis url:http://www.mayoclinic.com/health/osteoarthritis/DS00019 url:http://www.nlm.nih.gov/medlineplus/ency/article/000423.htm A bone inflammation disease that involves a response to irritation or injury, characterized by joint pain, swelling, stiffness located_in joint. ICD10CM:M19.90 MESH:D001168 NCI:C2883 SNOMEDCT_US_2023_03_01:372091005 UMLS_CUI:C0003864 Inflammatory disorder of joint disease_ontology DOID:848 arthritis MESH:D001168 DOID:848 A bone inflammation disease that involves a response to irritation or injury, characterized by joint pain, swelling, stiffness located_in joint. url:http://en.wikipedia.org/wiki/Arthritis url:http://www.arthritis.org/ url:http://www.nlm.nih.gov/medlineplus/ency/article/001243.htm url:https://www.cdc.gov/arthritis/index.htm ls:IEDB DOID:8516 pulmonary embolism and infarction DOID:8517 Acute cor pulmonale is a form of acute right heart failure produced by a sudden increase in resistance to blood flow in the pulmonary circulation, which is now rapidly recognized by bedside echocardiography. (PMID: 19186411) Wikipedia:Pulmonary_heart_disease Pulmonary heart disease acute cor pulmonale Wikipedia:Pulmonary_heart_disease Pulmonary heart disease, also known as cor pulmonale, is the enlargement and failure of the right ventricle of the heart as a response to increased vascular resistance (such as from pulmonic stenosis) or high blood pressure in the lungs Chronic pulmonary heart disease usually results in right ventricular hypertrophy (RVH), whereas acute pulmonary heart disease usually results in dilatation. Dilatation is a stretching (in length) of the ventricle in response to acute increased pressure. The causes of pulmonary heart disease (cor pulmonale) are the following: Acute respiratory distress syndrome (ARDS) etc. DOID:934 A disease by infectious agent that results in infection, has_material_basis_in Viruses. viral infectious disease DOID:9351 A glucose metabolism disease characterized by chronic hyperglycaemia with disturbances of carbohydrate, fat and protein metabolism resulting from defects in insulin secretion, insulin action, or both. MESH:D003920 NCI:C298 diabetes mellitus DOID:9352 A diabetes mellitus that involves high blood glucose resulting from cells fail to use insulin properly. ICD10CM:E11 MESH:D003924 NCI:C26747 SNOMEDCT_US_2018_03_01 NIDDM non-insulin-dependent diabetes mellitus type II diabetes mellitus type 2 diabetes mellitus DOID:9452 A lipid storage disease characterized by the accumulation of large vacuoles of triglyceride fat in liver cells via the process of steatosis. Steatosis of liver hepatic lipidosis fatty liver disease DOID:9477 An artery disease characterized by a blockage of the main artery of the lung or one of its branches by a substance that has travelled from elsewhere in the body, e.g. a blood clot. pulmonary embolism DOID:9744 A diabetes mellitus that results from the body's failure to produce insulin and has_material_basis_in autoimmune destruction of insulin-producing beta cells of the pancreas. MESH:D003922 OMIM:222100 IDDM insulin-dependent diabetes mellitus type I diabetes mellitus type 1 diabetes mellitus DOID:9970 An overnutrition that is characterized by excess body fat, traditionally defined as an elevated ratio of weight to height (specifically 30 kilograms per meter squared), has_material_basis_in a multifactorial etiology related to excess nutrition intake, decreased caloric utilization, and genetic susceptibility, and possibly medications and certain disorders of metabolism, endocrine function, and mental illness. obesity (disease) DRON:00014332 A recombinant humanized monoclonal antibody directed against the vascular endothelial growth factor (VEGF), a pro-angiogenic cytokine. Bevacizumab binds to VEGF and inhibits VEGF receptor binding, thereby preventing the growth and maintenance of tumor blood vessels. (https://www.ebi.ac.uk/ols/ontologies/ncit/terms?iri=http%3A%2F%2Fpurl.obolibrary.org%2Fobo%2FNCIT_C2039) CAS:216974-75-3 PMID:33547300 Bevacizumab HOIP_0040731 PMID:33547300 Hypoxia induces VEGF expression through activation of the Prolyl hydroxylases (PHD)-hypoxia-inducible factor (HIF)-1 pathway, which upregulates VEGF expression through transcription activation. VEGF is a potent vascular permeability factor that induces vascular leakiness in Covid-19-infected lung tissues, resulting in plasma extravasation and pulmonary edema, which further increases tissue hypoxia. Additionally, VEGF participates in lung inflammation. Bevacizumab plus standard care markedly improves the PaO2/FiO2 ratios at days 1 and 7. By day 28, 24 (92%) patients show improvement in oxygen-support status, 17 (65%) patients are discharged, and none show worsen oxygen-support status nor die. DRON:00019607 A recombinant, humanized IgG1 monoclonal antibody directed against the interleukin-6 receptor (IL-6R) with immunosuppressant activity. Tocilizumab targets and binds to both the soluble form of IL-6R (sIL-6R) and the membrane-bound form (mIL-6R), thereby blocking the binding of IL-6 to its receptor. This prevents IL-6-mediated signaling. Il-6, a pro-inflammatory cytokine that plays an important role in the regulation of the immune response, is overproduced in autoimmune disorders, certain types of cancers and possibly various other inflammatory conditions. (https://www.ebi.ac.uk/ols/ontologies/ncit/terms?iri=http%3A%2F%2Fpurl.obolibrary.org%2Fobo%2FNCIT_C84217) ATC:C1609165 CHEMBL:1237022 PMID:32325025 Wikipedia:Tocilizumab tocilizumab PMID:32325025 It is possible that the enhanced pro-inflammatory cytokines are induced by the IL-6 Amp. Considering that the anti-IL-6R antibody tocilizumab is an effective treatment for CRS in CAR-T cell therapies (Neelapu et al., 2018), researchers might want to consider drugs with a similar mechanism of action for CRS in COVID-19. DRON:00750805 PMID:34031531 siltuximab PMID:34031531 Our data suggest that a timely modulation of PTX3 by siltuximab represents a local effect of IL-6 inhibition in reducing inflammation in the lung bronchoalveolar lavage fluid [7, 8]. Moreover, modulation of IL-8 levels by siltuximab suggests an inhibition of systemic inflammation, which may prevent IL-8–mediated recruitment and activation of neutrophil DRON:00789755 A recombinant, human immunoglobulin (IgG) monoclonal antibody targeting the interleukin 6 receptor (IL-6R), with potential anti-inflammatory activity. Upon intravenous administration of sarilumab, this agent targets and binds to both soluble IL-6 receptor (sIL-6R) and membrane-bound IL-6 receptor (mIL-6R). This inhibits the binding of the pro-inflammatory cytokine IL-6 to the IL-6 receptor (IL-6R), which results in the blockade of the IL-6/IL-6R-mediated signal transduction pathway. This may inhibit IL-6/IL-6R-mediated inflammation. (https://www.ebi.ac.uk/ols/ontologies/ncit/terms?iri=http%3A%2F%2Fpurl.obolibrary.org%2Fobo%2FNCIT_C152302) PMID:33930329 PMID:33995419 sarilumab PMID:33930329 Tocilizumab and sarilumab are monoclonal antibodies that target the IL-6 receptor (IL-6R) and are approved for the treatment of the aforementioned IL-6-mediated conditions. Although most RCTs did not identify safety concerns with tocilizumab, surveillance for potentially detrimental effects, such as increased risk of infection, once the drug is used more widely should be heightened. Third, the extent to which the benefit observed with tocilizumab can be extended to sarilumab remains unknown. PMID:33995419 By analyzing clinical and serological variables associated with positive response to anti-cytokine therapies, we found that IL-1 and IL-6 inhibition improved long-term survival when initiated in the early phases of COVID-19 pneumonia before the establishment of severe ARDS (namely, PaO2/FiO2 ratio < 100 mmHg). The survival advantage offered by sarilumab and tocilizumab, in fact, was lost in patients with severe respiratory failure, and the efficacy of anakinra was markedly reduced although still proving superior to standard management. These findings demonstrate that the likelihood of response to IL-1 or IL-6 blocking strategies in patients with COVID-19 depends on the degree of respiratory impairment at the time of treatment administration and underscore the existence of a window of opportunity in which cytokine-blocking agents - as well as of more common anti-inflammatory therapies such as glucocorticoids and colchicine - might effectively counteract rampant inflammation in COVID-19. DRON:00831727 An orally bioavailable inhibitor of Janus kinases 1 and 2 (JAK1/2), with potential anti-inflammatory, immunomodulating and antineoplastic activities. Upon administration, baricitinib binds to JAK1/2, which inhibits JAK1/2 activation and leads to the inhibition of the JAK-signal transducers and activators of transcription (STAT) signaling pathway. This decreases the production of inflammatory cytokines and may prevent an inflammatory response. In addition, baricitinib may induce apoptosis and reduce proliferation of JAK1/2-expressing tumor cells. JAK kinases are intracellular enzymes involved in cytokine signaling, inflammation, immune function and hematopoiesis; they are also upregulated and/or mutated in various tumor cell types. (https://www.ebi.ac.uk/ols/ontologies/ncit/terms?iri=http%3A%2F%2Fpurl.obolibrary.org%2Fobo%2FNCIT_C127012) CAS:1187594-09-7 PMID:33510353 Baricitinib PMID:33510353 In the viral systems both edges and vertex cover were associated with acuteness of viral infections. In the JAK/STAT system already infected with coronavirus, maximum reduction in size was achieved with baricitinib. To conclude, algebraic and combinatorial invariant of a network may explain its biological behaviour. At least theoretically, baricitinib may be an attractive target for treatment of coronavirus infection. During the process of peer-review results from two clinical trials were published, which, similar to our hypothesized results, showed that baricitinib-treated patients with coronavirus related cytokine storm had a marked reduction in serum levels of several cytokines and rapid recovery in circulating T and B cell frequencies, and another trial reported that In patients with moderate to severe coronaviral pneumonia combination of baricitinib with corticosteroids was associated with greater pulmonary functional improvement compared to corticosteroids alone ENVO:01000373 Biological waste is waste containing mostly natural organic materials (remains of plants, animal excrement, biological sludge from waste-water treatment plants and so forth). Biological waste is waste containing mostly natural organic materials (remains of plants, animal excrement, biological sludge from waste-water treatment plants and so forth). biological waste material Biological waste is waste containing mostly natural organic materials (remains of plants, animal excrement, biological sludge from waste-water treatment plants and so forth). ISBN:9789211613865 ENVO:01000665 waste role ENVO:01001023 A process during which energy is emitted or transmitted in the form of waves or particles through space or a material medium. radiation GOCHE:22586 Substance with antioxidant role is a subtype of substance with role. This entity is participating in a oxidative stress response and playing an antioxidant role. substance with antioxidant role GOCHE:50906 Substance with role is a subtype of object. This entity is participating in a specific process and playing a role. In YAMATO ontology theory, an entity (continuant) playing a role in a specific context is called a role holder. substance with role GOCHE:52214 Substance with ligand role is a subtype of substance with role. This entity is participating in signaling and playing a ligand role. This entity is inferred from Description Logic. substance with ligand role GO:0000022 The cell cycle process in which the distance is lengthened between poles of the mitotic spindle. Mitotic spindle elongation begins during mitotic prophase and ends during mitotic anaphase B. meitotic spindle elongation GO:0000062 Interacting selectively and non-covalently with acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group. Interacting selectively and non-covalently with acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group. acyl-CoA or acyl binding fatty-acyl-CoA binding Interacting selectively and non-covalently with acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group. ISBN:0198506732 GO:0000070 The cell cycle process in which replicated homologous chromosomes are organized and then physically separated and apportioned to two sets during the mitotic cell cycle. Each replicated chromosome, composed of two sister chromatids, aligns at the cell equator, paired with its homologous partner. One homolog of each morphologic type goes into each of the resulting chromosome sets. mitotic sister chromatid segregation GO:0000075 A signaling process that controls cell cycle progression by monitoring the integrity of specific cell cycle events. A cell cycle checkpoint begins with detection of deficiencies or defects and ends with signal transduction. cell cycle checkpoint signaling GO:0000076 A signal transduction process that contributes to a DNA replication checkpoint, that prevents the initiation of nuclear division until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome. DNA replication checkpoint signal transduction involved in DNA replication checkpoint signal transduction resulting in cell cycle arrest DNA replication checkpoint signaling GO:0000077 A signal transduction process that contributes to a DNA damage checkpoint DNA damage checkpoint signal transduction involved in DNA damage checkpoint signal transduction resulting in cell cycle arrest DNA damage checkpoint signaling GO:0000122 Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. negative regulation of transcription by RNA polymerase II GO:0000139 The lipid bilayer surrounding any of the compartments of the Golgi apparatus. Golgi membrane GO:0000151 A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex. ubiquitin ligase complex GO:0000212 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a meiotic cell cycle. meiotic spindle organization GO:0000229 A chromosome found in the cytoplasm. cytoplasmic interphase chromosome cytoplasmic chromosome GO:0000235 Any of the spindle microtubules that radiate in all directions from the spindle poles and are thought to contribute to the forces that separate the poles and position them in relation to the rest of the cell. astral microtubule GO:0000242 A network of small fibers that surrounds the centrioles in cells; contains the microtubule nucleating activity of the centrosome. PCM pericentriolar material GO:0000266 The division of a mitochondrion within a cell to form two or more separate mitochondrial compartments. The division of a mitochondrion within a cell to form two or more separate mitochondrial compartments. mitochondrial proliferation mitochondrial division mitochondrial fission The division of a mitochondrion within a cell to form two or more separate mitochondrial compartments. PMID:11038192 GO:0000278 Progression through the phases of the mitotic cell cycle, the most common eukaryotic cell cycle, which canonically comprises four successive phases called G1, S, G2, and M and includes replication of the genome and the subsequent segregation of chromosomes into daughter cells. In some variant cell cycles nuclear replication or nuclear division may not be followed by cell division, or G1 and G2 phases may be absent. Wikipedia:Mitosis mitosis mitotic cell cycle GO:0000279 A cell cycle phase during which nuclear division occurs, and which is comprises the phases: prophase, metaphase, anaphase and telophase. Wikipedia:M_phase M phase GO:0000280 The division of a cell nucleus into two nuclei, with DNA and other nuclear contents distributed between the daughter nuclei. nuclear division GO:0000281 The division of the cytoplasm and the plasma membrane of a cell and its partitioning into two daughter cells. mitotic cytokinesis GO:0000288 A major pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of ordered steps that includes poly(A) tail shortening and that can regulate mRNA stability. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay GO:0000307 Cyclin-dependent protein kinases (CDKs) are enzyme complexes that contain a kinase catalytic subunit associated with a regulatory cyclin partner. cyclin-dependent protein kinase holoenzyme complex GO:0000422 The autophagic process in which mitochondria are delivered to the vacuole and degraded in response to changing cellular conditions. Wikipedia:Mitophagy mitochondrion autophagy autophagy of mitochondrion GO:0000423 Degradation of a mitochondrion by macroautophagy. PMID:22406072 mitohagy GO:0000425 The selective autophagy process in which a peroxisome is degraded by macroautophagy. The selective autophagy process in which a peroxisome is degraded by macroautophagy. pexophagy The selective autophagy process in which a peroxisome is degraded by macroautophagy. PMID:12914914 PMID:16973210 GO:0000723 Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins, the length of telomeric DNA and the replication and repair of the DNA. These processes includes those that shorten, lengthen, replicate and repair the telomeric DNA sequences. WikiPathway: WP1928 telomere maintenance GO:0000724 The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule. double-strand break repair via homologous recombination GO:0000768 The formation of a syncytium, a mass of cytoplasm containing several nuclei enclosed within a single plasma membrane, by the fusion of the plasma membranes of two or more individual cells. syncytium formation by plasma membrane fusion GO:0000781 The end of a linear chromosome, required for the integrity and maintenance of the end. A chromosome telomere usually includes a region of telomerase-encoded repeats the length of which rarely exceeds 20 bp each and that permits the formation of a telomeric loop (T-loop). The telomeric repeat region is usually preceded by a sub-telomeric region that is gene-poor but rich in repetitive elements. Some telomeres only consist of the latter part (for eg. D. melanogaster telomeres). chromosome, telomeric region GO:0000785 The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. NIF_Subcellular:sao1615953555 chromosome scaffold cytoplasmic chromatin nuclear chromatin chromatin GO:0000792 A compact and highly condensed form of chromatin that is refractory to transcription. NIF_Subcellular:sao581845896 Wikipedia:Heterochromatin nuclear heterochromatin transcriptionally inactive chromatin transcriptionally silent chromatin heterochromatin GO:0000819 The cell cycle process in which sister chromatids are organized and then physically separated and apportioned to two or more sets. sister chromatid segregation GO:0000910 A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells. cytokinesis GO:0000922 Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules. spindle pole GO:0001046 core promoter sequence-specific DNA binding Binding to a sequence of DNA that is part of a core promoter region. The core promoter is composed of the transcription start site and binding sites for the RNA polymerase and the basal transcription machinery. The transcribed region might be described as a gene, cistron, or operon. core promoter sequence-specific DNA binding GO:0001660 The heat generation process that results in a rise in body temperature above the normal, often as a response to infection. fever generation GO:0001666 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. response to hypoxia GO:0001676 The chemical reactions and pathways involving long-chain fatty acids, A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. long-chain fatty acid metabolism long-chain fatty acid metabolic process GO:0001708 The process involved in the specification of cell identity. Once specification has taken place, a cell will be committed to differentiate down a specific pathway if left in its normal environment. cell fate specification GO:0001709 A process involved in cell fate commitment. Once determination has taken place, a cell becomes committed to differentiate down a particular pathway regardless of its environment. cell fate determination GO:0001732 Joining of the large subunit, with release of IF2/eIF2 and IF3/eIF3. This leaves the functional ribosome at the AUG, with the methionyl/formyl-methionyl-tRNA positioned at the P site. formation of cytoplasmic translation initiation complex GO:0001775 A change in the morphology or behavior of a cell resulting from exposure to an activating factor such as a cellular or soluble ligand. cell activation GO:0001781 Any apoptotic process in a neutrophil, any of the immature or mature forms of a granular leukocyte that in its mature form has a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. neutrophil apoptotic process GO:0001787 The expansion of a natural killer cell population by cell division. natural killer cell proliferation GO:0001788 Cytolysis of target cells by natural killer cells, eosinophils, neutrophils, monocytes, or macrophages following engagement of antibodies bound to the target cells by Fc receptors on the effector cells. antibody-dependent cellular cytotoxicity GO:0001816 cytokine production The appearance of a cytokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Note that this term is intended for use when a gene product is seen to cause apparent increases in intracellular or extracellular cytokine levels, without specific regard as to whether the increase is due to increased biosynthesis, increased secretion of preexisting cytokine molecules, or increased conversion from precursor molecules. cytokine production GO:0001818 Any process that stops, prevents, or reduces the rate of production of a cytokine. negative regulation of cytokine production GO:0001820 The regulated release of serotonin by a cell. Serotonin (5-hydroxytryptamine, or 5-HT) is a monoamine synthesised in serotonergic neurons in the central nervous system, enterochromaffin cells in the gastrointestinal tract and some immune system cells. serotonin secretion GO:0001821 The regulated release of histamine by a cell or tissue. It is formed by decarboxylation of histidine and it acts through receptors in smooth muscle and in secretory systems. histamine secretion GO:0001836 The process that results in the movement of cytochrome c from the mitochondrial intermembrane space into the cytosol, which is part of the apoptotic signaling pathway and leads to caspase activation. The process that results in the movement of cytochrome c from the mitochondrial intermembrane space into the cytosol, which is part of the apoptotic signaling pathway and leads to caspase activation. PMID:20850011 http://purl.obolibrary.org/obo/HINO_0007325 release of cytochrome c from mitochondria The process that results in the movement of cytochrome c from the mitochondrial intermembrane space into the cytosol, which is part of the apoptotic signaling pathway and leads to caspase activation. ISBN:0721639976 PMID:12925707 PMID:9560217 PMID:20850011 The release of cytochrome c from mitochondria is a central event in the signaling phase of the apoptotic process, and it is often used by researchers to monitor this type of cell death. Any event that induces apoptosis will at some point induce the release of cytochrome c from mitochondria. Therefore, this term should only be used to annotate gene products that are directly involved in this process. GO:0001837 A transition where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell. epithelial to mesenchymal transition GO:0001845 The process that results in the fusion of a phagosome, a vesicle formed by phagocytosis, with a lysosome. late phagosome biosynthesis late phagosome formation phagolysosome formation phagolysosome assembly GO:0001865 The process in which a precursor cell type acquires the specialized features of a NK T cell. Note that NK T cells are a distinct lineage of T cells expressing natural killer cell markers and having T cell receptors characterized by the usage of a restricted repertoire of variable region gene segments. Note that immunologists typically use the word 'development' to refer to cells of B or T cell lineages undergoing the process that GO describes as 'cell differentiation'. NK T cell differentiation GO:0001867 Any process involved in the activation of any of the steps of the lectin pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. complement activation, lectin pathway GO:0001905 The activation of the membrane attack complex components of the complement cascade which can result in death of a target cell through cytolysis. activation of membrane attack complex GO:0001909 The directed killing of a target cell by a leukocyte. leukocyte mediated cytotoxicity GO:0001913 The directed killing of a target cell by a T cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. T cell mediated cytotoxicity GO:0001939 The pronucleus originating from the ovum that is being fertilized. female pronucleus GO:0001940 The pronucleus originating from the spermatozoa that was involved in fertilization. male pronucleus GO:0002021 The physiological process in which dietary excess is sensed by the central nervous system, resulting in a reduction in food intake and increased energy expenditure. response to dietary excess GO:0002040 The extension of new blood vessels from existing vessels into avascular tissues, this process includes the specialization of endothelial cells into leading tip and stalk cells, proliferation and migration of the endothelial cells and cell adhesion resulting in angiogenic sprout fusion or lumen formation. sprouting angiogenesis GO:0002041 Intussusceptive angiogenesis is a subtype of biological structure formation: A process that constructs an alternate blood vessels. Intussusceptive angiogenesis also known as splitting angiogenesis, is a type of angiogenesis, the process whereby a new blood vessel is created. (https://en.wikipedia.org/wiki/Intussusceptive_angiogenesis) 重積血管新生 Intussusceptive angiogenesis GO:0002221 Any series of molecular signals generated as a consequence of a pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species, or damage-associated molecular pattern (DAMPs), endogenous molecules released from damaged cells. pattern recognition receptor signaling pathway GO:0002224 Any series of molecular signals generated as a consequence of binding to a toll-like receptor. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response. toll-like receptor signaling pathway TLR signaling pathway GO:0002228 The promotion of an immune response by natural killer cells through direct recognition of target cells or through the release of cytokines. NK cell mediated immunity natural killer cell mediated immunity GO:0002250 adaptive immune response An immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory). adaptive immune response GO:0002280 The change in morphology and behavior of a monocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. monocyte activation involved in immune response GO:0002281 A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. macrophage activation involved in immune response GO:0002283 The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. neutrophil activation involved in immune response GO:0002286 The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific, leading to the initiation or perpetuation of an immune response. T cell activation involved in immune response GO:0002291 The change in morphology and behavior of a mature or immature T cell resulting from exposure to an antigen for which its T cell receptor is specific bound to an MHC molecule on an antigen presenting cell, leading to the initiation or perpetuation of an immune response. T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell GO:0002312 The change in morphology and behavior of a mature or immature B cell during an immune response, resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. B cell activation involved in immune response GO:0002319 The process in which a B cell acquires the specialized features of a memory B cell. Memory B cells are cells that can respond rapidly to antigen re-exposure by production of high-affinity antibody. memory B cell differentiation GO:0002347 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a tumor cell response to tumor cell proliferation GO:0002351 The synthesis or release of serotonin following a stimulus as part of an inflammatory response, resulting in an increase in its intracellular or extracellular levels. serotonin production involved in inflammatory response GO:0002353 A series of reactions that takes place outside the cell occurring in response to tissue damage and initiated within blood plasma by the action of activated Factor XII (Hageman Factor) on prekallikrein to convert it to plasma kallikrein, and the subsequent reaction of plasma kallikrein with high molecular weight kininogen. The ultimate product of the plasma kallikrein-kinin cascade is bradykinin, an agent known to induce smooth muscle contraction, vasoconstriction, and increased vascular permeability. カリクレイン-キニン系 plasma kallikrein-kinin cascade GO:0002366 A change in morphology and behavior of a leukocyte resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. leukocyte activation involved in immune response GO:0002367 cytokine production involved in immune response The appearance of a cytokine due to biosynthesis or secretion following a cellular stimulus contributing to an immune response, resulting in an increase in its intracellular or extracellular levels. cytokine production involved in immune response GO:0002369 Any process that contributes to cytokine production by a T cell. T cell cytokine production GO:0002370 Any process that contributes to cytokine production by a natural killer cell. natural killer cell cytokine production GO:0002377 The appearance of immunoglobulin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. antibody production immunoglobulin production GO:0002384 An immune response taking place in the liver. hepatic immune response GO:0002391 The synthesis or release of platelet activating factor following a stimulus as part of an inflammatory response, resulting in an increase in its intracellular or extracellular levels. platelet activating factor production involved in inflammatory response GO:0002418 An immune system process that functions in the response of an organism to a tumor cell. immune response to tumor cell GO:0002426 The synthesis and release of immunoglobulin in the mucosal tissue. immunoglobulin production in mucosal tissue GO:0002440 The synthesis or release of any molecular mediator of the immune response, resulting in an increase in its intracellular or extracellular levels. production of molecular mediator of immune response GO:0002441 The regulated release of histamine by a cell as part of an inflammatory response. histamine secretion involved in inflammatory response GO:0002446 Any process involved in the carrying out of an immune response by a neutrophil. neutrophil mediated immunity GO:0002456 Any process involved in the carrying out of an immune response by a T cell. T cell response T cell mediated immunity GO:0002472 The process in which a macrophage expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. macrophage antigen processing and presentation GO:0002504 The process in which an antigen-presenting cell expresses antigen (peptide or polysaccharide) on its cell surface in association with an MHC class II protein complex. antigen processing and presentation of exogenous peptide antigen via MHC class II GO:0002507 A process that directly activates any of the steps required for tolerance, a physiologic state in which the immune system does not react destructively against the components of an organism that harbors it or against antigens that are introduced to it. tolerance induction GO:0002521 The process in which a relatively unspecialized hemopoietic precursor cell acquires the specialized features of a leukocyte. A leukocyte is an achromatic cell of the myeloid or lymphoid lineages capable of ameboid movement, found in blood or other tissue. leucocyte differentiation leukocyte differentiation GO:0002532 The synthesis or release of any molecular mediator of the inflammatory response following an inflammatory stimulus, resulting in an increase in its intracellular or extracellular levels. Wikipedia:Inflammation production of molecular mediator involved in inflammatory response Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. GO:0002533 The regulated release of lysosomal enzymes by a cell as part of an inflammatory response. lysosomal enzyme secretion involved in inflammatory response GO:0002534 The synthesis or release of a cytokine following a inflammatory stimulus as part of an inflammatory response, resulting in an increase in its intracellular or extracellular levels. GO:0002534 cytokine production involved in inflammatory response GO:0002536 A phase of elevated metabolic activity, during which oxygen consumption increases following a stimulus as part of an inflammatory response; this leads to the production, by an NADH dependent system, of hydrogen peroxide (H2O2), superoxide anions and hydroxyl radicals, resulting in an increase in their intracellular or extracellular levels. respiratory burst involved in inflammatory response GO:0002538 The synthesis or release of products of arachidonic acid metabolism following a stimulus as part of an inflammatory response, resulting in an increase in their intracellular or extracellular levels. arachidonic acid metabolite production involved in inflammatory response GO:0002548 The movement of a monocyte in response to an external stimulus. monocyte chemotaxis GO:0002576 The regulated exocytosis of secretory granules containing preformed mediators such as histamine and serotonin by a platelet. platelet degranulation GO:0002714 Any process that activates or increases the frequency, rate, or extent of B cell mediated immunity. positive regulation of B cell mediated immunity GO:0002747 Antigen processing and presentation which is initiated by uptake of antigen via phagocytosis. antigen processing and presentation following phagocytosis GO:0002753 Any series of molecular signals generated as a consequence of a cytoplasmic pattern recognition receptor (PRR) binding to one of its physiological ligands. PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species. cytoplasmic pattern recognition receptor signaling pathway GO:0002819 Any process that modulates the frequency, rate, or extent of an adaptive immune response. regulation of adaptive immune response GO:0002821 Any process that activates or increases the frequency, rate, or extent of an adaptive immune response. up-regulation of adaptive immune response positive regulation of T-helper 1 type immune response GO:0002825 Any process that modulates the frequency, rate, or extent of a T-helper 1 type immune response. regulation of T-helper 1 type immune response GO:0002870 Any process contributing to anergy in T cells, a state of functional inactivation which is part of T cell tolerance induction. T cell anergy GO:0003094 The process in which plasma is filtered through the glomerular membrane which consists of capillary endothelial cells, the basement membrane, and epithelial cells. The glomerular filtrate is the same as plasma except it has no significant amount of protein. glomerular filtration GO:0003674 A molecular process that can be carried out by the action of a single macromolecular machine, usually via direct physical interactions with other molecular entities. Function in this sense denotes an action, or activity, that a gene product (or a complex) performs. These actions are described from two distinct but related perspectives: (1) biochemical activity, and (2) role as a component in a larger system/process. Note that, in addition to forming the root of the molecular function ontology, this term is recommended for use for the annotation of gene products whose molecular function is unknown. When this term is used for annotation, it indicates that no information was available about the molecular function of the gene product annotated as of the date the annotation was made; the evidence code 'no data' (ND), is used to indicate this. Despite its name, this is not a type of 'function' in the sense typically defined by upper ontologies such as Basic Formal Ontology (BFO). It is instead a BFO:process carried out by a single gene product or complex. molecular function GO:0003677 Process of any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). GO:0003677 DNA binding GO:0003824 GO:0003964 GO:00042181 The chemical reactions and pathways resulting in the formation of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups. ketone anabolism ketone biosynthesis ketone formation ketone synthesis ketone biosynthetic process GO:00042770 A cascade of processes induced by the detection of DNA damage within a cell. DNA damage response, signal transduction signal transduction in response to DNA damage GO:0005488 The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. In the definition of GO:0005488 binding is a subtype of Molecular function. binding (with molecule) GO:0005504 Interacting selectively and non-covalently with fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. GO:0005504 fatty acid binding GO:0005515 Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). GO:0005515 protein amino acid binding protein binding GO:0005543 Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester. GO:0005543 phospholipid binding GO:0005575 cellular component The part of a cell or its extracellular environment in which a gene product is located. A gene product may be located in one or more parts of a cell and its location may be as specific as a particular macromolecular complex, that is, a stable, persistent association of macromolecules that function together. cellular_component GO:0005576 The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. Wikipedia:Extracellular extracellular Note that this term is intended to annotate gene products that are not attached to the cell surface. For gene products from multicellular organisms which are secreted from a cell but retained within the organism (i.e. released into the interstitial fluid or blood), consider the cellular component term 'extracellular space ; GO:0005615'. extracellular region GO:0005577 A highly soluble, elongated protein complex found in blood plasma and involved in clot formation. It is converted into fibrin monomer by the action of thrombin. In the mouse, fibrinogen is a hexamer, 46 nm long and 9 nm maximal diameter, containing two sets of nonidentical chains (alpha, beta, and gamma) linked together by disulfide bonds. fibrinogen fibrinogen complex GO:0005579 A protein complex produced by sequentially activated components of the complement cascade inserted into a target cell membrane and forming a pore leading to cell lysis via ion and water flow. membrane attack complex C5bからC9で構成されるタンパク質複合体．病原体表面に親水性孔を開けて溶解させる． https://www.ncbi.nlm.nih.gov/books/NBK27100/ MAC membrane attack complex GO:0005615 That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. NIF_Subcellular:sao1425028079 intercellular space Note that for multicellular organisms, the extracellular space refers to everything outside a cell, but still within the organism (excluding the extracellular matrix). Gene products from a multi-cellular organism that are secreted from a cell into the interstitial fluid or blood can therefore be annotated to this term. extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. ISBN:0198547684 GO:0005622 The living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm. The living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm. Wikipedia:Intracellular internal to cell protoplasm intracellular The living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm. ISBN:0198506732 GO:0005634 A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. NIF_Subcellular:sao1702920020 Wikipedia:Cell_nucleus cell nucleus nucleus GO:0005635 The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). Wikipedia:Nuclear_envelope nuclear envelope GO:0005638 Any of a group of intermediate-filament proteins that form the fibrous matrix on the inner surface of the nuclear envelope. They are classified as lamins A, B and C. type V intermediate filament lamin filament GO:0005652 The fibrous, electron-dense layer lying on the nucleoplasmic side of the inner membrane of a cell nucleus, composed of lamin filaments. The polypeptides of the lamina are thought to be concerned in the dissolution of the nuclear envelope and its re-formation during mitosis. The lamina is composed of lamin A and lamin C filaments cross-linked into an orthogonal lattice, which is attached via lamin B to the inner nuclear membrane through interactions with a lamin B receptor, an IFAP, in the membrane. NIF_Subcellular:sao1455996588 Wikipedia:Nuclear_lamina nuclear lamina GO:0005694 A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. Wikipedia:Chromosome chromatid Chromosomes include parts that are not part of the chromatin. Examples include the kinetochore. chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. ISBN:019857684 GO:0005737 All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. Wikipedia:Cytoplasm cytoplasm All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. ISBN:0198547684 GO:0005739 mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. NIF_Subcellular:sao1860313010 Wikipedia:Mitochondrion mitochondria mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. ISBN:0198506732 GO:0005741 The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope. NIF_Subcellular:sao1289741256 Wikipedia:Outer_mitochondrial_membrane mitochondrial outer membrane GO:0005743 The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. NIF_Subcellular:sao1371347282 Wikipedia:Inner_mitochondrial_membrane inner mitochondrial membrane mitochondrial inner membrane GO:0005747 A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. It contains about 25 different polypeptide subunits, including NADH dehydrogenase (ubiquinone), flavin mononucleotide and several different iron-sulfur clusters containing non-heme iron. The iron undergoes oxidation-reduction between Fe(II) and Fe(III), and catalyzes proton translocation linked to the oxidation of NADH by ubiquinone. A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. It contains about 25 different polypeptide subunits, including NADH dehydrogenase (ubiquinone), flavin mononucleotide and several different iron-sulfur clusters containing non-heme iron. The iron undergoes oxidation-reduction between Fe(II) and Fe(III), and catalyzes proton translocation linked to the oxidation of NADH by ubiquinone. mitochondrial respiratory chain complex I A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. It contains about 25 different polypeptide subunits, including NADH dehydrogenase (ubiquinone), flavin mononucleotide and several different iron-sulfur clusters containing non-heme iron. The iron undergoes oxidation-reduction between Fe(II) and Fe(III), and catalyzes proton translocation linked to the oxidation of NADH by ubiquinone. https://www.worldcat.org/search?q=bn%3A0198547684 GO:0005751 A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the 13 polypeptide subunits of cytochrome c oxidase, including cytochrome a and cytochrome a3. Catalyzes the oxidation of reduced cytochrome c by dioxygen (O2). A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the 13 polypeptide subunits of cytochrome c oxidase, including cytochrome a and cytochrome a3. Catalyzes the oxidation of reduced cytochrome c by dioxygen (O2). mitochondrial respiratory chain complex IV A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the 13 polypeptide subunits of cytochrome c oxidase, including cytochrome a and cytochrome a3. Catalyzes the oxidation of reduced cytochrome c by dioxygen (O2). https://www.worldcat.org/search?q=bn%3A0198547684 GO:0005764 A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. PMID:10751143 Wikipedia:Lysosome Another function of the ER in eucaryotic cells is to sequester Ca2+ from the cytosol. Cell lysosome A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. ISBN:0198506732 PMID:10751143 Lysosome-endosome fusion and lysosome biogenesis. lysosomes can fuse directly with late endosomes to form a hybrid organelle. This has a led to a hypothesis that dense core lysosomes are in essence storage granules for acid hydrolases and that, when the former fuse with late endosomes, a hybrid organelle for digestion of endocytosed macromolecules is created. Lysosomes are then re-formed from hybrid organelles by a process involving condensation of contents. GO:0005765 The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm. lysosomal membrane GO:0005768 A vacuole to which materials ingested by endocytosis are delivered. A vacuole to which materials ingested by endocytosis are delivered. NIF_Subcellular:sao1720343330 Wikipedia:Endosome endosome A vacuole to which materials ingested by endocytosis are delivered. ISBN:0198506732 PMID:19696797 GO:0005769 A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways. A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways. early endosome A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways. PMID:19696797 GO:0005770 A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center. late endosome GO:0005773 A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol. A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol. Wikipedia:Vacuole vacuole A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol. ISBN:0198506732 GO:0005776 A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the vacuole/lysosome for degradation as part of macroautophagy. A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the vacuole/lysosome for degradation as part of macroautophagy. autophagosome A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the vacuole/lysosome for degradation as part of macroautophagy. PMID:11099404 GO:0005777 A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. PMID:9302272 GO:0005783 The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). ISBN:0815332181 NIF_Subcellular:sao1036339110 Wikipedia:Endoplasmic_reticulum ER endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). ISBN:0198506732 ISBN:0815332181 The ER has a central role in lipid and protein biosynthesis. Its membrane is the site of production of all the transmembrane proteins and lipids for most of the cell's organelles, including the ER itself, the Golgi apparatus, lysosomes, endosomes, secretory vesicles, and the plasma membrane. Another function of the ER in eucaryotic cells is to sequester Ca2+ from the cytosol. GO:0005788 The volume enclosed by the membranes of the endoplasmic reticulum. ER cisterna ER lumen endoplasmic reticulum cisterna endoplasmic reticulum lumen GO:0005789 The lipid bilayer surrounding the endoplasmic reticulum. ER membrane endoplasmic reticulum membrane GO:0005790 The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER. The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER. ISBN:0815332181 NIF_Subcellular:sao710427438 Wikipedia:Endoplasmic_reticulum#Smooth_endoplasmic_reticulum The hepatocyte is a cell with an abundant smooth ER. smooth endoplasmic reticulum The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER. ISBN:0198506732 ISBN:0815332181 It is usually prominent in cells that specialize in lipid metabolism. Cells that synthesize steroid hormones from cholesterol, for example, have an expanded smooth ER compartment to accommodate the enzymes needed to make cholesterol and to modify it to form the hormones. It is the principal site of production of lipoprotein particles, which carry lipids via the bloodstream to other parts of the body. The enzymes that synthesize the lipid components of lipoproteins are located in the membrane of the smooth ER, which also contains enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and various harmful compounds produced by metabolism. GO:0005791 The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae. The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae. NIF_Subcellular:sao1881364067; Wikipedia:Endoplasmic_reticulum#Rough_endoplasmic_reticulum RER rough ER rough endoplasmic reticulum The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae. ISBN:0198506732 GO:0005794 A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions. A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions. NIF_Subcellular:sao451912436 Wikipedia:Golgi_apparatus Golgi complex Note that the Golgi apparatus can be located in various places in the cytoplasm. In plants and lower animal cells, the Golgi apparatus exists as many copies of discrete stacks dispersed throughout the cytoplasm, while the Golgi apparatus of interphase mammalian cells is a juxtanuclear, often pericentriolar reticulum, where the discrete Golgi stacks are stitched together to form a compact and interconnected ribbon, sometimes called the Golgi ribbon. golgi apparatus A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions. ISBN:0198506732 GO:0005796 The volume enclosed by the membranes of any cisterna or subcompartment of the Golgi apparatus, including the cis- and trans-Golgi networks. Golgi lumen GO:0005813 A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. centrosome GO:0005814 A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle. centriole GO:0005815 An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides. An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides. Wikipedia:Microtubule_organizing_center MOC microtubule organising centre microtubule organizing center An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides. ISBN:0815316194 PMID:17072892 PMID:17245416 GO:0005819 The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart. Wikipedia:Spindle_apparatus spindle GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. NIF_Subcellular:sao101633890 Wikipedia:Cytosol cytosol GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. NIF_Subcellular:sao1429207766 Wikipedia:Ribosome free ribosome free ribosome membrane bound ribosome membrane bound ribosome ribosomal RNA ribosome An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. ISBN:0198506732 free ribosome NIF_Subcellular:sao1139385046 membrane bound ribosome NIF_Subcellular:sao1291545653 GO:0005856 Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. Wikipedia:Cytoskeleton cytoskeleton Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. ISBN:0198547684 PMID:16959967 GO:0005874 Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. Wikipedia:Microtubule microtubuli microtubulus microtubule GO:0005876 Any microtubule that is part of a mitotic or meiotic spindle; anchored at one spindle pole. spindle microtubule GO:0005884 A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane. FMA:63850 Wikipedia:Actin microfilament actin filament GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins NIF_Subcellular:sao1663586795 Wikipedia:Cell_membrane cell membrane cellular membrane cytoplasmic membrane plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins ISBN:0716731363 GO:0005938 The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins. cell cortex GO:0005942 A protein complex capable of phosphatidylinositol 3-kinase activity and containing subunits of any phosphatidylinositol 3-kinase (PI3K) enzyme. These complexes are divided in three classes (called I, II and III) that differ for their presence across taxonomic groups and for the type of their constituents. Catalytic subunits of phosphatidylinositol 3-kinase enzymes are present in all 3 classes; regulatory subunits of phosphatidylinositol 3-kinase enzymes are present in classes I and III; adaptor proteins have been observed in class II complexes and may be present in other classes too. phosphatidylinositol 3-kinase complex GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule. Wikipedia:Carbohydrate_metabolism carbohydrate metabolic process GO:0005977 The chemical reactions and pathways involving glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues in alpha-(1->4) glycosidic linkage, joined together by alpha-(1->6) glycosidic linkages. glycogen metabolic process GO:0005978 The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. Reactome:REACT_1736 glycogen anabolism glycogen biosynthesis glycogen formation glycogen synthesis glycogen biosynthetic process The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. ISBN:0198506732 Reactome:REACT_1736 Glycogen synthesis, Homo sapiens GO:0005980 The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. Reactome:REACT_1008 glycogen breakdown glycogen catabolism glycogen degradation glycogenolysis glycogen catabolic process The chemical reactions and pathways resulting in the breakdown of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. ISBN:0198506732 Reactome:REACT_1008 Glycogen breakdown (glycogenolysis), Homo sapiens GO:0006006 The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides. glucose metabolic process GO:0006066 The chemical reactions and pathways involving alcohols, any of a class of compounds containing one or more hydroxyl groups attached to a saturated carbon atom. The chemical reactions and pathways involving alcohols, any of a class of compounds containing one or more hydroxyl groups attached to a saturated carbon atom. alcohol metabolism alcohol metabolic process The chemical reactions and pathways involving alcohols, any of a class of compounds containing one or more hydroxyl groups attached to a saturated carbon atom. CHEBI:30879 ISBN:0198506732 GO:0006091 The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances. generation of precursor metabolites and energy GO:0006094 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. Reactome:R-HSA-70263 glucose biosynthesis glucose biosynthetic process gluconeogenesis Reactome:R-HSA-70263 Gluconeogenesis, Homo sapiens GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. glycolysis glycolytic process GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. Reactome: R-HSA-71403.2 Krebs cycle TCA cycle Wikipedia:Tricarboxylic_acid_cycle citric acid cycle tricarboxylic acid cycle GO:0006109 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving carbohydrates. regulation of carbohydrate metabolism regulation of carbohydrate metabolic process GO:0006119 The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis. The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis. respiratory-chain phosphorylation oxidative phosphorylation The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis. ISBN:0198506732 ISBN:0471331309 GO:0006120 The transfer of electrons from NADH to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex I. The transfer of electrons from NADH to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex I. oxidative phosphorylation, NADH to ubiquinone complex I (NADH to ubiquinone) mitochondrial electron transport, NADH to ubiquinone The transfer of electrons from NADH to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex I. ISBN:0716731363 GO:0006121 The transfer of electrons from succinate to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex II. The transfer of electrons from succinate to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex II. mitochondrial electron transport, succinate to coenzyme Q complex II (succinate to ubiquinone) oxidative phosphorylation, succinate to ubiquinone mitochondrial electron transport, succinate to ubiquinone The transfer of electrons from succinate to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex II. ISBN:0716731363 GO:0006122 The transfer of electrons from ubiquinol to cytochrome c that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex III. The transfer of electrons from ubiquinol to cytochrome c that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex III. complex III (ubiquinone to cytochrome c) mitochondrial electron transport, ubiquinol to cytochrome c The transfer of electrons from ubiquinol to cytochrome c that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex III. ISBN:0716731363 GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. DNA replication GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. PMID:11563486 GO:0006284 In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Wikipedia:Base_excision_repair base-excision repair GO:0006302 The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. PMID:23230272 double-strand break repair PMID:23230272 Herein, we describe a direct link between rapid and short-lived poly(ADP-ribose) (PAR) polymerase 1 (PARP1) activation and PARylation at DNA damage sites, PAR-dependent recruitment of the BAL1 macrodomain-containing protein and its partner E3 ligase, local BBAP-mediated ubiquitylation, and subsequent recruitment of the checkpoint mediators 53BP1 and BRCA1. The PARP1-dependent localization of BAL1-BBAP functionally limits both early and delayed DNA damage and enhances cellular viability independent of ATM, MDC1, and RNF8. These data establish that BAL1 and BBAP are bona fide members of a DNA damage response pathway and are directly associated with PARP1 activation, BRCA1 recruitment, and double-strand break repair. GO:0006303 The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear. double-strand break repair via nonhomologous end joining GO:0006305 The addition of alkyl groups to many positions on all four bases of DNA. Alkylating agents can also modify the bases of incoming nucleotides in the course of DNA synthesis. DNA alkylation GO:0006306 The covalent transfer of a methyl group to either N-6 of adenine or C-5 or N-4 of cytosine. DNA methylation GO:0006308 The cellular DNA metabolic process resulting in the breakdown of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one. DNA catabolic process GO:0006309 The cleavage of DNA during apoptosis, which usually occurs in two stages: cleavage into fragments of about 50 kbp followed by cleavage between nucleosomes to yield 200 bp fragments. PMID:15723341 Apoptosis induced DNA fragmentation DNA fragmentation in response to apoptotic signals is achieved through the activity of apoptotic nucleases. In human, these include DNA fragmentation factor (DFF) or caspase-activated DNase (CAD) and endonuclease G (Endo G) (reviewed in PMID:15723341). Caution is needed when apoptotic DNA laddering assays show presence of fragmented DNA. A positive assay may simply reflect the end point of a whole apoptotic process. Unless clear experimental evidence is available to show that a gene product is directly involved in fragmenting DNA, please do not annotate to GO:0006309 'apoptotic DNA fragmentation' and consider annotating instead to a more upstream process such as, e.g., GO:0042981 'regulation of apoptotic process', GO:0006915 'apoptotic process', GO:0097190 'apoptotic signaling pathway'. Also, note that gene products involved in compartmentalization of apoptotic nucleases and in activation or repression of their enzymatic activity should be annotated to the regulation term GO:1902510 'regulation of apoptotic DNA fragmentation' or to one of its children (see PMID:15723341). apoptotic DNA fragmentation GO:0006338 Dynamic structural changes to eukaryotic chromatin occurring throughout the cell division cycle. These changes range from the local changes necessary for transcriptional regulation to global changes necessary for chromosome segregation. chromatin remodeling GO:0006351 The cellular synthesis of RNA on a template of DNA. GO:0006351 http://purl.obolibrary.org/obo/IEV_0000183 DNA-dependent transcription cellular transcription, DNA-dependent transcription, DNA-templated GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. regulation of cellular transcription, DNA-dependent regulation of transcription, DNA-templated GO:0006366 The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs). transcription by RNA polymerase II GO:0006379 Any process in which a pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner. mRNA cleavage GO:0006401 The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. RNA catabolic process GO:0006402 The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes. mRNA catabolic process GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. Wikipedia:Translation_(genetics) translation GO:0006417 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. regulation of protein anabolism regulation of protein biosynthesis regulation of protein formation regulation of protein synthesis regulation of translation GO:0006457 The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. PMID:15459659 PMID:15519848 Reactome:R-HSA-391251 Wikipedia:Protein_folding Due to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and associate with proteins in their non-native state and facilitate their folding by stabilizing the conformation of productive folding intermediates. Chaperones that take part broadly in de novo protein folding, such as the Hsp70s and the chaperonins, facilitate the folding process through cycles of substrate binding and release regulated by their ATPase activity (see Young et al., 2004; Spiess et al., 2004; Bigotti and Clarke, 2008). Due to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and associate with proteins in their non-native state and facilitate their folding by stabilizing the conformation of productive folding intermediates. Chaperones that take part broadly in de novo protein folding, such as the Hsp70s and the chaperonins, facilitate the folding process through cycles of substrate binding and release regulated by their ATPase activity (see Young et al., 2004; Spiess et al., 2004; Bigotti and Clarke, 2008). protein folding Due to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and associate with proteins in their non-native state and facilitate their folding by stabilizing the conformation of productive folding intermediates. Chaperones that take part broadly in de novo protein folding, such as the Hsp70s and the chaperonins, facilitate the folding process through cycles of substrate binding and release regulated by their ATPase activity (see Young et al., 2004; Spiess et al., 2004; Bigotti and Clarke, 2008). R-HSA-391251 GO:0006461 The aggregation, arrangement and bonding together of a set of components to form a protein complex. protein complex formation protein complex assembly GO:0006468 The process of introducing a phosphate group on to a protein. protein phosphorylation GO:0006473 The addition of an acetyl group to a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid. protein acetylation GO:0006476 The removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid. protein deacetylation GO:0006486 A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. protein glycosylation GO:0006497 The covalent attachment of lipid groups to an amino acid in a protein. lipid:protein modification protein lipidation GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. Wikipedia:Proteolysis This term was intentionally placed under 'protein metabolic process ; GO:0019538' rather than 'protein catabolic process ; GO:0030163' to cover all processes centered on breaking peptide bonds, including those involved in protein processing. proteolysis GO:0006511 The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein. ubiquitin-dependent protein catabolic process GO:0006517 The removal of sugar residues from a glycosylated protein. protein deglycosylation GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells. amino acid and derivative metabolism amino acid metabolic process cellular amino acid and derivative metabolic process cellular amino acid metabolism cellular amino acid metabolic process GO:0006555 The chemical reactions and pathways involving methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. methionine metabolism methionine metabolic process GO:0006556 The chemical reactions and pathways resulting in the formation of S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism. S-adenosylmethionine biosynthetic process GO:0006629 The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. lipid metabolism lipid metabolic process GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. Wikipedia:Fatty_acid_metabolism fatty acid metabolism fatty acid metabolic process The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. ISBN:0198547684 GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. MetaCyc:PWY-4381 Wikipedia:Fatty_acid_synthesis fatty acid anabolism fatty acid biosynthesis fatty acid formation fatty acid synthesis fatty acid biosynthetic process GO:0006635 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). fatty acid beta-oxidation A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). ISBN:0198506732 GO:0006644 The chemical reactions and pathways involving phospholipids, any lipid containing phosphoric acid as a mono- or diester. The chemical reactions and pathways involving phospholipids, any lipid containing phosphoric acid as a mono- or diester. phospholipid metabolism phospholipid metabolic process The chemical reactions and pathways involving phospholipids, any lipid containing phosphoric acid as a mono- or diester. ISBN:0198506732 GO:0006646 The chemical reactions and pathways resulting in the formation of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. The chemical reactions and pathways resulting in the formation of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. phosphatidylethanolamine anabolism phosphatidylethanolamine biosynthesis phosphatidylethanolamine formation phosphatidylethanolamine synthesis phosphatidylethanolamine biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. ISBN:0198506732 GO:0006649 The transfer of a phospholipid from its site of synthesis to the plasma membrane. phospholipid transfer to membrane GO:0006650 The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. glycerophospholipid metabolism phosphoglyceride metabolic process phosphoglyceride metabolism alpha-glycerophosphate pathway glycerophospholipid metabolic process The chemical reactions and pathways involving glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. ISBN:0198506732 GO:0006654 The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. phosphatidic acid anabolism phosphatidic acid biosynthesis phosphatidic acid formation phosphatidic acid synthesis phosphatidic acid biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. ISBN:0198506732 GO:0006655 The chemical reactions and pathways resulting in the formation of phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. The chemical reactions and pathways resulting in the formation of phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. phosphatidylglycerol anabolism phosphatidylglycerol biosynthesis phosphatidylglycerol formation phosphatidylglycerol synthesis phosphatidylglycerol biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. ISBN:0198506732 GO:0006656 The chemical reactions and pathways resulting in the formation of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. The chemical reactions and pathways resulting in the formation of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. phosphatidylcholine anabolism phosphatidylcholine biosynthesis phosphatidylcholine formation phosphatidylcholine synthesis phosphatidylcholine biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. ISBN:0198506732 GO:0006658 The chemical reactions and pathways involving phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. They are important constituents of cell membranes. The chemical reactions and pathways involving phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. They are important constituents of cell membranes. phosphatidylserine metabolism phosphatidylserine metabolic process The chemical reactions and pathways involving phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. They are important constituents of cell membranes. ISBN:0198506732 GO:0006659 The chemical reactions and pathways resulting in the formation of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. The chemical reactions and pathways resulting in the formation of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. phosphatidylserine anabolism phosphatidylserine biosyntheis phosphatidylserine biosynthesis phosphatidylserine formation phosphatidylserine synthesis phosphatidylserine biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. ISBN:0198506732 The chemical reactions and pathways resulting in the formation of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. ISBN:0198506732 GO:0006660 The chemical reactions and pathways resulting in the breakdown of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. The chemical reactions and pathways resulting in the breakdown of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. phosphatidylserine breakdown phosphatidylserine catabolism phosphatidylserine degradation phosphatidylserine catabolic process The chemical reactions and pathways resulting in the breakdown of phosphatidylserines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of L-serine. ISBN:0198506732 GO:0006661 The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. Phosphatidylinositol (PI) is synthesized when phosphatidic acid (PA) and cytidine triphosphate (CTP) are converted into cytidine diphosphate-diacylglycerol (CDP-DAG) followed by conversion into PI and cytidine monophosphate (CMP) (Stuhne-Sekalec et al 1986, Lykidis et al. 1997). http://purl.obolibrary.org/obo/HINO_0013926 PtdIns biosynthesis PtdIns biosynthetic process phosphatidylinositol anabolism phosphatidylinositol biosynthesis phosphatidylinositol formation phosphatidylinositol synthesis phosphoinositide biosynthesis phosphoinositide biosynthetic process phosphatidylinositol biosynthetic process The chemical reactions and pathways resulting in the formation of phosphatidylinositol, any glycophospholipid in which the sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. CHEBI:28874 ISBN:0198506732 GO:0006665 The chemical reactions and pathways involving sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid). sphingolipid metabolism sphingolipid metabolic process GO:0006684 The chemical reactions and pathways involving sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine, any of a class of phospholipids in which the amino group of sphingosine is in amide linkage with one of several fatty acids, while the terminal hydroxyl group of sphingosine is esterified to phosphorylcholine. The chemical reactions and pathways involving sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine, any of a class of phospholipids in which the amino group of sphingosine is in amide linkage with one of several fatty acids, while the terminal hydroxyl group of sphingosine is esterified to phosphorylcholine. sphingomyelin metabolism sphingomyelin metabolic process The chemical reactions and pathways involving sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine, any of a class of phospholipids in which the amino group of sphingosine is in amide linkage with one of several fatty acids, while the terminal hydroxyl group of sphingosine is esterified to phosphorylcholine. ISBN:0198506732 GO:0006685 The chemical reactions and pathways resulting in the breakdown of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. The chemical reactions and pathways resulting in the breakdown of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. sphingomyelin breakdown sphingomyelin catabolism sphingomyelin degradation sphingomyelin catabolic process The chemical reactions and pathways resulting in the breakdown of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. ISBN:0198506732 GO:0006686 The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. sphingomyelin anabolism sphingomyelin biosynthesis sphingomyelin formation sphingomyelin synthesis sphingomyelin biosynthetic process The chemical reactions and pathways resulting in the formation of sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine. ISBN:0198506732 GO:0006695 The chemical reaction resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. GO:0006695 cholesterol biosynthetic process GO:0006699 The chemical reactions resulting in the formation of bile acids, any of a group of steroid carboxylic acids occurring in bile. bile acid biosynthetic process GO:0006711 The chemical reactions and pathways resulting in the breakdown of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants estrogen breakdown estrogen catabolism estrogen degradation estrogen catabolic process GO:0006735 A metabolic process that generates a pool of NADH by the reduction of NAD+. NAD (reduced) regeneration reduced NAD regeneration reduced nicotinamide adenine dinucleotide regeneration NADH regeneration GO:0006740 A metabolic process that generates a pool of NADPH by the reduction of NADP+. Reactome:R-HSA-389542 https://reactome.org/PathwayBrowser/#/R-HSA-389542 NADP (reduced) regeneration reduced NADP regeneration reduced nicotinamide adenine dinucleotide phosphate regeneration NADPH regeneration GO:0006749 The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle CHEBI:16856 ISBN:0198506732 glutathione metabolism glutathione metabolic process GO:0006750 The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins. GO:0006750 https://reactome.org/PathwayBrowser/#/R-HSA-174403 glutathione anabolism glutathione biosynthesis glutathione formation glutathione synthesis glutathione biosynthetic process GO:0006754 The chemical reaction resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0006754 ATP anabolism ATP biosynthesis ATP formation ATP synthesis ATP regeneration ATP biosynthetic process GO:0006783 The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors. heme anabolism heme biosynthesis heme formation heme synthesis heme biosynthetic process GO:0006793 The chemical reactions and pathways involving the nonmetallic element phosphorus or compounds that contain phosphorus, usually in the form of a phosphate group (PO4). phosphorus metabolic process phosphorus metabolic process GO:0006805 The chemical reactions and physical changes involving a xenobiotic compound, a compound foreign to living organisms. Used of chemical compounds, e. g. a xenobiotic chemical, such as a pesticide. (Gene Ontology) ISBN:0071769234 xenobiotic biotransformation Xenobiotic biotransformation is metabolic conversion of xenobiotic chemicals to more hydrophilic (water-soluble) compounds. xenobiotic metabolic process ISBN:0071769234 Biotransfomation to harmful products is called toxication/metabolic activation [casarett and doull's toxicology 8th ed.] GO:0006810 The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein. biological transport GO:0006811 The directed movement of charged atoms or small charged molecules into, out of, within or between cells. ion transport GO:0006813 The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. potassium ion transport GO:0006816 The directed movement of calcium ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. calcium ion transport GO:0006836 The directed movement of a neurotransmitter into, out of, within or between cells. Neurotransmitters are any chemical substance that is capable of transmitting (or inhibiting the transmission of) a nerve impulse from a neuron to another cell. neurotransmitter transport GO:0006869 The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. lipid transport The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. ISBN:0198506732 GO:0006897 A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle. A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle. Wikipedia:Endocytosis endocytosis A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle. ISBN:0198506732 ISBN:0716731363 GO:0006898 An endocytosis process in which cell surface receptors ensure specificity of transport. A specific receptor on the cell surface binds tightly to the extracellular macromolecule (the ligand) that it recognizes; the plasma-membrane region containing the receptor-ligand complex then undergoes endocytosis, forming a transport vesicle containing the receptor-ligand complex and excluding most other plasma-membrane proteins. Receptor-mediated endocytosis generally occurs via clathrin-coated pits and vesicles. Wikipedia:Receptor-mediated_endocytosis receptor mediated endocytosis receptor-mediated endocytosis GO:0006909 A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. Wikipedia:Phagocytosis phagocytosis A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. ISBN:0198506732 GO:0006910 The initial step in phagocytosis involving adhesion to bacteria, immune complexes and other particulate matter, or an apoptotic cell and based on recognition of factors such as bacterial cell wall components, opsonins like complement and antibody or protein receptors and lipids like phosphatidyl serine, and leading to intracellular signaling in the phagocytosing cell. recognition of phagocytosed substance by phagocytic cell Note that cell surface molecules involved in the direct binding of bacteria may be also annotated to the molecular function term 'bacterial cell surface binding ; GO:0051635'. Note that cell surface molecules involved in the direct binding to opsonins such as complement components or antibodies may be also annotated to the term 'opsonin binding ; GO:0001846'. phagocytosis, recognition GO:0006913 The directed movement of molecules between the nucleus and the cytoplasm. nucleocytoplasmic transport GO:0006914 The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation Wikipedia:Autophagy_(cellular) autophagy The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation ISBN:0198547684 PMID:11099404 PMID:9412464 GO:0006915 A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. IEV:0000070 (obsolete) Wikipedia:Apoptosis apoptotic cell death apoptotic programmed cell death programmed cell death by apoptosis apoptotic process GO:0006925 Any apoptotic process in an inflammatory cell, any cell participating in the inflammatory response to a foreign substance e.g. neutrophil, macrophage. inflammatory cell apoptotic process GO:0006928 Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another. cell locomotion cell movement movement of a cell cell motility GO:0006939 A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. smooth muscle contraction GO:0006950 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in organismal or cellular homeostasis, usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). response to stress GO:0006954 Inflammatory response is a subtype of changing material: The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. inflammation inflammatory response HOIP_0000192 GO:0006955 Any immune system process that functions in the calibrated response of an organism to a potential internal or invasive threat. immune response GO:0006956 Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway. complement activation GO:0006957 Any process involved in the activation of any of the steps of the alternative pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. complement activation, alternative pathway GO:0006958 Any process involved in the activation of any of the steps of the classical pathway of the complement cascade which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes. complement activation, classical pathway GO:0006959 An immune response mediated through a body fluid. humoral immune response GO:0006974 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. cellular response to DNA damage stimulus DNA damage response GO:0006978 A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, resulting in the induction of the transcription of p21 (also known as WAF1, CIP1 and SDI1) or any equivalent protein, in response to the detection of DNA damage. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. PMID:121115731 GO:0006996 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an organelle within a cell. An organelle is an organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. organelle organisation organelle organization GO:0007004 The maintenance of proper telomeric length by the addition of telomeric repeats by telomerase. telomere maintenance via telomerase GO:0007005 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components. mitochondrion organization GO:0007010 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures. cytoskeleton organisation cytoskeleton organization GO:0007015 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. actin filament organization GO:0007028 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the cytoplasm. The cytoplasm is all of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. cytoplasm organisation cytoplasm organization GO:0007033 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a vacuole. vacuole organization GO:0007041 The directed movement of substances into, out of or within a lysosome. lysosomal transport GO:0007049 The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division. cell cycle GO:0007052 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle. mitotic spindle organization GO:0007059 The process in which genetic material, in the form of chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. In eukaryotes, chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles. chromosome segregation GO:0007077 The mitotic cell cycle process in which the controlled partial or complete breakdown of the nuclear membranes during occurs during mitosis. NEB mitotic nuclear membrane disassembly HOIP_0050072 GO:0007079 The cell cycle process in which the directed movement of chromosomes from the center of the spindle towards the spindle poles occurs. This mediates by the shortening of microtubules attached to the chromosomes, during mitosis. mitotic chromosome movement towards spindle pole GO:0007080 The cell cycle process in which chromosomes are aligned at the metaphase plate, a plane halfway between the poles of the mitotic spindle, during mitosis. mitotic metaphase plate congression GO:0007084 nuclear envelope repair mitotic nuclear envelope reassembly The mitotic cell cycle process involving ESCRTIII that results in reformation of the nuclear envelope after mitotic nuclear division. In organisms undergoing closed mitosis this involves resealing or 'repair' of the nuclear envelope in the nuclear bridge. mitotic nuclear membrane reassembly GO:0007097 The directed movement of the nucleus to a specific location within a cell. nuclear migration GO:0007127 The first meiotic nuclear division in which homologous chromosomes are paired and segregated from each other, producing two haploid daughter nuclei. meiosis I GO:0007135 The second nuclear division of meiosis, in which the two chromatids in each chromosome are separated, resulting in four daughter nuclei from the two nuclei produced in meiosis II. meiosis II GO:0007143 A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the female germline. female meiotic nuclear division GO:0007144 The cell cycle process in which the first meiotic division occurs in the female germline. female meiosis I GO:0007147 The cell cycle process in which the second meiotic division occurs in the female germline. female meiosis II GO:0007155 The attachment of a cell, either to another cell or to the extracellular matrix, via cell adhesion molecules. Wikipedia:Cell_adhesion cell adhesion GO:0007163 Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns. cell polarity establishment or maintenance of cell polarity GO:0007173 A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. EGF receptor signaling pathway EGFR signaling pathway epidermal growth factor receptor signaling pathway GO:0007179 A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription. TGF-beta receptor signaling pathway transforming growth factor beta receptor signaling pathway GO:0007219 A series of molecular signals initiated by the binding of an extracellular ligand to the receptor Notch on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Notch signaling pathway GO:0007249 The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. PMID:12773372 I-kappaB kinase-NF-kappaB signal transduction pathway I-kappaB kinase/NF-kappaB signaling canonical NF-kappaB signal transduction GO:0007253 The selective interaction of the transcription factor NF-kappaB with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus. cytoplasmic sequestering of NF-kappaB GO:0007264 Any series of molecular signals in which a small monomeric GTPase relays one or more of the signals. small GTPase mediated signal transduction GO:0007266 A series of molecular signals within the cell that are mediated by a member of the Ras superfamily of proteins switching to a GTP-bound active state. Ras protein signal transduction GO:0007315 Establishment of the specialized cytoplasm found at the poles of the egg. An example of this is found in Drosophila melanogaster. pole plasm assembly GO:0007343 The process in which the egg becomes metabolically active, initiates protein and DNA synthesis and undergoes structural changes to its cortex and/or cytoplasm. egg activation GO:0007344 The merging of two pronuclei in a fertilized egg to fuse and produce a single zygotic genome. pronuclear fusion GO:0007354 The specification of the anterior/posterior axis of the embryo by products of genes expressed in the zygote; exemplified in insects by the gap genes, pair rule genes and segment polarity gene cascade. zygotic determination of anterior/posterior axis, embryo GO:0007389 Any developmental process that results in the creation of defined areas or spaces within an organism to which cells respond and eventually are instructed to differentiate. pattern biosynthesis pattern formation pattern specification process GO:0007568 A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700). Wikipedia:Aging aging GO:0007596 The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. Wikipedia:Coagulation blood clotting blood coagulation GO:0007597 A protein activation cascade that contributes to blood coagulation and consists of the interactions among high molecular weight kininogen, prekallikrein, and factor XII that lead to the activation of clotting factor X. blood coagulation, intrinsic pathway GO:0007598 A protein activation cascade that contributes to blood coagulation and consists of the self-limited process linking exposure and activation of tissue factor to the activation of clotting factor X. blood coagulation, extrinsic pathway GO:0007599 The stopping of bleeding (loss of body fluid) or the arrest of the circulation to an organ or part. Wikipedia:Hemostasis hemostasis GO:0007631 Behavior associated with the intake of food. Wikipedia:List_of_feeding_behaviours feeding behavior GO:0008090 The directed movement of organelles or molecules along microtubules from the cell periphery toward the cell body in nerve cell axons. retrograde axonal transport GO:0008104 Any process in which a protein is transported to, or maintained in, a specific location. protein localization GO:0008150 Note that, in addition to forming the root of the biological process ontology, this term is recommended for use for the annotation of gene products whose biological process is unknown. When this term is used for annotation, it indicates that no information was available about the biological process of the gene product annotated as of the date the annotation was made; the evidence code 'no data' (ND), is used to indicate this. biological process GO:0008152 The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation. The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation. Wikipedia:Metabolism metabolism Note that metabolic processes do not include single functions or processes such as protein-protein interactions, protein-nucleic acids, nor receptor-ligand interactions. metabolic process The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation. ISBN:0198547684 GO:0008210 The chemical reactions and pathways involving estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants. estrogen metabolic process GO:0008219 Any biological process that results in permanent cessation of all vital functions of a cell. A cell should be considered dead when any one of the following molecular or morphological criteria is met: (1) the cell has lost the integrity of its plasma membrane; (2) the cell, including its nucleus, has undergone complete fragmentation into discrete bodies (frequently referred to as apoptotic bodies). The cell corpse (or its fragments) may be engulfed by an adjacent cell in vivo, but engulfment of whole cells should not be considered a strict criteria to define cell death as, under some circumstances, live engulfed cells can be released from phagosomes (see PMID:18045538). cell death GO:0008228 The process in which a microorganism (or other particulate material) is rendered more susceptible to phagocytosis by coating with an opsonin, a blood serum protein such as a complement component or antibody. opsonization GO:0008283 The multiplication or reproduction of cells, resulting in the rapid expansion of a cell population. This term was moved out from being a child of 'cellular process' because it is a cell population-level process, and cellular processes are restricted to those processes that involve individual cells. Also note that this term is intended to be used for the proliferation of cells within a multicellular organism, not for the expansion of a population of single-celled organisms. cell proliferation GO:0008284 Any process that activates or increases the rate or extent of cell proliferation. positive regulation of cell population proliferation positive regulation of cell proliferation GO:0008286 The series of molecular signals generated as a consequence of the insulin receptor binding to insulin. https://reactome.org/PathwayBrowser/#/R-HSA-74752 insulin receptor signalling pathway insulin receptor signaling pathway GO:0008289 Interacting selectively and non-covalently with a lipid. lipid binding GO:0008356 The asymmetric division of cells to produce two daughter cells with different developmental potentials. It is of fundamental significance for the generation of cell diversity. Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook, doi/10.1895/wormbook.1.30.2, http://www.wormbook.org. asymmetric cell division Rose L. and Gönczy P. Polarity establishment, asymmetric division and segregation of fate determinants in early C. elegans embryos (December 30, 2014), WormBook, ed. The C. elegans Research Community, WormBook, doi/10.1895/wormbook.1.30.2, http://www.wormbook.org. During development, cells acquire distinct fates, and one prominent mechanism by which this is achieved is asymmetric division. In the early embryo of C. elegans, five asymmetric divisions produce six founder cells: AB, MS, E, C, D, and P4 (Figure 1). The first asymmetric division cleaves the one-cell zygote into a larger anterior blastomere, AB, and a smaller posterior blastomere, P1. Thereafter, P1 undergoes an asymmetric division that gives rise to EMS and P2. Subsequent asymmetric divisions of EMS into MS and E, then of P2 into C and P3, and finally of P3 into D and P4, complete the generation of the six founder cells whose descendants each produce specific cell types (Sulston et al., 1983) GO:0008358 The specification of the anterior/posterior axis of the embryo by gradients of maternally-transcribed gene products; exemplified in insects by the morphogens, bicoid and nanos. maternal determination of anterior/posterior axis, embryo GO:0008380 The process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA. RNA splicing GO:0008385 A trimeric protein complex that phosphorylates inhibitory-kappaB (I-kappaB) proteins. The complex is composed of two kinase subunits (alpha and beta) and a regulatory gamma subunit (also called NEMO). In a resting state, NF-kappaB dimers are bound to inhibitory IKB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. http://purl.obolibrary.org/obo/PR_000035833 IKK complex heterotrimeric IKK complex I-kappaB kinase complex GO:0008429 Interacting selectively and non-covalently with phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. GO:0008429 Interacting selectively and non-covalently with phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. phosphatidylethanolamine binding Interacting selectively and non-covalently with phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. ISBN:0198506732 GO:0008610 The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. lipid anabolism lipid biosynthesis lipid formation lipogenesis lipid biosynthetic process GO:0008625 A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with a ligand binding to a death domain receptor on the cell surface, and ends when the execution phase of apoptosis is triggered. PMID:21525013 https://reactome.org/PathwayBrowser/#/R-HSA-140534&PATH=R-HSA-5357801,R-HSA-109581,R-HSA-5357769 extrinsic apoptotic signaling pathway via death domain receptors PMID:21525013 Gene products that may be annotated to this term include: 1) ligands such as FASL; 2) receptors such as FAS/CD95 (though care should be taken because FAS can also act as a non-apoptotic signal transducer); 3) signaling molecules such as FADD (FAS-associated protein with a death domain), cIAPs (cellular inhibitor of apoptosis proteins), c-FLIPs and caspases 8 and 10. Examples are TWEAK (TNF12) and FN14 (TNFRSF12A) (UniProt symbols O43508 and Q9NP84) GO:0008626 A series of molecular signals induced by granzymes which triggers the apoptotic death of a cell. The pathway starts with reception of a granzyme signal, and ends when the execution phase of apoptosis is triggered. Granzymes are serine proteases that are secreted by cytotoxic T cells and natural killer cells to induce apoptosis in target cells. granzyme-mediated apoptotic signaling pathway GO:0008643 The directed movement of carbohydrate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Carbohydrates are any of a group of organic compounds based of the general formula Cx(H2O)y. GO:0008643 sugar transport carbohydrate transport GO:0008654 The chemical reactions and pathways resulting in the formation of phospholipids, any lipid containing phosphoric acid as a mono- or diester. The chemical reactions and pathways resulting in the formation of phospholipids, any lipid containing phosphoric acid as a mono- or diester. phospholipid anabolism phospholipid biosynthesis phospholipid formation phospholipid synthesis phospholipid biosynthetic process The chemical reactions and pathways resulting in the formation of phospholipids, any lipid containing phosphoric acid as a mono- or diester. ISBN:0198506732 GO:0009056 The chemical reactions and pathways resulting in the breakdown of substances, including the breakdown of carbon compounds with the liberation of energy for use by the cell or organism. The chemical reactions and pathways resulting in the breakdown of substances, including the breakdown of carbon compounds with the liberation of energy for use by the cell or organism. Wikipedia:Catabolism catabolic process The chemical reactions and pathways resulting in the breakdown of substances, including the breakdown of carbon compounds with the liberation of energy for use by the cell or organism. ISBN:0198547684 GO:0009058 The chemical reactions and pathways resulting in the formation of substances; typically the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones. anabolism biosynthesis synthesis biosynthetic process GO:0009062 The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. Wikipedia:Fatty_acid_degradation fatty acid catabolism fatty acid degradation fatty acid catabolic process GO:0009236 The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. vitamin B12 biosynthesis cobalamin biosynthetic process GO:0009247 The chemical reactions and pathways resulting in the formation of glycolipid, a class of 1,2-di-O-acylglycerols joined at oxygen 3 by a glycosidic linkage to a carbohydrate part (usually a mono-, di- or tri-saccharide). glycolipid anabolism glycolipid biosynthesis glycolipid biosynthetic process GO:0009386 Translational attenuation is a regulatory mechanism analogous to ribosome-mediated transcriptional attenuation. the system requires the presence of a short orf, called a leader peptide, encoded in the mrna upstream of the ribosome-binding site and start codon of the gene whose translation is to be regulated. certain conditions, such as presence of the antibiotic tetracycline in bacteria or amino acid starvation, may cause slowing or stalling of the ribosome translating the leader peptide. the stalled ribosome masks a region of the mrna and affects which of two alternative mrna folded structures will form, therefore controlling whether or not a ribosome will bind and initiate translation of the downstream gene. translational attenuation is analogous to ribosome-mediated transcriptional attenuation, in which mrna remodeling caused by ribosome stalling regulates transcriptional termination rather than translational initiation. Translational attenuation is a regulatory mechanism analogous to ribosome-mediated transcriptional attenuation. the system requires the presence of a short orf, called a leader peptide, encoded in the mrna upstream of the ribosome-binding site and start codon of the gene whose translation is to be regulated. certain conditions, such as presence of the antibiotic tetracycline in bacteria or amino acid starvation, may cause slowing or stalling of the ribosome translating the leader peptide. the stalled ribosome masks a region of the mrna and affects which of two alternative mrna folded structures will form, therefore controlling whether or not a ribosome will bind and initiate translation of the downstream gene. translational attenuation is analogous to ribosome-mediated transcriptional attenuation, in which mrna remodeling caused by ribosome stalling regulates transcriptional termination rather than translational initiation. attenuation of translation Translational attenuation is a regulatory mechanism analogous to ribosome-mediated transcriptional attenuation. the system requires the presence of a short orf, called a leader peptide, encoded in the mrna upstream of the ribosome-binding site and start codon of the gene whose translation is to be regulated. certain conditions, such as presence of the antibiotic tetracycline in bacteria or amino acid starvation, may cause slowing or stalling of the ribosome translating the leader peptide. the stalled ribosome masks a region of the mrna and affects which of two alternative mrna folded structures will form, therefore controlling whether or not a ribosome will bind and initiate translation of the downstream gene. translational attenuation is analogous to ribosome-mediated transcriptional attenuation, in which mrna remodeling caused by ribosome stalling regulates transcriptional termination rather than translational initiation. PMID:15694341 PMID:15805513 GO:0009395 The chemical reactions and pathways resulting in the breakdown of phospholipids, any lipid containing phosphoric acid as a mono- or diester. phospholipid breakdown phospholipid catabolism phospholipid degradation phospholipid catabolic process GO:0009404 The chemical reactions and pathways involving a toxin, a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism. toxin metabolism toxin metabolic process GO:0009566 The union of gametes of opposite sexes during the process of sexual reproduction to form a zygote. It involves the fusion of the gametic nuclei (karyogamy) and cytoplasm (plasmogamy). fertilization GO:0009605 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an external stimulus. response to environmental stimulus Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. response to external stimulus GO:0009719 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus arising within the organism. Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. response to endogenous stimulus GO:0009790 The process whose specific outcome is the progression of an embryo from its formation until the end of its embryonic life stage. The end of the embryonic stage is organism-specific. For example, for mammals, the process would begin with zygote formation and end with birth. For insects, the process would begin at zygote formation and end with larval hatching. For plant zygotic embryos, this would be from zygote formation to the end of seed dormancy. For plant vegetative embryos, this would be from the initial determination of the cell or group of cells to form an embryo until the point when the embryo becomes independent of the parent plant. Wikipedia:Embryogenesis embryogenesis embryo development GO:0009798 The establishment, maintenance and elaboration of a pattern along a line or around a point. axis specification GO:0009880 The process that results in the patterns of cell differentiation that will arise in an embryo. embryonic pattern biosynthesis embryonic pattern specification GO:0009948 The establishment, maintenance and elaboration of the anterior/posterior axis. The anterior-posterior axis is defined by a line that runs from the head or mouth of an organism to the tail or opposite end of the organism. anterior/posterior axis determination anterior/posterior axis specification GO:0009949 Any process resulting in the establishment of polarity along the anterior/posterior axis. polarity specification of anterior/posterior axis GO:0010008 The lipid bilayer surrounding an endosome. endosome membrane GO:0010069 The division of the zygote into two daughter cells that will adopt developmentally distinct potentials. zygote asymmetric cell division GO:0010324 The infolding of a membrane. membrane invagination GO:0010467 The process in which a gene's sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. Wikipedia:Gene_expression A changing process to convert a gene's sequenes into a mature gene prduct(s), i.e., (m)RNA, or protein. gene expression GO:0010468 Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. Wikipedia:Regulation_of_gene_expression regulation of protein expression This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression. For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation. regulation of gene expression GO:0010498 The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome. proteasome-mediated protein catabolic process proteasome-mediated protein catabolism proteasomal protein catabolic process GO:0010506 Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. regulation of autophagy GO:0010507 Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. negative regulation of autophagy GO:0010508 Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. positive regulation of autophagy GO:0010608 Any process that modulates the frequency, rate or extent of gene expression after the production of an RNA transcript. post-transcriptional regulation of gene expression GO:0010628 Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. positive regulation of gene expression GO:0010629 Any process that decreases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. This term covers any process that negatively regulates the rate of production of a mature gene product, and so includes processes that negatively regulate that rate by reducing the level, stability or availability of intermediates in the process of gene expression. For example, it covers any process that reduces the level, stability or availability of mRNA or circRNA for translation and thereby reduces the rate of production of the encoded protein via translation. negative regulation of gene expression GO:0010716 Any process that decreases the rate, frequency or extent of extracellular matrix disassembly. Extracellular matrix disassembly is a process that results in the breakdown of the extracellular matrix. negative regulation of extracellular matrix disassembly GO:0010742 The process in which a monocyte acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions. macrophage derived foam cell differentiation GO:0010743 Any process that modulates the rate, frequency or extent of macrophage derived foam cell differentiation. Macrophage derived foam cell differentiation is the process in which a macrophage acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions. regulation of macrophage derived foam cell differentiation GO:0010744 Any process that increases the rate, frequency or extent of macrophage derived foam cell differentiation. Macrophage derived foam cell differentiation is the process in which a macrophage acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions. positive regulation of macrophage derived foam cell differentiation GO:0010745 Any process that decreases the rate, frequency or extent of macrophage derived foam cell differentiation. Macrophage derived foam cell differentiation is the process in which a macrophage acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions. negative regulation of macrophage derived foam cell differentiation GO:0010818 The directed movement of a T cell in response to an external stimulus. A T cell is a type of lymphocyte whose defining characteristic is the expression of a T cell receptor complex. T cell chemotaxis GO:0010833 Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins and lengthening the telomeric DNA. telomere maintenance via telomere lengthening GO:0010878 The accumulation and maintenance in cells or tissues of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. GO:0010878 cholesterol sequestration sequestration of cholesterol cholesterol storage GO:0010888 Any process that decreases the rate, frequency or extent of lipid storage. Lipid storage is the accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development. negative regulation of lipid storage GO:0010900 Any process that decreases the rate, frequency or extent of phosphatidylcholine catabolism. Phosphatidylcholine catabolic processes are the chemical reactions and pathways resulting in the breakdown of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. negative regulation of phosphatidylcholine catabolic process GO:0010941 Any process that modulates the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death. [ regulation of cell death GO:0010955 Any process that decreases the rate, frequency or extent of protein maturation by peptide bond cleavage. negative regulation of protein processing GO:0014065 A series of reactions within the signal-receiving cell, mediated by the intracellular phosphatidylinositol 3-kinase (PI3K). Many cell surface receptor linked signaling pathways signal through PI3K to regulate numerous cellular functions. A series of reactions within the signal-receiving cell, mediated by the intracellular phosphatidylinositol 3-kinase (PI3K). Many cell surface receptor linked signaling pathways signal through PI3K to regulate numerous cellular functions. PI3K signaling phosphatidylinositol 3-kinase signaling A series of reactions within the signal-receiving cell, mediated by the intracellular phosphatidylinositol 3-kinase (PI3K). Many cell surface receptor linked signaling pathways signal through PI3K to regulate numerous cellular functions. PMID:22525052 GO:0015721 The directed movement of bile acid and bile salts into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. The directed movement of bile acid and bile salts into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. bile acid transport bile acid and bile salt transport The directed movement of bile acid and bile salts into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. PMID:12663868 PMID:14699511 GO:0015722 Enables the transfer of bile acid from one side of a hepatocyte plasma membrane into a bile canaliculus. Bile canaliculi are the thin tubes formed by hepatocyte membranes. Bile acids are any of a group of steroid carboxylic acids occurring in bile, where they are present as the sodium salts of their amides with glycine or taurine. canalicular bile acid transport GO:0015871 The directed movement of choline into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Choline (2-hydroxyethyltrimethylammonium) is an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine. choline transport GO:0015893 The directed movement of a drug, a substance used in the diagnosis, treatment or prevention of a disease, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. drug transport GO:0015908 The directed movement of fatty acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Fatty acids are aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis fatty acid transport GO:0015909 The directed movement of long-chain fatty acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. long-chain fatty acid transport GO:0015910 The directed movement of long-chain fatty acids into a peroxisome. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. long-chain fatty acid import into peroxisome GO:0015914 The directed movement of phospholipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Phospholipids are any lipids containing phosphoric acid as a mono- or diester. phospholipid transport GO:0015990 The transport of protons against an electrochemical gradient, using energy from electron transport. electron transport coupled proton transport GO:0016032 A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle. A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle. GO:0022415 Wikipedia:Viral_life_cycle virus process virus process viral infection virulence See also the biological process terms 'viral infectious cycle ; GO:0019058' and 'lysogeny ; GO:0030069'. viral process A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle. GOC:bf GOC:jl GOC:mah virus process GOC:bf GOC:jl GO:0016042 The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Wikipedia:Lipid_catabolism lipid breakdown lipid catabolism lipid degradation lipolysis lipid catabolic process GO:0016049 The process in which a cell irreversibly increases in size over time by accretion and biosynthetic production of matter similar to that already present. cellular growth growth of cell cell growth GO:0016051 The chemical reactions and pathways resulting in the formation of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. anabolic carbohydrate metabolic process anabolic carbohydrate metabolism carbohydrate anabolism carbohydrate biosynthesis carbohydrate formation carbohydrate synthesis carbohydrate biosynthetic process GO:0016052 The chemical reactions and pathways resulting in the breakdown of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. The chemical reactions and pathways resulting in the breakdown of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. carbohydrate biosynthesis carbohydrate catabolism carbohydrate degradation catabolic carbohydrate metabolic process catabolic carbohydrate metabolism carbohydrate catabolic process The chemical reactions and pathways resulting in the breakdown of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. ISBN:0198506732 GO:0016064 An immune response mediated by immunoglobulins, whether cell-bound or in solution. immunoglobulin mediated immune response GO:0016192 A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane. vesicle transport vesicular transport vesicle trafficking vesicle-mediated transport GO:0016197 The directed movement of substances mediated by an endosome, a membrane-bounded organelle that carries materials enclosed in the lumen or located in the endosomal membrane. endosomal transport GO:0016233 A process in which telomeres are protected from degradation and fusion, thereby ensuring chromosome stability by protecting the ends from both degradation and from being recognized as damaged DNA. May be mediated by specific single- or double-stranded telomeric DNA binding proteins. telomere capping GO:0016264 Assembly of gap junctions, which are found in most animal tissues, and serve as direct connections between the cytoplasms of adjacent cells. They provide open channels through the plasma membrane, allowing ions and small molecules (less than approximately a thousand daltons) to diffuse freely between neighboring cells, but preventing the passage of proteins and nucleic acids. Reactome:REACT_9509 gap junction assembly GO:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. EC:2.7.-.- Wikipedia:Phosphorylation phosphorylation GO:0016311 The process of removing one or more phosphoric (ester or anhydride) residues from a molecule. dephosphorylation GO:0016441 The inactivation of gene expression that occurs after transcription. post-transcriptional gene silencing GO:0016477 The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms. Wikipedia:Cell_migration cell migration GO:0016482 The directed movement of substances or organelles within the cytosol. cytosolic transport GO:0016485 Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. protein maturation by peptide bond cleavage protein processing GO:0016570 GO:0016579 The removal of one or more ubiquitin groups from a protein. protein deubiquitination GO:0016925 The process in which a SUMO protein (small ubiquitin-related modifier) is conjugated to a target protein via an isopeptide bond between the carboxyl terminus of SUMO with an epsilon-amino group of a lysine residue of the target protein. Wikipedia:SUMO_protein SUMO-protein conjugation protein sumolation sumoylation protein sumoylation GO:0017129 Interacting selectively and non-covalently with any triester of glycerol. Interacting selectively and non-covalently with any triester of glycerol. GO:0017129 triglyceride binding GO:0017144 The chemical reactions and pathways involving a drug, a substance used in the diagnosis, treatment or prevention of a disease; as used here antibiotic substances (see antibiotic metabolism) are considered to be drugs, even if not used in medical or veterinary practice. Wikipedia:Drug_metabolism drug metabolism drug metabolic process GO:0017145 The self-renewing division of a stem cell. A stem cell is an undifferentiated cell, in the embryo or adult, that can undergo unlimited division and give rise to one or several different cell types. stem cell division GO:0018377 The covalent attachment of a myristoyl group to a protein. protein myristoylation GO:0018411 The modification of a protein by amino acid glucuronidation. glucronide conjugation protein glucuronidation GO:0019012 The complete fully infectious extracellular virus particle. The complete fully infectious extracellular virus particle. virion The complete fully infectious extracellular virus particle. ISBN:078171832 GO:0019028 The protein coat that surrounds the infective nucleic acid in some virus particles. It comprises numerous regularly arranged subunits, or capsomeres. viral capsid GO:0019031 The lipid bilayer of a virion that surrounds the protein capsid. May also contain glycoproteins. viral outside membrane viral envelope GO:0019042 The process by which, after initial infection, a virus lies dormant within a cell and viral production ceases. The process ends when the virus switches from latency and starts to replicate. viral latency GO:0019043 A process by which a virus establishes a latent state within its host, either as an integrated provirus within the host genome or as an episome, where viral genome remains in the cytoplasm or nucleus as distinct objects. GO:0075601 lysogenic commitment phage lysogeny establishment of viral latency GO:0019044 The perpetuation of a latent state, generally by repressing the viruses own lytic genes expression and ensuring expression of viral genes which function to keep the viral genome from being detected by the host defense mechanisms. The perpetuation of a latent state, generally by repressing the viruses own lytic genes expression and ensuring expression of viral genes which function to keep the viral genome from being detected by the host defense mechanisms. GO:0032360 GO:0075716 latent virus maintenance prophage maintenance provirus maintenance maintenance of viral latency The perpetuation of a latent state, generally by repressing the viruses own lytic genes expression and ensuring expression of viral genes which function to keep the viral genome from being detected by the host defense mechanisms. GOC:jl GO:0019045 Any process required for latent viral replication in a cell. Any process required for latent viral replication in a cell. latent virus replication Any process required for latent viral replication in a cell. ISBN:0781702534 GO:0019048 The process in which a virus effects a change in the structure or processes of its host organism. The process in which a virus effects a change in the structure or processes of its host organism. https://github.com/geneontology/go-ontology/issues/18605 https://github.com/geneontology/go-ontology/issues/18719 GO:0044661 GO:0044792 virus-host interaction VZ:886 host-virus interaction modulation by virus of host anatomy or process viral interaction with host viral-host process virus-host process disruption by virus of host cell modulation by virus of host anatomical structure or process modulation by virus of host morphology or physiology modulation by virus of host process The process in which a virus effects a change in the structure or processes of its host organism. ISBN:0781718325 UniProtKB-KW:KW-0945 VZ:886 Vertebrate host-virus interactions GO:0019058 A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome. A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome. viral infectious cycle viral life cycle A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome. ISBN:15558112 GO:0019061 The process by which an incoming virus is disassembled in the host cell to release a replication-competent viral genome. viral uncoating uncoating of virus GO:0019062 The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. VZ:956 viral absorption virion attachment to host cell surface receptor viral attachment to host cell viral attachment to host cell virion attachment to host cell The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. GOC:bf GOC:jl UniProtKB-KW:KW-1161 VZ:956 VZ:956 Viral attachment to host cell viral attachment to host cell GOC:bf GOC:jl GO:0019064 Fusion of a viral membrane with the host cell membrane during viral entry. Results in release of the virion contents into the cytoplasm. fusion of virus membrane with host plasma membrane GO:0019065 Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. receptor mediated endocytosis by host of virus particle receptor mediated endocytosis of virus by host receptor mediated endocytosis of virus particle by host receptor-mediated endocytosis of virus by host viral receptor mediated endocytosis virus receptor-mediated endocytosis by host viral entry into host cell via receptor-mediated endocytosis receptor-mediated endocytosis of virus by host cell Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell. ISBN:0781702534 GO:0019068 A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. GO:0042963 viral assembly viral particle assembly virion assembly and maintenance virion assembly and maintenance virion organization virion organization virus assembly virus assembly virus particle assembly bacteriophage assembly bacteriophage assembly phage assembly phage assembly virion assembly A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed. ISBN:0121585336 virion assembly and maintenance GOC:bf GOC:jl virion organization GOC:bf GOC:jl virus assembly GOC:dph GOC:tb bacteriophage assembly GOC:bm phage assembly GOC:bm GO:0019069 The assembly of a virus capsid from its protein subunits. The assembly of a virus capsid from its protein subunits. viral capsid assembly The assembly of a virus capsid from its protein subunits. ISBN:0781702534 UniProtKB-KW:KW-0118 GO:0019070 The processes involved in creating a mature, stable viral genome. Begins after genome replication with a newly synthesized nucleic acid and ends when the genome is ready to be packaged. Includes the addition of proteins to the newly synthesized genome, and DNA repair processes. The processes involved in creating a mature, stable viral genome. Begins after genome replication with a newly synthesized nucleic acid and ends when the genome is ready to be packaged. Includes the addition of proteins to the newly synthesized genome, and DNA repair processes. viral genome maturation The processes involved in creating a mature, stable viral genome. Begins after genome replication with a newly synthesized nucleic acid and ends when the genome is ready to be packaged. Includes the addition of proteins to the newly synthesized genome, and DNA repair processes. GOC:pk PMID:21490093 GO:0019075 The refolding and structural rearrangements of virion parts to transition from the intermediate virion to the more mature virion. Maturation usually involves proteolysis events and changes in the folding of the virion proteins. Can occur inside the host cell or after release. viral maturation virus maturation GO:0019076 The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. VZ:1076 release of virus from host viral exit viral release viral shedding virus exit from host cell virus exit from host cell ウイルス排出 viral release from host cell The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. GOC:jl VZ:1076 Virus exit from host cell virus exit from host cell GOC:bf GOC:jl GO:0019079 Any process involved directly in viral genome replication, including viral nucleotide metabolism. viral genome replication GO:0019080 A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. viral genome expression viral genome expression viral gene expression A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation. GOC:bf GOC:jl ISBN:0121585336 viral genome expression GOC:jl GO:0019081 A process by which viral mRNA is translated into viral protein, using the host cellular machinery. A process by which viral mRNA is translated into viral protein, using the host cellular machinery. viral protein anabolism viral protein biosynthesis viral protein biosynthetic process viral protein biosynthetic process viral protein formation viral protein synthesis viral translation A process by which viral mRNA is translated into viral protein, using the host cellular machinery. GOC:bf GOC:jl ISBN:0781702534 viral protein biosynthetic process ISBN:0781702534 GO:0019082 Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. viral protein processing Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. GOC:bf GOC:jl ISBN:0781702534 GO:0019083 The process by which a viral genome, or part of a viral genome, is transcribed within the host cell. The process by which a viral genome, or part of a viral genome, is transcribed within the host cell. viral transcription The process by which a viral genome, or part of a viral genome, is transcribed within the host cell. GOC:jl ISBN:0781702534 GO:0019084 The viral transcription that takes place after early transcription in the viral life cycle, and which involves the transcription of genes required for replication. middle viral transcription GO:0019085 The first phase of viral transcription that occurs after entry of the virus into the host cell, but prior to viral genome replication. It involves the transcription of genes for non-structural proteins, and for lytic viruses, the early gene products are involved in establishing control over the host cell. early viral transcription GO:0019086 The transcription of the final group of viral genes of the viral life cycle, following middle transcription, or where middle transcription doesn't occur, following early transcription. Involves the transcription of genes encoding structural proteins. late viral transcription GO:0019087 A virus-induced cellular transformation resulting in immortalized cells, or cells capable of indefinite replication. A virus-induced cellular transformation resulting in immortalized cells, or cells capable of indefinite replication. GO:0019088 GO:0020021 Wikipedia:Viral_transformation host cell immortalization host cell transformation immortalization of host cell transformation of host cell viral immortalization viral transformation viral transformation of host cell immortalization of host cell by virus transformation of host cell by virus A virus-induced cellular transformation resulting in immortalized cells, or cells capable of indefinite replication. ISBN:0781702534 PMID:11119620 PMID:18366075 PMID:24373315 GO:0019216 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving lipids. regulation of lipid metabolism regulation of lipid metabolic process GO:0019221 A series of molecular signals initiated by the binding of a cytokine to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. cytokine-mediated signaling pathway GO:0019222 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways within a cell or an organism. regulation of metabolism regulation of metabolic process GO:0019395 The removal of one or more electrons from a fatty acid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. The removal of one or more electrons from a fatty acid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. fatty acid oxidation The removal of one or more electrons from a fatty acid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. ISBN:0198506732 GO:0019430 Any process, acting at the cellular level, involved in removing superoxide radicals (O2-) from a cell or organism, e.g. by conversion to dioxygen (O2) and hydrogen peroxide (H2O2). removal of superoxide radicals GO:0019538 The chemical reactions and pathways involving a protein. Includes protein modification. Wikipedia:Protein_metabolism protein metabolism protein metabolic process GO:0019585 The chemical reactions and pathways involving glucuronate, any salt or ester of glucuronic acid, the uronic acid formally derived from glucose by oxidation of the hydroxymethylene group at C-6 to a carboxyl group. glucuronate metabolic process GO:0019724 Any process involved with the carrying out of an immune response by a B cell, through, for instance, the production of antibodies or cytokines, or antigen presentation to T cells. B cell mediated immunity GO:0019835 The rupture of cell membranes and the loss of cytoplasm. Wikipedia:Cytolysis cytolysis GO:0019882 The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex. antigen processing and presentation GO:0019915 The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development. lipid retention lipid sequestering retention of lipids sequestration of lipid sequestration of lipids storage of lipids lipid storage GO:0020002 The plasma membrane surrounding a host cell. host cell plasma membrane GO:0022403 One of the distinct periods or stages into which the cell cycle is divided. Each phase is characterized by the occurrence of specific biochemical and morphological events. cell cycle phase GO:0022411 A process that results in the breakdown of the extracellular matrix. extracellular matrix disassembly GO:0022607 The aggregation, arrangement and bonding together of a cellular component. cellular component assembly at cellular level cellular component assembly GO:0022900 A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. Wikipedia:Electron_transport_chain electron transport chain GO:0022904 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. Wikipedia:Electron_transfer electron transfer respiratory electron transport chain A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. ISBN:0716720094 GO:0023051 Any process that modulates the frequency, rate or extent of a signaling process. regulation of signaling GO:0023052 The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered. molecular signaling Note that a signal is any variable property or parameter that serves to convey information, and may be a physical entity such as a gene product or small molecule, a photon, or a change in state such as movement or voltage change. biological signaling GO:0023057 Any process that stops, prevents, or reduces the frequency, rate or extent of a signaling process. negative regulation of signaling GO:0030010 The specification and formation of anisotropic intracellular organization or cell growth patterns. cell polarization establishment of cell polarity GO:0030011 The maintenance of established anisotropic intracellular organization or cell growth patterns. maintenance of cell polarity GO:0030032 Formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell. lamellipodium biogenesis GO:0030036 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. actin cytoskeleton organization and biogenesis GO:0030073 The regulated release of proinsulin from secretory granules accompanied by cleavage of proinsulin to form mature insulin. In vertebrates, insulin is secreted from B granules in the B cells of the vertebrate pancreas and from insulin-producing cells in insects. The regulated release of proinsulin from secretory granules accompanied by cleavage of proinsulin to form mature insulin. In vertebrates, insulin is secreted from B granules in the B cells of the vertebrate pancreas and from insulin-producing cells in insects. insulin secretion The regulated release of proinsulin from secretory granules accompanied by cleavage of proinsulin to form mature insulin. In vertebrates, insulin is secreted from B granules in the B cells of the vertebrate pancreas and from insulin-producing cells in insects. ISBN:0198506732 GO:0030091 The process of restoring a protein to its original state after damage by such things as oxidation or spontaneous decomposition of residues. protein repair GO:0030098 The process in which a relatively unspecialized precursor cell acquires specialized features of a lymphocyte. A lymphocyte is a leukocyte commonly found in the blood and lymph that has the characteristics of a large nucleus, a neutral staining cytoplasm, and prominent heterochromatin. lymphocyte cell differentiation lymphocytic blood cell differentiation lymphocyte development Note that immunologists typically use the word 'development' to refer to cells of B or T cell lineages undergoing the process that GO describes as 'cell differentiation'. lymphocyte differentiation GO:0030101 The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor. NK cell activation natural killer cell activation GO:0030154 The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state. The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state. Wikipedia:Cellular_differentiation cell differentiation The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state. ISBN:0198506732 GO:0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. Wikipedia:Protein_catabolism protein breakdown protein catabolism protein degradation This term refers to the breakdown of mature proteins. For cleavage events involved in generating a mature protein from a precursor, consider instead the term 'protein maturation ; GO:0051604' and its children. protein catabolic process GO:0030168 A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug. platelet activation GO:0030193 Any process that modulates the frequency, rate or extent of blood coagulation. regulation of blood coagulation http://purl.obolibrary.org/obo/GO_0030193 GO:0030194 Any process that activates or increases the frequency, rate or extent of blood coagulation. positive regulation of blood coagulation GO:0030198 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures in the space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane, and also covers the host cell environment outside an intracellular parasite. extracellular matrix organization GO:0030217 The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex. T lymphocyte differentiation T-cell differentiation T-lymphocyte differentiation T cell differentiation GO:0030224 The process in which a relatively unspecialized myeloid precursor cell acquires the specialized features of a monocyte. monocyte differentiation GO:0030225 The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. macrophage cell differentiation macrophage differentiation The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. ISBN:0781735149 GO:0030242 The process in which peroxisomes are delivered to the vacuole and degraded in response to changing nutrient conditions. PMID:10547367 PMID:20083110 autophagy of peroxisome GO:0030301 The directed movement of cholesterol, cholest-5-en-3-beta-ol, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. The directed movement of cholesterol, cholest-5-en-3-beta-ol, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. cholesterol transport The directed movement of cholesterol, cholest-5-en-3-beta-ol, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. ISBN:0198506732 GO:0030330 A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage. DNA damage response, signal transduction by p53 class mediator GO:0030430 The cytoplasm of a host cell. [ host cell cytoplasm GO:0030473 The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins. nuclear migration along microtubule GO:0030512 Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway. negative regulation of transforming growth factor beta receptor signaling pathway GO:0030595 The movement of a leukocyte in response to an external stimulus. immune cell chemotaxis leucocyte chemotaxis leukocyte chemotaxis GO:0030719 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of polar granules, cytoplasmic, non-membranous RNA/protein complex aggregates in the primordial germ cells of many higher eukaryotes. P granule organization GO:0030728 The release of a mature ovum/oocyte from an ovary. ovulation GO:0030730 The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system. GO:0030730 retention of triacylglycerol retention of triglyceride sequestering of triacylglycerol triacylglycerol sequestering triacylglycerol sequestration triacylglycerol storage triglyceride storage sequestering of triglyceride GO:0030855 The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium. The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium. epithelial cell differentiation The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium. PMID:11839751 GO:0030908 The post-translational removal of peptide sequences from within a protein sequence. protein splicing GO:0030968 The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation. The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation. ER unfolded protein response Note that this term should not be confused with 'response to unfolded protein ; GO:0006986', which refers to any response to the presence of unfolded proteins anywhere in the cell or in multicellular organism. Also see 'ER-associated protein catabolic process ; GO:0030433'. endoplasmic reticulum unfolded protein response The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation. PMID:12042763 GO:0030970 The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon. The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon. PMID:11994744 protein retrotranslocation, ER to cytosol retrograde protein transport, endoplasmic reticulum to cytosol retrograde protein transport, ER to cytosol The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon. PMID:11994744 GO:0031012 A structure lying external to one or more cells, which provides structural support for cells or tissues. MESH:D005109 NCIT:C13232 extracellular matrix GO:0031090 A membrane that is one of the two lipid bilayers of an organelle envelope or the outermost membrane of single membrane bound organelle. intracellular membrane organelle membrane GO:0031098 A series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays one or more of the signals. PMID:11790549 JNK signal transduction pathway stress-activated protein kinase signaling cascade PMID:11790549 An intracellular protein kinase cascade containing at least a JNK (a MAPK), a JNKK (a MAPKK) and a JUN3K (a MAP3K). The cascade can also contain two additional tiers: the upstream MAP4K and the downstream MAP Kinase-activated kinase (MAPKAPK). The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell. GO:0031161 The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. PtdIns catabolic process PtdIns catabolism phosphatidylinositol breakdown phosphatidylinositol catabolism phosphatidylinositol degradation phosphatidylinositol catabolic process The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. GOC:mah GO:0031210 Interacting selectively and non-covalently with phosphatidylcholine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of choline. GO:0031210 phosphatidylcholine binding GO:0031333 Any process that stops, prevents, or reduces the frequency, rate or extent of protein complex assembly. down regulation of protein complex assembly down-regulation of protein complex assembly downregulation of protein complex assembly inhibition of protein complex assembly negative regulation of protein complex assembly negative regulation of protein complex assembly GO:0031381 A virus-specific protein complex that possesses RNA-dependent RNA polymerase activity and replicates the genome of an RNA virus. viral RNA-directed RNA polymerase complex GO:0031461 Any ubiquitin ligase complex in which the catalytic core consists of a member of the cullin family and a RING domain protein; the core is associated with one or more additional proteins that confer substrate specificity. cullin-RING ubiquitin ligase complex GO:0031468 The reformation of the nuclear membranes following their breakdown in the context of a normal process. nuclear membrane reassembly GO:0031532 A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts of cytoskeletal structures comprising actin filaments and their associated proteins. actin cytoskeleton remodeling actin cytoskeleton reorganization GO:0031622 Any process that activates or increases the frequency, rate, or extent of fever generation. positive regulation of fever generation GO:0031649 Any homeostatic process in which an organism produces heat, thereby raising its internal temperature. heat generation GO:0031929 A series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors. TOR signaling cascade TOR signaling pathway target of rapamycin signaling pathway TOR signaling pathway GO:0031931 A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p. Wikipedia:MTORC1 TOR complex 1 mTORC1 complex TOR complex GO:0031965 Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space. NIF_Subcellular:sao1687101204 nuclear membrane GO:0031966 Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. NIF_Subcellular:sao1045389829 mitochondrial membrane GO:0031982 Any small, fluid-filled, spherical organelle enclosed by membrane. membrane-bounded vesicle membrane-enclosed vesicle vesicle GO:0032043 The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA. mitochondrial DNA catabolic process GO:0032049 The chemical reactions and pathways resulting in the formation of cardiolipin, 1,3-bis(3-phosphatidyl)glycerol. The chemical reactions and pathways resulting in the formation of cardiolipin, 1,3-bis(3-phosphatidyl)glycerol. MetaCyc:PWY-5269 diphosphatidylglycerol biosynthesis diphosphatidylglycerol biosynthetic process cardiolipin biosynthetic process The chemical reactions and pathways resulting in the formation of cardiolipin, 1,3-bis(3-phosphatidyl)glycerol. CHEBI:28494 GOC:mah GO:0032060 The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Plasma membrane blebbing occurs during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses. membrane blebbing PMID:12083798 PMID:16624291 http://en.wikipedia.org/wiki/Bleb_(cell_biology) cell blebbing plasma membrane bleb assembly bleb assembly GO:0032065 A process in which a protein or protein complex is maintained in a specific location in the cell cortex. maintenance of protein location in cell cortex GO:0032200 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of telomeres, terminal regions of a linear chromosome that include the telomeric DNA repeats and associated proteins. chromosome organization, telomeric telomere organisation telomere organization GO:0032259 The process in which a methyl group is covalently attached to a molecule. methylation GO:0032310 The regulated release of a prostaglandin, any of a group of biologically active metabolites which contain a cyclopentane ring, from a cell or a tissue. prostaglandin secretion GO:0032456 The directed movement of membrane-bounded vesicles from recycling endosomes back to the plasma membrane where they are recycled for further rounds of transport. The directed movement of membrane-bounded vesicles from recycling endosomes back to the plasma membrane where they are recycled for further rounds of transport. retrograde transport of endocytic vesicles endocytic recycling The directed movement of membrane-bounded vesicles from recycling endosomes back to the plasma membrane where they are recycled for further rounds of transport. PMID:16473635 GO:0032481 Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. positive regulation of type I IFN production upregulation of type I interferon production positive regulation of type I interferon production GO:0032488 A series of molecular signals within the cell that are mediated by the Cdc42 protein switching to a GTP-bound active state. Cdc42 protein signal transduction GO:0032502 A biological process whose specific outcome is the progression of an integrated living unit: an anatomical structure (which may be a subcellular structure, cell, tissue, or organ), or organism over time from an initial condition to a later condition. development developmental process GO:0032602 chemokine production The appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. chemokine production GO:0032604 The appearance of GM-CSF (granulocyte macrophage colony-stimulating factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. GM-CSF production granulocyte macrophage colony-stimulating factor production GO:0032606 The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. type I interferon production GO:0032607 The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interferon-alpha production GO:0032608 The appearance of interferon-beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interferon-beta production GO:0032609 interferon-gamma production The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon. type II interferon production interferon-gamma production GO:0032610 The appearance of interleukin-1 alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. IL-1 alpha production interleukin-1 alpha biosynthetic process interleukin-1 alpha secretion interleukin-1 alpha production GO:0032611 The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. IL-1 beta production GO:0032612 interleukin-1 production The appearance of interleukin-1 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. GO:0032612 interleukin-1 production GO:0032613 The appearance of interleukin-10 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interleukin-10 production GO:0032620 The appearance of any member of the interleukin-17 family of cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. The appearance of any member of the interleukin-17 family of cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interleukin-17 production The appearance of any member of the interleukin-17 family of cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Wikipedia:Interleukin_17 GO:0032623 The appearance of interleukin-2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interleukin-2 production GO:0032626 The appearance of interleukin-22 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interleukin-22 production GO:0032633 The appearance of interleukin-4 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interleukin-4 production GO:0032635 The appearance of interleukin-6 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interleukin-6 production GO:0032636 The appearance of interleukin-7 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. interleukin-7 production HOIP_0040331 GO:0032637 The appearance of interleukin-8 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. CXCL8 production interleukin-8 production GO:0032640 tumor necrosis factor production The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. TNF alpha production tumor necrosis factor production GO:0032688 Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production. down regulation of interferon-beta production down-regulation of interferon-beta production downregulation of interferon-beta production negative regulation of IFN-beta production negative regulation of type I interferon production GO:0032727 Any process that activates or increases the frequency, rate, or extent of interferon-alpha production. up regulation of interferon-alpha production positive regulation of interferon-alpha production GO:0032782 The regulated release of bile acid, composed of any of a group of steroid carboxylic acids occurring in bile, by a cell or a tissue. Bile contains bile acids, glutathione, phospholipids, cholesterol, bilirubin, and other organic anions, proteins, metals, ions, and xenobiotics. Hepatocytes begins the formation of bile by transporting bile acids, glutathione, and other solutes including Xenobiotics and their metabolites into the canalicular lumen. The major driving force of bile formation is the active transport of bile salts and other osmolytes into the canalicular lumen. Most conjugated bile acids (taurine and glycine conjugates) and some unconjugated bile acids are transported into hepatocytes by sodium-dependent transporters. Sodium-independent uptake of conjugated and unconjugated bile acids is performed by members of the organic anion-transporting polypeptides (OATPs). OATPs also transport numerous drugs and hepatotoxicants. Lipophilic cationic drugs, estrogens, and lipids are exported by the canalicular multiple-drug resistance (MDR) P-glycoproteins, one of which is exclusive for phospholipids. Conjugates of glutathione, glucuronide, and sulfate are exported by multidrug resistance-associated protein2 (MRP2). bile acid secretion GO:0032869 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. cellular response to insulin stimulus GO:0032870 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hormone stimulus. cellular response to hormone stimulus GO:0032880 Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location. regulation of protein localization GO:0032905 transforming growth factor beta1 production The appearance of transforming growth factor-beta1 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. transforming growth factor beta1 production GO:0032981 The aggregation, arrangement and bonding together of a set of components to form mitochondrial respiratory chain complex I. mitochondrial NADH dehydrogenase complex (ubiquinone) assembly mitochondrial complex I assembly mitochondrial respiratory chain complex I assembly GO:0032982 A supramolecular fiber containing myosin heavy chains, plus associated light chains and other proteins, in which the myosin heavy chains are arranged into a filament. myosin filament GO:0032991 GO:0033108 The aggregation, arrangement and bonding together of a set of components to form a mitochondrial respiratory chain complex. mitochondrial respiratory chain complex assembly GO:0033209 A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. tumor necrosis factor-mediated signaling pathway GO:0033260 The DNA-dependent DNA replication that occurs in the nucleus of eukaryotic organisms as part of the cell cycle. DNA replication involved in S phase DNA replication during S phase nuclear DNA replication GO:0033299 The controlled release of lysosomal enzymes by a cell. secretion of lysosomal enzymes GO:0033344 The directed movement of cholesterol, cholest-5-en-3-beta-ol, out of a cell or organelle. cholesterol export cholesterol efflux GO:0033554 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). cellular response to stress GO:0033617 The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex IV (also known as cytochrome c oxidase) in the mitochondrial inner membrane. mitochondrial cytochrome c oxidase biogenesis mitochondrial cytochrome c oxidase complex assembly mitochondrial respiratory chain complex IV assembly GO:0033700 The directed movement of a phospholipid out of a cell or organelle. phospholipid efflux GO:0034061 GO:0034138 Any series of molecular signals generated as a consequence of binding to toll-like receptor 3. TLR3 signaling pathway toll-like receptor 3 signaling pathway HOIP_0036107 GO:0034142 Any series of molecular signals generated as a consequence of binding to toll-like receptor 4. TLR4 signaling pathway toll-like receptor 4 signaling pathway GO:0034154 Any series of molecular signals generated as a consequence of binding to toll-like receptor 7. toll-like receptor 7 signaling pathway GO:0034158 Any series of molecular signals generated as a consequence of binding to toll-like receptor 8. toll-like receptor 8 signaling pathway GO:0034162 Any series of molecular signals generated as a consequence of binding to toll-like receptor 9. TLR9 signaling pathway toll-like receptor 9 signaling pathway GO:0034197 The directed movement of triglyceride into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Triglycerides are important components of plant oils, animal fats and animal plasma lipoproteins. triacylglycerol transport triglyceride transport GO:0034329 A cellular process that results in the aggregation, arrangement and bonding together of a set of components to form a cell junction. cell junction assembly GO:0034333 The aggregation, arrangement and bonding together of a set of components to form an adherens junction. An adherens junction is a cell junction at which the cytoplasmic face of the plasma membrane is attached to actin filaments. adherens junction assembly GO:0034379 The non-covalent aggregation and arrangement of proteins and lipids in the liver to form a very-low-density lipoprotein particle. very-low-density lipoprotein particle assembly GO:0034389 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid particle. lipid droplet organization GO:0034440 The removal of one or more electrons from a lipid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. lipid oxidation GO:0034478 The chemical reactions and pathways resulting in the breakdown of phosphatidylglycerols, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. The chemical reactions and pathways resulting in the breakdown of phosphatidylglycerols, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. phosphatidylglycerol breakdown phosphatidylglycerol catabolism phosphatidylglycerol degradation phosphatidylglycerol catabolic process The chemical reactions and pathways resulting in the breakdown of phosphatidylglycerols, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. GOC:mah GO:0034551 The aggregation, arrangement and bonding together of a set of components to form the cytochrome bc(1) complex (also known as ubiquinol-cytochrome c reductase), in the mitochondrial inner membrane. mitochondrial cytochrome bc(1) complex assembly mitochondrial respiratory chain complex III assembly GO:0034553 The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex II, in the mitochondrial inner membrane. mitochondrial respiratory chain complex II assembly GO:0034635 The directed movement of glutathione, the tripeptide glutamylcysteinylglycine, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. glutathione transport GO:0034638 The chemical reactions and pathways resulting in the breakdown of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. The chemical reactions and pathways resulting in the breakdown of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. phosphatidylcholine breakdown phosphatidylcholine catabolism phosphatidylcholine degradation phosphatidylcholine catabolic process The chemical reactions and pathways resulting in the breakdown of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. GOC:jp GO:0034976 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. ER stress response cellular response to endoplasmic reticulum stress response to ER stress response to endoplasmic reticulum stress GO:0035023 Any process that modulates the frequency, rate or extent of Rho protein signal transduction. regulation of Rho protein signal transduction GO:0035046 The directed movement of the male and female pronuclei towards each other prior to their fusion. pronuclear migration GO:0035047 The rotation of centrosomes and associated pronuclei in one-cell embryos such as those of Caenorhabditis elegans, occurring as a transition between pronuclear migration and pronuclear fusion. centrosomal and pronuclear rotation GO:0035189 A multiprotein complex containing a heterodimeric E2F transcription factor and a Retinoblastoma (Rb) family member. This complex is capable of repressing transcription of E2F-regulated genes in order to regulate cell cycle progression. retinoblastoma-E2F complex Rb-E2F complex A multiprotein complex containing a heterodimeric E2F transcription factor and a Retinoblastoma (Rb) family member. This complex is capable of repressing transcription of E2F-regulated genes in order to regulate cell cycle progression. PMID:14616073 GO:0035194 A posttranscriptional gene silencing pathway in which regulatory RNAs elicit silencing of specific target genes, either by mRNA destabilization or inhibition of translation. RNA interference RNAi Wikipedia:RNA_interference ncRNA-mediated post-transcriptional gene silencing regulatory ncRNA-mediated post-transcriptional gene silencing GO:0035195 Downregulation of gene expression through the action of microRNAs (miRNAs), endogenous 21-24 nucleotide small RNAs processed from stem-loop RNA precursors (pre-miRNAs). Once incorporated into a RNA-induced silencing complex (RISC), miRNAs can downregulate gene expression by either of two posttranscriptional mechanisms: endolytic cleavage of mRNA cleavage or translational repression, usually accompanied by poly-A tail shortening and subsequent degradation of the mRNA. Downregulation of gene expression through the action of microRNAs (miRNAs), endogenous 21-24 nucleotide small RNAs processed from stem-loop RNA precursors (pre-miRNAs). Once incorporated into a RNA-induced silencing complex (RISC), miRNAs can downregulate gene expression by either of two posttranscriptional mechanisms: endolytic cleavage of mRNA cleavage or translational repression, usually accompanied by poly-A tail shortening and subsequent degradation of the mRNA. gene silencing by miRNA Downregulation of gene expression through the action of microRNAs (miRNAs), endogenous 21-24 nucleotide small RNAs processed from stem-loop RNA precursors (pre-miRNAs). Once incorporated into a RNA-induced silencing complex (RISC), miRNAs can downregulate gene expression by either of two posttranscriptional mechanisms: endolytic cleavage of mRNA cleavage or translational repression, usually accompanied by poly-A tail shortening and subsequent degradation of the mRNA. PMID:14744438 PMID:15066275 PMID:23209154 GO:0035371 The growing (plus) end of a microtubule. In vitro, microtubules polymerize more quickly at the plus end than at the minus end. In vivo, microtubule growth occurs only at the plus end, and the plus end switches between periods of growth and shortening, a behavior known as dynamic instability. microtubule plus-end GO:0035397 Positive regulation of an adaptive immune response mediated via cytokine production by helper T cell. helper T cell enhancement of adaptive immune response GO:0035525 A heterodimer of NF-kappa B p50 and p65 subunits. Note that the p50 subunit is encoded by NFKB1 gene in human and the p65 subunit is encoded by the RELA gene in human. Similar nomenclature is used in other vertebrate species. The p50 subunit has a precursor form p105 in some publications. NF-kappaB p50/p65 complex GO:0035601 The removal of an acyl group, any group or radical of the form RCO- where R is an organic group, from a protein amino acid. protein deacylation GO:0035696 The migration of a monocyte from the blood vessels into the surrounding tissue. monocyte extravasation GO:0035710 The change in morphology and behavior of a CD4-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. CD4-positive, alpha-beta T cell activation GO:0035711 The change in morphology and behavior of a T-helper 1 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. T-helper 1 cell activation GO:0035712 The change in morphology and behavior of a T helper 2 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. T-helper 2 cell activation GO:0035722 A series of molecular signals initiated by the binding of interleukin-12 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. IL-12-mediated signaling pathway interleukin-12-mediated signaling pathway interleukin-12-mediated signaling pathway GO:0035733 A change in the morphology or behavior of a hepatic stellate cell resulting from exposure to a cytokine, chemokine, hormone, cellular ligand or soluble factor. hepatic stellate cell activation GO:0035739 The expansion of a CD4-positive, alpha-beta T cell population by cell division. CD4-positive, alpha-beta T cell proliferation GO:0035740 The expansion of a CD8-positive, alpha-beta T cell population by cell division. CD8-positive, alpha-beta T cell proliferation GO:0035743 Any process that contributes to cytokine production by a CD4-positive, alpha-beta T cell. CD4-positive, alpha-beta T cell cytokine production GO:0035744 Any process that contributes to cytokine production by a T-helper 1 cell. T-helper 1 cell cytokine production GO:0035745 Any process that contributes to cytokine production by a T-helper 1 cell. T-helper 2 cell cytokine production GO:0035747 The directed movement of a natural killer cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). natural killer cell chemotaxis GO:0035770 A non-membranous macromolecular complex containing proteins and translationally silenced mRNAs. RNA granules contain proteins that control the localization, stability, and translation of their RNA cargo. Different types of RNA granules (RGs) exist, depending on the cell type and cellular conditions. RNP granule mRNP granule RNA granule ribonucleoprotein granule GO:0035794 Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane. positive regulation of mitochondrial membrane permeability GO:0035825 A DNA recombination process that results in the exchange of an equal amount of genetic material between highly homologous DNA molecules. homologous recombination GO:0035890 The directed movement of an organism out of the body, tissues or cells of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. exit from host GO:0035891 The directed movement of an organism out of a cell of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. host cell exit ejection from host cell exit from host cell GO:0035915 The aggregation, arrangement and bonding together of a set of components by an organism to form a pore complex in a membrane of another organism. pore formation in membrane of other organism GO:0035985 A transcriptionally-silent heterochromatin structure present in senescent cells. Contains the condensed chromatin of one chromosome and is enriched for histone modifications. Thought to repress expression of proliferation-promoting genes. SAHF senescence-associated heterochromatin foci senescence-associated heterochromatin foci senescence-associated heterochromatin focus senescence-associated heterochromatin foci PMID:15621527 PMID:21248468 GO:0036037 The change in morphology and behavior of a CD8-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. CD8-positive, alpha-beta T cell activation GO:0036041 Interacting selectively and non-covalently with a long-chain fatty acid. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. long-chain fatty acid binding GO:0036042 Interacting selectively and non-covalently with a long-chain fatty acyl-CoA. A long-chain fatty acyl-CoA is any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more. long-chain fatty acyl-CoA binding GO:0036211 The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). protein modification process GO:0036337 A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription. Fas is a death domain-containing member of the tumor necrosis factor receptor (TNFR) superfamily. Fas signaling pathway GO:0036338 The lipid bilayer of a virion, a complete fully infectious extracellular virus particle. viral membrane GO:0036345 A developmental process, independent of morphogenetic (shape) change, that is required for a platelet to attain its fully functional state. A platelet is a non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation. platelet maturation GO:0036449 The end of a microtubule that does not preferentially grow (polymerize). microtubule minus-end GO:0036453 An RNA interference where the silencing signal spreads along the target mRNA in a 5' or 3' direction, outside of the initial target sequence. transitive RNAi transitive RNA interference GO:0036464 A ribonucleoprotein granule located in the cytoplasm. cytoplasmic ribonucleoprotein granule GO:0036498 A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB. A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB. UPR signaling by IRE1 stress sensor endoplasmic reticulum unfolded protein response; IRE1 signaling IRE1-mediated unfolded protein response A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB. PMID:22013210 GO:0036499 A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity. A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity. UPR signaling by PERK stress sensor endoplasmic reticulum unfolded protein response; PERK signaling PERK-mediated unfolded protein response A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity. PMID:22013210 GO:0036500 A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity. A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity. activating transcription factor 6 signaling in unfolded protein response endoplasmic reticulum unfolded protein response; ATF6 signaling ATF6-mediated unfolded protein response A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity. PMID:22013210 GO:0036503 The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. endoplasmic reticulum-associated degradation protein degradation by ERAD ER-associated protein degradation (ERAD) pathways target misfolded ER lumenal proteins (ERAD-L), ER membrane proteins (ERAD-M), and ER proteins with misfolded cytosolic domains (ERAD-C) by recognizing aberrant proteins, retrotranslocating these substrates to the cytosol, followed by substrate ubiquitination and proteosomal-mediated degradation. In contrast the stress-induced homeostatically regulated protein degradation (SHRED) pathway (GO:0120174), although inducible by stress, targets diverse ER membrane, and cytosolic proteins as well as numerous other native proteins in the absence of stress. Stress results in the protease-mediated (Nma111p) generation of a Roq1p cleavage product that then binds to the type-1 active site of Ubr1p, altering its substrate specificity, and leading to the proteasome-mediated degradation of both misfolded and native proteins. Although the SHRED pathway may contain some components in common with ERAD pathways (GO:0036503), such as UBR1, RAD6 and CDC48, other ERAD components, such as HRD1 and DOA10, do not appear to be involved, and as such these pathways are currently considered to be distinct. ERAD pathway The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. PMID:20940304 PMID:21969857 GO:0038001 The transfer of information from one cell to another, where the signal travels from the signal-producing cell to the receiving cell by passive diffusion or bulk flow in intercellular fluid. The signaling cell and the receiving cell are usually in the vicinity of each other. paracrine signaling GO:0038028 An insulin receptor signaling pathway in which the signal is transmitted via the phosphatidylinositol 3-kinase cascade. insulin receptor signaling pathway via phosphatidylinositol 3-kinase GO:0038066 An intracellular protein kinase cascade containing at least a p38 MAPK, a MAPKK and a MAP3K. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell. p38 cascade p38 signal transduction pathway p38 signaling cascade GO:0038094 A series of molecular signals initiated by the binding of the Fc portion of immunoglobulin G (IgG) to an Fc-gamma receptor on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region. Fc-gamma receptor signaling pathway GO:0038110 A series of molecular signals initiated by the binding of interleukin-2 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. IL-2-mediated signaling pathway interleukin-2-mediated signaling pathway GO:0038111 A series of molecular signals initiated by the binding of interleukin-7 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. IL-7-mediated signaling pathway interleukin-7-mediated signaling pathway interleukin-7-mediated signaling pathway GO:0038148 A series of molecular signals initiated by the binding of the C-C chemokine CCL2 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. CCL2-mediated signaling pathway chemokine (C-C motif) ligand 2 signaling pathway GO:0038201 A protein complex that contains at least TOR (target of rapamycin) in complex with other signaling components. Mediates the phosphorylation and activation of downstream signaling components including PKB (AKT) or S6K. TOR complex GO:0038202 A series of intracellular molecular signals mediated by TORC1; TOR (target of rapamycin) in complex with at least Raptor (regulatory-associated protein of TOR), or orthologs of, and other signaling components. TORC1 signaling GO:0038203 A series of intracellular molecular signals mediated by TORC2; TOR (rapamycin-insensitive companion of TOR) in complex with at least Rictor (regulatory-associated protein of TOR), or orthologs of, and other signaling components. TORC1 signaling GO:0039503 Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the innate immune response of the host organism, the host's first line of defense. suppression by virus of host innate immune response GO:0039528 Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. cytoplasmic pattern recognition receptor signaling pathway in response to virus GO:0039530 Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. MDA-5 signaling pathway GO:0039548 Any process in which a virus stops, prevents, or reduces the activity of host IRF3 (interferon regulatory factor-3), a transcription factor in the RIG-I/MDA-5 signaling pathway. Viral infection triggers phosphorylation of cytoplasmic IRF3, which allows IRF3 to form a homodimer, migrate to the nucleus, and activate transcription of IFN-alpha and IFN-beta genes. suppression by virus of host IRF3 activity GO:0039585 A series of reactions in which a signal is passed on to downstream proteins within the cell via PKR (also known as EIF2AK3), an intracellular protein kinase that is activated by stress signals or upon binding to double-stranded RNA (dsRNA), followed by autophosphorylation. PKR plays a role in the antiviral response, phosphorylating proteins such as the translation initiation factor eIF2 to inhibit protein synthesis during viral infection. Begins with activation of PKR activity, and ends with regulation of a downstream cellular process, e.g. regulation of transcription or inhibition of translation. PKR-mediated signaling GO:0039604 Any process in which a virus prevents or reduces the frequency, rate or extent of translation of host mRNA. suppression by virus of host translation GO:0039654 Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. fusion of virus membrane with host endosomal membrane fusion of virus membrane with host endosome membrane GO:0039663 Merging of the virion membrane and a host membrane (host plasma membrane or host organelle membrane) that is involved in the uptake of a virus into a host cell. membrane fusion involved in viral entry into host cell GO:0039664 The viral-induced lysis of an organelle (endosome, lysosome, or caveosome) that is involved in the uptake of a virus into a host cell. Occurs once the virus is within the organelle, and results in transfer of the viral contents from the organelle compartment into the cytoplasm. The viral-induced lysis of an organelle (endosome, lysosome, or caveosome) that is involved in the uptake of a virus into a host cell. Occurs once the virus is within the organelle, and results in transfer of the viral contents from the organelle compartment into the cytoplasm. VZ:984 viral penetration via lysis of host organellar membrane viral penetration via lysis of host organellar membrane viral entry into host cell via endosome membrane lysis viral entry into host cell via endosome membrane lysis viral entry into host cell via lysis of host organelle membrane viral membrane-lytic protein viral membrane-lytic protein lysis of host organelle involved in viral entry into host cell The viral-induced lysis of an organelle (endosome, lysosome, or caveosome) that is involved in the uptake of a virus into a host cell. Occurs once the virus is within the organelle, and results in transfer of the viral contents from the organelle compartment into the cytoplasm. UniProtKB-KW:KW-1174 VZ:984 VZ:984 Viral penetration via lysis of host organellar membrane viral penetration via lysis of host organellar membrane UniProtKB-KW:KW-984 viral entry into host cell via endosome membrane lysis VZ:984 viral membrane-lytic protein UniProtKB-KW:KW-1174 GO:0039665 Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm. Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm. VZ:985 viral penetration via perforation of host organellar membrane by virus viral penetration via perforation of host organellar membrane by virus viral entry into host cell via permeabilization of host organelle membrane viral membrane-penetration protein viral membrane-penetration protein permeabilization of host organelle membrane involved in viral entry into host cell Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm. UniProtKB-KW:KW-1173 VZ:985 VZ:985 Viral penetration via permeabilization of host organellar membrane viral penetration via perforation of host organellar membrane by virus UniProtKB-KW:KW-1173 viral membrane-penetration protein UniProtKB-KW:KW-1173 GO:0039674 The directed movement of the viral genome or a viral particle out of the host cell nucleus. The directed movement of the viral genome or a viral particle out of the host cell nucleus. VZ:2177 exit of virus from host cell nucleus The directed movement of the viral genome or a viral particle out of the host cell nucleus. VZ:2177 VZ:2177 Nuclear exit of viral genome GO:0039690 A viral genome replication process where the template genome is positive stranded, single stranded RNA ((+)ssRNA). Replication of the positive strand leads to dsRNA formation, which in turn is transcribed into positive single stranded RNA. positive stranded viral RNA replication GO:0039692 A viral genome replication where the template is single-stranded RNA (ssRNA), and which proceeds via a double stranded DNA (dsDNA) intermediate molecule. Viral genomic RNA is first reverse transcribed into dsDNA, which integrates into the host chromosomal DNA, where it is transcribed by host RNA polymerase II. single stranded viral RNA replication via double stranded DNA intermediate GO:0039696 A transcription process that uses viral RNA as a template. A transcription process that uses viral RNA as a template. RNA-templated viral transcription A transcription process that uses viral RNA as a template. GOC:bf GOC:jl GO:0039697 A viral transcription process that uses negative stranded (-) single stranded (ss) RNA as a template. A viral transcription process that uses negative stranded (-) single stranded (ss) RNA as a template. VZ:1096 negative stranded viral RNA transcription A viral transcription process that uses negative stranded (-) single stranded (ss) RNA as a template. VZ:1096 VZ:1096 Negative stranded RNA virus replication GO:0039701 The directed movement of the viral genome or a viral particle towards the cell periphery using host microtubules. Mostly used by viruses that replicate their genome near or in the nucleus to allows newly assembled viral progeny to reach the plasma membrane. VZ:1816 microtubule-dependent intracellular transport of viral material towards cell periphery GO:0039708 The assembly of a virus capsid that occurs in the nucleus. The assembly of large icosahedral shells for herpesviridae and adenoviridae requires structural proteins that act as chaperones for assembly. The assembly of a virus capsid that occurs in the nucleus. The assembly of large icosahedral shells for herpesviridae and adenoviridae requires structural proteins that act as chaperones for assembly. VZ:1516 nuclear capsid assembly The assembly of a virus capsid that occurs in the nucleus. The assembly of large icosahedral shells for herpesviridae and adenoviridae requires structural proteins that act as chaperones for assembly. VZ:1516 VZ:1516 Nuclear capsid assembly GO:0039709 The assembly of a virus capsid that occurs in the cytoplasm. The assembly of a virus capsid that occurs in the cytoplasm. VZ:1950 cytoplasmic capsid assembly The assembly of a virus capsid that occurs in the cytoplasm. VZ:1950 VZ:1950 Cytoplasmic capsid assembly/packaging GO:0039723 Any process in which a virus stops, prevents, or reduces the activity of the host serine/threonine kinase TBK1. suppression by virus of host TBK1 activity GO:0040007 The increase in size or mass of an entire organism, a part of an organism or a cell. growth GO:0040011 Self-propelled movement of a cell or organism from one location to another. locomotion GO:0040016 The first few specialized divisions of an activated animal egg. embryonic cleavage GO:0040029 Any process that modulates the frequency, rate or extent of gene expression; the process is mitotically or meiotically heritable, or is stably self-propagated in the cytoplasm of a resting cell, and does not entail a change in DNA sequence. epigenetic regulation of gene expression Any process that modulates the frequency, rate or extent of gene expression; the process is mitotically or meiotically heritable, or is stably self-propagated in the cytoplasm of a resting cell, and does not entail a change in DNA sequence. PMID:10521337 GO:0042025 A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction. host cell nucleus GO:0042026 The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. PMID:23637286 protein refolding GO:0042059 Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity. down regulation of epidermal growth factor receptor signaling pathway negative regulation of EGF receptor signaling pathway negative regulation of EGF receptor signalling pathway negative regulation of EGFR signaling pathway negative regulation of epidermal growth factor receptor signaling pathway negative regulation of epidermal growth factor receptor signaling pathway GO:0042060 The series of events that restore integrity to a damaged tissue, following an injury. wound healing GO:0042088 An immune response which is associated with resistance to intracellular bacteria, fungi, and protozoa, and pathological conditions such as arthritis, and which is typically orchestrated by the production of particular cytokines by T-helper 1 cells, most notably interferon-gamma, IL-2, and lymphotoxin. T-helper 1 type immune response GO:0042089 The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. cytokine anabolism cytokine biosynthesis cytokine formation cytokine biosynthetic process The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. ISBN:0198506732 ISBN:0198599471 GO:0042092 An immune response which is associated with resistance to extracellular organisms such as helminths and pathological conditions such as allergy, which is orchestrated by the production of particular cytokines, most notably IL-4, IL-5, IL-10, and IL-13, by any of a variety of cell types including T-helper 2 cells, eosinophils, basophils, mast cells, and nuocytes, resulting in enhanced production of certain antibody isotypes and other effects. T-helper 2 type immune response type 2 immune response GO:0042093 The process in which a relatively unspecialized thymocyte acquires specialized features of a T-helper cell. T-helper cell differentiation GO:0042098 The expansion of a T cell population by cell division. Follows T cell activation. The expansion of a T cell population by cell division. Follows T cell activation. T lymphocyte proliferation T-cell proliferation T-lymphocyte proliferation T cell proliferation The expansion of a T cell population by cell division. Follows T cell activation. GO:0042098 GO:0042100 The expansion of a B cell population by cell division. Follows B cell activation. The expansion of a B cell population by cell division. Follows B cell activation. B lymphocyte proliferation B-cell proliferation B-lymphocyte proliferation B cell proliferation The expansion of a B cell population by cell division. Follows B cell activation. GO:0042100 GO:0042110 The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. T cell activation GO:0042113 The change in morphology and behavior of a mature or immature B cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. B cell activation GO:0042116 A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. macrophage polarization macrophage activation GO:0042117 The change in morphology and behavior of a monocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. monocyte activation GO:0042158 The chemical reaction resulting in the formation of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids. lipoprotein anabolism lipoprotein biosynthesis lipoprotein biosynthetic process GO:0042177 Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. negative regulation of protein catabolic process GO:0042245 Any process that results in the repair of damaged RNA. RNA repair GO:0042246 The regrowth of lost or destroyed tissues. tissue regeneration GO:0042267 The directed killing of a target cell by a natural killer cell through the release of granules containing cytotoxic mediators or through the engagement of death receptors. natural killer cell mediated cytotoxicity GO:0042310 A decrease in the diameter of blood vessels, especially arteries, due to constriction of smooth muscle cells that line the vessels, and usually causing an increase in blood pressure. vasoconstriction GO:0042311 An increase in the internal diameter of blood vessels, especially arterioles or capillaries, due to relaxation of smooth muscle cells that line the vessels, and usually resulting in a decrease in blood pressure. vasodilation GO:0042445 The chemical reactions and pathways involving any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone. The chemical reactions and pathways involving any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone. hormone metabolism hormone metabolic process The chemical reactions and pathways involving any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone. CHEBI:24621 GO:0042571 GO:0042575 DNA polymerase complex A protein complex that possesses DNA polymerase activity and is involved in template directed synthesis of DNA. DNA polymerase complex GO:0042579 Cytoplasmic organelles, spherical or oval in shape, that are bounded by a single membrane and contain oxidative enzymes, especially those utilizing hydrogen peroxide (H2O2). microbody GO:0042590 The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules. antigen processing and presentation of exogenous peptide antigen via MHC class I GO:0042592 Any biological process involved in the maintenance of an internal steady state. homeostatic process GO:0042641 Any complex of actin, myosin, and accessory proteins. actomyosin GO:0042730 A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin. Wikipedia:Fibrinolysis fibrinolysis GO:0042773 The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP. ATP synthesis coupled electron transport GO:0042775 The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP, as it occurs in the mitochondrial inner membrane or chloroplast thylakoid membrane. The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP, as it occurs in the mitochondrial inner membrane or chloroplast thylakoid membrane. mitochondrial ATP synthesis coupled electron transport The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP, as it occurs in the mitochondrial inner membrane or chloroplast thylakoid membrane. ISBN:0716731363 GO:0042981 Any process that modulates the occurrence or rate of cell death by apoptotic process. Reactome:R-HSA-169911 regulation of apoptotic process Reactome:R-HSA-169911 http://www.reactome.org/content/detail/REACT_13648 GO:0043065 Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process. positive regulation of apoptotic process up regulation of apoptosis up-regulation of apoptosis upregulation of apoptosis activation of apoptosis pro-apoptosis positive regulation of apoptotic process GO:0043066 Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. GO:0043066 anti-apoptosis down regulation of apoptosis down-regulation of apoptosis downregulation of apoptosis inhibition of apoptosis negative regulation of apoptosis pro-survival negative regulation of apoptotic process GO:0043161 The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. proteasome-mediated ubiquitin-dependent protein catabolic process GO:0043186 A small cytoplasmic, non-membranous RNA/protein complex aggregate in the primordial germ cells of many higher eukaryotes. ISBN:0879695323 PMID:25050955 P granule ISBN:0879695323 P granules become localized in the posterior half of the embryo, concentrated around the cortex C. Elegans II Riddle, Donald GO:0043226 Organized structure of distinctive morphology and function. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton, and prokaryotic structures such as anammoxosomes and pirellulosomes. Excludes the plasma membrane. NIF_Subcellular:sao1539965131 Wikipedia:Organelle organelle GO:0043227 membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. membrane-bounded organelle GO:0043233 The internal volume enclosed by the membranes of a particular organelle; includes the volume enclosed by a single organelle membrane, e.g. endoplasmic reticulum lumen, or the volume enclosed by the innermost of the two lipid bilayers of an organelle envelope, e.g. nuclear lumen. organelle lumen GO:0043247 Any process that occur in response to the presence of critically short or damaged telomeres. telomere maintenance in response to DNA damage GO:0043266 Any process that modulates the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. regulation of potassium ion transport GO:0043267 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. negative regulation of potassium ion transport GO:0043268 Any process that activates or increases the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. positive regulation of potassium ion transport GO:0043276 Apoptosis triggered by inadequate or inappropriate adherence to substrate e.g. after disruption of the interactions between normal epithelial cells and the extracellular matrix. An adherent cell-restricted lethal cascade that is ignited by detachment from the matrix and that is characterized by (i) lack of beta1-integrin engagement, (ii) downregulation of EGFR expression, (iii) inhibition of extracellular-regulated kinase 1 (ERK1) signaling, and (iv) overexpression of the BCL-2 family member BIM. It should be noted that in most, if not all, instances, the cell death program ignited by anoikis is executed by the molecular machinery for intrinsic apoptosis. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252826/ Wikipedia:Anoikis anoikis GO:0043277 The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. apoptotic cell removal apoptotic cell clearance The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte. PMID:14685684 GO:0043316 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a cytotoxic T cell. cytotoxic T cell degranulation GO:0043320 The regulated exocytosis of secretory granules containing preformed mediators such as perforin and granzymes by a natural killer cell. natural killer cell degranulation GO:0043335 The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state. chaperone-mediated protein transport involved in chaperone-mediated autophagy subClassOf : has_part some protein unfolding protein unfolding GO:0043467 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and the processes involved in the liberation of energy from these substances. regulation of generation of precursor metabolites and energy GO:0043473 The aggregation of coloring matter in a particular location in an organism, tissue or cell, occurring in response to some external stimulus. accumulation of pigments GO:0043491 A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase B (also called AKT), which occurs as a result of a single trigger reaction or compound. PMID:20517722 GO:0043491 AKT signaling protein kinase B signaling pathway GO:0043543 The addition of an acyl group, any group or radical of the form RCO- where R is an organic group, to a protein amino acid. protein acylation GO:0043565 sequence-specific DNA binding Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. sequence-specific DNA binding GO:0044030 GO:0044167 The lipid bilayer surrounding the host cell endoplasmic reticulum. host cell endoplasmic reticulum membrane GO:0044178 The lipid bilayer surrounding any of the compartments of the host cell Golgi apparatus. host cell Golgi membrane GO:0044200 Either of the lipid bilayers that surround the host nucleus and form the nuclear envelope; excludes the intermembrane space. host cell nuclear membrane GO:0044281 Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides. The chemical reactions and pathways involving small molecules, any low molecular weight, monomeric, non-encoded molecule. small molecule metabolic process GO:0044342 The multiplication or reproduction of pancreatic B cells, resulting in the expansion of an pancreatic B cell population. Pancreatic B cell are cells of the pancreas that secrete insulin. type B pancreatic cell proliferation GO:0044381 The directed movement of the hexose monosaccharide glucose into a cell as a result of an insulin stimulus. glucose import in response to insulin stimulus GO:0044403 A process carried out by gene products in an organism that enable the organism to engage in a symbiotic relationship, a more or less intimate association, with another organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts. symbiotic process GO:0044565 The expansion of a dendritic cell population by cell division. A dendritic cell is a cell of hematopoietic origin, typically resident in particular tissues, specialized in the uptake, processing, and transport of antigens to lymph nodes for the purpose of stimulating an immune response via T cell activation. dendritic cell proliferation GO:0044659 The killing by a virus of a cell by means of the rupture of cell membranes and the loss of cytoplasm. The killing by a virus of a cell by means of the rupture of cell membranes and the loss of cytoplasm. https://github.com/geneontology/go-ontology/issues/18852 GO:0019077 GO:0046756 VZ:1077 lytic viral release viral exit from host cell by cytolysis viral release by cell lysis viral release by host cell lysis cytolysis by virus of host cell lytic viral life cycle viral release from host cell by cytolysis The killing by a virus of a cell by means of the rupture of cell membranes and the loss of cytoplasm. GOC:jl PMID:26728778 VZ:1077 Cell lysis GO:0044662 A process by which a virus has a negative effect on the functioning of a host cellular membrane. disruption by virus of host cell membrane GO:0044694 Injection by a non-enveloped virus of the viral genome into the host cytoplasm through creation of a pore or channel in the host cell membrane(s). Usually mediated by a viral pore-forming peptide associated with the viral capsid or bacteriophage tail. pore-mediated entry of viral genome into host cell GO:0044770 The cell cycle process by which a cell commits to entering the next cell cycle phase. cell cycle transition cell cycle phase transition GO:0044786 The DNA-dependent DNA replication that takes place as part of the cell cycle. cell cycle DNA replication GO:0044818 Mitotic G2/M transition checkpoint is a subtype of negative regulation of G2/M transition of mitotic cell cycle: A cell cycle checkpoint that detects and negatively regulates progression from G2 to M phase as part of a mitotic cell cycle. mitotic G2/M transition checkpoint GO:0044826 The insertion into a host genome of viral DNA, usually by the action of an integrase enzyme. Once integrated, the provirus persists in the host cell and serves as a template for the transcription of viral genes and replication of the viral genome, leading to the production of new viruses. The insertion into a host genome of viral DNA, usually by the action of an integrase enzyme. Once integrated, the provirus persists in the host cell and serves as a template for the transcription of viral genes and replication of the viral genome, leading to the production of new viruses. viral genome integration viral genome integration into host DNA The insertion into a host genome of viral DNA, usually by the action of an integrase enzyme. Once integrated, the provirus persists in the host cell and serves as a template for the transcription of viral genes and replication of the viral genome, leading to the production of new viruses. PMID:19091057 GO:0044838 A specialized resting state that cells enter in response to cues from the cell's environment. Quiescence is characterized by the absence of cell growth and division, by a reprogramming of global gene expression, and by changes characteristic of the organism and specific cell type. Depending on external conditions, quiescence may persist until cell death or cells may resume cell growth and division. In some cell types or under certain conditions, cellular metabolism may proceed. G0 phase cell quiescence GO:0044839 The cell cycle process by which a cell in G2 phase commits to M phase. cell cycle G2/M phase transition GO:0044843 The cell cycle process by which a cell in G1 phase commits to S phase. cell cycle G1/S phase transition GO:0045063 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 1 (Th1) cell. A Th1 cell is a CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive and produces interferon-gamma. T-helper 1 cell differentiation GO:0045065 The process in which a relatively unspecialized T cell acquires specialized features of a cytotoxic T cell. cytotoxic T lymphocyte selection cytotoxic T cell differentiation GO:0045070 Any process that activates or increases the frequency, rate or extent of viral genome replication. positive regulation of viral genome replication GO:0045071 Negative regulation of positive stranded viral RNA replication is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication. negative regulation of viral genome replication GO:0045087 Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. innate immunity innate immune response GO:0045088 Any process that modulates the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection. regulation of innate immune response GO:0045089 Any process that activates or increases the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection. positive regulation of innate immune response GO:0045120 The nucleus of either the ovum or the spermatozoon following fertilization. Thus, in the fertilized ovum, there are two pronuclei, one originating from the ovum, the other from the spermatozoon that brought about fertilization; they approach each other, but do not fuse until just before the first cleavage, when each pronucleus loses its membrane to release its contents. pronucleus GO:0045123 The migration of a leukocyte from the blood vessels into the surrounding tissue. Wikipedia:Inflammation Wikipedia:Leukocyte_extravasation immune cell cellular extravasation leucocyte cellular extravasation transendothelial leukocyte migration cellular extravasation Wikipedia:Inflammation At the onset of an infection, burn, or other injuries, these cells undergo activation (one of the PRRs recognize a PAMP or DAMP) and release inflammatory mediators responsible for the clinical signs of inflammation. Vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor). Increased permeability of the blood vessels results in an exudation (leakage) of plasma proteins and fluid into the tissue (edema), which manifests itself as swelling (tumor). Some of the released mediators such as bradykinin increase the sensitivity to pain (hyperalgesia, dolor). The mediator molecules also alter the blood vessels to permit the migration of leukocytes, mainly neutrophils and macrophages, outside of the blood vessels (extravasation) into the tissue. The neutrophils migrate along a chemotactic gradient created by the local cells to reach the site of injury. GO:0045132 The process in which genetic material, in the form of chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets during M phase of the meiotic cell cycle. meiotic chromosome segregation GO:0045165 The cellular developmental process by which a cell establishes the intrinsic character of a cell or tissue region irreversibly committing it to a particular fate. cell fate commitment GO:0045167 Any process in which a protein is transported to, or maintained in, a specific asymmetric distribution, resulting in the formation of daughter cells of different types. asymmetric protein localization involved in cell fate determination GO:0045185 Any process in which a protein is maintained in a location and prevented from moving elsewhere. These include sequestration, stabilization to prevent transport elsewhere and the active retrieval of proteins that do move away. maintenance of protein location GO:0045190 The switching of activated B cells from IgM biosynthesis to biosynthesis of other isotypes of immunoglobulin, accomplished through a recombination process involving an intrachromosomal deletion involving switch regions that reside 5' of each constant region gene segment in the immunoglobulin heavy chain locus. isotype switching GO:0045234 The covalent attachment of a palmitoleyl group to a protein. protein palmitoleylation GO:0045321 A change in morphology and behavior of a leukocyte resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor. immune cell activation leucocyte activation leukocyte activation GO:0045341 The chemical reactions and pathways resulting in the formation of major histocompatibility protein class I. MHC class I biosynthetic process GO:0045342 The chemical reactions and pathways resulting in the formation of major histocompatibility protein class II. MHC class II biosynthetic process GO:0045345 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class I. positive regulation of MHC class I biosynthetic process GO:0045444 The process whereby a relatively unspecialized cell acquires specialized features of an adipocyte, an animal connective tissue cell specialized for the synthesis and storage of fat. adipocyte cell differentiation adipose cell differentiation fat cell differentiation Adipocyte differentiation GO:0045445 The process in which a relatively unspecialized cell acquires specialized features of a myoblast. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into striated muscle fibers. myoblast cell differentiation myoblast differentiation GO:0045446 The process in which a mesodermal, bone marrow or neural crest cell acquires specialized features of an endothelial cell, a thin flattened cell. A layer of such cells lines the inside surfaces of body cavities, blood vessels, and lymph vessels, making up the endothelium. endothelial cell differentiation GO:0045448 The eukaryotic cell cycle in which a cell is duplicated without changing ploidy, occurring in the embryo. mitotic cell cycle, embryonic GO:0045582 Any process that activates or increases the frequency, rate or extent of T cell differentiation. positive regulation of T cell differentiation GO:0045595 Any process that modulates the frequency, rate or extent of cell differentiation, the process in which relatively unspecialized cells acquire specialized structural and functional features. regulation of cell differentiation GO:0045721 Any process that stops, prevents, or reduces the frequency, rate or extent of gluconeogenesis. down regulation of gluconeogenesis down-regulation of gluconeogenesis downregulation of gluconeogenesis negative regulation of gluconeogenesis GO:0045738 Negative regulation of DNA repair is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of DNA repair. negative regulation of DNA repair GO:0045786 Negative regulation of cell cycle is a subtype of negative regulation process: Any process that stops, prevents or reduces the rate or extent of progression through the cell cycle. negative regulation of cell cycle GO:0045787 Any process that activates or increases the rate or extent of progression through the cell cycle. positive regulation of cell cycle progression positive regulation of progression through cell cycle positive regulation of cell cycle GO:0045806 Any process that stops, prevents, or reduces the frequency, rate or extent of endocytosis. negative regulation of endocytosis GO:0045820 Any process that stops, prevents, or reduces the frequency, rate or extent of glycolysis. down regulation of glycolysis down-regulation of glycolysis downregulation of glycolysis negative regulation of glycolytic process GO:0045830 Any process that activates or increases the frequency, rate or extent of isotype switching. positive regulation of isotype switching GO:0045862 Any process that activates or increases the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein. positive regulation of proteolysis GO:0045892 Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. down regulation of transcription, DNA-dependent down-regulation of transcription, DNA-dependent negative regulation of transcription, DNA-templated GO:0045927 Any process that activates or increases the rate or extent of growth, the increase in size or mass of all or part of an organism. positive regulation of growth GO:0046034 The chemical reactions and pathways involving ATP, adenosine triphosphate, a universally important coenzyme and enzyme regulator. ATP metabolic process GO:0046222 The chemical reactions and pathways involving aflatoxin, a fungal metabolite found as a contaminant in moldy grains that induces liver cancer. Aflatoxin induces a G to T transversion at codon 249 of p53, leading to its inactivation. Aflatoxin is converted to a chemical carcinogen by P450. aflatoxin metabolism aflatoxin metabolic process GO:0046338 The chemical reactions and pathways resulting in the breakdown of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. The chemical reactions and pathways resulting in the breakdown of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. phosphatidylethanolamine breakdown phosphatidylethanolamine catabolism phosphatidylethanolamine degradation phosphatidylethanolamine catabolic process The chemical reactions and pathways resulting in the breakdown of phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. ISBN:0198506732 GO:0046470 The chemical reactions and pathways involving phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. They are important constituents of cell membranes. The chemical reactions and pathways involving phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. They are important constituents of cell membranes. phosphatidylcholine metabolism phosphatidylcholine metabolic process The chemical reactions and pathways involving phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. They are important constituents of cell membranes. ISBN:0198506732 GO:0046471 The chemical reactions and pathways involving phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. They are important constituents of cell membranes. The chemical reactions and pathways involving phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. They are important constituents of cell membranes. phosphatidylglycerol metabolism phosphatidylglycerol metabolic process The chemical reactions and pathways involving phosphatidylglycerols, any of a class of phospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol. They are important constituents of cell membranes. ISBN:0198506732 GO:0046473 The chemical reactions and pathways involving phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. The chemical reactions and pathways involving phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. phosphatidic acid metabolism phosphatidic acid metabolic process The chemical reactions and pathways involving phosphatidic acid, any derivative of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. ISBN:0198506732 GO:0046474 The chemical reactions and pathways resulting in the formation of glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. The chemical reactions and pathways resulting in the formation of glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. glycerophospholipid anabolism glycerophospholipid biosynthesis glycerophospholipid formation glycerophospholipid synthesis phosphoglyceride biosynthesis phosphoglyceride biosynthetic process glycerophospholipid biosynthetic process The chemical reactions and pathways resulting in the formation of glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. ISBN:0198506732 GO:0046475 The chemical reactions and pathways resulting in the breakdown of glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. The chemical reactions and pathways resulting in the breakdown of glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. glycerophospholipid breakdown glycerophospholipid catabolism glycerophospholipid degradation phosphoglyceride catabolic process phosphoglyceride catabolism glycerophospholipid catabolic process The chemical reactions and pathways resulting in the breakdown of glycerophospholipids, any derivative of glycerophosphate that contains at least one O-acyl, O-alkyl, or O-alkenyl group attached to the glycerol residue. ISBN:0198506732 GO:0046488 The chemical reactions and pathways involving phosphatidylinositol, any glycophospholipid in which a sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. The chemical reactions and pathways involving phosphatidylinositol, any glycophospholipid in which a sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. PtdIns metabolic process PtdIns metabolism phosphatidylinositol metabolism phosphoinositide metabolic process phosphoinositide metabolism phosphatidylinositol metabolic process The chemical reactions and pathways involving phosphatidylinositol, any glycophospholipid in which a sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. CHEBI:28874 ISBN:0198506732 GO:0046513 The chemical reactions and pathways resulting in the formation of ceramides, any N-acylated sphingoid. ceramide anabolism ceramide biosynthesis ceramide formation ceramide synthesis ceramide biosynthetic process GO:0046514 The chemical reactions and pathways resulting in the breakdown of ceramides, any N-acetylated sphingoid. catabolosm ceramide breakedown ceramide degradation ceramide catabolic process GO:0046597 Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell. negative regulation of viral entry into host cell GO:0046618 The directed movement of a drug, a substance used in the diagnosis, treatment or prevention of a disease, out of a cell or organelle. drug export GO:0046649 A change in morphology and behavior of a lymphocyte resulting from exposure to a specific antigen, mitogen, cytokine, chemokine, cellular ligand, or soluble factor. http://purl.obolibrary.org/obo/IEV_0003879 lymphocyte activation GO:0046651 The expansion of a lymphocyte population by cell division. lymphocyte proliferation GO:0046676 Any process that stops, prevents, or reduces the frequency, rate or extent of the release of insulin. negative regulation of insulin secretion GO:0046693 The retention of sperm by a female following mating. retention of sperm sequestering of sperm sequestration of sperm sperm retention sperm sequestering sperm sequestration storage of sperm sperm storage GO:0046718 The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. GO terms are based on the viral side viewpoint. So, it is a part of viral life cycle. viral entry into host cell GO:0046740 The transport of a virus between adjacent cells in a multicellular organism. VZ:1018 cell to cell spread of virus within host intercellular virus transport transport of virus in host (cell to cell) GO:0046741 The transport of a virus between tissues in a multicellular organism. spread of virus within host, tissue to tissue tissue to tissue spread of virus within host transport of virus in host, tissue to tissue GO:0046753 The exit of a viral particle from a cell that does not involve cell lysis. The exit of a viral particle from a cell that does not involve cell lysis. https://github.com/geneontology/go-ontology/issues/18852 non-lytic viral release The exit of a viral particle from a cell that does not involve cell lysis. ISBN:0072370319 GO:0046754 The exit of enveloped or unenveloped virion particles from the host cell by exocytosis, without causing cell lysis. The exit of enveloped or unenveloped virion particles from the host cell by exocytosis, without causing cell lysis. viral exocytosis The exit of enveloped or unenveloped virion particles from the host cell by exocytosis, without causing cell lysis. ISBN:0072370319 GO:0046755 A viral process by which enveloped viruses acquire a host-derived membrane enriched in viral proteins to form their external envelope. The process starts when nucleocapsids, assembled or in the process of being built, induce formation of a membrane curvature in the host plasma or organelle membrane and wrap up in the forming bud. The process ends when the bud is eventually pinched off by membrane scission to release the enveloped particle into the lumenal or extracellular space. A viral process by which enveloped viruses acquire a host-derived membrane enriched in viral proteins to form their external envelope. The process starts when nucleocapsids, assembled or in the process of being built, induce formation of a membrane curvature in the host plasma or organelle membrane and wrap up in the forming bud. The process ends when the bud is eventually pinched off by membrane scission to release the enveloped particle into the lumenal or extracellular space. GO:0046744 VZ:1947 virion budding viral capsid envelopment virus budding viral budding A viral process by which enveloped viruses acquire a host-derived membrane enriched in viral proteins to form their external envelope. The process starts when nucleocapsids, assembled or in the process of being built, induce formation of a membrane curvature in the host plasma or organelle membrane and wrap up in the forming bud. The process ends when the bud is eventually pinched off by membrane scission to release the enveloped particle into the lumenal or extracellular space. ISBN:0781718325 VZ:1947 VZ:1947 Viral budding GO:0046760 A viral budding that starts with formation of a membrane curvature in the host Golgi membrane. A viral budding that starts with formation of a membrane curvature in the host Golgi membrane. GO:0046750 GO:0046763 Golgi membrane viral budding virus budding from Golgi membrane Golgi membrane viral budding during viral capsid envelopment viral budding from Golgi membrane by viral capsid envelopment viral budding from Golgi membrane during viral capsid envelopment virus budding from Golgi membrane by viral capsid envelopment virus budding from Golgi membrane during viral capsid envelopment virus budding from Golgi membrane during viral capsid envelopment viral budding from Golgi membrane A viral budding that starts with formation of a membrane curvature in the host Golgi membrane. GOC:bf ISBN:0072370319 VZ:1947 virus budding from Golgi membrane during viral capsid envelopment GOC:tb GO:0046761 A viral budding that starts with formation of a membrane curvature in the host plasma membrane. A viral budding that starts with formation of a membrane curvature in the host plasma membrane. GO:0046766 GO:0046767 plasma membrane viral budding virus budding from plasma membrane virus budding from plasma membrane by viral capsid envelopment plasma membrane viral budding during viral capsid envelopment viral budding from plasma membrane by viral capsid envelopment viral budding from plasma membrane during viral capsid envelopment virus budding from plasma membrane during viral capsid envelopment virus budding from plasma membrane during viral capsid envelopment viral budding from plasma membrane A viral budding that starts with formation of a membrane curvature in the host plasma membrane. GOC:bf ISBN:0072370319 PMID:9394621 VZ:1947 virus budding from plasma membrane during viral capsid envelopment GOC:tb GO:0046762 A viral budding that starts with formation of a membrane curvature in the host ER membrane. A viral budding that starts with formation of a membrane curvature in the host ER membrane. GO:0046751 GO:0046764 ER membrane viral budding endoplasmic reticulum membrane viral budding viral budding from ER membrane virus budding from ER membrane virus budding from ER membrane by viral capsid envelopment ER membrane viral budding during viral capsid envelopment endoplasmic reticulum membrane viral budding during viral capsid envelopment viral budding from ER membrane by viral capsid envelopment viral budding from ER membrane during viral capsid envelopment virus budding from ER membrane during viral capsid envelopment virus budding from ER membrane during viral capsid envelopment viral budding from endoplasmic reticulum membrane A viral budding that starts with formation of a membrane curvature in the host ER membrane. GOC:bf GOC:jl ISBN:0072370319 VZ:1947 virus budding from ER membrane during viral capsid envelopment GOC:tb GO:0046765 A viral budding that starts with formation of a membrane curvature in the host nuclear membrane. A viral budding that starts with formation of a membrane curvature in the host nuclear membrane. GO:0046749 nuclear membrane viral budding virus budding from nuclear membrane virus budding from nuclear membrane by viral capsid envelopment nuclear membrane viral budding during viral capsid envelopment viral budding from nuclear membrane by viral capsid envelopment viral budding from nuclear membrane during viral capsid envelopment virus budding from nuclear membrane during viral capsid envelopment virus budding from nuclear membrane during viral capsid envelopment viral budding from nuclear membrane A viral budding that starts with formation of a membrane curvature in the host nuclear membrane. GOC:bf ISBN:0072370319 virus budding from nuclear membrane during viral capsid envelopment GOC:tb GO:0046777 The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). protein autophosphorylation GO:0046786 The process of organizing and assembling viral replication proteins in preparation for viral replication. The process of organizing and assembling viral replication proteins in preparation for viral replication. viral replication complex formation and maintenance The process of organizing and assembling viral replication proteins in preparation for viral replication. ISBN:0781718325 GO:0046789 Interacting selectively and non-covalently with a receptor on the host cell surface host cell surface receptor binding GO:0046790 Interacting selectively and non-covalently with a virion, either by binding to components of the capsid or the viral envelope. virion binding GO:0046794 The directed movement of a virus, or part of a virus, into, out of, or within a host cell. viral transport virion transport transport of virus GO:0046802 The directed movement of an assembled viral particle out of the host cell nucleus by budding and fusion through the nuclear membranes. In this process, enveloped viral particles are formed by budding through the inner nuclear membrane. These perinuclear enveloped particles then fuse with the outer nuclear membrane to deliver a naked capsid into the host cytoplasm The directed movement of an assembled viral particle out of the host cell nucleus by budding and fusion through the nuclear membranes. In this process, enveloped viral particles are formed by budding through the inner nuclear membrane. These perinuclear enveloped particles then fuse with the outer nuclear membrane to deliver a naked capsid into the host cytoplasm exit of virus from host cell nucleus by nuclear egress The directed movement of an assembled viral particle out of the host cell nucleus by budding and fusion through the nuclear membranes. In this process, enveloped viral particles are formed by budding through the inner nuclear membrane. These perinuclear enveloped particles then fuse with the outer nuclear membrane to deliver a naked capsid into the host cytoplasm PMID:21494278 PMID:22858153 PMID:9601512 PMID:9765421 GO:0046806 A complex of proteins that form a scaffold around which the viral capsid is constructed. viral scaffold GO:0046807 The assembly and maintenance of the viral scaffold around which the viral capsid is constructed. The assembly and maintenance of the viral scaffold around which the viral capsid is constructed. See also the cellular component term 'viral scaffold ; GO:0046806'. viral scaffold assembly and maintenance The assembly and maintenance of the viral scaffold around which the viral capsid is constructed. ISBN:0072370319 GO:0046812 Interacting selectively and non-covalently with the surface of a host cell. host cell surface binding GO:0046813 The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface. receptor-mediated virion attachment to host cell GO:0046816 A vesicle used to transport the partial or complete virion between cellular compartments. virion transport vesicle GO:0046889 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of lipids. positive regulation of lipid biosynthetic process GO:0046951 ketone body biosynthetic process is a subtype of generating: A process that synthesizes ketone body resulting in having output (s). ketone body biosynthetic process GO:0048012 The series of molecular signals generated as a consequence of the hepatocyte growth factor receptor binding to one of its physiological ligands. hepatocyte growth factor receptor signaling pathway HGFR signal transduction pathway GO:0048016 Any intracellular signal transduction in which the signal is passed on within the cell via an inositol phosphate. Includes production of the inositol phosphate, and downstream effectors that further transmit the signal within the cell. Inositol phosphates are a group of mono- to poly-phosphorylated inositols, and include inositol monophosphate (IP), inositol trisphosphate (IP3), inositol pentakisphosphate (IP5) and inositol hexaphosphate (IP6). inositol phosphate-mediated signaling pathway GO:0048193 The directed movement of substances into, out of or within the Golgi apparatus, mediated by vesicles. Golgi vesicle transport GO:0048246 The movement of a macrophage in response to an external stimulus. macrophage chemotaxis GO:0048285 The creation of two or more organelles by division of one organelle. organelle fission GO:0048291 The switching of activated B cells from IgM biosynthesis to biosynthesis of an IgG isotype, accomplished through a recombination process involving an intrachromosomal deletion between switch regions that reside 5' of the IgM and one of the IgG constant region gene segments in the immunoglobulin heavy chain locus. isotype switching to IgG isotypes GO:0048304 Any process that activates or increases the frequency, rate or extent of isotype switching to IgG isotypes. positive regulation of isotype switching to IgG isotypes GO:0048770 A small, subcellular membrane-bounded vesicle containing pigment and/or pigment precursor molecules. Pigment granule biogenesis is poorly understood, as pigment granules are derived from multiple sources including the endoplasmic reticulum, coated vesicles, lysosomes, and endosomes. pigment granule GO:0048771 The reorganization or renovation of existing tissues. This process can either change the characteristics of a tissue such as in blood vessel remodeling, or result in the dynamic equilibrium of a tissue such as in bone remodeling. tissue remodeling GO:0048856 The biological process whose specific outcome is the progression of an anatomical structure from an initial condition to its mature state. This process begins with the formation of the structure and ends with the mature structure, whatever form that may be including its natural destruction. An anatomical structure is any biological entity that occupies space and is distinguished from its surroundings. Anatomical structures can be macroscopic such as a carpel, or microscopic such as an acrosome. anatomical structure development GO:0048866 The process in which a cell becomes capable of differentiating autonomously into a stem cell in an environment that is neutral with respect to the developmental pathway. Upon specification, the cell fate can be reversed. stem cell fate specification GO:0048878 Any biological process involved in the maintenance of an internal steady state of a chemical. chemical homeostasis GO:0050663 The regulated release of cytokines from a cell. Cytokines are any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. The regulated release of cytokines from a cell. Cytokines are any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. cytokine secretion The regulated release of cytokines from a cell. Cytokines are any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. ISBN:0198599471 GO:0050728 Negative regulation of inflammatory response is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of inflammatory response. negative regulation of inflammatory response HOIP_0002243 GO:0050729 Any process that activates or increases the frequency, rate or extent of the inflammatory response. positive regulation of inflammatory response GO:0050766 Any process that activates or increases the frequency, rate or extent of phagocytosis. positive regulation of phagocytosis GO:0050776 Any process that modulates the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus. regulation of immune response GO:0050777 Any process that stops, prevents, or reduces the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus. Negative regulation of immune response GO:0050851 A series of molecular signals initiated by the cross-linking of an antigen receptor on a B or T cell. antigen receptor-mediated signaling pathway GO:0050852 A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell. TCR signaling pathway T cell receptor signaling pathway GO:0050853 A series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell. B cell receptor signaling pathway GO:0050865 Any process that modulates the frequency, rate or extent of cell activation, the change in the morphology or behavior of a cell resulting from exposure to an activating factor such as a cellular or soluble ligand. regulation of cell activation GO:0050866 Any process that stops, prevents, or reduces the frequency, rate or extent of cell activation. negative regulation of cell activation GO:0050867 Any process that activates or increases the frequency, rate or extent of cell activation. positive regulation of cell activation GO:0050870 Any process that activates or increases the frequency, rate or extent of T cell activation. positive regulation of T cell activation GO:0050871 Any process that activates or increases the frequency, rate or extent of B cell activation. positive regulation of B cell activation GO:0050878 Any process that modulates the levels of body fluids regulation of body fluid levels GO:0050896 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus. The process begins with detection of the stimulus and ends with a change in state or activity or the cell or organism. response to stimulus GO:0050900 The movement of a leukocyte within or between different tissues and organs of the body. The movement of a leukocyte within or between different tissues and organs of the body. immune cell migration immune cell trafficking leucocyte migration leucocyte trafficking leukocyte trafficking leukocyte migration The movement of a leukocyte within or between different tissues and organs of the body. ISBN:0781735149 PMID:14680625 PMID:14708592 PMID:7507411 PMID:8600538 GO:0050996 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of lipids. positive regulation of lipid catabolic process GO:0051049 Any process that modulates the frequency, rate or extent of the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. regulation of transport (biology) GO:0051055 Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of lipids. down regulation of lipid biosynthetic process down-regulation of lipid biosynthetic process downregulation of lipid biosynthetic process negative regulation of lipid anabolism negative regulation of lipid biosynthesis negative regulation of lipid formation negative regulation of lipid biosynthetic process GO:0051078 The cell cycle process in which the controlled breakdown of the nuclear membranes during meiotic cell division occurs. meiotic nuclear membrane disassembly GO:0051079 The controlled breakdown of the nuclear membranes during the first division of meiosis. meiosis I nuclear membrane disassembly GO:0051080 The controlled breakdown of the nuclear membranes during the second division of meiosis. meiosis II nuclear membrane disassembly GO:0051081 The controlled breakdown of the nuclear membranes, for example during cellular division. nuclear envelope breakdown nuclear envelope catabolism nuclear envelope degradation nuclear membrane disassembly HOIP_0050068 GO:0051132 The change in morphology and behavior of a mature or immature natural killer T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. NK T cell activation GO:0051168 The directed movement of substances out of the nucleus. The directed movement of substances out of the nucleus. export from nucleus nucleus export nuclear export The directed movement of substances out of the nucleus. GO:0051168 GO:0051169 The directed movement of substances into, out of, or within the nucleus. nucleus transport nuclear transport GO:0051170 The directed movement of substances into the nucleus. nuclear import nucleus import substance nuclear import import into nucleus GO:0051208 The process of binding or confining calcium ions such that they are separated from other components of a biological system. calcium ion (Ca2+) retention calcium ion (Ca2+) sequestering calcium ion (Ca2+) sequestration calcium ion (Ca2+) storage retention of calcium ion (Ca2+) sequestering of calcium ion (Ca2+) storage of calcium ion (Ca2+) sequestering of calcium ion GO:0051209 The process in which calcium ions sequestered in the endoplasmic reticulum, Golgi apparatus or mitochondria are released into the cytosolic compartment. release of sequestered calcium ion into cytosol GO:0051225 The aggregation, arrangement and bonding together of a set of components to form the spindle, the array of microtubules and associated molecules that serves to move duplicated chromosomes apart. spindle assembly GO:0051231 The cell cycle process in which the distance is lengthened between poles of the spindle. spindle elongation GO:0051232 The lengthening of the distance between poles of the spindle during a meiotic cell cycle. meiotic spindle elongation GO:0051234 Any process that localizes a substance or cellular component. This may occur via movement, tethering or selective degradation. establishment of localization GO:0051235 Any process in which a cell, substance or cellular entity, such as a protein complex or organelle, is maintained in a location and prevented from moving elsewhere. maintenance of location GO:0051258 The process of creating protein polymers, compounds composed of a large number of component monomers; polymeric proteins may be made up of different or identical monomers. Polymerization occurs by the addition of extra monomers to an existing poly- or oligomeric protein. protein polymerization GO:0051259 The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer. protein complex oligomerization GO:0051276 chromosome organization A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of chromosomes, structures composed of a very long molecule of DNA and associated proteins that carries hereditary information. This term covers covalent modifications at the molecular level as well as spatial relationships among the major components of a chromosome. chromosome organization GO:0051293 The directed movement of the spindle to a specific location in the cell. establishment of spindle localization GO:0051294 Any process that set the alignment of spindle relative to other cellular structures establishment of spindle orientation 2 GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. Wikipedia:Cell_division http://purl.obolibrary.org/obo/IEV_0003382　(obsolete) cell division GO:0051304 The cell cycle process in which paired chromosomes are detached from each other. Chromosome separation begins with the release of cohesin complexes from chromosomes; in budding yeast, this includes the cleavage of cohesin complexes along the chromosome arms, followed by the separation of the centromeric regions. Chromosome separation also includes formation of chromatid axes mediated by condensins, and ends with the disentangling of inter-sister catenation catalyzed by topoisomerase II (topo II). chromosome separation GO:0051305 The directed movement of chromosomes in the center of the spindle towards the spindle poles, mediated by the shortening of microtubules attached to the chromosomes. chromosome movement towards spindle pole GO:0051310 The alignment of chromosomes at the metaphase plate (spindle equator), a plane halfway between the poles of the spindle. metaphase plate congression GO:0051311 metaphase plate congression during meiosis meiotic metaphase plate congression GO:0051318 The cell cycle 'gap' phase which is the interval between the completion of DNA segregation (usually by mitosis or meiosis) and the beginning of DNA synthesis. MeSH:D016193 G1 phase GO:0051319 The cell cycle 'gap' phase which is the interval between the completion of DNA synthesis and the beginning of DNA segregation (usually by mitosis or meiosis). MeSH:D016195 PMID:24885854 Wikipedia:G2_phase Note that this term should not be used for direct annotation. If you are trying to make an annotation to x phase, it is likely that the correct annotation is 'regulation of x/y phase transition' or to a process which occurs during the reported phase (i.e mitotic DNA replication for mitotic S-phase). To capture the phase when a specific location or process is observed, the phase term can be used in an annotation extension (PMID:24885854) applied to a cellular component term (with the relation exists_during) or a biological process term (with the relation happens_during). G2 phase GO:0051320 The cell cycle phase, following G1, during which DNA synthesis takes place. MeSH:D016196 S phase GO:0051321 Progression through the phases of the meiotic cell cycle, in which canonically a cell replicates to produce four offspring with half the chromosomal content of the progenitor cell via two nuclear divisions. meiotic cell cycle GO:0051640 Any process in which an organelle is transported to, and/or maintained in, a specific location. organelle localization GO:0051642 Any process in which a centrosome is transported to, and/or maintained in, a specific location within the cell. centrosome localization GO:0051653 Any process in which is the spindle is transported to, and/or maintained in, a specific location. establishment and maintenance of spindle localization spindle localization GO:0051660 The directed movement of the centrosome to a specific location. establishment of centrosome localization GO:0051661 Any process in which a centrosome is maintained in a specific location within a cell and prevented from moving elsewhere. maintenance of centrosome location GO:0051726 Any process that modulates the rate or extent of progression through the cell cycle. cell cycle modulation cell cycle regulation control of cell cycle progression modulation of cell cycle progression regulation of cell cycle progression regulation of progression through cell cycle regulation of cell cycle GO:0051781 Any process that activates or increases the frequency, rate or extent of cell division. up regulation of cell division positive regulation of cell division GO:0051898 Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B. negative regulation of AKT signalling cascade negative regulation of PKB signaling cascade negative regulation of protein kinase B signaling negative regulation of protein kinase B signaling GO:0051918 Negative regulation of DNA repair is a subtype of negative regulation process: A process that stops, prevents, or reduces the frequency, rate or extent of fibrinolysis negative regulation of fibrinolysis GO:0052697 The modification of a xenobiotic substance by the conjugation of glucuronic acid. The resultant glucuronosides are often much more water-soluble than the xenobiotic precursor, enabling efficient excretion. xenobiotic glucuronidation GO:0055037 An organelle consisting of a network of tubules that functions in targeting molecules, such as receptors transporters and lipids, to the plasma membrane. endosomal recycling compartment ERC endosome recycling compartment recycling endosome GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. membrane transport Transmembrane transport requires transport of a solute across a lipid bilayer. Note that transport through the nuclear pore complex is not transmembrane because the nuclear membrane is a double membrane and is not traversed. For transport through the nuclear pore, consider instead the term 'nucleocytoplasmic transport ; GO:0006913' and its children. Note also that this term is not intended for use in annotating lateral movement within membranes. transmembrane transport GO:0055091 Any process involved in the maintenance of an internal steady state of phospholipid within an organism or cell. maintaining phospholipid homeostasis GO:0055114 A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. oxidation reduction oxidoreductase process oxidation-reduction process GO:0060250 A homeostatic process involved in the maintenance of an internal steady state within the germ-line stem-cell niche. This includes control of cellular proliferation and death and control of metabolic function that allows the niche to continue to function. A gem-line stem-cell niche is an anatomical structure that regulates how germ-line stem-cells are used and saves them from depletion germ-line stem-cell niche homeostasis GO:0060290 The conversion of a differentiated cell of one fate into a differentiated cell of another fate without first undergoing cell division or reversion to a more primitive or stem cell-like fate. Wikipedia:Transdifferentiation Transdifferentiation GO:0060337 A series of molecular signals initiated by the binding of a type I interferon to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. type I interferon-activated signaling pathway type I interferon-mediated signalling pathway type I interferon signaling pathway GO:0060395 The cascade of processes by which a signal interacts with a receptor, causing a change in the activity of a SMAD protein, and ultimately effecting a change in the functioning of the cell. SMAD protein signal transduction pathway GO:0060697 Any process that increases the rate, frequency, or extent of phospholipid catabolism, the chemical reactions and pathways resulting in the breakdown of phospholipids, any lipid containing phosphoric acid as a mono- or diester. positive regulation of phospholipid catabolic process GO:0061024 A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins. cellular membrane organisation membrane organization GO:0061025 The membrane organization process that joins two lipid bilayers to form a single membrane. membrane fusion GO:0061028 The establishment of a barrier between endothelial cell layers, such as those in the brain, lung or intestine, to exert specific and selective control over the passage of water and solutes, thus allowing formation and maintenance of compartments that differ in fluid and solute composition. establishment of endothelial barrier GO:0061470 The process in which a relatively unspecialized T cell acquires specialized features of a mature T follicular helper cell. T follicular helper cell differentiation GO:0061702 A cytosolic protein complex that is capable of activating caspase-1. inflammasome complex GO:0061736 The membrane invagination process by which an autophagosomal membrane surrounds an object that will be degraded by macroautophagy. engulfment of target by autophagosome GO:0061802 The region that lies just beneath the plasma membrane in the part of a cell that is closest to the anterior as defined by the developing, or existing, anterior/posterior axis. anterior cell cortex GO:0061803 The region that lies just beneath the plasma membrane in the part of a cell that is closest to the posterior as defined by the developing, or existing, anterior/posterior axis. posterior cell cortex GO:0061867 The mitotic spindle organization process by which a mitotic spindle becomes asymmetric either in position or structure. establishment of mitotic spindle asymmetry GO:0062093 The selective autophagy process in which a damaged lysosome is degraded by macroautophagy. lysophagy GO:0065001 The pattern specification process in which the polarity of a body or organ axis is established and maintained. specification of axis polarity GO:0065003 The aggregation, arrangement and bonding together of a set of macromolecules to form a complex. macromolecular complex assembly protein-containing complex assembly GO:0065005 The aggregation, arrangement and bonding together of proteins and lipids to form a protein-lipid complex. protein-lipid complex assembly GO:0070051 Interacting selectively and non-covalently with fibrinogen, a highly soluble hexameric glycoprotein complex that is found in blood plasma and is converted to fibrin by thrombin in the coagulation cascade. fibrinogen binding GO:0070085 The covalent attachment and further modification of carbohydrate residues to a substrate molecule. glycosylation GO:0070090 The intracellular plane, located halfway between the poles of the spindle, where chromosomes align during metaphase of mitotic or meiotic nuclear division. metaphase plate GO:0070098 A series of molecular signals initiated by the binding of a chemokine to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. chemokine-mediated signaling pathway GO:0070102 A series of molecular signals initiated by the binding of interleukin-6 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. IL-6-mediated signaling pathway interleukin-6-mediated signalling pathway interleukin-6-mediated signaling pathway GO:0070246 Any apoptotic process in a natural killer cell, a lymphocyte that can spontaneously kill a variety of target cells without prior antigenic activation. natural killer cell apoptotic process GO:0070265 A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. cellular necrosis Note that the word necrosis has been widely used in earlier literature to describe forms of cell death which are now known by more precise terms, such as apoptosis. Necrosis can occur in a regulated fashion, involving a precise sequence of signals; in this case, consider annotating to GO:0097300 'programmed necrotic cell death' or to its more specific child GO:0070266 'necroptotic process'. necrosis A type of cell death that is morphologically characterized by an increasingly translucent cytoplasm, swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. Necrotic cells do not fragment into discrete corpses as their apoptotic counterparts do. Moreover, their nuclei remain intact and can aggregate and accumulate in necrotic tissues. PMID:18846107 PMID:20823910 GO:0070269 A caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18. PMID: 21760595 PMID:18846107 PMID:21760595 pyroptosis PMID: 21760595 The term ‘pyroptosis' has been introduced in 2000 by Brennan and Cookson to functionally describe the peculiar death of macrophages infected by Salmonella typhimurium. Several other bacterial triggers of this atypical cell death modality have been identified, including Shigella flexneri, Listeria monocytogenes, Pseudomonas aeruginosa, Francisella tularensis and the Bacillus anthracis. However, it has become clear that pyroptosis neither constitutes a macrophage-specific process nor a cell death subroutine that only results from bacterial infection. Of note, pyroptotic cells can exhibit apoptotic and/or necrotic morphological features. GO:0070293 A renal system process in which water, ions, glucose and proteins are taken up from the collecting ducts, glomerulus and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures. renal absorption GO:0070300 Interacting selectively and non-covalently with phosphatidic acid, any of a class of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. Interacting selectively and non-covalently with phosphatidic acid, any of a class of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. GO:0070300 phosphatidic acid binding Interacting selectively and non-covalently with phosphatidic acid, any of a class of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. CHEBI:16337 GO:0070314 A cell cycle arrest process that results in arrest during G1 phase, whereupon the cell enters a specialized resting state known as G0 or quiescence. establishment of cell quiescence G1 to G0 transition GO:0070493 The series of molecular signals generated as a consequence of a thrombin-activated receptor binding to one of its physiological ligands. thrombin-activated receptor signaling pathway GO:0070498 A series of molecular signals initiated by the binding of interleukin-1 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. IL-1-mediated signaling pathway interleukin-1-mediated signaling pathway IL-1 signal transduction pathway GO:0070527 The adhesion of one platelet to one or more other platelets via adhesion molecules. platelet aggregation GO:0070646 A protein modification process in which one or more covalently attached groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are removed from a target protein. protein modification by small protein removal GO:0070647 A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to or removed from a target protein. protein modification by small protein conjugation or removal GO:0070679 Interacting selectively and non-covalently with inositol 1,4,5 trisphosphate. inositol 1,4,5 trisphosphate binding GO:0070942 The directed killing of a target cell by a neutrophil. neutrophil mediated cytotoxicity GO:0070988 The process of removing one or more methyl groups from a molecule. demethylation GO:0071073 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of phospholipids. positive regulation of phospholipid biosynthetic process GO:0071141 A protein complex that consists of only SMAD proteins; may be homomeric or heteromeric. Heteromeric complexes act as transcription factors while homomeric complexes exist but are transcriptionally inactive. Hetero- versus homotrimerization is largely enthalpy driven. SMAD protein complex GO:0071357 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. cellular response to type I interferon GO:0071495 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus arising within the organism. cellular response to endogenous stimulus GO:0071604 transforming growth factor beta production The appearance of any member of the transforming growth factor-beta family of cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Transforming growth factor-beta family members include TGF-B1, TGF-B2, and TGF-B3. transforming growth factor beta production GO:0071605 The appearance of chemokine (C-C motif) ligand 2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. CCL2 production MCP-1 production monocyte chemotactic protein-1 production chemokine (C-C motif) ligand 2 production GO:0071606 chemokine (C-C motif) ligand 4 production The appearance of chemokine (C-C motif) ligand 4 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. chemokine (C-C motif) ligand 4 production GO:0071608 The appearance of chemokine (C-C motif) ligand 3 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. CCL3 production MIP-1alpha production Macrophage Inframmatory Protein-1 alpha production chemokine (C-C motif) ligand 3 production GO:0071610 The appearance of chemokine (C-C motif) ligand 1 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. CCL1 production T cell activation 3 production TCA-3 production chemokine (C-C motif) ligand 1 production GO:0071611 The appearance of granulocyte colony-stimulating factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. G-CSF production granulocyte colony-stimulating factor production HOIP_0040351 GO:0071612 The appearance of chemokine (C-C motif) ligand 10 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. IP-10 production chemokine (C-C motif) ligand 10 production GO:0071706 tumor necrosis factor superfamily cytokine production The appearance of any member of the TNF superfamily due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. tumor necrosis factor superfamily cytokine production GO:0071712 The chemical reactions and pathways resulting in the breakdown of misfolded proteins transported from the endoplasmic reticulum and targeted to cytoplasmic proteasomes for degradation. ER-associated misfolded protein breakdown ER-associated misfolded protein catabolism ER-associated misfolded protein degradation endoplasmic reticulum-associated misfolded protein catabolic process endoplasmic reticulum-associated misfolded protein catabolism endoplasmic reticulum-associated degradation GO:0071731 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nitric oxide stimulus. response to nitric oxide GO:0071840 A process that results in the biosynthesis of constituent macromolecules, assembly, arrangement of constituent parts, or disassembly of a cellular component. cellular component organization or biogenesis GO:0071887 Any apoptotic process in a leukocyte, an achromatic cell of the myeloid or lymphoid lineages capable of ameboid movement, found in blood or other tissue leukocyte apoptotic process GO:0071888 Any apoptotic process in a macrophage, a mononuclear phagocyte present in a variety of tissues. macrophage apoptotic process GO:0071897 The cellular DNA metabolic process resulting in the formation of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one. DNA anabolism DNA biosynthesis DNA formation DNA synthesis DNA biosynthetic process GO:0071944 The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures. cell periphery GO:0072331 A series of molecular signals transduced with the regulation of transcription of target genes by p53. signal transduction by p53 class mediator GO:0072377 A protein activation cascade that contributes to blood coagulation and consists of events leading from the formation of activated factor X to the formation of active thrombin, the cleavage of fibrinogen by thrombin, and the formation of cleaved fibrin into a stable multimeric, cross-linked complex. blood coagulation, common pathway GO:0072378 A protein activation cascade that contributes to blood coagulation and consists of the cascade of enzymatic reactions initiated by physical damage to the wall of a blood vessel, leading to the formation of a formation of a fibrin clot at the site of the injury. The process also includes numerous positive and negative regulatory events. blood coagulation, fibrin clot formation GO:0072539 The process in which a relatively unspecialized T cell acquires the specialized features of a T-helper 17 (Th17) cell. A Th17 cell is a CD4-positive, alpha-beta T cell with the phenotype RORgamma-t-positive that produces IL-17. T-helper 17 cell differentiation GO:0072574 The multiplication or reproduction of hepatocytes, resulting in the expansion of a cell population. Hepatocytes form the main structural component of the liver. They are specialized epithelial cells that are organized into interconnected plates called lobules. hepatocellular hyperplasia hepatocyte proliferation GO:0072583 An endocytosis process that begins when material is taken up into clathrin-coated pits, which then pinch off to form clathrin-coated endocytic vesicles. An endocytosis process that begins when material is taken up into clathrin-coated pits, which then pinch off to form clathrin-coated endocytic vesicles. cathrin-dependent endocytosis An endocytosis process that begins when material is taken up into clathrin-coated pits, which then pinch off to form clathrin-coated endocytic vesicles. PMID:18498251 PMID:8970738 PMID:9234965 GO:0072584 An endocytosis process that begins when material is taken up into plasma membrane caveolae, which then pinch off to form endocytic caveolar carriers. An endocytosis process that begins when material is taken up into plasma membrane caveolae, which then pinch off to form endocytic caveolar carriers. caveolin-mediated endocytosis An endocytosis process that begins when material is taken up into plasma membrane caveolae, which then pinch off to form endocytic caveolar carriers. PMID:8970738 GO:0072672 The migration of a neutrophil from the blood vessels into the surrounding tissue. neutrophil extravasation GO:0072678 The movement of a T cell within or between different tissues and organs of the body. T cell migration GO:0072683 The migration of a T cell from the blood vessels into the surrounding tissue. T cell extravasation GO:0072697 A process in which a protein is transported to, or maintained in, the cell cortex. protein localization to cell cortex GO:0075502 Induction of endosome membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with the capsid. Occurs after internalization of the virus through the endosomal pathway, and results in delivery of the virus contents into the host cell cytoplasm. Induction of endosome membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with the capsid. Occurs after internalization of the virus through the endosomal pathway, and results in delivery of the virus contents into the host cell cytoplasm. GO:0075518 viral entry into host cell via caveolae-mediated endocytosis followed by endosome membrane viral entry into host cell via caveolae-mediated endocytosis followed by endosome membrane viral entry into host cell via clathrin-mediated endocytosis followed by endosome membrane permeabilization viral entry into host cell via clathrin-mediated endocytosis followed by endosome membrane permeabilization endosome membrane permeabilization involved in viral entry into host cell Induction of endosome membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with the capsid. Occurs after internalization of the virus through the endosomal pathway, and results in delivery of the virus contents into the host cell cytoplasm. GOC:bf GOC:jl viral entry into host cell via caveolae-mediated endocytosis followed by endosome membrane GOC:bf GOC:jl viral entry into host cell via clathrin-mediated endocytosis followed by endosome membrane permeabilization GOC:bf GOC:jl GO:0075509 Any endocytosis that is involved in the uptake of a virus into a host cell. Any endocytosis that is involved in the uptake of a virus into a host cell. VZ:977 viral penetration via endocytosis followed by endosome disruption virus endocytosis by host virus endocytosis by host viral entry into host cell via endocytosis endocytosis involved in viral entry into host cell Any endocytosis that is involved in the uptake of a virus into a host cell. VZ:977 VZ:977 Virus endocytosis by host virus endocytosis by host UniProtKB-KW:KW-1164 GO:0075512 Any clathrin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins by invagination of a specific region of the host cell plasma membrane around the bound virus to form a clathrin-coated pit, which then pinches off to form a clathrin-coated endocytic vesicle containing the virus. Any clathrin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins by invagination of a specific region of the host cell plasma membrane around the bound virus to form a clathrin-coated pit, which then pinches off to form a clathrin-coated endocytic vesicle containing the virus. GO:0075516 VZ:957 clathrin-mediated endocytosis of virus by host cell viral penetration via clathrin-mediated endocytosis viral entry into host cell via clathrin-mediated endocytosis clathrin-dependent endocytosis of virus by host cell Any clathrin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins by invagination of a specific region of the host cell plasma membrane around the bound virus to form a clathrin-coated pit, which then pinches off to form a clathrin-coated endocytic vesicle containing the virus. VZ:957 VZ:957 Clathrin-mediated endocytosis of virus by host GO:0075513 Any caveolin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins when material is taken up into plasma membrane caveolae - specialized lipid rafts that form 50-70 nm flask-shaped invaginations of the plasma membrane - which then pinch off to form endocytic caveolar carriers containing the virus. Any caveolin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins when material is taken up into plasma membrane caveolae - specialized lipid rafts that form 50-70 nm flask-shaped invaginations of the plasma membrane - which then pinch off to form endocytic caveolar carriers containing the virus. VZ:976 viral entry into host cell via caveolae-mediated endocytosis viral penetration via caveolae-mediated endocytosis followed by endosome disruption viral entry into host cell via caveolin-mediated endocytosis caveolin-mediated endocytosis of virus by host cell Any caveolin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins when material is taken up into plasma membrane caveolae - specialized lipid rafts that form 50-70 nm flask-shaped invaginations of the plasma membrane - which then pinch off to form endocytic caveolar carriers containing the virus. VZ:976 VZ:976 Caveolin-mediated endocytosis of virus by host GO:0075514 Viral-induced lysis of the endosome involved in uptake of a virus into a host cell. Occurs after internalization of the virus through the endosomal pathway, and results in release of the viral contents from the endosome into the host cell cytoplasm. viral entry into host cell via caveolae-mediated endocytosis followed by endosome lysis endosome lysis involved in viral entry into host cell GO:0075519 The directed movement of the viral genome or viral particle within the host cell cytoplasm along host microtubules. Microtubule-dependent transport involves motor proteins like dynein and kinesin and is mostly used by viruses that target their genomes to the nucleus. microtubule-dependent intracellular transport of viral material GO:0075520 The directed movement of a virus, or part of a virus, within the host cell cytoplasm via the host's actin filaments. Actin-dependent transport is induced by viral proteins that interact with actin and/or host cell motor proteins like myosins or that promotes actin polymerization/depolymerization reactions. VZ:991 actin-dependent intracellular transport of viral material actin-dependent intracellular transport of virus GO:0075527 The process by which bases in viral mRNA are chemically altered during viral transcription. This is usually the incorporation of 1 - 6 additional nucleotides, which shifts the reading frame, allowing the generation of different protein products or through a specific nucleotide change that eliminates the termination codon. The process by which bases in viral mRNA are chemically altered during viral transcription. This is usually the incorporation of 1 - 6 additional nucleotides, which shifts the reading frame, allowing the generation of different protein products or through a specific nucleotide change that eliminates the termination codon. VZ:857 RNA editing involved in viral mRNA transcription RNA editing involved in viral mRNA transcription viral RNA editing The process by which bases in viral mRNA are chemically altered during viral transcription. This is usually the incorporation of 1 - 6 additional nucleotides, which shifts the reading frame, allowing the generation of different protein products or through a specific nucleotide change that eliminates the termination codon. PMID:1629949 VZ:857 VZ:857 RNA editing RNA editing involved in viral mRNA transcription GO:jl GO:0075733 The directed movement of a virus, or part of a virus, within the host cell. GO:0046788 GO:0046795 GO:0046796 egress of virus within host cell intracellular transport of viral material movement of virus within host cell viral genome transport in host cell intracellular virion transport intracellular transport of virus GO:0090024 Any process that decreases the frequency, rate, or extent of neutrophil chemotaxis. Neutrophil chemotaxis is the directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. negative regulation of neutrophil chemotaxis GO:0090077 The process in which a relatively unspecialized cell acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions. foam cell differentiation GO:0090117 The directed movement of low-density lipoprotein particle from endosomes to lysosomes. endosome to lysosome transport of LDL endosome to lysosome transport of low-density lipoprotein particle GO:0090158 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts of an endoplasmic reticulum membrane. endoplasmic reticulum membrane organization GO:0090307 Mitotic bipolar spindle assembly begins with spindle microtubule nucleation from the separated spindle pole body, includes spindle elongation during prometaphase, and is complete when all kinetochores are stably attached the spindle, and the spindle assembly checkpoint is satisfied. mitotic spindle assembly GO:0090323 The regulated release of a prostaglandin that contributes to the immune response. Prostaglandins are a group of biologically active metabolites which contain a cyclopentane ring. prostaglandin secretion involved in inflammatory response GO:0090398 A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. cellular senescence GO:0090399 A cell aging process associated with the dismantling of a cell as a response to telomere shortening and/or cellular aging. replicative senescence GO:0090716 An immune response directed against a previously encountered antigen, being quicker and quantitatively better compared with the primary response. adaptive immune memory response GO:0097121 A protein complex consisting of cyclin A1 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. A protein complex consisting of cyclin A1 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. http://purl.obolibrary.org/obo/PR_000029190 cyclin A1-CDK1 complex A protein complex consisting of cyclin A1 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. PMID:15935619 GO:0097123 A protein complex consisting of cyclin A1 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. A protein complex consisting of cyclin A1 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. http://purl.obolibrary.org/obo/PR_000029190 cyclin A1-CDK2 complex A protein complex consisting of cyclin A1 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. PMID:15935619 GO:0097125 A protein complex consisting of cyclin B1 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. http://purl.obolibrary.org/obo/PR_000029190 cyclin B1-CDK1 complex GO:0097128 A protein complex consisting of cyclin D1 and cyclin-dependent kinase 4 (CDK4). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. A cyclin-dependent protein kinase holoenzyme complex that has a cyclin-D1 regulatory subunit and a Cdk4 kinase subunit. http://purl.obolibrary.org/obo/PR_000026740 cyclin D1-CDK4 complex cyclin D1:Cdk4 cyclin D1-CDK4 complex cyclin D1-CDK4 complex GO:0097131 A protein complex consisting of cyclin D1 and cyclin-dependent kinase 6 (CDK6). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. cyclin D1:Cdk6 cyclin D1-CDK6 complex GO:0097193 A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP). intrinsic apoptotic signaling pathway GO:0097278 Cell killing caused by the membrane attack complex formed following complement activation. complement-dependent cytotoxicity GO:0097314 The aggregation, arrangement and bonding together of the apoptosome, a multisubunit protein complex involved in the signaling phase of the apoptotic process. apoptosome assembly GO:0097350 The selective elimination of senescent neutrophils from the body by autoregulatory mechanisms. neutrophil clearance GO:0097390 chemokine (C-X-C motif) ligand 12 production The appearance of chemokine (C-X-C motif) ligand 12 (CXCL12) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. chemokine (C-X-C motif) ligand 12 production GO:0097400 A series of molecular signals initiated by the binding of interleukin-17 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. interleukin-17-mediated signaling pathway GO:0097431 Either of the ends of a mitotic spindle, a spindle that forms as part of mitosis, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules. mitotic spindle pole GO:0097698 A telomere maintenance process that occurs by base-excision repair of telomeric DNA in response to DNA damage. Telomeric sequences are particularly susceptible to oxidative DNA damage, due to their G-rich nature. telomere maintenance via base-excision repair GO:0097707 A programmed cell death characterized morphologically by the presence of smaller than normal mitochondria with condensed mitochondrial membrane densities, reduction or vanishing of mitochondria crista, and outer mitochondrial membrane rupture. Activation of mitochondrial voltage-dependent anion channels and mitogen-activated protein kinases, upregulation of endoplasmic reticulum stress, and inhibition of cystine/glutamate antiporter are involved in the induction of ferroptosis. This process is characterized by the accumulation of lipid peroxidation products and lethal reactive oxygen species (ROS) derived from iron metabolism. Glutathione peroxidase 4 (GPX4), heat shock protein beta-1, and nuclear factor erythroid 2-related factor 2 function as negative regulators of ferroptosis by limiting ROS production and reducing cellular iron uptake, respectively. In contrast, NADPH oxidase and p53 act as positive regulators of ferroptosis by promotion of ROS production and inhibition of expression of SLC7A11 (a specific light-chain subunit of the cystine/glutamate antiporter), respectively. Misregulated ferroptosis has been implicated in multiple physiological and pathological processes. pmid:25236395 pmid:26794443 feroptosis GO:0098001 Process by which a bacteriophage, using its tail fibers, spikes or a baseplate component, initially recognizes and binds to its specific receptor on the host cell surface. This process is reversible and allows the release of a bacteriophage without affecting infection. Process by which a bacteriophage, using its tail fibers, spikes or a baseplate component, initially recognizes and binds to its specific receptor on the host cell surface. This process is reversible and allows the release of a bacteriophage without affecting infection. reversible bacteriophage attachment, binding of host cell surface receptor phage reversible adsorption This process was historically defined by the release, by Waring blending or sonication, by dilution and centrifugation, or by filtration and washing, of infective virions from their complexes with cells, thus contrary to what is observed after irreversible adsorption. receptor-mediated bacteriophage reversible attachment to host cell Process by which a bacteriophage, using its tail fibers, spikes or a baseplate component, initially recognizes and binds to its specific receptor on the host cell surface. This process is reversible and allows the release of a bacteriophage without affecting infection. GOC:bm GO:0098002 The processes by which a bacteriophage initially commits to infection by binding the host receptor irreversibly. Disruption of the phage:cell complex at this step results in the loss of infective phage virions since the process is characterized by conformational changes of bacteriophage head and tail proteins and injection of bacteriophage proteins into the infected cell. The processes by which a bacteriophage initially commits to infection by binding the host receptor irreversibly. Disruption of the phage:cell complex at this step results in the loss of infective phage virions since the process is characterized by conformational changes of bacteriophage head and tail proteins and injection of bacteriophage proteins into the infected cell. irreversible bacteriophage attachment, binding of host cell surface receptor irreversible bacteriophage attachment, binding of host cell surface receptor phage irreversible adsorption phage irreversible adsorption receptor-mediated bacteriophage irreversible attachment to host cell The processes by which a bacteriophage initially commits to infection by binding the host receptor irreversibly. Disruption of the phage:cell complex at this step results in the loss of infective phage virions since the process is characterized by conformational changes of bacteriophage head and tail proteins and injection of bacteriophage proteins into the infected cell. GOC:bm irreversible bacteriophage attachment, binding of host cell surface receptor GOC:bf GOC:jl phage irreversible adsorption GOC:bm GO:0098534 A cellular process that results in the assembly of one or more centrioles. centriole assembly GO:0098670 The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration. The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration. VZ:3942 viral attachment to host entry receptor viral attachment to host entry receptor entry receptor-mediated virion attachment to host cell The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration. PMID:18351291 VZ:3942 viral attachment to host entry receptor VZ:3942 GO:0098671 The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that does not mediate or trigger entry into the host cell. This binding is typically reversible and enhances significantly infectivity by concentrating the virus in the vicinity of its entry receptors, or bringing it to an organ in which its target cells are located. The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that does not mediate or trigger entry into the host cell. This binding is typically reversible and enhances significantly infectivity by concentrating the virus in the vicinity of its entry receptors, or bringing it to an organ in which its target cells are located. VZ:3943 viral attachment to host adhesion receptor viral attachment to host adhesion receptor adhesion receptor-mediated virion attachment to host cell The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that does not mediate or trigger entry into the host cell. This binding is typically reversible and enhances significantly infectivity by concentrating the virus in the vicinity of its entry receptors, or bringing it to an organ in which its target cells are located. PMID:18351291 VZ:3943 viral attachment to host adhesion receptor VZ:3943 GO:0098677 Maturation of a virion after separation from the host cell. Not all viruses mature after separation. In those that do, maturation typically involves rearangement and/or cleavage of viral proteins, resulting in the virion becoming competent for reinfection. Maturation of a virion after separation from the host cell. Not all viruses mature after separation. In those that do, maturation typically involves rearangement and/or cleavage of viral proteins, resulting in the virion becoming competent for reinfection. UniProtKB-KW:KW-0917 VZ:1946 viral particle maturation virus particle maturation virion maturation Maturation of a virion after separation from the host cell. Not all viruses mature after separation. In those that do, maturation typically involves rearangement and/or cleavage of viral proteins, resulting in the virion becoming competent for reinfection. ISBN:0781718325 UniProtKB-KW:KW-0917 VZ:1946 GO:0098687 Any subdivision of a chromosome along its length. chromosomal region GO:0098754 Any process that reduces or removes the toxicity of a toxic substance. These may include transport of the toxic substance away from sensitive areas and to compartments or complexes whose purpose is sequestration of the toxic substance. detoxification GO:0098800 Any protein complex that is part of the inner mitochondrial membrane. inner mitochondrial membrane protein complex GO:0098813 The process in which genetic material, in the form of nuclear chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. Nuclear chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles. nuclear chromosome segregation GO:0098863 The directed movement of the nucleus by pushing forces exerted by polymerization of backward-extending microtubules. nuclear migration by microtubule mediated pushing forces GO:0098869 Any process carried out at the cellular level that reduces or removes the toxicity superoxide radicals or hydrogen peroxide. cellular oxidant detoxification GO:0099006 The entry of a non-enveloped virus into a host eukaryotic cell, following endocytosis, via permeabilization of the endosomal membrane by membrane penetration protein(s) associated with the viral capsid. In some cases, viral membrane-penetration protein require first to be activated to display its membrane penetrating activity. Activation can be due to receptor binding or the acidic pH of the endosomal lumen. viral entry via permeabilization of endosomal membrane GO:0099024 An infolding of the plasma membrane. plasma membrane invagination GO:0099045 The process whereby a filamentous phage particle is released from a bacterial host cell via a concerted mechanism of assembly and secretion. Neosynthesized virions are coordinately exported as they are assembled at the cell surface in a secretory process that leaves the host cell fully viable. Non-capsid proteins form structures that facilitate translocation through the inner membrane and outer membranes. A viral single-stranded DNA binding protein coats progeny viral DNA molecules to generate the intracellular precursor for assembly of phage particles as they are extruded through the membranes of the bacterial host. The structural proteins of the virus are anchored in the inner membrane before their incorporation into the phage particle. As assembly proceeds, the phage genome traverses the inner and outer membranes until the entire DNA molecule has been coated and extruded. The process whereby a filamentous phage particle is released from a bacterial host cell via a concerted mechanism of assembly and secretion. Neosynthesized virions are coordinately exported as they are assembled at the cell surface in a secretory process that leaves the host cell fully viable. Non-capsid proteins form structures that facilitate translocation through the inner membrane and outer membranes. A viral single-stranded DNA binding protein coats progeny viral DNA molecules to generate the intracellular precursor for assembly of phage particles as they are extruded through the membranes of the bacterial host. The structural proteins of the virus are anchored in the inner membrane before their incorporation into the phage particle. As assembly proceeds, the phage genome traverses the inner and outer membranes until the entire DNA molecule has been coated and extruded. VZ:3951 viral extrusion The process whereby a filamentous phage particle is released from a bacterial host cell via a concerted mechanism of assembly and secretion. Neosynthesized virions are coordinately exported as they are assembled at the cell surface in a secretory process that leaves the host cell fully viable. Non-capsid proteins form structures that facilitate translocation through the inner membrane and outer membranes. A viral single-stranded DNA binding protein coats progeny viral DNA molecules to generate the intracellular precursor for assembly of phage particles as they are extruded through the membranes of the bacterial host. The structural proteins of the virus are anchored in the inner membrane before their incorporation into the phage particle. As assembly proceeds, the phage genome traverses the inner and outer membranes until the entire DNA molecule has been coated and extruded. PMID:2024582831 VZ:3951 GO:0099512 A polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure. supramolecular fiber GO:0099513 A component of the cytoskeleton consisting of a homo or heteropolymeric fiber constructed from an indeterminate number of protein subunits. polymeric cytoskeletal fiber GO:0099636 The directed flow of cytosol (the liquid component of the cytoplasm) and the organelles it contains. Wikipedia:Cytoplasmic_streaming cytoplasmic streaming GO:0110165 A part of a cellular organism that is either an immaterial entity or a material entity with granularity above the level of a protein complex but below that of an anatomical system. Or, a substance produced by a cellular organism with granularity above the level of a protein complex. cellular anatomical entity GO:0120157 A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC. PAR3/PAR6/aPKC PAR6-PAR3-aPKC complex PAR polarity complex GO:0140013 One of the two nuclear divisions that occur as part of the meiotic cell cycle. meiotic nuclear division GO:0140014 A mitotic cell cycle process comprising the steps by which the nucleus of a eukaryotic cell divides; the process involves condensation of chromosomal DNA into a highly compacted form. Canonically, mitosis produces two daughter nuclei whose chromosome complement is identical to that of the mother cell. mitotic nuclear division GO:0140105 A series of molecular signals initiated by the binding of interleukin-10 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. IL-10-mediated signaling pathway interleukin-10-mediated signaling pathway interleukin-10-mediated signaling pathway GO:0140267 The entry of a virus into the cytoplasm of a host cell, triggered by an interaction between the bilayer of a host membrane and a membrane-penetration capsid protein. Results in release of the virus contents into the host cell cytoplasm. The entry of a virus into the cytoplasm of a host cell, triggered by an interaction between the bilayer of a host membrane and a membrane-penetration capsid protein. Results in release of the virus contents into the host cell cytoplasm. viral entry via permeabilization of host membrane The entry of a virus into the cytoplasm of a host cell, triggered by an interaction between the bilayer of a host membrane and a membrane-penetration capsid protein. Results in release of the virus contents into the host cell cytoplasm. PMID:2042756 PMID:25055856 GO:0140374 A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogen antiviral innate immune response GO:0140766 A post-transcriptional gene silencing pathway in which small interfering RNAs (siRNAs) elicit silencing of specific target genes. siRNAs are 21-23 nucleotide RNA duplexes that are fully complementary to their target mRNA. siRNAs can be exported and act in other cells, including in germline cells. Once incorporated into a RNA-induced silencing complex (RISC), siRNAs can downregulate gene expression by either of two posttranscriptional mechanisms: endonucleolytic cleavage of the mRNA or mRNA translational repression. siRNAs are present in lower animals and plants, but not found in mammals; whereas miRNAs are present in all the animals and in plants. siRNA-mediated gene silencing siRNA-mediated post-transcriptional gene silencing A post-transcriptional gene silencing pathway in which small interfering RNAs (siRNAs) elicit silencing of specific target genes. siRNAs are 21-23 nucleotide RNA duplexes that are fully complementary to their target mRNA. siRNAs can be exported and act in other cells, including in germline cells. Once incorporated into a RNA-induced silencing complex (RISC), siRNAs can downregulate gene expression by either of two posttranscriptional mechanisms: endonucleolytic cleavage of the mRNA or mRNA translational repression. siRNAs are present in lower animals and plants, but not found in mammals; whereas miRNAs are present in all the animals and in plants. PMID:26372022 GO:1900016 Any process that stops, prevents or reduces the frequency, rate or extent of cytokine production involved in inflammatory response. negative regulation of cytokine production involved in inflammatory response GO:1900409 Any process that activates or increases the frequency, rate or extent of cellular response to oxidative stress. positive regulation of cellular response to oxidative stress GO:1901524 Any process that modulates the frequency, rate or extent of macromitophagy. regulation of mitophagy GO:1901526 Any process that activates or increases the frequency, rate or extent of mitophagy. positive regulation of mitophagy GO:1901567 Interacting selectively and non-covalently with fatty acid derivative. fatty acid derivative binding GO:1901611 Interacting selectively and non-covalently with phosphatidylglycerol. GO:1901611 phosphatidylglycerol binding GO:1901731 Any process that activates or increases the frequency, rate or extent of platelet aggregation. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules. positive regulation of platelet aggregation GO:1901797 Any process that stops, prevents or reduces the frequency, rate or extent of signal transduction by p53 class mediator. downregulation of signal transduction by p53 class mediator negative regulation of p53 signaling GO:1901799 Any process that stops, prevents or reduces the frequency, rate or extent of proteasomal protein catabolic process. negative regulation of proteasomal protein catabolic process GO:1901889 Negative regulation of cell junction assembly is a subtype of negative regulation process: Any process that stops, prevents or reduces the frequency, rate or extent of cell junction assembly. inhibition of cell junction assembly negative regulation of cell junction assembly GO:1901988 Any process that modulates the frequency, rate or extent of cell cycle phase transition. regulation of cell cycle phase transition HOIP_0060082 GO:1902188 Any process that activates or increases the frequency, rate or extent of viral release from host cell. positive regulation of viral release from host cell GO:1902292 Any DNA replication initiation that is involved in cell cycle DNA replication. DNA replication initiation involved in cell cycle DNA replication DNA-dependent DNA replication initiation involved in cell cycle DNA replication cell cycle DNA replication initiation GO:1902483 Any apoptotic process in a cytotoxic T cell. cytotoxic T cell apoptotic process GO:1902576 Any process that stops, prevents or reduces the frequency, rate or extent of nuclear cell cycle DNA replication. down regulation of DNA replication involved in S phase negative regulation of nuclear cell cycle DNA replication GO:1902600 The directed movement of a proton across a membrane. proton transmembrane transport GO:1902750 Negative regulation of cell cycle G2/M phase transition is a subtype of negative regulation of cell cycle: Any process that stops, prevents or reduces the frequency, rate or extent of cell cycle G2/M phase transition. negative regulation of cell cycle G2/M phase transition HOIP_0000370 GO:1902807 Any signalling pathway that decreases or inhibits the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the cell cycle. negative regulation of cell cycle G1/S phase transition GO:1902957 Any process that stops, prevents or reduces the frequency, rate or extent of mitochondrial electron transport, NADH to ubiquinone. negative regulation of mitochondrial electron transport, NADH to ubiquinone GO:1903107 Any insulin receptor signaling pathway that is involved in dauer larval development. insulin receptor signaling pathway involved in dauer larval development GO:1903144 Any actin filament that is part of a actomyosin contractile ring. actomyosin contractile ring actin filament GO:1903145 Any actin filament that is part of a cell cortex of cell tip. actin filament of cell cortex of cell tip GO:1903409 The chemical reaction resulting in the formation of reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. reactive oxygen species biosynthesis reactive oxygen species formation reactive oxygen species synthesis reactive oxygen species synthesis reactive oxygen species biosynthetic process reactive oxygen species synthesis PMID:24252804 GO:1903426 Any process that activates or increases the frequency, rate or extent of reactive oxygen species biosynthetic process. positive regulation of reactive oxygen species biosynthetic process GO:1903427 Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ROS. negative regulation of reactive oxygen species biosynthetic process negative regulation of ROS formation GO:1903514 The directed movement of calcium ion from endoplasmic reticulum to cytosol. release of sequestered calcium ion into cytosol by endoplasmic reticulum GO:1903597 Any process that stops, prevents or reduces the frequency, rate or extent of gap junction assembly. negative regulation of gap junction assembly GO:1903788 Any process that activates or increases the frequency, rate or extent of glutathione biosynthetic process. positive regulation of glutathione anabolism positive regulation of glutathione biosynthesis positive regulation of glutathione formation positive regulation of glutathione synthesis up regulation of glutathione anabolism up regulation of glutathione biosynthesis positive regulation of glutathione biosynthetic process GO:1903828 Any process that stops, prevents or reduces the frequency, rate or extent of cellular protein localization. Cellular protein localization is any process in which a protein is transported to, and/or maintained in, a specific location and encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell. negative regulation of cellular protein localization GO:1903863 The aggregation, arrangement and bonding together of a set of components to form a P granule. P granule assembly GO:1904294 Any process that activates or increases the frequency, rate or extent of ERAD pathway. positive regulation of ERAD GO:1904592 Any process that activates or increases the frequency, rate or extent of protein refolding. up regulation of protein refolding up-regulation of protein refolding upregulation of protein refolding positive regulation of protein refolding GO:1904777 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell cortex. negative regulation of protein localization to cell cortex GO:1904785 Any process that modulates the frequency, rate or extent of asymmetric protein localization involved in cell fate determination. regulation of asymmetric protein localization involved in cell fate determination GO:1904786 Any process that stops, prevents or reduces the frequency, rate or extent of asymmetric protein localization involved in cell fate determination. negaitive regulation of asymmetric protein localization involved in cell fate determination GO:1904787 Any process that activates or increases the frequency, rate or extent of asymmetric protein localization involved in cell fate determination. positive regulation of asymmetric protein localization involved in cell fate determination GO:1905517 The orderly movement of a macrophage from one site to another. macrophage migration GO:1905766 Any process that activates or increases the frequency, rate or extent of protection from non-homologous end joining at telomere. positive regulation of protection from NHEJ-mediated telomere fusion up regulation of protection from NHEJ-mediated telomere fusion positive regulation of protection from non-homologous end joining at telomere GO:1990231 A protein dimer containing two STING monomers. It binds cyclic purine di-nucleotides. Activation of the sting complex by 2',5'-3'-5'-cyclic GMP-AMP activates nuclear transcription factor kB (NF-kB) and interferon regulatory factor 3 (IRF3) which then induce transcription of the genes encoding type I IFN and cytokines active in the innate immune response. A protein dimer containing two STING monomers. It binds cyclic purine di-nucleotides. Activation of the sting complex by 2',5'-3'-5'-cyclic GMP-AMP activates nuclear transcription factor kB (NF-kB) and interferon regulatory factor 3 (IRF3) which then induce transcription of the genes encoding type I IFN and cytokines active in the innate immune response. stimulator of interferon genes complex stimulator of interferon genes complex STING complex A protein dimer containing two STING monomers. It binds cyclic purine di-nucleotides. Activation of the sting complex by 2',5'-3'-5'-cyclic GMP-AMP activates nuclear transcription factor kB (NF-kB) and interferon regulatory factor 3 (IRF3) which then induce transcription of the genes encoding type I IFN and cytokines active in the innate immune response. PMID:22705373 PMID:23706668 stimulator of interferon genes complex PMID:22705373 GO:1990266 The orderly movement of a neutrophil from one site to another. neutrophil migration GO:1990748 Any process carried out at the cellular level that reduces or removes the toxicity of a toxic substance. These may include transport of the toxic substance away from sensitive areas and to compartments or complexes whose purpose is sequestration of the toxic substance. cellular detoxification GO:1990752 Any end of a microtubule. Microtubule ends differ in that the so-called microtubule plus-end is the one that preferentially grows by polymerization, with respect to the minus-end. microtubule end GO:1990773 The regulated release of matrix metallopeptidases, a family of zinc-dependent endopeptidases that can degrade extracellular matrix proteins and process other types of proteins. matrix metallopeptidase secretion GO:1990922 The multiplication or reproduction of hepatic stellate cells, resulting in the expansion of a hepatic stellate cell population. Hepatic stellate cells are found in the perisinusoidal space of the liver, and are capable of multiple roles including storage of retinol, presentation of antigen to T cells (including CD1d-restricted NKT cells), and upon activation, production of extracellular matrix components. This cell type comprises approximately 8-15% of total cells in the liver. Ito cell proliferation hepatic perisinusoidal cell proliferation perisinusoidal cell proliferation hepatic stellate cell proliferation GO:2000042 Any process that stops, prevents or reduces the frequency, rate or extent of double-strand break repair via homologous recombination. negative regulation of HDR negative regulation of double-strand break repair via homologous recombination GO:2000773 Any process that stops, prevents or reduces the frequency, rate or extent of cellular senescence. negative regulation of cellular senescence GO:2000774 Any process that activates or increases the frequency, rate or extent of cellular senescence. up regulation of cell division positive regulation of cellular senescence GO:2000781 Any process that activates or increases the frequency, rate or extent of positive regulation of double-strand break repair. positive regulation of double-strand break repair GO:2001033 Any process that stops, prevents or reduces the frequency, rate or extent of double-strand break repair via nonhomologous end joining. This entity is a specific course-dependent process. This process can constitute the course of chronic cellular senescence. PMID:34676498 negative regulation of double-strand break repair via nonhomologous end joining PMID:34676498 Here, we identify cGAS as an essential regulator in inhibiting mitotic DNA double-strand break (DSB) repair and protecting short telomeres from end-to-end fusion independent of the canonical cGAS-STING pathway. cGAS associates with telomeric/subtelomeric DNA during mitosis when TRF1/TRF2/POT1 are deficient on telomeres. Depletion of cGAS leads to mitotic chromosome end-to-end fusions predominantly occurring between short telomeres. Mechanistically, cGAS interacts with CDK1 and positions them to chromosome ends. Thus, CDK1 inhibits mitotic non-homologous end joining (NHEJ) by blocking the recruitment of RNF8. GO:2001034 Any process that activates or increases the frequency, rate or extent of positive regulation of double-strand break repair via nonhomologous end joining. positive regulation of double-strand break repair via nonhomologous end joining HINO:0016226 As a result of binding to Bid, Bax oligomerizes and integrates in the outer mitochondrial membrane that triggers cytochrome c release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis (Eskes et al., 2000) As a result of binding to Bid, Bax oligomerizes and integrates in the outer mitochondrial membrane that triggers cytochrome c release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis (Eskes et al., 2000) Reactome:R-HSA-114294.2 Activation, translocation and oligomerization of BAX As a result of binding to Bid, Bax oligomerizes and integrates in the outer mitochondrial membrane that triggers cytochrome c release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis (Eskes et al., 2000) Reactome HINO:0016227 tBID binds to its mitochondrial partner BAK to release cytochrome c. Activated tBID results in an allosteric activation of BAK. This may induce its intramembranous oligomerization into a pore for cytochrome c efflux. Reactome:R-HSA-114294.2 Activation and oligomerization of BAK protein HINO:0016241 Activation of BH3-only proteins HINO:0016364 Xenobiotics that contain either a carboxylic group or an aromatic hydroxylamine group are possible substrates for amino acid conjugation. Xenobiotics with a carboxylic group conjugate with an amino group of amino acids such as glycine, taurine and glutamine. The hydroxylamine group conjugates with the carboxylic group of amino acids such as proline and serine. amino acid conjugation HINO:0016374 The combination of glutamate, cysteine and ATP is required to form glutathione. The steps involved in the synthesis and recycling of glutathione are outlined (Meister, 1988). PMID:3053703 Reactome: R-HSA-174403.4 Glutathione synthesis and recycling Reactome: R-HSA-174403.4 https://reactome.org/PathwayBrowser/#/R-HSA-156580&SEL=R-HSA-174403 HINO:0017769 Transport of NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters, from the cytoplasm into the nucleus, across the nuclear membrane. Translocation of NF-kappaB from the cytosol to the nucleus HP:0000020 Loss of the ability to control the urinary bladder leading to involuntary urination. MSH:D014549 SNOMEDCT_US:165232002 UMLS:C0042024 Bladder incontinence Loss of bladder control Urinary incontinence (phenotype) HP:0000093 Increased levels of protein in the urine. High urine protein levels Protein in urine Proteinuria (phenotype) HP:0000118 A phenotypic abnormality. Phenotypic abnormality HP:0000458 An inability to perceive odors. This is a general term describing inability to smell arising in any part of the process of smelling from absorption of odorants into the nasal mucous overlying the olfactory epithelium, diffusion to the cilia, binding to olfactory receptor sites, generation of action potentials in olfactory neurons, and perception of a smell. Anosmia (phenotype) HP:0000716 Frequent feelings of being down, miserable, and/or hopeless; difficulty recovering from such moods; pessimism about the future; pervasive shame; feeling of inferior self-worth; thoughts of suicide and suicidal behavior. MSH:D003866 SNOMEDCT_US:21061000119107 SNOMEDCT_US:35489007 SNOMEDCT_US:78667006 UMLS:C0011581 Depression Depressivity Depressive disorder Depression (phenotype) HP:0000969 An abnormal accumulation of fluid beneath the skin, or in one or more cavities of the body. Dropsy Fluid retention Hydrops Oedema Water retention edema (phenotype) HP:0001288 The term gait disturbance can refer to any disruption of the ability to walk. In general, this can refer to neurological diseases but also fractures or other sources of pain that is triggered upon walking. However, in the current context gait disturbance refers to difficulty walking on the basis of a neurological or muscular disease. SNOMEDCT_US:22325002 UMLS:C0575081 Abnormal gait Abnormal walk Gait abnormalities Gait difficulties Gait disturbances Impaired gait Gait disturbance (phenotype) HP:0001681 Paroxysmal chest pain that occurs with exertion or stress and is related to myocardial ischemia. Angina pectoris HP:0001873 A reduction in the number of circulating thrombocytes. Thrombocytopenia HP:0001941 Abnormal acid accumulation or depletion of base. Acidosis HP:0001944 dehydration (phenotype) HP:0001945 Elevated body temperature due to failed thermoregulation. Fever HP:0001946 Presence of elevated levels of ketone bodies in the body. Ketosis HP:0001953 A type of diabetic metabolic abnormality with an accumulation of ketone bodies. Diabetic ketoacidosis HP:0001974 An abnormal increase in the number of leukocytes in the blood. Leukocytosis HP:0002113 A pulmonary infiltrate is a substance denser than air, such as pus, blood, or protein, which lingers within the parenchyma of the lungs. Pulmonary infiltrates are associated with pneumonia, and tuberculosis. (https://en.wikipedia.org/wiki/Pulmonary_infiltrate) pulmonary infiltrates HP:0002170 Hemorrhage occurring within the skull. Intracranial hemorrhage (phenotype) HP:0002321 An abnormal sensation of spinning while the body is actually stationary. Vertigo (phenotype) HP:0002664 An organ or organ-system abnormality that consists of uncontrolled autonomous cell-proliferation which can occur in any part of the body as a benign or malignant neoplasm (tumor). Tumor Neoplasm (phenotype) HP:0002835 Inspiration of a foreign object into the airway. Aspiration HP:0002904 An increased amount of bilirubin in the blood. Hyperbilirubinemia (phenotype) HP:0003074 An increased concentration of glucose in the blood. High blood glucose High blood sugar Hyperglycemia (phenotype) HP:0003077 Hyperlipidemia is an elevation of the blood levels of lipids including primarily cholesterol, phospholipids and triglycerides and cholesterol esters. The lipids are transported on lipoproteins some of which are commonly used for clinical measurements, including chylomicrons, very-low density lipoproteins (VLDL), intermediate-density lipoproteins (IDL), low-density lipoproteins, and high-density lipoproteins (HDL). Elevated lipids in blood Hyperlipidemia (phenotype) HP:0003236 An elevation of the level of the enzyme creatine kinase (also known as creatine phosphokinase, CPK; EC 2.7.3.2) in the blood. CPK levels can be elevated in a number of clinical disorders such as myocardial infarction, rhabdomyolysis, and muscular dystrophy. Elevated serum creatine kinase HP:0003281 Abnormal raised concentration of ferritin, a ubiquitous intracellular protein that stores iron, in the blood. Elevated serum ferritin Hyperferritinaemia Increased circulating ferritin concentration HP:0004360 Abnormality of acid-base homeostasis (phenotype) HP:0006530 HP:0006580 Fibroblast proliferation and fiber expansion from the portal areas to the lobule. Portal fibrosis (phenotype) HP:0006965 Acute necrotizing encephalopathy (phenotype) HP:0010783 Redness of the skin, caused by hyperemia of the capillaries in the lower layers of the skin. Erythema (phenotype) HP:0011105 An increase in the amount of intravascular fluid, particularly in the volume of the circulating blood. Hypervolemia HP:0011106 An decrease in the amount of intravascular fluid, particularly in the volume of the circulating blood. Hypovolemia HP:0011227 An abnormal elevation of the C-reactive protein level in serum. Elevated C-reactive protein level HP:0011897 Increased number of neutrophils circulating in blood. Neutrophilia HP:0011899 Increased concentration of fibrinogen in the blood. Hyperfibrinogenemia (phenotype) HP:0012399 A type of ulcer that is caused when an area of skin is subject to pressure over a prolonged period of time, ranging in range in severity from patches of discolored skin to open wounds that expose the underlying bone or muscle. The most common sites are the sacrum, coccyx, heels and the hips. Bedsore Decubitus Ulcer Pressure Sore Pressure ulcer pressure ulcer (phenotype) HP:0012418 An abnormally low level of blood oxygen. Hypoxemia HP:0012592 Increased concentration of albumin in the urine. High urine albumin levels albumin in urine albuminuria (phenotype) HP:0012735 A sudden, audible expulsion of air from the lungs through a partially closed glottis, preceded by inhalation. The European Respiratory Society Task Force recommended two possible definitions of cough: (1) A three-phase expulsive motor act characterized by an inspiratory effort (inspiratory phase) followed by a forced expiratory effort against a closed glottis (compressive phase) and then by opening of the glottis and rapid expiratory airflow (expulsive phase);and (2) A forced expiratory manoeuvre, usually against a closed glottis and associated with a characteristic sound. The term Cough or any of its more specific descendents can be modified by the terms Acute (HP:0011009), Subacute (HP:0011011), and Chronic (HP:0011010). In adults, an acute cough lasts less than 3 weeks, a subacute cough from 3 to 8 weeks, and a chronic cough longer than 8 weeks. In children aged less than 15 years a chronic cough is defined as a daily cough lasting for over 4 weeks. cough (phenotype) HP:0020071 The presence of virus in the blood. viraemia viremia (phenotype) HOIP_0040945 HP:0025179 Ground-glass opacification is a non-specific sign and can be observed with many conditions including infection, chronic interstitial disease and acute alveolar disease. A descriptive term that is applied to computer tomography imaging and that refers to a hazy area of increased attenuation in the lung with preserved bronchial and vascular markings. Ground-glass opacification is a non-specific sign and can be observed with many conditions including infection, chronic interstitial disease and acute alveolar disease. Ground-glass opacification on pulmonary HRCT HP:0025435 An elevated level of the enzyme lactate dehydrogenase in serum. Increased lactate dehydrogenase level HP:0031005 Abnormally increased sensitivity to pain. Hyperalgesia (phenotype) HP:0031258 A state of sudden and severe confusion. Delirium (phenotype) HP:0031956 An abnormally high concentration in the circulation of aspartate aminotransferase (AST). Elevated serum aspartate aminotransferase HP:0031964 An abnormally high concentration in the circulation of alanine aminotransferase (ALT), which is an enzyme that catalyzes the transfer of amino groups to form the hepatic metabolite oxaloacetate. ALT is found abundantly in the cytosol of the hepatocyte. ALT activity in the liver is about 3000 times that of serum activity. Thus, in the case of hepatocellular injury or death, release of ALT from damaged liver cells increases measured ALT activity in the serum. Although it is generally thought to be specific to the liver, it is also found in the kidney, and, in much smaller quantities, in heart and skeletal muscle cells. Elevated serum alanine aminotransferase HP:0033041 Excessive or uncontrolled release of proinflammatory cytokines. hypercytokinaemia hypercytokinemia Cytokine storm HP:0033106 An increased concentration of D-dimers, a marker of fibrin degradation, in the blood circulation. Elevated D-dimers HP:0033675 A clinically recognizable state of increased vulnerability resulting from a decline in reserve and function across multiple physiologic systems such that the ability to cope with everyday or acute stressors is compromised. Frailty (phenotype) HP:0040183 SNOMEDCT_US:302690004 UMLS:C2945606 Stool holding Stool soiling Encopresis (phenotype) HP:0041051 A rare condition that is characterized by a complete loss of taste function of the tongue. Ageusia (phenotype) HP:0100512 A reduced concentration of Vitamin D. Low levels of vitamin D HP:0100543 Abnormal cognition with deficits in thinking, reasoning, or remembering. MSH:D060825 SNOMEDCT_US:386806002 UMLS:C0338656 UMLS:C0683322 Abnormality of cognition Cognitive abnormality Cognitive defects Cognitive deficits Cognitive impairment Intellectual impairment Cognitive impairment (phenotype) HP:0100699 HP:0100806 Systemic inflammatory response to infection. Sepsis (phenotype) HP:0100820 Inflammatory or noninflammatory diseases affecting the glomeruli of the nephron. Glomerulopathy (phenotype) HP:0200042 A discontinuity of the skin exhibiting complete loss of the epidermis and often portions of the dermis and even subcutaneous fat. Skin ulcer (phenotype) HP:0410173 An increased concentration of tropnin I in the blood, which is a cardiac regulatory protein that controls the calcium mediated interaction between actin and myosin. Raised cardiac troponin concentrations are now accepted as the standard biochemical marker for the diagnosis of myocardial infarction. Increased troponin I level in blood HP:0410174 An increased concentration of tropnin T in the blood, which is a cardiac regulatory protein that controls the calcium mediated interaction between actin and myosin. Raised cardiac troponin concentrations are now accepted as the standard biochemical marker for the diagnosis of myocardial infarction. Increased troponin T level in blood IAO:0000003 A measurement unit label is as a label that is part of a scalar measurement datum and denotes a unit of measure. measurement unit label IAO:0000005 objective specification In the protocol of a ChIP assay the objective specification says to identify protein and DNA interaction. A directive information entity that describes an intended process endpoint. When part of a plan specification the concretization is realized in a planned process in which the bearer tries to effect the world so that the process endpoint is achieved. 2009-03-16: original definition when imported from OBI read: "objective is an non realizable information entity which can serve as that proper part of a plan towards which the realization of the plan is directed." 2014-03-31: In the example of usage ("In the protocol of a ChIP assay the objective specification says to identify protein and DNA interaction") there is a protocol which is the ChIP assay protocol. In addition to being concretized on paper, the protocol can be concretized as a realizable entity, such as a plan that inheres in a person. The objective specification is the part that says that some protein and DNA interactions are identified. This is a specification of a process endpoint: the boundary in the process before which they are not identified and after which they are. During the realization of the plan, the goal is to get to the point of having the interactions, and participants in the realization of the plan try to do that. Answers the question, why did you do this experiment? PERSON: Alan Ruttenberg PERSON: Barry Smith PERSON: Bjoern Peters PERSON: Jennifer Fostel goal specification OBI Plan and Planned Process/Roles Branch OBI_0000217 objective specification IAO:0000007 Pour the contents of flask 1 into flask 2 A directive information entity that describes an action the bearer will take. Alan Ruttenberg OBI Plan and Planned Process branch action specification IAO:0000009 A label is a symbol that is part of some other datum and is used to either partially define the denotation of that datum or to provide a means for identifying the datum as a member of the set of data with the same label datum label IAO:0000027 data item Data items include counts of things, analyte concentrations, and statistical summaries. An information content entity that is intended to be a truthful statement about something (modulo, e.g., measurement precision or other systematic errors) and is constructed/acquired by a method which reliably tends to produce (approximately) truthful statements. data data item IAO:0000030 A generically dependent continuant that is about some thing. information content entity 1 1 IAO:0000032 10 feet. 3 ml. A scalar measurement datum is a measurement datum that is composed of two parts, numerals and a unit label. 2009-03-16: we decided to keep datum singular in scalar measurement datum, as in this case we explicitly refer to the singular form Would write this as: has_part some 'measurement unit label' and has_part some numeral and has_part exactly 2, except for the fact that this won't let us take advantage of OWL reasoning over the numbers. Instead use has measurment value property to represent the same. Use has measurement unit label (subproperty of has_part) so we can easily say that there is only one of them. PERSON: Alan Ruttenberg PERSON: Melanie Courtot scalar measurement datum IAO:0000033 An information content entity whose concretizations indicate to their bearer how to realize them in a process. 2009-03-16: provenance: a term realizable information entity was proposed for OBI (OBI_0000337) , edited by the PlanAndPlannedProcess branch. Original definition was "is the specification of a process that can be concretized and realized by an actor" with alternative term "instruction".It has been subsequently moved to IAO where the objective for which the original term was defined was satisfied with the definitionof this, different, term. 2013-05-30 Alan Ruttenberg: What differentiates a directive information entity from an information concretization is that it can have concretizations that are either qualities or realizable entities. The concretizations that are realizable entities are created when an individual chooses to take up the direction, i.e. has the intention to (try to) realize it. 8/6/2009 Alan Ruttenberg: Changed label from "information entity about a realizable" after discussions at ICBO Werner pushed back on calling it realizable information entity as it isn't realizable. However this name isn't right either. An example would be a recipe. The realizable entity would be a plan, but the information entity isn't about the plan, it, once concretized, *is* the plan. -Alan PERSON: Alan Ruttenberg PERSON: Bjoern Peters directive information entity IAO:0000064 algorithm PMID: 18378114.Genomics. 2008 Mar 28. LINKGEN: A new algorithm to process data in genetic linkage studies. A plan specification which describes the inputs and output of mathematical functions as well as workflow of execution for achieving an predefined objective. Algorithms are realized usually by means of implementation as computer programs for execution by automata. Philippe Rocca-Serra PlanAndPlannedProcess Branch OBI_0000270 adapted from discussion on OBI list (Matthew Pocock, Christian Cocos, Alan Ruttenberg) algorithm IAO:0000098 data format specification A data format specification is the information content borne by the document published defining the specification. Example: The ISO document specifying what encompasses an XML document; The instructions in a XSD file 2009-03-16: provenance: term imported from OBI_0000187, which had original definition "A data format specification is a plan which organizes information. Example: The ISO document specifying what encompasses an XML document; The instructions in a XSD file" PERSON: Alan Ruttenberg PlanAndPlannedProcess Branch OBI branch derived OBI_0000187 data format specification IAO:0000100 data set Intensity values in a CEL file or from multiple CEL files comprise a data set (as opposed to the CEL files themselves). A data item that is an aggregate of other data items of the same type that have something in common. Averages and distributions can be determined for data sets. 2009/10/23 Alan Ruttenberg. The intention is that this term represent collections of like data. So this isn't for, e.g. the whole contents of a cel file, which includes parameters, metadata etc. This is more like java arrays of a certain rather specific type 2014-05-05: Data sets are aggregates and thus must include two or more data items. We have chosen not to add logical axioms to make this restriction. person:Allyson Lister person:Chris Stoeckert OBI_0000042 group:OBI data set IAO:0000101 image An image is an affine projection to a two dimensional surface, of measurements of some quality of an entity or entities repeated at regular intervals across a spatial range, where the measurements are represented as color and luminosity on the projected on surface. person:Alan Ruttenberg person:Allyson person:Chris Stoeckert OBI_0000030 group:OBI image IAO:0000104 plan specification PMID: 18323827.Nat Med. 2008 Mar;14(3):226.New plan proposed to help resolve conflicting medical advice. A directive information entity with action specifications and objective specifications as parts that, when concretized, is realized in a process in which the bearer tries to achieve the objectives by taking the actions specified. 2009-03-16: provenance: a term a plan was proposed for OBI (OBI_0000344) , edited by the PlanAndPlannedProcess branch. Original definition was " a plan is a specification of a process that is realized by an actor to achieve the objective specified as part of the plan". It has been subsequently moved to IAO where the objective for which the original term was defined was satisfied with the definitionof this, different, term. 2014-03-31: A plan specification can have other parts, such as conditional specifications. Alternative previous definition: a plan is a set of instructions that specify how an objective should be achieved Alan Ruttenberg OBI Plan and Planned Process branch OBI_0000344 2/3/2009 Comment from OBI review. Action specification not well enough specified. Conditional specification not well enough specified. Question whether all plan specifications have objective specifications. Request that IAO either clarify these or change definitions not to use them plan specification IAO:0000109 A measurement datum is an information content entity that is a recording of the output of a measurement such as produced by a device. measurement datum IAO:0000308 figure Any picture, diagram or table An information content entity consisting of a two dimensional arrangement of information content entities such that the arrangement itself is about something. PERSON: Lawrence Hunter figure IAO:0000400 IAO:0000414 A scalar measurement datum that is the result of measurement of mass quality 2009/09/28 Alan Ruttenberg. Fucoidan-use-case Person:Alan Ruttenberg mass measurement datum IAO:0000416 A scalar measurement datum that is the result of measuring a temporal interval 2009/09/28 Alan Ruttenberg. Fucoidan-use-case Person:Alan Ruttenberg time measurement datum IAO:0000582 time stamped measurement datum IAO:0000584 A data set that is an aggregate of data recording some measurement at a number of time points. The time series data set is an ordered list of pairs of time measurement data and the corresponding measurement data acquired at that time. time sampled measurement data set IDOMAL:0000822 A immunoglobulin protein that is secreted into the blood or lymph in response to an antigenic stimulus, such as a bacterium, virus, parasite, or transplanted organ, and that neutralizes the antigen by binding specifically to it. antibody IDOMAL:50000026 A permanent change in the DNA sequence of a gene that alters the genetic message carried by that gene. mutation HOIP_0001985 IDO:0000509 An aggregate of organisms of the same type. organism population IDO:0000604 An establishment of localization in host process in which an organism establishes itself in a host. Establishment of one organism in the extended organism of another (the host) involves at least one of (1) movement of the organism to a location within the host in which the organism can persist, or (2) adherence or attachment of the organism to part of the host. colonization of host IDO:0000625 An establishment of localization process in which a material entity reaches a site in an organism in which it can survive, grow, multiply, or mature. An organism begins bearing a particular host role as soon as the extended organism contains the relevant material entity, regardless of that entity's location in the extended organism. An establishment process is any process by which the entity reaches a location in the extended organism in which it can persist and continue its lifecycle. For example, an organism is host to a virus as soon as any part of the extended organism is occupied by virus particles. During an establishment process, virus particles enter host cells of the relevant type, and viral DNA is integrated into host DNA. establishment of localization in host IDO:0000636 A process that is a systemic inflammatory response to infection. sepsis (process) IMR:0000003 GO:0005110 Wnt IMR:0000004 GO:0005113 Hh hedgehog IMR:0000005 NCBI-Human-GeneID:6469 NCBI-Mouse-GeneID:20423 NCBI-Rat-GeneID:29499 HHG-1 Sonic hedgehog SHH (mol) NCBI-Human-GeneID:6469 https://www.ncbi.nlm.nih.gov/gene/6469 NCBI-Mouse-GeneID:20423 https://www.ncbi.nlm.nih.gov/gene/20423 NCBI-Rat-GeneID:29499 https://www.ncbi.nlm.nih.gov/gene/29499 IMR:0000007 IL Interleukin IMR:0000015 Wikipedia:Thrombopoietin thrombopoietin TPO IMR:0000016 GO:0005128 OMIM: 133170 Wikipedia:Erythropoietin erythropoietin EPO IMR:0000017 granulocyte colony-stimulating factor related molecular function GO:0005130 G-CSF family IMR:0000018 OMIM: 138960 granulocyte-macrophage colony-stimulating factor relate molecular function GO:0005129 GM-CSF IMR:0000019 OMIM: 159540 leukemia inhibitory factor LIF IMR:0000020 OMIM: 184745 Wikipedia:Stem_cell_factor related molecular function GO:0005173 stem cell factor SCF IMR:0000021 GO:0005164 IPR:006052 TNF superfamily IMR:0000022 CD178 antigen CD95L Fas ligand FasL Tumor necrosis factor ligand superfamily member 6 FasL IMR:0000023 GO:0005174 CD154 CD40 ligand gp39 CD40L IMR:0000026 TNF beta lymphotoxin lymphotoxin alpha LT alpha IMR:0000027 IFN Interferon IMR:0000032 GO:0005161 platelet derived growth factor PDGF IMR:0000033 GO:0005171 hepatocyte growth factor scatter factor HGF IMR:0000034 GO:0005165 nerve growth factor family neurotrophin NGF family IMR:0000035 acidic cytokeratin type I cytokeratin IMR:0000036 The TGF-beta superfamily of growth factors regulate many cellular functions, which includes TGF-betas, activins and inhibins, nodal, BMPs and GDFs. TGF-beta/BMP-like proteins are found in various species, including Xenopus, C.elegans and D.melanogaster. The TGF-beta superfamily of growth factors regulate many cellular functions, which includes TGF-betas, activins and inhibins, nodal, BMPs and GDFs. TGF-beta/BMP-like proteins are found in various species, including Xenopus, C.elegans and D.melanogaster. GO:0005160 transforming growth factor beta superfamily TGF-beta superfamily The TGF-beta superfamily of growth factors regulate many cellular functions, which includes TGF-betas, activins and inhibins, nodal, BMPs and GDFs. TGF-beta/BMP-like proteins are found in various species, including Xenopus, C.elegans and D.melanogaster. PMID:12485160 PMID:18000526 PMID:9759503 IMR:0000037 GO:0016916 inhibin IMR:0000039 GO:0016915 activin IMR:0000040 BMPs belong to the TGF-beta superfamily. BMP-like molecules have been identified in various species including D.melanogaster (Dpp, Gbb/60A and Scw) and C.elegans. BMPs belong to the TGF-beta superfamily. BMP-like molecules have been identified in various species including D.melanogaster (Dpp, Gbb/60A and Scw) and C.elegans. Bone morphogenetic protein family BMP family BMPs belong to the TGF-beta superfamily. BMP-like molecules have been identified in various species including D.melanogaster (Dpp, Gbb/60A and Scw) and C.elegans. PMID:15871923 PMID:9720756 PMID:9759503 IMR:0000045 GO:0005160 Glial cell line-derived neurotrophic factor GDNF IMR:0000046 Nodal family IMR:0000047 epidermal growth factor family EGF family IMR:0000048 NRG neuregulin IMR:0000049 GO:0005104 Fibroblast growth factor HBGF Heparin-binding growth factor FGF IMR:0000050 neutral to basic cytokeratin type II cytokeratin IMR:0000051 leptin IMR:0000053 cytokeratin 1 IMR:0000056 GO:0005027 tumor necrosis factor receptor family TNFR family IMR:0000057 GO:0005028 CD40 IMR:0000058 Apo-1 CD95 Fas receptor FasR IMR:0000060 GO:0005032 tumor necrosis factor receptor, type I TNFR1 IMR:0000061 GO:0005033 tumor necrosis factor receptor, type II TNFR2 IMR:0000068 GO:0005017 platelet derived growth factor receptor PDGF receptor IMR:0000069 GO:0005018 alpha platelet derived growth factor receptor alpha PDGF receptor IMR:0000070 GO:0005019 beta platelet derived growth factor receptor beta PDGF receptor IMR:0000075 insulin receptor family IMR:0000076 anaplastic lymphoma kinase ALK IMR:0000077 leukocyte tyrosine kinase LTK IMR:0000080 The vertebrate Fgfr gene family consists of four highly related genes, Fgfr1-4. The vertebrate Fgfr gene family consists of four highly related genes, Fgfr1-4. GO:0005007 fibroblast growth factor receptor FGFR family The vertebrate Fgfr gene family consists of four highly related genes, Fgfr1-4. PMID:15689573 IMR:0000081 GO:0005006 epidermal growth factor receptor EGFR (mol) IMR:0000084 GO:0008095 IP3R inositol-1,4,5-triphosphate receptor IP3 receptor IMR:0000086 GO:0004887 c-erbA thyroid hormone receptor TR IMR:0000087 cytokeratin 3 IMR:0000088 Estrogen receptor IMR:0000089 transcription factors that are activated by ligands and heterodimerize with RETINOID X RECEPTORS and bind to peroxisome proliferator response elements in the promoter regions of target genes. http://purl.bioontology.org/ontology/MESH/D047492 Peroxisome proliferator activated receptor PPAR IMR:0000090 Retinoic acid receptor RAR IMR:0000092 GO:0005024 Transforming growth factor-beta receptor TGF-beta receptor IMR:0000093 GO:0005025 Transforming growth factor-beta receptor type I TGF-beta receptor type I IMR:0000094 GO:0005026 Transforming growth factor-beta receptor type II TGF-beta receptor type II IMR:0000096 GO:0004907 interleukin receptor IMR:0000097 GO:0004911 interleukin-2 receptor IL-2 receptor IMR:0000101 GO:0004914 interleukin-5 receptor IL-5 receptor IMR:0000104 GO:0004915 interleukin-6 receptor IL-6 receptor IMR:0000107 GO:0004913 interleukin-4 receptor IL-4 receptor IMR:0000109 GO:0004912 interleukin-3 receptor IL-3 receptor IMR:0000111 GO:0004917 interleukin-7 receptor IL-7 receptor IMR:0000113 GO:0004919 interleukin-9 receptor IL-9 receptor IMR:0000115 GO:0016515 interleukin-13 receptor IL-13 receptor IMR:0000117 GO:0042010 interleukin-15 receptor IL-15 receptor IMR:0000120 GO:0004908 interleukin-1 receptor IL-1 receptor IMR:0000123 GO:0042008 IL-1Rrp IL1 receptor-related protein Interleukin-18 receptor IL-18 receptor IMR:0000125 OB-R leptin receptor IMR:0000134 GO:0004904 interferon receptor IFNR IMR:0000135 A protein family that is a translation product of the IFNAR type I gene or a 1:1 ortholog thereof. IFNAR Interferon alpha/beta receptor IFNR type I IMR:0000136 A protein family that is a translation product of the IFNAR type I gene or a 1:1 ortholog thereof. IFNGR Interferon-gamma receptor IFNR type II IMR:0000142 GO:0042611 major histocompatibility complex MHC family IMR:0000143 MHC class Ia (classical) molecules, termed human leukocyte antigen (HLA)-A, HLA-B and HLA-C in humans and H2-K, H2-D and H2-L in mice, are highly polymorphic glycoproteins composed of a single membrane-spanning alpha chain paired with the soluble protein beta2 microglobulin. MHC class Ia (classical) molecules, termed human leukocyte antigen (HLA)-A, HLA-B and HLA-C in humans and H2-K, H2-D and H2-L in mice, are highly polymorphic glycoproteins composed of a single membrane-spanning alpha chain paired with the soluble protein beta2 microglobulin. GO:0042612 MHC class Ia molecule classical MHC class I molecule major histocompatibility complex class I molecule MHC class I molecule MHC class Ia (classical) molecules, termed human leukocyte antigen (HLA)-A, HLA-B and HLA-C in humans and H2-K, H2-D and H2-L in mice, are highly polymorphic glycoproteins composed of a single membrane-spanning alpha chain paired with the soluble protein beta2 microglobulin. ISBN:0815340729 PMID:10607669 PMID:16860610 IMR:0000144 MHC class II molecules are composed of membrane-spanning alpha and beta chains. MHC class II molecules are composed of membrane-spanning alpha and beta chains. GO:0042613 classical MHC class II molecule major histocompatibility complex class II molecule MHC class II molecule MHC class II molecules are composed of membrane-spanning alpha and beta chains. ISBN:0815340729 PMID:10607669 IMR:0000146 cytokeratin 4 IMR:0000151 T-cell receptor TCR family IMR:0000153 GO:0019815 B cell receptor B cell receptor complex B-cell antigen receptor BCR complex BCR IMR:0000156 FcR IMR:0000157 FcepsilonRI IMR:0000158 High affinity immunoglobulin gamma Fc receptor I FcgammaRI IMR:0000159 Low affinity immunoglobulin gamma FC region receptor III FcgammaRIII IMR:0000160 Low affinity immunoglobulin gamma Fc region receptor II FcgammaRII IMR:0000162 cytokeratin 5 IMR:0000163 cytokeratin 7 IMR:0000164 cytokeratin 8 IMR:0000165 IMR:0000260 cytokeratin 6D cytokeratin 6A IMR:0000167 cadherin IMR:0000169 A-CAM Neural-cadherin cadherin-2 N-cadherin IMR:0000170 Retinal-cadherin cadherin-4 R-cadherin IMR:0000171 Vascular endothelial-cadherin cadherin-5 VE-cadherin IMR:0000172 Integrins comprise a large family of cell surface receptors that are found in many animal species, ranging from sponge to mammals. They are composed of two subunits, alpha and beta, and each alpha beta combination has its own binding specificity and signaling properties. Integrins comprise a large family of cell surface receptors that are found in many animal species, ranging from sponge to mammals. They are composed of two subunits, alpha and beta, and each alpha beta combination has its own binding specificity and signaling properties. integrin Integrins comprise a large family of cell surface receptors that are found in many animal species, ranging from sponge to mammals. They are composed of two subunits, alpha and beta, and each alpha beta combination has its own binding specificity and signaling properties. PMID:10446041 IMR:0000173 Integrin alpha IMR:0000174 Integrin beta IMR:0000176 alpha-catenin IMR:0000177 named 'beta-catenin family' formerly. beta-catenin IMR:0000178 intercellular adhesion molecule ICAM IMR:0000180 neuronal cell adhesion molecule N-CAM IMR:0000187 paxillin IMR:0000188 A role played by the protein contributes to the integrity of the actin cytoskeleton. IMR:0000188 (obsolete) actin filament cytoskeletal protein related cellular component GO:0015629 actin cytoskeleton protein IMR:0000189 alpha-actinin IMR:0000190 actin IMR:0000191 myosin IMR:0000192 tropomyosin IMR:0000193 Troponin, or the troponin complex, is a complex of three regulatory proteins (troponin C, troponin I, and troponin T) that are integral to muscle contraction[2] in skeletal muscle and cardiac muscle, but not smooth muscle. (https://en.wikipedia.org/wiki/Troponin) troponin IMR:0000199 kinesin IMR:0000200 dynein IMR:0000202 cytokeratin keratin IMR:0000203 GO:0005883 neurofilament protein IMR:0000204 dystrophin IMR:0000205 Adenomatous Polyposis Coli Protein APC IMR:0000206 ankyrin IMR:0000208 IMR:0000302 cytokeratin 6F cytokeratin 6B IMR:0000211 MeSH:D019061 Src family IMR:0000212 C-terminal Src kinase Csk IMR:0000217 Fak/Pyk2 IMR:0000218 GO:0004717 Focal adhesion kinase Fak IMR:0000219 CADTK Cak beta RAFTK calcium-dependent tyrosine kinase cell adhesion kinase beta prolin-rich tyrosine kinase 2 related adhesion focal tyrosine kinase Pyk2 IMR:0000220 ZAP-70/Syk IMR:0000221 ZAP-70 IMR:0000222 Spleen tyrosine kinase Syk IMR:0000224 Mammals express at least four distinctly regulated groups of MAPKs, ERK-1/2, JNK/SAPK, p38 and ERK5. MAPKs are activated by dual phosphorylation on both tyrosine and threonine residues of a conserved TXY motif. Mammals express at least four distinctly regulated groups of MAPKs, ERK-1/2, JNK/SAPK, p38 and ERK5. MAPKs are activated by dual phosphorylation on both tyrosine and threonine residues of a conserved TXY motif. GO:0004707 IPR:003527 MAP kinase mitogen-activated protein kinase MAPK Mammals express at least four distinctly regulated groups of MAPKs, ERK-1/2, JNK/SAPK, p38 and ERK5. MAPKs are activated by dual phosphorylation on both tyrosine and threonine residues of a conserved TXY motif. PMID:11242034 PMID:9922370 IMR:0000225 GO:0016909 IPR:008351 c-jun N-terminal kinase stress-activated protein kinase JNK/SAPK IMR:0000227 ERK1 and ERK2 are isoforms of the 'classical' MAPK. Both ERK1 and ERK2 (referred to as ERK1/2) are activated by MAP/ERK kinase 1 (MEK1) and MEK2 (referred to as MEK1/2). MEK1/2 phosphorylates threonine and tyrosine residues in the Thr-Glu-Tyr (TEY) sequence of ERK1/2. Activated ERK1/2 phosphorylates many substrates including transcription factors, such as Elk1 and c-Myc, and protein kinases, such as ribosomal S6 kinase (RSK). ERK1 and ERK2 are isoforms of the 'classical' MAPK. Both ERK1 and ERK2 (referred to as ERK1/2) are activated by MAP/ERK kinase 1 (MEK1) and MEK2 (referred to as MEK1/2). MEK1/2 phosphorylates threonine and tyrosine residues in the Thr-Glu-Tyr (TEY) sequence of ERK1/2. Activated ERK1/2 phosphorylates many substrates including transcription factors, such as Elk1 and c-Myc, and protein kinases, such as ribosomal S6 kinase (RSK). IPR:008349 ERK Extracellular signal-regulated kinase MAPK/ERK p42/p44 MAP kinase p42/p44 MAPK ERK1/2 ERK1 and ERK2 are isoforms of the 'classical' MAPK. Both ERK1 and ERK2 (referred to as ERK1/2) are activated by MAP/ERK kinase 1 (MEK1) and MEK2 (referred to as MEK1/2). MEK1/2 phosphorylates threonine and tyrosine residues in the Thr-Glu-Tyr (TEY) sequence of ERK1/2. Activated ERK1/2 phosphorylates many substrates including transcription factors, such as Elk1 and c-Myc, and protein kinases, such as ribosomal S6 kinase (RSK). PMID:16880823 IMR:0000229 GO:0004709 MAP kinase kinase kinase MAPKK kinase MKKK MAPKKK IMR:0000230 c-mos mos IMR:0000231 Raf IMR:0000232 MOM-4 TGF-bata activated kinase 1 TAK1 IMR:0000233 Cot Est Tumor progression locus 2 cancer Osaka thyroid oncogene Tpl2 IMR:0000234 GO:0004710 MAPK/ERK kinase kinase MEKK IMR:0000238 PAK IMR:0000239 MLK family IMR:0000242 GO:0004704 NF-kappa B-inducing kinase NIK IMR:0000244 IMR:0000270 cytokeratin 6E cytokeratin 6C IMR:0000245 GO:0004697 protein kinase C PKC IMR:0000246 novel PKC isoforms (delta, epsilon, eta and theta) are regulated by DAG and phospholipids. novel PKC isoforms (delta, epsilon, eta and theta) are regulated by DAG and phospholipids. novel protein kinase C nPKC novel PKC isoforms (delta, epsilon, eta and theta) are regulated by DAG and phospholipids. PMID:15282562 IMR:0000247 atypical PKC isoforms (zeta and lambda/iota; PKC-lambda is the mouse ortholog of human PKC-iota) are insensitive to both calcium and DAG. atypical PKC isoforms (zeta and lambda/iota; PKC-lambda is the mouse ortholog of human PKC-iota) are insensitive to both calcium and DAG. GO:0004700 atypical protein kinase C aPKC atypical PKC isoforms (zeta and lambda/iota; PKC-lambda is the mouse ortholog of human PKC-iota) are insensitive to both calcium and DAG. PMID:15282562 IMR:0000248 A family of 90 kDa ribosomal S6 kinases (RSK; also known as p90rsk or MAPK-activated protein kinase-1, MAPKAP-K1). The RSK family of kinases includes three isoforms: RSK1, RSK2 and RSK3 that are encoded by distinct genes and show 75-80% amino acid identity. RSK proteins is regulated by the ERK kinase pathway. A family of 90 kDa ribosomal S6 kinases (RSK; also known as p90rsk or MAPK-activated protein kinase-1, MAPKAP-K1). The RSK family of kinases includes three isoforms: RSK1, RSK2 and RSK3 that are encoded by distinct genes and show 75-80% amino acid identity. RSK proteins is regulated by the ERK kinase pathway. GO:0004711 90 kDa ribosomal S6 kinase MAPK-activated protein kinase-1 MAPKAP kinase-1 MAPKAP-K1 p90rsk RSK A family of 90 kDa ribosomal S6 kinases (RSK; also known as p90rsk or MAPK-activated protein kinase-1, MAPKAP-K1). The RSK family of kinases includes three isoforms: RSK1, RSK2 and RSK3 that are encoded by distinct genes and show 75-80% amino acid identity. RSK proteins is regulated by the ERK kinase pathway. PMID:10411321 IMR:0000249 PKA is comprised of two types of subunits. Two catalytic (C) subunits bind to a regulatory (R) subunit dimer to form an inactive holoenzyme complex. Binding of cAMP to the regulatory subunit causes the catalytic subunit to be unleashed. PKA is comprised of two types of subunits. Two catalytic (C) subunits bind to a regulatory (R) subunit dimer to form an inactive holoenzyme complex. Binding of cAMP to the regulatory subunit causes the catalytic subunit to be unleashed. GO:0004691 GO:0005952 cAMP-dependent protein kinase protein kinase A PKA PKA is comprised of two types of subunits. Two catalytic (C) subunits bind to a regulatory (R) subunit dimer to form an inactive holoenzyme complex. Binding of cAMP to the regulatory subunit causes the catalytic subunit to be unleashed. PMID:17996741 IMR:0000251 GO:0004692 cGMP-dependent protein kinase PKG IMR:0000252 Ste20 homolog family IMR:0000253 mammalian Ste20-like kinases (MAPKKKK) IMR:0000254 G-protein coupled receptor kinase IMR:0000256 polo-like kinase Plk IMR:0000257 GO:0004696 glycogen synthase kinase 3 GSK3 IMR:0000259 GO:0004708 MAP kinase kinase MAPK kinase MAPKK IMR:0000261 MEK1 and MEK2 phosphorylate and activate ERK1 and ERK2 MAP kinases. MEK1 and MEK2 phosphorylate and activate ERK1 and ERK2 MAP kinases. MAPKK1/2 MEK MEK1/2 MKK1/2 MEK1/2(MKK1/2) MEK1 and MEK2 phosphorylate and activate ERK1 and ERK2 MAP kinases. PMID:11242034 PMID:9922370 IMR:0000262 MKK4 and MKK7 phosphorylate and activate JNK MAP kinases. MKK4 and MKK7 phosphorylate and activate JNK MAP kinases. MKK4/7(JNKK1/2) MKK4 and MKK7 phosphorylate and activate JNK MAP kinases. PMID:11242034 PMID:9922370 IMR:0000263 MKK3 and MKK6 phosphorylate and activate p38 MAP kinases. MKK3 and MKK6 phosphorylate and activate p38 MAP kinases. MKK3/6 MKK3 and MKK6 phosphorylate and activate p38 MAP kinases. PMID:11242034 PMID:9922370 IMR:0000265 Catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol + ATP = a 1-phosphatidyl-1D-myo-inositol 3-phosphate + ADP + 2 H(+). GO:0016303 PI3K phosphatidylinositol 3-kinase PI3-kinase IMR:0000266 Phosphatidylinositol 3-kinase p85 regulatory subunit PI3-kinase p85 subunit IMR:0000267 Phosphatidylinositol 3-kinase p110 catalytic subunit PI3-kinase p110 subunit IMR:0000269 Receptor interacting protein Receptor-interacting serine/threonine protein kinase RIP IMR:0000271 Src homology-2 domain-containing inositol 5'-phosphatase SHIP IMR:0000274 SHP family IMR:0000275 HCP PTP1C SH-PTP1 Src homology 2-containing protein tyrosine phosphatase-1 SHP-1 IMR:0000276 PTP1D SH-PTP2 Src homology 2-containing protein tyrosine phosphatase-2 Syp SHP-2 IMR:0000283 phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. EC:3.1.1.4 GO:0004623 PMID:30077006 phospholipase A2 PLA2 (mol) IMR:0000284 EC:3.1.4.11 GO:0004629 phospholipase C PLC (mol) IMR:0000285 MeSH: D051966 phospholipase C gamma PLC gamma IMR:0000286 phospholipase C beta PLCbeta IMR:0000287 EC:3.1.4.4 GO:0004630 phospholipase D PLD IMR:0000289 IPR:003577 Ras family IMR:0000290 Ras GTPase RAS IMR:0000292 related to Ras R-Ras IMR:0000293 Ras-like Ral IMR:0000294 Ras proximal Rap IMR:0000295 IPR:003578 Rho family IMR:0000296 Rho IMR:0000297 Rac IMR:0000299 IPR:003579 Ras genes from rat brain Rab IMR:0000300 IPR:002041 Ras-like nuclear protein TC4 Ran IMR:0000301 Arf/Sar IMR:0000304 A protease is an enzyme that hydrolyzes the peptide bonds in a protein or a peptide. EC:3.4.-.- GO:0008233 peptidase protease IMR:0000305 GO:0030693 caspase (family) IMR:0000306 effector caspase IMR:0000308 signaling (initiator) caspase IMR:0000310 The 26S proteasome is a 2.5-MDa molecular machine built from ~31 different subunits, which catalyzes protein degradation. It contains a barrel-shaped proteolytic core complex (the 20S proteasome), capped at one or both ends by 19S regulatory complexes, which recognize ubiquitinated proteins. The 26S proteasome is a 2.5-MDa molecular machine built from ~31 different subunits, which catalyzes protein degradation. It contains a barrel-shaped proteolytic core complex (the 20S proteasome), capped at one or both ends by 19S regulatory complexes, which recognize ubiquitinated proteins. 26S proteasome The 26S proteasome is a 2.5-MDa molecular machine built from ~31 different subunits, which catalyzes protein degradation. It contains a barrel-shaped proteolytic core complex (the 20S proteasome), capped at one or both ends by 19S regulatory complexes, which recognize ubiquitinated proteins. PMID:10872471 PMID:9228274 PMID:9647729 IMR:0000316 EC:3.6.5.1 G-protein, alpha subunit Guanine nucleotide-binding protein, alpha subunit G-alpha IMR:0000317 G-alpha-s class IMR:0000318 G-alpha-i class IMR:0000319 G-alpha-i IMR:0000320 Galphao, the most abundant G protein in mammalian brain, occurs at least in two subforms, i.e., Galphao1 and Galphao2, derived by alternative splicing of the mRNA. Galphao, the most abundant G protein in mammalian brain, occurs at least in two subforms, i.e., Galphao1 and Galphao2, derived by alternative splicing of the mRNA. IMR:0100371 IMR:0100372 G-alpha-o Galphao, the most abundant G protein in mammalian brain, occurs at least in two subforms, i.e., Galphao1 and Galphao2, derived by alternative splicing of the mRNA. PMID:9990023 IMR:0000321 transducin alpha G-alpha-t IMR:0000322 G-alpha-z IMR:0000323 G-alpha-q class IMR:0000324 G-alpha-12/13 class IMR:0000327 Catalysis role of the reaction: E1 + ubiquitin + ATP--> E1-ubiquitin + AMP + PPi, where the E1-ubiquitin linkage is a thioester bond between the C-terminal glycine of Ub and a sulfhydryl side group of an E1 cysteine residue. This is the first step in a cascade of reactions in which ubiquitin is ultimately added to a protein substrate. EC:6.2.1.45 IMR:0000327 (obsolete) Wikipedia:Ubiquitin-activating_enzyme E1 ubiquitin-activating enzyme E1 ubiquitin-activating enzyme ubiquitin-activating enzyme (E1) related molecular function GO:0004839 ubiquitin activating enzyme E1 ubiquitin-activating enzyme http://enzyme.expasy.org/EC/6.2.1.45 IMR:0000331 EC:1.14.99.1 prostaglandin endoperoxide synthase COX IMR:0000335 Alternative splicing of the mammal crk gene yields two translation products designated the 28-kDa Crk-I and the 42-kDa Crk-II protein. Alternative splicing of the mammal crk gene yields two translation products designated the 28-kDa Crk-I and the 42-kDa Crk-II protein. CT-10 regulator of kinase Proto-oncogene C-crk Crk Alternative splicing of the mammal crk gene yields two translation products designated the 28-kDa Crk-I and the 42-kDa Crk-II protein. PMID:10393272 IMR:0000336 Crk I IMR:0000337 Crk-like protein Crk-L IMR:0000338 Crk II IMR:0000339 The best characterised member of the SH2/SH3 adaptor protein family is Grb2, the human homologue of the nematode Caenorhabditis elegans protein Sem-5. The structure of Grb2 consists of one SH2 domain flanked by two SH3 domains. Recently, further members of the Grb2 family have been isolated, Grap protein and Gads. The best characterised member of the SH2/SH3 adaptor protein family is Grb2, the human homologue of the nematode Caenorhabditis elegans protein Sem-5. The structure of Grb2 consists of one SH2 domain flanked by two SH3 domains. Recently, further members of the Grb2 family have been isolated, Grap protein and Gads. Grb2 family The best characterised member of the SH2/SH3 adaptor protein family is Grb2, the human homologue of the nematode Caenorhabditis elegans protein Sem-5. The structure of Grb2 consists of one SH2 domain flanked by two SH3 domains. Recently, further members of the Grb2 family have been isolated, Grap protein and Gads. PMID:10393272 IMR:0000340 IMR:0010276 ASH protein Ash GRB2 adapter protein Growth factor receptor-bound protein 2 SH2/SH3 adapter GRB2 abundant Src homology protein growth factor receptor bound protein 2 Grb2 IMR:0000341 Grb2-related adaptor protein Grap IMR:0000342 The widely expressed Nck is a 47-kDa cytosolic protein exclusively composed of one SH2 and three SH3 domains. Recently, a second member of the Nck family has been isolated (Nck beta/Grb4) which shows 68% amino acid identity to Nck (Nck alpha). The widely expressed Nck is a 47-kDa cytosolic protein exclusively composed of one SH2 and three SH3 domains. Recently, a second member of the Nck family has been isolated (Nck beta/Grb4) which shows 68% amino acid identity to Nck (Nck alpha). Nck family The widely expressed Nck is a 47-kDa cytosolic protein exclusively composed of one SH2 and three SH3 domains. Recently, a second member of the Nck family has been isolated (Nck beta/Grb4) which shows 68% amino acid identity to Nck (Nck alpha). PMID:10393272 IMR:0000343 IMR:0011207 Cytoplasmic protein NCK1 IRS-4a-P NCK adaptor protein 1 Nck alpha SH2/SH3 adaptor protein NCK-alpha Nck IMR:0000344 IMR:0011208 Cytoplasmic protein NCK2 IRS-4b-P NCK adaptor protein 2 Nck-2 SH2/SH3 adaptor protein NCK-beta Nck beta/Grb4 IMR:0000347 src homology and collagen Shc IMR:0000350 SH2 domain-containing leukocyte protein of 76 kD SLP-76 IMR:0000351 insulin receptor substrate IRS IMR:0000352 cytokeratin 9 IMR:0000353 BLNK/SLP-65 IMR:0000356 Cbl IMR:0000357 Growth factor receptor-bound protein 7 Grb7 IMR:0000362 cytokeratin 10 IMR:0000363 cytokeratin 12 IMR:0000364 cytokeratin 13 IMR:0000365 cytokeratin 14 IMR:0000366 cytokeratin 15 IMR:0000367 cytokeratin 16 IMR:0000371 There are five vertebrate R-Smads, Smad1, Smad2, Smad3, Smad5 and Smad8 and they are phosphorylated in response to different types of TGF-beta ligands. Phosphorylated R-Smads can form complexes with Smad4 and positively or negatively regulate transcription. The Mad protein in Drosophila is the ortholog of Smad1/5, whereas dSmad2 is the ortholog of Smad2/3. In C. elegans, sma-2 and sma-3 proved to be homologous to Mad of Drosophila. There are five vertebrate R-Smads, Smad1, Smad2, Smad3, Smad5 and Smad8 and they are phosphorylated in response to different types of TGF-beta ligands. Phosphorylated R-Smads can form complexes with Smad4 and positively or negatively regulate transcription. The Mad protein in Drosophila is the ortholog of Smad1/5, whereas dSmad2 is the ortholog of Smad2/3. In C. elegans, sma-2 and sma-3 proved to be homologous to Mad of Drosophila. receptor-activated Smad receptor-regulated Smad R-Smad There are five vertebrate R-Smads, Smad1, Smad2, Smad3, Smad5 and Smad8 and they are phosphorylated in response to different types of TGF-beta ligands. Phosphorylated R-Smads can form complexes with Smad4 and positively or negatively regulate transcription. The Mad protein in Drosophila is the ortholog of Smad1/5, whereas dSmad2 is the ortholog of Smad2/3. In C. elegans, sma-2 and sma-3 proved to be homologous to Mad of Drosophila. PMID:16322555 PMID:18061509 PMID:9393997 PMID:9880789 IMR:0000372 Co-Smad forms hetero-oligomers with R-Smads, which in turn translocate into the nucleus and regulate transcriptional responses. Only Smad4 has been identified as a common-mediator Smad in vertebrates. A Smad4 homologue has been identified in Drosophila (Medea) and C. elegans (Sma-4). Co-Smad forms hetero-oligomers with R-Smads, which in turn translocate into the nucleus and regulate transcriptional responses. Only Smad4 has been identified as a common-mediator Smad in vertebrates. A Smad4 homologue has been identified in Drosophila (Medea) and C. elegans (Sma-4). Smad4 co-mediator Smad common Smad common-mediator Smad common-partner Smad Co-Smad Co-Smad forms hetero-oligomers with R-Smads, which in turn translocate into the nucleus and regulate transcriptional responses. Only Smad4 has been identified as a common-mediator Smad in vertebrates. A Smad4 homologue has been identified in Drosophila (Medea) and C. elegans (Sma-4). PMID:16322555 PMID:9393997 IMR:0000373 Smad6 and Smad7 are inhibitory Smads that serve as decoys interfering with Smad-receptor or Smad-Smad interactions. Inhibitory Smads have also been detected in Drosophila (Dad). Smad6 and Smad7 are inhibitory Smads that serve as decoys interfering with Smad-receptor or Smad-Smad interactions. Inhibitory Smads have also been detected in Drosophila (Dad). inhibitory Smad I-Smad Smad6 and Smad7 are inhibitory Smads that serve as decoys interfering with Smad-receptor or Smad-Smad interactions. Inhibitory Smads have also been detected in Drosophila (Dad). PMID:16322555 PMID:9393997 IMR:0000376 signal transducer and activator of transcription 2 STAT2 IMR:0000378 signal transducer and activator of transcription 4 STAT4 IMR:0000379 signal transducer and activator of transcription 5a STAT5a IMR:0000380 signal transducer and activator of transcription 5b STAT5b IMR:0000381 signal transducer and activator of transcription 6 STAT6 IMR:0000383 NCBI-Human-GeneID:4609 NCBI-Mouse-GeneID:17869 NCBI-Rat-GeneID:24577 c-Myc Myc (mol) NCBI-Human-GeneID:4609 http://www.ncbi.nlm.nih.gov/gene/4609 NCBI-Mouse-GeneID:17869 http://www.ncbi.nlm.nih.gov/gene/17869 NCBI-Rat-GeneID:24577 http://www.ncbi.nlm.nih.gov/gene/24577 IMR:0000397 IPR:000418 E26 transformation-specific ets IMR:0000398 ets-related gene ERG IMR:0000402 EGR family IMR:0000403 Krox24 NGFI-A TIS8 Zif268 pAT225 EGR1 (mol) IMR:0000404 Krox20 pAT591 EGR2 IMR:0000405 EGR3 IMR:0000406 NGFI-C pAT133 EGR4 IMR:0000408 c-Myb Myb IMR:0000409 The NFI family is composed of four members in vertebrates (NFI-A, NFI-B, NFI-C and NFI-X). The NFI family is composed of four members in vertebrates (NFI-A, NFI-B, NFI-C and NFI-X). IPR:000647 CCAAT box-binding transcription factor CTF NFI nuclear factor 1 NF1 (mol) The NFI family is composed of four members in vertebrates (NFI-A, NFI-B, NFI-C and NFI-X). PMID:10831836 IMR:0000411 IPR:004826 musculoaponeurotic fibrosarcoma Maf family IMR:0000413 cytokeratin 17 IMR:0000414 The AP-1 (activator protein 1) transcription factor is a dimeric complex that comprises members of the JUN, FOS, ATF (activating transcription factor) and MAF (musculoaponeurotic fibrosarcoma) protein families. The AP-1 complex can therefore form many different combinations of heterodimers and homodimers, and this combination determines the genes that are regulated by AP-1. The AP-1 (activator protein 1) transcription factor is a dimeric complex that comprises members of the JUN, FOS, ATF (activating transcription factor) and MAF (musculoaponeurotic fibrosarcoma) protein families. The AP-1 complex can therefore form many different combinations of heterodimers and homodimers, and this combination determines the genes that are regulated by AP-1. AP-1 The AP-1 (activator protein 1) transcription factor is a dimeric complex that comprises members of the JUN, FOS, ATF (activating transcription factor) and MAF (musculoaponeurotic fibrosarcoma) protein families. The AP-1 complex can therefore form many different combinations of heterodimers and homodimers, and this combination determines the genes that are regulated by AP-1. PMID:14668816 IMR:0000415 IPR:000837 FOS family IMR:0000416 IPR:002112 JUN (mol) IMR:0000417 BCL-6 belongs to a subset of transcription factors which all have a similar structure composed of an amino-terminal 'POZ' domain and several zinc finger modules at the carboxy-terminus. BCL-6 is highly conserved among vertebrate species. BCL-6 homologues have been identified from human, mouse, frog, and chicken species. BCL-6 belongs to a subset of transcription factors which all have a similar structure composed of an amino-terminal 'POZ' domain and several zinc finger modules at the carboxy-terminus. BCL-6 is highly conserved among vertebrate species. BCL-6 homologues have been identified from human, mouse, frog, and chicken species. BCL-6 BCL-6 belongs to a subset of transcription factors which all have a similar structure composed of an amino-terminal 'POZ' domain and several zinc finger modules at the carboxy-terminus. BCL-6 is highly conserved among vertebrate species. BCL-6 homologues have been identified from human, mouse, frog, and chicken species. PMID:11796228 IMR:0000418 T-cell factor/lymphoid-enhancer factor TCF/LEF-1 family IMR:0000421 NFAT proteins are a family of transcription factors (NFATC1~C4) whose activation is controlled by calcineurin, a Ca2+-dependent phosphatase. NFAT proteins are a family of transcription factors (NFATC1~C4) whose activation is controlled by calcineurin, a Ca2+-dependent phosphatase. Nuclear factor of activated T-cells NF-AT NFAT proteins are a family of transcription factors (NFATC1~C4) whose activation is controlled by calcineurin, a Ca2+-dependent phosphatase. PMID:11877454 PMID:11983154 IMR:0000422 CCAAT/enhancer binding protein C/EBP IMR:0000426 p300/CBP IMR:0000431 RGS proteins act as negative regulators of G protein dependent signaling, at least in part, because they stimulate hydrolysis of the GTP bound to activated G alpha subunits. RGS proteins act as negative regulators of G protein dependent signaling, at least in part, because they stimulate hydrolysis of the GTP bound to activated G alpha subunits. GO:0016299 regulator of G protein signaling RGS RGS proteins act as negative regulators of G protein dependent signaling, at least in part, because they stimulate hydrolysis of the GTP bound to activated G alpha subunits. PMID:9064301 IMR:0000432 Axin/conductin Axin IMR:0000433 GO:0005085 guanine nucleotide exchange factor GEF IMR:0000435 Drosophila Son of Sevenless (SOS) is homologous to the yeast exchange factor for Ras, CDC25. Mammalian cells contain two closely related homologs of Drosophila SOS: SOS1 and SOS2. Biochemical studies have established that SOS indeed functions as a guanine nucleotide exchange factor for Ras. Drosophila Son of Sevenless (SOS) is homologous to the yeast exchange factor for Ras, CDC25. Mammalian cells contain two closely related homologs of Drosophila SOS: SOS1 and SOS2. Biochemical studies have established that SOS indeed functions as a guanine nucleotide exchange factor for Ras. son of sevenless Sos Drosophila Son of Sevenless (SOS) is homologous to the yeast exchange factor for Ras, CDC25. Mammalian cells contain two closely related homologs of Drosophila SOS: SOS1 and SOS2. Biochemical studies have established that SOS indeed functions as a guanine nucleotide exchange factor for Ras. UniProt:12177507 IMR:0000439 GO:0008321 Ral guanine nucleotide exchange factor RalGEF IMR:0000440 RasGRF IMR:0000442 A role played by the protein that binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP. GTPase activating protein GTPase activator GAP IMR:0000443 GO:0005099 Ras GTPase-activating protein Ras GAP IMR:0000444 GO:0005092 GDP-dissociation inhibitor guanine nucleotide dissociation inhibitor GDI IMR:0000445 GO:0004861 cyclin-dependent kinase inhibitor cyclin-dependent protein kinase inhibitor CKI IMR:0000446 Cip/Kip family IMR:0000447 INK4 family IMR:0000451 The Bcl-2 family consists of about 20 homologues of important pro- and anti-apoptotic regulators of programmed cell death. The Bcl-2 family consists of about 20 homologues of important pro- and anti-apoptotic regulators of programmed cell death. B cell lymphoma/leukemia-2 family Bcl-2 family The Bcl-2 family consists of about 20 homologues of important pro- and anti-apoptotic regulators of programmed cell death. PMID:14634621 PMID:14996506 IMR:0000454 inhibitor of apoptosis-family IAP-family IMR:0000458 cytokeratin 18 IMR:0000459 cytokeratin 19 IMR:0000460 CIS Cytokine-inducible SH2 protein SSI STAT induced STAT inhibitor Suppressor of cytokine signaling SOCS IMR:0000462 TNF receptor associated factor family TRAF family IMR:0000463 I-kappaB family IMR:0000466 cytokeratin 20 IMR:0000467 cytokeratin 23 IMR:0000469 cytokeratin 6 IMR:0000471 cytokeratin 21 IMR:0000472 NF-H IMR:0000474 NF-L IMR:0000475 NF-M IMR:0000479 alpha-actinin 1 IMR:0000483 alpha-actinin 2 IMR:0000484 alpha-actinin 3 IMR:0000485 alpha-actinin 4 IMR:0000486 cytoplasmic actin beta-actin IMR:0000487 cardiac muscle actin alpha-cardiac actin IMR:0000488 gamma-actin IMR:0000489 skeletal muscle alpha-actin alpha-actin 1 IMR:0000490 alpha-actin IMR:0000491 gamma-actin 2 gamma-enteric actin smooth muscle (enteric type) gamma-actin smooth muscle gamma-actin alpha-actin 3 IMR:0000492 smooth muscle alpha-actin (aortic type) alpha-actin 2 IMR:0000515 caveolin IMR:0000520 arrestin IMR:0000522 Aquaporin IMR:0000526 connexin IMR:0000535 myelin protein IMR:0000546 fibronectin IMR:0000547 elastin IMR:0000552 Proteoglycans are a diverse family of molecules characterized by a core protein to which is attached one or more glycosaminoglycan (GAG) side-chains. Proteoglycans are a diverse family of molecules characterized by a core protein to which is attached one or more glycosaminoglycan (GAG) side-chains. proteoglycan Proteoglycans are a diverse family of molecules characterized by a core protein to which is attached one or more glycosaminoglycan (GAG) side-chains. ISBN:0120689111 IMR:0000554 laminin family IMR:0000555 kalinin IMR:0000558 disabled IMR:0000559 The MyD118/CR6/Gadd45 gene family (also termed Gadd45b, Gadd45g, Gadd45a) encodes for small (18 kd), evolutionary conserved proteins that are highly homologous to each other (55 57% overall identity at the amino acid level), are highly acidic (pI=4.0 4.2), and are primarily localized within the cell nucleus. MyD118/CR6/GADD45 serve similar, but not identical, functions along different apoptotic and growth inhibitory pathways. They interact with cell cycle proteins. The MyD118/CR6/Gadd45 gene family (also termed Gadd45b, Gadd45g, Gadd45a) encodes for small (18 kd), evolutionary conserved proteins that are highly homologous to each other (55 57% overall identity at the amino acid level), are highly acidic (pI=4.0 4.2), and are primarily localized within the cell nucleus. MyD118/CR6/GADD45 serve similar, but not identical, functions along different apoptotic and growth inhibitory pathways. They interact with cell cycle proteins. growth arrest and DNA damage inducible 45 GADD45 The MyD118/CR6/Gadd45 gene family (also termed Gadd45b, Gadd45g, Gadd45a) encodes for small (18 kd), evolutionary conserved proteins that are highly homologous to each other (55 57% overall identity at the amino acid level), are highly acidic (pI=4.0 4.2), and are primarily localized within the cell nucleus. MyD118/CR6/GADD45 serve similar, but not identical, functions along different apoptotic and growth inhibitory pathways. They interact with cell cycle proteins. PMID:12032777 IMR:0000560 presenilin IMR:0000568 Placental-cadherin cadherin-3 P-cadherin IMR:0000569 Kidney-cadherin cadherin-6 K-cadherin IMR:0000574 IFN alpha-4 IMR:0000575 IFN alpha-5 IMR:0000576 IFN alpha-6 IMR:0000577 IFN alpha-7 IMR:0000578 IFN alpha-8 IMR:0000579 IFN alpha-9 IMR:0000580 IFN alpha-10 IMR:0000581 IFN alpha-14 IMR:0000582 IFN alpha-16 IMR:0000583 IFN alpha-17 IMR:0000584 IFN alpha-21 IMR:0000593 IL-1RI : IL-1R AcP IMR:0000594 IL-1RII : IL-1R AcP IMR:0000600 GO:0030368 interleukin-17 receptor IL-17 receptor IMR:0000602 GO:0016517 interleukin-12 receptor IL-12 receptor IMR:0000605 GO:0004918 interleukin-8 receptor IL-8 receptor IMR:0000606 interleukin-8 receptor A IL-8RA IMR:0000607 interleukin-8 receptor B IL-8RB IMR:0000608 GO:0004920 interleukin-10 receptor IL-10 receptor IMR:0000611 GO:0004921 IL-11 receptor IMR:0000614 NRG-1 neuregulin-1 IMR:0000615 NRG-2 neuregulin-2 IMR:0000616 NRG-3 neuregulin-3 IMR:0000617 NRG-4 neuregulin-4 IMR:0000618 intercellular adhesion molecule 1 ICAM-1 IMR:0000619 intercellular adhesion molecule 2 ICAM-2 IMR:0000620 intercellular adhesion molecule 3 ICAM-3 IMR:0000621 intercellular adhesion molecule 4 ICAM-4 IMR:0000622 intercellular adhesion molecule 5 ICAM-5 IMR:0000623 Integrin alpha-1 IMR:0000624 Integrin alpha-2 IMR:0000625 Integrin alpha-3 IMR:0000626 Integrin alpha-4 IMR:0000627 Integrin alpha-5 IMR:0000628 Integrin alpha-6 IMR:0000629 Integrin alpha-7 IMR:0000630 Integrin alpha-8 IMR:0000631 Integrin alpha-9 IMR:0000632 Integrin alpha-10 IMR:0000633 Integrin alpha-11 IMR:0000634 Integrin alpha-IIb IMR:0000635 Integrin alpha-D IMR:0000636 Integrin alpha-E IMR:0000637 Integrin alpha-L IMR:0000638 Integrin alpha-M IMR:0000639 Integrin alpha-V IMR:0000640 Integrin alpha-X IMR:0000641 Integrin beta-1 IMR:0000642 Integrin beta-2 IMR:0000643 Integrin beta-3 IMR:0000644 Integrin beta-4 IMR:0000645 Integrin beta-5 IMR:0000646 Integrin beta-6 IMR:0000647 Integrin beta-7 IMR:0000648 Integrin beta-8 IMR:0000649 CD44 (mol) IMR:0000650 LFA-1 IMR:0000669 PAK2 IMR:0000670 PAK3 IMR:0000671 PAK4 IMR:0000672 PAK5 PAK6 IMR:0000673 PAK5 PAK7 IMR:0000674 A-Raf IMR:0000675 B-Raf IMR:0000676 IMR:0000678 type I alpha cGMP-dependent protein kinase type I beta cGMP-dependent protein kinase cGMP-dependent protein kinase I IMR:0000677 type II cGMP-dependent protein kinase cGMP-dependent protein kinase II IMR:0000679 Plk1 IMR:0000680 Plk3 IMR:0000683 SAPK-1 p54 gamma SAPK JNK1 IMR:0000684 p54 alpha SAPK JNK2 IMR:0000685 p54 beta SAPK JNK3 IMR:0000695 IMR:0011341 NCBI-Human-GeneID:3265 NCBI-Mouse-GeneID:15461 NCBI-Rat-GeneID:293621 H-Ras HRAS Ha-ras Transforming protein p21/H-Ras-1 c-H-ras HRAS (mol) NCBI-Human-GeneID:3265 https://www.ncbi.nlm.nih.gov/gene/3265 NCBI-Mouse-GeneID:15461 https://www.ncbi.nlm.nih.gov/gene/15461 NCBI-Rat-GeneID:293621 https://www.ncbi.nlm.nih.gov/gene/293621 IMR:0000696 IMR:0011343 NCBI-Human-GeneID:4893 NCBI-Mouse-GeneID:18176 NCBI-Rat-GeneID:24605 N-Ras Transforming protein N-Ras NRAS NCBI-Human-GeneID:4893 https://www.ncbi.nlm.nih.gov/gene/4893 NCBI-Mouse-GeneID:18176 https://www.ncbi.nlm.nih.gov/gene/18176 NCBI-Rat-GeneID:24605 https://www.ncbi.nlm.nih.gov/gene/24605 IMR:0000697 IMR:0011342 K-Ras 2A K-Ras4A KRAS2 Ki-Ras Transforming protein p21A c-K-ras K-Ras2A IMR:0000698 K-Ras4B K-Ras2B IMR:0000699 Cdc42 IMR:0000701 GO:0008384 I-kappaB kinase family IKK family IMR:0000714 phospholipase C beta 1 PLCbeta1 IMR:0000715 phospholipase C beta 2 PLCbeta2 IMR:0000716 phospholipase C beta 3 PLCbeta3 IMR:0000717 phospholipase C beta 4 PLCbeta4 IMR:0000728 phospholipase D1 PLD1 IMR:0000729 phospholipase D2 PLD2 IMR:0000732 phospholipase C gamma 1 PLC gamma1 IMR:0000733 phospholipase C gamma 2 PLC gamma2 IMR:0000734 prostaglandin endoperoxide synthase 2 COX-1 IMR:0000735 NCBI-Human-GeneID:5743 NCBI-Mouse-GeneID:19225 NCBI-Rat-GeneID:29527 cyclooxygenase 2 prostaglandin endoperoxide synthase 2 COX-2 (mol) NCBI-Human-GeneID:5743 https://www.ncbi.nlm.nih.gov/gene/5743 NCBI-Mouse-GeneID:19225 https://www.ncbi.nlm.nih.gov/gene/19225 NCBI-Rat-GeneID:29527 https://www.ncbi.nlm.nih.gov/gene/29527 IMR:0000736 IMR:0010277 GRB10 adaptor protein Growth factor receptor-bound protein 10 Insulin receptor binding protein GRB-IR Grb10 IMR:0000737 Grb14 IMR:0000738 IMR:0010596 IMR:0011555 ShcA IMR:0000739 ShcB IMR:0000740 ShcC IMR:0000741 Gads is a member of the family of SH2 and SH3 domain containing adaptor proteins that is expressed specifically in hematopoietic cells and functions in the coordination of tyrosine kinase mediated signal transduction. Gads is a unique member of the Grb2 adaptor family. Gads is a member of the family of SH2 and SH3 domain containing adaptor proteins that is expressed specifically in hematopoietic cells and functions in the coordination of tyrosine kinase mediated signal transduction. Gads is a unique member of the Grb2 adaptor family. Grb2-related adaptor downstream of Shc Gads Gads is a member of the family of SH2 and SH3 domain containing adaptor proteins that is expressed specifically in hematopoietic cells and functions in the coordination of tyrosine kinase mediated signal transduction. Gads is a unique member of the Grb2 adaptor family. PMID:11607830 IMR:0000745 Alternative splicing of the mammal crk gene yields two translation products designated the 28-kDa Crk-I and the 42-kDa Crk-II protein. The Crk-II protein contains an amino-terminal SH2 domain followed by two SH3 domains. The Crk-I protein does not contain the second SH3 domain. The 36-kDa Crk-L protein is similar to CrkII, but is encoded by a separate gene. Alternative splicing of the mammal crk gene yields two translation products designated the 28-kDa Crk-I and the 42-kDa Crk-II protein. The Crk-II protein contains an amino-terminal SH2 domain followed by two SH3 domains. The Crk-I protein does not contain the second SH3 domain. The 36-kDa Crk-L protein is similar to CrkII, but is encoded by a separate gene. Crk family Alternative splicing of the mammal crk gene yields two translation products designated the 28-kDa Crk-I and the 42-kDa Crk-II protein. The Crk-II protein contains an amino-terminal SH2 domain followed by two SH3 domains. The Crk-I protein does not contain the second SH3 domain. The 36-kDa Crk-L protein is similar to CrkII, but is encoded by a separate gene. PMID:10393272 IMR:0000774 RyR ryanodine receptor IMR:0000805 GADD45 alpha IMR:0000806 MyD118 GADD45 beta IMR:0000807 CR6 GADD45 gamma IMR:0000808 disabled-1 IMR:0000809 DOC-2 disabled-2 IMR:0000811 B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. B7.1 CD80 B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. PMID:14647476 IMR:0000812 B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. B7.2 CD86 B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. PMID:14647476 IMR:0000813 c-FOS IMR:0000814 FOSB IMR:0000815 FRA-1 IMR:0000816 FRA-2 IMR:0000817 AP-1 c-JUN IMR:0000818 JUNB (mol) IMR:0000819 JUND (mol) IMR:0000820 c-Maf IMR:0000821 MafF IMR:0000822 MafG IMR:0000823 MafK IMR:0000824 MafB IMR:0000825 activating transcription factor ATF IMR:0000826 activating transcription factor 1 ATF-1 (mol) IMR:0000827 activating transcription factor 2 ATF-2 (mol) IMR:0000830 activating transcription factor 5 ATF-5 (mol) IMR:0000831 activating transcription factor 6 alpha ATF-6 alpha IMR:0000832 activating transcription factor 6 beta ATF-6 beta IMR:0000833 ATF-a activating transcription factor 7 ATF-7 (mol) IMR:0000834 CCAAT/enhancer binding protein alpha C/EBP alpha IMR:0000835 CCAAT/enhancer binding protein beta C/EBP beta IMR:0000836 CCAAT/enhancer binding protein delta C/EBP delta IMR:0000837 CCAAT/enhancer binding protein gamma C/EBP gamma IMR:0000838 CCAAT/enhancer binding protein epsilon C/EBP epsilon IMR:0000855 NF-ATc1 IMR:0000856 NF-ATc2 IMR:0000857 NF-ATc3 IMR:0000858 NF-ATc4 IMR:0000866 A-Myb IMR:0000867 B-Myb IMR:0000868 Myb family IMR:0000869 IMR:0010365 CCAAT-box binding transcription factor CTF NF-I/A NF1-A NFI-A Nuclear factor 1 A-type Nuclear factor 1/A TGGCA-binding protein NF1-A IMR:0000870 IMR:0010366 CCAAT-box binding transcription factor CTF NF-I/B NF1-B NFI-B Nuclear factor 1 B-type Nuclear factor 1/B TGGCA-binding protein NF1-B IMR:0000871 IMR:0010367 CCAAT-box binding transcription factor CTF NF-I/C NF1-C NFI-C Nuclear factor 1 C-type Nuclear factor 1/C TGGCA-binding protein NF1-C IMR:0000872 IMR:0010368 CCAAT-box binding transcription factor CTF NF-I/X NF1-X NFI-X Nuclear factor 1 X-type Nuclear factor 1/X TGGCA-binding protein NF1-X IMR:0000873 NF-kappaB2 NFKB2 p100 p52 IMR:0000877 CHEBI:24020 fat-soluble vitamin IMR:0000883 TFIIA IMR:0000884 TFIID IMR:0000885 TFIIE IMR:0000886 TFIIF IMR:0000887 TFIIH IMR:0000888 pol II general transcription factor transcription factor for RNA polymerase II TFII IMR:0000890 IL-1 receptor-associated kinase 1 Interleukin-1 receptor-associated kinase 1 IRAK-1 IMR:0000891 IL-1 receptor-associated kinase 2 Interleukin-1 receptor-associated kinase-2 IRAK-2 IMR:0000892 IL-1 receptor-associated kinase 4 Interleukin-1 receptor-associated kinase-4 IRAK-4 IMR:0000894 Toll-interacting protein Tollip IMR:0000896 40S ribosomal protein IMR:0000897 60S ribosomal protein IMR:0000902 heterotrimer of alpha, beta, gamma subunits. binds the initiator Met-tRNA to the 40S ribosomal subunit. GTP binding to eIF2 is necessary for formation of a stable eIF2:GTP:Met-tRNA ternary complex (TC). Following TC binding to the ribosome triggers GTP hydrolysis by eIF2. heterotrimer of alpha, beta, gamma subunits. binds the initiator Met-tRNA to the 40S ribosomal subunit. GTP binding to eIF2 is necessary for formation of a stable eIF2:GTP:Met-tRNA ternary complex (TC). Following TC binding to the ribosome triggers GTP hydrolysis by eIF2. eukaryotic initiation factor 2 eIF2 heterotrimer of alpha, beta, gamma subunits. binds the initiator Met-tRNA to the 40S ribosomal subunit. GTP binding to eIF2 is necessary for formation of a stable eIF2:GTP:Met-tRNA ternary complex (TC). Following TC binding to the ribosome triggers GTP hydrolysis by eIF2. PMID:12581660 PMID:14635255 IMR:0000903 heteropentamer of alpha, beta, gamma, delta, epsilon subunits. guanine nucleotide exchange factor (GEF) activity of eIF2B is necessary to recycle eIF2:GTP to eIF2:GTP. heteropentamer of alpha, beta, gamma, delta, epsilon subunits. guanine nucleotide exchange factor (GEF) activity of eIF2B is necessary to recycle eIF2:GTP to eIF2:GTP. eukaryotic initiation factor 2B eIF2B heteropentamer of alpha, beta, gamma, delta, epsilon subunits. guanine nucleotide exchange factor (GEF) activity of eIF2B is necessary to recycle eIF2:GTP to eIF2:GTP. PMID:12581660 PMID:14635255 IMR:0000904 consists of a core of five non-identical subunits (eIF3a, eIF3b, eIF3c, eIF3i and eIF3g in yeast) and up to six additional subunits in mammals (eIF3d, eIF3e, eIF3f, eIF3h, eIFj and eIF3k). binding to and stabilization of ternary complex, binding to the 40S ribosome, facilitating the binding of mRNA to the 40S ribosome, and promoting dissociation of 40S and 60S ribosomal subunits consists of a core of five non-identical subunits (eIF3a, eIF3b, eIF3c, eIF3i and eIF3g in yeast) and up to six additional subunits in mammals (eIF3d, eIF3e, eIF3f, eIF3h, eIFj and eIF3k). binding to and stabilization of ternary complex, binding to the 40S ribosome, facilitating the binding of mRNA to the 40S ribosome, and promoting dissociation of 40S and 60S ribosomal subunits eukaryotic initiation factor 3 eIF3 consists of a core of five non-identical subunits (eIF3a, eIF3b, eIF3c, eIF3i and eIF3g in yeast) and up to six additional subunits in mammals (eIF3d, eIF3e, eIF3f, eIF3h, eIFj and eIF3k). binding to and stabilization of ternary complex, binding to the 40S ribosome, facilitating the binding of mRNA to the 40S ribosome, and promoting dissociation of 40S and 60S ribosomal subunits PMID:11426420 PMID:14635255 IMR:0000906 eIF4A is a DEADbox helicase that can unwind RNA secondary structure in the cap-proximal region of the mRNA. eIF4A is a DEADbox helicase that can unwind RNA secondary structure in the cap-proximal region of the mRNA. eukaryotic initiation factor 4A eIF4A eIF4A is a DEADbox helicase that can unwind RNA secondary structure in the cap-proximal region of the mRNA. PMID:14635255 IMR:0000908 eIF1 (mol) IMR:0000909 eIF4F is a heterotrimeric complex that binds to the cap structure at the 50 end of the mRNA. It is composed of eIF4G and the cap-binding protein eIF4E and the ATPdependent RNA helicase eIF4A. eIF4F is a heterotrimeric complex that binds to the cap structure at the 50 end of the mRNA. It is composed of eIF4G and the cap-binding protein eIF4E and the ATPdependent RNA helicase eIF4A. eIF4F eIF4F is a heterotrimeric complex that binds to the cap structure at the 50 end of the mRNA. It is composed of eIF4G and the cap-binding protein eIF4E and the ATPdependent RNA helicase eIF4A. PMID:14635255 IMR:0000910 Mammalian cells contain two isoforms of eIF4G (I&II). eIF4G is a subunit of the heterotrimeric eIF4F complex that binds to the cap structure at the 50 end of the mRNA. Mammalian cells contain two isoforms of eIF4G (I&II). eIF4G is a subunit of the heterotrimeric eIF4F complex that binds to the cap structure at the 50 end of the mRNA. eukaryotic translation initiation factor 4G eIF4G Mammalian cells contain two isoforms of eIF4G (I&II). eIF4G is a subunit of the heterotrimeric eIF4F complex that binds to the cap structure at the 50 end of the mRNA. PMID:14635255 IMR:0000911 Eukaryotic translation initiation factor 4 gamma 3 eIF-4-gamma 3 eIF-4-gamma II eIF-4G 3 eIF4G 3 eIF4GII IMR:0000912 eIF4F subunit IMR:0000913 eIF2 subunit IMR:0000915 eIF2B subunit IMR:0000916 eIF3 subunit IMR:0000962 LDL receptor-related protein 3 low density lipoprotein receptor-related protein 3 LRP3 IMR:0000963 LDL receptor-related protein 4 low density lipoprotein receptor-related protein 4 LRP4 IMR:0000964 LDL receptor-related protein 5 LRP7 low density lipoprotein receptor-related protein 5 LRP5 IMR:0000966 chemical hormone IMR:0000970 LDL receptor-related protein 6 low density lipoprotein receptor-related protein 6 LRP6 IMR:0000973 LDL receptor-related protein 8 low density lipoprotein receptor-related protein 8 LRP8 (mol) IMR:0000974 GO:0005041 LDLR family low density lipoprotein receptor family low-density lipoprotein receptor family LDL receptor family IMR:0000975 LDL receptor-related protein 1B LRP1B IMR:0000976 LDL receptor-related protein 10 LRP10 IMR:0000977 LDL receptor-related protein 11 LRP11 IMR:0000978 LDL receptor-related protein 12 LRP12 IMR:0000979 low density lipoprotein receptor low-density lipoprotein receptor LDL receptor IMR:0001016 cAMP-specific 3',5'-cyclic phosphodiesterase 4A IMR:0001017 cAMP-specific 3',5'-cyclic phosphodiesterase 4B IMR:0001018 cAMP-specific 3',5'-cyclic phosphodiesterase 4C IMR:0001019 cAMP-specific 3',5'-cyclic phosphodiesterase 4D IMR:0001020 High-affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A IMR:0001021 cAMP-specific 3',5'-cyclic phosphodiesterase 7B IMR:0001022 CGB-PDE cGMP-binding cGMP-specific phosphodiesterase cGMP-specific 3',5'-cyclic phosphodiesterase IMR:0001023 High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A IMR:0001024 GMP-PDE gamma Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase gamma-subunit IMR:0001025 Rod cGMP-specific 3',5'-cyclic phosphodiesterase alpha-subunit IMR:0001026 GMP-PDE beta Rod cGMP-specific 3',5'-cyclic phosphodiesterase beta-subunit IMR:0001027 Cone cGMP-specific 3',5'-cyclic phosphodiesterase alpha'-subunit IMR:0001028 GMP-PDE delta Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase delta-subunit IMR:0001029 GMP-PDE gamma Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase gamma-subunit IMR:0001030 group III secretory phospholipase A2 IMR:0001031 group V phospholipase A2 IMR:0001032 group VI phospholipase A2 IMR:0001033 group IIA phospholipase A2 IMR:0001034 group IID secretory phospholipase A2 IMR:0001035 group IIE secretory phospholipase A2 IMR:0001036 group IIF secretory phospholipase A2 IMR:0001037 group X secretory phospholipase A2 IMR:0001038 group XIIA secretory phospholipase A2 IMR:0001039 group XIIB secretory phospholipase A2-like protein IMR:0001040 group IVA phospholipase A2 IMR:0001041 group IVC phospholipase A2 IMR:0001042 group IIC secretory phospholipase A2 IMR:0001043 EC:3.1.2.- thiolester hydrolases IMR:0001044 EC:3.1.2.15 ubiquitin carboxy-terminal esterase ubiquitin carboxy-terminal hydrolase ubiquitin thiolesterase IMR:0001084 KPNA1 NPI-1 importin alpha S1 importin alpha5 karyopherin alpha1 importin alpha1 IMR:0001085 KPNA2 importin alpha P1 importin alpha1 karyopherin alpha2 importin alpha2 IMR:0001086 KPNA3 importin alpha Q2 importin alpha4 karyopherin alpha3 importin alpha3 IMR:0001087 KPNA4 Qip1 importin alpha Q1 importin alpha3 karyopherin alpha4 importin alpha4 IMR:0001088 KPNA5 karyopherin alpha5 importin alpha6 IMR:0001089 KPNA6 importin alpha S2 karyopherin alpha6 importin alpha7 IMR:0001090 exportin 1 CRM1 IMR:0001091 Members of importin beta family (importins/exportins, karyopherins) have been classified as importins or exportins on the basis of the direction they carry their cargo. Members of importin beta family (importins/exportins, karyopherins) have been classified as importins or exportins on the basis of the direction they carry their cargo. Kap inportin beta family inportin beta-like family inportin beta-like protein inportin beta-like receptor karyopherin karyopherin beta family importin/exportin Members of importin beta family (importins/exportins, karyopherins) have been classified as importins or exportins on the basis of the direction they carry their cargo. PMID:11423015 PMID:11729264 PMID:12600309 PMID:15450977 IMR:0001092 FLI1 IMR:0001093 ETV5 ERM IMR:0001094 Elk-1 IMR:0001095 Elk-4 Sap-1 IMR:0001096 importin beta2 karyopherin beta2 transportin 1 IMR:0001097 transportin SR IMR:0001098 exportin 4 IMR:0001099 RanBP16 exportin 7 IMR:0001100 exportin-t IMR:0001101 RanBP5 karyopherin beta3 importin 5 IMR:0001102 RanBP7 importin 7 IMR:0001103 importin 11 IMR:0001104 Elk-3 Sap-2 Net IMR:0001105 importin 13 IMR:0001106 PU.1 IMR:0001108 karyopherin beta2b transportin 2 IMR:0001109 RanBP17 IMR:0001110 RanBP6 IMR:0001111 RanBP8 importin 8 IMR:0001112 importin 4 IMR:0001113 importin 9 IMR:0001114 exportin 5 IMR:0001125 HSPG heparan sulfate proteoglycan IMR:0001126 chondroitin sulfate proteoglycan chondroitin sulfate proteoglycan IMR:0001127 chondroitin/dermatan sulfate proteoglycan chondroitin/dermatan sulfate proteoglycan IMR:0001128 keratan sulfate proteoglycan IMR:0001129 lumican IMR:0001130 neurocan IMR:0001131 basement membrane heparan sulfate proteoglycan perlecan IMR:0001132 PG-M versican IMR:0001133 aggrecan IMR:0001134 agrin IMR:0001136 brevican IMR:0001137 decorin IMR:0001138 keratocan IMR:0001139 GPI-anchored membrane heparan sulfate proteoglycan glypican (mol) IMR:0001140 glypican-1 IMR:0001141 HSPG-M13 cerebroglycan IMR:0001142 K-glypican IMR:0001143 biglycan IMR:0001144 NG2 IMR:0001145 PKC alpha IMR:0001146 PKC beta IMR:0001147 PKC gamma IMR:0001148 PKC delta IMR:0001149 PKC epsilon IMR:0001150 PKC-L PKC eta IMR:0001151 PKC zeta IMR:0001152 PKC lambda/iota IMR:0001200 Apo-2 ligand Apo2L TNF-related apoptosis inducing ligand TNFSF10 TRAIL IMR:0001201 DR4 TNF-related apoptosis-inducing ligand receptor 1 TRAIL receptor-1 TRAIL-R1 death receptor 4 TRAIL-R1 IMR:0001202 DR5 KILLER TRAIL receptor-2 TRAIL-R2 TRICK2 death receptor 5 TRAIL-R2 IMR:0001204 Apaf-1 IMR:0001206 Cytochromes of the c type that are found in eukaryotic MITOCHONDRIA. They serve as redox intermediates that accept electrons from MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX III and transfer them to MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX IV. MeSH:D003574 MeSH:D045304 Cyt c cytochrome c IMR:0001208 Bmf IMR:0001209 DLC8b dynein light chain 2 DLC2 IMR:0001210 Noxa IMR:0001211 bbc3 Puma IMR:0001213 DLC8a PIN dynein light chain 1 protein inhibitor of neuronal nitric oxide synthase DLC1 IMR:0001215 Axin Axin1 IMR:0001216 Axil Axin-like protein conductin Axin2 IMR:0001355 CHEBI:23447 cyclic nucleotide IMR:0001357 IMR:0200191 GDP IMR:0001363 Gli1 IMR:0001366 Gli2 IMR:0001368 Gli3 IMR:0001372 Ci/Gli IMR:0001385 phosphoinositol inositol phosphate IMR:0001404 CREB-binding protein CBP IMR:0001409 Gab proteins contain a pleckstrin homology (PH) domain and binding sites for SH2 and SH3 domains. Gab family include mammalian Gab1, Gab2, Gab3, Drosophila Dos, and C. elegans Soc1. Gab proteins contain a pleckstrin homology (PH) domain and binding sites for SH2 and SH3 domains. Gab family include mammalian Gab1, Gab2, Gab3, Drosophila Dos, and C. elegans Soc1. Grb2-associated binder Gab Gab proteins contain a pleckstrin homology (PH) domain and binding sites for SH2 and SH3 domains. Gab family include mammalian Gab1, Gab2, Gab3, Drosophila Dos, and C. elegans Soc1. PMID:14662016 IMR:0001410 Grb2-associated binder 1 Gab1 (mol) IMR:0001411 Grb2-associated binder 2 Gab2 IMR:0001412 Grb2-associated binder 3 Gab3 IMR:0001422 ISGF3 is a heterotrimer of STAT1, STAT2 and p48/ISGF3gamma/IRF9. ISGF3 is a heterotrimer of STAT1, STAT2 and p48/ISGF3gamma/IRF9. IFN-stimulated gene factor 3 interferon-stimulated gene factor 3 ISGF3 ISGF3 is a heterotrimer of STAT1, STAT2 and p48/ISGF3gamma/IRF9. PMID:11050435 PMID:12040185 IMR:0001423 STAT1 dimers form the IFNgamma-activated factor (GAF). STAT1 dimers form the IFNgamma-activated factor (GAF). IFNgamma-activated factor gamma-activated factor GAF STAT1 dimers form the IFNgamma-activated factor (GAF). PMID:11050435 PMID:12040185 IMR:0001424 BMP2 Bone morphogenetic protein 2 BMP-2 IMR:0001426 BMP3 Bone morphogenetic protein 3 BMP-3 IMR:0001427 BMP3b Bone morphogenetic protein 3b GDF-10 GDF10 BMP-3b IMR:0001428 BMP4 Bone morphogenetic protein 4 BMP-4 IMR:0001429 BMP5 Bone morphogenetic protein 5 BMP-5 IMR:0001430 BMP6 Bone morphogenetic protein 6 Vgr-1 BMP-6 IMR:0001431 BMP7 Bone morphogenetic protein 7 OP-1 BMP-7 IMR:0001432 BMP8a Bone morphogenetic protein 8a OP-2 BMP-8a IMR:0001433 BMP8b Bone morphogenetic protein 8b OP-3 BMP-8b IMR:0001434 BMP10 Bone morphogenetic protein 10 BMP-10 IMR:0001435 BMP15 Bone morphogenetic protein 15 GDF-9b GDF9b Growth/differentiation factor 9B BMP-15 IMR:0001436 BMP-11 BMP11 Bone morphogenetic protein 11 GDF11 Growth/differentiation factor 11 GDF-11 IMR:0001437 BMP-9 BMP9 Bone morphogenetic protein 9 Growth/differentiation factor-2 GDF-2 IMR:0001501 Rac1 IMR:0001502 Rac2 IMR:0001503 Rac3 IMR:0001504 Rap1 IMR:0001505 Rap1A IMR:0001506 Rap1B IMR:0001507 Rap2 IMR:0001508 Rap2A IMR:0001509 Rap2B IMR:0001510 Rap2C IMR:0001527 RalA IMR:0001528 RalB IMR:0001532 R-Ras1 IMR:0001533 R-Ras2 IMR:0001534 R-Ras3 M-Ras IMR:0001547 Rab1A IMR:0001549 Rab1B IMR:0001552 Rab2A IMR:0001553 Rab2B IMR:0001556 Rab3A IMR:0001558 Rab3B IMR:0001560 Rab3C IMR:0001563 Rab3D IMR:0001564 Rab4A IMR:0001565 Rab4B IMR:0001567 Rab5A IMR:0001568 Rab5B IMR:0001569 Rab5C IMR:0001572 Rab6A IMR:0001573 Rab6B IMR:0001574 Rab6C IMR:0001577 Rab7 IMR:0001578 Rab7L IMR:0001579 Rab8A IMR:0001580 Rab8B IMR:0001581 Rab9A IMR:0001582 Rab9B IMR:0001586 Rab10 IMR:0001588 Rab11A IMR:0001589 Rab11B IMR:0001592 Rab12 IMR:0001593 Rab13 (mol) IMR:0001595 Rab14 IMR:0001598 Rab15 IMR:0001601 Rab17 IMR:0001602 Rab18 IMR:0001603 Rab19 IMR:0001604 Rab20 IMR:0001605 Rab21 IMR:0001606 Rab22A IMR:0001607 Rab23 IMR:0001608 Rab24 IMR:0001610 Rab25 IMR:0001611 Rab26 IMR:0001612 Rab27A IMR:0001613 Rab27B IMR:0001614 Rab28 IMR:0001616 Rab30 IMR:0001617 Rab31 IMR:0001618 Rab32 IMR:0001623 Rab33A IMR:0001624 Rab33B (mol) IMR:0001625 Rab34 IMR:0001626 Rab35 IMR:0001627 Rab36 IMR:0001628 Rab37 IMR:0001629 Rab38 IMR:0001632 Rab39A IMR:0001633 Rab39B IMR:0001634 Rab40A IMR:0001635 Rab40B IMR:0001636 Rab40C IMR:0001645 RABL2A IMR:0001646 RABL2B IMR:0001647 Cav-1 caveolin-1 IMR:0001648 Cav-2 caveolin-2 IMR:0001649 Cav-3 caveolin-3 IMR:0001656 CHEBI:27305 vitamin IMR:0001659 RGS1 IMR:0001660 RGS2 IMR:0001661 RGS3 IMR:0001662 RGS4 IMR:0001663 RGS5 IMR:0001664 RGS6 IMR:0001665 RGS7 IMR:0001666 RGS8 IMR:0001667 RGS9 IMR:0001668 RGS10 IMR:0001669 RGS11 IMR:0001670 RGS12 IMR:0001671 RGS13 IMR:0001672 RGS14 IMR:0001673 RGS16 IMR:0001674 RGS17 IMR:0001675 RGS18 IMR:0001676 RGS19 IMR:0001677 RGS20 IMR:0001689 MAPKAPK2 and MAPKAPK3 can be activated by p38 and activated MAPKAPK2/3 can phosphorylate small heat shock protein 27 (HSP27). MAPKAPK2 and MAPKAPK3 can be activated by p38 and activated MAPKAPK2/3 can phosphorylate small heat shock protein 27 (HSP27). MAP kinase-activated protein kinase 2/3 MAPK-activated protein kinase 2/3 MAPKAPK2/3 MAPKAPK2 and MAPKAPK3 can be activated by p38 and activated MAPKAPK2/3 can phosphorylate small heat shock protein 27 (HSP27). PMID:9628874 IMR:0001690 MAP kinase signal-integrating kinase 1 MAP kinase-interacting kinase 1 MNK1 IMR:0001691 MAP kinase signal-integrating kinase 2 MAP kinase-interacting kinase 2 MNK2 IMR:0001692 HSP27 IMR:0001693 A group of compounds derived from ammonia by substituting organic radicals for the hydrogens. (From Grant & Hackh's Chemical Dictionary, 5th ed) A group of compounds derived from ammonia by substituting organic radicals for the hydrogens. (From Grant & Hackh's Chemical Dictionary, 5th ed) CHEBI:32952 MeSH:D000588 amine A group of compounds derived from ammonia by substituting organic radicals for the hydrogens. (From Grant & Hackh's Chemical Dictionary, 5th ed) MeSH:D000588 IMR:0001694 CHEBI:33567 catecholamine IMR:0001698 Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed) Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed) glycoside Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed) MeSH:D006027 IMR:0001699 Peptidoglycan (PGN) is a unique and essential component of the cell wall of virtually all bacteria, is not present in eukaryotes, and is an excellent target for the innate immune system. Peptidoglycan (PGN) is a unique and essential component of the cell wall of virtually all bacteria, is not present in eukaryotes, and is an excellent target for the innate immune system. MeSH:D010457 PGN murein peptidoglycan Peptidoglycan (PGN) is a unique and essential component of the cell wall of virtually all bacteria, is not present in eukaryotes, and is an excellent target for the innate immune system. PMID:16263004 IMR:0001789 component of fungal cell walls. component of fungal cell walls. MeSH:C033363 (1 --> 3)-beta-D-glucan (1,3)-beta-D-glucan (1-->3)-beta-D-glucan (1->3)-beta-D-glucan beta-1,3-D-glucan beta-1,3-glucan component of fungal cell walls. MeSH:C033363 IMR:0001844 ribosomal S6 protein kinase S6K IMR:0001845 70 kDa ribosomal S6 kinase p70S6K IMR:0001846 90 kDa ribosomal S6 kinase1 p90RSK1 RSK1 IMR:0001847 90 kDa ribosomal S6 kinase2 p90RSK2 RSK2 IMR:0001848 90 kDa ribosomal S6 kinase3 p90RSK3 RSK3 IMR:0001865 a disintegrin and metalloproteinase ADAM family IMR:0001871 a disintegrin and metalloproteinase 10 ADAM10 IMR:0001923 mastermind family MAM family IMR:0001924 MAML1 IMR:0001953 RhoA IMR:0001954 GO:0005089 Rho guanine nucleotide exchange factor RhoGEF IMR:0001976 GO:0017034 Rap guanine nucleotide exchange factor RapGEF IMR:0002044 NDK5 IMR:0002046 NDK6 IMR:0002049 NDK7 IMR:0002055 fibroblast growth factor receptor 1 FGFR1 IMR:0002056 fibroblast growth factor receptor 2 FGFR2 IMR:0002057 fibroblast growth factor receptor 3 FGFR3 IMR:0002058 fibroblast growth factor receptor 4 FGFR4 IMR:0002090 Antibody molecule (immunoglobulin) consists of four polypeptides chains, two identical light (L) chains and two identical heavy (H) chains. In mammals, there are five classes of antibodies, IgA, IgD, IgE, IgG, and IgM. Antibody molecule (immunoglobulin) consists of four polypeptides chains, two identical light (L) chains and two identical heavy (H) chains. In mammals, there are five classes of antibodies, IgA, IgD, IgE, IgG, and IgM. GO:0003823 Ig antibody immunoglobulin Antibody molecule (immunoglobulin) consists of four polypeptides chains, two identical light (L) chains and two identical heavy (H) chains. In mammals, there are five classes of antibodies, IgA, IgD, IgE, IgG, and IgM. ISBN:0815340729 IMR:0002091 immunoglobulin A IgA IMR:0002093 immunoglobulin E IgE IMR:0002094 immunoglobulin G IgG IMR:0002120 CHEBI:27584 11beta,21-Dihydroxy-3,20-dioxo-4-pregnen-18-al Aldosterone aldosterone IMR:0002121 A group of naturally occurring amines derived by enzymatic decarboxylation of the natural amino acids. Many have powerful physiological effects (e.g., histamine, serotonin, epinephrine, tyramine). Those derived from aromatic amino acids, and also their synthetic analogs (e.g., amphetamine), are of use in pharmacology. A group of naturally occurring amines derived by enzymatic decarboxylation of the natural amino acids. Many have powerful physiological effects (e.g., histamine, serotonin, epinephrine, tyramine). Those derived from aromatic amino acids, and also their synthetic analogs (e.g., amphetamine), are of use in pharmacology. CHEBI:22879 MeSH:D001679 biogenic amine A group of naturally occurring amines derived by enzymatic decarboxylation of the natural amino acids. Many have powerful physiological effects (e.g., histamine, serotonin, epinephrine, tyramine). Those derived from aromatic amino acids, and also their synthetic analogs (e.g., amphetamine), are of use in pharmacology. MeSH:D001679 IMR:0002345 beta-LPH beta lipotropin IMR:0002346 gamma-LPH gamma lipotropin IMR:0002394 T-cell receptor gamma TCR gamma IMR:0002395 T-cell receptor delta TCR delta IMR:0002411 Uev1A IMR:0002515 The MHC class Ib family members include HLA-E, HLA-F, HLA-G and HFE (HLA-H) in humans and gene products from the H2-M, H2-Q and H2-T regions in mice. The MHC class Ib family members include HLA-E, HLA-F, HLA-G and HFE (HLA-H) in humans and gene products from the H2-M, H2-Q and H2-T regions in mice. MHC class Ib molecule nonclassical MHC class I molecule The MHC class Ib family members include HLA-E, HLA-F, HLA-G and HFE (HLA-H) in humans and gene products from the H2-M, H2-Q and H2-T regions in mice. PMID:10607669 PMID:16860610 IMR:0002516 MHC class II-like proteins are produced from the class II region of the MHC, HLA-DM (DM) and HLA-DO (DO) (called H2-M, or H2-DM and H2-O in the mouse). MHC class II-like proteins are produced from the class II region of the MHC, HLA-DM (DM) and HLA-DO (DO) (called H2-M, or H2-DM and H2-O in the mouse). nonclassical MHC class II molecule MHC class II-like proteins are produced from the class II region of the MHC, HLA-DM (DM) and HLA-DO (DO) (called H2-M, or H2-DM and H2-O in the mouse). PMID:10837054 IMR:0002576 Ins(1,4,5)P3 3-kinases (IP3-3K) are the enzymes responsible for the ATP-dependent conversion of Ins(1,4,5)P3 to Ins(1,3,4,5)P4. Three mammalian isoforms of this enzyme have so far been isolated and designated the A, B and C isoforms. Ins(1,4,5)P3 3-kinases (IP3-3K) are the enzymes responsible for the ATP-dependent conversion of Ins(1,4,5)P3 to Ins(1,3,4,5)P4. Three mammalian isoforms of this enzyme have so far been isolated and designated the A, B and C isoforms. GO:0008440 IP(3) 3-kinase IP(3)K IP3 3-kinase IP3-3K IP3K Ins(1,4,5)P3 3-kinase inositol 1,4,5-trisphosphate 3-kinase Ins(1,4,5)P3 3-kinases (IP3-3K) are the enzymes responsible for the ATP-dependent conversion of Ins(1,4,5)P3 to Ins(1,3,4,5)P4. Three mammalian isoforms of this enzyme have so far been isolated and designated the A, B and C isoforms. PMID:15093605 PMID:15740635 IMR:0002577 IP3K-A inositol 1,4,5-trisphosphate 3-kinase A IMR:0002578 IP3K-B inositol 1,4,5-trisphosphate 3-kinase B IMR:0002579 IP3K-C inositol 1,4,5-trisphosphate 3-kinase C IMR:0002658 CARMEN CIPER CLAP c-E10 mE10 BCL10 IMR:0002688 IGFBPs are a family of secreted proteins that bind IGF with high affinities that are equal to or greater than those of the IGF-IR. Six distinct IGFBPs, designated as IGFBP-1 to -6, have been isolated and characterized from human and a variety of vertebrate species. IGFBPs are a family of secreted proteins that bind IGF with high affinities that are equal to or greater than those of the IGF-IR. Six distinct IGFBPs, designated as IGFBP-1 to -6, have been isolated and characterized from human and a variety of vertebrate species. IGF-binding protein insulin-like growth factor-binding protein IGFBP IGFBPs are a family of secreted proteins that bind IGF with high affinities that are equal to or greater than those of the IGF-IR. Six distinct IGFBPs, designated as IGFBP-1 to -6, have been isolated and characterized from human and a variety of vertebrate species. PMID:12466191 PMID:15862547 PMID:15935690 IMR:0002690 IGFBP-2 IMR:0002691 IGFBP-3 IMR:0002692 IGFBP-4 IMR:0002693 IGFBP-5 IMR:0002694 IGFBP-6 IMR:0002717 GO:0042020 interleukin-23 receptor IL-23 receptor IMR:0002721 TOR IMR:0002777 AMPK beta subunit IMR:0002778 AMPK gamma subunit IMR:0002798 S6K1 IMR:0002799 S6K2 IMR:0002804 FOXO proteins are conserved from worm to human. To date, only one FOXO species has been identified in invertebrates (called dauer formation-16 in Caenorhabditis elegans and dFOXO in Drosophila). In mammals, four subfamily members have been identified: FOXO1 (previously known as FKHR), FOXO3 (previously known as FKHRL1), FOXO4 (previously known as AFX) and FOXO6. FOXO proteins are conserved from worm to human. To date, only one FOXO species has been identified in invertebrates (called dauer formation-16 in Caenorhabditis elegans and dFOXO in Drosophila). In mammals, four subfamily members have been identified: FOXO1 (previously known as FKHR), FOXO3 (previously known as FKHRL1), FOXO4 (previously known as AFX) and FOXO6. FOXO family FOXO proteins are conserved from worm to human. To date, only one FOXO species has been identified in invertebrates (called dauer formation-16 in Caenorhabditis elegans and dFOXO in Drosophila). In mammals, four subfamily members have been identified: FOXO1 (previously known as FKHR), FOXO3 (previously known as FKHRL1), FOXO4 (previously known as AFX) and FOXO6. PMID:18391973 IMR:0002807 FOXO4 IMR:0002808 FOXO6 IMR:0002950 B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. B7.1/B7.2 CD80/CD86 B7.1 (CD80) and B7.2 (CD86) - the two structurally homologous ligands of CD28 - are expressed by professional antigen-presenting cells (APCs), such as dendritic cells (DCs), macrophages and activated B cells, belong to the immunoglobulin superfamily and might exist as dimers and monomers, respectively. PMID:14647476 IMR:0002951 Arrow/Lrp5/Lrp6 is a subfamily of the LDL receptor (LDLR) family. Arrow, and also its counterparts LRP5 and LRP6 in mammals and in frogs, appears to function as a coreceptor for Wnt together with the seven-transmembrane receptor Frizzled (frz) in forming the Wnt receptor signaling complex. Arrow/Lrp5/Lrp6 is a subfamily of the LDL receptor (LDLR) family. Arrow, and also its counterparts LRP5 and LRP6 in mammals and in frogs, appears to function as a coreceptor for Wnt together with the seven-transmembrane receptor Frizzled (frz) in forming the Wnt receptor signaling complex. Arrow/LRP5/LRP6 Arrow/Lrp5/Lrp6 is a subfamily of the LDL receptor (LDLR) family. Arrow, and also its counterparts LRP5 and LRP6 in mammals and in frogs, appears to function as a coreceptor for Wnt together with the seven-transmembrane receptor Frizzled (frz) in forming the Wnt receptor signaling complex. PMID:12045102 PMID:15084453 IMR:0002954 Lrp5 and Lrp6 are highly homologous, and are widely co-expressed during embryogenesis and in adult tissues. An orthologue in Drosophila melanogaster is known as arrow, a gene that functions in the canonical Wnt signaling pathway. Lrp5 and Lrp6 are highly homologous, and are widely co-expressed during embryogenesis and in adult tissues. An orthologue in Drosophila melanogaster is known as arrow, a gene that functions in the canonical Wnt signaling pathway. LRP5/LRP6 Lrp5 and Lrp6 are highly homologous, and are widely co-expressed during embryogenesis and in adult tissues. An orthologue in Drosophila melanogaster is known as arrow, a gene that functions in the canonical Wnt signaling pathway. PMID:12045102 PMID:15084453 IMR:0002955 GRK2 IMR:0002956 beta-arrestin 1 IMR:0002957 beta-arrestin 2 IMR:0002958 Dlp/Dally IMR:0002980 ETV6 TEL TEL1 IMR:0003014 Kif3A IMR:0003045 The BMP-1/TLD metalloproteinases, conserved in species ranging from Drosophila to humans, act in dorsal-ventral patterning via activation of BMP2, BMP4 (vertebrates) and Dpp (arthropods). There are four mammalian BMP-1/TLD-like proteinases, including BMP-1/mTLD, which is encoded by alternatively spliced mRNA produced by the Bmp1 gene, and TLL1 and TLL2, which are genetically distinct. The BMP-1/TLD metalloproteinases, conserved in species ranging from Drosophila to humans, act in dorsal-ventral patterning via activation of BMP2, BMP4 (vertebrates) and Dpp (arthropods). There are four mammalian BMP-1/TLD-like proteinases, including BMP-1/mTLD, which is encoded by alternatively spliced mRNA produced by the Bmp1 gene, and TLL1 and TLL2, which are genetically distinct. bone morphogenetic protein-1/tolloid family BMP-1/TLD family The BMP-1/TLD metalloproteinases, conserved in species ranging from Drosophila to humans, act in dorsal-ventral patterning via activation of BMP2, BMP4 (vertebrates) and Dpp (arthropods). There are four mammalian BMP-1/TLD-like proteinases, including BMP-1/mTLD, which is encoded by alternatively spliced mRNA produced by the Bmp1 gene, and TLL1 and TLL2, which are genetically distinct. PMID:17560775 PMID:19429706 IMR:0003062 CDMP-1 Growth/differentiation factor-5 cartilage-derived morphogenetic protein-1 GDF-5 IMR:0003065 BMP-13 Bone morphogenetic protein-13 CDMP-2 Growth/differentiation factor 6 cartilage-derived morphogenetic protein-2 GDF-6 IMR:0003069 BMP-12 Bone morphogenetic protein-12 Growth/differentiation factor 7 GDF-7 IMR:0003073 Growth/differentiation factor-8 myostatin GDF-8 IMR:0003077 Growth/differentiation factor-9 GDF-9 IMR:0003080 Growth/differentiation factor-3 Vgr-2 GDF-3 IMR:0003083 BMP-related proteins can be subdivided into several groups based on their structures and functions. BMP-2, BMP-4, and the Drosophila Dpp form one subgroup. BMP-related proteins can be subdivided into several groups based on their structures and functions. BMP-2, BMP-4, and the Drosophila Dpp form one subgroup. BMP-2/4 group BMP-2 subfamily BMP-related proteins can be subdivided into several groups based on their structures and functions. BMP-2, BMP-4, and the Drosophila Dpp form one subgroup. PMID:15871923 PMID:9720756 PMID:9759503 IMR:0003084 BMP-related proteins can be subdivided into several groups based on their structures and functions. BMP-5, BMP-6, BMP-7 (OP-1), BMP-8 (OP-2), and the Drosophila Gbb form one subgroup. BMP-related proteins can be subdivided into several groups based on their structures and functions. BMP-5, BMP-6, BMP-7 (OP-1), BMP-8 (OP-2), and the Drosophila Gbb form one subgroup. OP-1 group BMP-5 subfamily BMP-related proteins can be subdivided into several groups based on their structures and functions. BMP-5, BMP-6, BMP-7 (OP-1), BMP-8 (OP-2), and the Drosophila Gbb form one subgroup. PMID:15871923 PMID:9720756 PMID:9759503 IMR:0003085 BMP-related proteins can be subdivided into several groups based on their structures and functions. GDF-5 (CDMP- 1), GDF-6 (CDMP-2 or BMP-13), and GDF-7 (BMP-12) form one sugroup. BMP-related proteins can be subdivided into several groups based on their structures and functions. GDF-5 (CDMP- 1), GDF-6 (CDMP-2 or BMP-13), and GDF-7 (BMP-12) form one sugroup. GDF-5 subfamily BMP-related proteins can be subdivided into several groups based on their structures and functions. GDF-5 (CDMP- 1), GDF-6 (CDMP-2 or BMP-13), and GDF-7 (BMP-12) form one sugroup. PMID:15871923 PMID:9720756 PMID:9759503 IMR:0010012 Nucleoside diphoshate kinases (NDKs), an evolutionarily conserved family of proteins, synthesize nucleoside triphosphates from nucleoside diphosphates and ATP. To date, eight human NDK homologues have been identified. Nucleoside diphoshate kinases (NDKs), an evolutionarily conserved family of proteins, synthesize nucleoside triphosphates from nucleoside diphosphates and ATP. To date, eight human NDK homologues have been identified. EC:2.7.4.6 GO:0004550 NDK NDP kinase NME Nm23 nucleoside diphosphate kinase Nucleoside diphoshate kinases (NDKs), an evolutionarily conserved family of proteins, synthesize nucleoside triphosphates from nucleoside diphosphates and ATP. To date, eight human NDK homologues have been identified. PMID:11768308 PMID:16313181 IMR:0010013 negative elongation factor NELF IMR:0010016 Translation initiation in eukaryotes is an intricate process requiring at least 11 eukaryotic initiation factors (eIFs). Translation initiation in eukaryotes is an intricate process requiring at least 11 eukaryotic initiation factors (eIFs). eukaryotic initiation factor eIF Translation initiation in eukaryotes is an intricate process requiring at least 11 eukaryotic initiation factors (eIFs). PMID:11426420 PMID:12581660 PMID:14635255 IMR:0010020 SIII Elongin IMR:0010024 Heterogeneous nuclear ribonucleoprotein IMR:0010252 A role played by the entity which catalyses the reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = long-chain fatty acid + n+1 CoA + n CO2 + 2n NADP+. EC:2.3.1.85 related molecular function GO:0004312 fatty acid synthase IMR:0010278 EC:1.11.1.9 Cellular glutathione peroxidase GSHC GSHPx-1 Glutathione peroxidase 1 glutathione peroxidase monomer Glutathione peroxidase IMR:0010280 GTR1 Glucose transporter type 1, erythrocyte/brain HepG2 glucose transporter Solute carrier family 2, facilitated glucose transporter, member 1 GLUT1 IMR:0010281 GTR2 Glucose transporter type 2, liver Solute carrier family 2, facilitated glucose transporter, member 2 GLUT2 IMR:0010387 Solute carrier family 25, member 15 Mitochondrial ornithine transporter 1 IMR:0010429 57 kDa RNA-binding protein PPTB-1 Heterogeneous nuclear ribonucleoprotein I PTB hnRNP I Polypyrimidine tract-binding protein 1 IMR:0010453 Negative elongation factor E RD protein NELF-E IMR:0010505 ROA0 hnRNP A0 Heterogeneous nuclear ribonucleoprotein A0 IMR:0010506 Helix-destabilizing protein ROA1 Single-strand binding protein hnRNP A1 hnRNP core protein A1 Heterogeneous nuclear ribonucleoprotein A1 IMR:0010507 ROA2 hnRNP A2 hnRNP A2 / hnRNP B1 Heterogeneous nuclear ribonucleoproteins A2/B1 IMR:0010508 D10S102 ROA3 hnRNP A3 Heterogeneous nuclear ribonucleoprotein A3 IMR:0010509 ROC hnRNP C1 / hnRNP C2 hnRNP C1/C2 Heterogeneous nuclear ribonucleoproteins C1/C2 IMR:0010510 AU-rich element RNA-binding protein 1 ROD hnRNP D0 Heterogeneous nuclear ribonucleoprotein D0 IMR:0010511 ROF hnRNP F Heterogeneous nuclear ribonucleoprotein F IMR:0010512 Glycoprotein p43 RNA binding motif protein, X chromosome ROG hnRNP G Heterogeneous nuclear ribonucleoprotein G IMR:0010513 ROH1 hnRNP H Heterogeneous nuclear ribonucleoprotein H IMR:0010514 FTP-3 ROH2 hnRNP H' Heterogeneous nuclear ribonucleoprotein H' IMR:0010515 CSBP DC-stretch binding protein ROK TUNP Transformation upregulated nuclear protein hnRNP K Heterogeneous nuclear ribonucleoprotein K IMR:0010516 ROL hnRNP L Heterogeneous nuclear ribonucleoprotein L IMR:0010517 ROM hnRNP M Heterogeneous nuclear ribonucleoprotein M IMR:0010518 ROR hnRNP R Heterogeneous nuclear ribonucleoprotein R IMR:0010519 ROU SAF-A Scaffold attachment factor A hnRNP U Heterogenous nuclear ribonucleoprotein U IMR:0010628 Transcription elongation factor A protein 1 Transcription elongation factor A protein 1 (Transcription elongation factor S-II protein 1) (Transcription elongation factor TFIIS.o) Transcription elongation factor S-II protein 1 Transcription elongation factor TFIIS.o TFIIS protein IMR:0010630 General transcription factor TFIIB RNA polymerase II alpha initiation factor S300-II Transcription factor E Transcription initiation factor IIB TFIIB IMR:0011133 IMR:0011979 EIF- 2alpha EIF-2A Eukaryotic translation initiation factor 2 alpha subunit Eukaryotic translation initiation factor 2 subunit 1 eIF-2-alpha translation initiation factor 2 alpha subunit translation initiation factor 2, subunit 1 eIF2-alpha IMR:0011134 Eukaryotic translation initiation factor 2 subunit 2 eIF-2-beta eukaryotic translation initiation factor 2 beta subunit eukaryotic translation initiation factor 2, subunit 2 eIF2-beta IMR:0011135 Eukaryotic translation initiation factor 2 subunit 3 eIF-2-gamma eukaryotic translation initiation factor 2 gamma subunit eukaryotic translation initiation factor 2, subunit 3 eIF2-gamma IMR:0011136 Translation initiation factor eIF-2B alpha subunit eIF-2B GDP-GTP exchange factor eIF-2B GDP-GTP exchange factor, alpha subunit translation initiation factor 2B alpha subunit eIF2B-alpha IMR:0011137 S20I15 S20III15 Translation initiation factor eIF-2B beta subunit eIF-2B GDP-GTP exchange factor eIF-2B GDP-GTP exchange factor, beta subunit translation initiation factor 2B beta subunit eIF2B-beta IMR:0011138 Translation initiation factor eIF-2B delta subunit eIF-2B GDP-GTP exchange factor eIF-2B GDP-GTP exchange factor, delta subunit translation initiation factor 2B delta subunit eIF2B-delta IMR:0011139 Translation initiation factor eIF-2B epsilon subunit eIF-2B GDP-GTP exchange factor eIF-2B GDP-GTP exchange factor, epsilon subunit translation initiation factor 2B epsilon subunit eIF2B-epsilon IMR:0011140 Translation initiation factor eIF-2B gamma subunit eIF-2B GDP-GTP exchange factor eIF-2B GDP-GTP exchange factor, gamma subunit translation initiation factor 2B gamma subunit eIF2B-gamma IMR:0011141 This subunit is not part of the Saccharomyces cerevisiae core eIF3 complex. This subunit is not part of the Saccharomyces cerevisiae core eIF3 complex. Possible eukaryotic translation initiation factor 3 30 kDa subunit eIF-3 30 kDa eIF-3 alpha eIF3 p35 eukaryotic translation initiation factor 3 subunit 1 eIF3j This subunit is not part of the Saccharomyces cerevisiae core eIF3 complex. PMID:11426420 IMR:0011142 Eukaryotic translation initiation factor 3 39 kDa subunit Suppressor of uncontrolled mitosis 1 TGF-beta receptor interacting protein 1 TRIP-1 Translation initiation factor eIF3, p39 subunit eIF-3 beta eIF3 p36 eIF3 p39 eukaryotic translation initiation factor 3 subunit 2 eIF3i IMR:0011143 Eukaryotic translation initiation factor 3 RNA-binding subunit Translation initiation factor eIF3, p33 subunit eIF-3 RNA-binding subunit eIF-3 delta eIF3 p33 eIF3 p42 eIF3 p44 eukaryotic translation initiation factor 3 subunit 4 eIF3g IMR:0011144 eIF-3 epsilon eIF3 p47 eIF3 p47 subunit eukaryotic translation initiation factor 3 subunit 5 eIF3f IMR:0011145 Cell cycle regulation and translation initiation protein Eukaryotic translation initiation factor 3 90 kDa subunit eIF-3 eta eIF3 p110 eIF3 p116 eIF3 p90 eukaryotic translation initiation factor 3 subunit 9 eIF3b IMR:0011146 eIF-3 gamma eIF3 p40 eIF3 p40 subunit eukaryotic translation initiation factor 3 subunit 3 eIF3h IMR:0011147 Translation initiation factor eIF3, p110 subunit eIF-3 theta eIF3 p110 eIF3 p167 eIF3 p180 eIF3 p185 eukaryotic translation initiation factor 3 subunit 10 eIF3a IMR:0011148 eIF-3 zeta eIF3 p66 eukaryotic translation initiation factor 3 subunit 7 eIF3d IMR:0011149 Eukaryotic translation initiation factor 3 93 kDa subunit Eukaryotic translation initiation factor 3 subunit 8 Nuclear transport protein NIP1 eIF3 p110 eIF3 p93 eIF3c IMR:0011150 Eukaryotic translation initiation factor 3 subunit 6 Mammary tumor-associated protein INT-6 Viral integration site protein INT-6 eIF-3 p48 eIF3e IMR:0011151 ARG134 Eukaryotic translation initiation factor 3 subunit 11 HSPC029 Muscle specific gene M9 protein PTD001 eIF-3 p25 eukaryotic translation initiation factor 3 subunit 11 eIF3k IMR:0011152 Eukaryotic translation initiation factor 1A, X-chromosomal Eukaryotic translation initiation factor 1A, Y-chromosomal eIF-1A eIF-1A X isoform eIF-1A Y isoform eIF-4C eukaryotic translation initiation factor 1A eIF1A IMR:0011153 eIF-4A-I eIF4AI eukaryotic initiation factor 4A-I eIF4A-I IMR:0011154 IMR:0011606 eIF-4A-II eIF4AII eukaryotic initiation factor 4A-II eIF4A-II IMR:0011155 IMR:0011556 IF4E eIF-4E eIF-4F 25 kDa subunit eukaryotic translation initiation factor 4E mRNA cap-binding protein eIF4E IMR:0011157 P220 eIF-4-gamma 1 eIF-4G eIF-4G1 eukaryotic translation initiation factor 4 gamma 1 eIF4GI IMR:0011158 eIF-4B eukaryotic translation initiation factor 4B eIF4B IMR:0011159 Williams-Beuren syndrome chromosome region 1 protein eIF-4H eukaryotic translation initiation factor 4H eIF4H IMR:0011160 Eukaryotic translation initiation factor 5 eIF-5 eIF5 IMR:0011347 EloA Elongin 110 kDa subunit Elongin A MSTP059 RNA polymerase II transcription factor SIII subunit A1 SIII p110 Transcription elongation factor B polypeptide 3 Elongin A1 protein IMR:0011348 EloC Elongin 15 kDa subunit Elongin C RNA polymerase II transcription factor SIII subunit C SIII p15 Transcription elongation factor B polypeptide 1 Elongin B protein IMR:0011349 EloB Elongin 18 kDa subunit Elongin B RNA polymerase II transcription factor SIII subunit B SIII p18 Transcription elongation factor B polypeptide 2 Elongin C protein IMR:0011350 NELF-A Negative elongation factor A P/OKCL.15 Wolf-Hirshhorn syndrome candidate 2 protein mWHSC2 NELF-A protein IMR:0011351 Cofactor of BRCA1 NELF-B Negative elongation factor B NELF-B protein IMR:0011352 HSPC130 NELF-C/D Negative elongation factor C/D TH1-like protein NELF-C/D protein IMR:0011414 NDKA IMR:0011415 NDKB IMR:0011416 NDK3 IMR:0011423 NDKM IMR:0100002 EC:3.1.4.35 GO:0004116 cGMP-specific PDE cGMP-specific phosphodiesterase cyclic GMP phosphodiesterase cGMP phosphodiesterase IMR:0100010 importin IMR:0100015 exportin IMR:0100019 Naturally occurring compounds derived from the parent C20 acid, prostanoic acid. CAS:11000-26-3 prostaglandin IMR:0100021 Any icosanoid from that family of C20 polyunsaturated fatty acids and their derivatives generated by leukocytes from arachidonic acid, each member having four double bonds of which three are conjugated. leukotriene IMR:0100024 3',5'-Cyclic AMP Adenosine 3',5'-phosphate Cyclic AMP Cyclic adenylic acid cAMP IMR:0100025 IMR:0200372 3',5'-Cyclic GMP Cyclic GMP Guanosine 3',5'-cyclic monophosphate Guanosine 3',5'-cyclic phosphate cGMP IMR:0100027 DAG DG Diglyceride diacylglyceride diacylglycerol IMR:0100028 IMR:0200332 1,4,5-InsP3 1D-myo-Inositol 1,4,5-trisphosphate D-myo-Inositol 1,4,5-trisphosphate Inositol 1,4,5-Trisphosphate IP3 IMR:0100029 IMR:0200210 1D-myo-Inositol 1,3,4,5-tetrakisphosphate D-myo-Inositol 1,3,4,5-tetrakisphosphate Inositol 1,3,4,5-tetrakisphosphate Ins(1,3,4,5)P4 IP4 IMR:0100033 CHEBI:26764 steroid hormone IMR:0100034 4-Pregnene-3,20-dione progesterone IMR:0100036 stress hormone glucocorticoid IMR:0100037 CHEBI:25354 mineralocorticoid IMR:0100040 vitamin D IMR:0100041 Retin A Tretinoin all-trans-Retinoic Acid all-trans-Vitamin A acid vitamin A acid retinoic acid IMR:0100042 MeSH:D013963 thyroid hormone (substance) IMR:0100043 MeSH:D013974 3,5,3'5'-Tetraiiodo-L-thyronine L-Thyroxine Levothyroxin O-(4-Hydroxy-3,5-diidophenyl)-3,5-diiodo-L-tyrosine T4 Thyroid Hormone thyroxine IMR:0100044 MeSH:D014284 3,3'5-Triiodo-L-thyronine 3,5,3'-Triiodo-L-thyronine 3,5,3'-Triiodothyronine L-3,5,3'-Triiodothyronine Liothyronine T3 Thyroid Hormone Triiodothyronine triiodothyronine IMR:0100045 A peptide hormone that lowers calcium concentration in the blood. In humans, it is released by thyroid cells and acts to decrease the formation and absorptive activity of osteoclasts. Its role in regulating plasma calcium is much greater in children and in certain diseases than in normal adults. A peptide hormone that lowers calcium concentration in the blood. In humans, it is released by thyroid cells and acts to decrease the formation and absorptive activity of osteoclasts. Its role in regulating plasma calcium is much greater in children and in certain diseases than in normal adults. MeSH:D002116 calcitonin A peptide hormone that lowers calcium concentration in the blood. In humans, it is released by thyroid cells and acts to decrease the formation and absorptive activity of osteoclasts. Its role in regulating plasma calcium is much greater in children and in certain diseases than in normal adults. MeSH:D002116 IMR:0100048 A peptide, of about 33 amino acids, secreted by the upper INTESTINAL MUCOSA and also found in the central nervous system. It causes gallbladder contraction, release of pancreatic exocrine (or digestive) enzymes, and affects other gastrointestinal functions. Cholecystokinin may be the mediator of satiety. A peptide, of about 33 amino acids, secreted by the upper INTESTINAL MUCOSA and also found in the central nervous system. It causes gallbladder contraction, release of pancreatic exocrine (or digestive) enzymes, and affects other gastrointestinal functions. Cholecystokinin may be the mediator of satiety. MeSH:D002766 CCK cholecystokinin A peptide, of about 33 amino acids, secreted by the upper INTESTINAL MUCOSA and also found in the central nervous system. It causes gallbladder contraction, release of pancreatic exocrine (or digestive) enzymes, and affects other gastrointestinal functions. Cholecystokinin may be the mediator of satiety. MeSH:D002766 IMR:0100050 A gastrointestinal peptide hormone of about 43-amino acids. A gastrointestinal peptide hormone of about 43-amino acids. MeSH:D005749 GIP gastric inhibitory polypeptide A gastrointestinal peptide hormone of about 43-amino acids. MeSH:D005749 IMR:0100051 A peptide of about 22-amino acids isolated from the DUODENUM. At low pH it inhibits gastric motor activity, whereas at high pH it has a stimulating effect. A peptide of about 22-amino acids isolated from the DUODENUM. At low pH it inhibits gastric motor activity, whereas at high pH it has a stimulating effect. MeSH:D009037 motilin A peptide of about 22-amino acids isolated from the DUODENUM. At low pH it inhibits gastric motor activity, whereas at high pH it has a stimulating effect. MeSH:D009037 IMR:0100055 A polypeptide hormone that originates in the hypothalamus and stimulates the secretion of prolactin in the pituitary gland. A polypeptide hormone that originates in the hypothalamus and stimulates the secretion of prolactin in the pituitary gland. MeSH:D011390 PRF PRH PrRP prolactin-releasing factor rolactin-releasing peptide prolactin-releasing hormone A polypeptide hormone that originates in the hypothalamus and stimulates the secretion of prolactin in the pituitary gland. MeSH:D011390 IMR:0100056 A tripeptide hormone that originates in the HYPOTHALAMUS and stimulates the secretion of THYROTROPIN from the PITUITARY GLAND. In humans, it also acts as a prolactin-releasing factor. It is also a neurotransmitter in the central nervous system. A tripeptide hormone that originates in the HYPOTHALAMUS and stimulates the secretion of THYROTROPIN from the PITUITARY GLAND. In humans, it also acts as a prolactin-releasing factor. It is also a neurotransmitter in the central nervous system. MeSH:D013973 5-oxo-prolyl-histidyl-prolinamide TRH protirelin thyroliberin thyrotropin-releasing hormone A tripeptide hormone that originates in the HYPOTHALAMUS and stimulates the secretion of THYROTROPIN from the PITUITARY GLAND. In humans, it also acts as a prolactin-releasing factor. It is also a neurotransmitter in the central nervous system. MeSH:D013973 IMR:0100057 Hypothalamic peptide that regulates the synthesis and secretion of GROWTH HORMONE in the anterior pituitary gland. Hypothalamic peptide that regulates the synthesis and secretion of GROWTH HORMONE in the anterior pituitary gland. MeSH:D013007 GHRH SRH Somatoliberin somatotropin-releasing hormone growth hormone-releasing hormone Hypothalamic peptide that regulates the synthesis and secretion of GROWTH HORMONE in the anterior pituitary gland. MeSH:D013007 IMR:0100058 MSHRH MSH-releasing hormone IMR:0100064 A peptide hormone of about 22 amino acids. It is derived from PRO-OPIOMELANOCORTIN and has natriuretic activity. A peptide hormone of about 22 amino acids. It is derived from PRO-OPIOMELANOCORTIN and has natriuretic activity. MeSH:D019824 beta-Melanotropin beta-MSH A peptide hormone of about 22 amino acids. It is derived from PRO-OPIOMELANOCORTIN and has natriuretic activity. MeSH:D019824 IMR:0100069 IMR:0200455 MeSH:D008550 Melatonin N-Acetyl-5-methoxytryptamine melatonin IMR:0100070 Neuropeptide and gut hormone that helps regulate GASTRIC ACID secretion and motor function. Once released from nerves in the antrum of the STOMACH, the neuropeptide stimulates release of GASTRIN from the GASTRIN-SECRETING CELLS. Neuropeptide and gut hormone that helps regulate GASTRIC ACID secretion and motor function. Once released from nerves in the antrum of the STOMACH, the neuropeptide stimulates release of GASTRIN from the GASTRIN-SECRETING CELLS. MeSH:D019886 GRP gastrin-releasing peptide Neuropeptide and gut hormone that helps regulate GASTRIC ACID secretion and motor function. Once released from nerves in the antrum of the STOMACH, the neuropeptide stimulates release of GASTRIN from the GASTRIN-SECRETING CELLS. MeSH:D019886 IMR:0100071 A highly basic, 28 amino acid neuropeptide released from intestinal mucosa. It has a wide range of biological actions affecting the cardiovascular, gastrointestinal, and respiratory systems and is neuroprotective. It binds special receptors ( RECEPTORS, VASOACTIVE INTESTINAL PEPTIDE). A highly basic, 28 amino acid neuropeptide released from intestinal mucosa. It has a wide range of biological actions affecting the cardiovascular, gastrointestinal, and respiratory systems and is neuroprotective. It binds special receptors ( RECEPTORS, VASOACTIVE INTESTINAL PEPTIDE). MeSH:D014660 VIP vasoactive intestinal peptide A highly basic, 28 amino acid neuropeptide released from intestinal mucosa. It has a wide range of biological actions affecting the cardiovascular, gastrointestinal, and respiratory systems and is neuroprotective. It binds special receptors ( RECEPTORS, VASOACTIVE INTESTINAL PEPTIDE). MeSH:D014660 IMR:0100072 HORMONES secreted by the gastrointestinal mucosa that affect the timing or the quality of secretion of digestive enzymes, and regulate the motor activity of the digestive system organs. HORMONES secreted by the gastrointestinal mucosa that affect the timing or the quality of secretion of digestive enzymes, and regulate the motor activity of the digestive system organs. MeSH:D005768 Enteric Hormone Intestinal Hormone gastrointestinal hormones HORMONES secreted by the gastrointestinal mucosa that affect the timing or the quality of secretion of digestive enzymes, and regulate the motor activity of the digestive system organs. MeSH:D005768 IMR:0100074 A 36-amino acid peptide produced by the L cells of the distal small intestine and colon. Peptide YY inhibits gastric and pancreatic secretion. A 36-amino acid peptide produced by the L cells of the distal small intestine and colon. Peptide YY inhibits gastric and pancreatic secretion. MeSH:D019894 peptide YY A 36-amino acid peptide produced by the L cells of the distal small intestine and colon. Peptide YY inhibits gastric and pancreatic secretion. MeSH:D019894 IMR:0100075 A peptide hormone of about 27 amino acids from the duodenal mucosa that activates pancreatic secretion and lowers the blood sugar level. A peptide hormone of about 27 amino acids from the duodenal mucosa that activates pancreatic secretion and lowers the blood sugar level. MeSH:D012633 secretin A peptide hormone of about 27 amino acids from the duodenal mucosa that activates pancreatic secretion and lowers the blood sugar level. MeSH:D012633 IMR:0100076 Peptide hormones secreted into the blood by cells in the ISLETS OF LANGERHANS of the pancreas. The alpha cells secrete glucagon; the beta cells secrete insulin; the delta cells secrete somatostatin; and the PP cells secrete pancreatic polypeptide. Peptide hormones secreted into the blood by cells in the ISLETS OF LANGERHANS of the pancreas. The alpha cells secrete glucagon; the beta cells secrete insulin; the delta cells secrete somatostatin; and the PP cells secrete pancreatic polypeptide. MeSH:D010187 pancreatic hormone Peptide hormones secreted into the blood by cells in the ISLETS OF LANGERHANS of the pancreas. The alpha cells secrete glucagon; the beta cells secrete insulin; the delta cells secrete somatostatin; and the PP cells secrete pancreatic polypeptide. MeSH:D010187 IMR:0100077 A pancreatic peptide hormone of about 29 amino acids secreted by PANCREATIC ALPHA CELLS. It has an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. A pancreatic peptide hormone of about 29 amino acids secreted by PANCREATIC ALPHA CELLS. It has an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. MeSH:D005934 glucagon A pancreatic peptide hormone of about 29 amino acids secreted by PANCREATIC ALPHA CELLS. It has an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. MeSH:D005934 IMR:0100082 Hormones isolated from the hypothalamus which exercise control over other organs, primarily the pituitary gland. Well-known members include certain pituitary hormone-releasing hormones and pituitary hormone release inhibiting hormones. Vasopressin and oxytocin which are found in the posterior pituitary may also be secreted by the hypothalamus but are not grouped here ( PITUITARY HORMONES, POSTERIOR). Hormones isolated from the hypothalamus which exercise control over other organs, primarily the pituitary gland. Well-known members include certain pituitary hormone-releasing hormones and pituitary hormone release inhibiting hormones. Vasopressin and oxytocin which are found in the posterior pituitary may also be secreted by the hypothalamus but are not grouped here ( PITUITARY HORMONES, POSTERIOR). MeSH:D007028 hypothalamic hormone Hormones isolated from the hypothalamus which exercise control over other organs, primarily the pituitary gland. Well-known members include certain pituitary hormone-releasing hormones and pituitary hormone release inhibiting hormones. Vasopressin and oxytocin which are found in the posterior pituitary may also be secreted by the hypothalamus but are not grouped here ( PITUITARY HORMONES, POSTERIOR). MeSH:D007028 IMR:0100083 Parathormone parathyroid hormone IMR:0100084 Hormones secreted by the PITUITARY GLAND including those from the anterior lobe (adenohypophysis), the posterior lobe (neurohypophysis), and the ill-defined intermediate lobe. Hormones secreted by the PITUITARY GLAND including those from the anterior lobe (adenohypophysis), the posterior lobe (neurohypophysis), and the ill-defined intermediate lobe. MeSH:D010907 pituitary hormone Hormones secreted by the PITUITARY GLAND including those from the anterior lobe (adenohypophysis), the posterior lobe (neurohypophysis), and the ill-defined intermediate lobe. MeSH:D010907 IMR:0100086 Hormones produced by the placenta include CHORIONIC GONADOTROPIN, and PLACENTAL LACTOGEN. Not include steroid hormones ( ESTROGENS; PROGESTERONE). Hormones produced by the placenta include CHORIONIC GONADOTROPIN, and PLACENTAL LACTOGEN. Not include steroid hormones ( ESTROGENS; PROGESTERONE). MeSH:D010926 placental hormone, peptide Hormones produced by the placenta include CHORIONIC GONADOTROPIN, and PLACENTAL LACTOGEN. Not include steroid hormones ( ESTROGENS; PROGESTERONE). MeSH:D010926 IMR:0100087 Hormones that stimulate gonadal functions such as GAMETOGENESIS and sex steroid hormone production in the OVARY and the TESTIS. Major gonadotropins are glycoproteins produced primarily by the adenohypophysis ( GONADOTROPINS, PITUITARY) and the placenta ( CHORIONIC GONADOTROPIN). In some species, pituitary PROLACTIN and PLACENTAL LACTOGEN exert some luteotropic activities. Hormones that stimulate gonadal functions such as GAMETOGENESIS and sex steroid hormone production in the OVARY and the TESTIS. Major gonadotropins are glycoproteins produced primarily by the adenohypophysis ( GONADOTROPINS, PITUITARY) and the placenta ( CHORIONIC GONADOTROPIN). In some species, pituitary PROLACTIN and PLACENTAL LACTOGEN exert some luteotropic activities. MeSH:D006062 gonadotropin Hormones that stimulate gonadal functions such as GAMETOGENESIS and sex steroid hormone production in the OVARY and the TESTIS. Major gonadotropins are glycoproteins produced primarily by the adenohypophysis ( GONADOTROPINS, PITUITARY) and the placenta ( CHORIONIC GONADOTROPIN). In some species, pituitary PROLACTIN and PLACENTAL LACTOGEN exert some luteotropic activities. MeSH:D006062 IMR:0100089 thymus hormone IMR:0100090 Polypeptide hormones produced in the hypothalamus which inhibit the release of pituitary hormones. Used for PHRIH in general or for which there is no specific heading. Polypeptide hormones produced in the hypothalamus which inhibit the release of pituitary hormones. Used for PHRIH in general or for which there is no specific heading. MeSH:D010905 PHRIH pituitary hormone release inhibiting hormone Polypeptide hormones produced in the hypothalamus which inhibit the release of pituitary hormones. Used for PHRIH in general or for which there is no specific heading. MeSH:D010905 IMR:0100091 MSHRIH Melanostatin MSH release-inhibiting hormone IMR:0100092 PIH prolactin release-inhibiting hormone IMR:0100093 Hormones released by one structure (e.g., the hypothalamus or the thyroid gland) that effect the secretion of hormones from the pituitary gland. Hormones released by one structure (e.g., the hypothalamus or the thyroid gland) that effect the secretion of hormones from the pituitary gland. MeSH:D010906 PHRH pituitary hormone-releasing hormone Hormones released by one structure (e.g., the hypothalamus or the thyroid gland) that effect the secretion of hormones from the pituitary gland. MeSH:D010906 IMR:0100094 CRH Corticotropin-releasing factor corticotropin-releasing hormone IMR:0100095 A decapeptide hormone released by the hypothalamus. It stimulates the synthesis and secretion of both FOLLICLE STIMULATING HORMONE and luteinizing hormone (LH) from the pituitary gland. A decapeptide hormone released by the hypothalamus. It stimulates the synthesis and secretion of both FOLLICLE STIMULATING HORMONE and luteinizing hormone (LH) from the pituitary gland. MeSH:D007987 FSH-Releasing Hormone GnRH LH-Releasing Hormone LHRH gonadoliberin gonadorelin gonadotropin-releasing hormone A decapeptide hormone released by the hypothalamus. It stimulates the synthesis and secretion of both FOLLICLE STIMULATING HORMONE and luteinizing hormone (LH) from the pituitary gland. MeSH:D007987 IMR:0100096 Hormones secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Hormones secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). MeSH:D010908 pituitary hormone, anterior Hormones secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). MeSH:D010908 IMR:0100097 The alpha chain of pituitary glycoprotein hormones ( THYROTROPIN; FOLLICLE STIMULATING HORMONE; LUTEINIZING HORMONE) and the placental CHORIONIC GONADOTROPIN. Within a species, the alpha subunits of these four hormones are identical; the distinct functional characteristics of these glycoprotein hormones are determined by the unique beta subunits. Both subunits, the non-covalently bound heterodimers, are required for full biologic activity. The alpha chain of pituitary glycoprotein hormones ( THYROTROPIN; FOLLICLE STIMULATING HORMONE; LUTEINIZING HORMONE) and the placental CHORIONIC GONADOTROPIN. Within a species, the alpha subunits of these four hormones are identical; the distinct functional characteristics of these glycoprotein hormones are determined by the unique beta subunits. Both subunits, the non-covalently bound heterodimers, are required for full biologic activity. MeSH:D015292 glycoprotein hormone, alpha subunit The alpha chain of pituitary glycoprotein hormones ( THYROTROPIN; FOLLICLE STIMULATING HORMONE; LUTEINIZING HORMONE) and the placental CHORIONIC GONADOTROPIN. Within a species, the alpha subunits of these four hormones are identical; the distinct functional characteristics of these glycoprotein hormones are determined by the unique beta subunits. Both subunits, the non-covalently bound heterodimers, are required for full biologic activity. MeSH:D015292 IMR:0100098 Hormones secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR) that stimulate gonadal functions in both males and females. They include FOLLICLE STIMULATING HORMONE that stimulates germ cell maturation ( OOGENESIS; SPERMATOGENESIS), and LUTEINIZING HORMONE that stimulates the production of sex steroids ( ESTROGENS; PROGESTERONE; ANDROGENS). Hormones secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR) that stimulate gonadal functions in both males and females. They include FOLLICLE STIMULATING HORMONE that stimulates germ cell maturation ( OOGENESIS; SPERMATOGENESIS), and LUTEINIZING HORMONE that stimulates the production of sex steroids ( ESTROGENS; PROGESTERONE; ANDROGENS). MeSH:D006065 gonadotropin, pituitary Hormones secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR) that stimulate gonadal functions in both males and females. They include FOLLICLE STIMULATING HORMONE that stimulates germ cell maturation ( OOGENESIS; SPERMATOGENESIS), and LUTEINIZING HORMONE that stimulates the production of sex steroids ( ESTROGENS; PROGESTERONE; ANDROGENS). MeSH:D006065 IMR:0100099 A major gonadotropin secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. A major gonadotropin secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. MeSH:D005640 FSH follitropin follicle stimulating hormone A major gonadotropin secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. MeSH:D005640 IMR:0100100 A major gonadotropin secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. A major gonadotropin secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. MeSH:D005640 LH lutropin luteinizing hormone A major gonadotropin secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. MeSH:D005640 IMR:0100102 A polypeptide that is secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Growth hormone, also known as somatotropin, stimulates mitosis, cell differentiation and cell growth. Species-specific growth hormones have been synthesized. A polypeptide that is secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Growth hormone, also known as somatotropin, stimulates mitosis, cell differentiation and cell growth. Species-specific growth hormones have been synthesized. MeSH:D013006 GH somatotropin growth hormone (mol) A polypeptide that is secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Growth hormone, also known as somatotropin, stimulates mitosis, cell differentiation and cell growth. Species-specific growth hormones have been synthesized. MeSH:D013006 IMR:0100103 Hormones released from the posterior lobe of the pituitary, including vasopressin (antidiuretic hormone) and oxytocin. They are formed in the neuronal cells of the hypothalamic nuclei and stored in nerve cell endings in the posterior pituitary (neurohypophysis). Hormones released from the posterior lobe of the pituitary, including vasopressin (antidiuretic hormone) and oxytocin. They are formed in the neuronal cells of the hypothalamic nuclei and stored in nerve cell endings in the posterior pituitary (neurohypophysis). MeSH:D010909 Pituitrin pituitary hormone, posterior Hormones released from the posterior lobe of the pituitary, including vasopressin (antidiuretic hormone) and oxytocin. They are formed in the neuronal cells of the hypothalamic nuclei and stored in nerve cell endings in the posterior pituitary (neurohypophysis). MeSH:D010909 IMR:0100104 A nonapeptide posterior pituitary hormone that causes UTERINE CONTRACTIONS and stimulates MILK EJECTION. A nonapeptide posterior pituitary hormone that causes UTERINE CONTRACTIONS and stimulates MILK EJECTION. MeSH:D010121 OXT Ocytocin Pitocin oxtocin oxytocin A nonapeptide posterior pituitary hormone that causes UTERINE CONTRACTIONS and stimulates MILK EJECTION. MeSH:D010121 IMR:0100105 A polypeptide hormone of approximately 25 kDa that is produced by the SYNCYTIOTROPHOBLASTS of the PLACENTA, also known as chorionic somatomammotropin. It has both GROWTH HORMONE and PROLACTIN activities on growth, lactation, and luteal steroid production. A polypeptide hormone of approximately 25 kDa that is produced by the SYNCYTIOTROPHOBLASTS of the PLACENTA, also known as chorionic somatomammotropin. It has both GROWTH HORMONE and PROLACTIN activities on growth, lactation, and luteal steroid production. MeSH:D010928 Choriomammotropin placental lactogen A polypeptide hormone of approximately 25 kDa that is produced by the SYNCYTIOTROPHOBLASTS of the PLACENTA, also known as chorionic somatomammotropin. It has both GROWTH HORMONE and PROLACTIN activities on growth, lactation, and luteal steroid production. MeSH:D010928 IMR:0100106 A gonadotropic glycoprotein hormone produced primarily by the PLACENTA. Similar to the pituitary LUTEINIZING HORMONE in structure and function, chorionic gonadotropin is involved in maintaining the CORPUS LUTEUM during pregnancy. CG consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is virtually identical to the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. A gonadotropic glycoprotein hormone produced primarily by the PLACENTA. Similar to the pituitary LUTEINIZING HORMONE in structure and function, chorionic gonadotropin is involved in maintaining the CORPUS LUTEUM during pregnancy. CG consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is virtually identical to the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. MeSH:D006063 CG chorionic gonadotropin A gonadotropic glycoprotein hormone produced primarily by the PLACENTA. Similar to the pituitary LUTEINIZING HORMONE in structure and function, chorionic gonadotropin is involved in maintaining the CORPUS LUTEUM during pregnancy. CG consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is virtually identical to the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity. MeSH:D006063 IMR:0100108 Thymulin thymic factor, circulating IMR:0100109 thymopoietin IMR:0100110 thymosin IMR:0100111 O-Acetylcholine acetylcholine IMR:0100113 IMR:0200003 2-(3,4-Dihydroxyphenyl)ethylamine 3,4-Dihydroxyphenethylamine 4-(2-Aminoethyl)-1,2-benzenediol 4-(2-Aminoethyl)benzene-1,2-diol Dopamine dopamine IMR:0100114 IMR:0200335 (R)-(-)-Adnephrine (R)-(-)-Adrenaline (R)-(-)-Epinephrine (R)-(-)-Epirenamine 4-[(1R)-1-Hydroxy-2-(methylamino)ethyl]-1,2-benzenediol L-Adrenaline adrenalin IMR:0100115 IMR:0200116 4-[(1R)-2-Amino-1-hydroxyethyl]-1,2-benzenediol Arterenol L-Noradrenaline LEVOPHED (TN) Norepinephrine noradrenalin IMR:0100117 IMR:0200145 4-Amino-butanoic acid 4-aminobutanoic acid GABA gamma-aminobutyric acid IMR:0100118 IMR:0200057 Aminoacetic acid Gly Glycine glycine IMR:0100119 IMR:0200156 L-Glutamate L-Glutamic acid L-Glutaminic acid glutamic acid IMR:0100120 IMR:0200071 2-aminoethanesulfonic acid Taurine taurine IMR:0100122 1-(4-Hydroxyphenyl)-2-aminoethanol p-hydroxyphenylethanolamine octopamine IMR:0100123 IMR:0200412 3-(2-Aminoethyl)-1H-indol-5-ol 5-Hydroxytryptamine Serotonin enteramine serotonin IMR:0100124 IMR:0200018 2-(p-Hydroxyphenyl)ethylamine Tyramine tyramine IMR:0100125 IMR:0200295 1H-Imidazole-4-ethanamine 2-(4-Imidazolyl)ethylamine Histamine histamine IMR:0100135 beta-endorphin IMR:0100143 Somatomedin is a group of hormones that is produced, when stimulated by somatotropin (STH), to promote cell growth and division. In this way, they mediate the effect of somatotropin (also known as growth hormone). They have similar biological effects to somatotropin. Three forms include: * somatomedin A, which is another name for insulin-like growth factor 2 * somatomedin B, which is derived from vitronectin * somatomedin C, which is another name for insulin-like growth factor 1 Somatomedin is a group of hormones that is produced, when stimulated by somatotropin (STH), to promote cell growth and division. In this way, they mediate the effect of somatotropin (also known as growth hormone). They have similar biological effects to somatotropin. Three forms include: * somatomedin A, which is another name for insulin-like growth factor 2 * somatomedin B, which is derived from vitronectin * somatomedin C, which is another name for insulin-like growth factor 1 MeSH:D013002 somatomedin Somatomedin is a group of hormones that is produced, when stimulated by somatotropin (STH), to promote cell growth and division. In this way, they mediate the effect of somatotropin (also known as growth hormone). They have similar biological effects to somatotropin. Three forms include: * somatomedin A, which is another name for insulin-like growth factor 2 * somatomedin B, which is derived from vitronectin * somatomedin C, which is another name for insulin-like growth factor 1 Wikipedia:http://en.wikipedia.org/wiki/Somatomedin IMR:0100149 An angiotensinogen proteolytic cleavage product that is formed via the action of angiotensin converting enzyme on angiotensin. MeSH:D000809 angiotensin IMR:0100153 opioid peptide IMR:0100154 endorphin IMR:0100155 alpha-endorphin IMR:0100156 gamma-endorphin IMR:0100157 enkephalin IMR:0100158 leucine enkephalin IMR:0100159 adrenorphin IMR:0100160 alpha-neoendorphin IMR:0100161 rimorphin IMR:0100166 21-Amino-acid peptides produced by vascular endothelial cells and functioning as potent vasoconstrictors. The endothelin family consists of three members, ENDOTHELIN-1; ENDOTHELIN-2; and ENDOTHELIN-3. All three peptides contain 21 amino acids, but vary in amino acid composition. The three peptides produce vasoconstrictor and pressor responses in various parts of the body. However, the quantitative profiles of the pharmacological activities are considerably different among the three isopeptides. 21-Amino-acid peptides produced by vascular endothelial cells and functioning as potent vasoconstrictors. The endothelin family consists of three members, ENDOTHELIN-1; ENDOTHELIN-2; and ENDOTHELIN-3. All three peptides contain 21 amino acids, but vary in amino acid composition. The three peptides produce vasoconstrictor and pressor responses in various parts of the body. However, the quantitative profiles of the pharmacological activities are considerably different among the three isopeptides. MeSH:D016232 endothelin 21-Amino-acid peptides produced by vascular endothelial cells and functioning as potent vasoconstrictors. The endothelin family consists of three members, ENDOTHELIN-1; ENDOTHELIN-2; and ENDOTHELIN-3. All three peptides contain 21 amino acids, but vary in amino acid composition. The three peptides produce vasoconstrictor and pressor responses in various parts of the body. However, the quantitative profiles of the pharmacological activities are considerably different among the three isopeptides. MeSH:D016232 IMR:0100167 ET-1 endothelin-1 IMR:0100168 ET-2 endothelin-2 IMR:0100169 ET-3 endothelin-3 IMR:0100192 kinesin superfamily IMR:0100193 kinesin-like protein IMR:0100194 A lactogenic hormone secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). It is a polypeptide of approximately 23 kD. Besides its major action on lactation, in some species prolactin exerts effects on reproduction, maternal behavior, fat metabolism, immunomodulation and osmoregulation. Prolactin receptors are present in the mammary gland, hypothalamus, liver, ovary, testis, and prostate. A lactogenic hormone secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). It is a polypeptide of approximately 23 kD. Besides its major action on lactation, in some species prolactin exerts effects on reproduction, maternal behavior, fat metabolism, immunomodulation and osmoregulation. Prolactin receptors are present in the mammary gland, hypothalamus, liver, ovary, testis, and prostate. MeSH:D011388 PRL prolactin A lactogenic hormone secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). It is a polypeptide of approximately 23 kD. Besides its major action on lactation, in some species prolactin exerts effects on reproduction, maternal behavior, fat metabolism, immunomodulation and osmoregulation. Prolactin receptors are present in the mammary gland, hypothalamus, liver, ovary, testis, and prostate. MeSH:D011388 IMR:0100195 An anterior pituitary hormone that stimulates the secretion of CORTICOSTEROIDS and induces growth of the ADRENAL CORTEX. It is a single-chain polypeptide of about 39 amino acids, the first 24 of which are identical in all species. This 24-amino acid segment is said to be responsible for the biological activity of the peptide while the remaining 15-amino acid segment is said to be necessary for any immunological specificity. An anterior pituitary hormone that stimulates the secretion of CORTICOSTEROIDS and induces growth of the ADRENAL CORTEX. It is a single-chain polypeptide of about 39 amino acids, the first 24 of which are identical in all species. This 24-amino acid segment is said to be responsible for the biological activity of the peptide while the remaining 15-amino acid segment is said to be necessary for any immunological specificity. MeSH:D000324 ACTH Adrenocorticotropic hormone corticotropin An anterior pituitary hormone that stimulates the secretion of CORTICOSTEROIDS and induces growth of the ADRENAL CORTEX. It is a single-chain polypeptide of about 39 amino acids, the first 24 of which are identical in all species. This 24-amino acid segment is said to be responsible for the biological activity of the peptide while the remaining 15-amino acid segment is said to be necessary for any immunological specificity. MeSH:D000324 IMR:0100196 A 13-amino acid peptide derived from the ANTERIOR PITUITARY GLAND in man and from the pars intermedia in lower vertebrates. Its amino acid sequence is identical to the first 13 amino acids of ACTH. It influences the formation of deposition of MELANIN in the body. A 13-amino acid peptide derived from the ANTERIOR PITUITARY GLAND in man and from the pars intermedia in lower vertebrates. Its amino acid sequence is identical to the first 13 amino acids of ACTH. It influences the formation of deposition of MELANIN in the body. MeSH:D000521 alpha-MSH A 13-amino acid peptide derived from the ANTERIOR PITUITARY GLAND in man and from the pars intermedia in lower vertebrates. Its amino acid sequence is identical to the first 13 amino acids of ACTH. It influences the formation of deposition of MELANIN in the body. MeSH:D000521 IMR:0100197 Lipotropic or pituitary lipotropic hormone. A pituitary hormone mobilizing fat from adipose tissue. Beta-lipotropin is a single-chain peptide of about 90 residues that contains the sequences of endorphins and metenkephalin, and may be a precursor of beta-melanotropin and beta-endorphin. Gamma-lipotropin is shorter and is identical in sequence to the first 58 residues of beta-lipotropin. Both contain sequences common to ACTH and beta-melanotropin. Lipotropic or pituitary lipotropic hormone. A pituitary hormone mobilizing fat from adipose tissue. Beta-lipotropin is a single-chain peptide of about 90 residues that contains the sequences of endorphins and metenkephalin, and may be a precursor of beta-melanotropin and beta-endorphin. Gamma-lipotropin is shorter and is identical in sequence to the first 58 residues of beta-lipotropin. Both contain sequences common to ACTH and beta-melanotropin. MeSH:D008083 LPH lipotropin Lipotropic or pituitary lipotropic hormone. A pituitary hormone mobilizing fat from adipose tissue. Beta-lipotropin is a single-chain peptide of about 90 residues that contains the sequences of endorphins and metenkephalin, and may be a precursor of beta-melanotropin and beta-endorphin. Gamma-lipotropin is shorter and is identical in sequence to the first 58 residues of beta-lipotropin. Both contain sequences common to ACTH and beta-melanotropin. MeSH:D008083 IMR:0100198 Peptide hormones secreted by the intermediate lobe of the pituitary that stimulate melanin release and dispersal. Melanocyte-stimulating hormones are also found in the brain where they are presumed to play a signaling role. Peptide hormones secreted by the intermediate lobe of the pituitary that stimulate melanin release and dispersal. Melanocyte-stimulating hormones are also found in the brain where they are presumed to play a signaling role. MeSH:D009074 Intermedin Melanotropin MSH Peptide hormones secreted by the intermediate lobe of the pituitary that stimulate melanin release and dispersal. Melanocyte-stimulating hormones are also found in the brain where they are presumed to play a signaling role. MeSH:D009074 IMR:0100199 A peptide hormone of about 11 amino acids derived from PRO-OPIOMELANOCORTIN that has natriuretic activity. A peptide hormone of about 11 amino acids derived from PRO-OPIOMELANOCORTIN that has natriuretic activity. MeSH:D019825 gamma-Melanotropin gamma-MSH A peptide hormone of about 11 amino acids derived from PRO-OPIOMELANOCORTIN that has natriuretic activity. MeSH:D019825 IMR:0100200 A glycoprotein hormone secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Thyrotropin stimulates THYROID GLAND by increasing the iodide transport, synthesis and release of thyroid hormones ( THYROXINE and TRIIODOTHYRONINE). Thyrotropin consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the pituitary glycoprotein hormones (TSH; LUTEINIZING HORMONE and FSH), but the beta subunit is unique and confers its biological specificity. A glycoprotein hormone secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Thyrotropin stimulates THYROID GLAND by increasing the iodide transport, synthesis and release of thyroid hormones ( THYROXINE and TRIIODOTHYRONINE). Thyrotropin consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the pituitary glycoprotein hormones (TSH; LUTEINIZING HORMONE and FSH), but the beta subunit is unique and confers its biological specificity. MeSH:D013972 TSH thyroid-stimulating hormone thyrotropin A glycoprotein hormone secreted by the adenohypophysis ( PITUITARY GLAND, ANTERIOR). Thyrotropin stimulates THYROID GLAND by increasing the iodide transport, synthesis and release of thyroid hormones ( THYROXINE and TRIIODOTHYRONINE). Thyrotropin consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the pituitary glycoprotein hormones (TSH; LUTEINIZING HORMONE and FSH), but the beta subunit is unique and confers its biological specificity. MeSH:D013972 IMR:0100201 Octapeptide antidiuretic hormones released by the NEUROHYPOPHYSIS of all vertebrates (chemical composition varies with species). They control water metabolism and balance by regulating LUNG; GILLS; KIDNEY; etc., and water loss, and also contract smooth muscle. They may also be NEUROTRANSMITTERS. Octapeptide antidiuretic hormones released by the NEUROHYPOPHYSIS of all vertebrates (chemical composition varies with species). They control water metabolism and balance by regulating LUNG; GILLS; KIDNEY; etc., and water loss, and also contract smooth muscle. They may also be NEUROTRANSMITTERS. MeSH:D014667 ADH Antidiuretic hormone VP vasopressin Octapeptide antidiuretic hormones released by the NEUROHYPOPHYSIS of all vertebrates (chemical composition varies with species). They control water metabolism and balance by regulating LUNG; GILLS; KIDNEY; etc., and water loss, and also contract smooth muscle. They may also be NEUROTRANSMITTERS. MeSH:D014667 IMR:0100202 karyopherin alpha importin alpha IMR:0100203 karyopherin beta1 importin beta IMR:0100204 CAS/CSE IMR:0100205 Regulator of chromosome condensation RCC1 IMR:0100206 GO:0005098 Ran GTPase-activating protein Ran GAP IMR:0100207 GO:0008349 MAP kinase kinase kinase kinase MAPKKKK IMR:0100211 A family of gastrointestinal peptide hormones that excite the secretion of GASTRIC JUICE. They may also occur in the central nervous system where they are presumed to be neurotransmitters. A family of gastrointestinal peptide hormones that excite the secretion of GASTRIC JUICE. They may also occur in the central nervous system where they are presumed to be neurotransmitters. MeSH:D005755 gastrin A family of gastrointestinal peptide hormones that excite the secretion of GASTRIC JUICE. They may also occur in the central nervous system where they are presumed to be neurotransmitters. MeSH:D005755 IMR:0100212 A 36-amino acid polypeptide secreted by the PANCREAS that has physiological regulatory functions. Plasma pancreatic polypeptide increases after ingestion of food, with age, and in disease states. A lack of pancreatic polypeptide in the ISLETS OF LANGERHANS has been associated with the OBESITY in rats and mice. A 36-amino acid polypeptide secreted by the PANCREAS that has physiological regulatory functions. Plasma pancreatic polypeptide increases after ingestion of food, with age, and in disease states. A lack of pancreatic polypeptide in the ISLETS OF LANGERHANS has been associated with the OBESITY in rats and mice. MeSH:D010191 pancreatic polypeptide A 36-amino acid polypeptide secreted by the PANCREAS that has physiological regulatory functions. Plasma pancreatic polypeptide increases after ingestion of food, with age, and in disease states. A lack of pancreatic polypeptide in the ISLETS OF LANGERHANS has been associated with the OBESITY in rats and mice. MeSH:D010191 IMR:0100213 A polypeptide hormone produced in the HYPOTHALAMUS, and other tissues and organs. It inhibits the release of growth hormone ( SOMATOTROPIN), and also modulates important physiological functions of the kidney, pancreas, and gastrointestinal tract. Somatostatin receptors are widely expressed throughout the body. Somatostatin also acts as a neurotransmitter in the central and peripheral nervous systems. A polypeptide hormone produced in the HYPOTHALAMUS, and other tissues and organs. It inhibits the release of growth hormone ( SOMATOTROPIN), and also modulates important physiological functions of the kidney, pancreas, and gastrointestinal tract. Somatostatin receptors are widely expressed throughout the body. Somatostatin also acts as a neurotransmitter in the central and peripheral nervous systems. MeSH:D013004 SRIH growth hormone-release inhibiting factor growth hormone-release inhibiting hormone somatotropin release-inhibiting hormone somatostatin A polypeptide hormone produced in the HYPOTHALAMUS, and other tissues and organs. It inhibits the release of growth hormone ( SOMATOTROPIN), and also modulates important physiological functions of the kidney, pancreas, and gastrointestinal tract. Somatostatin receptors are widely expressed throughout the body. Somatostatin also acts as a neurotransmitter in the central and peripheral nervous systems. MeSH:D013004 IMR:0100216 ERK5, also known as big MAP kinase 1 (BMK1), is twice the size of other MAPKs. The amino-terminal half contains the kinase domain, which is similar to that of ERK1/2 and has the TEY activation motif, whereas the carboxy-terminal half is unique. MEK5 phosphorylates and activates ERK5, and then the activated ERK5 phosphorylates substrates including myocyte enhancer factor 2 (MEF2). ERK5, also known as big MAP kinase 1 (BMK1), is twice the size of other MAPKs. The amino-terminal half contains the kinase domain, which is similar to that of ERK1/2 and has the TEY activation motif, whereas the carboxy-terminal half is unique. MEK5 phosphorylates and activates ERK5, and then the activated ERK5 phosphorylates substrates including myocyte enhancer factor 2 (MEF2). BMK1 ERK5 ERK5, also known as big MAP kinase 1 (BMK1), is twice the size of other MAPKs. The amino-terminal half contains the kinase domain, which is similar to that of ERK1/2 and has the TEY activation motif, whereas the carboxy-terminal half is unique. MEK5 phosphorylates and activates ERK5, and then the activated ERK5 phosphorylates substrates including myocyte enhancer factor 2 (MEF2). PMID:16880823 IMR:0100218 Apoptosis signal-regulating kinase 1 MAPK/ERK kinase kinase 5 MAPKKK5 MEK kinase 5 MEKK 5 apoptosis inducing kinase1 ASK1 IMR:0100219 TAO1 IMR:0100221 MAPKKK6 ASK2 IMR:0100222 MAPK/ERK kinase kinase 1 MEK kinase 1 MEKK1 IMR:0100224 MAP kinase kinase 5 MAPK/ERK kinase 5 MAPKK 5 MEK5 MKK5 MEK5(MKK5) IMR:0100248 MLK7 MLTK MRK zipper sterile alpha motif kinase ZAK IMR:0100249 mixed lineage kinase MLK IMR:0100250 MAP3K9 MLK1 IMR:0100251 MAP3K10 MKN28 derived serine / threonine kinase MST MLK2 IMR:0100252 MAP3K11 PTK1 SH3 domain containing proline rich kinase SPRK protein tyrosine kinase 1 MLK3 IMR:0100253 MLK4 IMR:0100254 dual leucine zipper bearing kinase DLK IMR:0100255 Dual leucine zipper bearing kinase Leucine-zipper protein kinase MAP3K12 MAPK upstream kinase MUK ZPK zipper protein kinase DLK family IMR:0100256 MAP3K13 leucine zipper kinase LZK IMR:0100258 SLP-76 family IMR:0100267 3PK MAP kinase-activated protein kinase 3 MAPK- activated protein kinase 3 MAPKAPK3 IMR:0100268 GO:0005100 Rho GTPase-activating protein Rho GAP IMR:0100269 GO:0005097 Rab GTPase-activating protein Rab GAP IMR:0100270 GO:0008060 Arf GTPase-activating protein Arf GAP IMR:0100271 Four groups of kinases have been shown to be activated by MAP kinases, ribosomal S6 kinase (RSK also known as MAPKAPK1), MAP kinase-activated protein kinase 2/3 (MAPKAPK2/3), MAP kinase-interacting kinase or MAP kinase signal-integrating kinase (MNK) and MAPKAPK5 (PRAK). Four groups of kinases have been shown to be activated by MAP kinases, ribosomal S6 kinase (RSK also known as MAPKAPK1), MAP kinase-activated protein kinase 2/3 (MAPKAPK2/3), MAP kinase-interacting kinase or MAP kinase signal-integrating kinase (MNK) and MAPKAPK5 (PRAK). MAP kinase-activated protein kinase MAP kinase-regulated protein kinase MAPK-activated protein kinase MAPKAPK Four groups of kinases have been shown to be activated by MAP kinases, ribosomal S6 kinase (RSK also known as MAPKAPK1), MAP kinase-activated protein kinase 2/3 (MAPKAPK2/3), MAP kinase-interacting kinase or MAP kinase signal-integrating kinase (MNK) and MAPKAPK5 (PRAK). PMID:12639708 PMID:9628874 IMR:0100272 MAPKAPK5 (PRAK) activity is regulated by p38 and activated MAPKAPK5 in turn phosphorylates small heat shock protein 27 (HSP27). MAPKAPK5 (PRAK) activity is regulated by p38 and activated MAPKAPK5 in turn phosphorylates small heat shock protein 27 (HSP27). MAP kinase-activated protein kinase 5 MAPK-activated protein kinase 5 PRAK MAPKAPK5 MAPKAPK5 (PRAK) activity is regulated by p38 and activated MAPKAPK5 in turn phosphorylates small heat shock protein 27 (HSP27). PMID:9628874 IMR:0100273 MNK1/2 are regulated by p38 and ERK, but not by JNK. MNK1/2 can phosphorylate eukaryotic initiation factor-4E (eIF-4E). MNK1/2 are regulated by p38 and ERK, but not by JNK. MNK1/2 can phosphorylate eukaryotic initiation factor-4E (eIF-4E). MAP kinase signal-integrating kinase MAP kinase-interacting kinase MNK MNK1/2 are regulated by p38 and ERK, but not by JNK. MNK1/2 can phosphorylate eukaryotic initiation factor-4E (eIF-4E). PMID:9628874 IMR:0100274 AR SDGF amphiregulin IMR:0100275 BTC betacellulin IMR:0100276 EPR epiregulin IMR:0100277 heparin-binding EGF-like growth factor HB-EGF IMR:0100278 transforming growth factor alpha TGF-alpha IMR:0100279 GO:0005154　epidermal growth factor receptor binding epidermal growth factor EGF (mol) IMR:0100281 IkB-beta inhibitor of NF-kappaB beta I-kappaB beta IMR:0100282 IkB-epsilon inhibitor of NF-kappaB epsilon I-kappaB epsilon IMR:0100288 Bad (mol) IMR:0100289 Bid (mol) IMR:0100290 Bcl-2 interacting killer Bik IMR:0100291 BIM (mol) IMR:0100297 caspase-6 IMR:0100298 caspase-7 IMR:0100299 caspase-9 IMR:0100300 caspase-8 IMR:0100301 caspase-10 IMR:0100303 caspase-2 (mol) IMR:0100304 caspase-4 IMR:0100305 caspase-5 IMR:0100306 caspase-11 IMR:0100307 caspase-12 IMR:0100308 caspase-14 IMR:0100309 caspase-13 IMR:0100310 Smad1 IMR:0100311 Smad2 IMR:0100312 Smad3(mol) IMR:0100313 Smad5 IMR:0100314 Smad9 Smad8 IMR:0100315 Smad4 IMR:0100317 Smad6 IMR:0100318 Smad7 IMR:0100320 JAK2 IMR:0100321 JAK3 IMR:0100322 Tyk2 IMR:0100328 neuronal apoptosis inhibitory protein NAIP IMR:0100329 HIAP2 MIHB cellular inhibitor of apoptosis protein-1 mammalian IAP homologue B c-IAP1 IMR:0100330 HIAP1 MIHC cellular inhibitor of apoptosis protein-2 mammalian IAP homologue C c-IAP2 IMR:0100331 IAP-like protein ILP-1 MIHA X-linked IAP mammalian IAP homologue A XIAP IMR:0100332 Survivin IMR:0100349 RasGRP IMR:0100350 T-cell receptor alpha TCR alpha IMR:0100351 T-cell receptor beta TCR beta IMR:0100352 P59-FYN SLK SYN Fyn IMR:0100353 LSK P56-LCK T cell-specific protein-tyrosine kinase Lck IMR:0100355 c-Raf c-Raf-1 Raf-1 IMR:0100356 PAK1 IMR:0100363 Cbl-b IMR:0100364 Cbl-c Cbl-3 IMR:0100366 G-alpha-s IMR:0100367 G-alpha-olf IMR:0100368 G-alpha-i 1 IMR:0100369 G-alpha-i 2 IMR:0100370 G-alpha-i 3 IMR:0100373 transducin alpha-1 G-alpha-t 1 IMR:0100374 transducin alpha-2 G-alpha-t 2 IMR:0100375 G-alpha-11 IMR:0100376 G-alpha-14 IMR:0100377 G-alpha-15 IMR:0100378 G-alpha-q IMR:0100379 G-alpha-Y IMR:0100380 G-alpha-12 IMR:0100381 G-alpha-13 IMR:0100382 Grb7/10/14 family IMR:0100383 Cdk inhibitor protein cyclin-dependent kinase inhibitor 1 p21 Cip1 IMR:0100384 cyclin-dependent kinase inhibitor p27 p27Kip1 IMR:0100385 cyclin-dependent kinase inhibitor p57 p57KIP2 IMR:0100387 Interferon omega IFN omega IMR:0100389 Interferon delta IFN delta IMR:0100393 IMR:0010311 IMR:0011340 IMR:0011552 IRS1 insulin receptor substrate-1 IRS-1 IMR:0100394 IMR:0010312 IMR:0011553 IRS2 insulin receptor substrate-2 IRS-2 IMR:0100395 insulin receptor substrate-3 pp60 IRS-3 IMR:0100396 insulin receptor substrate-4 IRS-4 IMR:0100407 GO:0005163 nerve growth factor NGF IMR:0100408 brain-derived neurotrophic factor BDNF IMR:0100409 neurotrophic factor 3 neurotrophin-3 NT-3 IMR:0100410 NT-4 NT-5 neurotrophic factor 4 neurotrophic factor 5 neurotrophin-4 neurotrophin-5 NT-4/5 IMR:0100418 TR alpha 1 IMR:0100419 c-erbA-alpha 2 TR alpha 2 IMR:0100420 TR beta 1 IMR:0100421 TR beta 2 IMR:0100422 TNF receptor associated factor 1 TRAF1 IMR:0100423 TNF receptor associated factor 2 TRAF2 (mol) IMR:0100424 TNF receptor associated factor 3 TRAF3 (mol) IMR:0100425 TNF receptor associated factor 4 TRAF4 IMR:0100426 TNF receptor associated factor 5 TRAF5 IMR:0100427 TNF receptor associated factor 6 TRAF6 IMR:0100433 RalGEF RalGDS IMR:0100440 GO:0005088 Ras guanine nucleotide exchange factor RasGEF IMR:0100450 MAPK/ERK kinase kinase 2 MEK kinase 2 MEKK2 IMR:0100451 MAPK/ERK kinase kinase 3 MEK kinase 3 MEKK3 IMR:0100452 ERK activator kinase 1 MAP kinase kinase 1 MAPK/ERK kinase 1 MAPKK 1 MEK1 MKK1 MEK1(MKK1) IMR:0100453 ERK activator kinase 2 MAP kinase kinase 2 MAPK/ERK kinase 2 MAPKK 2 MEK2 MKK2 MEK2(MKK2) IMR:0100454 JNK activating kinase 1 JNKK JNKK 1 JNKK1 MAP kinase kinase 4 MKK4 SAPK/ERK kinase 1 SEK1 c- Jun N-terminal kinase kinase 1 MKK4(JNKK1)(SEK1) IMR:0100455 JNK activating kinase 2 JNK kinase 2 JNKK 2 JNKK2 MAP kinase kinase 7 MAPK/ERK kinase 7 MAPKK 7 MKK7 SKK4 c-Jun N-terminal kinase kinase 2 MKK7(JNKK2) IMR:0100456 MAP kinase kinase 3 MAPK/ERK kinase 3 MAPKK 3 MKK3 IMR:0100457 MAP kinase kinase 6 MAPK/ERK kinase 6 MAPKK 6 SAPKK3 MKK6 IMR:0100458 Inhibitor of nuclear factor kappa-B kinase alpha subunit IKK alpha IMR:0100459 Inhibitor of nuclear factor kappa B kinase beta subunit IKK beta IMR:0100460 NEMO NF-kappaB essential modulator IKK gamma IMR:0100461 IKK epsilon IMR:0100463 Fas-associated death domain MORT1 mediator of receptor-induced toxicity FADD IMR:0100464 TNF receptor-associated death domain TNFR-associated death domain tumor necrosis factor receptor-associated death domain TRADD (mol) IMR:0100465 myeloid differentiation factor 88 MyD88 IMR:0100466 RAIDD RIP-associated ICH-1/CED-3-homologous protein with a death domain caspase and RIP adaptor with death domain CRADD IMR:0100470 SCF ubiquitin ligase complex is a subtype of molecular complex. Skp1/Cul1/F-box protein complex SCF ubiquitin ligase complex IMR:0100484 protein kinase C theta PKC theta IMR:0100486 classical PKC isoforms (alpha, betaI, betaII and gamma) are regulated by calcium, diacylglycerol (DAG) and phospholipids. classical PKC isoforms (alpha, betaI, betaII and gamma) are regulated by calcium, diacylglycerol (DAG) and phospholipids. conventional PKC cPKC classical PKC isoforms (alpha, betaI, betaII and gamma) are regulated by calcium, diacylglycerol (DAG) and phospholipids. PMID:15282562 IMR:0100488 IL-1 receptor-associated kinase Interleukin-1 receptor-associated kinase Pelle-like protein kinase IRAK IMR:0100504 Smads 2 and 3 serve principally as substrates for the TGFbeta, activin, and Nodal receptors. Smads 2 and 3 serve principally as substrates for the TGFbeta, activin, and Nodal receptors. Smad2/3 Smads 2 and 3 serve principally as substrates for the TGFbeta, activin, and Nodal receptors. PMID:16322555 IMR:0100507 Smads 1, 5, and 8 serve principally as substrates for the BMP and anti-Muellerian receptors. Smads 1, 5, and 8 serve principally as substrates for the BMP and anti-Muellerian receptors. Smad1/5/8 Smads 1, 5, and 8 serve principally as substrates for the BMP and anti-Muellerian receptors. PMID:16322555 IMR:0100512 Smad ubiquitin regulatory factors Smurf IMR:0100513 E3 ubiquitin ligase Smad-specific E3 ubiquitin ligase 1 Ubiquitin--protein ligase SMURF1 Ubiquitin-protein ligase hSMURF1 xSMURF1 Smurf1 IMR:0100514 Smad-specific E3 ubiquitin ligase 2 Ubiquitin--protein ligase SMURF2 hSMURF2 Smurf2 IMR:0100535 GCK family IMR:0100536 germinal center kinase GCK IMR:0100537 GCK related KHS1 germinal center kinase related GCKR IMR:0100538 GCK-like kinase GLK IMR:0100540 Sequestosome 1 p62 IMR:0100543 GO:0004685 Ca2+/calmodulin-dependent protein kinase CaM-kinase CaMK IMR:0100548 Ca2+/calmodulin-dependent protein kinase II CaMKII CaM-kinase II IMR:0100549 PDGF A-chain IMR:0100550 PDGF B-chain IMR:0100551 AFGF Acidic fibroblast growth factor Beta-endothelial cell growth factor ECGF-beta HBGF-1 FGF-1 IMR:0100552 BFGF Basic fibroblast growth factor HBGF-2 Prostatropin FGF-2 IMR:0100553 Fibroblast growth factor-3 HBGF-3 INT-2 FGF-3 IMR:0100554 HBGF-4 HST HST-1 Heparin secretory transforming protein K-fibroblast growth factor KFGF Transforming protein KS3 FGF-4 IMR:0100555 HBGF-5 Smag-82 FGF-5 IMR:0100556 HBGF-6 HST-2 FGF-6 IMR:0100557 Fibroblast growth factor-7 HBGF-7 KGF FGF-7 IMR:0100558 AIGF Fibroblast growth factor-8 HBGF-8 FGF-8 IMR:0100559 Fibroblast growth factor-9 GAF HBGF-9 FGF-9 IMR:0100560 Keratinocyte growth factor 2 FGF-10 IMR:0100561 FHF-3 Fibroblast growth factor homologous factor 3 FGF-11 IMR:0100562 FHF-1 Fibroblast growth factor homologous factor 1 Myocyte-activating factor FGF-12 IMR:0100563 FHF-2 Fibroblast growth factor homologous factor 2 FGF-13 IMR:0100564 FHF-4 Fibroblast growth factor homologous factor 4 FGF-14 IMR:0100565 FGF-15 IMR:0100566 FGF-16 IMR:0100567 FGF-17 IMR:0100568 zFGF5 FGF-18 IMR:0100569 FGF-19 IMR:0100570 FGF-20 IMR:0100571 FGF-21 IMR:0100572 FGF-22 IMR:0100573 Tumor-derived hypophosphatemia inducing factor FGF-23 IMR:0100575 NCBI-Human-GeneID:6714 NCBI-Mouse-GeneID:20779 NCBI-Rat-GeneID:83805 c-Src p60-Src Src (mol) NCBI-Human-GeneID:6714 https://www.ncbi.nlm.nih.gov/gene/6714 NCBI-Mouse-GeneID:20779 https://www.ncbi.nlm.nih.gov/gene/20779 NCBI-Rat-GeneID:83805 https://www.ncbi.nlm.nih.gov/gene/83805 IMR:0100579 transmembrane heparan sulfate proteoglycan syndecan IMR:0100580 CD138 antigen SYND1 syndecan-1 IMR:0100581 HSPG Heparan sulfate proteoglycan core protein SYND2 fibroglycan syndecan-2 IMR:0100582 N-syndecan Neuroglycan SYND3 syndecan-3 IMR:0100583 Amphiglycan Ryudocan core protein SYND4 syndecan-4 IMR:0100589 IMR:0010392 PI3K Phosphatidylinositol 3-kinase regulatory alpha subunit PtdIns-3-kinase p85-alpha PI3-kinase p85-alpha subunit IMR:0100590 IMR:0010393 Phosphatidylinositol 3-kinase regulatory beta subunit PtdIns-3-kinase p85-beta PI3-kinase p85-beta subunit IMR:0100592 IMR:0010389 PI3K Phosphatidylinositol 3-kinase catalytic subunit, alpha isoform (EC 2.7.1.137) (PI3-kinase p110 subunit alpha) (PtdIns-3-kinase p110) (PI3K) Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, alpha isoform PtdIns-3-kinase p110 PI3-kinase p110 subunit alpha IMR:0100593 IMR:0010390 PI3K PI3Kbeta Phosphatidylinositol 3-kinase catalytic subunit, beta isoform (EC 2.7.1.137) (PI3-kinase p110 subunit beta) (PtdIns-3-kinase p110) (PI3K) (PI3Kbeta) Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, beta isoform PtdIns-3-kinase p110 PI3-kinase p110 subunit beta IMR:0100594 PI3K Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, delta isoform PtdIns-3-kinase p110 p110delta PI3-kinase p110 subunit delta IMR:0100597 IMR:0010763 CDC28 CDK1 Cdc2 Cell division control protein 2 homolog Cell division control protein 2 homolog (EC 2.7.1.-) (p34 protein kinase) (Cyclin-dependent kinase 1) (CDK1) Cell division control protein 2 homolog (EC 2.7.1.-) (p34 protein kinase) (Cyclin-dependent kinase 1) (CDK1) form Cyclin-dependent kinase 1 p34 protein kinase Cdc2 (mol) IMR:0100599 Cell division protein kinase 3 CDK3(mol) IMR:0100601 CRK6 Cell division protein kinase 5 Serine/threonine protein kinase PSSALRE TPKII catalytic subunit Tau protein kinase II catalytic subunit CDK5(mol) IMR:0100603 IMR:0010771 39 kDa protein kinase 39 protein kinase CAK CAK1 CDK-activating kinase CR4 protein kinase Cdk7 Cell division protein kinase 7 Cell division protein kinase 7 (EC 2.7.1.-) (CDK-activating kinase) (CAK)(TFIIH) (basal transcription factor complex kinase subunit) (39 kDa protein kinase) (P39 Mo15)(STK1)(CAK1) P39 Mo15 Protein-tyrosine kinase MPK-7 STK1 TFIIH basal transcription factor complex kinase subunit CDK7(mol) IMR:0100604 Cell division protein kinase 8 Protein kinase K35 CDK8(mol) IMR:0100605 IMR:0010181 C-2K Cdk 9 protein Cell division protein kinase 9 Serine/threonine-protein kinase PITALRE CDK9(mol) IMR:0100607 cyclin A IMR:0100608 IMR:0010764 IMR:0011589 CGA1 Cyclin A1 cyclin A1 IMR:0100609 IMR:0010768 IMR:0011591 CGA2 Cyclin A Cyclin A2 cyclin A cyclin A2 IMR:0100613 cyclin C IMR:0100614 cyclin D IMR:0100616 IMR:0010668 IMR:0011614 CGD2 G1/S-specific cyclin D2 Vin-1 proto-oncogene cyclin D2 IMR:0100617 IMR:0010666 IMR:0011615 CGD3 G1/S-specific cyclin D3 cyclin D3 IMR:0100620 IMR:0010672 IMR:0011595 CGE2 G1/S-Specific cyclin E2 cyclin E2 IMR:0100621 G2/mitotic-specific cyclin F cyclin F IMR:0100622 cyclin G IMR:0100623 cyclin G cyclin G1 IMR:0100624 cyclin G2 IMR:0100625 IMR:0010772 IMR:0011707 CYCH Cyclin H MO15-associated protein p34 p37 cyclin H IMR:0100626 cyclin I IMR:0100627 cyclin K IMR:0100628 cyclin T IMR:0100629 IMR:0010177 IMR:0011619 CCT1 CycT1 Cyclin T Cyclin T1 cyclin T cyclin T1 IMR:0100630 IMR:0010178 Cyclin T2 cyclin T2 IMR:0100636 CDK-activating kinase CAK IMR:0100645 CDK inhibitor p40 SIC1 protein Sic1 IMR:0100648 Caspase-like protein ESPL1 Cut1 Esp1 Extra spindle poles-like 1 protein separin separase IMR:0100661 G1/S-specific cyclin CLN1 Cln1 IMR:0100662 G1/S-specific cyclin CLN2 Cln2 IMR:0100663 G1/S-specific cyclin CLN3 Cln3 IMR:0100664 G2/mitotic-specific cyclin 1 Clb1 IMR:0100665 G2/mitotic-specific cyclin 2 Clb2 IMR:0100666 G2/mitotic-specific cyclin 3 Clb3 IMR:0100667 G2/mitotic-specific cyclin 4 Clb4 IMR:0100668 S-phase entry cyclin 5 Clb5 IMR:0100669 S-phase entry cyclin 6 Clb6 IMR:0100670 G1-cyclin IMR:0100671 G1/S-cyclin IMR:0100672 S-cyclin IMR:0100673 G2/M-cyclin M-cyclin IMR:0100674 TNF alpha receptor IMR:0100677 CD221 antigen Insulin-like growth factor I receptor precursor IGF-1 receptor IMR:0100698 IMR:0200368 1D-myo-Inositol 1,4-bisphosphate D-myo-Inositol 1,4-bisphosphate Inositol 1,4-bisphosphate myo-Inositol 1,4-bisphosphate IP2 IMR:0100700 EC:3.1.4.17 GO:0004115 cAMP-specific PDE cAMP-specific phosphodiesterase cyclic AMP phosphodiesterase cAMP phosphodiesterase IMR:0100702 GO:0008603 cAMP-dependent protein kinase regulatory chain PKA regulatory subunit IMR:0100703 GO:0004691 cAMP-dependent protein kinase catalytic subunit PKA catalytic subunit IMR:0100704 Prothrombin thrombin IMR:0100707 pro-apoptotic Bcl-2 family IMR:0100708 Bax subfamily IMR:0100709 Bik family BH3 subfamily IMR:0100712 IPR:008297 N Notch IMR:0100714 NCBI-Human-GeneID:4851 NCBI-Mouse-GeneID:18128 NCBI-Rat-GeneID:25496 Notch-1 Notch1 Notch 1 (mol) NCBI-Human-GeneID:4851 https://www.ncbi.nlm.nih.gov/gene/4851 NCBI-Mouse-GeneID:18128 https://www.ncbi.nlm.nih.gov/gene/18128 NCBI-Rat-GeneID:25496 https://www.ncbi.nlm.nih.gov/gene/25496 IMR:0100715 NCBI-Human-GeneID:4853 NCBI-Mouse-GeneID:18129 NCBI-Rat-GeneID:29492 Notch-2 Notch2 Notch 2 (mol) NCBI-Human-GeneID:4853 https://www.ncbi.nlm.nih.gov/gene/4853 NCBI-Mouse-GeneID:18129 https://www.ncbi.nlm.nih.gov/gene/18129 NCBI-Rat-GeneID:29492 https://www.ncbi.nlm.nih.gov/gene/29492 IMR:0100716 NCBI-Human-GeneID:4854 NCBI-Mouse-GeneID:18131 NCBI-Rat-GeneID:56761 Neurogenic locus notch homolog protein 3 precursor Notch-3 Notch3 Notch 3 (mol) NCBI-Human-GeneID:4854 https://www.ncbi.nlm.nih.gov/gene/4854 NCBI-Mouse-GeneID:18131 https://www.ncbi.nlm.nih.gov/gene/18131 NCBI-Rat-GeneID:56761 https://www.ncbi.nlm.nih.gov/gene/56761 IMR:0100717 Notch-4 Notch4 Notch 4 IMR:0100718 Delta IMR:0100720 DLL1 Delta1 Delta-like1 IMR:0100721 DLL3 Delta-like3 IMR:0100722 DLL4 Delta4 Delta-like4 IMR:0100731 PS-1 S182 protein presenilin 1 IMR:0100732 AD3LP AD5 ALG-3 Alzheimer disease 4 homolog E5-1 PS-2 STM-2 presenilin 2 IMR:0100733 STAT5 IMR:0100736 GSK-3 alpha IMR:0100738 NCBI-Human-GeneID:50846 NCBI-Mouse-GeneID:13363 NCBI-Rat-GeneID:84380 Desert hedgehog HHG-3 DHH (mol) NCBI-Human-GeneID:50846 https://www.ncbi.nlm.nih.gov/gene/50846 NCBI-Mouse-GeneID:13363 https://www.ncbi.nlm.nih.gov/gene/13363 NCBI-Rat-GeneID:84380 https://www.ncbi.nlm.nih.gov/gene/84380 IMR:0100739 NCBI-Human-GeneID:3549 NCBI-Mouse-GeneID:16147 NCBI-Rat-GeneID:84399 HHG-2 Indian hedgehog IHH (mol) NCBI-Human-GeneID:3549 https://www.ncbi.nlm.nih.gov/gene/3549 NCBI-Mouse-GeneID:16147 https://www.ncbi.nlm.nih.gov/gene/16147 NCBI-Rat-GeneID:84399 https://www.ncbi.nlm.nih.gov/gene/84399 IMR:0100744 T cell-specific transcription factor 1-alpha TCF1-alpha LEF-1 IMR:0100745 T-cell factor 1 T-cell-specific transcription factor 1 TCF-1 TCF7 Transcription factor 7 TCF-1 IMR:0100746 HMG-box transcription factor 3 TCF-3 TCF7L1 Transcription factor 7-like 1 mTCF-3 TCF-3 IMR:0100747 HMG box transcription factor 4 T-cell-specific transcription factor 4 TCF-4 TCF7L2 hTCF-4 mTCF-4 TCF-4 IMR:0100755 IPR:008339 dishevelled family Dsh family IMR:0100757 DSH homolog 1 Dishevelled-1 Dvl-1 IMR:0100758 DSH homolog 2 Dishevelled-2 Dvl-2 IMR:0100759 DSH homolog 3 Dishevelled-3 Dvl-3 IMR:0100760 DSH homolog 1-like Dishevelled-1-like Dvl-1-like IMR:0100765 Int-1 Wnt-1 IMR:0100766 IRP protein Int-1 related protein Wnt-2 IMR:0100767 Wnt-13 Wnt-2b IMR:0100768 Wnt-3 IMR:0100769 Wnt-3a IMR:0100770 Wnt-4 IMR:0100771 Wnt-5a IMR:0100772 Wnt-5b IMR:0100773 Wnt-6 IMR:0100774 Wnt-7a IMR:0100775 Wnt-7b IMR:0100776 Wnt-8d Wnt-8a IMR:0100777 Wnt-8b IMR:0100778 Wnt-14 Wnt-9a IMR:0100779 Wnt-14b Wnt-15 Wnt-9b IMR:0100780 Wnt-10a IMR:0100781 Wnt-12 Wnt-10b IMR:0100782 Wnt-11 IMR:0100783 Wnt-16 IMR:0100798 LDL receptor-related protein low density lipoprotein receptor-related protein low-density lipoprotein receptor-related protein LRP family IMR:0100799 LDL receptor-related protein 1 low density lipoprotein receptor-related protein 1 low-density lipoprotein receptor-related protein 1 LRP1 IMR:0100800 Glycoprotein 330 LDL-receptor-related protein 2 Megalin gp330 low density lipoprotein (LDL) receptor-related protein 2 LRP2 IMR:0100809 GO:0004681 Casein kinase I IMR:0100810 CK1 Casein kinase I, alpha isoform CKI-alpha IMR:0100811 Casein kinase I, gamma 1 isoform CKI-gamma 1 IMR:0100812 Casein kinase I, gamma 2 isoform CKI-gamma 2 IMR:0100813 Casein kinase I, gamma 3 isoform CKI-gamma 3 IMR:0100814 CKId Casein kinase I, delta isoform CKI-delta IMR:0100815 CKIe Casein kinase I, epsilon isoform CKI-epsilon IMR:0100837 JAB JAK-binding protein SSI-1 STAT induced STAT inhibitor 1 Suppressor of cytokine signaling 1 TIP-3 Tec-interacting protein 3 SOCS-1 IMR:0100838 CIS-2 Cytokine-inducible SH2 protein 2 SSI-2 STAT induced STAT inhibitor 2 Suppressor of cytokine signaling 2 SOCS-2 IMR:0100839 CIS-3 Cytokine-inducible SH2 protein 3 Protein EF-10 SSI-3 STAT induced STAT inhibitor 3 Suppressor of cytokine signaling 3 SOCS-3 IMR:0100840 CIS-4 Cytokine-inducible SH2 protein 4 Suppressor of cytokine signaling 4 SOCS-4 IMR:0100841 CIS-6 Cytokine-inducible SH2 protein 6 Suppressor of cytokine signaling 5 SOCS-5 IMR:0100842 NAP-4 Nck, Ash and phospholipase C gamma-binding protein Nck-associated protein 4 Suppressor of cytokine signaling 6 SOCS-6 IMR:0100843 Suppressor of cytokine signaling 7 SOCS-7 IMR:0100847 TSE1 Tissue-specific extinguisher-1 cAMP-dependent protein kinase type I-alpha regulatory chain PKA type I alpha regulatory subunit IMR:0100848 cAMP-dependent protein kinase type I-beta regulatory chain PKA type I beta regulatory subunit IMR:0100849 cAMP-dependent protein kinase type II-alpha regulatory chain PKA type II alpha regulatory subunit IMR:0100850 cAMP-dependent protein kinase type II-beta regulatory chain PKA type II beta regulatory subunit IMR:0100851 PKA C-alpha cAMP-dependent protein kinase, alpha-catalytic subunit PKA alpha catalytic subunit IMR:0100852 PKA C-beta cAMP-dependent protein kinase, beta-catalytic subunit PKA beta catalytic subunit IMR:0100853 PKA C-gamma cAMP-dependent protein kinase, gamma-catalytic subunit PKA gamma catalytic subunit IMR:0200113 L-Asparagine IMR:0200137 L-Histidine IMR:0200140 L-Lysine IMR:0200154 L-Threonine IMR:0200183 L-Proline IMR:0200240 L-Tyrosine IMR:0200251 L-Alanine IMR:0200272 L-Isoleucine IMR:0200274 L-Phenylalanine IMR:0200290 L-Dopa IMR:0200292 GMP IMR:0200307 L-Tryptophan IMR:0200342 L-Ornithine IMR:0200428 L-Arginine IMR:0200448 L-Glutamine IMR:0200453 L-Serine IMR:0200459 L-Aspartic acid IMR:0200467 L-Cysteine IMR:0200488 L-Methionine IMR:0200492 L-Leucine IMR:0200501 L-Valine MONDO:0005542 Signs and symptoms related to acute ischemia of the myocardium secondary to coronary artery disease. The clinical presentation covers a spectrum of heart diseases from unstable angina to myocardial infarction. Acute coronary syndrome (ACS) is a syndrome (a set of signs and symptoms) due to decreased blood flow in the coronary arteries such that part of the heart muscle is unable to function properly or dies. (https://en.wikipedia.org/wiki/Acute_coronary_syndrome) acute coronary syndrome MONDO:0015292 An inflammatory disease involving a pathogenic inflammatory response in the endothelium. endotheliitis MONDO:0044033 An acute or subacute reversible condition characterized by headaches, mental status changes, visual disturbances, and seizures associated with imaging findings of posterior leukoencephalopathy. It has been observed in association with hypertensive encephalopathy, eclampsia, and immunosuppressive and cytotoxic drug treatment. reversible posterior leukoencephalopathy syndrome posterior leukoencephalopathy syndrome MONDO:0044079 A disorder of the heart and kidneys in which dysfunction of one of the organs induces dysfunction of the other organ. Cardiorenal syndrome MPATH:181 Reactive formation of fibrous tissue. fibrosis MP:0005039 Reduced oxygenation of body tissues resulting in the decreased pressure of this component of body gases; commonly due to hypoxemia decreased tissue partial O2 level hypoxia MP:0011018 Abnormal presence of an eosinophilic hyaline (glass-like) material composed of fibrin, proteinaceous exudate and cellular debris, and lining or filling the alveoli, alveolar ducts and bronchioles; hyaline membranes block gas exchange and are usually found at autopsy in individuals that have died of respiratory distress syndrome. pulmonary hyaline membrane formation NCBITaxon:10090 house mouse mouse mus musculus NCBITaxon:10114 rat rats rattus NCBITaxon:10239 GC_ID:1 Vira Viridae viruses virus NCBITaxon:11118 GC_ID:1 coronavirus Coronaviridae NCBITaxon:1206794 Ecdysozoa NCBITaxon:1335626 Middle East respiratory syndrome-related coronavirus (MERS-CoV), or EMC/2012 (HCoV-EMC/2012), is a species of coronavirus which infects humans, bats, and camels. Middle East respiratory syndrome-related coronavirus (MERS-CoV), or EMC/2012 (HCoV-EMC/2012), is a species of coronavirus which infects humans, bats, and camels. middle East respiratory syndrome-related coronavirus MERS coronavirus MERS virus Middle East Respiratory Syndrome Coronavirus (MERS-CoV) MERS-CoV Middle East respiratory syndrome-related coronavirus (MERS-CoV), or EMC/2012 (HCoV-EMC/2012), is a species of coronavirus which infects humans, bats, and camels. Wikipedia:Middle_East_respiratory_syndrome–related_coronavirus NCBITaxon:2499399 GC_ID:1 Cornidovirineae NCBITaxon:2501931 GC_ID:1 Orthocoronavirinae NCBITaxon:2509494 Merbecovirus is a subgenus of viruses in the genus Betacoronavirus.The viruses in this subgenus were previously known as group 2c coronaviruses. Merbecovirus is a subgenus of viruses in the genus Betacoronavirus.The viruses in this subgenus were previously known as group 2c coronaviruses. Merbecovirus Merbecovirus is a subgenus of viruses in the genus Betacoronavirus.The viruses in this subgenus were previously known as group 2c coronaviruses. Wikipedia:Merbecovirus NCBITaxon:2509511 GC_ID:1 Sarbecovirus NCBITaxon:2559587 RNA viruses RNA viruses and viroids Riboviria NCBITaxon:2759 PMID:23020233 eucaryotes eukaryotes Eukaryota NCBITaxon:33154 Opisthokonta NCBITaxon:33213 Bilateria NCBITaxon:40674 http://purl.bioontology.org/ontology/STY/T015 mammal mammals mammalia NCBITaxon:6239 Caenorhabditis elegans NCBITaxon:694002 NCBITaxon:156439 GC_ID:1 Coronavirus Coronavirus group 2 Group 2 species Betacoronavirus NCBITaxon:694009 Severe acute respiratory syndrome–related coronavirus (SARS-CoV or SARSr-CoV) is a species of coronavirus that infects humans, bats and certain other mammals. Severe acute respiratory syndrome–related coronavirus (SARS-CoV or SARSr-CoV) is a species of coronavirus that infects humans, bats and certain other mammals. HCoV-SARS SARS SARSr-CoV Human coronavirus (strain SARS) SARS coronavirus SARS virus SARS-like coronavirus SARS-related coronavirus Severe acute respiratory syndrome coronavirus Severe acute respiratory syndrome-related coronavirus Severe acute respiratory syndrome–related coronavirus (SARS-CoV or SARSr-CoV) is a species of coronavirus that infects humans, bats and certain other mammals. Wikipedia:Severe_acute_respiratory_syndrome–related_coronavirus NCBITaxon:7227 Drosophila melanogaster NCBITaxon:76804 GC_ID:1 Nidovirales NCBITaxon:7742 Vertebrata vertebrates vertebrate NCBITaxon:9606 http://purl.bioontology.org/ontology/STY/T016 human homo sapiens NCBITaxon:9989 rodent rodentia NCIT:C1029 A synthetic amino acid. Buthionine sulfoximine irreversibly inhibits gamma-glutamylcysteine synthase, thereby depleting cells of glutathione, a metabolite that plays a critical role in protecting cells against oxidative stress, and resulting in free radical-induced apoptosis. Elevated glutathione levels are associated with tumor cell resistance to alkylating agents and platinum compounds. By depleting cells of glutathione, this agent may enhance the in vitro and in vivo cytotoxicities of various chemotherapeutic agents in drug-resistant tumors. Buthionine sulfoximine may also exhibit antiangiogenesis activity. (NCI04) BSO Buthionine sulfoximine NCIT:C116387 Non-neoplastic macrophages that are found in close proximity to or within a tumor mass. [ NCI ] CD163-positive cells TAM tumor-associated macrophage NCIT:C121992 A protein family comprised of chromo and chromo shadow domain-containing, methyl-lysine binding proteins that are localized to heterochromatin. These proteins are involved in gene silencing, transcriptional activation, and the formation and stabilization of heterochromatin. HP1 Heterochromatin Protein 1 NCIT:C15632 The use of synthetic or naturally-occurring chemicals for the treatment of diseases. Chemotherapy NCIT:C16407 http://jglobal.jst.go.jp/en/detail?JGLOBAL_ID=200906081082476489 http://purl.bioontology.org/ontology/MESH/D002470 cell survival NCIT:C16507 Drug-, radiation-induced, or spontaneous injuries to DNA that introduce deviations from its normal double-helical conformation. These changes include structural distortions that interfere with replication and transcription, as well as point mutations that disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. If the damage is minor, it can often be repaired (DNA repair); extensive damage can induce apoptosis. MeSH:D004249 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C16507 DNA damage NCIT:C16672 A constellation of responses that occur when an organism is exposed to excessive heat and other environmental stresses. Responses include synthesis of some proteins, repression of other proteins, and expression of new proteins. (From Segen, Dictionary of Modern Medicine, 1992) Heat-Shock Response NCIT:C16702 A chemical reaction that uses water to break down a compound. hydrolysis NCIT:C16936 Any chemical, biological or physical agents that increase the risk of neoplasms in humans or animals. Carcinogens include natural or synthesized compounds, certain viruses, and various sources of radiation. A carcinogen may directly alter the genetic material of cells (genotoxic), thereby initiating or promoting the process of malignant transformation; it also may induce cancers by mechanisms that do not involve a direct alteration of cellular genetic material (non-genotoxic). Oncogene NCIT:C174109 A post-translationally modified form of histone H3 where the lysine residue at position 9 is trimethylated. This modification is associated with heterochromatin formation and plays a role in embryonic stem cell lineage commitment and maintenance of lineage fidelity. H3K9me3 Histone H3 Trimethyl Lys9 Histone H3 Trimethyl Lys9 NCIT:C17609 A pathologic process in which alterations at the molecular level result in a more aggressive cytologic and phenotypic profile and clinical course of a neoplasm. Wikipedia:Tumor_progression tumor progression Wikipedia:Tumor_progression Tumor progression is the third and last phase in tumor development.[1] This phase is characterised by increased growth speed and invasiveness of the tumor cells. As a result of the progression, phenotypical changes occur and the tumor becomes more aggressive and acquires greater malignant potential. Together with the progression, more and more aneuploidy occurs. This may be evident as nuclear polymorphism. NCIT:C18078 A pathological process in which normal cells are transformed into malignant cancer cells within a primary tumor. http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C18078 ncit:C18078 Carcinogenesis carcinogenesis NCIT:C18121 A pathologic process that involves the transformation of normal cells to a neoplastic state and resulting in polyclonal or monoclonal neoplastic cell proliferation. A pathologic process that involves the transformation of normal cells to a neoplastic state and resulting in polyclonal or monoclonal neoplastic cell proliferation. http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C18121 ncit:C18121 Oncogenesis tumorigenesis NCIT:C186726 A reduction in muscle mass and function that is associated with aging or disuse. Sarcopenia NCIT:C18909 Any DNA sequence alteration process occurring in a proto-oncogene, resulting in loss of regulation of the gene product, and predisposing the cell to neoplastic transformation. Proto-oncogenes are ordinarilly involved in transduction of signals that regulate cell growth and differentiation. Activation of such genes overrides the normal mechanisms of regulation and is an important step in the process of cellular transformation. oncogene activation NCIT:C19098 The second step in two-stage carcinogenesis: the conversion of an initiated (premalignant) cell to malignancy. Wikipedia:Tumor_promotion tumor promotion NCIT:C19151 The spread or migration of cancer cells from one part of the body (the organ in which it first appeared) to another. The secondary tumor contains cells that are like those in the original (primary) tumor. metastasis NCIT:C19427 The processes which result in cancers in the liver. http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C19427 ncit:C19427 liver carcinogenesis hepatocarcinogenesis NCIT:C20325 Members of this family of high mobility group (HMG) proteins participate in a wide variety of nuclear processes ranging from chromosome and chromatin mechanics to acting as architectural transcription factors that regulate the expression of numerous genes. As a consequence, they function in the cell as highly connected nodes of protein-DNA and protein-protein interactions that influence a diverse array of normal biological processes including growth, proliferation, differentiation and death. Each protein contains three copies of the AT-hook, that preferentially binds to the minor groove of stretches of AT-rich sequence. HMGA genes are bona fide proto-oncogenes that promote tumor progression and metastasis when overexpressed. High constitutive HMGA protein levels are among the most consistent feature observed in all types of cancers with increasing concentrations being correlated with increasing malignancy. HMGA is a family of high mobility group proteins characterized by an AT-hook. They code for a "small, nonhistone, chromatin-associated protein that has no intrinsic transcriptional activity but can modulate transcription by altering the chromatin architecture".[1] Mammals have two orthologs: HMGA1 and HMGA2. HMGA is a family of high mobility group proteins characterized by an AT-hook. They code for a "small, nonhistone, chromatin-associated protein that has no intrinsic transcriptional activity but can modulate transcription by altering the chromatin architecture".[1] Mammals have two orthologs: HMGA1 and HMGA2. Wikipedia:HMGA high mobility group AT-hook protein HMGA HMGA is a family of high mobility group proteins characterized by an AT-hook. They code for a "small, nonhistone, chromatin-associated protein that has no intrinsic transcriptional activity but can modulate transcription by altering the chromatin architecture".[1] Mammals have two orthologs: HMGA1 and HMGA2. Wikipedia:HMGA NCIT:C20613 Multiplication or reproduction by cell division of a population of identical cells descended from a single progenitor. In immunology, may refer to the clonal proliferation of cells responsive to a specific antigen as part of an immune response. (NCI) http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C20613 clonal expansion NCIT:C3340 A usually exophytic mass attached to the underlying tissue by a broad base or a thin stalk. Polyps can be neoplastic or non-neoplastic. Neoplastic polyps usually represent proliferations of the epithelium, and are commonly seen in the gastrointestinal tract. Polyps of the gastrointestinal tract are often called adenomas, are associated with dysplasia, and may eventually transform into carcinomas. Non-neoplastic polyps may be inflammatory, degenerative, or the result of malformations. polyp NCIT:C347 Any chemical, biological or physical agents that increase the risk of neoplasms in humans or animals. Carcinogens include natural or synthesized compounds, certain viruses, and various sources of radiation. A carcinogen may directly alter the genetic material of cells (genotoxic), thereby initiating or promoting the process of malignant transformation; it also may induce cancers by mechanisms that do not involve a direct alteration of cellular genetic material (non-genotoxic). Carcinogen NCIT:C49508 The level of degree is high in comparison to medium. high level NCIT:C50678 Obstruction or a closure of hollow organ, passageway or vessel; also the transient approximation of the edges of a natural opening; imperforation. The act of closure or the state of being closed; an obstruction; the relationship between all of the components of the masticatory system in normal function, dysfunction, and parafunction; momentary complete closure of some area in the vocal tract, causing stoppage of the breath and accumulation of pressure. http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C50678 occlusion NCIT:C50773 Tissue damage is a subtype of damaging: A process that injures the structure of the tissue as the direct or indirect result of an external force. tissue damage NCIT:C54214 A set or series of interactions, often forming a network, which biologists have found useful to group together for organizational, historic, biophysical, or other reasons. pathway NCIT:C83001 A blood vessel located in the following sites: upper extremities, lower extremities, lower abdomen, head, or neck. Peripheral Blood Vessel NCIT:C90808 C23H26N6O2 InChI=1S/C23H26N6O2/c1-18-5-4-6-19(15-18)17-25-28-21-16-22(29-10-13-30-14-11-29)27-23(26-21)31-12-8-20-7-2-3-9-24-20/h2-7,9,15-17H,8,10-14H2,1H3,(H,26,27,28)/b25-17+ HSKAZIJJKRAJAV-KOEQRZSOSA-N CC1=CC(=CC=C1)C=NNC2=CC(=NC(=N2)OCCC3=CC=CC=N3)N4CCOCC4 CAS:541550-19-0 PMID:32221306 PubChem:10173277 STA 5326 STA-5326 apilimod mesylate Apilimod PMID:32221306 Inhibition of PIKfyve by apilimod significantly reduced entry of SARS-CoV S pseudovirions on 293/hACE2 cells in a dose dependent manner (Fig. 3b), whereas it had no effect on entry of VSV-G pseudovirions, which occurs in early endosomes. As expected, apilimod treatment inhibited entry of SARS-CoV-2 S pseudovirions in a dose dependent manner (Fig. 3d). OBI:0000010 fluorescent reporter intensity A measurement datum that represents the output of a scanner measuring the intensity value for each fluorescent reporter. person:Chris Stoeckert group:OBI From the DT branch: This term and definition were originally submitted by the community to our branch, but we thought they best fit DENRIE. However we see several issues with this. First of all the name 'probe' might not be used in OBI. Instead we have a 'reporter' role. Also, albeit the term 'probe intensity' is often used in communities such as the microarray one, the name 'probe' is ambiguous (some use it to refer to what's on the array, some use it to refer to what's hybed to the array). Furthermore, this concept could possibly be encompassed by combining different OBI terms, such as the roles of analyte, detector and reporter (you need something hybed to a probe on the array to get an intensity) and maybe a more general term for 'measuring intensities'. We need to find the right balance between what is consistent with OBI and combinations of its terms and what is user-friendly. Finally, note that 'intensity' is already in the OBI .owl file and is also in PATO. Why didn't OBI import it from PATO? This might be a problem. fluorescent reporter intensity OBI:0000011 A processual entity that realizes a plan which is the concretization of a plan specification. planned process OBI:0000015 biological feature identification objective Biological_feature_identification_objective is an objective role carried out by the proposition defining the aim of a study designed to examine or characterize a particular biological feature. Jennifer Fostel biological feature identification objective OBI:0000017 a role which inheres in material entities and is realized in the processes of making, enforcing or being defined by legislation or orders issued by a governmental body. OBI, CDISC Regulatory agency, Ethics committee, Approval letter; example: Browse these EPA Regulatory Role subtopics http://www.epa.gov/ebtpages/enviregulatoryrole.html Feb 29, 2008 govt agents responsible for creating regulations; proxies for enforcing regulations. CDISC definition: regulatory authorities. Bodies having the power to regulate. NOTE: In the ICH GCP guideline the term includes the authorities that review submitted clinical data and those that conduct inspections. These bodies are sometimes referred to as competent regulatory role OBI:0000025 reference substance role Calibration standard, positive control substance, vehicle Good Laboratory Practices: Questions and Answers - Test Control and Reference Substance Characterization http://www.epa.gov/enforcement/monitoring/programs/fifra/glpqanda-character.html a role inhering in a material entity that is realized when characteristics or responses elicited by the substance are used for comparison or reference. Person:Jennifer Fostel reference substance OBI reference substance role OBI:0000047 processed material Examples include gel matrices, filter paper, parafilm and buffer solutions, mass spectrometer, tissue samples Is a material entity that is created or changed during material processing. PERSON: Alan Ruttenberg processed material OBI:0000064 positive reference substance role MMS mutagen a reference role in which the characteristics or responses elicited by the substance playing the reference substance role are used to establish a "100%" response Person: Jennifer Fostel positive reference substance positive reference substance role OBI:0000067 evaluant role When a specimen of blood is assayed for glucose concentration, the blood has the evaluant role. When measuring the mass of a mouse, the evaluant is the mouse. When measuring the time of DNA replication, the evaluant is the DNA. When measuring the intensity of light on a surface, the evaluant is the light source. a role that inheres in a material entity that is realized in an assay in which data is generated about the bearer of the evaluant role Role call - 17nov-08: JF and MC think an evaluant role is always specified input of a process. Even in the case where we have an assay taking blood as evaluant and outputting blood, the blood is not the specified output at the end of the assay (the concentration of glucose in the blood is) examples of features that could be described in an evaluant: quality.... e.g. "contains 10 pg/ml IL2", or "no glucose detected") GROUP: Role Branch OBI Feb 10, 2009. changes after discussion at OBI Consortium Workshop Feb 2-6, 2009. accepted as core term. evaluant role OBI:0000070 A planned process with the objective to produce information about the material entity that is the evaluant, by physically examining it or its proxies. scientific observation assay OBI:0000079 culture medium A growth medium or culture medium is a substance in which microorganisms or cells can grow. Wikipedia, growth medium, Feb 29, 2008 a processed material that provides the needed nourishment for microorganisms or cells grown in vitro. changed from a role to a processed material based on on Aug 22, 2011 dev call. Details see the tracker item: http://sourceforge.net/tracker/?func=detail&aid=3325270&group_id=177891&atid=886178 Modification made by JZ. Person: Jennifer Fostel, Jie Zheng OBI culture medium OBI:0000086 reagent role Buffer, dye, a catalyst, a solvating agent. A role inhering in a biological or chemical entity that is intended to be applied in a scientific technique to participate (or have molecular components that participate) in a chemical reaction that facilitates the generation of data about some entity distinct from the bearer, or the generation of some specified material output distinct from the bearer. PERSON:Matthew Brush reagent PERSON:Matthew Brush Feb 10, 2009. changes after discussion at OBI Consortium Workshop Feb 2-6, 2009. accepted as core term. May 28 2013. Updated definition taken from ReO based on discussions initiated in Philly 2011 workshop. Former defnition described a narrower view of reagents in chemistry that restricts bearers of the role to be chemical entities ("a role played by a molecular entity used to produce a chemical reaction to detect, measure, or produce other substances"). Updated definition allows for broader view of reagents in the domain of biomedical research to include larger materials that have parts that participate chemically in a molecular reaction or interaction. (copied from ReO) Reagents are distinguished from instruments or devices that also participate in scientific techniques by the fact that reagents are chemical or biological in nature and necessarily participate in or have parts that participate in some chemical interaction or reaction during their intended participation in some technique. By contrast, instruments do not participate in a chemical reaction/interaction during the technique. Reagents are distinguished from study subjects/evaluants in that study subjects and evaluants are that about which conclusions are drawn and knowledge is sought in an investigation - while reagents, by definition, are not. It should be noted, however, that reagent and study subject/evaluant roles can be borne by instances of the same type of material entity - but a given instance will realize only one of these roles in the execution of a given assay or technique. For example, taq polymerase can bear a reagent role or an evaluant role. In a DNA sequencing assay aimed at generating sequence data about some plasmid, the reagent role of the taq polymerase is realized. In an assay to evaluate the quality of the taq polymerase itself, the evaluant/study subject role of the taq is realized, but not the reagent role since the taq is the subject about which data is generated. In regard to the statement that reagents are 'distinct' from the specified outputs of a technique, note that a reagent may be incorporated into a material output of a technique, as long as the IDENTITY of this output is distinct from that of the bearer of the reagent role. For example, dNTPs input into a PCR are reagents that become part of the material output of this technique, but this output has a new identity (ie that of a 'nucleic acid molecule') that is distinct from the identity of the dNTPs that comprise it. Similarly, a biotin molecule input into a cell labeling technique are reagents that become part of the specified output, but the identity of the output is that of some modified cell specimen which shares identity with the input unmodified cell specimen, and not with the biotin label. Thus, we see that an important criteria of 'reagent-ness' is that it is a facilitator, and not the primary focus of an investigation or material processing technique (ie not the specified subject/evaluant about which knowledge is sought, or the specified output material of the technique). reagent role OBI:0000093 a role which inheres in a person and is realized by the process of being under the care of a physician or health care provider OBI, CDISC CDISC definition: patient. Person under a physician's care for a particular disease or condition. NOTE: A subject in a clinical trial is not necessarily a patient, but a patient in a clinical trial is a subject. See also subject, trial subject, healthy volunteer. Often used interchangeably patient role OBI:0000094 material processing A cell lysis, production of a cloning vector, creating a buffer. A planned process which results in physical changes in a specified input material PERSON: Bjoern Peters PERSON: Frank Gibson PERSON: Jennifer Fostel PERSON: Melanie Courtot PERSON: Philippe Rocca Serra material transformation OBI branch derived material processing OBI:0000101 measured expression level Examples are quantified data from an expression microarray experiment, PCR measurements, etc. A measurement datum that is the outcome of the quantification of an assay for the activity of a gene, or the number of RNA transcripts. person:Chris Stoeckert OBI Data Transformation branch measured expression level OBI:0000112 specimen role liver section; a portion of a culture of cells; a nemotode or other animal once no longer a subject (generally killed); portion of blood from a patient. a role borne by a material entity that is gained during a specimen collection process and that can be realized by use of the specimen in an investigation 22Jun09. The definition includes whole organisms, and can include a human. The link between specimen role and study subject role has been removed. A specimen taken as part of a case study is not considered to be a population representative, while a specimen taken as representing a population, e.g. person taken from a cohort, blood specimen taken from an animal) would be considered a population representative and would also bear material sample role. Note: definition is in specimen creation objective which is defined as an objective to obtain and store a material entity for potential use as an input during an investigation. blood taken from animal: animal continues in study, whereas blood has role specimen. something taken from study subject, leaves the study and becomes the specimen. parasite example - when parasite in people we study people, people are subjects and parasites are specimen - when parasite extracted, they become subject in the following study specimen can later be subject. GROUP: Role Branch OBI specimen role OBI:0000113 sequence feature identification objective Sequence_feature_identification_objective is a biological_feature_identification_objective role describing a study designed to examine or characterize molecular features exhibited at the level of a macromolecular sequence, e.g. nucleic acid, protein, polysaccharide. Jennifer Fostel sequence feature identification objective OBI:0000118 gene list Gene lists may arise from analysis to determine differentially expressed genes, may be collected from the literature for involvement in a particular process or pathway (e.g., inflammation), or may be the input for gene set enrichment analysis. A data set of the names or identifiers of genes that are the outcome of an analysis or have been put together for the purpose of an analysis. person:Chris Stoeckert group:OBI kind of report. (alan) need to be careful to distinguish from output of a data transformation or calculation. A gene list is a report when it is published as such? Relates to question of whether report is a whole, or whether it can be a part of some other narrative object. gene list OBI:0000131 molecular feature identification objective Molecular_feature_identification_objective is a biological_feature_identification_objective role describing a study designed to examine or characterize molecular features of a biological system, e.g. expression profiling, copy number of molecular components, epigenetic modifications. Jennifer Fostel molecular feature identification objective OBI:0000164 cDNA library PMID:6110205. collection of cDNA derived from mouse splenocytes. Mixed population of cDNAs (complementaryDNA) made from mRNA from a defined source, usually a specific cell type. This term should be associated only to nucleic acid interactors not to their proteins product. For instance in 2h screening use living cells (MI:0349) as sample process. ALT DEF (PRS):: a cDNA library is a collection of host cells, typically E.Coli cells but not exclusively. modified by transfer of plasmid DNA molecule used as vector containing a fragment or totality of cDNA molecule (the insert) . cDNA library may have an array of role and applications. PERSON: Luisa Montecchi PERSON: Philippe Rocca-Serra GROUP: PSI PRS: 22022008. class moved under population, modification of definition and replacement of biomaterials in previous definition with 'material' addition of has_role restriction clonal cDNA library OBI:0000185 An imaging assay is an assay to produce a picture of an entity. imaging assay OBI:00001975 chromatin immunoprecipitation Yang et al, Int J Clin Exp Pathol. 2015; 8(3): 2746–275 PMID:26045780. Cells were lysed and sonicated to shear DNA to lengths between 200-1000 bp. The sample was then incubated with antibodies against Acety-H3 to immunoprecipitate protein-DNA complexes using protein A agarose beads. The isolated protein-DNA complexes were treated with proteinase K digestion to remove histones. QPCR was then performed using primers specific for TGF-β1, MMP-9 and PI3K promoters at 95°C for 5 min, followed by 40 cycles at 95 °C for 20 s, 58°C for 20 s, and 72°C for 20 s. Each QPCR reaction was repeated in triplicate. QPCR was followed by a melt curve analysis to determine the reaction specificity. The relative gene expression was calculated using 2-ΔΔCt method. An immunoprecipitation in which chromatin (i.e. packaged DNA which can include protein and RNA complexes) is cut into short regions, reversibly cross linked, and antibodies or tags are used to select for pieces of chromatin with desired characteristics. Bjoern Peters, Randi Vita, James A. Overton ChIP OBI chromatin immunoprecipitation OBI:0000231 enzymatic cleavage Polymorphism R62W results in resistance of CD23 to enzymatic cleavage in cultured cells. Genes Immun. 2007 Apr;8(3):215-23. Epub 2007 Feb 15. PMID: 17301828 a material processing that digests the fraction of input material that is susceptible to that enzyme PlanAndPlannedProcess Branch OBI branch derived enzymatic cleavage OBI:0000250 dye role A molecular label role which inheres in a material entity and which is realized in the process of detecting a molecular dye that imparts color to some material of interest. Jennifer Fostel dye A substance used to color materials www.answers.com/topic/dye 19feb09 dye role OBI:0000253 artificially induced nucleic acid hybridization www.ornl.gov/sci/techresources/Human_Genome/publicat/97pr/09gloss.html, http://www.accessexcellence.org/RC/VL/GG/nucleic.html, http://omrf.ouhsc.edu/~frank/HYBNOTES.html. http://en.wikipedia.org/wiki/Nucleic_acid_hybridization,http://www.pnas.org/cgi/reprint/46/8/1044.pdf Is a material transformation in which strands of nucleic acids that are (somewhat) complementary form a double-stranded molecule. Has input at least two single stranded molecules of nucleic acid molecules. PlanAndPlannedProcess Branch OBI branch derived artificially induced nucleic acid hybridization OBI:0000257 DNA extraction A DNA extraction is a nucleic acid extraction where the desired output material is DNA. PlanAndPlannedProcess Branch OBI branch derived DNA extraction OBI:0000274 adding a material entity into a target Injecting a drug into a mouse. Adding IL-2 to a cell culture. Adding NaCl into water. is a process with the objective to place a material entity bearing the 'material to be added role' into a material bearing the 'target of material addition role'. Class was renamed from 'administering substance', as this is commonly used only for additions into organisms. BP branch derived adding a material entity into a target OBI:0000275 A measurand role borne by a molecular entity or an atom and realized in an analyte assay which achieves the objective to measure the magnitude/concentration/amount of the analyte in the entity bearing evaluant role. analyte role OBI:0000291 transcription factor binding site assay Transcription factor binding site identification in yeast: a comparison of high-density oligonucleotide and PCR-based microarray platforms. An assay tthat determines DNA regions specifically recognized by proteins that function as transcription factors Philippe Rocca-Serra TF binding OBI https://sourceforge.net/p/obi/obi-terms/767/ transcription factor binding site assay OBI:0000319 material to be added role drug added to a buffer contained in a tube; substance injected into an animal; A role of a material entity that is realized in an "adding a material entity into a target" process where the bearer of the role is added into another material entity (the target). Role Branch OBI 9 March 09 from discussion with PA branch material to be added role OBI:0000341 histological sample preparation histological sample preparation is the preparation of an input tissue via slicing and labeling to make tissue microstructure of interest visible in a future histology assay PERSON:Bjoern Peters OBI branch derived histological sample preparation OBI:0000367 light emission function A light emission function is an excitation function to excite a material to a specific excitation state that it emits light. Bill Bug Daniel Schober Frank Gibson Melanie Courtot light emission function OBI:0000368 record function A record function is a function that registers or collects information in a particular format on a particular recording medium. For example on paper or a digital representation Bill Bug Daniel Schober Frank Gibson Melanie Courtot record function OBI:0000369 magnify function A magnify function is a function to increase the size of a transmitted object image through the precise arrangement of energy diffraction elements along an imaging path. Bill Bug Daniel Schober Frank Gibson Melanie Courtot magnify function OBI:0000370 contain function A syringe, a beaker A contain function is a function to constrain a material entities location in space Bill Bug Daniel Schober Frank Gibson Melanie Courtot contain function OBI:0000371 heat function A heat function is a function that increases the internal kinetic energy of a material Bill Bug Daniel Schober Frank Gibson Melanie Courtot heat function OBI:0000372 material separation function A material separation function is a function that increases the resolution between two or more material entities. The to distinction between the entities is usually based on some associated physical quality. Bill Bug Daniel Schober Frank Gibson Melanie Courtot material separation function OBI:0000374 excitation function A excitation function is a function to inject energy by bombarding a material with energetic particles (e.g., photons) thereby imbuing internal material components such as electrons with additional energy. These internal, 'excited' particles may lead to the rupturing of covalent chemical bonds or may quickly relax back to there unexcited state with an exponential time course thereby locally emitting energy in the form of photons. Bill Bug Daniel Schober Frank Gibson Melanie Courtot excitation function OBI:0000375 freeze function A freeze function is a function to decrease the internal kinetic energy of a material below the freezing point of that type of material. Bill Bug Daniel Schober Frank Gibson Melanie Courtot freeze function OBI:0000376 synthesizing function A synthesizing function is a function to assemble new output materials from distinct input materials. The output materials typically consist of chemically distinct monomeric objects or object aggregate polymers. Bill Bug Daniel Schober Frank Gibson Melanie Courtot synthesizing function OBI:0000377 perturb function A perturb function is a function that disrupts the normal function of a system induced through either internal or external means. External means of perturbation include: (1) displacement fields in the physical sense - e.g., temperature change, osmotic shock, pressure change; (2) application of small molecules such as drugs or toxins to perturb the function of specific pathways or application of surfactants to perturb the normal function of plasma membrane. Internal means of perturbation include: (1) manipulation of gene function via gene knockout or transcript knockdown via RNAi; (2) directed genetic mutation leading to minimal aa alterations that interfere with peptide function. Bill Bug Daniel Schober Frank Gibson Melanie Courtot http://en.wikipedia.org/wiki/Perturbation_biology perturb function OBI:0000379 mechanical function A mechanical function is a function that is realised via mechanical work (through an certain amount of energy transferred by some force). Bill Bug Daniel Schober Frank Gibson Melanie Courtot http://en.wikipedia.org/wiki/Mechanical_work mechanical function OBI:0000383 transfer function A transfer function is a function to displace a material from one location to another. Bill Bug Daniel Schober Frank Gibson Melanie Courtot transfer function OBI:0000387 cool function A cool function is a function to decrease the internal kinetic energy of a material below the initial kinetic energy of that type of material. Daniel Schober Frank Gibson Melanie Courtot cool function OBI:0000392 information processor function An information processor function is a function that converts information from one form to another, by a lossless process or an extraction process. Frank Gibson data processor function information processor function OBI:0000393 signal conversion function A signal conversion function is an information processor function which transforms a signal into another type of signal. For example an analog-to-digital_converter, Ac/Ac converter, a synapse converts electrical action potentials into an intermediate chemical signal. The post synapse converts it back into an electric one passed on to the axon. Bill Bug Daniel Schober Frank Gibson Melanie Courtot transduction function signal conversion function OBI:0000395 signal amplification function A signal amplification function is a signal conversion function to inject energy into an input signal so as to produce an output signal with increased differential magnitude while also seeking to minimize increases in the signal to noise ratio. For example, to produce a 0.1 KW output signal from a 1 mW RMS input signal. Bill Bug Daniel Schober Frank Gibson Melanie Courtot signal amplification function OBI:0000397 image acquisition function An image acquisition function is a function to acquire an image of a material Frank Gibson image acquisition function OBI:0000398 image acquisition device An image creation device is a device which captures a digitized image of an object Frank Gibson image acquisition device sep:00096 image creation device OBI:0000400 display function A display function is a function to present information by translating that information through some lookup process into visual form. Bill Bug Daniel Schober Frank Gibson Melanie Courtot display function OBI:0000405 primer role a complementary nucleotide probe role which inheres in nucleic acid molecular entity and is realized by the use of the entity bearing the role to initiate chain elongation. (cell and molecular biology) A short strand of RNA that is synthesized along single-stranded DNA during replication, initiating DNA polymerase-catalyzed synthesis of the complementary strand. http://www.answers.com/topic/rna-primer primer role OBI:0000406 PCR product PCR products are the results of amplifcation process. Detection of a PCR products is used to detect DNA and RNA. is double stranded DNA that is the specified output of a polymerase chain reaction We are using PCR and not the written out words, as this is the most common used. GROUP: OBI BIomaterial Branch GROUP: OBI BIomaterial Branch PCR product OBI:0000409 nucleic acid template role a model or standard for making comparisons; wordnet.princeton.edu/perl/webwn 19 feb 2009 a reference substance role which inheres in nucleic acid material entity and is realized in the process of using the nucleic acid bearing the template role as a reference during synthesis of a reverse copy. nucleic acid template role OBI:0000410 recombinant plasmid a plasmid in which extraneous DNA has been inserted. PERSON: Bjoern Peters PERSON: Kevin Clancy PERSON: Melanie Courtot GROUP: OBI Biomaterial Branch recombinant plasmid OBI:0000411 cloning vector role pBluescript plays the role of a cloning vector A material to be added role played by a small, self-replicating DNA or RNA molecule - usually a plasmid or chromosome - and realized in a process whereby foreign DNA or RNA is inserted into the vector during the process of cloning. JZ: related tracker: https://sourceforge.net/p/obi/obi-terms/102/ PERSON: Helen Parkinson cloning vector role OBI:0000415 polymerase chain reaction Opisthorchis viverrini: Detection by polymerase chain reaction (PCR) in human stool samples. Exp Parasitol. 2008 Sep 9. PMID: 18805413 PCR is the process in which a DNA polymerase is used to amplify a piece of DNA by in vitro enzymatic replication. As PCR progresses, the DNA thus generated is itself used as a template for replication. This sets in motion a chain reaction in which the DNA template is exponentially amplified. OBI Plan PCR adapted from wikipedai polymerase chain reaction OBI:0000416 cloning insert role cloning insert role is a role which inheres in DNA or RNA and is realized by the process of being inserted into a cloning vector in a cloning process. Feb 20, 2009. from Wikipedia: cloning of any DNA fragment essentially involves four steps: DNA fragmentation with restriction endonucleases, ligation of DNA fragments to a vector, transfection, and screening/selection. There are multiple processes involved, it is not just "cloning process" GROUP: Role branch OBII and Wikipedia cloning insert role OBI:0000419 reverse transcriptase enzyme and has_function some GO:0003964 (RNA-directed DNA polymerase activity) person:Melanie Courtot group:OBI reverse transcriptase OBI:0000423 extract Up-regulation of inflammatory signalings by areca nut extract and role of cyclooxygenase-2 -1195G>a polymorphism reveal risk of oral cancer. Cancer Res. 2008 Oct 15;68(20):8489-98. PMID: 18922923 an extract is a material entity which results from an extraction process PERSON: Philippe Rocca-Serra extracted material GROUP: OBI Biomatrial Branch extract OBI:0000427 enzyme (protein or rna) or has_part (protein or rna) and has_function some GO:0003824 (catalytic activity) MC: known issue: enzyme doesn't classify under material entity for now as it isn't stated that anything that has_part some material entity is a material entity. If we add as equivalent classes to material entity has_part some material entity and part_of some material entity (each one in his own necessary and sufficient block) Pellet in P3 doesn't classify any more. person: Melanie Courtot GROUP:OBI enzyme OBI:0000430 plasmid plasmid = DNA and has_quality circular and has_function (is_realized_as some gene expression) GO:0010467 person:Melanie Courtot group:OBI plasmid OBI:0000432 polyacrylamide gel Assessing CMT cell line stability by two dimensional polyacrylamide gel electrophoresis and mass spectrometry based proteome analysis. J Proteomics. 2008 Jul 21;71(2):160-7. PMID: 18617143 a material entity resulting from the polymerization of acrylamide with TEMED in some buffer solution PERSON: Jie Zheng PERSON: Philippe Rocca-Serra GROUP: OBI Biomaterial Branch polyacrylamide gel OBI:0000434 adding material objective creating a mouse infected with LCM virus is the specification of an objective to add a material into a target material. The adding is asymmetric in the sense that the target material largely retains its identity BP adding material objective OBI:0000437 analyte measurement objective The objective to measure the concentration of glucose in a blood sample an assay objective to determine the presence or concentration of an analyte in the evaluant PERSON: Bjoern Peters PPPB branch analyte measurement objective OBI:0000439 agarose gel Performance comparison of capillary and agarose gel electrophoresis for the identification and characterization of monoclonal immunoglobulins. Am J Clin Pathol. 2008 Mar;129(3):451-8. PMID: 18285269 a material entity resulting from the polymerization of agarose after heating agarose suspended in some buffer solution PERSON: Philippe Rocca-Serra GROUP: OBI Biomaterial Branch agarose gel OBI:0000441 assay objective the objective to determine the weight of a mouse. an objective specification to determine a specified type of information about an evaluated entity (the material entity bearing evaluant role) PPPB branch PPPB branch assay objective OBI:0000444 target of material addition role peritoneum of an animal receiving an interperitoneal injection; solution in a tube receiving additional material; location of absorbed material following a dermal application. A role of a material entity that is realized in an "adding a material entity into a target" process where the bearer of the role (the target) receives the addition of another material entity. From Branch discussion with BP, AR, MC -- there is a need for the recipient to interact with the administered material. for example, a tooth receiving a filling was not considered to be a target role. GROUP: Role Branch OBI target of material addition role OBI:0000445 mass measurement assay The patients was weighed and mass was determined to be 47 kilograms An assay that determines the mass of an evaluant Helen Parkinson OBI mass measurement assay OBI:0000453 measure function A glucometer measures blood glucose concentration, the glucometer has a measure function. Measure function is a function that is borne by a processed material and realized in a process in which information about some entity is expressed relative to some reference. PERSON: Daniel Schober PERSON: Helen Parkinson PERSON: Melanie Courtot PERSON:Frank Gibson measure function OBI:0000455 consume data function Process data function is a function that is borne by in a material entity by virtue of its structure. When realized the material entity consumes data. PERSON: Daniel Schober PERSON: Frank Gibson PERSON: Melanie Courtot consume data function OBI:0000456 material transformation objective The objective to create a mouse infected with LCM virus. The objective to create a defined solution of PBS. an objective specifiction that creates an specific output object from input materials. PERSON: Bjoern Peters PERSON: Frank Gibson PERSON: Jennifer Fostel PERSON: Melanie Courtot PERSON: Philippe Rocca-Serra artifact creation objective GROUP: OBI PlanAndPlannedProcess Branch material transformation objective OBI:0000512 isolation of cell population removing CD4+ cells from PBMCs using magnetic beads. a process in which a population of cells with certain characteristics is isolated from a larger population Person: Bjoern Peters isolation of cell population OBI:0000552 reverse transcribed polymerase chain reaction Harmonisation of multi-centre real-time reverse-transcribed PCR results of a candidate prognostic marker in breast cancer: an EU-FP6 supported study of members of the EORTC - PathoBiology Group. Span PN, Sieuwerts AM, Heuvel JJ, Spyratos F, Duffy MJ, Eppenberger-Castori S, Vacher S, O'Brien K, McKiernan E, Pierce A, Vuaroqueaux V, Foekens JA, Sweep FC, Martens JW. Eur J Cancer. 2009 Jan;45(1):74-81. PMID: 19008094 reverse transcribe pcr is a process which allow amplification of cDNA during a pcr reaction while the cDNA results from a retrotranscription of messenger RNA isolated from a material entity. 3/21/10, BP:Modified definition to clarify that this is not the assay, but the material transformation Philippe Rocca-Serra RT-PCR reverse transcription polymerase chain reaction reverse transcribed polymerase chain reaction OBI:0000576 scattered molecular aggregate the sodium and chloride ions in a glass of salt water a material entity that consists of all the molecules of a specific type that are located in some bounded region and which is part of a more massive material entity that has parts that are other such aggregates PERSON: Alan Ruttenberg Collective Discussion in Karslruhe with, among others, Alan Rector, Stefan Schulz, Marijke Keet, Melanie Courtot, and Alan Ruttenberg. With inspiration from the paper Granularity, scale and collectivity: When size does and does not matter, Alan Recto, Jeremy Rogers, Thomas Bittner, Journal of Biomedical Informatics 39 (2006) 333-349 scattered molecular aggregate OBI:0000626 DNA sequencing assay Illumina (Solexa) sequencing is an example of DNA sequencing A sequencing assay which determines information on the sequence of a DNA molecule. Philippe Rocca-Serra nucleotide sequencing url:https://en.wikipedia.org/wiki/DNA_sequencing DNA sequencing assay OBI:0000634 DNA methylation profiling assay Genome-wide, high-resolution DNA methylation profiling using bisulfite-mediated cytosine conversion. Reinders J, Delucinge Vivier C, Theiler G, Chollet D, Descombes P, Paszkowski J._PMID:18218979 An assay that measures the state of methylation of DNA molecules using genomic DNA collected from a material entity using a range of techniques and instrument such as DNA sequencers and often relying on treatment with bisulfites to ensure cytosine conversion. Philippe Rocca-Serra DNA methylation profiling OBI branch derived DNA methylation profiling assay OBI:0000639 material separation objective The objective to obtain multiple aliquots of an enzyme preparation. The objective to obtain cells contained in a sample of blood. is an objective to transform a material entity into spatially separated components. PPPB branch PPPB branch material separation objective OBI:0000652 material combination Mixing two fluids. Adding salt into water. Injecting a mouse with PBS. is a material processing with the objective to combine two or more material entities as input into a single material entity as output. created at workshop as parent class for 'adding material into target', which is asymmetric, while combination encompasses all addition processes. bp bp material combination OBI:0000659 specimen collection process drawing blood from a patient for analysis, collecting a piece of a plant for depositing in a herbarium, buying meat from a butcher in order to measure its protein content in an investigation A planned process with the objective of collecting a specimen. Note: definition is in specimen creation objective which is defined as an objective to obtain and store a material entity for potential use as an input during an investigation. Philly2013: A specimen collection can have as part a material entity acquisition, such as ordering from a bank. The distinction is that specimen collection necessarily involves the creation of a specimen role. However ordering cell lines cells from ATCC for use in an investigation is NOT a specimen collection, because the cell lines already have a specimen role. Philly2013: The specimen_role for the specimen is created during the specimen collection process. label changed to 'specimen collection process' on 10/27/2014, details see tracker: http://sourceforge.net/p/obi/obi-terms/716/ Bjoern Peters specimen collection 5/31/2012: This process is not necessarily an acquisition, as specimens may be collected from materials already in posession 6/9/09: used at workshop specimen collection process OBI:0000671 sample from organism a material obtained from an organism in order to be a representative of the whole 5/29: This is a helper class for now we need to work on this: Is taking a urine sample a material separation process? If not, we will need to specify what 'taking a sample from organism' entails. We can argue that the objective to obtain a urine sample from a patient is enough to call it a material separation process, but it could dilute what material separation was supposed to be about. sample from organism OBI:0000678 portioning objective The objective to obtain multiple aliquots of an enzyme preparation. A material separation objective aiming to separate material into multiple portions, each of which contains a similar composition of the input material. portioning objective OBI:0000681 separation into different composition objective The objective to obtain cells contained in a sample of blood. A material separation objective aiming to separate a material entity that has parts of different types, and end with at least one output that is a material with parts of fewer types (modulo impurities). We should be using has the grain relations or concentrations to distinguish the portioning and other sub-objectives separation into different composition objective OBI:0000684 specimen collection objective The objective to collect bits of excrement in the rainforest. The objective to obtain a blood sample from a patient. A objective specification to obtain a material entity for potential use as an input during an investigation. Bjoern Peters Bjoern Peters specimen collection objective OBI:0000685 creating a mixture of molecules in solution The production of PBS is a process with the objective to prepare a liquid solution of one or more chemicals at desired concentrations. Bjoern Peters PERSON: Helen Parkinson creating a mixture of molecules in solution OBI:0000686 material combination objective is an objective to obtain an output material that contains several input materials. PPPB branch bp material combination objective OBI:0000687 nucleotide overhang cloning Cloning vectors are commercially available and supplied in linearized form with 3' dT overhangs Nucleotide overhang cloning is the process of inserting nucleic acid into a vector using nucleotide overhangs used to prevent self ligation Helen Parkinson nucleotide overhang cloning OBI:0000690 immunoprecipitation PMID: 19419533. Arabidopsis RNA immunoprecipitation. Terzi LC, Simpson GG. Plant J. 2009 Jul;59(1):163-8. is a process which realizes a material separation objective by relying on antibodies to specifically binding to material entity Philippe Rocca-Serra OBI plan and planned process branch immunoprecipitation OBI:0000692 recombination enzyme based cloning a recombination enzyme based cloning is a recombinant vector cloning process that uses complementary nucleotide sequences in both the insert genetic material and the cloning vector with a recombination enzyme to directly create a recombinant vector recombination enzyme based cloning OBI:0000709 yeast artificial chromosome vector a double-stranded DNA that was engineered to contain a yeast origin of replication, encodes for a selectable gene product, contains a cloning site, and has yeast telomerase sequences this should be a child of 'chromosome' if we import that from another source Kevin Clancy, Bjoern Peters YAC yeast artificial chromosome vector OBI:0000711 library preparation PMID: 19570239. Construction and analysis of cotton (Gossypium arboreum L.) drought-related cDNA library. Zhang L, Li FG, Liu CL, Zhang CJ, Zhang XY. BMC Res Notes. 2009 Jul 2;2:120. is a process which results in the creation of a library from fragments of DNA using cloning vectors or oligonucleotides with the role of adaptors. Philippe Rocca-Serra library construction library preparation OBI:0000716 ChIP-seq assay PMID: 19275939 An assay in which chromatin is immunoprecipitated and subsequently analyzed using a DNA sequencing step to identify which parts of DNA are part of the isolated chromatin Bjoern Peters Philippe Rocca-Serra chromatin immunoprecipitation sequencing assay url:https://en.wikipedia.org/wiki/ChIP-sequencing ChIP-seq assay OBI:0000718 pathogen role is a role which inheres in an organism and realized in the process of disease course in the organism bearing host role caused by the organism bearing pathogen role OBI pathogen role OBI:0000722 paired-end library PMID: 19339662. Next-generation DNA sequencing of paired-end tags (PET) for transcriptome and genome analyses. Genome Res. 2009 Apr;19(4):521-32. Fullwood MJ, Wei CL, Liu ET, Ruan Y. is a collection of short paired tags from the two ends of DNA fragments are extracted and covalently linked as ditag constructs Philippe Rocca-Serra mate-paired library paired-end tag (PET) library adapted from information provided by Solid web site paired-end library OBI:0000725 host role is a role played by an organism and realized by providing nourishment, shelter or a means of reproduction to another organism within the organism playing the host role host role OBI:0000729 cloning plasmid A cloning plasmid is a plasmid that was engineered to contain a bacterial origin of replication, encodes for a selectable gene product and contains a cloning site. Note: 'cloning vector role' is really a function. Should be dealt with globally cloning plasmid OBI:0000731 recombinant vector A recombinant vector is created by a recombinant vector cloning process, and contains nucleic acids that can be amplified. It retains functions of the original cloning vector. recombinant vector OBI:0000732 restriction enzyme The enzyme EcoR1 cuts DNA at the canonical cleavage site CAATTG an enzyme that has a specific target cleavage sites within nucleic acids Kevin Clancy, Bjoern Peters 5/22 Need to explore if there are GO / other classes exist that capture this. We need it now for cloning experiments restriction enzyme OBI:0000736 single fragment library is a collection of short tags from DNA fragments, are extracted and covalently linked as single tag constructs Philippe Rocca-Serra fragment library single fragment library OBI:0000737 cloning vector A cloning vector is an engineered material that is used as an input material for a recombinant vector cloning process to carry inserted nucleic acids. It contains an origin of replication for a specific destination host organism, encodes for a selectable gene product and contains a cloning site. cloning vector OBI:0000738 restriction enzyme based cloning restriction enzyme based cloning is a recombinant vector cloning process that has as an input genetic material that was cleaved with restriction enzymes, and a cloning vector that was cleaved with complementary restriction enzymes. It uses ligase to chemically join the input genetic material and the cloning vector to create a recombinant vector. Kevin Clancy, Bjoern Peters restriction enzyme based cloning OBI:0000740 material sample role a role borne by a portion of blood taken to represent all the blood in an organism; the role borne by a population of humans with HIV enrolled in a study taken to represent patients with HIV in general. A material sample role is a specimen role borne by a material entity that is the output of a material sampling process. 7/13/09: Note that this is a relational role: between the sample taken and the 'sampled' material of which the sample is thought to be representative off. material sample role OBI:0000742 nucleic acid restriction enzyme digest A nucleic acid digest is a material that is the output of a process in which nucleic acids are combined with a restriction enzyme resulting in digested fragments with defined ends based on the enzymes cleavage site Kevin Clancy, Bjoern Peters nucleic acid restriction enzyme digest OBI:0000744 material sampling process A specimen gathering process with the objective to obtain a specimen that is representative of the input material entity sample collection sampling https://github.com/obi-ontology/obi/issues/1002 material sampling process OBI:0000747 material sample blood drawn from patient to measure his systemic glucose level. A population of humans with HIV enrolled in a study taken to represent patients with HIV in general. A material entity that has the material sample role OBI: workshop sample population sample material sample OBI:0000748 bisulfite sequencing assay PMID: 19581485. High definition profiling of mammalian DNA methylation by array capture and single molecule bisulfite sequencing. Hodges E, Smith A, Kendall J, Xuan Z, Ravi K, Rooks M, Zhang M, Ye K, Battacharjee A, Brizuela L, McCombie WR, Wigler M, Hannon GJ, Hicks J. A DNA methylation profiling assay which determines the methylation status of genomic DNA using DNA sequencing techniques preceded by a bisulfite based chemical modification of genomic DNA at CpG island location. Philippe Rocca-Serra Sagar Jain url:https://en.wikipedia.org/wiki/Bisulfite_sequencing bisulfite sequencing assay OBI:0000790 recombinant BAC cloning Recombinant BAC cloning is a process with the objective to insert genetic material into an F plasmid based bacterial artificial chromosome for future replication of the inserted material http://en.wikipedia.org/wiki/Bacterial_artificial_chromosome recombinant BAC cloning OBI:0000799 recombinant phage cloning Insert selection by BamHI methyltransferase protection in P1 phage-based cloning Recombinant phage cloning is the process of using a phage plus some insert nucleic acid for the purposes of amplification of the insert material achieved by phage assembly in vitro. Helen Parkinson http://www.ncbi.nlm.nih.gov/books/bv.fcgi?rid=mcb.section.1611 recombinant phage cloning OBI:0000800 cross linking cross linking can be used as a probe to link proteins together, to check protein protein interactions A process in which bonds are created that link one polymer to another PERSON: Chris Stoeckert http://en.wikipedia.org/wiki/Cross-link cross linking OBI:0000806 material maintenance objective An objective specification maintains some or all of the qualities of a material over time. PERSON: Bjoern Peters PERSON: Bjoern Peters material maintenance objective OBI:0000809 amplified DNA Amplied DNA created by PCR DNA that has been produced in an enzymatic amplification process PERSON: Alan Ruttenberg Alan Ruttenberg amplified DNA OBI:0000811 primary structure of DNA macromolecule a quality of a DNA molecule that inheres in its bearer due to the order of its DNA nucleotide residues. placeholder for SO BP et al primary structure of DNA macromolecule OBI:0000824 recombinant YAC cloning Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21 Recombinant YAC cloning is a process with the objective to insert genetic material into a yeast artificial chromosome vector for future replication of the inserted material Helen Parkinson http://www.ncbi.nlm.nih.gov/books/bv.fcgi?rid=mcb.section.1611 recombinant YAC cloning OBI:0000832 measurement device A ruler, a microarray scanner, a Geiger counter. A device in which a measure function inheres. GROUP:OBI Philly workshop OBI measurement device OBI:0000834 high molecular weight DNA extract Extraction of chromosomal DNA from mammalian cells by first isolating nucei The output of an extraction process in which DNA molecules above a molecular weight cutoff are purified in order to exclude DNA from organellas. PERSON:Chris Stoeckert OBI high molecular weight DNA extract OBI:0000838 material maintenance a process with that achieves the objective to maintain some or all of the characteristics of an input material over time material maintenance OBI:0000839 labeled oligonucleotide a labeled oligonucleotide is a short nucleic acid which underwent a labeling process resulting in a radioactive isotope such as P32 or P33 added to its backbone for instance by end labeling with polynucleotide kinase which added radiolabeled ATP to the 5' end of oligonucleotide 2010-01-31: Philippe Rocca-Serra placeholder Person: Philippe Rocca-Serra labeled oligonucleotide OBI:0000845 primary structure of RNA molecule The primary structure of an RNA molecule that is completely defined by the set of its nucleic residue parts and the linear order induced by the peptide bonds that hold them together Person:Bjoern Peters primary structure of RNA molecule OBI:0000849 organellar RNA extraction A RNA extraction process in which the desired output material is RNA in the organelle(s). Person: Chris Stoeckert Person: Jie Zheng UPenn Group organellar RNA extraction OBI:0000855 total RNA extraction A RNA extraction process in which total cellular and organelle RNA are extracted. Person: Chris Stoeckert Person: Jie Zheng UPenn Group total RNA extraction OBI:0000857 complementary nucleotide probe role A primer in a PCR reaction. A probe on an Affymetrix chip. A role played by a nucleic acid molecule that is used in a planned process for its ability to bind a nucleic acid molecules with complementary nucleotide sequence PERSON:Bjoern Peters complementary nucleotide probe role OBI:0000859 cytoplasmic RNA extraction A RNA extraction process in which the desired output material is RNA in the cytoplasm. Person: Chris Stoeckert Person: Jie Zheng UPenn Group cytoplasmic RNA extraction OBI:0000862 nuclear RNA extract Isolation and purification of nuclear RNA from animal cells using Norgen Bioteck corp. cytoplasmic and nuclear RNA purification kit (http://www.norgenbiotek.com/display-product.php?ID=30) A RNA extract that is the output of an extraction process in which RNA molecules found in the nucleus, including mRNA precursors (pre-mRNA), are extracted. PERSON: Chris Stoeckert PERSON: Jie Zheng UPenn Group nuclear RNA extract OBI:0000867 establishing cancer cell line Establishment of HeLa immortal cell line is a planned process in which the objective is to generate a cell line from a natural population of cancer cells which are already immortal Helen Parkinson establishing cancer cell line OBI:0000873 pre-mortem specimen material obtained through a liver biopsy from a human patient a specimen that was taken from a live organism Bjoern Peters MO_705 premortem pre-mortem specimen OBI:0000876 cytoplasmic RNA extract Cytoplasmic RNA extraction from mammalian tissues to create cDNA library (Carninci P, Nakamura M, Sato K, Hayashizaki Y, Brownstein MJ. Cytoplasmic RNA extraction from fresh and frozen mammalian tissues. Biotechniques. 2002;33:306–309.) A RNA extract that is the output of a RNA extraction process in which RNA molecules found in the cytoplasm are extracted. PERSON: Chris Stoeckert PERSON: Jie Zheng UPenn Group cytoplasmic RNA extract OBI:0000877 cell line immortalization Production of a cell line for the purposes of experimentation e.g. EBV transformation of PBMs an establishing cell line process whereby a mortal cell line is intentionally genetically modified to be capable of indefinite propagation and re-established as a new immortal cell line 4-20-13 MHB: This class was repositioned as a child of 'establishing cell line', based on the existing definition ("the planned process of experimentally creating a cell line which is capable of dividing indefinitely in vitro"), and examples and other annotations indicating the intent to describe a process through which a new immortal cell line is established from an existing mortal cell line using genetic modification techniques. The definition above was modified to clarify this perspective. Bjoern Peters 'establishing immortal cell line through directed genetic modification' OBI A immortalizing genetic transformation of an existing population of cell line cells is required as part of this process, as are additional steps for selecting and propagating the cells output form this process into a cell line. cell line immortalization OBI:0000879 random primed DNA labeling PMID: 8713846. Random primed 32P-labeling of DNA. Smith DR. Methods Mol Biol. 1996;58:27-9. a labeling in which random primers are used to uniformly label input DNA need to add Klenow subunit of DNA polymerase I under material entity Person: Bjoern Peters Person: Chris Stoeckert Person: Philippe Rocca-Serra PMID: 6312838. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Feinberg AP, Vogelstein B. Anal Biochem. 1983 Jul 1;132(1):6-13. random primed DNA labeling OBI:0000880 RNA extract an extract which is the output of an extraction process in which RNA molecules are isolated from a specimen. PERSON: Chris Stoeckert PERSON: Jie Zheng Group: UPenn Group RNA extract OBI:0000888 nuclear RNA extraction A RNA extraction process in which the desired output material is RNA in the nucleus. Person: Chris Stoeckert Person: Jie Zheng UPenn Group nuclear RNA extraction OBI:0000893 real time polymerase chain reaction assay An assay, based on the PCR, that amplifies and simultaneously quantifies a specific DNA molecule based on the use of complementary probes/primers. It enables both detection and quantification (as absolute number of copies or relative amount when normalized to DNA input or additional normalizing genes) of one or more specific sequences in a DNA sample. Bjoern Peters Melanie Courtot Q-PCR kinetic polymerase chain reaction qPCR quantitative real time polymerase chain reaction url:http://en.wikipedia.org/wiki/Real-time_polymerase_chain_reaction real time polymerase chain reaction assay OBI:0000894 protein extract PMID: 20032479. A bovine whey protein extract stimulates human neutrophils to generate bioactive IL-1Ra through a NF-kappaB- and MAPK-dependent mechanism. Rusu D, Drouin R, Pouliot Y, Gauthier S, Poubelle PE. J Nutr. 2010 Feb;140(2):382-91. Epub 2009 Dec 23. a protein extract is the output of an extraction process from tissues or cell cultures resulting in a solution of cellular and/or organellar proteins in buffer solution used to prevent degradation, Person: Philippe Rocca-Serra OBI & wikipedia protein extract OBI:0000895 total RNA extract Extraction of total RNA from cells with Qiagen mini RNeasy kit. A RNA extract that is the output of an extraction process in which total celluar and organelle RNA molecules are isolated from a specimen. PERSON: Chris Stoeckert PERSON: Jie Zheng UPenn Group total RNA extract OBI:0000899 organellar RNA extract Extraction of organellar RNA from plant cells using organellar RNA binding protein. A RNA extract that is the output of an extraction process in which RNA molecules found in an organelle, e.g., mitochondrion, ER, or chloroplast, excluding the nucleus, are extracted. PERSON: Chris Stoeckert PERSON: Jie Zheng UPenn Group organellar RNA extract OBI:0000902 post mortem specimen the spleen taken from a dead mouse a specimen that was taken from a dead organism Bjoern Peters MO_416 postmortem post mortem specimen OBI:0000908 labeled DNA extract a labeled specimen that is the output of a labeling process and has grain labeled DNA to be able to detect DNA in future experiments. Need to find out if we consider labeled nucleotides still nucleotides. It is after consulting with ChEBI group. Added duirng Mar 1, 2010 dev call Group: OBI group Group: OBI group labeled DNA extract OBI:0000911 real time reverse-transcription polymerase chain reaction assay An assay that uses a reverse transcription step (an RNA strand is reverse transcribed into its DNA complement using the enzyme reverse transcriptase) before a PCR assay. Bjoern Peters Melanie Courtot RRT-PCR RT-rt PCR qRT-PCR real time reverse-transcription polymerase chain reaction assay OBI:0000921 labeled RNA extract a labeled specimen that is the output of a labeling process and has grain labeled RNA to be able to detect RNA in future experiments. Need to find out if we consider labeled nucleotides still nucleotides. It is after consulting with ChEBI group. Added duirng Mar 1, 2010 dev call Group: OBI group Group: OBI group labeled RNA extract OBI:0000924 labeled specimen A specimen that has been modified in order to be able to detect it in future experiments added during call 3/1/2010 OBI group labeled specimen OBI:0000932 material separation device flow cytometer A device with a separation function realized in a planed process material separation device OBI:0000933 positron emission tomography scanner A device that produces a three-dimensional image or picture of functional processes in the body. It detects pairs of gamma rays emitted indirectly by a positron-emitting radionuclide (tracer), which is introduced into the body on a biologically active molecule. PERSON:Bjoern Peters PET scanner? http://en.wikipedia.org/wiki/Positron_emission_tomography positron emission tomography scanner OBI:0000940 optical microscope A microscope that produces an image of an object by targeting it with an electro-magnetic beam in the visible frequency range PERSON:Bjoern Peters optical microscope OBI:0000946 sterilization function a function to remove viable organisms from an input material sterilization function OBI:0000953 processed specimen A tissue sample that has been sliced and stained for a histology study. A blood specimen that has been centrifuged to obtain the white blood cells. A specimen that has been intentionally physically modified. Bjoern Peters Bjoern Peters A tissue sample that has been sliced and stained for a histology study. processed specimen OBI:0000960 reagent application function An automatic tissue processor automatically applies antibodies and buffers to histological tissue preparations. A function that is realized when a reagent is automatically added to some research material. PERSON: Nicole Vasilevsky, Matthew Brush PERSON: Nicole Vasilevsky, Matthew Brush 4/10/2011: It is unclear if we need / want this, or what this is supposed to be for. Lots of the functions we have are reagent specific. Will this only confuse people? reagent application function OBI:0000961 addition of molecular tracer function Immunohistochemical labeling of tissue sections by an autostainer staining system. A reagent application function that is realized when a molecular tracer, such as an antibody or probe is automatically transferred to a biological specimen. PERSON: Nicole Vasilevsky, Matthew Brush PERSON: Nicole Vasilevsky, Matthew Brush addition of molecular tracer function OBI:0000968 device A voltmeter is a measurement device which is intended to perform some measure function. An autoclave is a device that sterlizes instruments or contaminated waste by applying high temperature and pressure. A material entity that is designed to perform a function in a scientific investigation, but is not a reagent. 2012-12-17 JAO: In common lab usage, there is a distinction made between devices and reagents that is difficult to model. Therefore we have chosen to specifically exclude reagents from the definition of "device", and are enumerating the types of roles that a reagent can perform. 2013-6-5 MHB: The following clarifications are outcomes of the May 2013 Philly Workshop. Reagents are distinguished from devices that also participate in scientific techniques by the fact that reagents are chemical or biological in nature and necessarily participate in some chemical interaction or reaction during the realization of their experimental role. By contrast, devices do not participate in such chemical reactions/interactions. Note that there are cases where devices use reagent components during their operation, where the reagent-device distinction is less clear. For example: (1) An HPLC machine is considered a device, but has a column that holds a stationary phase resin as an operational component. This resin qualifies as a device if it participates purely in size exclusion, but bears a reagent role that is realized in the running of a column if it interacts electrostatically or chemically with the evaluant. The container the resin is in (“the column”) considered alone is a device. So the entire column as well as the entire HPLC machine are devices that have a reagent as an operating part. (2) A pH meter is a device, but its electrode component bears a reagent role in virtue of its interacting directly with the evaluant in execution of an assay. (3) A gel running box is a device that has a metallic lead as a component that participates in a chemical reaction with the running buffer when a charge is passed through it. This metallic lead is considered to have a reagent role as a component of this device realized in the running of a gel. In the examples above, a reagent is an operational component of a device, but the device itself does not realize a reagent role (as bearing a reagent role is not transitive across the part_of relation). In this way, the asserted disjointness between a reagent and device holds, as both roles are never realized in the same bearer during execution of an assay. PERSON: Helen Parkinson instrument OBI development call 2012-12-17. device OBI:0000973 sequence data example of usage: the representation of a nucleotide sequence in FASTA format used for a sequence similarity search. A measurement datum that representing the primary structure of a macromolecule(it's sequence) sometimes associated with an indicator of confidence of that measurement. Person:Chris Stoeckert GROUP: OBI sequence data OBI:0000982 computed tomography scanner An image acquisition device that generates a three-dimensional image of the inside of an object from a large series of two-dimensional X-ray images taken around a single axis of rotation. PERSON:Bjoern Peters CT scanner X-ray computed tomography scanner http://en.wikipedia.org/wiki/X-ray_computed_tomography computed tomography scanner OBI:0000990 electron microscope A microscope that produces an image of an object by targeting it with an electron beam electron microscope OBI:0000995 administration of material to specimen Staining cells in a tissue slice with a dye. The directed combination of a material entity with a specimen. Bjoern Peters Bjoern Peters administration of material to specimen OBI:0001007 image acquisition Taking a polaroid picture of a patients skin lesion; Using a digital camera to take a picture of a gel A planned process that captures an image of an object. PERSON: Jie Zheng image acquisition image creation OBI:0001010 nucleic acid extract An extract that is the output of an extraction process in which nucleic acid molecules are isolated from a specimen. PERSON: Jie Zheng UPenn Group nucleic acid extract OBI:0001036 specimen fixation function e.g the function of a bar code reader used to read slide bar codes a function that allows specific identification of individual speciment from one another. EAGLE-I specimen fixation function OBI:0001041 stabilization function A stabilization function is a function that holds or isolates an entity such as an instrument or specimen steadfast or at an unfluctuating level or quantity. EAGLE-I isolation function stabilization function OBI:0001051 DNA extract The output of an extraction process in which DNA molecules are purified in order to exclude DNA from organellas. Person: Jie Zheng Group: UPenn group DNA extract OBI:0001055 spinning-disk confocal microscope A confocal microscope that uses a Nipkow disk, a mechanical, geometrically operating image scanning device. PERSON: Erik Segerdell http://en.wikipedia.org/wiki/Nipkow_disk spinning-disk confocal microscope OBI:0001065 stereo microscope An optical microscope that uses two separate optical paths with two objectives and two eyepieces to provide slightly different viewing angles to the left and right eyes. PERSON: Erik Segerdell http://en.wikipedia.org/wiki/Optical_microscope#Stereo_microscope stereo microscope OBI:0001068 SPECT scanner A nuclear medicine tomographic imaging device that uses gamma rays to provide 3D information, typically presented as cross-sectional slices through the specimen but with the ability to be freely reformatted or manipulated as required. PERSON: Erik Segerdell http://en.wikipedia.org/wiki/Single_photon_emission_computed_tomography SPECT scanner OBI:0001071 programmable array microscope A confocal microscope that uses a programmable spatial light modulator for generating an arbitrary pattern of conjugate illumination and detection apertures. PERSON: Erik Segerdell Verveer et al, Journal of Microscopy, vol. 189, pt. 3, pp. 192-8 programmable array microscope OBI:0001079 confocal microscope A microscope that is used to increase micrograph contrast and/or reconstruct three-dimensional images by using a spatial pinhole to eliminate out-of-focus light in specimens that are thicker than the focal plane. PERSON: Erik Segerdell http://en.wikipedia.org/wiki/Confocal_microscopy confocal microscope OBI:0001096 laser capture microdissection microscope A microscope that uses low-energy laser beams and special transfer film to lift single cells from a tissue. PERSON: Erik Segerdell http://www.answers.com/topic/laser-capture-microdissection-microscope-in-medicine laser capture microdissection microscope OBI:0001099 immunoblot scanner A device that is used for the imaging of immunoblots. PERSON: Erik Segerdell PERSON: Erik Segerdell immunoblot scanner OBI:0001105 scanning force microscope A microscope that forms images of surfaces using a physical probe that scans the specimen. PERSON: Erik Segerdell http://en.wikipedia.org/wiki/Scanning_probe_microscopy scanning force microscope OBI:0001108 nucleic acid sequencer An device that is used to determine the order of nucleotides in nucleic acid sequences. PERSON: Erik Segerdell PERSON: Erik Segerdell nucleic acid sequencer OBI:0001125 laser scanning confocal microscope A confocal microscope that obtains high-resolution optical images with depth selectivity, in which a laser beam passes through a light source aperture and then is focused by an objective lens into a small (ideally diffraction limited) focal volume within or on the surface of a specimen. PERSON: Erik Segerdell http://en.wikipedia.org/wiki/Confocal_laser_scanning_microscopy laser scanning confocal microscope OBI:0001126 digital microscope A microscope that uses optics and a charge-coupled device (CCD) camera to output a digital image to a monitor. PERSON: Erik Segerdell http://en.wikipedia.org/wiki/Digital_microscope digital microscope OBI:0001137 protein sequencer An device that is used to determine the order of amino acids in protein sequences. PERSON: Erik Segerdell PERSON: Erik Segerdell protein sequencer OBI:0001143 labeled nucleic acid extract a labeled specimen that is the output of a labeling process and has grain labeled nucleic acid for detection of the nucleic acid in future experiments. Person: Jie Zheng labeled extract MO_221 labeledExtract labeled extract labeled nucleic acid extract OBI:0001146 binding assay Determination of KD value for an antibody binding a protein using a BIACORE assay. Using plate bound antigen in an ELISA to determine if a mixture of serum antibodies bind the antigen. The following are NOT binding assays, as the desired output is not binding data: RNA microarray experiments to determine levels of gene expression. ChIP experiments to determine where in DNA a transcription factor binds. Using an IL-2 antibody on an ELISA plate to determine presence of IL-2 after stimulating a T cell culture. An assay with the objective to characterize the disposition of two or more material entities to form a complex. Bjoern Peters Jason Greenbaum Randi Vita binding assay OBI:0001147 cell culture expansion a process that results in the increase of cell numbers including grow of yeast and bacteria PERSON: Chris Stoeckert, Jie Zheng MO_758 grow BP: add it as subclass of 'cell culturing' JZ: No 'cell culturing' in OBI Has term 'cell co-culturing' and 'maintaining cell culture'. Don't think either of it fit. So leave the term under process. cell culture expansion OBI:0001148 gene knock out a genetic transformation that renders a gene non-functional, e.g. due to a point mutation, or the removal of all, or part of, the gene using recombinant methods. PERSON: Chris Stoeckert, Jie Zheng MO_771 gene_knock_out gene knock out OBI:0001149 gene knock in a genetic transformation that involves the insertion of a protein coding cDNA sequence at a particular locus in an organism's chromosome. Typically, this is done in mice since the technology for this process is more refined, and because mouse embryonic stem cells are easily manipulated. The difference between knock-in technology and transgenic technology is that a knock-in involves a gene inserted into a specific locus, and is a "targeted" insertion. PERSON: Chris Stoeckert, Jie Zheng MO_437 gene_knock_in WEB: http://en.wikipedia.org/wiki/Gene_Knock-in gene knock in OBI:0001150 chromosomal substitution A genetic transformation in which all, or part, of a chromosome from a donor replaces that of the recipient. It does not include chromosome recombination. For single gene insertion, use the term 'gene knock in'. PERSON: Chris Stoeckert, Jie Zheng MO_995 chromosomal_substitution chromosomal substitution OBI:0001151 genetically modified material a material entity, organism or cell, that is the output of a genetic transformation process. PERSON: Jie Zheng GROUP: OBI term is proposed by BP on Oct 25, 2010 dev call genetically modified material OBI:0001152 transfection a genetic transformation which relies on the use of physical, electrical and chemical phenomena to introduce DNA or RNA into a cell PERSON: Chris Stoeckert, Jie Zheng MO_366 transfection transfection OBI:0001153 genetic transformation objective a material transformation objective aims to create genetically modified organism or cell Person: Jie Zheng Person: Jie Zheng suggested to be added by BP and AR during Oct 25, 2010 dev call genetic transformation objective OBI:0001154 induced mutagenesis A genetic transformation that is the modification of the genetic material (either coding or non-coding) of an organism caused by mutagenic processes, compounds, or irradiation. Label and definition were clarified as per https://github.com/obi-ontology/obi/issues/1366 PERSON: Chris Stoeckert, Jie Zheng MO_564 induced_mutation induced mutagenesis OBI:0001170 reverse transcription polymerase chain reaction assay An assay that determines the concentration of RNA in a sample in which an RNA strand is first reverse transcribed into its DNA complement (complementary DNA, or cDNA) using the enzyme reverse transcriptase, and the resulting cDNA is amplified using traditional or real-time PCR. Chris Stoeckert Jie Zheng Penn Group reverse transcription polymerase chain reaction assay OBI:0001181 binding datum A data item that states if two or more material entities have the disposition to form a complex, and if so, how strong that disposition is. Bjoern Peters; Randi Vita binding datum OBI:0001234 epigenetic modification identification objective A molecular feature identification objective that aims to detect epigenetic modifications, such as DNA methylation, histone modifications. Chris Stoeckert, Jie Zheng Person: Chris Stoeckert epigenetic modification identification objective OBI:0001266 DNA methylation profiling by high throughput sequencing assay A DNA methylation profiling assay in which the methylation state of DNA is determined and can be compared between samples using sequencing based technology ArrayExpress production team Helen Parkinson James Malone EFO:0002761 DNA methylation profiling by high throughput sequencing assay OBI:0001331 transcription profiling identification objective A molecular feature identification objective that aims to characterize the abundance of transcripts Person: Chris Stoeckert, Jie Zheng Group: Penn Group transcription profiling identification objective OBI:0001398 protein and DNA interaction identification objective A sequence feature identification objective that aims to characterize the interactions between protein and DNA which includes identification of transcription factor binding sites. Person: Chris Stoeckert, Jie Zheng MO_933 binding_site_identification_design protein and DNA interaction identification objective OBI:0001479 specimen from organism A specimen that derives from an anatomical part or substance arising from an organism. Examples of tissue specimen include tissue, organ, physiological system, blood, or body location (arm). PERSON: Chris Stoeckert, Jie Zheng tissue specimen MO_954 organism_part specimen from organism OBI:0001483 cell collecting A planned process that collects cells from culture. PERSON: Chris Stoeckert, Jie Zheng MO_982 harvest cell collecting OBI:0001499 binding assay using fluorescence detection A binding assay that uses fluorescence detection as an indicator of binding. Bjoern Peters Randi Vita IEDB binding assay using fluorescence detection OBI:0001501 fluorescence detection assay Using a laser to stimulate a cell culture that was previously labeled with fluorescent antibodies to detect light emmission at a different wavelength in order to determine the presence of surface markers the antibodies are specific for. An assay in which a material's fluorescence is determined. IEDB IEDB fluorescence detection assay OBI:0001506 specimen with pre- or post-mortem status A specimen that has been established to be taken from a live (pre-mortem) or dead (post-mortem) organism. organizational term, used in description of specimen that is created from known pre- or post-mortem status PERSON: Chris Stoeckert, Jie Zheng MO_84 OrganismStatus specimen with pre- or post-mortem status OBI:0001508 sampling time measurement datum A time measurement datum when an observation is made or a sample is taken from a material as measured from some reference point. Person: Chris Stoeckert time point MO_738 timepoint sampling time measurement datum OBI:0001573 DNA sequence data The part of a FASTA file that contains the letters ACTGGGAA A sequence data item that is about the primary structure of DNA OBI call; Bjoern Peters OBI call; Melanie Courtout 8/29/11 call: This is added after a request from Melanie and Yu. They should review it further. This should be a child of 'sequence data', and as of the current definition will infer there. DNA sequence data OBI:0001588 binding A peptide binding to an MHC molecule to form a complex. The process of material entities forming complexes. 9/28/11 BP: The disposition referenced is the one of the ligand to bind the molecule. This along with binding as a function / process needs to be figured out with GO which is inconsistent at this point. PERSON: Bjoern Peters, Randi Vita IEDB binding OBI:0001619 specimen collection time measurement datum A time measurement datum that is the measure of the time when the specimens are collected. Person: Chris Stoeckert, Jie Zheng collection date NIAID GSCID-BRC metadata working group Specimen Collection Date NIAID GSCID-BRC specimen collection time measurement datum OBI:0001620 latitude coordinate measurement datum A measurement datum that is the measure of the latitude coordinate of a site. Person: Chris Stoeckert, Jie Zheng latitude NIAID GSCID-BRC metadata working group Specimen Collection Location - Latitude NIAID GSCID-BRC latitude coordinate measurement datum OBI:0001621 longitude coordinate measurement datum A measurement datum that is the measure of the longitude coordinate of a site. Person: Chris Stoeckert, Jie Zheng longitude NIAID GSCID-BRC metadata working group Specimen Collection Location - Longitude NIAID GSCID-BRC longitude coordinate measurement datum OBI:0001631 An imaging assay in which an electrons are used to probe the density, shape and composition of an input material which are detected in an electron microscope and utilized to produce an image of the material. electron microscopy imaging assay OBI:0001672 gene knock-down assay An assay which transiently disrupts gene transcripts by expressing antisense RNA constructs or delivering RNA interfering molecules in cells. Marcus Chibucos Philippe Rocca-Serra PMID:17430206 gene knock-down assay OBI:0001755 selection criterion rats should be aged between 6 and 8 weeks and weight between 180-250grams A directive information entity which defines and states a principle of standard by which selection process may take place. Person: Philippe Rocca-Serra selection rule OBI discussion summarized under the following tracker item : http://sourceforge.net/p/obi/obi-terms/678/ selection criterion OBI:0001852 paired-end library preparation A library preparation that results in the creation of a library of the 5' and 3' ends of DNA or cDNA fragments using adaptors and endonucleases. The preparation may or may not include cloning process. Person: Venkat Malladi, Jie Zheng Venkat Malladi, Jie Zheng ENCODE project paired-end library preparation OBI:0001854 protein and RNA interaction identification objective A sequence feature identification objective that aims to characterize the interactions between protein and RNA. JZ: Term added for ENCODE project requested assays. Definition adapted from 'protein and DNA interaction identification objective'. Person: Jie Zheng Jie Zheng protein and RNA interaction identification objective OBI:0001866 secondary cultured cell secondary cultured cell A cultured cell that has been passaged or derives from a cell that has been passaged in culture. A cultured cell that has been passaged or derives from a cell that has been passaged in culture. The term 'secondary cell culture' is generally used in biological texts/protocols to refer to any culture following an initial passage. We include it here because there are often a number of passages between a primary culture and the establishment of a stable, homogenous cell line. Such cultures are considered to be 'secondary cultures' but not 'cell lines' during this intermediate passaging/selection period between their derivation from a 'primary cell culture' and derivation into a 'cell line', which is a more specific type of secondary culture. Person: Matthew Brush Person: Matthew Brush PERSON: Matthew Brush A secondary cultured cell has been passaged in culture or is a descendant of such a cell that is derived through propagation in culture. A secondary cultured cell has been passaged in culture or is a descendant of such a cell that is derived through propagation in culture. secondary cultured cell secondary cultured cell OBI:0001867 establishing cell line a process whereby a new type of cell line is created, either through passaging of a primary cell culture to relative genetic stability and compositional homogeneity, or through some experimental modification of an existing cell line to produce a new line with novel characteristics (e.g. immortalization or some other stable genetic modification, or selection of some defined subset). 2013-4-20 MHB: For cases of initial establilshment of a line from a primary culture, successive passaging and/or selection processes can confer increasing degrees of genetic stability and compositional homogeneity as compared to the input primary culture. Historically, many texts consider the first passage as the clearest point to define the beginning of a line. However, in practice it is more often that case that more than one passage, and possibly additional selective techniques, may be required before a culture is deemed to have sufficient stability and homogeneity to be considered cell line. This is the view taken in OBI. Regardless, what is important is that some intentional, experimental step has been taken to establish a more homogenous and stable culture that can be characterized and progatated over time. Person: Matthew Brush PERSON:Matthew Brush establishing cell line OBI:0001876 cell culture A material entity comprised of cultured cells and the media in which they are being propagated or stored. PERSON:Matthew Brush OBI-CLO Alignment Working Group (Spring 2013) A cell culture includes the cells in culture, as well as the media and all additives in which the cells are being grown or in which they are stored. cell culture OBI:0001878 establishing primary cell culture Effects of establishing cell cultures and cell culture conditions on the proliferative life span of human fibroblasts isolated from different tissues and donors of different ages. Exp Cell Res. 2002 Apr 1;274(2):275-87. PMID: 11900488 When harvesting blood from a human, isolating T cells, and then limited dilution cloning of the cells, the establishing_cell_culture step comprises preparing the cells at a certain dilution and plating them in a container with growth medium. an establishing cell culture process whereby cells explanted directly from an organismal source or specimen, and placed in culture for maintenance or propagation as a primary cell culture PERSON: Matthew Brush Cells are originally plated at a certain concentration referred to as seeding density. Upon a first passage this primary culture becomes a secondary cell culture that can be propagated to become a stable and homogneous cell line. This class covers establishment of primary cultures from any native cell - 'in vivo' cells isolated from some multicellular organism, or 'in environment' unicellular organisms isolated from some natural environment. establishing primary cell culture OBI:0001879 reagent A biological or chemical entity that bears a reagent role in virtue of it being intended for application in a scientific technique to participate in (or have molecular parts that participate in) a chemical reaction that facilitates the generation of data about some distinct entity, or the generation of some distinct material specified output. 2013-6-5 MHB: Clarifications regarding the distinction between reagetns and devices were made at the May 2013 Philly Workshop. Reagents are distinguished from devices that also participate in scientific techniques by the fact that reagents are chemical or biological in nature and necessarily participate in some chemical interaction or reaction during the realization of their experimental role. By contrast, devices do not participate in such chemical reactions/interactions. Note that there are cases where devices use reagent components during their operation, where the reagent-device distinction is less clear. For examples, see editor note on OBI:device. PERSON:Matthew Brush PERSON:Matthew Brush (copied from ReO) Reagents are distinguished from devices/instruments that also serve as facilitators in scientific techniques by the fact that reagents are chemical or biological in nature and necessarily participate in or have parts that participate in some chemical interaction or reaction during their intended participation in some technique. By contrast, devices do not participate in a chemical reaction/interaction during the technique. Reagents are distinguished from study subjects/evaluants in that study subjects and evaluants are that about which conclusions are drawn and knowledge is sought in an investigation - while reagents, by definition, are not. It should be noted, however, that reagent and study subject/evaluant roles can be borne by instances of the same type of material entity - but a given instance can only realize one of these roles in the execution of a given assay. For example, taq polymerase can bear a reagent role or an evaluant role. In a DNA sequencing assay aimed at generating sequence data about some plasmid, the reagent role of the taq polymerase is realized. In an assay to evaluate the quality of the taq polymerase itself, the evaluant/study subject role of the taq is realized, but not the reagent role since the taq is the subject about which data is generated. In regard to the statement that reagents are 'distinct' from the specified outputs of a technique: note that a reagent may be incorporated into a material output of a technique, as long as the IDENTITY of this output is distinct from that of the bearer of the reagent role. For example, dNTPs input into a PCR are reagents that become part of the material output of this technique, but this output has a new identity (ie that of a 'nucleic acid molecule') that is distinct from the identity of the dNTPs that comprise it. Similarly, a biotin molecule input into a cell labeling technique are reagents that become part of the specified output, but the identity of the output is that of some modified cell specimen which shares identity with the input unmodified cell specimen, and not with the biotin label. Thus, we see that an important criteria of 'reagent-ness' is that it is a facilitator, and not the primary focus of an investigation or material processing technique (ie not the specified subject/evaluant about which knowledge is sought, or the specified output material of the technique). reagent OBI:0001905 secondary cultured cell population A cultured cell population that is derived through one or more passages in culture. The term 'secondary cell culture' is generally used in biological texts/protocols to refer to any culture of cells following an initial passage. We include it here because there are often a number of passages between a primary culture and the establishment of a stable, homogenous cell line. Such cultures are considered to be 'secondary cultures' but not 'cell lines' during this intermediate passaging/selection period between their derivation from a 'primary cell culture' and derivation into a 'cell line', which is a more specific type of secondary culture. PERSON:Matthew Brush secondary cell culture sample PERSON:Matthew Brush The concept of a 'secondary cultured cell population' covers cell lines as well as cultured cell populations more immediately derived from a primary culture which have yet to achieve adequate genetic stability and compositional homogeneity to be considered a cell line. The extent of the collection of cells in a 'secondary cultured cell population' is restricted only in that all cell members must share a propagation history (ie be derived through a common lineage of passages from an initial culture). Secondary cultured cell populations can be under active culture, stored in a quiescent state for future use, or applied experimentally. secondary cultured cell population OBI:0001906 cancer cell line An immortal cell line derived from a transformed cell that was part of a malignant tumor. cancer cell line OBI:0001907 immortalizing cell line transformation a genetic transformation of a cell line cell with transgenic constructs intended to confer the capability for indefinite propagation in culture immortalizing cell line transformation OBI:0001910 primary cell culture A cell culture comprised of primary cultured cells and the media in which they are being actively propaged or quiescently stored. PERSON:Matthew Brush OBI-CLO Alignment Working Group (Spring 2013) primary cell culture OBI:0001911 cell line culture A cell culture comprised of cell line cells and the media in which they are being actively propagated or quiescently stored. PERSON:Matthew Brush OBI-CLO Alignment Working Group (Spring 2013) A cell line culture includes the cells in culture, as well as the media and all additives/reagents in which the cells are being grown or in which they are stored. cell line culture OBI:0001912 cell freezing medium A processed material that serves as a liquid vehicle for freezing cells for long term quiescent stroage, which contains chemicls needed to sustain cell viability across freeze-thaw cycles. PERSON: Matthew Brush cell freezing medium OBI:0001914 multiplex ligation-mediated amplification A polymerase chain reaction that amplifies multiple targets with a single primer pair mediated by hybridization of a primer with its target sequence using ligation. Chris Stoeckert, Jie Zheng LMA MLPA Multiplex ligation-dependent probe amplification web: http://en.wikipedia.org/wiki/Multiplex_Ligation-dependent_Probe_Amplification Pubmed: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1867615/ multiplex ligation-mediated amplification OBI:0001916 DNA replication identification objective A molecular feature identification objective that aims to examine charateristics of DNA replication, such as replication time. Chris Stoeckert, Jie Zheng Group: Penn Group DNA replication identification objective OBI:0001917 chromosome conformation identification objective A molecular feature identification objective that aims to determine spatial organization of chromatin. Chris Stoeckert, Jie Zheng Group: Penn Group chromosome conformation identification objective OBI:0001925 chromatin immunoprecipitation with exonuclease sequencing assay Rhee et al. Comprehensive Genome-wide Protein-DNA Interactions Detected at Single-Nucleotide Resolution. Cell. 2011 Dec;147(6):1408-19. [PMID:22153082] A ChIP-seq assay which uses immunoprecipitation to isolate protein bound DNA followed by an exonuclease step to degrade DNA that is not protein bound to provide greater resolution of the DNA binding site Bjoern Peters Chris Stoeckert Jie Zheng Venkat Malladi ChIP-exo assay PMID:22153082 chromatin immunoprecipitation with exonuclease sequencing assay OBI:0001928 selection PMID: 24023800. In this study, a set of eleven genes (VATP16, 60 S, UQCC, SMD3, EF1α, UBQ, SAND, GAPDH, ACT, PsaB, PTB2) was evaluated to identify reference genes during the first hours of interaction (6, 12, 18 and 24 hpi) between two V. vinifera genotypes and P. viticola. Two analyses were used for the selection of reference genes: direct comparison of susceptible, Trincadeira, and resistant, Regent, V. vinifera cultivars at 0 h, 6, 12, 18 and 24 hours post inoculation with P. viticola (genotype effect); and comparison of each genotype with mock inoculated samples during inoculation time-course (biotic stress effect). Three statistical methods were used, GeNorm, NormFinder, and BestKeeper, allowing to identify UBQ, EF1α and GAPDH as the most stable genes for the genotype effect. A planned process which results in the creation of group of entity from a larger group by the application of predefined criteria. this term refers to a planned process and therefore is distinct from the notion of 'natural selection', a process covering the operation of natural causes by which those individuals of a species that are best adapted to the environment tend to be preserved and to transmit their characters, while those less adapted die out, so that in the course of generations the degree of adaptation to the environment tends progressively to increase. (as defined by Oxford English Dictionary) Person: Philippe Rocca-Serra selection process OBI selection 1 1 OBI:0001931 scalar value specification A value specification that consists of two parts: a numeral and a unit label PERSON:Bjoern Peters scalar value specification OBI:0001933 value specification The value of 'positive' in a classification scheme of "positive or negative"; the value of '20g' on the quantitative scale of mass. An information content entity that specifies a value within a classification scheme or on a quantitative scale. This term is currently a descendant of 'information content entity', which requires that it 'is about' something. A value specification of '20g' for a measurement data item of the mass of a particular mouse 'is about' the mass of that mouse. However there are cases where a value specification is not clearly about any particular. In the future we may change 'value specification' to remove the 'is about' requirement. PERSON:Bjoern Peters value specification OBI:0001936 molecular-labeled material a material entity that is the specified output of an addition of molecular label process that aims to label some molecular target to allow for its detection in a detection of molecular label assay PERSON:Matthew Brush OBI developer call, 3-12-12 molecular-labeled material OBI:0001946 forward PCR primer SP6 promoter, forward primer (SP6 TTTAGGTGACACTATAG) A short oligonucleotide complementary to target DNA (5'->3' on plus strand) that acts as the leader for DNA extension in a PCR reaction. The polymerase starts replication at the 3'-end of the primer, and copies the opposite strand. A primer is characterized by its 'melting temperature' (Tm) and pairs of primers should have similar Tm. Philippe Rocca-Serra 5' primer forward primer sense primer adapted from http://www.ncbi.nlm.nih.gov/projects/genome/probe/doc/Glossary.shtml#p forward PCR primer OBI:0001951 reverse PCR primer 5' end of luciferase, reverse primer (LucNrev CCTTATGCAGTTGCTCTCC) A short oligonucleotide complementary to target DNA (5'->3' on minus strand) that acts as the leader for DNA extension in a PCR reaction. The polymerase starts replication at the 3'-end of the primer, and copies the opposite strand. A primer is characterized by its 'melting temperature' (Tm) and pairs of primers should have similar Tm. Philippe Rocca-Serra 3' primer antisense primer reverse primer adapted from "http://www.ncbi.nlm.nih.gov/projects/genome/probe/doc/Glossary.shtml#p" reverse PCR primer OBI:0001954 ChIP assay PMID: 6379641 An assay in which portions of chromatin, the ordered and organized complex of DNA and its interaction partners that make up a chormosome, is extracted and purified by immunoprecipitation with antibodies or tags, and subsequently analyzed Bjoern Peters Philippe Rocca-Serra chromatin immunoprecipitation assay url:https://en.wikipedia.org/wiki/Chromatin_immunoprecipitation ChIP assay OBI:0001959 multiplexed nucleotide library sequencing http://www.illumina.com/technology/multiplexing_sequencing_assay.ilmn A planned process which consists in running a set of samples as a pool on a sequencing instrument, while retaining the ability to associate individual results to each of the individual input samples through the use of a ligated oligonucleotide (the "multiplex identifier sequence"). This oligonucleotide is introduced during the sequence library preparation, and is unique to and specific for all library fragments derived from each sample in a sample pool. Dan Berrios PERSON:Philippe Rocca-Serra OBI multiplexed nucleotide library sequencing OBI:0001967 multiplexing sequence identifier We designed primers specifically to amplify protease and reverse transcriptase from Brazilian HIV subtypes and developed a multiplexing scheme using multiplex identifier tags to minimize cost while providing more robust data than traditional genotyping techniques. in http://www.ncbi.nlm.nih.gov/pubmed/22574170 A multiplexing sequence identifier is a nucleic acid sequence which is used in a ligation step of library preparation process to allow pooling of samples while maintaining ability to identify individual source material and creation of a multiplexed library PERSON:Philippe Rocca-Serra OBI multiplexing sequence identifier OBI:0001970 multiplexed sequencing library http://www.ncbi.nlm.nih.gov/pubmed/24997861 Nat Methods. 2014 Aug;11(8):834-40. doi: 10.1038/nmeth.3022. Epub 2014 Jul 6. Accelerated chromatin biochemistry using DNA-barcoded nucleosome libraries. a multiplexed library is a material entity which is the output of a library preparation process that uses a ligation step to attach a unique multiplexing sequence identifier to a specific sample, then mixes several such tagged samples prior to the library amplification process proper. A multiplexed library allows the sequencing of several samples in one sequencing run. PERSON:Philippe Rocca-Serra DNA-barcoded sequencing library PRS for OBI multiplexed sequencing library OBI:0002017 histone modification identification by ChIP-Seq assay An epigenetic modification assay that identifies regions containing specific histones and their modifications using ChIP-Seq techniques. Chris Stoeckert Jie Zheng histone modification ChIP-Seq Penn group histone modification identification by ChIP-Seq assay OBI:0002019 transcription factor binding site identification by ChIP-Seq assay A transcription factor binding site assay that utilizes ChIP-seq technology. Chris Stoeckert Jie Zheng TF Binding ChIP-Seq Penn group transcription factor binding site identification by ChIP-Seq assay OBI:0002020 epigenetic modification assay An assay that identifies epigenetic modifications including histone modifications, open chromatin, and DNA methylation. Chris Stoeckert Jie Zheng Penn group epigenetic modification assay OBI:0002028 SAGE ditag library preparation A library preparation in which tags identifiying transcripts are created, ligated to form ditags, amplified, concatemerized and ligated into a vector to create a library. Related tracker:https://sourceforge.net/p/obi/obi-terms/720/ Person:Chris Stoeckert PMID:15905473 SAGE ditag library preparation OBI:0002078 specimen set collection process Collection of both blood and urine specimens in one clinical visit; Taking out liver and brain specimens during an autopsy. A specimen collection process that generates multiple specimens from one source (e.g. one organism) during a time period which for the purpose of the study can be considered to be taken at the same sampling time. Chris Stoeckert, Jie Zheng OBIB, OBI specimen set collection process OBI:0002084 transcription cofactor activity region identification by ChIP-Seq assay PMID 19212405: "we present the results of chromatin immunoprecipitation with the enhancer-associated protein p300 followed by massively parallel sequencing, and map several thousand in vivo binding sites of p300 in mouse embryonic forebrain, midbrain and limb tissue" A ChIP-seq assay that identifies regions of chromatin bound to a chromatin modifying protein, e.g. a histone acetyltransferase. Paul D. Thomas Yang Chai chromatin modifier binding site identification by ChIP-Seq assay PMID:19212405 https://github.com/obi-ontology/obi/issues/782 transcription cofactor activity region identification by ChIP-Seq assay OBI:0002087 containing a specimen function A contain function that involves physical contact with a specimen. This function is typically performed in such a way that the specimen is usable for an investigation or assay. For details see tracker item: http://sourceforge.net/p/obi/obi-terms/792/ Chris Stoeckert Duke Biobank, OBIB Biobank containing a specimen function OBI:0002118 exome sequencing assay DNA was extracted from the Ficoll pellet of blood taken from congenital asplenia patients. Unamplified, high-molecular weight, RNase-treated genomic DNA (4_6 _g) was used for whole exome sequencing (WES) with the use of Agilent 71 Mb (V4 + UTR) singlesample capture and an Illumina HiSeq 2000. Sequencing was carried out so as to obtain 30_ coverage from 2 _ 100-bp paired-end reads. We used the Annovar tool (25) to annotate the resulting highquality (HQ) variants. In the regions targeted by WES capture (81.5% of the consensus coding genome), the mean numbers of single-nucleotide variants (SNVs) and small insertions/deletions (indels) detected per sample were 84,192 and13,325, respectively. After filtering, a mean of 74,398 (95.3%) high-quality (HQ) SNVs and 9,033 (70.6%) HQ indels were called. A mean of 105 coding HQ SNVs and 32 indels was identified. A DNA sequencing assay that intends to provide information about the sequence of the protein coding components of a genome (exons). ImmPort WES PMID:25827230 exome sequencing assay OBI:0002119 microscopy assay Lung, liver, and spleen tissue samples were collected from female BALB/c mice and fixed in 100% formalin solution, embedded in paraffin, sectioned, and stained with hematoxylin and eosin. The stained samples were examined for signs of pathological changes under light microscopy. An imaging assay that utilizes a microscope to magnify features of the visualized material of interest that are not visible to naked eye. PMID:21685355 CHMO:0000067 http://www.ebi.ac.uk/efo/EFO_0002909 microscopy assay OBI:0002160 multiplexed indexed T7 ChIP-seq assay A ChIP-seq assay which leverages T7 promoter amplification to allow low sample input and chromatin barcoding and pool-and-split multiplexing for high-throughput, quantitative profiling of chromatin states. Chris Stoeckert Jason Hilton Mint-ChIP Mint-ChIP-seq url:http://www.cell.com/molecular-cell/abstract/S1097-2765(15)00863-1 https://github.com/obi-ontology/obi/issues/829 ENCODE DCC multiplexed indexed T7 ChIP-seq assay OBI:0002169 ChIP-qPCR assay A ChIP assay that uses quantitative PCR to determine levels of specific DNA in immunoprecipitated samples. Chris Stoeckert PMID:18388953 ChIP-qPCR assay OBI:0002461 BCL format A data format specification that is a binary file containing base calling data. These files are created by sequencing machines during the act of sequencing, and contain data about each of the nucleotide clusters on a sequencing flow cell. Stephen A. Fisher, Junhyong Kim, Dan Berrios BCL format OBI:0002580 aligned sequence data The results of a sequence alignment. Dan Berrios Dan Berrios aligned sequence data OBI:0002583 DNA methylation profiling data The results of a DNA methylation profiling assay DNA methylation profiling data OBI:0002598 inverse polymerase chain reaction A polymerase chain reaction which amplifies DNA with only one known sequence from which primers may be designed. A series of restriction digestions and ligations result in a looped DNA fragment which can be primed for PCR. Rebecca Tauber inverse PCR url:https://en.wikipedia.org/wiki/Chromosome_conformation_capture inverse polymerase chain reaction OBI:0002602 multiplexed sequence data Sequence data from a sequence library generated from at least two different sources, where each read in the sequence data includes base calls from a multiplex identifier sequence that can be used to trace the source of the read to its source. Dan Berrios Dan Berrios multiplexed sequence data OBI:0002619 site-directed mutagenesis Site-directed mutagenesis was used to prepare mutants of the Hypoxia-inducible factor-1 (HIF-1) alpha subunit to investigate the role of certain amino acids in hypoxia. (PMID:12393189) An induced mutation in which a specific base change is programmed into the sequence of a synthetic primer. Rebecca Jackson url:https://www.ncbi.nlm.nih.gov/books/NBK21945/ https://github.com/obi-ontology/obi/issues/1058 site-directed mutagenesis OBI:0002620 random mutagenesis Error-prone PCR was used to introduce amino acid mutations to the cAMP receptor protein (CRP) of E. coli to investigate strain engineering to improve osmotolerance for industrial requirements. (PMID:22179860) An induced mutation that produces a random mutation, either by introducing the organism to mutagens, or through a process such as error-prone PCR. Rebecca Jackson PMID:15153637 https://github.com/obi-ontology/obi/issues/1058 random mutagenesis OBI:0002623 whole metagenome sequencing assay A DNA sequencing assay that intends to provide information on the DNA sequences of multiple genomes (a metagenome) from different organisms present in the same input sample. Whole metagenome sequencing has been used to explore the composition and metabolic capability of communities of microbes found in the environment (e.g. in soil, water, etc.) and in humans and other species (e.g. in the gut, oral cavity, etc.). Rebecca Jackson WMS Bjoern Peters Michelle Giglio https://github.com/obi-ontology/obi/issues/1056 whole metagenome sequencing assay OBI:0002625 gene knockdown A genetic transformation which reduces the expression of a specific gene or genes in an organism. Rebecca Jackson gene knock-down url:https://en.wikipedia.org/wiki/Gene_knockdown 遺伝子ノックダウン OBI:0002626 RNAi gene knockdown A gene knockdown that silences genes through artificially-induced RNA interference. This is accomplished by introducing small double-stranded interfering RNA complementary to the target mRNA to be silenced, which is then cleaved by a ribonuclease. Rebecca Jackson RNA interference gene knockdown url:https://en.wikipedia.org/wiki/Gene_knockdown RNAi gene knockdown OBI:0002628 RNAi knockdown assay "Here, we described the development of RNAi by micro-injection of double-stranded RNA (dsRNA) in the pea aphid Acyrthosiphon pisum. Injection of dsRNA into whole aphid body induced the silencing of two marker genes with different expression patterns: the ubiquitously expressed Ap-crt genes encoding a calreticulin and the gut specific Ap-cath-L gene encoding a cathepsin-L." (PMID:17903251) A gene knockdown assay in which RNAi gene knockdown is used to disrupt gene transcripts. Rebecca Jackson RNA interference knockdown assay RNAi gene knockdown assay Rebecca Jackson https://github.com/obi-ontology/obi/issues/1057 RNAi knockdown assay OBI:0002650 biopsy Biopsy of a potentially cancerous mole. A specimen collection that obtains a sample of tissue or cell from a living multicellular organism body for diagnostic purposes by means intended to be minimally invasive. Damion Dooley Nicole Vasilevsky https://en.wikipedia.org/wiki/Biopsy biopsy OBI:0002683 short interspersed nuclear elements polymerase chain reaction A polymerase chain reaction that amplifies short interspersed nuclear elements (SINEs). Jie Zheng short interspersed elements PCR PMID: 12711348 https://github.com/obi-ontology/obi/issues/1117 VEuPathDB short interspersed nuclear elements polymerase chain reaction OBI:0002684 nested polymerase chain reaction A polymerase chain reaction with modification intended to reduce non-specific binding in products due to the amplification of unexpected primer binding sites. The nested polymerase chain reaction (PCR) involves the use of two primer sets and two successive PCR reactions. The first set of primers are designed to anneal to sequences upstream from the second set of primers and are used in an initial PCR reaction. Jie Zheng nested PCR nested-PCR https://en.wikipedia.org/wiki/Nested_polymerase_chain_reaction https://github.com/obi-ontology/obi/issues/1117 VEuPathDB nested polymerase chain reaction OBI:0002685 immunoelectrophoresis An electrophoresis that separates and characterize proteins based on reaction with antibodies. Jie Zheng IEP https://en.wikipedia.org/wiki/Immunoelectrophoresis https://github.com/obi-ontology/obi/issues/1117 VEuPathDB immunoelectrophoresis OBI:0002692 polymerase chain reaction assay An assay that uses polymerase chain reaction technique to amplify DNA. VEuPathDB VEuPathDB https://github.com/obi-ontology/obi/issues/1117 VEuPathDB polymerase chain reaction assay OBI:0002743 molecular label role A reagent role inhering in a molecular entity intended to associate with some molecular target to serve as a proxy for the presence, abundance, or location of this target in a detection of molecular label assay. MHB (9-29-13): 'molecular label role' imported from the Reagent Ontology and replaced OBI:OBI_0000140 (label role). JZ (3-30-20): discussed on the OBI call. Since the REO was never actually registered, we decided to adopt the term into OBI and replaced REO_0000171 by newly assigned ID: OBI:0002743. Group: OBI molecular tracer role OBI developer call, 3-12-12 https://github.com/obi-ontology/obi/issues/1135 molecular label role OBI:0002744 molecular label A molecular reagent intended to associate with some molecular target to serve as a proxy for the presence, abundance, or location of this target in a detection of molecular label assay JZ (3-30-20): discussed on the OBI call. Since the REO was never actually registered, we decided to adopt the term into OBI and replaced OBI:0002744 by newly assigned ID: OBI:0002744. Group: OBI molecular tracer OBI developer call, 3-12-12 https://github.com/obi-ontology/obi/issues/1135 molecular label OBI:0002754 cDNA library cDNA library lacks the non-coding and regulatory elements found in genomic DNA A collection of DNA molecules with sequences complementary to a specified set of mRNA molecules and commonly developed by enzymatic reverse transcription. Dan Berrios modified from Wikipedia cDNA library OBI:0002988 duration of specimen collection Specimen collection duration of 3 nights that a trap is set out for collection of mosquitoes. Urine collected over a 24 hour period of specimen collection duration. A time measurement datum that is the count of collection cycles over which a specimen collection process occurs. specimen collection duration VEuPathDB specimen collection duration OBI:0003129 chemical mutagenesis 129/Sv male mice were injected with ENU and mated to C57BL/6 females. Their first-generation (G1) male progeny were again crossed to C57BL/6 females, and then backcrossed to one of their second-generation (G2) daughters to yield a third-generation (G3). PMID:18802465 A form of random mutagenesis that produces a mutation by introducing the organism to a chemical mutagen. Equivalent to FlyBase "chemical" (FBcv:0000525) in the origin of mutation branch and Dd mutagenesis meth0d term chemical mutagenesis (DDMUMET:0000014). Susan Bello ORCID:orcid.org/0000-0003-4606-0597 url:https://pubmed.ncbi.nlm.nih.gov/25646611/ chemical mutagenesis OBI:0003130 irradiation mutagenesis Groups of (101 x C3H)F1 hybrid male mice 11 weeks old were exposed to two different doses of 137Cs gamma rays. PMID:7035547 A form of random mutagenesis that produces a random mutation by exposing the organism to radiation. Equivalent to FlyBase "irradiation" (FBcv:0000503) in the origin of mutation branch. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 radiation induced mutagenesis url:http://purl.obolibrary.org/obo/FBcv_0000503 irradiation mutagenesis OBI:0003131 directed mutagenesis Exons 20 and 21 were targeted for deletion because they encode the signature and Walker B motifs of the first ATP-binding domain, elements that are known to be critical for ABCA1 function. PMID:15550377 An induced mutation in which a specific gene(s) or part of a gene(s) is altered. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 url:https://www.ncbi.nlm.nih.gov/books/NBK21878/def-item/A4754/ directed mutagenesis OBI:0003132 endonuclease mediated mutagenesis We have generated a WMS mouse model with S236X mutation in ADAMTS10 which is similar to the R237X mutation identifiedin WMS patients using CRISPR-Cas9. PMID:30060141 A directed mutagenesis in which guide RNAs and an endonuclease (cas9, TALEN) are used to introduce a mutation at a specific location in a gene. Equivalent to FlyBase term "site specific cleavage" (FBcv:0003007) in the origin of mutation branch. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 url:https://pubmed.ncbi.nlm.nih.gov/28177771/ endonuclease mediated mutagenesis OBI:0003133 cas mediated mutagenesis Briefly, to create Adar1 M249A/M249A mice, guide RNA targeting 5’-ACCTTCTGAGCCTCTTGACA-3’ was synthesized by using Gene Art Precisiong RNA Synthesis Kit (ThermoFisherScientific). Pronuclear-stage mouse embryos (CLEA Japan Inc., Tokyo, Japan) were electroporated to introduce Cas9 mRNA, the guide RNA and a single-stranded donor... PMID:33983932 An endonuclease mediated mutagenesis in which guide RNAs and cas are used to introduce a mutation at a specific location in the genome. Equivalent (narrow match) to FlyBase term "CRISPR/Cas9" (FBcv:0003008, narrow match as the OBI term covers all forms of cas) in the origin of mutation branch and Dd mutagenesis method term "CRISPR/Cas9" (DDMUMET:0000025). Susan Bello ORCID:orcid.org/0000-0003-4606-0597 CRISPR mediated mutagenesis CRISPR/cas mediated mutagenesis url:https://pubmed.ncbi.nlm.nih.gov/28177771/ cas mediated mutagenesis OBI:0003134 TALEN mediated mutagenesis We designed transcription activator-like effector nucleases (TALENs) and a single-stranded oligo (ssOligo) donor template to edit the endogenous Actb locus within the mouse genome. PMID:30012594 An endonuclease mediated mutagenesis in which guide RNAs and transcription activator-like effector nucleases (TALENs) are used to introduce a mutation at a specific location in the genome. Equivalent to FlyBase term "TALEN" (FBcv:0003009) in the origin of mutation branch. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 url:https://pubmed.ncbi.nlm.nih.gov/23664777/ TALEN mediated mutagenesis OBI:0003135 zinc finger mediated mutagenesis ZFN constructs targeting the third exon of the mouse Apoc2 gene were designed and synthetized by Sigma Aldrich... PMID:26574515 An endonuclease mediated mutagenesis in which synthetic zinc-finger proteins designed to target specific DNA sequences are used to introduce a mutation at a specific location in the genome. Equivalent to FlyBase term "ZFN" (FBcv:0003239) in the origin of mutation branch. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 ZFN mediated mutagenesis url:https://pubmed.ncbi.nlm.nih.gov/23664777/ zinc finger mediated mutagenesis OBI:0003136 transgenic mutagenesis Transgenic mice were then generated by pronuclear injection of either the mixed MoPrP-PS1 and MoPrP-APP or the bicistronic MoPrP–APP/IRES/PS1 expression cassettes into single cell embryos derived from F2 hybrids of C57BL/6J and C3H/HeJ mice... PMID:11337275 A form of random mutagenesis that produces a mutation by introducing a construct into the genome of an organism in a random or semi-random fashion. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 url:https://pubmed.ncbi.nlm.nih.gov/23996268/ transgenic mutagenesis OBI:0003137 gene-trap mutagenesis Constructs lacking a promoter and including a B3-galactosidase gene, or a reporter gene encoding a protein with both B3-galactosidase and neomycin phosphotransferase activity, were designed so that activation of the reporter gene depends on its insertion within an active transcription unit. PMID:1653172 A transgenic mutagenesis that produces a mutation by introducing a construct designed to capture the expression of an endogenous gene by creating a spliced fusion transcript when inserted into the genome of an organism. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 url:https://pubmed.ncbi.nlm.nih.gov/17877761/ gene-trap mutagenesis OBI:0003138 enhancer-trap mutagenesis We generated several lines of enhancer trap mice carrying an enhancer detector cassette expressing Cre recombinase under the transcriptional control of the minimal promoter (129 base pairs) of the mouse Thy-1.2 gene. PMID:22492032 A transgenic mutagenesis that produces a mutation by introducing a construct designed to monitor transcriptionally active regions when inserted into the genome of an organism by inserting a reporter gene that requires cis-acting DNA sequences in the genome to activate reporter gene expression. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 url:https://pubmed.ncbi.nlm.nih.gov/17877761/ enhancer-trap mutagenesis OBI:0003139 targeted mutagenesis To disrupt the mdr1a gene a 1.6 kb NheI genomic fragment containing exons 6 and 7 was replaced by a hygromycin phosphotransferase cassette in a targeting vector. PMID:7910522 A directed mutation in which a construct is used to introduce a mutation into a specific genome location through homologous recombination. Equivalent to FlyBase term "gene targeting by homologous recombination" (FBcv:0000710) in the origin of mutation branch. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 gene targeting by homologous recombination url:https://pubmed.ncbi.nlm.nih.gov/23996268/ targeted mutagenesis OBI:0003140 transposon-induced mutagenesis In order to achieve SB transposon-mediated mutagenesis in mice, we employed the gene trap scheme using a novel transposon vector, and we have generated a large number of mutant mice, approximately 30% of which displayed the phenotype. PMID:16880528 A random mutagenesis in which expression of a transposase causes the mobilization of an artificial or modified transposable element with the insertion of the element into the genome creating a mutation. Equivalent to FlyBase "transposable element activity" (FBcv:0000483) in the origin of mutation branch. Susan Bello ORCID:orcid.org/0000-0003-4606-0597 url:https://pubmed.ncbi.nlm.nih.gov/32050713/ transposon-induced mutagenesis OBI:0003327 image data set The output produced by a digital imaging technique, such as microscopy, MRI, or CT. A data set that is comprised of multidimensional structured measurements and metadata required for a morphological representation of an entity. An image data set can be the source from which an image (such as a 2D image using pixels or a 3D image using voxels) is produced. https://orcid.org/0000-0001-9625-1899 "William D. Duncan" https://orcid.org/0000-0001-9676-7377 "Alexander D. Bartnik" https://orcid.org/0000-0001-9990-8331 "Alexander D. Diehl" https://orcid.org/0000-0002-2104-0568 "Lucas M. Serra" https://orcid.org/0000-0002-7245-3450 "Lauren M. Wishnie" https://orcid.org/0000-0002-9821-4132 "Mackenzie T. Smith" https://github.com/obi-ontology/obi/issues/1481 image data set OBI:0003355 The process of deriving a data item from an image data set using computer algorithms. The produced data item can be an image data set, data measurement, or any other data item. image data set analysis OBI:0003368 detection technique Using a radioactivity detection assay as part of a tritiated thymidine incorporation assay to determine the degree to which cells are replicating by detecting radioactivity of tritiated thymidine, where radioactivity of tritiated thymidine in a cell is a proxy for cells that were actively replicating. An assay (A) that is part of another assay (B), where the target entities of A and B are disjoint, and the target entity of A is a proxy for the target of assay B. Bjoern Peters Hector Guzman-Orozco OBI https://github.com/obi-ontology/obi/issues/1488 detection technique OBI:0005246 injection function The function of a device realized when administering a substance in vivo, applied particularly to the forcible insertion of a liquid or gas by means of a syringe, pump, etc. PERSON: Alan Ruttenberg PERSON: Melanie Courtot adapted from WEB: http://www.dictionary.net/injection injection function OBI:0100026 An organism is material entity that is an individual living system, such as animal, plant, bacteria or virus, that is capable of replicating or reproducing, growth and maintenance in the right environment. An organism may be unicellular or made up, like humans, of many billions of cells divided into specialized tissues and organs. A material entity that is an individual living system, such as animal, plant, bacteria or virus, that is capable of replicating or reproducing, growth and maintenance in the right environment. An organism may be unicellular or made up, like humans, of many billions of cells divided into specialized tissues and organs. http://purl.obolibrary.org/obo/obi.owl Its function is to do life activity. organism OBI:0100051 specimen Biobanking of blood taken and stored in a freezer for potential future investigations stores specimen. A material entity that has the specimen role. Note: definition is in specimen creation objective which is defined as an objective to obtain and store a material entity for potential use as an input during an investigation. PERSON: James Malone PERSON: Philippe Rocca-Serra GROUP: OBI Biomaterial Branch specimen OBI:0100060 cultured cell population A cultured cell population applied in an experiment: "293 cells expressing TrkA were serum-starved for 18 hours and then neurotrophins were added for 10 min before cell harvest." (Lee, Ramee, et al. "Regulation of cell survival by secreted proneurotrophins." Science 294.5548 (2001): 1945-1948). A cultured cell population maintained in vitro: "Rat cortical neurons from 15 day embryos are grown in dissociated cell culture and maintained in vitro for 8–12 weeks" (Dichter, Marc A. "Rat cortical neurons in cell culture: culture methods, cell morphology, electrophysiology, and synapse formation." Brain Research 149.2 (1978): 279-293). A processed material comprised of a collection of cultured cells that has been continuously maintained together in culture and shares a common propagation history. 2013-6-5 MHB: This OBI class was formerly called 'cell culture', but label changed and definition updated following CLO alignment efforts in spring 2013, during which the intent of this class was clarified to refer to portions of a culture or line rather than a complete cell culture or line. PERSON:Matthew Brush cell culture sample PERSON:Matthew Brush The extent of a 'cultured cell population' is restricted only in that all cell members must share a propagation history (ie be derived through a common lineage of passages from an initial culture). In being defined in this way, this class can be used to refer to the populations that researchers actually use in the practice of science - ie are the inputs to culturing, experimentation, and sharing. The cells in such populations will be a relatively uniform population as they have experienced similar selective pressures due to their continuous co-propagation. And this population will also have a single passage number, again owing to their common passaging history. Cultured cell populations represent only a collection of cells (ie do not include media, culture dishes, etc), and include populations of cultured unicellular organisms or cultured multicellular organism cells. They can exist under active culture, stored in a quiescent state for future use, or applied experimentally. cultured cell population OBI:0100061 primary cultured cell population Spleen cells put directly into culture; Cold storage of biopsies from wild endangered native Chilean species in field conditions and subsequent isolation of primary culture cell lines. In Vitro Cell Dev Biol Anim. 2008 Jul 2. PMID: 18594934 cells that have been isolated from some organismal source, expanded in culture, but not undergone a complete passaging (ie are still in culture, or have been lifted from culture and frozen in aliquots for future use) A cultured cell population comprised of cells expanded directly from living tissue prior to being passaged. 2013-6-5 MHB: This OBI class was formerly called 'primary cell culture', but label changed and definition updated following CLO alignment work. Previous definition: 'a primary cell culture is a cell culture where the cells derive from a fresh tissue source.' PERSON:Matthew Brush primary cell culture primary cell culture sample PERSON:Matthew Brush primary cultured cell population 0 consider if we really want to be so strict here . . . ie maybe we we say that they have not been output from an 'establishing cell line' process, but in some cases a passage or two may be allowed for a primary culture. the establishing of a line requires some procedss that attains a degree of homogeneity in the culture. OBI:0100066 organ section A liver slice used in a perfusion experiment. Thyroidectomy during laryngectomy for advanced laryngeal carcinoma--whole organ section study with long-term functional evaluation. Clin Otolaryngol Allied Sci. 1995 Apr;20(2):145-9. PMID: 7634521 A processed material which derives from an organ and results from a process of dissection or histological sample preparation a portion(formerly an organ section is portion of an organ removed from the context of the organ) PERSON: Helen Parkinson PERSON: Philippe Rocca-Serra GROUP: CEBS GROUP: OBI Biomaterial Branch organ section OBI:0200000 data transformation The application of a clustering protocol to microarray data or the application of a statistical testing method on a primary data set to determine a p-value. A planned process that produces output data from input data. Elisabetta Manduchi Helen Parkinson James Malone Melanie Courtot Philippe Rocca-Serra Richard Scheuermann Ryan Brinkman Tina Hernandez-Boussard data analysis data processing Branch editors data transformation OBI:0200031 differential expression analysis objective Analyses implemented by the SAM (http://www-stat.stanford.edu/~tibs/SAM), PaGE (www.cbil.upenn.edu/PaGE) or GSEA (www.broad.mit.edu/gsea/) algorithms and software A differential expression analysis objective is a data transformation objective whose input consists of expression levels of entities (such as transcripts or proteins), or of sets of such expression levels, under two or more conditions and whose output reflects which of these are likely to have different expression across such conditions. Elisabetta Manduchi PERSON: Elisabetta Manduchi differential expression analysis objective OBI:0200052 probabilistic algorithm A probabilistic algorithm is one which involves an element of probability or randomness in the transformation of the data. James Malone PERSON: James Malone probabilistic algorithm OBI:0200081 sequence analysis objective A sequence analysis objective is a data transformation objective which aims to analyse some ordered biological data for sequential patterns. James Malone PERSON: James Malone sequence analysis objective OBI:0200166 data transformation objective normalize objective An objective specification to transformation input data into output data Modified definition in 2013 Philly OBI workshop James Malone PERSON: James Malone data transformation objective OBI:0302716 pool of specimens A pool of specimens is a mixture of a population of samples which have been gathered from one or more sample populations, obtained by the physical process of mixing individual specimens, e.g. mixing the DNA collected from the individual fish. check with advisors as to how to represent multiple instances of any class? a set of specimens which have been gathered from one or more sample_populations, obtained by the physical process of mixing individual specimens, e.g. mixing the DNA collected from the individual fish PERSON: Jennifer Fostel GROUP: CEBS pool of specimens OBI:0302729 chemical solution PMID: 18289311.Anesth Analg. 2008 Apr;106(4):1078-86.Less impairment of hemostasis and reduced blood loss in pigs after resuscitation from hemorrhagic shock using the small-volume concept with hypertonic saline/hydroxyethyl starch as compared to administration of 4% gelatin or 6% hydroxyethyl starch solution. A material entity that is made up of at least 2 scattered molecular aggregates, one playing the role of solvent and the other one playing the role of solute. PERSON: Bjoern Peters PERSON: Philippe Rocca-Serra liquid chemical solution GROUP: OBI Biomaterial Branch chemical solution OBI:0302732 solvent role PMID: 18373502.Transfusion. 2008 Mar 25. Solvent/detergent treatment of platelet concentrates enhances the release of growth factors. solvent role is a role which inheres in a molecular entity capable of ensuring the dissolution of another chemical entity and realized by the process of solvation Philippe Rocca-Serra adpated from wikipedia (http://en.wikipedia.org/wiki/Solvatation) solvent role OBI:0302733 solute role PMID: 18380397.Pharmazie. 2008 Feb;63(2):113-21.Deviations of drug solubility in water-cosolvent mixtures from the Jouyban-Acree model--effect of solute structure. solute role is a role played by a chemical entity which is dissolved by another chemical entity (the solvent) when creating a solution Philippe Rocca-Serra adapted from wikipedia (http://en.wikipedia.org/wiki/Solute) solute role OBI:0302859 genetically modified organism A protocol for removal of antibiotic resistance cassettes from human embryonic stem cells genetically modified by homologous recombination or transgenesis. Nat Protoc. 2008;3(10):1550-8. PMID: 18802436 An organism that is the output of a genetic transformation process. an organism that is the output of a genetic transformation process PERSON: Philippe Rocca-Serra OBI Biomaterial genetically modified organism OBI:0302867 A data item that was generated on the basis of a calculation or logical reasoning predicted data item OBI:0302876 dissolved material entity Salt molecules that have been mixed into water A material entity that has been going through a process of being put into solution Person:Bjoern Peters Philippe Rocca-Serra dissolved material entity OBI:0302884 extraction nucleic acid extraction using phenol chloroform A material separation in which a desired component of an input material is separated from the remainder Current the output of material processing defined as the molecular entity, main component in the output material entity, rather than the material entity that have grain molecular entity. 'nucleic acid extract' is the output of 'nucleic acid extraction' and has grain 'nucleic acid'. However, the output of 'nucleic acid extraction' is 'nucleic acid' rather than 'nucleic acid extract'. We are aware of this issue and will work it out in the future. Person:Bjoern Peters Philippe Rocca-Serra extraction OBI:0302889 A planned process by which a material entity is exposed to radiative energy, which could be ionizing radiation (such as gamma rays, X-rays, charged particles or neutrons) or non-ionizing radiation (such as UV light or microwaves) planned irradiation OBI:0302891 trypsination The use of mild trypsinization conditions in the detachment of endothelial cells to promote subsequent endothelialization on synthetic surfaces. Biomaterials. 2007 Sep;28(27):3928-35. PMID: 17570483 trypsination is a protease cleavage which uses enzyme trypsin to act on proteins present in an input material entity Philippe Rocca-Serra OBI PA trypsination OBI:0302892 enzymatic ligation PMID: 17853876. Enzymatic ligation assisted by nucleases: simultaneous ligation and digestion promote the ordered assembly of DNA. Nat Protoc. 2007;2(9):2198-202. An enzymatic ligation is a planned process in which molecules are joined by covalent bonds through the action of an material entity with a ligase activity Philippe Rocca-Serra OBI-Branch enzymatic ligation OBI:0302906 DNA Subtraction PMID: 10718422. Identification of genes overexpressed in head and neck squamous cell carcinoma using a combination of complementary DNA subtraction and microarray analysis. Laryngoscope. 2000 Mar;110(3 Pt 1):374-81 a material separation process by which repetitive genomic DNA is removed during the construction of cDNA library. Philippe Rocca-Serra OBI-Branch DNA Subtraction OBI:0400103 DNA sequencer ABI 377 DNA Sequencer, ABI 310 DNA Sequencer A DNA sequencer is an instrument that determines the order of deoxynucleotides in deoxyribonucleic acid sequences. Trish Whetzel MO DNA sequencer OBI:0400168 microtome PMID: 9974145.Serial sectioning of thick tissue with a novel vibrating blade microtome. Brain Res Brain Res Protoc. 1999 Jan;3(3):302-7. A microtome is a mechanical instrument used to cut biological specimens into very thin segments for further treatment (e.g. ISH) and ultimately microscopic or histologic examination. Most microtomes provide cooling facilities (cryo-microtome) and use a steel blade to cut a slice of defined thickness. Some are automatic, and some are driven by hand. PERSON: Phillippe Rocca-Serra PERSON: Daniel Schober microtome OBI:0400169 microscope PMID:18466942. A light and transmission electron microscope study of hepatic portal tracts in the rhesus monkey (Macacus rhesus). Tissue Cell. 2008 May 6 A microscope is an instrument which magnifies the view on objects (too small to be viewed by the naked eye) under increased resolution. A microscope can be an optical instrument but also and electronic instrument. There are various kind of optical microscopes, e.g confocal microscope, epifluoresence microscope) PERSON: Phillippe Rocca-Serra wikipedia CHMO:0000953 microscope OBI:0500000 study design A plan specification comprised of protocols (which may specify how and what kinds of data will be gathered) that are executed as part of an investigation and is realized during a study design execution. study design OBI:0600000 adding substance to cell culture adding fetal calf serum to a 96 well plate containing a cell culture derived from a blood sample of a patient is process in which a material substance is added to a cell culture renamed from 'administering substance to cell culture', to reflect that administration is commonly used only for organisms Bjoern Peters IEDB adding substance to cell culture OBI:0600005 collecting specimen from organism taking a sputum sample from a cancer patient, taking the spleen from a killed mouse, collecting a urine sample from a patient a process with the objective to obtain a material entity that was part of an organism for potential future use in an investigation PERSON:Bjoern Peters IEDB collecting specimen from organism 1 OBI:0600007 administering substance in vivo Balb/c mice received an intracameral or subconjunctival injection of trinitrophenylated spleen cells injecting mice with 10 ug morphine intranasally, a patient taking two pills of 1 mg aspirin orally A process by which a substance is intentionally given to an organism resulting in exposure of the organism to that substance. 2009-11-10. Tracker: https://sourceforge.net/tracker/?func=detail&aid=2893050&group_id=177891&atid=886178 Different routes and means of administration should go as children underneath this Update the definition based on the discussion. Details see the tracker: https://sourceforge.net/p/obi/obi-terms/738/ needs roles such as perturber and perturbee (children of input role). Perturb is too strong. Host might be the name for one role. Others considered: Doner, Donated, Acceptor. Bjoern Peters Person:Bjoern Peters IEDB administering substance in vivo OBI:0600008 acquisition Downloading a 3D structure from the PDB. Purchasing antibodies from sigma. the planned process of gaining possession of a continuant. 5/31/2012 - OBI workshop: This process is not implying ownership of the material / information. Following OBI call November 2012,5th: addition of a restriction to acquisition class to capture the need of having selection criteria Relates to the creation of a class 'selection rule' Bjoern Peters IEDB This needs to be fleshed out and logical definitions added that will allow to place the children terms automatically under acquisition acquisition OBI:0600010 material acquisition Acquiring 50 C57BL/6 mice bred in the animal facility of the institute as a service to investigators. Purchasing 1 mg of peptides synthesized by Mimotopes at 80% purity. Getting a gift of purified CD4+ specific antibodies presented by Stephen Schoenberger at LIAI. An acquisition in which possession of a material entity is gained. The assumption is that the object already exists in its current state, e.g, an available mouse strain purchased from the Jackson Lab, this is the differentia from specimen creation This excludes processes that create or change materials, such as material transformations. Bjoern Peters, Alan Ruttenberg, Helen Parkinson material procurement IEDB material acquisition OBI:0600013 information acquisition Gathering all influenza HA sequences from GenBank, Retrieveing HLA allele frequencies in the North American populations from dbMHC An acquisition in which possession of information is gained. This excludes processes that create or change information, such as assays and data transformations. Bjoern Peters data collection OBI branch derived information acquisition OBI:0600014 material component separation Using a cell sorter to separate a mixture of T cells into two fractions; one with surface receptor CD8 and the other lacking the receptor, or purification a material processing in which components of an input material become segregated in space Bjoern Peters IEDB material component separation 2 OBI:0600016 pooling specimens http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=104564; Combining spleens of 20 mice, Combining supernatant from a cell culture obtained at different time points physical combination of several instances of like material PlanAndPlannedProcess Branch sample pooling OBI branch derived like' is one of the things that you should be controling for in a well-designed experiment. The instances of material need to have the same class. pooling specimens OBI:0600019 non-specific labeling The addition of phycoerytherin label to an anti-CD8 antibody, to label all antibodies. The addition of a reagent labeling the entire input biomaterial enabling future detection of the output biomaterial PlanAndPlannedProcess Branch OBI branch derived definition blessed by Allyson, Bjoern, Jay & Randi non-specific labeling OBI:0600023 non specific enzymatic cleavage The use of agarase to digest an agar gel an enzymatic cleavage that uses an enzyme without a strong affinity for specific cleavage sites in the input material PERSON:Kevin Clancy OBI branch derived non specific enzymatic cleavage OBI:0600024 maintaining cell culture When harvesting blood from a human, isolating T cells, and then limited dilution cloning of the cells, the maintaining_cell_culture step comprises all steps after the initial dilution and plating of the cells into culture, e.g. placing the culture into an incubator, changing or adding media, and splitting a cell culture a protocol application in which cells are kept alive in a defined environment outside of an organism. part of cell_culturing PlanAndPlannedProcess Branch OBI branch derived maintaining cell culture OBI:0600028 artificially induced reverse transcription The use of M-MLV reverse transcriptase from the Moloney murine leukemia virus to transcribe an RNA sample into cDNA a protocol with the objective to transcribe single-stranded RNA into complementary DNA (cDNA) It could also be added that the reverse transcriptase is bearer of a GO:0003964 RNA-directed DNA polymerase activity, which is realized in this process. We need to indicate the relationship between the cDNA generated and the RNA that was used as a template. This may be outside of the OBI scope PERSON:Kevin Clancy OBI branch derived artificially induced reverse transcription OBI:0600029 isolation of cell culture supernatant Pouring out a portion of the fluid part of an adherant cell culture growing in a flask.; The centrifugation of a T cell culture followed by aspiration of the supernatant while the cellular pellet remains in the centrifuge tube. a protocol which results in the separation of supernatant material from a cell culture This does not apply to the case where the cells are lysed PlanAndPlannedProcess Branch OBI branch derived isolation of cell culture supernatant OBI:0600033 cell permeabilization Electroporation of HeLa cells to allow transfection with pUC19. A protocol application to permeabilize cell membranes, allowing molecules to more easily pass through the membrane than was possible prior to the protocol application need to add output cell has_quality permeable PERSON:Bjoern Peters OBI branch derived definition blessed by Jay, Alan, Randi cell permeabilization OBI:0600036 'establishing cell culture' a process through which a new type of cell culture or cell line is created, either through the isolation and culture of one or more cells from a fresh source, or the deliberate experimental modification of an existing cell culture (e.g passaging a primary culture to become a secondary culture or line, or the immortalization or stable genetic modification of an existing culture or line). PERSON:Matthew Brush PERSON:Matthew Brush A 'cell culture' as used here referes to a new lineage of cells in culture deriving from a single biological source.. New cultures are established through the initial isolation and culturing of cells from an organismal source, or through changes in an existing cell culture or line that result in a new culture with unique characteristics. This can occur through the passaging/selection of a primary culture into a secondary culture or line, or experimental modifications of an existing cell culture or line such as an immortalization process or other stable genetic modification. This class covers establishment of cultures of either multicellular organism cells or unicellular organisms. establishing cell culture OBI:0600037 cell culture splitting The act of taking a cell culture of high density, counting the cells, removing part of the cells, and re-seeding a select number of the cells into new flasks with fresh tissue culture media. The act of taking part of a homogeneous cell culture and creating one or more additional separate cultures of similar qualities. input: cell_culture, output cell_culture min cardinality 2. part of cell culturing PlanAndPlannedProcess Branch cell culture passaging OBI branch derived An active cell culture is typically split when it has grown to confluence in its culture dish. Cell culture splitting of a cell culture sample results in an increase in its passage number, which measures how long a sample has been propagated in vitro, and therefore how many selective or genetic changes it is likely to have undergone. cell culture splitting OBI:0600038 addition of molecular label The addition of phycoerytherin label to an anti-CD8 antibody, to label all antibodies. The addition of anti-CD8-PE to a population of cells, to label the subpopulation cells that are CD8+. a material processing technique intended to add a molecular label to some input material entity, to allow detection of the molecular target of this label in a detection of molecular label assay PERSON:Matthew Brush labeling OBI developer call, 3-12-12 addition of molecular label OBI:0600039 artificially induced methylation the use of enzymes to add methyl groups to DNA molecules A planned process of adding methyl groups to polymers PERSON:Kevin Clancy OBI branch derived artificially induced methylation OBI:0600042 recombinant plasmid cloning The DNA fragment encoding the p35 gene from Mycobacterium avium complex was inserted into pcDNAII and expressed in E coli in order to study p35. the insertion of a particular DNA fragment into a plasmid in order to make copies of a biomaterial PERSON:Kevin Clancy OBI branch derived recombinant plasmid cloning OBI:0600043 genetic transformation The transduction of E. coli through the introduction of a plasmid encoding for M. avium p35 the introduction. alteration or integration of genetic material into a cell or organism PERSON:Kevin Clancy genetic modification OBI branch derived genetic transformation OBI:0600047 sequencing assay The use of the Sanger method of DNA sequencing to determine the order of the nucleotides in a DNA template An assay the uses chemical or biochemical means to infer the sequence of a biomaterial PlanAndPlannedProcess Branch OBI branch derived sequencing assay OBI:0600048 vector mediated amplification E coli expressing the gene for M avium p35 were cultured in order to produce p35. The process of creating a copy of some biological entity in cell culture PERSON:Kevin Clancy OBI branch derived vector mediated amplification OBI:0600050 specific enzymatic cleavage The use of a protease to digest a protein into peptides an enzymatic cleavage that uses an enzyme with a strong affinity for specific cleavage sites in the input material PERSON:Kevin Clancy OBI branch derived specific enzymatic cleavage OBI:0600053 electrophoresis Loading a mixture of proteins into a polyacrylamide gel and the application of an electrical current to the gel to separate the proteins by size and change. a protocol application that uses an electrical potential to move material through a defined matrix in order to separate it by its resistance to movement and its charge PERSON:Kevin Clancy OBI branch derived Need to define more terms like gel_separation, matrix,centrifugation, and the connection between the force used to separate materials and the medium or barriers. electrophoresis OBI:0600055 DNA cleavage, restriction analysis the use of the restriction enzymes SalPI and PstI to cleave DNA into fragments, assay made up of components A specific enzymatic cleavage of DNA molecules using endonucleases that cleave DNA molecules at specific sites based on the surrounding nucleotide sequence PERSON:Kevin Clancy restriction enzyme assay DNA restriction enzyme digestion OBI:0600056 protease cleavage the use of trypsin to cleave pepsin into peptide fragments protease cleavage is an enzymatic cleavage which relies on enzyme with protease activity to act on proteins and produce polypeptides (protein fragments). enzymatic digestion PlanAndPlannedProcess Branch OBI branch derived protease cleavage OBI:0600058 enzymatic amplification the use of a polymerase chain reaction to amplify a fragment of DNA the use of enzymes to increase the number of molecules of a biomaterial PERSON:Kevin Clancy OBI branch derived enzymatic amplification OBI:0600059 DNA transduction The transfer of a recombinant bacterial plasmid into E.coli to facilitate amplification of a specific protein a genetic transformation which relies on the use of lysogenic infection to transfer DNA sequences into an organism PERSON:Kevin Clancy OBI branch derived DNA transduction OBI:0600060 DNA transfection The use of electroporation to permeabilize a cell membrane in order to introduce a plasmid encoding for a labeled protein of interest a transfection which relies on the use of physical, electrical and chemical phenomena to introduce DNA into a cell PERSON:Kevin Clancy OBI branch derived DNA transfection OBI:0600063 vector mediated expression Construction of pRSS1327 expression vector by molecular cloning of a 1327-bp cDNA, which includes sequences of the entire coding region for RSS, into pBluescript. Expression in Escherichia coli of a functional, full-length RSS was confirmed by immunoblot analysis and enzymatic activity. vector mediated expression is the generation of copies of biomaterial by in a cell_culture modified for this purpose by insertion of an expression vector needs defined relationship to cell culture PlanAndPlannedProcess Branch OBI branch derived vector mediated expression OBI:0600064 recombinant vector cloning a planned process with the objective to insert genetic material into a cloning vector for future replication of the inserted material pa_branch (Alan, Randi, Kevin, Jay, Bjoern) molecular cloning OBI branch derived recombinant vector cloning OBI:0600067 specific labeling The addition of anti-CD8 antibody for an ICCS assay in order to selectively stain the CD8+ cells a labeling in which the labeling reagent used has a specificity to bind only certain components of the input material PlanAndPlannedProcess Branch OBI branch derived definition blessed by Allyson, Bjoern, Jay & Randi specific labeling OBI:0666666 RNA extraction A RNA extraction is a nucleic acid extraction where the desired output material is RNA PlanAndPlannedProcess Branch OBI branch derived requested by Helen Parkinson for MO RNA extraction OBI:0666667 nucleic acid extraction Phenol / chlorophorm extraction disolvation of protein content folllowed by ethanol precipitation of the nucleic acid fraction over night in the fridge followed by centrifugation to obtain a nucleic acid pellet. a material separation to recover the nucleic acid fraction of an input material PlanAndPlannedProcess Branch OBI branch derived requested by Helen Parkinson for MO. Could be defined class nucleic acid extraction OBI:1000023 cell culture supernatant solution containing RPMI, fetal calf sera, antibiotics, and monoclonal antibody UCHT1. Isolation of proliferation factor of immature T-cell clone in concanavalin A-stimulated splenocyte culture supernatant. Immunology. 2003 Jun;109(2):209-16. PMID: 12757615 Supernatant of a cell culture is a material entity which contains media, supplements, and secreted products of the cells and becomes the environment of cultivated cell. PERSON: Bjoern Peters GROUP: IEDB cell culture supernatant OBI:1000029 phage display library PMID: 15905471.Nucleic Acids Res. 2005 May 19;33(9):e81.Oligonucleotide-assisted cleavage and ligation: a novel directional DNA cloning technology to capture cDNAs. Application in the construction of a human immune antibody phage-display library. [Phage display library encoding fragments of human antibodies. m-rna library encoding for 9-mer peptides] a phage display library is a collection of materials in which a mixture of genes or gene fragments is expressed and can be individually selected and amplified. PERSON: Bjoern Peters PERSON: Philippe Rocca-Serra display library WEB: http://www.immuneepitope.org/home.do PRS: 22022008. class moved under population, modification of definition and replacement of biomaterials in previous definition with 'material' addition of has_role restriction phage display library OBI:1000048 transgenic organism HLA-A*0201 transgenic mice, Vaccinia virus expressing the LCMV gp protein Possible ecological risks of transgenic organism release when transgenes affect mating success: sexual selection and the Trojan gene hypothesis. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13853-6. PMID: 10570162 A transgenic organism is material entity which derives from an organism which has been modified to express a gene not normally part of it. a transgenic organism is material entity which derives from an organism which has been modified to express a gene not normally part of it PRS:22-02-2008: is a organism which has output_role during genetic modification of type (KO) protocol-application PERSON: Bjoern Peters PERSON: Philippe Rocca-Serra GROUP:IEDB transgenic organism OBI:1110028 293-T cell line A cell line derived from human embryonic kidney cells. This cell line contains the SV40 Large T-antigen, allowing episomal replication of transfected plasmids containing the SV40 origin of replication. IEDB IEDB http://www.biotech.ist.unige.it/cldb/cl5008.html 293-T cell line OBI:1110032 HeLa cell culture A cell line derived from human cervical cancer cells. IEDB IEDB http://www.biotech.ist.unige.it/cldb/cl1597.html HeLa cell line OBI:1110035 Jurkat cell line A cell line derived from human T cells. IEDB IEDB http://www.biotech.ist.unige.it/cldb/cl5296.html Jurkat cell line OBI:1110109 target of material addition A cell culture into which a mixture of peptides is being added. A material entity that receives the addition of another material entity in an “adding a material entity into a target” process. 10/26/09: This defined class is used as a 'macro' to reduce the size of the IEDB export. IEDB target of material addition OGG:0000000002 A gene is a material entity that represents the entire DNA sequence required for synthesis of a functional protein or RNA molecule. A gene is a material entity that represents the entire DNA sequence required for synthesis of a functional protein or RNA molecule. Physical and functional unit of heredity, which carries information from one generation to the next. In molecular terms, it is the entire DNA sequence including exons, introns, and noncoding transcription-control regions necessary for production of a functional protein or RNA. Physical and functional unit of heredity, which carries information from one generation to the next. In molecular terms, it is the entire DNA sequence including exons, introns, and noncoding transcription-control regions necessary for production of a functional protein or RNA. gene A gene is a material entity that represents the entire DNA sequence required for synthesis of a functional protein or RNA molecule. http://www.ncbi.nlm.nih.gov/books/NBK21640/ Physical and functional unit of heredity, which carries information from one generation to the next. In molecular terms, it is the entire DNA sequence including exons, introns, and noncoding transcription-control regions necessary for production of a functional protein or RNA. ISBN:9780716737063 OGG:2000002759 A gene of an organism of Eukaryota Yue Liu, Bin Zhao, Oliver He 2759 gene of Eukaryota OGG:2000009606 A gene of an organism of Homo sapiens Yue Liu, Bin Zhao, Oliver He 9606 gene of Homo sapiens OGG:2060009606 A gene of Homo sapiens that has a protein-coding gene disposition Bin Zhao, Oliver He 9606 protein-coding gene of Homo sapiens OGG:2070009606 A gene of Homo sapiens that has a pseudo gene disposition Bin Zhao, Oliver He 9606 pseudo gene of Homo sapiens OGG:2100009606 A gene of Homo sapiens that has a ncRNA gene disposition Bin Zhao, Oliver He 9606 ncRNA gene of Homo sapiens OGG:2110009606 A gene of Homo sapiens that has a RNA gene disposition Bin Zhao, Oliver He 9606 RNA gene of Homo sapiens OGG:3000000012 Bin Zhao, Yue Liu, Oliver He AACT ACT GIG25 WEB: http://www.ncbi.nlm.nih.gov/gene SERPINA3 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 12 GIG24 14q32.1 9606 14 Official from a nomenclature committee GO_0003677 (EC: TAS, PMID: 14668352); GO_0004867 (EC: IBA); GO_0004867 (EC: TAS, PMID: 2404007); GO_0005515 (EC: IPI, PMID: 12709365); GO_0005576 (EC: IBA); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005622 (EC: NAS, PMID: 9880565); GO_0005634 (EC: TAS, PMID: 14668352); GO_0006953 (EC: IEA); GO_0006954 (EC: NAS, PMID: 12475184); GO_0010951 (EC: IBA); GO_0019216 (EC: NAS, PMID: 11835318); GO_0030162 (EC: IBA); GO_0030277 (EC: NAS, PMID: 8647626); GO_0070062 (EC: IDA, PMID: 19056867); GO_0072562 (EC: IDA) PMID: 123121; 1311327; 1351206; 1618300; 2016749; 2190106; 2404007; 2432851; 2435303; 2456771; 2787670; 2945424; 3028924; 3257719; 3260956; 3485824; 3490907; 3492865; 3637050; 6547997; 6556193; 6606438; 6687683; 6762318; 7521171; 7528097; 7588564; 7759598; 7873202; 7924407; 7966721; 8011628; 8216224; 8226889; 8244391; 8267879; 8365378; 8376411; 8647626; 8718849; 8732755; 8739078; 8836107; 8849841; 9042371; 9261179; 9428387; 9521649; 9580375; 9635374; 9698370; 9824262; 9880565; 10048303; 10209959; 10228625; 10512690; 10618372; 10660528; 10759471; 10829039; 11096092; 11099722; 11132933; 11161981; 11274154; 11289720; 11290389; 11295654; 11317942; 11385264; 11692021; 11735417; 11769703; 11798857; 11835318; 11916200; 11936240; 11959399; 11992569; 12023832; 12126519; 12324297; 12475184; 12477932; 12600202; 12685871; 12709365; 12736093; 12754519; 12782964; 14668352; 14687906; 14702039; 14718574; 14760718; 15014966; 15131125; 15159602; 15482730; 15489334; 15530656; 15542006; 15546506; 15612581; 15638460; 15653173; 15659365; 15718509; 15907346; 15935385; 16099106; 16137793; 16278826; 16303762; 16335952; 16424370; 16453284; 16565071; 16712791; 16892178; 16968986; 17207965; 17608807; 17690329; 17854420; 18056971; 18078695; 18248459; 18383875; 18401426; 18408372; 18842294; 18991685; 19008959; 19056867; 19165527; 19247692; 19341158; 19390575; 19525388; 19578796; 19590686; 19789190; 19907165; 19913121; 19933216; 19959196; 20117085; 20158662; 20302328; 20378355; 20444200; 20628086; 21067581; 21296644; 21674799; 21693707; 21730889; 21988832; 22079093; 22246292; 22272609; 22294107; 22806587; 22869038; 23669352; 24172014 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 Ensembl:ENSG00000196136 HGNC:16 HPRD:00120 MIM:107280 Vega:OTTHUMG00000029851 Other designations: alpha-1-antichymotrypsin|cell growth-inhibiting gene 24/25 protein|growth-inhibiting protein 24|growth-inhibiting protein 25|serine (or cysteine) proteinase inhibitor, clade A, member 3|serpin A3 SERPINA3 OGG:3000000031 Bin Zhao, Yue Liu, Oliver He ACAC ACACAD ACC ACC1 ACCA WEB: http://www.ncbi.nlm.nih.gov/gene ACACA acetyl-CoA carboxylase alpha 31 17q21 9606 17 Official from a nomenclature committee GO_0001894 (EC: IEA); GO_0003989 (EC: ISS); GO_0003989 (EC: TAS); GO_0004075 (EC: IEA); GO_0005515 (EC: IPI, PMID: 16326698); GO_0005524 (EC: IEA); GO_0005739 (EC: IEA); GO_0005829 (EC: ISS); GO_0005829 (EC: TAS); GO_0006084 (EC: ISS); GO_0006112 (EC: TAS); GO_0006633 (EC: ISS); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0006768 (EC: TAS); GO_0006853 (EC: TAS); GO_0019432 (EC: TAS); GO_0031325 (EC: TAS); GO_0035338 (EC: TAS); GO_0044255 (EC: TAS); GO_0044268 (EC: IEA); GO_0044281 (EC: TAS); GO_0046872 (EC: IEA); GO_0051289 (EC: ISS); GO_0055088 (EC: IEA); GO_2001295 (EC: IEA) PMID: 2900138; 2900140; 2906852; 7732023; 7905825; 7907095; 7915280; 8944226; 10677481; 10737800; 11052978; 12360400; 12477932; 12810950; 14643797; 15302935; 15333468; 15607423; 16169070; 16326698; 16698035; 16713569; 16794074; 16806233; 17081983; 17372234; 17521700; 17620599; 17631500; 18031993; 18056116; 18303054; 18452305; 18455495; 18487259; 18614941; 18614968; 18660489; 18678647; 18996102; 19061860; 19343720; 19380743; 19543203; 19710915; 19720090; 19723093; 19738201; 19842072; 19846279; 19913121; 20139635; 20379614; 20431927; 20457939; 20562859; 20602615; 20628086; 20877624; 20965718; 21139048; 21344388; 21471234; 21638027; 21642987; 21726077; 21890473; 21906983; 22238651; 22268729; 22505724; 22586326; 22863883; 22939629; 23000302; 23181366; 23383273; 23455922; 23535730; 23886516; 24457600 acetyl-CoA carboxylase alpha Ensembl:ENSG00000132142 HGNC:84 HPRD:01938 MIM:200350 Vega:OTTHUMG00000133064 Other designations: ACC-alpha|acetyl-CoA carboxylase 1|acetyl-Coenzyme A carboxylase alpha ACACA OGG:3000000032 Bin Zhao, Yue Liu, Oliver He ACC2 ACCB HACC275 WEB: http://www.ncbi.nlm.nih.gov/gene ACACB acetyl-CoA carboxylase beta 32 12q24.11 9606 12 Official from a nomenclature committee GO_0003989 (EC: IDA); GO_0004075 (EC: IEA); GO_0005515 (EC: IPI, PMID: 16794074); GO_0005524 (EC: IEA); GO_0005741 (EC: TAS); GO_0005829 (EC: TAS); GO_0006084 (EC: IDA); GO_0006112 (EC: TAS); GO_0006633 (EC: IEA); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0006768 (EC: TAS); GO_0006853 (EC: TAS); GO_0009374 (EC: IEA); GO_0012505 (EC: IEA); GO_0014070 (EC: IEA); GO_0031325 (EC: TAS); GO_0042493 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0046872 (EC: IEA); GO_0051289 (EC: IDA); GO_2001295 (EC: IEA) PMID: 8670171; 8876158; 9099716; 9148944; 9284908; 10677481; 11257506; 12086953; 12413941; 12477932; 14532170; 14613924; 14627750; 15060529; 15590647; 16054041; 16794074; 16854592; 17223360; 17521700; 18029348; 18031993; 18455495; 18976975; 18996102; 19034549; 19190759; 19322201; 19390150; 19618481; 19720090; 19846279; 19900410; 20085763; 20139635; 20168990; 20379614; 20468064; 20514549; 20519229; 20599696; 20602615; 20799892; 20855566; 20877624; 20965718; 21139048; 21344388; 21553357; 21887335; 21906983; 21908218; 21953464; 23081748; 23156397; 23455922; 23460794; 24255178 acetyl-CoA carboxylase beta Ensembl:ENSG00000076555 HGNC:85 HPRD:07044 MIM:601557 Vega:OTTHUMG00000169250 Other designations: ACC-beta|acetyl-CoA carboxylase 2|acetyl-Coenzyme A carboxylase beta ACACB OGG:3000000051 Bin Zhao, Yue Liu, Oliver He ACOX PALMCOX SCOX WEB: http://www.ncbi.nlm.nih.gov/gene ACOX1 acyl-CoA oxidase 1, palmitoyl 51 17q25.1 9606 17 GO_0000038 (EC: IMP, PMID:18536048); GO_0003995 (EC: IEA); GO_0003997 (EC: IDA, PMID:8117268); GO_0003997 (EC: IGI, PMID:17458872); GO_0003997 (EC: IMP, PMID:18536048); GO_0003997 (EC: TAS); GO_0005102 (EC: IPI); GO_0005504 (EC: IEA); GO_0005739 (EC: IEA); GO_0005777 (EC: IDA, PMID:17881773); GO_0005778 (EC: IEA); GO_0005782 (EC: TAS); GO_0006091 (EC: IMP, PMID:7876265); GO_0006629 (EC: IDA, PMID:8117268); GO_0006693 (EC: IMP, PMID:7876265); GO_0007283 (EC: IEA); GO_0016401 (EC: IDA, PMID:17603022); GO_0016401 (EC: IEA); GO_0016559 (EC: IGI); GO_0019395 (EC: IGI); GO_0019395 (EC: IMP, PMID:7876265); GO_0030165 (EC: IDA); GO_0033540 (EC: IEA); GO_0033540 (EC: IMP, PMID:18536048); GO_0033540 (EC: TAS); GO_0033559 (EC: TAS); GO_0036109 (EC: TAS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0047485 (EC: IPI, PMID:18281296); GO_0050660 (EC: IEA); GO_0055088 (EC: IDA); GO_0055088 (EC: IGI); GO_0071949 (EC: IDA, PMID:17603022); GO_2000189 (EC: IGI) PMID:1464743; 7668838; 7876265; 8040306; 8117268; 8125298; 8159712; 8507686; 8798738; 10856712; 10960480; 11076863; 11230166; 11815777; 12477932; 14702039; 15489334; 15489336; 16381901; 16396496; 16756494; 17081983; 17458872; 17603022; 17881773; 18281296; 18536048; 18660489; 20178365; 20195242; 21139048; 22002062; 22939629 acyl-CoA oxidase 1, palmitoyl Ensembl:ENSG00000161533 HGNC:119 HPRD:02030 MIM:609751 Vega:OTTHUMG00000180027 Other designations: AOX|acyl-CoA oxidase, straight-chain|acyl-Coenzyme A oxidase 1, palmitoyl|palmitoyl-CoA oxidase|peroxisomal acyl-coenzyme A oxidase 1|peroxisomal fatty acyl-CoA oxidase|straight-chain acyl-CoA oxidase ACOX1 OGG:3000000101 Bin Zhao, Yue Liu, Oliver He CD156 CD156a MS2 WEB: http://www.ncbi.nlm.nih.gov/gene ADAM8 ADAM metallopeptidase domain 8 101 10q26.3 9606 10 Official from a nomenclature committee GO_0000902 (EC: ISS); GO_0001525 (EC: ISS); GO_0002102 (EC: IDA, PMID: 15220135); GO_0002523 (EC: ISS); GO_0002675 (EC: ISS); GO_0004222 (EC: IEA); GO_0005509 (EC: ISS); GO_0005515 (EC: IPI, PMID: 12777399); GO_0005737 (EC: IDA, PMID: 18397961); GO_0005886 (EC: IDA, PMID: 17548643); GO_0005886 (EC: TAS); GO_0005887 (EC: IDA, PMID: 18397961); GO_0006954 (EC: IDA, PMID: 17548643); GO_0008237 (EC: IDA, PMID: 12777399); GO_0008270 (EC: TAS, PMID: 18397961); GO_0009986 (EC: IDA, PMID: 17548643); GO_0010954 (EC: NAS, PMID: 17548643); GO_0016337 (EC: IEA); GO_0022407 (EC: IDA, PMID: 17548643); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0032010 (EC: IDA, PMID: 17548643); GO_0032127 (EC: IDA, PMID: 17548643); GO_0033089 (EC: ISS); GO_0035419 (EC: ISS); GO_0042581 (EC: IDA, PMID: 17548643); GO_0043524 (EC: ISS); GO_0043621 (EC: TAS, PMID: 12777399); GO_0045780 (EC: ISS); GO_0045785 (EC: ISS); GO_0048247 (EC: ISS); GO_0050714 (EC: IC, PMID: 17548643); GO_0050839 (EC: IPI, PMID: 12777399); GO_0051044 (EC: IDA, PMID: 15220135); GO_0051092 (EC: ISS); GO_0051897 (EC: ISS); GO_0070245 (EC: ISS); GO_0070820 (EC: IDA, PMID: 17548643); GO_0071065 (EC: IDA, Qualifier: colocalizes_with, PMID: 15220135); GO_0071133 (EC: ISS); GO_0071456 (EC: IDA, PMID: 18566576); GO_2000309 (EC: ISS); GO_2000391 (EC: IDA, PMID: 17548643); GO_2000415 (EC: ISS); GO_2000418 (EC: ISS) PMID: 9126482; 10354553; 12135759; 12477932; 12777399; 15220135; 15574124; 15623614; 16344560; 16385451; 17339047; 17548643; 17979891; 18397961; 18566576; 18682798; 18691140; 18710625; 18811590; 19284887; 19397475; 19469654; 19575316; 19601829; 19714641; 19766586; 20453887; 20628624; 21077325; 21640993; 21679521; 21728902; 21983884; 22215309; 22229154; 22878099; 22941466; 22959284; 22965687; 23670189 ADAM metallopeptidase domain 8 Ensembl:ENSG00000151651 HGNC:215 HPRD:03777 MIM:602267 Vega:OTTHUMG00000019309 Other designations: a disintegrin and metalloproteinase domain 8|cell surface antigen MS2|disintegrin and metalloproteinase domain-containing protein 8|human leukocyte differentiation antigen ADAM8 OGG:3000000123 Bin Zhao, Yue Liu, Oliver He ADFP ADRP WEB: http://www.ncbi.nlm.nih.gov/gene PLIN2 perilipin 2 123 RP11-151J10.1 9p22.1 9606 9 Official from a nomenclature committee GO_0005576 (EC: TAS, PMID: 9003395); GO_0005634 (EC: IEA); GO_0005783 (EC: TAS, PMID: 9003395); GO_0005811 (EC: IDA, PMID: 14741744); GO_0005886 (EC: TAS); GO_0014070 (EC: IEA); GO_0015909 (EC: IEA); GO_0019915 (EC: IEA); GO_0042493 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS) PMID: 1518805; 7829101; 9003395; 9799447; 12114189; 12387890; 12477932; 12591929; 14671211; 14707038; 14741744; 15136565; 15146197; 15336557; 15489334; 15545278; 16230742; 16391323; 16489205; 16808905; 16884492; 16936283; 17200350; 17322100; 17446422; 17620659; 17927964; 18188946; 18393390; 18606814; 18624398; 18827892; 18832575; 19054096; 19169702; 19351497; 19460752; 19602560; 19638644; 19843633; 19851831; 20032580; 20118912; 20143336; 20504295; 20661576; 20887090; 21566511; 21828233; 21906983; 22238364; 22496505; 22667335; 22949030; 22952953; 23129790; 23603836; 23688400 perilipin 2 Ensembl:ENSG00000147872 HGNC:248 HPRD:00057 MIM:103195 Vega:OTTHUMG00000019624 Other designations: adipophilin|adipose differentiation-related protein|perilipin-2 PLIN2 OGG:3000000125 Bin Zhao, Yue Liu, Oliver He ADH2 HEL-S-117 WEB: http://www.ncbi.nlm.nih.gov/gene ADH1B alcohol dehydrogenase 1B (class I), beta polypeptide 125 4q23 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0004024 (EC: IDA, PMID: 9982); GO_0005829 (EC: TAS); GO_0006069 (EC: IDA, PMID: 2398055); GO_0006069 (EC: TAS); GO_0006805 (EC: TAS); GO_0008270 (EC: IDA, PMID: 9982); GO_0044281 (EC: TAS) PMID: 9982; 1896463; 2169444; 2210383; 2295648; 2347582; 2398055; 2547609; 2679216; 2737681; 2935533; 2935875; 2986130; 3000832; 3006456; 3397059; 3619918; 6374651; 6391920; 8201622; 8663387; 8889548; 10424757; 10733556; 11051375; 11117576; 11238183; 11259352; 11274460; 11398342; 11410735; 11584144; 11696658; 11748356; 11781503; 11781511; 11966948; 12080432; 12081471; 12089173; 12153842; 12173598; 12189549; 12211622; 12213289; 12244546; 12351924; 12419833; 12452180; 12461493; 12477932; 12505800; 12517056; 12519453; 12545748; 12554615; 12658118; 12668919; 12710951; 12713190; 12777946; 12824748; 12884000; 12915514; 12915519; 14634838; 14693654; 14745297; 14768474; 15084894; 15162847; 15220553; 15318096; 15318112; 15327835; 15342556; 15456134; 15489334; 15511718; 15519646; 15534263; 15542751; 15597094; 15842823; 15863807; 15886702; 15902904; 15957670; 16006997; 16078602; 16086315; 16117582; 16127737; 16135443; 16163053; 16184481; 16235983; 16307179; 16309369; 16324524; 16332725; 16358724; 16385179; 16404797; 16423594; 16440362; 16520888; 16600530; 16608143; 16685648; 16702384; 16737450; 16758956; 16822169; 16930209; 16958672; 16970620; 17036331; 17071628; 17134659; 17134660; 17180580; 17185388; 17207821; 17250612; 17268812; 17279314; 17285601; 17289126; 17292341; 17293864; 17295732; 17421009; 17454860; 17471563; 17486761; 17489985; 17515815; 17517051; 17559546; 17618743; 17631643; 17762315; 17847010; 17850643; 17885622; 17923853; 17963305; 18033686; 18049455; 18056758; 18078815; 18216179; 18254707; 18266839; 18299763; 18322963; 18331377; 18336668; 18336671; 18382665; 18439068; 18500343; 18510611; 18516948; 18715275; 18761854; 18763293; 18773092; 18782342; 18784359; 18818748; 18936436; 18996923; 19019335; 19068087; 19094228; 19124091; 19124506; 19164089; 19185835; 19193628; 19250143; 19262484; 19298323; 19339270; 19343046; 19365573; 19403456; 19420105; 19449376; 19452585; 19469618; 19486361; 19527514; 19550411; 19618839; 19655364; 19667493; 19687126; 19698717; 19706845; 19751749; 19769429; 19799139; 19812523; 19826048; 19860798; 19861527; 19874574; 19887496; 19898482; 19913121; 19948975; 20010786; 20025435; 20031627; 20077761; 20101753; 20140262; 20171022; 20180859; 20205700; 20219057; 20336794; 20357489; 20401433; 20403997; 20437850; 20462248; 20477764; 20477767; 20494945; 20568895; 20598484; 20628086; 20634891; 20685249; 20700531; 20806441; 20833657; 21048924; 21133627; 21157980; 21166830; 21168396; 21284671; 21303386; 21351086; 21355870; 21378355; 21437268; 21497796; 21517275; 21576033; 21601984; 21635275; 21895720; 21917409; 21968928; 21988832; 22004471; 22048268; 22150722; 22231434; 22287615; 22292652; 22325912; 22363810; 22560290; 22674868; 22690706; 22703580; 22930414; 22931071; 22960999; 23149980; 23266708; 23285246; 23296215; 23414439; 23456092; 23468174; 23550892; 23615284; 23701534; 23743675; 23806636; 24217933 alcohol dehydrogenase 1B (class I), beta polypeptide HGNC:250 HPRD:00065 MIM:103720 Other designations: ADH, beta subunit|alcohol dehydrogenase 1B|alcohol dehydrogenase 2 (class I), beta polypeptide|alcohol dehydrogenase subunit beta|aldehyde reductase|epididymis secretory protein Li 117 ADH1B OGG:3000000185 Bin Zhao, Yue Liu, Oliver He AG2S AGTR1B AT1 AT1AR AT1B AT1BR AT1R AT2R1 HAT1R WEB: http://www.ncbi.nlm.nih.gov/gene AGTR1 angiotensin II receptor, type 1 185 3q24 20140408 9606 3 protein-coding Official from a nomenclature committee GO_0001558 (EC: NAS, PMID: 17159080); GO_0001596 (EC: IDA, PMID: 10993080); GO_0001596 (EC: IPI, PMID: 1378723); GO_0001822 (EC: IMP, PMID: 16116425); GO_0002018 (EC: NAS, PMID: 17159080); GO_0002034 (EC: IC, PMID: 10993080); GO_0003081 (EC: IC, PMID: 1378723); GO_0004945 (EC: IDA, PMID: 15611106); GO_0005515 (EC: IPI, PMID: 1378723); GO_0005886 (EC: IDA, PMID: 19023134); GO_0005886 (EC: TAS); GO_0005887 (EC: IC, PMID: 1378723); GO_0007186 (EC: IDA, PMID: 1378723); GO_0007200 (EC: NAS, PMID: 17159080); GO_0007204 (EC: IDA, PMID: 1567413); GO_0007266 (EC: IDA, PMID: 15611106); GO_0010744 (EC: IC, PMID: 18971559); GO_0010873 (EC: IMP, PMID: 18971559); GO_0016021 (EC: NAS, PMID: 8135787); GO_0019229 (EC: IC, PMID: 1378723); GO_0019229 (EC: IDA, PMID: 15117835); GO_0019229 (EC: NAS, PMID: 17159080); GO_0019722 (EC: IDA, PMID: 1567413); GO_0031711 (EC: IPI, PMID: 10993080); GO_0032270 (EC: IMP, PMID: 18971559); GO_0032430 (EC: IMP, PMID: 17069818); GO_0033864 (EC: TAS, PMID: 17159080); GO_0034374 (EC: NAS, PMID: 17069818); GO_0035813 (EC: NAS, PMID: 17159080); GO_0038166 (EC: IDA, PMID: 15611106); GO_0042127 (EC: NAS, PMID: 17159080); GO_0042312 (EC: IC, PMID: 1378723); GO_0046982 (EC: IPI, PMID: 10993080); GO_0050727 (EC: IC, PMID: 1378723); GO_0050729 (EC: TAS, PMID: 17159080); GO_0051482 (EC: IDA, PMID: 1567413); GO_0060326 (EC: IDA, PMID: 15635042); GO_0086097 (EC: IDA, PMID: 10993080); GO_0086097 (EC: IPI, PMID: 1378723); GO_2000379 (EC: TAS, PMID: 17159080) PMID: 1378723; 1508224; 1543512; 1550596; 1567413; 1683828; 7491117; 7746328; 7792812; 7980575; 8021009; 8135787; 8166699; 8185574; 8662816; 8753867; 9074770; 9211925; 9468203; 9516477; 9606715; 9766385; 10510297; 10972591; 10993080; 11079515; 11081769; 11082147; 11085286; 11106322; 11110972; 11122322; 11136175; 11137090; 11152457; 11158334; 11208365; 11213892; 11226259; 11246471; 11250978; 11279203; 11288810; 11289708; 11317203; 11324803; 11330506; 11336183; 11341749; 11354780; 11355019; 11359462; 11444146; 11484170; 11531970; 11575217; 11577832; 11579203; 11593098; 11682489; 11687736; 11688760; 11689223; 11692158; 11696658; 11696688; 11707217; 11707686; 11709400; 11709801; 11711524; 11733189; 11752456; 11774217; 11775887; 11776100; 11793101; 11793845; 11798574; 11799082; 11852019; 11865575; 11881039; 11882570; 11903322; 11909563; 11910300; 11910301; 11913624; 11923700; 11924723; 11926202; 11938025; 11967817; 11999641; 12006574; 12031955; 12034692; 12045255; 12048678; 12095411; 12117739; 12127057; 12133421; 12133518; 12187084; 12358135; 12390711; 12394950; 12425365; 12436935; 12446192; 12446598; 12450401; 12454231; 12460700; 12473660; 12476891; 12477932; 12482634; 12511523; 12513040; 12514663; 12522132; 12522467; 12534336; 12544439; 12544508; 12556231; 12579398; 12579405; 12591176; 12593997; 12597535; 12624609; 12627871; 12627873; 12631360; 12660887; 12694873; 12694874; 12695419; 12716844; 12728975; 12747597; 12778448; 12832734; 12842881; 12860335; 12865608; 12891302; 12897464; 12898858; 12904590; 12925562; 12932862; 12950120; 12960024; 14502296; 14508191; 14521778; 14529856; 14530292; 14569094; 14597852; 14610337; 14627489; 14654250; 14657020; 14730619; 14749533; 14764974; 14765837; 14767013; 14987254; 14997233; 15013293; 15013322; 15013333; 15017542; 15031629; 15042429; 15045574; 15062885; 15080371; 15097234; 15108186; 15117835; 15126556; 15130920; 15153745; 15193870; 15193960; 15196067; 15212666; 15221785; 15238568; 15269283; 15295089; 15326089; 15332573; 15353577; 15355986; 15364762; 15376229; 15385810; 15452107; 15452121; 15454732; 15458433; 15480097; 15480098; 15492474; 15496309; 15498133; 15498791; 15498833; 15504143; 15505642; 15543360; 15545271; 15545843; 15563875; 15580058; 15590451; 15611106; 15612584; 15628301; 15635042; 15662219; 15673342; 15676177; 15683714; 15694792; 15718424; 15718497; 15743363; 15775779; 15785027; 15797649; 15824464; 15848528; 15863668; 15890659; 15905345; 15914614; 15923814; 15930094; 15934435; 15946912; 15949885; 16006956; 16012192; 16047641; 16061119; 16076618; 16088850; 16105049; 16108768; 16109085; 16109807; 16109907; 16112405; 16116425; 16152821; 16188060; 16189286; 16231503; 16271939; 16274774; 16276415; 16294326; 16314886; 16339777; 16344560; 16364240; 16369102; 16384824; 16395664; 16396964; 16398146; 16434990; 16468060; 16492203; 16498788; 16504375; 16519598; 16521052; 16522324; 16525943; 16525944; 16530863; 16550310; 16565729; 16603315; 16609364; 16611642; 16615274; 16636899; 16651460; 16672053; 16684954; 16685579; 16691016; 16736244; 16741369; 16741935; 16754659; 16775386; 16787961; 16790149; 16805920; 16823505; 16831865; 16876684; 16893516; 16911325; 16923768; 16954165; 16998258; 17008309; 17024648; 17051401; 17069818; 17097490; 17118372; 17118790; 17118791; 17143591; 17146658; 17159080; 17160213; 17165166; 17166941; 17173513; 17190732; 17207964; 17211247; 17211857; 17220293; 17223428; 17227479; 17229913; 17256744; 17261659; 17270098; 17274465; 17285438; 17293603; 17298481; 17299793; 17325239; 17326392; 17327458; 17334527; 17336987; 17375465; 17378368; 17393691; 17399955; 17429042; 17433630; 17446269; 17446655; 17486447; 17487826; 17499413; 17519002; 17520398; 17522061; 17524880; 17541127; 17546276; 17557241; 17569300; 17586411; 17586781; 17595257; 17617024; 17668390; 17702963; 17703434; 17710578; 17719203; 17725712; 17726226; 17728799; 17785770; 17851694; 17903694; 17914507; 17921131; 17921431; 17921816; 17984617; 17988266; 17992634; 17993594; 18006496; 18026817; 18059164; 18069999; 18088317; 18091746; 18158351; 18172057; 18188697; 18202720; 18205094; 18231736; 18239157; 18239384; 18240029; 18245065; 18260840; 18261537; 18296263; 18308844; 18328310; 18331441; 18347611; 18348177; 18364271; 18413189; 18413222; 18413308; 18414380; 18417209; 18432064; 18434621; 18446309; 18464745; 18464932; 18475152; 18488444; 18491423; 18497458; 18513389; 18534055; 18550062; 18550936; 18551012; 18563171; 18565507; 18575418; 18577758; 18594050; 18594540; 18612202; 18622242; 18633425; 18637188; 18641512; 18660489; 18676046; 18679149; 18698212; 18700314; 18703536; 18719072; 18767410; 18787507; 18787943; 18800139; 18830250; 18855530; 18856058; 18927546; 18953568; 18971559; 18974842; 18985387; 19014923; 19017652; 19021695; 19023134; 19023273; 19026696; 19040540; 19056482; 19057513; 19059460; 19064815; 19067809; 19082699; 19086053; 19102886; 19108684; 19110485; 19112833; 19131662; 19145770; 19162241; 19162259; 19166692; 19178574; 19185300; 19218102; 19236533; 19238444; 19242491; 19245071; 19247266; 19253715; 19254215; 19263529; 19274051; 19274077; 19276075; 19282863; 19286758; 19286759; 19288324; 19302184; 19304510; 19308748; 19309260; 19327134; 19330904; 19332265; 19341158; 19397700; 19408837; 19418628; 19420105; 19424575; 19461648; 19463113; 19479237; 19487683; 19503013; 19509012; 19520069; 19524223; 19546528; 19559392; 19578796; 19587357; 19593696; 19620885; 19635801; 19680137; 19681973; 19696781; 19706169; 19713412; 19716087; 19729965; 19752885; 19755917; 19779016; 19779330; 19779464; 19782519; 19811349; 19833117; 19853701; 19913121; 19929134; 19940150; 19948975; 19954723; 19956635; 19997001; 20026870; 20027122; 20066125; 20080265; 20108069; 20118823; 20137558; 20142115; 20161734; 20181817; 20223791; 20223792; 20300066; 20302034; 20304486; 20308035; 20351714; 20361261; 20452482; 20458733; 20465154; 20478903; 20486282; 20525211; 20536507; 20537417; 20537563; 20558762; 20559404; 20560294; 20563831; 20565774; 20570668; 20577119; 20580725; 20594303; 20602615; 20606419; 20628086; 20659024; 20667857; 20673868; 20703234; 20708651; 20714875; 20731749; 20732682; 20816596; 20824505; 20837730; 20838438; 20851291; 20854100; 20854388; 20856803; 20861505; 20864943; 20943774; 20945417; 20966899; 20975235; 20978160; 21052031; 21086617; 21152433; 21162207; 21163122; 21173159; 21176342; 21223556; 21234519; 21234654; 21316998; 21319597; 21330421; 21332426; 21412239; 21436209; 21449976; 21463477; 21502318; 21525005; 21570644; 21596033; 21600887; 21607620; 21628354; 21633717; 21636204; 21638051; 21641389; 21670585; 21671168; 21740964; 21771600; 21791198; 21808598; 21846682; 21856918; 21937042; 21970881; 21986569; 22021115; 22147663; 22237156; 22282354; 22291018; 22297600; 22323719; 22362742; 22387727; 22392878; 22407459; 22433249; 22475523; 22484478; 22555639; 22561363; 22569962; 22581182; 22590832; 22613986; 22645060; 22647632; 22703619; 22719026; 22758920; 22782431; 22939041; 23081748; 23145508; 23176211; 23210602; 23223579; 23273598; 23326349; 23386604; 23389452; 23451270; 23480300; 23480670; 23484035; 23505107; 23536940; 23564192; 23567951; 23585396; 23592774; 23603059; 23615648; 23681235; 23694962; 23700157; 23745680; 23755207; 23828384; 23880184; 23942655; 24015270; 24055489; 24202179; 24218433; 24400721 angiotensin II receptor, type 1 Ensembl:ENSG00000144891 HGNC:336 HPRD:00107 MIM:106165 Vega:OTTHUMG00000159503 AGTR1 OGG:3000000196 Bin Zhao, Yue Liu, Oliver He bHLHe76 WEB: http://www.ncbi.nlm.nih.gov/gene AHR aryl hydrocarbon receptor 196 7p15 9606 7 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0001568 (EC: NAS, PMID: 19538249); GO_0003677 (EC: IDA, PMID: 15681594); GO_0003677 (EC: TAS, PMID: 19538249); GO_0003700 (EC: IDA, PMID: 11782478); GO_0003705 (EC: IEA); GO_0004871 (EC: IEA); GO_0004879 (EC: IDA, PMID: 10395741); GO_0005515 (EC: IPI, PMID: 10395741); GO_0005634 (EC: IDA); GO_0005667 (EC: TAS, PMID: 19538249); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0006355 (EC: IDA, PMID: 10395741); GO_0006357 (EC: IDA, PMID: 15681594); GO_0006366 (EC: IDA, PMID: 10395741); GO_0006805 (EC: TAS, PMID: 19538249); GO_0006915 (EC: TAS, PMID: 12213388); GO_0006950 (EC: IDA, PMID: 7961644); GO_0007049 (EC: TAS, PMID: 12213388); GO_0008134 (EC: IPI, PMID: 9079689); GO_0009410 (EC: IDA, PMID: 7961644); GO_0010468 (EC: IDA, PMID: 15681594); GO_0030522 (EC: IDA, PMID: 10395741); GO_0030850 (EC: IEA); GO_0030888 (EC: IDA, PMID: 15681594); GO_0034752 (EC: TAS, PMID: 19538249); GO_0043565 (EC: IEA); GO_0044212 (EC: IDA, PMID: 15681594); GO_0045899 (EC: IEA); GO_0046982 (EC: TAS, PMID: 19538249); GO_0046983 (EC: TAS, PMID: 19538249); GO_0051879 (EC: IDA, PMID: 9079689) PMID: 7488247; 7515333; 7550366; 7566098; 7628454; 7716743; 7883760; 7961644; 7961671; 8074712; 8125016; 8246913; 8384309; 8393992; 8794892; 9079689; 9083006; 9111057; 9170146; 9446600; 9704006; 9712901; 9759704; 9787404; 9837941; 9887096; 9972449; 10048154; 10395741; 10428779; 10471301; 10497241; 10620335; 10644764; 10739168; 10903152; 10986286; 10999956; 11013261; 11032419; 11114727; 11207035; 11259606; 11259609; 11259615; 11393538; 11408954; 11425848; 11505220; 11689007; 11698344; 11742002; 11756572; 11768231; 11782478; 11805098; 11835227; 11866883; 12024042; 12065584; 12139968; 12181450; 12200463; 12203118; 12213388; 12213390; 12215427; 12237327; 12477932; 12480531; 12520072; 12566446; 12586752; 12592376; 12597446; 12612060; 12637498; 12690205; 12730383; 12774124; 12837759; 12852830; 12853948; 12917420; 14550747; 14560034; 14634838; 14973392; 14978034; 14985336; 15026081; 15069065; 15123621; 15190133; 15342792; 15474075; 15489334; 15499202; 15572374; 15641800; 15681594; 15728486; 15758562; 15774926; 15837795; 15863442; 15897893; 15917307; 15964790; 16084889; 16091746; 16103451; 16109480; 16153594; 16257957; 16337337; 16403814; 16480812; 16481407; 16538170; 16582008; 16619036; 16675542; 16762319; 16891617; 16922649; 16952353; 16985026; 16985033; 17053541; 17140257; 17174437; 17200336; 17209571; 17223712; 17244640; 17311112; 17392787; 17429315; 17490615; 17498780; 17502624; 17511620; 17552871; 17559847; 17596880; 17642299; 17823287; 17823304; 17900530; 17963696; 18029348; 18037991; 18059014; 18065768; 18259752; 18302886; 18303622; 18358233; 18359762; 18433817; 18483242; 18510611; 18515748; 18524851; 18628420; 18632753; 18636124; 18676680; 18677463; 18708059; 18708364; 18818557; 18923163; 18990750; 19013013; 19018768; 19027718; 19034627; 19114668; 19138996; 19158084; 19170196; 19255421; 19333233; 19340314; 19356061; 19356098; 19358281; 19360915; 19371443; 19380484; 19390533; 19415745; 19447902; 19460354; 19463884; 19465936; 19535631; 19536146; 19538249; 19556287; 19574409; 19592671; 19625176; 19651607; 19690180; 19692168; 19726680; 19736056; 19755661; 19789301; 19815066; 19821039; 19917880; 19941898; 20000589; 20032195; 20044593; 20053997; 20064835; 20130088; 20140206; 20146706; 20171126; 20237496; 20301892; 20354149; 20395535; 20401977; 20453000; 20460431; 20511231; 20619336; 20634891; 20676092; 20709182; 20804740; 20823264; 20878756; 20973933; 21072210; 21081473; 21205295; 21262915; 21316925; 21357676; 21374063; 21441140; 21462134; 21486221; 21490707; 21600206; 21613234; 21627536; 21640702; 21689841; 21693764; 21742528; 21804081; 21828262; 21878739; 21886157; 21906983; 21963094; 21976023; 21987572; 21988832; 21996739; 22052373; 22053597; 22071320; 22123295; 22138065; 22235307; 22273977; 22296396; 22311706; 22361730; 22388733; 22486318; 22495716; 22495806; 22539616; 22553215; 22596188; 22628113; 22649193; 22728919; 22754483; 22759865; 22761424; 22840970; 22854411; 22903824; 22915253; 23022626; 23030067; 23037589; 23141164; 23208493; 23228475; 23229511; 23288144; 23317198; 23370907; 23382382; 23419638; 23430108; 23439269; 23452206; 23492908; 23528250; 23583297; 23604401; 23614276; 23614742; 23723449; 23733406; 23802610; 23831623; 23994556; 24023334; 24091107; 24106308; 24302727; 24309559; 24316275; 24355420; 24380854 aryl hydrocarbon receptor Ensembl:ENSG00000106546 HGNC:348 HPRD:02596 MIM:600253 Vega:OTTHUMG00000149967 Other designations: AH-receptor|ah receptor|aromatic hydrocarbon receptor|class E basic helix-loop-helix protein 76 AHR OGG:3000000207 Bin Zhao, Yue Liu, Oliver He AKT CWS6 PKB PKB-ALPHA PRKBA RAC RAC-ALPHA WEB: http://www.ncbi.nlm.nih.gov/gene AKT1 v-akt murine thymoma viral oncogene homolog 1 207 14q32.32 9606 14 Official from a nomenclature committee GO_0000060 (EC: IMP, PMID: 16280327); GO_0001649 (EC: IEA); GO_0001893 (EC: IEA); GO_0001934 (EC: IDA, PMID: 19057511); GO_0001938 (EC: IMP, PMID: 19850054); GO_0004672 (EC: TAS, PMID: 10570282); GO_0004674 (EC: IDA, PMID: 10102273); GO_0004674 (EC: TAS); GO_0005080 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11154276); GO_0005524 (EC: IC, PMID: 11994271); GO_0005524 (EC: IDA, PMID: 16540465); GO_0005547 (EC: IDA, PMID: 19203586); GO_0005634 (EC: IDA); GO_0005634 (EC: TAS); GO_0005654 (EC: TAS); GO_0005737 (EC: IDA, PMID: 19203586); GO_0005737 (EC: ISS); GO_0005737 (EC: TAS); GO_0005819 (EC: IEA); GO_0005829 (EC: IDA); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA, PMID: 14749367); GO_0005886 (EC: TAS); GO_0005978 (EC: IEA); GO_0005979 (EC: IMP, PMID: 8940145); GO_0006006 (EC: IEA); GO_0006412 (EC: IEA); GO_0006417 (EC: IEA); GO_0006464 (EC: TAS, PMID: 10570282); GO_0006468 (EC: IDA, PMID: 11994271); GO_0006469 (EC: IMP, PMID: 9373175); GO_0006469 (EC: ISS); GO_0006809 (EC: TAS, PMID: 10376602); GO_0006915 (EC: TAS); GO_0006924 (EC: IMP, PMID: 14749367); GO_0006954 (EC: IEA); GO_0007165 (EC: TAS); GO_0007173 (EC: TAS); GO_0007186 (EC: TAS, PMID: 10570282); GO_0007281 (EC: IEA); GO_0007568 (EC: IEA); GO_0007596 (EC: TAS); GO_0008283 (EC: TAS); GO_0008286 (EC: IMP, PMID: 8978681); GO_0008543 (EC: TAS); GO_0008637 (EC: IEA); GO_0009408 (EC: TAS, PMID: 10958679); GO_0010467 (EC: TAS); GO_0010507 (EC: IMP, PMID: 18387192); GO_0010748 (EC: IMP, PMID: 16814735); GO_0010765 (EC: IEA); GO_0010907 (EC: IMP, PMID: 16814735); GO_0010951 (EC: IMP, PMID: 18387192); GO_0010975 (EC: ISS); GO_0015630 (EC: IDA); GO_0015758 (EC: IEA); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016301 (EC: IDA, PMID: 14749367); GO_0016310 (EC: IDA); GO_0016567 (EC: IEA); GO_0018105 (EC: IDA, PMID: 16139227); GO_0019899 (EC: ISS); GO_0030030 (EC: IEA); GO_0030154 (EC: TAS); GO_0030163 (EC: IEA); GO_0030168 (EC: TAS); GO_0030212 (EC: IEA); GO_0030235 (EC: IMP, PMID: 10376603); GO_0030307 (EC: IDA, PMID: 19203586); GO_0030334 (EC: IMP, PMID: 19934221); GO_0030334 (EC: TAS); GO_0031018 (EC: TAS); GO_0031295 (EC: TAS); GO_0031659 (EC: IDA, PMID: 18483258); GO_0031999 (EC: IMP, PMID: 16814735); GO_0032094 (EC: IEA); GO_0032270 (EC: ISS); GO_0032287 (EC: IEA); GO_0032436 (EC: IEA); GO_0032869 (EC: IMP, PMID: 16814735); GO_0032869 (EC: ISS); GO_0033138 (EC: IDA, PMID: 19667065); GO_0034405 (EC: IMP, PMID: 10376603); GO_0035556 (EC: IDA, PMID: 14749367); GO_0038095 (EC: TAS); GO_0042593 (EC: IEA); GO_0042640 (EC: IEA); GO_0042802 (EC: IPI, PMID: 7891724); GO_0043065 (EC: IEA); GO_0043066 (EC: IDA, PMID: 19203586); GO_0043154 (EC: ISS); GO_0043325 (EC: IDA, PMID: 19203586); GO_0043491 (EC: IEA); GO_0043536 (EC: IDA); GO_0044281 (EC: TAS); GO_0045087 (EC: TAS); GO_0045429 (EC: IMP, PMID: 10376603); GO_0045600 (EC: IMP, PMID: 8940145); GO_0045725 (EC: IMP, PMID: 16814735); GO_0045725 (EC: NAS, PMID: 17925406); GO_0045792 (EC: IEA); GO_0045861 (EC: IMP, PMID: 18387192); GO_0045907 (EC: IEA); GO_0045944 (EC: IEA); GO_0046209 (EC: TAS); GO_0046326 (EC: IMP, PMID: 16814735); GO_0046329 (EC: IEA); GO_0046777 (EC: TAS, PMID: 16280327); GO_0046889 (EC: IMP, PMID: 8940145); GO_0048009 (EC: IMP, PMID: 8978681); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0050999 (EC: TAS); GO_0051000 (EC: IMP, PMID: 10376603); GO_0051091 (EC: IDA, PMID: 19057511); GO_0051146 (EC: IEA); GO_0060644 (EC: TAS); GO_0060709 (EC: IEA); GO_0060716 (EC: IEA); GO_0061024 (EC: TAS); GO_0070141 (EC: IDA, PMID: 18483258); GO_0071260 (EC: IEA); GO_0071364 (EC: IEA); GO_0071456 (EC: IEA); GO_0071889 (EC: IPI, PMID: 10102273); GO_0090004 (EC: IMP, PMID: 8940145); GO_0090201 (EC: ISS); GO_0097193 (EC: TAS); GO_0097194 (EC: IEA); GO_1900740 (EC: TAS); GO_1901976 (EC: TAS); GO_1902176 (EC: NAS, PMID: 16604263); GO_2001240 (EC: TAS, PMID: 10748004) PMID: 1533586; 1718748; 1851997; 3037531; 3384441; 7774014; 7891724; 8524413; 8940145; 8978681; 9005852; 9019819; 9312003; 9368760; 9373175; 9381178; 9394803; 9395488; 9512493; 9736715; 9768361; 9812896; 9829964; 9973250; 10082674; 10085094; 10102273; 10217147; 10224060; 10226025; 10358014; 10376602; 10376603; 10438924; 10454575; 10485710; 10485711; 10490823; 10490848; 10491192; 10497255; 10527852; 10542266; 10570282; 10576742; 10617634; 10635328; 10698680; 10748004; 10833263; 10866658; 10869359; 10869418; 10872470; 10896934; 10910062; 10926925; 10930578; 10958679; 10983986; 10995457; 11035810; 11042204; 11116148; 11139588; 11154276; 11154281; 11156376; 11156964; 11162552; 11208609; 11274386; 11278835; 11278894; 11313365; 11313479; 11404460; 11410590; 11410591; 11425855; 11438723; 11445557; 11500364; 11504915; 11508278; 11509608; 11535620; 11546794; 11579209; 11583630; 11585925; 11598301; 11689711; 11696579; 11707444; 11707464; 11710897; 11715018; 11723139; 11756412; 11773441; 11777913; 11782427; 11809791; 11825911; 11828257; 11855836; 11877387; 11884598; 11902142; 11903042; 11923280; 11956222; 11960368; 11976320; 11994271; 11994280; 12009899; 12011046; 12042314; 12062056; 12062094; 12070137; 12077256; 12112022; 12124386; 12138087; 12138205; 12145204; 12149249; 12150915; 12167664; 12167717; 12176337; 12176338; 12176997; 12194869; 12218048; 12244133; 12244301; 12244302; 12244303; 12297295; 12376533; 12393747; 12438239; 12446767; 12446787; 12446789; 12458207; 12477932; 12524439; 12527373; 12529294; 12535517; 12586360; 12592338; 12621049; 12637511; 12722480; 12727836; 12734380; 12741986; 12750378; 12757707; 12768030; 12782295; 12783873; 12791994; 12808085; 12808093; 12853467; 12874217; 12888921; 12919677; 12952968; 12972603; 14499622; 14500673; 14505491; 14520710; 14523021; 14534536; 14560023; 14566704; 14568991; 14611643; 14612949; 14623889; 14625285; 14636889; 14645242; 14645548; 14647146; 14657000; 14679206; 14702039; 14713953; 14742298; 14749367; 14749388; 14749719; 14755253; 14761976; 14970221; 14973226; 14985374; 15001646; 15010337; 15016818; 15026145; 15047604; 15047866; 15060171; 15067058; 15102693; 15115729; 15118108; 15136501; 15146197; 15149849; 15156201; 15173318; 15183529; 15187088; 15187138; 15194442; 15203190; 15217935; 15231831; 15242771; 15262962; 15262978; 15263908; 15271644; 15283964; 15284024; 15306850; 15316080; 15326564; 15331441; 15342781; 15342917; 15385469; 15388791; 15389633; 15459205; 15465021; 15467757; 15470047; 15475446; 15489334; 15492215; 15522255; 15525681; 15527798; 15533996; 15539407; 15545269; 15545271; 15545519; 15546863; 15572689; 15574337; 15580267; 15581622; 15607733; 15609321; 15616007; 15665327; 15665818; 15668028; 15678105; 15688030; 15689238; 15705789; 15710591; 15718470; 15722337; 15723049; 15743789; 15778376; 15784622; 15800029; 15802268; 15806160; 15808505; 15809304; 15817639; 15818404; 15831676; 15833736; 15837948; 15840729; 15843522; 15845076; 15845651; 15856005; 15861136; 15879168; 15888491; 15896313; 15896703; 15905178; 15910284; 15911620; 15922745; 15961723; 15982448; 15987444; 15993382; 15994200; 15998799; 16007092; 16007163; 16007172; 16007182; 16009706; 16012720; 16019536; 16026766; 16027121; 16027165; 16027169; 16036916; 16049004; 16049961; 16055703; 16076959; 16091017; 16098514; 16099944; 16107690; 16114056; 16115861; 16123141; 16128748; 16139227; 16141217; 16142341; 16148125; 16160160; 16163388; 16174774; 16177823; 16186112; 16202996; 16210317; 16216590; 16224021; 16243840; 16263580; 16272144; 16274701; 16278380; 16280327; 16282323; 16293694; 16338927; 16354698; 16362038; 16365168; 16373405; 16395129; 16405925; 16407258; 16407271; 16412424; 16417524; 16428439; 16434970; 16453020; 16466644; 16474850; 16478297; 16508008; 16524887; 16532026; 16532036; 16537497; 16540465; 16543232; 16549426; 16551632; 16564100; 16568092; 16571745; 16583435; 16601838; 16603397; 16604263; 16613989; 16616456; 16644866; 16651639; 16670089; 16682946; 16684529; 16723503; 16732486; 16763222; 16774943; 16775835; 16785234; 16790501; 16790529; 16792529; 16797529; 16814735; 16818690; 16820098; 16820947; 16822839; 16836907; 16839745; 16840713; 16841089; 16842970; 16844778; 16849522; 16862180; 16897758; 16912864; 16916907; 16926151; 16932738; 16946008; 16951146; 16962653; 16972255; 16977260; 16981720; 16982329; 16987028; 16987250; 16988010; 16990258; 17006541; 17006756; 17008323; 17012749; 17015676; 17016437; 17024099; 17030608; 17041888; 17043653; 17050554; 17052453; 17060455; 17065200; 17068339; 17081983; 17088265; 17097759; 17098228; 17099727; 17113264; 17128418; 17136479; 17136481; 17141917; 17143278; 17148458; 17151107; 17157319; 17169805; 17173971; 17179152; 17210635; 17214972; 17215852; 17233643; 17235455; 17244606; 17274640; 17276404; 17287851; 17299206; 17300918; 17307335; 17310852; 17317726; 17317825; 17318185; 17318262; 17333095; 17335965; 17342093; 17349711; 17351066; 17360849; 17375124; 17383860; 17386267; 17400190; 17404186; 17406055; 17428466; 17443665; 17458890; 17461449; 17462862; 17468516; 17469127; 17470458; 17471535; 17478078; 17483438; 17493174; 17495954; 17495959; 17501982; 17504381; 17505062; 17507655; 17507800; 17512923; 17513297; 17513702; 17520698; 17521720; 17522055; 17522703; 17533377; 17535800; 17544405; 17544543; 17546049; 17549359; 17551921; 17553806; 17554339; 17565979; 17566113; 17569669; 17577629; 17580302; 17581609; 17584963; 17594810; 17599831; 17599906; 17601486; 17606718; 17609269; 17611497; 17612563; 17615157; 17616681; 17616684; 17616691; 17635910; 17638918; 17666398; 17681738; 17687643; 17696196; 17706139; 17712528; 17716861; 17721885; 17721920; 17725107; 17726016; 17761832; 17804197; 17804734; 17822324; 17823925; 17825267; 17825284; 17826033; 17827393; 17855350; 17868340; 17883592; 17890457; 17891137; 17892507; 17895832; 17898861; 17901375; 17906677; 17909223; 17914025; 17914096; 17915974; 17921701; 17924977; 17925406; 17925408; 17927847; 17928528; 17932490; 17935714; 17950696; 17951252; 17957242; 17959676; 17960583; 17962807; 17977950; 18021174; 18023414; 18029348; 18035048; 18037896; 18041764; 18046412; 18048359; 18048937; 18053070; 18059161; 18063683; 18064631; 18071906; 18072631; 18079201; 18083769; 18087195; 18097023; 18167217; 18172656; 18174256; 18182168; 18182859; 18184439; 18187454; 18187620; 18191226; 18194602; 18197291; 18198266; 18199533; 18199536; 18201823; 18204201; 18204829; 18216097; 18227124; 18231751; 18240972; 18247380; 18249092; 18256540; 18262492; 18264090; 18270579; 18273051; 18292230; 18300076; 18309287; 18316593; 18317451; 18319625; 18323784; 18331557; 18332138; 18332867; 18332868; 18339899; 18351386; 18353776; 18355439; 18355897; 18356162; 18374639; 18387192; 18392055; 18395956; 18395980; 18398749; 18400376; 18404535; 18409144; 18410456; 18411301; 18413665; 18420583; 18425364; 18434090; 18437054; 18439422; 18440314; 18450971; 18451027; 18451140; 18458059; 18458087; 18466879; 18469852; 18479604; 18483258; 18483275; 18487214; 18487454; 18490760; 18495460; 18497887; 18499442; 18504432; 18505677; 18505846; 18509361; 18512729; 18519641; 18519679; 18524825; 18550470; 18552504; 18562279; 18562319; 18566587; 18574502; 18583979; 18593948; 18596081; 18606817; 18611285; 18611860; 18617528; 18622039; 18624398; 18625725; 18635704; 18635812; 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19078992; 19079342; 19091404; 19095734; 19098000; 19103742; 19107873; 19109741; 19110052; 19114998; 19115062; 19116269; 19116273; 19118218; 19124015; 19132987; 19136058; 19138978; 19142871; 19142997; 19144640; 19147496; 19147772; 19151754; 19158829; 19160403; 19162005; 19164214; 19170196; 19176054; 19176518; 19176689; 19179443; 19188658; 19193378; 19201817; 19203586; 19219602; 19219857; 19224164; 19229860; 19236051; 19239323; 19240722; 19240976; 19250936; 19250983; 19261608; 19261616; 19262695; 19267882; 19270310; 19270694; 19270695; 19276265; 19278624; 19286607; 19303863; 19318457; 19323811; 19324870; 19328625; 19339247; 19353338; 19356729; 19357198; 19367581; 19376889; 19377290; 19389506; 19405949; 19406989; 19407222; 19409087; 19415690; 19417030; 19418217; 19420344; 19428048; 19429661; 19435822; 19437103; 19447872; 19453261; 19453843; 19457567; 19458356; 19461960; 19473116; 19473971; 19479051; 19479902; 19481529; 19482076; 19483721; 19484147; 19487299; 19488783; 19489223; 19491896; 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19882362; 19885574; 19885581; 19887561; 19887570; 19889638; 19889640; 19891769; 19897009; 19898424; 19903888; 19913121; 19917135; 19920252; 19922411; 19924282; 19925030; 19926313; 19931325; 19933775; 19934221; 19935854; 19940129; 19948975; 19953087; 19954644; 19956840; 19956847; 19965664; 19966853; 19995607; 19997873; 20003467; 20005908; 20008098; 20008289; 20012528; 20018888; 20018937; 20018949; 20019835; 20019839; 20022634; 20026048; 20026773; 20028853; 20030877; 20033742; 20041213; 20041238; 20042122; 20046382; 20048146; 20053726; 20054340; 20055757; 20056178; 20059950; 20067111; 20072648; 20081374; 20086095; 20086174; 20088406; 20093341; 20098747; 20100200; 20101210; 20102399; 20103602; 20106550; 20107185; 20109457; 20110348; 20126987; 20127017; 20127709; 20132317; 20133737; 20141546; 20154081; 20157733; 20159991; 20164223; 20164304; 20173664; 20182617; 20186153; 20186503; 20187936; 20190811; 20198299; 20201953; 20214684; 20216540; 20228224; 20231902; 20232298; 20237237; 20301425; 20306497; 20307589; 20308328; 20332111; 20333297; 20333651; 20336670; 20339081; 20339252; 20346214; 20346360; 20347887; 20354121; 20360004; 20361045; 20361981; 20362557; 20368287; 20371257; 20372801; 20372806; 20383191; 20388781; 20389136; 20395438; 20398329; 20400976; 20400979; 20407443; 20410674; 20412774; 20414143; 20416077; 20417028; 20419107; 20421846; 20432460; 20432929; 20436671; 20447721; 20453000; 20457218; 20458733; 20459571; 20471940; 20478633; 20484047; 20488790; 20490331; 20492754; 20493625; 20506505; 20506537; 20509930; 20512574; 20512787; 20513428; 20514448; 20514451; 20516073; 20520724; 20523723; 20525693; 20526288; 20530239; 20530298; 20530554; 20530982; 20534535; 20536315; 20541701; 20555032; 20557351; 20560677; 20562913; 20566894; 20574456; 20578837; 20585556; 20585984; 20586915; 20592362; 20595063; 20600027; 20605778; 20607350; 20620179; 20622004; 20622047; 20623644; 20628086; 20643654; 20648653; 20651405; 20657188; 20661303; 20671123; 20672329; 20679348; 20682768; 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21757645; 21757743; 21763505; 21765914; 21767636; 21775008; 21775054; 21775285; 21775495; 21775978; 21777568; 21777670; 21778238; 21788944; 21793738; 21794903; 21799016; 21819378; 21824802; 21828040; 21828127; 21832049; 21837363; 21837670; 21840940; 21842521; 21849454; 21855541; 21856935; 21859846; 21862580; 21868077; 21869603; 21872252; 21873248; 21873430; 21874010; 21878648; 21878679; 21880746; 21881167; 21884932; 21887250; 21890473; 21890492; 21900206; 21901101; 21906983; 21908613; 21908615; 21908616; 21910869; 21913799; 21914810; 21915031; 21915327; 21925532; 21930127; 21939655; 21945955; 21949775; 21954225; 21959954; 21975932; 21975935; 21978279; 21980128; 21987722; 21991300; 21994334; 22005766; 22014666; 22021428; 22029423; 22031597; 22031698; 22033727; 22045027; 22051934; 22070874; 22072736; 22084251; 22093097; 22094587; 22095135; 22105580; 22107784; 22116552; 22116667; 22117074; 22131882; 22140653; 22146375; 22146979; 22150081; 22169232; 22171994; 22173970; 22174934; 22183914; 22184110; 22185283; 22189542; 22192357; 22198382; 22199277; 22199300; 22199303; 22208359; 22213015; 22213475; 22231444; 22234835; 22235305; 22249415; 22251423; 22268450; 22270359; 22271581; 22277669; 22280833; 22285928; 22297255; 22301279; 22309289; 22314363; 22315412; 22328503; 22328975; 22334668; 22335196; 22336203; 22337773; 22339676; 22340730; 22343475; 22345097; 22351695; 22354785; 22360859; 22363436; 22363598; 22366458; 22375056; 22384056; 22384099; 22384145; 22389405; 22391209; 22391563; 22393424; 22394200; 22394497; 22394561; 22410793; 22417847; 22426999; 22430898; 22445357; 22451658; 22455883; 22457005; 22463491; 22465665; 22471665; 22480519; 22480544; 22487681; 22488590; 22491319; 22494103; 22496232; 22505016; 22508044; 22525159; 22532149; 22535956; 22539090; 22547695; 22552281; 22552284; 22554284; 22562131; 22563025; 22563076; 22567126; 22569334; 22569400; 22571340; 22575839; 22577119; 22588279; 22590527; 22591684; 22607554; 22614013; 22619175; 22626691; 22647853; 22648906; 22674407; 22675553; 22682934; 22685591; 22687243; 22705004; 22706160; 22727668; 22728329; 22740686; 22748472; 22752602; 22760211; 22768179; 22805337; 22808143; 22809628; 22815832; 22831980; 22833150; 22837212; 22840496; 22842582; 22875023; 22876373; 22895070; 22895078; 22896661; 22897592; 22901187; 22904195; 22905202; 22905203; 22907434; 22910909; 22923366; 22928011; 22929028; 22936801; 22938585; 22945510; 22952709; 22954457; 22957045; 22961111; 22964641; 22967500; 22975685; 22990118; 22995914; 23021375; 23035900; 23039130; 23041284; 23043959; 23046567; 23047954; 23060458; 23069661; 23082158; 23092880; 23092893; 23095753; 23097134; 23107319; 23112296; 23125486; 23127761; 23133535; 23134728; 23135917; 23135998; 23138182; 23147115; 23167739; 23169238; 23176396; 23182717; 23185040; 23188060; 23192081; 23192871; 23195959; 23200933; 23205493; 23208492; 23225414; 23227138; 23235274; 23236232; 23237847; 23246288; 23249714; 23255608; 23261389; 23271397; 23272133; 23280503; 23297824; 23300340; 23300741; 23303682; 23314850; 23315288; 23318419; 23319332; 23321169; 23325864; 23334667; 23338526; 23340251; 23340270; 23348505; 23352210; 23354687; 23354912; 23379509; 23380710; 23383273; 23384770; 23386617; 23389849; 23409016; 23409128; 23417403; 23418602; 23419514; 23421998; 23424671; 23429328; 23430973; 23434580; 23437141; 23440515; 23442539; 23444215; 23457304; 23457334; 23459592; 23463506; 23463670; 23474367; 23499907; 23504323; 23507869; 23511556; 23512990; 23521913; 23525579; 23546174; 23546450; 23546602; 23547889; 23553960; 23558942; 23561972; 23563091; 23563706; 23567263; 23574721; 23580656; 23583197; 23603894; 23613227; 23615537; 23615713; 23624506; 23625205; 23626817; 23629924; 23639623; 23640046; 23667466; 23677479; 23684008; 23685151; 23686362; 23708780; 23710442; 23710710; 23711387; 23724143; 23725225; 23726842; 23728071; 23740762; 23741320; 23742646; 23743572; 23754751; 23757022; 23765166; 23786162; 23788636; 23791833; 23792459; 23792604; 23796964; 23811754; 23812726; 23824745; 23832540; 23838801; 23840064; 23841076; 23843462; 23852728; 23863161; 23867821; 23869765; 23876532; 23884311; 23884447; 23884910; 23886157; 23896866; 23898095; 23923067; 23934627; 23996929; 24001613; 24005670; 24015256; 24030155; 24081328; 24095799; 24099783; 24113181; 24120917; 24152492; 24154876; 24157255; 24225136; 24297901; 24314632; 24321521; 24458280; 24600969 v-akt murine thymoma viral oncogene homolog 1 Ensembl:ENSG00000142208 HGNC:391 HPRD:01261 MIM:164730 Vega:OTTHUMG00000170795 Other designations: PKB alpha|RAC-PK-alpha|RAC-alpha serine/threonine-protein kinase|protein kinase B alpha|proto-oncogene c-Akt|rac protein kinase alpha AKT1 OGG:3000000208 Bin Zhao, Yue Liu, Oliver He HIHGHH PKBB PKBBETA PRKBB RAC-BETA WEB: http://www.ncbi.nlm.nih.gov/gene AKT2 v-akt murine thymoma viral oncogene homolog 2 208 19q13.1-q13.2 9606 19 Official from a nomenclature committee GO_0001934 (EC: ISS); GO_0004674 (EC: IDA, PMID: 16540465); GO_0004674 (EC: TAS); GO_0005515 (EC: IPI, PMID: 10490823); GO_0005524 (EC: IDA, PMID: 16540465); GO_0005634 (EC: IDA); GO_0005634 (EC: TAS); GO_0005829 (EC: TAS); GO_0005886 (EC: ISS); GO_0005886 (EC: TAS); GO_0005938 (EC: ISS); GO_0005978 (EC: IEA); GO_0006006 (EC: IEA); GO_0006417 (EC: IEA); GO_0006464 (EC: TAS, PMID: 1409633); GO_0006915 (EC: IEA); GO_0007165 (EC: TAS); GO_0008286 (EC: IMP, PMID: 16814735); GO_0008286 (EC: TAS); GO_0008643 (EC: IEA); GO_0010748 (EC: IMP, PMID: 16814735); GO_0010907 (EC: IMP, PMID: 16814735); GO_0016301 (EC: TAS); GO_0030334 (EC: TAS); GO_0031340 (EC: ISS); GO_0032000 (EC: IMP, PMID: 16814735); GO_0032287 (EC: IEA); GO_0032587 (EC: ISS); GO_0032859 (EC: IEA); GO_0032869 (EC: IMP, PMID: 16814735); GO_0045444 (EC: TAS); GO_0045725 (EC: IMP, PMID: 16814735); GO_0046326 (EC: IMP, PMID: 16814735); GO_0060644 (EC: TAS); GO_0061024 (EC: TAS); GO_0065002 (EC: ISS); GO_0071156 (EC: TAS); GO_0072659 (EC: IEA); GO_0090314 (EC: ISS); GO_2000147 (EC: IMP, PMID: 17332325); GO_2001275 (EC: IEA) PMID: 1409633; 1801921; 3037531; 8622988; 8889548; 9374542; 9394803; 9512493; 9528769; 9736715; 10490823; 10491192; 10869418; 10983986; 11139588; 11156964; 11208609; 11278835; 11313479; 11432835; 11445557; 11500317; 11507039; 11546794; 11707444; 11781143; 11903042; 11948187; 11988487; 11994280; 12048203; 12114503; 12149249; 12167664; 12176337; 12176997; 12181350; 12434148; 12477932; 12480711; 12482965; 12517337; 12517798; 12524439; 12545160; 12663464; 12697749; 12733712; 12791994; 12808085; 14500673; 14504284; 14612499; 14637151; 14645242; 14654898; 14699494; 14702039; 14735903; 14973226; 15010337; 15070827; 15102693; 15111130; 15144186; 15146197; 15166380; 15314020; 15489334; 15531580; 15557754; 15616007; 15678105; 15689238; 15890450; 15987444; 16221682; 16365168; 16402276; 16524887; 16540465; 16814735; 16841089; 16982699; 17012749; 17030088; 17157319; 17276404; 17327441; 17332325; 17349711; 17372934; 17482291; 17535800; 17576055; 17577629; 17804734; 17825284; 17895832; 17908691; 17914025; 17962807; 18048359; 18187620; 18281467; 18300076; 18316591; 18353613; 18660489; 18768676; 18826950; 18842333; 18996102; 19064572; 19074768; 19075230; 19079138; 19110052; 19164214; 19197940; 19261608; 19435822; 19453261; 19479051; 19713527; 19771908; 19797172; 19825827; 19843246; 19875456; 19913121; 19933843; 20012528; 20018949; 20019835; 20041213; 20056178; 20056908; 20059950; 20102399; 20109457; 20116920; 20133737; 20167810; 20186503; 20354455; 20398329; 20409325; 20447721; 20514445; 20602615; 20628086; 20661303; 20687898; 20688159; 20691427; 20818790; 20848774; 20856200; 21029719; 21048031; 21050850; 21092549; 21179235; 21182834; 21297943; 21423810; 21432781; 21483469; 21507933; 21518566; 21590431; 21606541; 21618512; 21636708; 21680733; 21697490; 21722267; 21763505; 21765914; 21832049; 21890473; 21906983; 21932427; 21979934; 21979951; 21988832; 22031698; 22107784; 22158034; 22261254; 22480544; 22556379; 22748472; 22778840; 22809628; 22904195; 22939624; 22952844; 23018889; 23092922; 23250987; 23305873; 23321478; 23444369; 23468863; 23567263; 23777806; 24030155; 24056770; 24250222; 24321521 v-akt murine thymoma viral oncogene homolog 2 Ensembl:ENSG00000105221 HGNC:392 HPRD:01262 MIM:164731 Vega:OTTHUMG00000137375 Other designations: PKB beta|RAC-PK-beta|RAC-beta serine/threonine-protein kinase|murine thymoma viral (v-akt) homolog-2|protein kinase Akt-2|protein kinase B beta|rac protein kinase beta AKT2 gene OGG:3000000211 Bin Zhao, Yue Liu, Oliver He ALAS ALAS3 ALASH MIG4 WEB: http://www.ncbi.nlm.nih.gov/gene ALAS1 aminolevulinate, delta-, synthase 1 211 OK/SW-cl.121 3p21.1 9606 3 Official from a nomenclature committee GO_0003870 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005739 (EC: IDA); GO_0005759 (EC: TAS); GO_0006778 (EC: TAS); GO_0006782 (EC: IEA); GO_0006783 (EC: TAS); GO_0030170 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS) PMID: 2095458; 2263504; 2347585; 3671094; 7698013; 8424176; 11267664; 11566198; 11929042; 11929048; 12433930; 12477932; 12878157; 15028279; 15123725; 15477213; 15489334; 15547665; 15710391; 15797241; 16234850; 16730941; 16751776; 17628775; 17672918; 18029348; 18719978; 19460752; 19477221; 19656447; 19913121; 20237496; 20628086; 20877624; 21048031; 21659532; 21900206; 21906983; 21926972; 21963094; 21987572; 21988832; 22505724; 23024262; 23974872; 24250222 aminolevulinate, delta-, synthase 1 Ensembl:ENSG00000023330 HGNC:396 HPRD:00505 MIM:125290 Vega:OTTHUMG00000158108 Other designations: 5-aminolevulinate synthase, nonspecific, mitochondrial|5-aminolevulinic acid synthase 1|ALAS-H|delta-ALA synthase 1|delta-aminolevulinate synthase 1|migration-inducing protein 4 ALAS1 OGG:3000000216 Bin Zhao, Yue Liu, Oliver He ALDC ALDH-E1 ALDH1 ALDH11 HEL-9 HEL-S-53e HEL12 PUMB1 RALDH1 WEB: http://www.ncbi.nlm.nih.gov/gene ALDH1A1 aldehyde dehydrogenase 1 family, member A1 216 RP11-151D14.2 9q21.13 9606 9 Official from a nomenclature committee GO_0001758 (EC: IEA); GO_0004029 (EC: EXP); GO_0005099 (EC: TAS, PMID: 1709013); GO_0005497 (EC: TAS, PMID: 1709013); GO_0005737 (EC: TAS, PMID: 2987944); GO_0005829 (EC: TAS); GO_0006069 (EC: TAS); GO_0006081 (EC: TAS, PMID: 1709013); GO_0006805 (EC: TAS); GO_0032320 (EC: TAS, PMID: 1709013); GO_0042572 (EC: IEA); GO_0044281 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 224930; 730161; 1709013; 2591967; 2776714; 2987944; 3013004; 3397064; 3676276; 4015823; 6427007; 6723659; 8214422; 8493914; 9166904; 9240474; 9723161; 12081471; 12174908; 12477932; 14506398; 14678778; 15489334; 15597079; 15852347; 16189514; 16857736; 16878979; 17175089; 17222227; 17286337; 17502835; 17628022; 18029348; 18082256; 18331377; 18343808; 18371393; 18450747; 18496131; 18644979; 18848913; 18854779; 19018242; 19025616; 19056867; 19129088; 19296407; 19329942; 19343046; 19385968; 19447584; 19450560; 19478994; 19696793; 19703508; 19706361; 19774675; 19808966; 19874574; 19911270; 20010854; 20019840; 20142235; 20228222; 20379614; 20422001; 20516116; 20585849; 20596639; 20606680; 20634891; 20889728; 20959018; 20959469; 21045151; 21098716; 21118965; 21231983; 21282737; 21336637; 21371077; 21399615; 21441790; 21482329; 21695188; 21708005; 21804471; 21827011; 21907803; 21988832; 22005464; 22012766; 22014057; 22080062; 22098156; 22101256; 22115706; 22123295; 22131125; 22195027; 22260461; 22380773; 22417385; 22430847; 22544210; 22581680; 22591209; 22608744; 22617249; 22649953; 22710732; 22725270; 22782852; 22877687; 22878609; 22887839; 22899292; 22928012; 22930220; 22938492; 23084350; 23112116; 23132408; 23220285; 23236537; 23252868; 23267077; 23295229; 23332924; 23434145; 23438482; 23454351; 23465277; 23483187; 23585015; 23759596; 23762304; 23787917; 23799031; 23805041; 23845466; 24043631; 24080087; 24120944; 24289252; 24511023 aldehyde dehydrogenase 1 family, member A1 Ensembl:ENSG00000165092 HGNC:402 HPRD:00001 MIM:100640 Vega:OTTHUMG00000020019 Other designations: ALDH class 1|ALHDII|RALDH 1|acetaldehyde dehydrogenase 1|aldehyde dehydrogenase 1, soluble|aldehyde dehydrogenase, liver cytosolic|epididymis luminal protein 12|epididymis luminal protein 9|epididymis secretory sperm binding protein Li 53e|retinal dehydrogenase 1|retinaldehyde dehydrogenase 1 ALDH1A1 OGG:3000000229 Bin Zhao, Yue Liu, Oliver He ALDB ALDO2 WEB: http://www.ncbi.nlm.nih.gov/gene ALDOB aldolase B, fructose-bisphosphate 229 RP11-490D19.1 9q21.3-q22.2 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0004332 (EC: EXP); GO_0004332 (EC: IDA, PMID: 10625657); GO_0005515 (EC: IPI, PMID: 18000879); GO_0005815 (EC: IDA, PMID: 18000879); GO_0005829 (EC: TAS); GO_0005975 (EC: TAS); GO_0006000 (EC: IMP, PMID: 3383242); GO_0006001 (EC: TAS); GO_0006006 (EC: TAS); GO_0006094 (EC: TAS); GO_0006096 (EC: IDA, PMID: 10625657); GO_0006096 (EC: IEA); GO_0006096 (EC: TAS); GO_0006116 (EC: IDA, PMID: 17576770); GO_0008092 (EC: IDA, PMID: 9244396); GO_0030388 (EC: IDA, PMID: 10625657); GO_0032781 (EC: IGI, PMID: 17576770); GO_0034451 (EC: IDA, PMID: 18000879); GO_0042802 (EC: IPI, PMID: 10625657); GO_0044281 (EC: TAS); GO_0051117 (EC: IDA, PMID: 17576770); GO_0070061 (EC: IMP, PMID: 10625657); GO_0070072 (EC: IGI, PMID: 17576770) PMID: 1967768; 2336380; 2410860; 2649152; 2830249; 3000275; 3016456; 3383242; 6548561; 6585824; 6689266; 7717389; 8162030; 8299883; 8535439; 9244396; 10024431; 10625657; 10970798; 11241348; 11399750; 11679716; 11752456; 12205126; 12417303; 12464284; 12477932; 14966907; 15063762; 15532022; 15880727; 16406649; 17292585; 17457694; 17576770; 17955389; 18000879; 18029348; 18541450; 18700007; 19817957; 20033295; 20162364; 20848650; 20882353; 21166391; 21832049; 21890473; 21963094; 21987572; 21988832; 22001757; 22505724; 22911800 aldolase B, fructose-bisphosphate Ensembl:ENSG00000136872 HGNC:417 HPRD:01972 MIM:612724 Vega:OTTHUMG00000020378 Other designations: aldolase 2|aldolase B, fructose-bisphosphatase|fructose-bisphosphate aldolase B|liver-type aldolase ALDOB OGG:3000000249 Bin Zhao, Yue Liu, Oliver He AP-TNAP APTNAP HOPS TNAP TNSALP WEB: http://www.ncbi.nlm.nih.gov/gene ALPL alkaline phosphatase, liver/bone/kidney 249 1p36.12 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0001501 (EC: TAS, PMID: 9781036); GO_0001958 (EC: IEA); GO_0003006 (EC: IEA); GO_0004035 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15208311); GO_0005615 (EC: IEA); GO_0005886 (EC: IEA); GO_0016021 (EC: IEA); GO_0016462 (EC: IDA, PMID: 19874193); GO_0031012 (EC: IEA); GO_0031225 (EC: IEA); GO_0032496 (EC: IEA); GO_0033280 (EC: IEP, PMID: 17023519); GO_0046677 (EC: IEA); GO_0046872 (EC: IEA); GO_0051384 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0071407 (EC: IEA); GO_0071529 (EC: IEA) PMID: 1321014; 1409720; 1458595; 2220817; 2346496; 2928120; 3165380; 3174660; 3410475; 3446011; 3532105; 3954357; 6933471; 7509208; 7833929; 8406453; 8954059; 9020858; 9192863; 9747027; 9781036; 9814472; 9823315; 9844100; 10094560; 10332035; 10508980; 10679946; 10690885; 10737975; 10834525; 10865224; 11073119; 11438998; 11479741; 11528114; 11745997; 11760847; 11810413; 11834095; 11855933; 11999978; 12357339; 12372831; 12397600; 12412800; 12477932; 12638946; 12788869; 12815606; 12920074; 14517339; 14702039; 14756545; 15135428; 15146197; 15208311; 15230135; 15248185; 15476587; 15489334; 15562030; 15629439; 15660230; 15694177; 15824850; 16344560; 16583221; 16602701; 16681433; 16893177; 16932897; 17023519; 17043047; 17195227; 17229666; 17242729; 17253930; 17395561; 17516619; 17563703; 17719863; 17922851; 18029348; 18037100; 18158785; 18160010; 18328985; 18422967; 18455459; 18469019; 18496130; 18500657; 18523927; 18572267; 18579124; 18605934; 18665784; 18724009; 18769922; 18940312; 19012630; 19056867; 19084045; 19303062; 19335222; 19419944; 19423565; 19453261; 19500388; 19631305; 19641839; 19729429; 19744961; 19751416; 19751417; 19856264; 19860546; 19874193; 19884277; 19888898; 19931660; 20048161; 20139978; 20175736; 20231843; 20301329; 20345388; 20355242; 20379614; 20558539; 20634292; 20809279; 20828673; 20888271; 20924064; 20977932; 21168482; 21179104; 21191615; 21289095; 21402707; 21419245; 21558934; 21713451; 21886157; 21956185; 22001757; 22024719; 22154904; 22167380; 22211102; 22228761; 22268729; 22300680; 22395920; 22569225; 22672431; 22702738; 22703652; 22994584; 23039266; 23124780; 23149655; 23223140; 23328739; 23419404; 23427088; 23432910; 23509830; 23612078; 23648065; 23897810 alkaline phosphatase, liver/bone/kidney Ensembl:ENSG00000162551 HGNC:438 HPRD:01377 MIM:171760 Vega:OTTHUMG00000002949 ALPL OGG:3000000283 Bin Zhao, Yue Liu, Oliver He ALS9 HEL168 RAA1 RNASE4 RNASE5 WEB: http://www.ncbi.nlm.nih.gov/gene ANG angiogenin, ribonuclease, RNase A family, 5 283 14q11.1-q11.2 9606 14 Official from a nomenclature committee GO_0001525 (EC: IDA, PMID: 8448182); GO_0001525 (EC: IMP, PMID: 17125737); GO_0001525 (EC: TAS, PMID: 16567967); GO_0001541 (EC: NAS, PMID: 12770725); GO_0001556 (EC: NAS, PMID: 11438326); GO_0001666 (EC: IDA, PMID: 10999833); GO_0001666 (EC: NAS, PMID: 15776477); GO_0001890 (EC: NAS, PMID: 11984825); GO_0001938 (EC: IDA, PMID: 9122172); GO_0003677 (EC: IC, PMID: 10649442); GO_0003779 (EC: IDA, PMID: 11782452); GO_0004519 (EC: TAS, PMID: 10103013); GO_0004540 (EC: IDA, PMID: 2424496); GO_0005102 (EC: IDA, PMID: 9122172); GO_0005507 (EC: IDA, PMID: 9245697); GO_0005515 (EC: IPI, PMID: 10413501); GO_0005605 (EC: IDA, PMID: 15166501); GO_0005615 (EC: IDA, PMID: 16461950); GO_0005634 (EC: IDA, PMID: 10649442); GO_0005730 (EC: ISS); GO_0006651 (EC: IDA, PMID: 2457905); GO_0007154 (EC: NAS, PMID: 10103013); GO_0007202 (EC: IMP, PMID: 2457905); GO_0008201 (EC: IDA, PMID: 10103013); GO_0008219 (EC: IEA); GO_0009303 (EC: IMP, PMID: 15735021); GO_0009725 (EC: IDA, PMID: 10999833); GO_0016477 (EC: IMP, PMID: 17125737); GO_0016892 (EC: IEA); GO_0017148 (EC: IEA); GO_0019843 (EC: TAS, PMID: 2457905); GO_0030041 (EC: ISS); GO_0030426 (EC: ISS); GO_0032148 (EC: IMP, PMID: 17125737); GO_0032311 (EC: IPI, PMID: 3470787); GO_0032431 (EC: IMP, PMID: 2646638); GO_0042277 (EC: IDA, PMID: 11782452); GO_0042327 (EC: IDA, PMID: 17125737); GO_0042592 (EC: NAS, PMID: 15166501); GO_0043025 (EC: ISS); GO_0048662 (EC: IDA, PMID: 10103013); GO_0050714 (EC: IDA, PMID: 2646638); GO_0050714 (EC: ISS); GO_0090305 (EC: TAS, PMID: 10103013); GO_0090501 (EC: IDA, PMID: 2424496) PMID: 1400510; 1978563; 2276743; 2424496; 2440105; 2457905; 2479414; 2646638; 2730651; 2742853; 2866794; 2866795; 3470787; 3619929; 3663649; 7679494; 7945327; 8127865; 8159679; 8448182; 9122172; 9245697; 9311977; 9461294; 9707554; 9918722; 10103013; 10413501; 10648935; 10649442; 10999833; 11374889; 11438326; 11468363; 11751393; 11752456; 11782452; 11847008; 11851402; 11919285; 11984825; 12168899; 12209593; 12477932; 12515546; 12705339; 12770725; 12842050; 14593238; 14671622; 14756559; 15064314; 15067362; 15128420; 15166501; 15182336; 15236995; 15489334; 15557516; 15558023; 15735021; 15737636; 15776477; 15979542; 16169070; 16322296; 16461950; 16490744; 16567967; 16712791; 16937522; 17113198; 17125737; 17207965; 17462671; 17703939; 17886298; 17900154; 17991437; 18087731; 18636464; 18808740; 18852347; 18936943; 18955785; 19158252; 19160530; 19253715; 19262607; 19287993; 19332886; 19363631; 19423182; 19625371; 19631914; 20045391; 20105109; 20137109; 20174961; 20301623; 20452482; 20472325; 20484129; 20577002; 20629092; 20673868; 20838751; 20923443; 20952631; 20955379; 21085671; 21091473; 21103661; 21154263; 21209106; 21364907; 21375772; 21439815; 21528671; 21539846; 21621297; 21711968; 21778318; 21800332; 21808991; 21919032; 21988832; 22148849; 22190368; 22194915; 22266868; 22292798; 22292843; 22372545; 22384259; 22438557; 22449478; 22526325; 22633874; 22694909; 22940420; 23229115; 23231972; 23351638; 23379493; 23409128; 23665167; 23989187; 24122807; 24337645 angiogenin, ribonuclease, RNase A family, 5 Ensembl:ENSG00000214274 HGNC:483 HPRD:00105 MIM:105850 Vega:OTTHUMG00000029576 Other designations: RNase 5|angiogenin|epididymis luminal protein 168|ribonuclease 5|ribonuclease A A1 ANG OGG:3000000284 Bin Zhao, Yue Liu, Oliver He AGP1 AGPT ANG1 WEB: http://www.ncbi.nlm.nih.gov/gene ANGPT1 angiopoietin 1 284 8q23.1 9606 8 GO_0001701 (EC: IEA); GO_0001936 (EC: IDA, Qualifier: NOT, PMID:8980223); GO_0002040 (EC: IDA, PMID:10218485); GO_0002092 (EC: IDA, PMID:19424712); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID:10218485); GO_0005886 (EC: IDA, PMID:19424712); GO_0005902 (EC: IDA, PMID:19424712); GO_0007162 (EC: IDA, PMID:19674970); GO_0007171 (EC: IDA, PMID:19424712); GO_0007596 (EC: TAS); GO_0010595 (EC: IDA, PMID:12958144); GO_0014068 (EC: IEA); GO_0014842 (EC: IDA, PMID:19733541); GO_0030097 (EC: IEA); GO_0030154 (EC: IEA); GO_0030210 (EC: IDA, PMID:19297368); GO_0030971 (EC: IPI, PMID:19922791); GO_0031398 (EC: IDA, PMID:19689429); GO_0031589 (EC: IEA); GO_0033138 (EC: IEA); GO_0034394 (EC: IDA, PMID:19615361); GO_0043066 (EC: IDA, PMID:10218485); GO_0043116 (EC: IDA, PMID:14978158); GO_0043524 (EC: IEA); GO_0043536 (EC: IDA, PMID:9660821); GO_0045121 (EC: IDA, PMID:19615361); GO_0045785 (EC: IEA); GO_0048014 (EC: IDA, PMID:19689429); GO_0050731 (EC: IDA, PMID:15851516); GO_0050900 (EC: TAS); GO_0050918 (EC: IDA, PMID:9660821); GO_0051897 (EC: IDA, PMID:18425120); GO_0070062 (EC: IDA, PMID:19199708); GO_0070374 (EC: IDA, PMID:18425120); GO_0072012 (EC: ISS); GO_2000352 (EC: IDA, PMID:19674970) PMID:7584026; 7584028; 7642106; 8980223; 8980224; 9204896; 9525952; 9545648; 9560344; 9660821; 9723709; 10051567; 10218485; 10343124; 10514510; 10706866; 10766762; 10854239; 10944458; 11165944; 11729102; 11776343; 11827452; 11856872; 11870550; 11891175; 11967990; 12138242; 12168954; 12213874; 12239588; 12243755; 12402160; 12427764; 12477932; 12612904; 12649156; 12717391; 12810673; 12816861; 12890486; 12958144; 12958167; 14561809; 14597243; 14665640; 14672554; 14715662; 14749497; 14978158; 14991531; 15001532; 15019820; 15094228; 15161644; 15198927; 15213103; 15242771; 15284220; 15381091; 15453096; 15498854; 15542434; 15562207; 15692086; 15694363; 15746084; 15769741; 15781448; 15823283; 15851516; 15892598; 16000309; 16020388; 16049136; 16229183; 16354591; 16547766; 16614513; 16645159; 16690881; 16723371; 16803467; 16830384; 16917117; 16956819; 17039426; 17168735; 17322632; 17341311; 17466926; 17525262; 17558601; 17562701; 17603084; 17637706; 17724803; 17728252; 17785951; 17803352; 17943167; 18035072; 18080866; 18092380; 18199826; 18269030; 18310225; 18326231; 18330951; 18382887; 18425120; 18664247; 18675456; 18807212; 18823985; 18991494; 18996102; 19010534; 19028450; 19082480; 19082594; 19086654; 19127216; 19148554; 19199708; 19223473; 19297368; 19300530; 19301945; 19322669; 19339077; 19351722; 19424712; 19460752; 19476937; 19478794; 19487284; 19543148; 19567053; 19615361; 19674970; 19689429; 19733541; 19815705; 19875484; 19916173; 19919521; 19922791; 19954476; 20036815; 20056911; 20072144; 20098680; 20099495; 20185425; 20208992; 20346360; 20378606; 20471887; 20554518; 20602615; 20629092; 20696814; 20863203; 21042788; 21140268; 21168819; 21179479; 21212269; 21273558; 21300047; 21380565; 21400522; 21660578; 21672190; 21710361; 21778249; 21849906; 21858121; 21878936; 21884468; 21885850; 21905000; 21905955; 21906428; 21948244; 21963094; 22000910; 22015631; 22033412; 22095586; 22143796; 22205728; 22229541; 22235284; 22334788; 22391155; 22449617; 22483377; 22496856; 22583143; 22642477; 22867989; 22901561; 22949515; 23024612; 23099117; 23123737; 23190105; 23232696; 23288163; 23302768; 23382691; 23504320; 23592718; 23652985; 23686433; 23770419; 23785018; 23835996; 23840065; 24010773 angiopoietin 1 Ensembl:ENSG00000154188 HGNC:484 HPRD:03392 MIM:601667 Vega:OTTHUMG00000164812 Other designations: ANG-1|angiopoietin-1 ANGPT1 OGG:3000000285 Bin Zhao, Yue Liu, Oliver He AGPT2 ANG2 WEB: http://www.ncbi.nlm.nih.gov/gene ANGPT2 angiopoietin 2 285 8p23.1 9606 8 GO_0001525 (EC: IEA); GO_0001666 (EC: IEA); GO_0005102 (EC: TAS, PMID:10766762); GO_0005515 (EC: IPI); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID:9660821); GO_0005634 (EC: IEA); GO_0005886 (EC: IEA); GO_0007165 (EC: TAS, PMID:10766762); GO_0007281 (EC: IEA); GO_0007596 (EC: TAS); GO_0009314 (EC: IEA); GO_0009612 (EC: IEA); GO_0009749 (EC: IEA); GO_0010812 (EC: IEA); GO_0014070 (EC: IEA); GO_0014823 (EC: IEA); GO_0016525 (EC: IEA); GO_0030971 (EC: IPI, PMID:19922791); GO_0031100 (EC: IEA); GO_0042995 (EC: IEA); GO_0043537 (EC: IDA, PMID:9660821); GO_0045766 (EC: IEA); GO_0046872 (EC: IEA); GO_0048014 (EC: IDA, PMID:19922791); GO_0050900 (EC: TAS); GO_0050928 (EC: IDA, PMID:9660821); GO_0060135 (EC: IEA); GO_0071363 (EC: IEA); GO_0072012 (EC: ISS) PMID:8125298; 9204896; 9545648; 9660821; 9723709; 9927494; 10051567; 10343124; 10514510; 10766762; 10964717; 11447223; 11578860; 11856872; 11861279; 12138242; 12176040; 12213874; 12427764; 12477932; 12612904; 12717391; 12810677; 12861074; 14507641; 14556828; 14568550; 14702352; 14726409; 14767538; 14768007; 14976056; 14991531; 15002056; 15003510; 15094228; 15112366; 15127326; 15161644; 15198927; 15213103; 15284088; 15284220; 15375511; 15489334; 15498854; 15542434; 15562207; 15642468; 15694966; 15734895; 15743799; 15769741; 15823283; 15893672; 16009172; 16020388; 16129411; 16182107; 16229183; 16242072; 16290311; 16338068; 16344560; 16417407; 16424009; 16458662; 16465407; 16525658; 16538528; 16614513; 16629644; 16690881; 16714355; 16723371; 16790091; 16803467; 16830384; 16877277; 16956819; 16978237; 16978614; 17003480; 17030814; 17141400; 17167981; 17200776; 17258205; 17287278; 17322632; 17341311; 17361220; 17395886; 17409768; 17505039; 17513791; 17558601; 17601353; 17630849; 17673702; 17704802; 17724803; 17785951; 17828495; 17904634; 17928052; 17931370; 17943167; 18006475; 18092380; 18182823; 18269030; 18310225; 18382887; 18483397; 18516587; 18541195; 18564921; 18568888; 18644593; 18664247; 18675456; 18720385; 18727515; 18791490; 18807212; 18952457; 18957536; 18991494; 18996102; 19010534; 19018553; 19082594; 19086654; 19102939; 19112163; 19164323; 19223473; 19226440; 19228739; 19271210; 19300530; 19339208; 19341361; 19351722; 19403561; 19435449; 19438587; 19476937; 19478794; 19499513; 19502452; 19539650; 19543148; 19551369; 19567053; 19616847; 19728062; 19815705; 19875484; 19913849; 19922791; 19954476; 20067780; 20068079; 20072144; 20088942; 20099495; 20179005; 20208992; 20213583; 20348331; 20359117; 20379614; 20382847; 20452482; 20482750; 20501615; 20519501; 20562294; 20583134; 20599737; 20629092; 20670479; 20673868; 20696814; 20806109; 20863203; 21042788; 21081932; 21119365; 21131273; 21143700; 21149250; 21163858; 21168819; 21179479; 21248670; 21257790; 21269615; 21300047; 21337734; 21368233; 21380565; 21400522; 21439064; 21450636; 21565611; 21575447; 21576085; 21603628; 21643812; 21672190; 21680733; 21685330; 21750433; 21762624; 21778249; 21809353; 21849906; 21851472; 21858121; 21884204; 21884468; 21900206; 21948244; 21956768; 21963094; 22000910; 22015631; 22095586; 22142364; 22182412; 22229541; 22279570; 22289349; 22311497; 22327175; 22342979; 22449617; 22483377; 22585576; 22640261; 22642477; 22659681; 22728324; 22730375; 22750392; 22770562; 22777681; 22949515; 22989097; 22995870; 23024612; 23099117; 23123737; 23149917; 23174599; 23190105; 23190218; 23232696; 23284823; 23302768; 23305976; 23409162; 23419030; 23421785; 23467610; 23503679; 23536671; 23587231; 23649549; 23652985; 23758184; 23785018; 23803577; 23826161; 23835996; 23899926; 24106271; 24355874; 24373251; 24421076 angiopoietin 2 Ensembl:ENSG00000091879 HGNC:485 HPRD:03563 MIM:601922 Vega:OTTHUMG00000090365 Other designations: ANG-2|Tie2-ligand|angiopoietin-2|angiopoietin-2B|angiopoietin-2a ANGPT2 OGG:3000000291 Bin Zhao, Yue Liu, Oliver He 1 AAC1 ANT ANT 1 ANT1 MTDPS12 PEO2 PEO3 T1 WEB: http://www.ncbi.nlm.nih.gov/gene SLC25A4 solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4 291 4q35 9606 4 Official from a nomenclature committee GO_0000002 (EC: TAS, PMID: 10926541); GO_0005515 (EC: IPI, PMID: 16507998); GO_0005739 (EC: IDA); GO_0005743 (EC: TAS); GO_0005887 (EC: TAS, PMID: 2823266); GO_0006091 (EC: TAS, PMID: 2823266); GO_0006112 (EC: TAS); GO_0006810 (EC: TAS, PMID: 2823266); GO_0008637 (EC: IEA); GO_0015207 (EC: TAS, PMID: 2823266); GO_0015853 (EC: TAS, PMID: 2823266); GO_0016032 (EC: TAS); GO_0044281 (EC: TAS); GO_0050796 (EC: TAS); GO_0060546 (EC: IMP, PMID: 16507998) PMID: 1582253; 2541251; 2547778; 2823266; 2829183; 8103757; 8479824; 8619474; 8644740; 9110174; 9748162; 9874241; 10364542; 10620603; 10926541; 11175251; 11181702; 11193032; 11287411; 11756592; 11756613; 11809823; 12039962; 12112115; 12140186; 12149099; 12450408; 12477932; 12565915; 12663490; 12707443; 12750393; 12750404; 14729611; 15033717; 15142377; 15231833; 15489334; 15551024; 15638722; 15725353; 15792871; 15817944; 15832179; 16020522; 16107323; 16120388; 16155110; 16226712; 16236267; 16354571; 16429131; 16492162; 16507998; 16511342; 16556444; 16887100; 17203973; 17328670; 17331040; 17420318; 17586316; 17586317; 18094160; 18504126; 18575922; 18781797; 18852887; 19149577; 19232058; 19275580; 19275583; 19275588; 19425506; 19840444; 19965780; 20007455; 20012529; 20160640; 20181062; 20186120; 20504995; 20528917; 20698827; 20843780; 20877624; 20972266; 21139048; 21145461; 21196320; 21318276; 21319273; 21586654; 21890473; 21906983; 21918813; 21963094; 22178446; 22187496; 22350218; 22354994; 22797925; 22939629; 23000965; 23246001; 23266187; 23401503; 23464991; 24244333 solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4 Ensembl:ENSG00000151729 HGNC:10990 HPRD:00058 MIM:103220 Vega:OTTHUMG00000134299 Other designations: ADP,ATP carrier protein 1|ADP,ATP carrier protein, heart/skeletal muscle|ADP/ATP translocase 1|adenine nucleotide translocator 1 (skeletal muscle)|heart/skeletal muscle ATP/ADP translocator|solute carrier family 25 member 4 SLC25A4 OGG:3000000317 Bin Zhao, Yue Liu, Oliver He APAF-1 CED4 WEB: http://www.ncbi.nlm.nih.gov/gene APAF1 apoptotic peptidase activating factor 1 317 12q23 9606 12 Official from a nomenclature committee GO_0000166 (EC: TAS, PMID: 10383829); GO_0001843 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10206961); GO_0005524 (EC: IEA); GO_0005634 (EC: IEA); GO_0005829 (EC: TAS); GO_0006309 (EC: IEA); GO_0006915 (EC: TAS); GO_0006919 (EC: IDA); GO_0006952 (EC: IEA); GO_0007399 (EC: TAS, PMID: 9753320); GO_0008635 (EC: IDA, PMID: 9267021); GO_0008635 (EC: TAS); GO_0008656 (EC: NAS, PMID: 15009102); GO_0030900 (EC: IEA); GO_0042802 (EC: IEA); GO_0042981 (EC: TAS, PMID: 10441496); GO_0043065 (EC: TAS, PMID: 18309324); GO_0043293 (EC: IDA); GO_0043293 (EC: TAS, PMID: 18309324); GO_0043531 (EC: IEA); GO_0051402 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0072432 (EC: TAS, PMID: 18309324); GO_0097193 (EC: TAS, PMID: 18309324); GO_2001235 (EC: IEA) PMID: 9267021; 9390557; 9455477; 9488720; 9539746; 9651578; 9753320; 9829980; 9837928; 9878060; 9922454; 10206961; 10322433; 10364241; 10376594; 10383829; 10393175; 10441496; 10486928; 10543941; 10578182; 10702682; 10722681; 10764728; 10934467; 10949025; 11113115; 11230124; 11242052; 11389439; 11457460; 11550094; 11864614; 12021264; 12147322; 12149244; 12168954; 12477932; 12549820; 12615903; 12637514; 12804598; 12963020; 14566819; 14747474; 14993223; 15001356; 15009102; 15026369; 15033720; 15103018; 15262985; 15305193; 15378005; 15590702; 15649154; 15692060; 15703181; 15735003; 15829969; 15832174; 15832175; 15863166; 15972851; 16046141; 16098052; 16231040; 16232302; 16331630; 16420245; 16595687; 16951219; 16979168; 17081983; 17133271; 17274640; 17348858; 17361096; 17418785; 17534194; 17541304; 17603079; 17876870; 17882496; 17885667; 18029348; 18042457; 18093951; 18309324; 18373966; 18439902; 18587251; 18676680; 18719738; 18834886; 19056867; 19058789; 19074885; 19141860; 19170196; 19238172; 19322201; 19455599; 19603830; 19625176; 19662370; 19675677; 19692168; 19698783; 19801675; 19809088; 19913121; 20345447; 20379614; 20453000; 20628086; 20959405; 20977544; 21104989; 21139048; 21297999; 21528061; 21659556; 21890473; 21906983; 21922274; 22101335; 22143029; 22246185; 22335196; 22632162; 22996741; 23085065; 23207240; 23326121; 23521171; 23822711 apoptotic peptidase activating factor 1 Ensembl:ENSG00000120868 HGNC:576 HPRD:03755 MIM:602233 Vega:OTTHUMG00000170214 Other designations: apoptotic protease-activating factor 1 APAF1 OGG:3000000325 Bin Zhao, Yue Liu, Oliver He HEL-S-92n PTX2 SAP WEB: http://www.ncbi.nlm.nih.gov/gene APCS amyloid P component, serum 325 1q21-q23 9606 1 Official from a nomenclature committee GO_0005576 (EC: NAS, PMID: 14718574); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA); GO_0006457 (EC: TAS, PMID: 10812074); GO_0006953 (EC: TAS, PMID: 2987268); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0043234 (EC: IEA); GO_0046872 (EC: IEA); GO_0051082 (EC: TAS, PMID: 10812074); GO_0051131 (EC: TAS, PMID: 10972085); GO_0070062 (EC: IDA, PMID: 19056867); GO_0072562 (EC: IDA) PMID: 81686; 1477104; 1602151; 2987268; 3029048; 3172210; 3211159; 3759147; 3915434; 4055725; 7592941; 8114934; 8144569; 8202534; 8417122; 8662978; 8999915; 9217261; 10631319; 10812074; 10972085; 11359830; 11441067; 11984001; 12015594; 12100475; 12126626; 12432394; 12477932; 12528126; 12767937; 14500533; 14519527; 14607961; 14718574; 15031287; 15174148; 15489334; 15649951; 15837583; 16335952; 16380821; 16643876; 16710414; 16784490; 17138933; 17530641; 17630380; 17676666; 18174230; 18624398; 19011614; 19052452; 19056867; 19948975; 20189569; 20237496; 20300636; 20930309; 20932823; 21044893; 21106539; 21223953; 21278351; 21360619; 21900206; 21988832; 22205573; 22396542; 22493081; 22867744; 22939635; 23385359; 23390551; 23423137; 23527487; 23544079; 23600950; 23966633 amyloid P component, serum Ensembl:ENSG00000132703 HGNC:584 HPRD:00101 MIM:104770 Vega:OTTHUMG00000022741 Other designations: 9.5S alpha-1-glycoprotein|epididymis secretory sperm binding protein Li 92n|pentaxin-related|serum amyloid P-component APCS OGG:3000000348 Bin Zhao, Yue Liu, Oliver He AD2 LDLCQ5 LPG WEB: http://www.ncbi.nlm.nih.gov/gene APOE apolipoprotein E 348 19q13.2 9606 19 Official from a nomenclature committee GO_0000302 (EC: NAS, PMID: 11743999); GO_0001523 (EC: TAS); GO_0001540 (EC: IDA, PMID: 11305869); GO_0001937 (EC: IDA, PMID: 9685360); GO_0002021 (EC: IEA); GO_0005319 (EC: IDA, PMID: 17305370); GO_0005515 (EC: IPI, PMID: 12950167); GO_0005543 (EC: IDA, PMID: 4066713); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA); GO_0005737 (EC: NAS, PMID: 8083695); GO_0005737 (EC: TAS, PMID: 9622609); GO_0005769 (EC: TAS); GO_0005770 (EC: IEA); GO_0005794 (EC: IEA); GO_0005886 (EC: TAS); GO_0006641 (EC: IDA, PMID: 9649566); GO_0006641 (EC: IMP, PMID: 3771793); GO_0006707 (EC: IEA); GO_0006874 (EC: IEA); GO_0006898 (EC: IDA, PMID: 1917954); GO_0007010 (EC: TAS, PMID: 9622609); GO_0007186 (EC: IDA, PMID: 16443932); GO_0007263 (EC: IDA, PMID: 8995232); GO_0007271 (EC: TAS, PMID: 9622609); GO_0007568 (EC: IEA); GO_0007603 (EC: TAS); GO_0008201 (EC: IDA, PMID: 2745454); GO_0008203 (EC: IDA, PMID: 9649566); GO_0008203 (EC: IMP, PMID: 3771793); GO_0008219 (EC: IEA); GO_0008289 (EC: IDA, PMID: 4066713); GO_0010544 (EC: IDA, PMID: 8995232); GO_0010873 (EC: IDA, PMID: 15654758); GO_0010875 (EC: IDA, PMID: 14754908); GO_0010875 (EC: IGI, PMID: 12401887); GO_0014012 (EC: IEA); GO_0016209 (EC: IDA, PMID: 9685360); GO_0017127 (EC: IEA); GO_0019934 (EC: IDA, PMID: 8995232); GO_0030195 (EC: IDA, PMID: 8995232); GO_0030425 (EC: NAS, PMID: 8083695); GO_0030516 (EC: TAS, PMID: 9622609); GO_0030828 (EC: IDA, PMID: 8995232); GO_0031232 (EC: IEA); GO_0032489 (EC: IDA, PMID: 16443932); GO_0032526 (EC: IEA); GO_0032805 (EC: IDA, PMID: 15950758); GO_0032868 (EC: IEA); GO_0033344 (EC: IDA, PMID: 11162594); GO_0033700 (EC: IDA, PMID: 11162594); GO_0034361 (EC: IDA, PMID: 17154273); GO_0034362 (EC: IDA, PMID: 8245722); GO_0034363 (EC: IDA, PMID: 17336988); GO_0034364 (EC: IDA, PMID: 210174); GO_0034372 (EC: IDA, PMID: 15654758); GO_0034372 (EC: IGI, PMID: 12401887); GO_0034374 (EC: IEA); GO_0034375 (EC: IGI, PMID: 12401887); GO_0034380 (EC: IDA, PMID: 17305370); GO_0034382 (EC: IMP, PMID: 7175379); GO_0034384 (EC: IDA, PMID: 210175); GO_0034447 (EC: IDA, PMID: 1917954); GO_0034447 (EC: IMP, PMID: 9649566); GO_0042157 (EC: TAS); GO_0042158 (EC: IEA); GO_0042159 (EC: IEA); GO_0042311 (EC: IEA); GO_0042627 (EC: IDA, PMID: 16935699); GO_0042632 (EC: IDA, PMID: 9649566); GO_0042802 (EC: IDA, PMID: 4066713); GO_0042803 (EC: IPI, PMID: 8245722); GO_0043025 (EC: NAS, PMID: 8083695); GO_0043407 (EC: IDA, PMID: 9685360); GO_0043524 (EC: IEA); GO_0043537 (EC: IDA, PMID: 9685360); GO_0043691 (EC: IDA, PMID: 8127890); GO_0044281 (EC: TAS); GO_0045471 (EC: IEA); GO_0045541 (EC: IDA, PMID: 1917954); GO_0045773 (EC: IEA); GO_0046848 (EC: IEA); GO_0046907 (EC: TAS, PMID: 9622609); GO_0046911 (EC: IDA, PMID: 9685360); GO_0048156 (EC: IPI, PMID: 7566652); GO_0048168 (EC: TAS, PMID: 9622609); GO_0048709 (EC: IEA); GO_0048844 (EC: IEA); GO_0050728 (EC: IC, PMID: 8995232); GO_0050750 (EC: IDA, PMID: 210175); GO_0050750 (EC: IPI, PMID: 17326667); GO_0051000 (EC: IDA, PMID: 8995232); GO_0051044 (EC: IDA, PMID: 15950758); GO_0051651 (EC: IEA); GO_0060228 (EC: IDA, PMID: 15654758); GO_0070062 (EC: IDA, PMID: 19056867); GO_0070326 (EC: IDA, PMID: 1384047); GO_0070326 (EC: IPI, PMID: 12950167); GO_0071347 (EC: IEA); GO_0071363 (EC: IEA); GO_0071397 (EC: IEA); GO_0071682 (EC: TAS); GO_0071813 (EC: IEA); GO_0072562 (EC: IDA) PMID: 210174; 210175; 759055; 1356443; 1360898; 1361196; 1384047; 1617762; 1674745; 1713245; 1730728; 1917954; 2063194; 2101409; 2313204; 2341812; 2470732; 2498325; 2539388; 2556398; 2738044; 2745454; 2760009; 2779654; 2851587; 2987927; 2992507; 3038959; 3243553; 3283935; 3771793; 3922972; 3947350; 4066713; 4345202; 6199196; 6289314; 6323533; 6325438; 6327682; 6897404; 7068630; 7175379; 7263700; 7498414; 7566652; 7581381; 7586659; 7635945; 7761390; 7768901; 7797576; 7833947; 7972031; 8063017; 8083695; 8127890; 8245722; 8287539; 8300609; 8346443; 8488843; 8620924; 8624078; 8626535; 8756331; 8995232; 9012418; 9147408; 9218423; 9236223; 9360638; 9512010; 9622609; 9649566; 9685360; 9831625; 9869645; 9931331; 10520737; 10559559; 10662539; 10850798; 10962542; 10993992; 11030801; 11032626; 11033977; 11042151; 11055796; 11058710; 11060506; 11061249; 11063158; 11064931; 11072138; 11074789; 11076057; 11079660; 11095479; 11095526; 11096027; 11099722; 11100124; 11106322; 11109009; 11110974; 11113217; 11118024; 11118260; 11118404; 11118932; 11119301; 11121165; 11125748; 11126401; 11129109; 11129992; 11140838; 11140944; 11141572; 11143490; 11152862; 11153762; 11156623; 11157409; 11160955; 11162594; 11166913; 11166947; 11171287; 11171894; 11172628; 11173876; 11173877; 11173882; 11176958; 11177205; 11182472; 11204323; 11218879; 11229422; 11231028; 11236867; 11244490; 11254923; 11256794; 11257253; 11257255; 11259129; 11269459; 11269753; 11273849; 11273909; 11277566; 11280044; 11281447; 11281508; 11285089; 11295126; 11299424; 11302074; 11303757; 11305732; 11305851; 11305869; 11311499; 11315514; 11320185; 11326299; 11328206; 11332642; 11334266; 11334897; 11340230; 11341749; 11343612; 11343837; 11351136; 11354629; 11355019; 11357958; 11359065; 11360807; 11376902; 11378846; 11383910; 11388660; 11398147; 11401504; 11401610; 11412677; 11420577; 11420784; 11421127; 11421132; 11421580; 11422615; 11431078; 11434425; 11445282; 11445633; 11454010; 11456487; 11458997; 11463413; 11471927; 11472462; 11474482; 11475012; 11477126; 11482130; 11484169; 11484172; 11487204; 11494308; 11495026; 11495633; 11500190; 11501342; 11502364; 11504565; 11509287; 11512679; 11516561; 11526473; 11535238; 11546879; 11552016; 11553047; 11558492; 11559372; 11560764; 11563433; 11568917; 11571342; 11574101; 11580926; 11585357; 11589721; 11592046; 11592592; 11665324; 11673588; 11673590; 11676289; 11676291; 11684342; 11684904; 11698154; 11701639; 11702052; 11711204; 11714857; 11714860; 11720484; 11721184; 11722155; 11723294; 11730829; 11738493; 11739991; 11740190; 11743999; 11748362; 11755017; 11755252; 11756600; 11769625; 11769703; 11769724; 11775232; 11780357; 11780396; 11784357; 11784371; 11788473; 11788960; 11791620; 11793025; 11798896; 11803456; 11804199; 11804704; 11805010; 11807891; 11807900; 11814460; 11820771; 11823668; 11830396; 11834531; 11836653; 11840773; 11840804; 11844848; 11849659; 11849755; 11857554; 11860878; 11860925; 11862316; 11863377; 11873594; 11879722; 11882334; 11882335; 11882522; 11882743; 11882744; 11884656; 11884660; 11885754; 11889238; 11890580; 11893833; 11901276; 11903341; 11903399; 11904138; 11910554; 11912196; 11920850; 11921083; 11922198; 11931575; 11931577; 11936239; 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22012848; 22013795; 22015765; 22016362; 22028770; 22039842; 22054870; 22055839; 22056199; 22056562; 22058162; 22068907; 22069463; 22069485; 22071360; 22074026; 22089642; 22100309; 22101739; 22101883; 22101914; 22102296; 22106308; 22108393; 22110642; 22113353; 22129783; 22130662; 22134129; 22138302; 22159055; 22159114; 22165672; 22173784; 22174202; 22178106; 22178110; 22179327; 22185986; 22189452; 22200909; 22204031; 22206590; 22206848; 22211488; 22221491; 22221592; 22225956; 22226379; 22226798; 22228589; 22232206; 22234866; 22238606; 22244650; 22245009; 22246233; 22251476; 22264578; 22266326; 22269984; 22272622; 22272623; 22285757; 22286219; 22291217; 22311091; 22322856; 22328704; 22329498; 22331829; 22334766; 22343410; 22344634; 22348880; 22349451; 22350157; 22353753; 22357643; 22359096; 22365656; 22381401; 22383234; 22383685; 22392034; 22394699; 22396775; 22398564; 22399527; 22410653; 22414761; 22414959; 22419519; 22440829; 22445724; 22462403; 22465377; 22481068; 22487820; 22490376; 22492035; 22502727; 22520940; 22532692; 22534472; 22535266; 22539578; 22542837; 22544617; 22549621; 22558310; 22562716; 22568769; 22580620; 22596266; 22612575; 22615372; 22621984; 22632920; 22633529; 22635103; 22637583; 22642392; 22675504; 22676395; 22689192; 22698480; 22699906; 22710912; 22712640; 22721421; 22728266; 22730380; 22735491; 22755192; 22760259; 22771913; 22784692; 22785395; 22787761; 22796460; 22815080; 22821396; 22825739; 22826377; 22832961; 22837136; 22844488; 22848551; 22862561; 22863665; 22868934; 22869155; 22874659; 22883220; 22883908; 22889670; 22890094; 22890095; 22898894; 22899317; 22902767; 22904031; 22914590; 22914594; 22916037; 22918225; 22921891; 22927174; 22935789; 22936261; 22949395; 22955176; 22961083; 22967844; 22971752; 22972946; 22976236; 22982410; 22984509; 22986607; 22991192; 23011382; 23022416; 23023254; 23031429; 23036023; 23040522; 23042108; 23042215; 23049877; 23050006; 23051684; 23051975; 23056479; 23060451; 23063453; 23064258; 23067351; 23071163; 23079898; 23088986; 23091810; 23096223; 23098561; 23100402; 23100439; 23102119; 23103838; 23110764; 23110818; 23113606; 23118302; 23123227; 23132858; 23134888; 23134962; 23142051; 23142524; 23146133; 23152815; 23159043; 23159296; 23171142; 23175721; 23183136; 23186985; 23204275; 23213264; 23232444; 23238736; 23242296; 23242623; 23247007; 23251595; 23255503; 23255822; 23270420; 23272070; 23273617; 23275593; 23286790; 23288845; 23289212; 23290018; 23291160; 23292450; 23293020; 23296339; 23302659; 23312054; 23317568; 23320904; 23321337; 23324992; 23326517; 23364031; 23371373; 23372804; 23380990; 23382465; 23384034; 23384292; 23385359; 23396426; 23407349; 23407718; 23408335; 23411028; 23413428; 23415434; 23419831; 23424640; 23429815; 23430611; 23430745; 23455636; 23466070; 23492875; 23503772; 23522842; 23525328; 23537987; 23546960; 23553344; 23562540; 23565137; 23571587; 23573206; 23576895; 23581910; 23583468; 23584199; 23587637; 23587689; 23588940; 23590983; 23593485; 23603214; 23612909; 23613766; 23620513; 23624169; 23631810; 23631828; 23642733; 23652625; 23660682; 23663404; 23669301; 23684315; 23687437; 23701536; 23723060; 23726366; 23729930; 23731072; 23737466; 23743349; 23769398; 23771217; 23773371; 23779114; 23786792; 23808899; 23815818; 23826174; 23844046; 23844141; 23855979; 23865355; 23876113; 23883936; 23888546; 23902934; 23902937; 23919842; 23965289; 24009459; 24023260; 24023310; 24023758; 24145446; 24145819; 24163986; 24239320; 24276092; 24291031; 24308640; 24340925; 24448836; 24464001 apolipoprotein E Ensembl:ENSG00000130203 HGNC:613 HPRD:00135 MIM:107741 Vega:OTTHUMG00000128901 Other designations: apo-E|apolipoprotein E3 APOE OGG:3000000355 Bin Zhao, Yue Liu, Oliver He ALPS1A APO-1 APT1 CD95 FAS1 FASTM TNFRSF6 WEB: http://www.ncbi.nlm.nih.gov/gene FAS Fas cell surface death receptor 355 RP11-399O19.7 10q24.1 9606 10 Official from a nomenclature committee GO_0002377 (EC: IEA); GO_0003014 (EC: IEA); GO_0004871 (EC: TAS, PMID: 10875918); GO_0004872 (EC: NAS, PMID: 7533181); GO_0004888 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10918185); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA); GO_0005829 (EC: NAS, PMID: 7533181); GO_0005886 (EC: IDA); GO_0005886 (EC: IMP); GO_0005886 (EC: TAS); GO_0006461 (EC: TAS, PMID: 10875918); GO_0006915 (EC: IDA, PMID: 9681877); GO_0006915 (EC: TAS); GO_0006919 (EC: TAS); GO_0006924 (EC: IEA); GO_0006925 (EC: IEA); GO_0006927 (EC: IEA); GO_0007165 (EC: TAS, PMID: 9360929); GO_0008625 (EC: IEA); GO_0009636 (EC: IEA); GO_0009897 (EC: IEA); GO_0009986 (EC: IDA); GO_0016021 (EC: IEA); GO_0019724 (EC: IEA); GO_0019900 (EC: IPI, PMID: 7538908); GO_0031264 (EC: IDA, PMID: 11101870); GO_0031265 (EC: IDA); GO_0032464 (EC: IEA); GO_0042802 (EC: IPI); GO_0042981 (EC: NAS, PMID: 7533181); GO_0043065 (EC: IDA); GO_0043065 (EC: IMP); GO_0043066 (EC: IEA); GO_0045060 (EC: IEA); GO_0045121 (EC: IDA); GO_0045619 (EC: IEA); GO_0045637 (EC: IEA); GO_0048536 (EC: IEA); GO_0050869 (EC: IEA); GO_0051260 (EC: IEA); GO_0051384 (EC: IEA); GO_0070062 (EC: IDA); GO_0071260 (EC: IEP, PMID: 19593445); GO_0071285 (EC: IEA); GO_0071455 (EC: IMP); GO_0097049 (EC: IEA); GO_0097190 (EC: TAS); GO_0097191 (EC: IMP); GO_0097192 (EC: IEA); GO_0097527 (EC: IMP, PMID: 16507998); GO_2001239 (EC: TAS); GO_2001241 (EC: IEA) PMID: 1375228; 1385299; 1385309; 1713127; 2469768; 2787530; 7510905; 7514572; 7529798; 7530336; 7533181; 7536190; 7536343; 7538907; 7538908; 7539892; 7540117; 7542559; 7543095; 7575433; 7859281; 8521815; 8524870; 8598453; 8626376; 8648105; 8681376; 8780394; 8864141; 8906799; 8929361; 8940097; 8967952; 8976184; 9002959; 9028321; 9028957; 9039262; 9045686; 9079683; 9082980; 9126929; 9159204; 9199966; 9208847; 9215629; 9223324; 9226175; 9228058; 9247148; 9257699; 9263011; 9267021; 9268734; 9322534; 9325248; 9360929; 9427646; 9475352; 9560245; 9681877; 9721089; 9727492; 9740801; 9751072; 9787134; 9821419; 9835052; 9847311; 9857224; 9920849; 9927496; 9971775; 10068040; 10072505; 10090885; 10200300; 10235259; 10340403; 10462485; 10505674; 10506221; 10535980; 10542291; 10620127; 10625668; 10630977; 10671224; 10706119; 10709732; 10713117; 10799864; 10871852; 10875918; 10918185; 10978533; 11003656; 11034606; 11035039; 11036836; 11048727; 11048730; 11101867; 11101870; 11112409; 11129341; 11177389; 11193028; 11208609; 11298454; 11323689; 11418480; 11436125; 11483955; 11495919; 11550967; 11606059; 11692157; 11733515; 11771526; 11773067; 11779855; 11782802; 11786482; 11786908; 11788891; 11790791; 11809905; 11824955; 11830507; 11836578; 11857317; 11861273; 11864613; 11867183; 11877055; 11891278; 11895550; 11909874; 11920253; 11941452; 11949822; 11961305; 11965496; 11975981; 11986289; 11994542; 12021072; 12032668; 12034188; 12037669; 12040174; 12049185; 12060388; 12060768; 12064832; 12067476; 12096347; 12096925; 12098516; 12107169; 12131184; 12137598; 12139945; 12140383; 12150947; 12163388; 12169207; 12177303; 12185583; 12188927; 12196516; 12198154; 12207331; 12207908; 12220552; 12221075; 12234263; 12244143; 12270344; 12324452; 12372427; 12388693; 12393468; 12393649; 12393889; 12397013; 12414525; 12415011; 12419941; 12452031; 12455036; 12466128; 12477932; 12482410; 12482505; 12485855; 12497631; 12507389; 12513829; 12515395; 12515623; 12516573; 12557947; 12581154; 12583439; 12586732; 12587820; 12604424; 12623840; 12629150; 12646947; 12679613; 12698366; 12699879; 12702723; 12706861; 12710855; 12717632; 12724420; 12742662; 12742739; 12753742; 12757469; 12770553; 12783210; 12788915; 12794152; 12803240; 12824926; 12855571; 12855687; 12867600; 12874203; 12880639; 12883671; 12887920; 12907599; 12923319; 12952224; 12963547; 14506242; 14512182; 14514471; 14530312; 14533029; 14534720; 14557654; 14573612; 14585083; 14594800; 14625033; 14625298; 14625471; 14637155; 14638442; 14644092; 14644197; 14644318; 14647422; 14668794; 14672901; 14676203; 14694156; 14698859; 14714559; 14719092; 14719118; 14724564; 14736971; 14739003; 14739535; 14739941; 14745445; 14759258; 14967838; 14977837; 14981943; 14991945; 15016553; 15019807; 15039424; 15042330; 15054468; 15055260; 15078899; 15138553; 15159312; 15159409; 15160902; 15161716; 15183989; 15203866; 15207703; 15214041; 15215233; 15218339; 15220220; 15238425; 15240787; 15251990; 15277733; 15280387; 15287856; 15289903; 15297424; 15301860; 15345718; 15365741; 15383280; 15390286; 15459302; 15465831; 15467462; 15480430; 15489334; 15492869; 15497017; 15500551; 15502938; 15514680; 15542843; 15556626; 15556941; 15557123; 15563545; 15592292; 15617242; 15632129; 15637757; 15641141; 15645122; 15659383; 15665818; 15670977; 15672026; 15680394; 15688389; 15695771; 15704653; 15723707; 15726829; 15748958; 15786554; 15795317; 15803113; 15806311; 15808689; 15816832; 15818415; 15829968; 15833141; 15838728; 15843521; 15855233; 15858021; 15860671; 15894356; 15907374; 15911745; 15917238; 15929764; 15936090; 15937082; 15938782; 15944736; 15962371; 15963548; 15967797; 15968727; 15972662; 15975999; 15996722; 16000573; 16018969; 16081586; 16087126; 16091761; 16124644; 16129703; 16143308; 16148554; 16157125; 16158329; 16163374; 16169070; 16215672; 16215685; 16255757; 16273638; 16304056; 16306044; 16313826; 16343245; 16344560; 16358967; 16364925; 16368755; 16385451; 16393952; 16403915; 16436054; 16438619; 16441482; 16463650; 16469115; 16472594; 16473667; 16474169; 16507928; 16507998; 16515587; 16524887; 16538171; 16538172; 16643620; 16691186; 16723718; 16736614; 16741989; 16750039; 16765090; 16788566; 16808908; 16820946; 16822901; 16895904; 16899302; 16914910; 16917513; 16921240; 16936193; 16937440; 16948902; 16972019; 16987075; 17000697; 17006606; 17009393; 17014078; 17014925; 17053166; 17056024; 17062728; 17130290; 17135269; 17159907; 17159908; 17161551; 17174268; 17183065; 17194564; 17195092; 17198275; 17203787; 17219051; 17336828; 17376892; 17406980; 17465232; 17485109; 17487740; 17493146; 17504511; 17516614; 17544837; 17545588; 17559541; 17561354; 17564320; 17589525; 17597021; 17598974; 17603079; 17622942; 17657164; 17657791; 17667965; 17684774; 17692455; 17704746; 17704785; 17708363; 17724145; 17762757; 17853317; 17878356; 17891455; 17909299; 17912028; 17912957; 17916181; 17932249; 17938571; 17941899; 17962219; 17962369; 17970696; 17978477; 17982483; 17993614; 17997887; 18000680; 18003704; 18029348; 18045865; 18056484; 18057579; 18068525; 18078642; 18078929; 18088463; 18090928; 18162459; 18174230; 18208868; 18217400; 18220834; 18227168; 18234961; 18243739; 18268284; 18292515; 18302883; 18316328; 18324486; 18328427; 18337305; 18342935; 18361934; 18383830; 18411295; 18422813; 18427836; 18439588; 18441236; 18445624; 18463097; 18473402; 18483392; 18488389; 18494554; 18505906; 18508922; 18508927; 18512812; 18548110; 18552209; 18561948; 18582468; 18588573; 18609513; 18614439; 18635548; 18666137; 18676032; 18679533; 18685642; 18718055; 18727868; 18753860; 18754288; 18757527; 18787411; 18796602; 18800686; 18804468; 18813857; 18818748; 18844072; 18844210; 18851835; 18854777; 18923451; 18948840; 18949391; 18949744; 18972838; 19004284; 19009351; 19010354; 19012493; 19015953; 19019335; 19019483; 19020991; 19037097; 19043361; 19047119; 19067240; 19073786; 19076218; 19077906; 19103758; 19112091; 19118384; 19125371; 19141320; 19141860; 19146781; 19155494; 19161534; 19168581; 19170196; 19173804; 19181929; 19219602; 19225810; 19240174; 19241965; 19262492; 19263494; 19266094; 19270351; 19272297; 19293475; 19298528; 19305072; 19332441; 19336370; 19391241; 19404646; 19458913; 19480241; 19487421; 19509307; 19521670; 19527514; 19538867; 19538884; 19542541; 19561642; 19565204; 19572057; 19573080; 19593445; 19615968; 19625176; 19628789; 19634684; 19653342; 19669200; 19680267; 19692168; 19692467; 19698994; 19716115; 19718569; 19723039; 19726736; 19737931; 19751723; 19758996; 19759548; 19766542; 19773279; 19788921; 19789190; 19798106; 19810143; 19811416; 19812265; 19817952; 19826071; 19890662; 19895798; 19911702; 19913121; 19926197; 19927299; 19937732; 19940360; 19941645; 19950259; 19954064; 19966861; 20012528; 20052288; 20064083; 20074157; 20085233; 20101431; 20106900; 20137575; 20140262; 20164160; 20181888; 20187936; 20193111; 20204402; 20205514; 20219325; 20222173; 20237496; 20301287; 20352431; 20353032; 20359312; 20360470; 20378664; 20380574; 20385987; 20393185; 20394629; 20396760; 20396799; 20408337; 20416077; 20438363; 20438666; 20453000; 20470393; 20501759; 20505730; 20534173; 20547950; 20553075; 20558744; 20568250; 20572163; 20618494; 20620960; 20628086; 20629322; 20638642; 20658220; 20666744; 20673483; 20682001; 20694011; 20726226; 20737708; 20800603; 20802294; 20813889; 20819778; 20822933; 20842669; 20876301; 20934723; 20935634; 20936988; 20947025; 20951677; 20953611; 20959405; 20960177; 20981796; 21036138; 21041692; 21048031; 21049406; 21076068; 21081533; 21087335; 21103345; 21107705; 21120501; 21131755; 21145805; 21167737; 21173302; 21196076; 21233219; 21250890; 21257927; 21271302; 21286777; 21317766; 21321117; 21324892; 21354149; 21359408; 21382479; 21390503; 21430781; 21454681; 21466843; 21468569; 21485506; 21490157; 21516345; 21518761; 21526201; 21526501; 21528407; 21530489; 21549565; 21550977; 21557211; 21557277; 21613217; 21619451; 21625619; 21651830; 21691772; 21706480; 21717192; 21729539; 21741956; 21752354; 21757675; 21762074; 21792914; 21793106; 21803845; 21806408; 21808135; 21852034; 21864388; 21864851; 21869830; 21879377; 21885602; 21906983; 21910009; 21912376; 21917312; 21940365; 21961589; 21963094; 21971214; 21988832; 22027769; 22036455; 22042271; 22065776; 22076446; 22084312; 22095627; 22147197; 22173501; 22182632; 22183068; 22186140; 22194871; 22197557; 22199270; 22207003; 22211869; 22237435; 22252758; 22285488; 22299671; 22331638; 22344564; 22352690; 22357491; 22364882; 22386066; 22398398; 22422199; 22425739; 22431000; 22438247; 22492046; 22499988; 22508480; 22609371; 22622132; 22631677; 22645131; 22649200; 22669972; 22670178; 22677152; 22683265; 22698280; 22702044; 22706245; 22726303; 22752343; 22771321; 22805310; 22806078; 22815944; 22821704; 22842170; 22864571; 22891283; 22898262; 22934709; 22946667; 22983578; 22992806; 23033661; 23045958; 23053964; 23065220; 23114924; 23152563; 23153021; 23166734; 23234803; 23235765; 23240581; 23251661; 23269121; 23280017; 23285481; 23322903; 23326385; 23326448; 23326557; 23327061; 23330016; 23333919; 23338968; 23364796; 23372841; 23392773; 23420824; 23430061; 23434371; 23492187; 23499736; 23524443; 23580232; 23582102; 23582741; 23590971; 23618817; 23619472; 23636796; 23662689; 23667901; 23681795; 23697029; 23762329; 23770605; 23792529; 23846229; 23865866; 23880344; 23894399; 23900676; 23923075; 23932896; 23979975; 24014103; 24043286; 24091673; 24178789; 24331540 Fas cell surface death receptor Ensembl:ENSG00000026103 HGNC:11920 HPRD:00609 MIM:134637 Vega:OTTHUMG00000018701 Other designations: APO-1 cell surface antigen|CD95 antigen|Delta Fas/APO-1/CD95|FAS 827dupA|FAS receptor variant 9|FASLG receptor|Fas (TNF receptor superfamily, member 6)|Fas AMA|TNF receptor superfamily member 6|apoptosis antigen 1|apoptosis-mediating surface antigen FAS|tumor necrosis factor receptor superfamily member 6|tumor necrosis factor receptor superfamily, member 6 FAS OGG:3000000356 Bin Zhao, Yue Liu, Oliver He ALPS1B APT1LG1 APTL CD178 CD95-L CD95L FASL TNFSF6 WEB: http://www.ncbi.nlm.nih.gov/gene FASLG Fas ligand (TNF superfamily, member 6) 356 1q23 9606 1 Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 17557115); GO_0005102 (EC: TAS, PMID: 7826947); GO_0005125 (EC: IEA); GO_0005164 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12198154); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 18835034); GO_0005634 (EC: IDA, PMID: 17557115); GO_0005887 (EC: TAS, PMID: 7826947); GO_0005901 (EC: IEA); GO_0006351 (EC: IEA); GO_0006915 (EC: TAS); GO_0006919 (EC: IGI, PMID: 19364818); GO_0006919 (EC: IMP, PMID: 18293083); GO_0006919 (EC: TAS); GO_0006925 (EC: IEA); GO_0006955 (EC: IEA); GO_0007165 (EC: TAS, PMID: 7826947); GO_0007267 (EC: TAS, PMID: 7826947); GO_0008284 (EC: IEA); GO_0008625 (EC: IDA, PMID: 18835034); GO_0009897 (EC: IEA); GO_0016525 (EC: IDA, PMID: 18835034); GO_0030644 (EC: IEA); GO_0032496 (EC: IEA); GO_0043065 (EC: IDA, PMID: 14749367); GO_0043123 (EC: IEP, PMID: 12761501); GO_0043202 (EC: IEA); GO_0043525 (EC: IEA); GO_0045742 (EC: IEA); GO_0046666 (EC: IEA); GO_0048388 (EC: IEA); GO_0048471 (EC: IEA); GO_0060205 (EC: IEA); GO_0070062 (EC: IDA, PMID: 17076679); GO_0070231 (EC: IDA, PMID: 17076679); GO_0070266 (EC: IDA, PMID: 11101870); GO_0070848 (EC: IEA); GO_0097190 (EC: IDA, PMID: 11101870); GO_0097190 (EC: TAS); GO_0097191 (EC: IDA); GO_0097527 (EC: IDA, PMID: 11101870); GO_2000353 (EC: IDA, PMID: 18835034); GO_2001239 (EC: TAS) PMID: 7505205; 7528780; 7530336; 7536190; 7539892; 7566174; 7589480; 7826947; 7980502; 8521815; 8681376; 8787672; 8906799; 8910274; 9002959; 9022072; 9126929; 9215629; 9226175; 9228058; 9247148; 9261095; 9405425; 9427603; 9475352; 9672636; 9721089; 9801169; 9872321; 9920849; 9971775; 10072505; 10224289; 10318773; 10630977; 10671224; 10799864; 11013215; 11036836; 11048727; 11101870; 11208609; 11276204; 11438180; 11500835; 11559749; 11606059; 11716959; 11739488; 11741599; 11751256; 11786482; 11788891; 11801650; 11809905; 11830480; 11845233; 11856352; 11882326; 11895550; 11908702; 11909874; 11925103; 11961305; 11965496; 11994433; 11994542; 12009596; 12021072; 12021310; 12023017; 12100038; 12113885; 12137598; 12161534; 12198154; 12208869; 12220636; 12372468; 12393889; 12414525; 12414956; 12421989; 12454289; 12464266; 12477932; 12482410; 12482505; 12490654; 12507389; 12513781; 12515623; 12557947; 12559631; 12583439; 12594300; 12618758; 12629150; 12637505; 12651606; 12698366; 12700199; 12707034; 12710855; 12717632; 12742662; 12742739; 12753742; 12761501; 12783210; 12787425; 12794109; 12803240; 12807917; 12849704; 12854132; 12867600; 12884192; 12887920; 12918731; 12923319; 12928375; 12930319; 14514471; 14534535; 14560009; 14602201; 14625471; 14634098; 14642527; 14644197; 14668794; 14669310; 14698859; 14705811; 14739003; 14739407; 14739535; 14749367; 14962292; 14967838; 14977837; 14988839; 14996347; 15019279; 15042330; 15073283; 15078178; 15093732; 15138553; 15173177; 15178561; 15183989; 15195700; 15218339; 15240787; 15272306; 15277733; 15287856; 15302589; 15314293; 15337758; 15339846; 15358139; 15457562; 15480896; 15489334; 15492869; 15542843; 15557763; 15579659; 15653751; 15659383; 15674374; 15686714; 15694838; 15791651; 15795317; 15803113; 15806311; 15814666; 15816832; 15833141; 15843521; 15849828; 15858021; 15870081; 15870181; 15907374; 15928037; 15936090; 15937082; 15938782; 15962391; 15968727; 15975999; 15979995; 15991293; 15996722; 16000573; 16081306; 16087126; 16124644; 16133992; 16155003; 16157125; 16157266; 16158329; 16163374; 16181301; 16186185; 16204241; 16212902; 16273638; 16282344; 16298578; 16306044; 16313826; 16318909; 16332967; 16332972; 16364925; 16441482; 16474169; 16487513; 16498403; 16512757; 16514159; 16538171; 16538172; 16595635; 16595663; 16601838; 16627752; 16691186; 16710414; 16736614; 16767155; 16770006; 16808908; 16858424; 16868256; 16902496; 16972019; 16987075; 16990614; 17000697; 17008914; 17014925; 17053166; 17056762; 17071607; 17076679; 17101499; 17118988; 17123522; 17123604; 17136494; 17164290; 17173971; 17183065; 17198275; 17290285; 17381722; 17465232; 17491259; 17545588; 17557115; 17559541; 17564320; 17598974; 17605793; 17654480; 17667919; 17688234; 17703232; 17704118; 17704746; 17727731; 17762757; 17823283; 17853317; 17912957; 17916181; 17938571; 17941899; 17943461; 17961631; 17962219; 17966039; 17969524; 17997887; 18000680; 18045865; 18050226; 18057579; 18068525; 18069935; 18076022; 18078642; 18162459; 18174230; 18217400; 18220834; 18292515; 18293083; 18302883; 18314443; 18316328; 18324486; 18359029; 18361934; 18374107; 18383830; 18392917; 18422813; 18427836; 18473402; 18483392; 18501631; 18505906; 18509086; 18541195; 18548110; 18561948; 18567840; 18577653; 18666137; 18676680; 18727868; 18757527; 18789888; 18800686; 18813857; 18818748; 18835034; 18844072; 18854777; 19009351; 19010354; 19015953; 19019335; 19041431; 19052714; 19079288; 19124506; 19141860; 19146781; 19155494; 19170196; 19176318; 19181929; 19183163; 19219602; 19240174; 19244619; 19266094; 19305072; 19332441; 19337311; 19364818; 19390575; 19403301; 19434529; 19458913; 19505222; 19527514; 19531476; 19535642; 19538867; 19542541; 19565204; 19572057; 19573080; 19614955; 19625176; 19628789; 19641134; 19692168; 19773279; 19779494; 19789190; 19807924; 19810143; 19812265; 19826071; 19854829; 19890662; 19926197; 19937732; 19941645; 19960225; 20012528; 20013612; 20074157; 20101459; 20106900; 20150914; 20165911; 20190752; 20193111; 20204402; 20219325; 20222173; 20237496; 20301287; 20353032; 20359312; 20371612; 20378615; 20379197; 20379614; 20385987; 20393600; 20394629; 20406899; 20408337; 20438363; 20501759; 20533543; 20568250; 20572163; 20602615; 20618494; 20624652; 20650551; 20673483; 20675370; 20726934; 20842669; 20959405; 21087335; 21102463; 21107701; 21122378; 21152963; 21159039; 21227011; 21270445; 21271302; 21285513; 21286777; 21354149; 21368861; 21466843; 21516345; 21528407; 21605112; 21691772; 21725926; 21729539; 21746966; 21803845; 21806408; 21807637; 21808135; 21864388; 21864851; 21879377; 21909273; 21910009; 21940365; 21955608; 22027769; 22161157; 22172872; 22182632; 22199323; 22207003; 22211869; 22330070; 22331638; 22341864; 22344564; 22449797; 22461695; 22499988; 22535954; 22558309; 22609371; 22631677; 22645131; 22702044; 22706245; 22726303; 22732091; 22763913; 22821704; 22842170; 22860894; 22927007; 22946667; 23045958; 23065018; 23076876; 23128233; 23153021; 23177026; 23184030; 23192951; 23234803; 23269121; 23280017; 23285481; 23330016; 23392773; 23405244; 23420824; 23504349; 23534738; 23582102; 23618817; 23681795; 23682624; 23697029; 23923075; 24072745; 24178789; 24184557; 24265545; 24291222 Fas ligand (TNF superfamily, member 6) Ensembl:ENSG00000117560 HGNC:11936 HPRD:00610 MIM:134638 Vega:OTTHUMG00000034841 Other designations: CD95 ligand|apoptosis (APO-1) antigen ligand 1|apoptosis antigen ligand|fas antigen ligand|tumor necrosis factor (ligand) superfamily, member 6|tumor necrosis factor ligand superfamily member 6 FASLG OGG:3000000427 Bin Zhao, Yue Liu, Oliver He AC ACDase ASAH PHP PHP32 SMAPME WEB: http://www.ncbi.nlm.nih.gov/gene ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1 427 HSD33 8p22 9606 8 Official from a nomenclature committee GO_0003824 (EC: TAS, PMID: 8955159); GO_0006665 (EC: TAS); GO_0006672 (EC: TAS, PMID: 8955159); GO_0006687 (EC: TAS); GO_0008219 (EC: IEA); GO_0010033 (EC: IEA); GO_0017040 (EC: TAS); GO_0030324 (EC: IEA); GO_0043202 (EC: TAS); GO_0044281 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 7744740; 8125298; 8889549; 8955159; 9838138; 10610716; 10959093; 10974027; 11241842; 11451951; 12477932; 12638942; 12754519; 12764132; 12815059; 14702039; 15088070; 15210766; 15489334; 16169070; 16263699; 16335952; 16344560; 16500425; 16806233; 17713573; 17881906; 18245333; 18477771; 19056867; 19298866; 19905902; 19913121; 20360068; 20379614; 20520628; 20628086; 20871013; 21139048; 21335555; 21375364; 21493710; 21504271; 21552555; 21700700; 21846728; 21890473; 21893389; 21988832; 22079093; 22261821; 22268729; 22322590; 22515519; 22703880; 22927646; 23423838; 23518908; 23602568; 23707712; 23777806; 24091326 N-acylsphingosine amidohydrolase (acid ceramidase) 1 Ensembl:ENSG00000104763 HGNC:735 HPRD:01969 MIM:613468 Vega:OTTHUMG00000096997 Other designations: acid CDase|acid ceramidase|acylsphingosine deacylase|putative 32 kDa heart protein ASAH1 OGG:3000000443 Bin Zhao, Yue Liu, Oliver He ACY2 ASP WEB: http://www.ncbi.nlm.nih.gov/gene ASPA aspartoacylase 443 17p13.3 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0004046 (EC: TAS, PMID: 8252036); GO_0005634 (EC: IEA); GO_0005737 (EC: IDA); GO_0006533 (EC: TAS, PMID: 8252036); GO_0016788 (EC: IEA); GO_0019807 (EC: IEA); GO_0022010 (EC: IEA); GO_0046872 (EC: IEA); GO_0048714 (EC: IEA) PMID: 27051; 3116332; 7599639; 7668285; 8023850; 8088831; 8252036; 8659549; 9407392; 10564886; 10837925; 10909858; 12205125; 12477932; 12638939; 12706335; 14699612; 15489334; 16189514; 16437572; 16669630; 16935940; 17027983; 17194761; 17391648; 18029348; 18264947; 18293939; 20201926; 20301412; 22019069; 22219087; 22468686; 22750302; 22878930; 23049088 aspartoacylase HGNC:756 HPRD:02033 MIM:608034 Other designations: ACY-2|aminoacylase 2|aminoacylase-2 ASPA OGG:3000000466 Bin Zhao, Yue Liu, Oliver He EWS-ATF1 FUS/ATF-1 TREB36 WEB: http://www.ncbi.nlm.nih.gov/gene ATF1 activating transcription factor 1 466 12q13 9606 12 GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0003700 (EC: TAS, PMID:2196176); GO_0003705 (EC: IEA); GO_0005515 (EC: IPI, PMID:10722738); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005667 (EC: IEA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0010976 (EC: IEA); GO_0014070 (EC: IEA); GO_0032025 (EC: IEA); GO_0032403 (EC: IEA); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035666 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0043565 (EC: IEA); GO_0043623 (EC: IEA); GO_0045087 (EC: TAS); GO_0045740 (EC: IEA); GO_0045944 (EC: IEA); GO_0046982 (EC: IEA); GO_0048011 (EC: TAS); GO_0051403 (EC: TAS) PMID:1655749; 2196176; 2516827; 7730336; 8384217; 8401579; 8570175; 8621702; 8663317; 8798441; 8889548; 9016641; 9671480; 9685505; 9824209; 10567391; 10585419; 10722738; 10945975; 11014230; 11018520; 11877423; 11909979; 11992546; 12195699; 12391222; 12444143; 12477932; 12527906; 12631284; 12734209; 12748173; 12760902; 12805554; 14767471; 15041276; 15276183; 15489334; 15806162; 15884099; 16227528; 16327442; 16344560; 16716376; 17565989; 18794154; 18950845; 19561568; 19714462; 19913121; 19950226; 20398657; 20413592; 20453000; 20536573; 20628086; 20945072; 20972440; 21484932; 21658281; 21890473; 21963094; 22052915; 22505724; 22510762; 22631637; 22939629; 23000965; 24051143 activating transcription factor 1 Ensembl:ENSG00000123268 HGNC:783 HPRD:00440 MIM:123803 Vega:OTTHUMG00000169482 Other designations: cAMP-dependent transcription factor ATF-1|cyclic AMP-dependent transcription factor ATF-1 ATF1 OGG:3000000467 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene ATF3 activating transcription factor 3 467 RP11-338C15.1 1q32.3 9606 1 GO_0003700 (EC: IEA); GO_0003714 (EC: TAS, PMID:7515060); GO_0005515 (EC: IPI, PMID:16291753); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA); GO_0006094 (EC: IEA); GO_0006351 (EC: IEA); GO_0006987 (EC: TAS); GO_0008284 (EC: IEA); GO_0030968 (EC: TAS); GO_0035914 (EC: IEA); GO_0042802 (EC: IPI, PMID:18255255); GO_0043565 (EC: IEA); GO_0044267 (EC: TAS); GO_0045892 (EC: IEA) PMID:1827203; 2516827; 7515060; 7692236; 8152431; 8576171; 8622660; 8649793; 11375399; 11726207; 11792711; 11810028; 12034827; 12161427; 12372430; 12386811; 12392999; 12477932; 12718878; 12805554; 12833146; 12881527; 14667575; 14673171; 14702039; 14759258; 15280448; 15385533; 15489334; 15670751; 15933712; 16079301; 16109718; 16169070; 16263788; 16286461; 16291753; 16306208; 16344560; 16484797; 16613840; 16912181; 16989641; 17014422; 17042743; 17102133; 17178897; 17295236; 17437852; 17599613; 17952119; 18001166; 18029348; 18192274; 18235102; 18255255; 18426833; 18692824; 18755691; 18802113; 18922905; 19050264; 19060337; 19136462; 19164757; 19219066; 19582787; 19647793; 19913121; 19932681; 20002170; 20110283; 20167600; 20180416; 20211142; 20215396; 20304822; 20351107; 20360311; 20398657; 20413626; 20423458; 20485437; 20581861; 20592017; 20628086; 20696134; 20930144; 21061913; 21129190; 21139048; 21191795; 21294679; 21300803; 21315420; 21324310; 21414204; 21421043; 21451046; 21454613; 21467165; 21495874; 21514952; 21554132; 21593605; 21629765; 21645504; 21668942; 21693764; 21801305; 21821004; 21844328; 21900211; 21906983; 21927023; 21986529; 22046379; 22179317; 22347845; 22475484; 22485215; 22665497; 22753726; 22764884; 22768301; 22851689; 22939624; 22978410; 22989952; 22991139; 23002211; 23088992; 23187734; 23269699; 23455924; 23536558; 23560949; 23661758; 23733932; 23868936; 23921126; 24098051 activating transcription factor 3 Other designations: cAMP-dependent transcription factor ATF-3|cyclic AMP-dependent transcription factor ATF-3 ATF3 OGG:3000000468 Bin Zhao, Yue Liu, Oliver He CREB-2 CREB2 TAXREB67 TXREB WEB: http://www.ncbi.nlm.nih.gov/gene ATF4 activating transcription factor 4 468 22q13.1 9606 22 GO_0003677 (EC: IDA, PMID:15788408); GO_0003677 (EC: ISS); GO_0003700 (EC: ISS); GO_0003700 (EC: TAS, PMID:12689582); GO_0005515 (EC: IPI, PMID:11238952); GO_0005634 (EC: IDA, PMID:16682973); GO_0005634 (EC: ISS); GO_0005654 (EC: TAS); GO_0005667 (EC: IEA); GO_0005737 (EC: ISS); GO_0005815 (EC: IEA); GO_0006094 (EC: ISS); GO_0006355 (EC: ISS); GO_0006366 (EC: ISS); GO_0006520 (EC: TAS, PMID:12689582); GO_0006987 (EC: TAS); GO_0007214 (EC: IEA); GO_0008022 (EC: IEA); GO_0030968 (EC: TAS); GO_0032590 (EC: IEA); GO_0034976 (EC: IDA, PMID:19061639); GO_0043267 (EC: IEA); GO_0043525 (EC: ISS); GO_0043565 (EC: IEA); GO_0044267 (EC: TAS); GO_0045893 (EC: IDA, PMID:15775988); GO_0045893 (EC: IMP, PMID:11960987); GO_0045893 (EC: ISS); GO_0045893 (EC: NAS, PMID:9190894); GO_0045944 (EC: IMP, PMID:15788408); GO_0045944 (EC: ISS); GO_0070059 (EC: ISS) PMID:1371974; 1534408; 1827203; 1847461; 2516827; 8939898; 9190894; 9295363; 9488481; 10419887; 10591208; 11018027; 11025215; 11087824; 11238952; 11274184; 11564156; 11960987; 12477932; 12689582; 12743605; 12805554; 12812986; 12860379; 14561767; 14623284; 14630807; 14630918; 14695168; 14747470; 15277680; 15314157; 15385533; 15461802; 15475356; 15489334; 15677469; 15775988; 15788408; 16169070; 16189514; 16219772; 16343488; 16682973; 16687408; 16751776; 17042743; 17346882; 17347301; 17369260; 17684156; 17707795; 17726049; 17822787; 17938202; 17996332; 18052253; 18163433; 18171674; 18189280; 18195013; 18255255; 18276110; 18408768; 18451308; 18635891; 18697751; 18940792; 19017641; 19053519; 19061639; 19073601; 19114033; 19164757; 19193809; 19251251; 19417138; 19447967; 19453261; 19509279; 19855386; 19922526; 19946894; 20022965; 20185790; 20211142; 20398657; 20473272; 20514020; 20551969; 20564243; 20592469; 20724472; 20732869; 20873783; 20936779; 21044953; 21087962; 21113145; 21203563; 21244365; 21683813; 21693764; 21706477; 21801305; 21832049; 21866569; 21906983; 21951999; 21963094; 21966512; 21988832; 22007000; 22016052; 22017875; 22050711; 22052162; 22082360; 22233381; 22246806; 22338651; 22363646; 22422769; 22435535; 22485215; 22609407; 22691366; 22813743; 22848420; 22915762; 22955275; 23001845; 23078367; 23090478; 23128233; 23153536; 23205607; 23241898; 23242184; 23339444; 23392669; 23471465; 23661758; 23665047; 23792164; 23908598; 23975372; 24021586 activating transcription factor 4 Ensembl:ENSG00000128272 HGNC:786 HPRD:06817 MIM:604064 Vega:OTTHUMG00000151099 Other designations: DNA-binding protein TAXREB67|cAMP response element-binding protein 2|cAMP-dependent transcription factor ATF-4|cAMP-responsive element-binding protein 2|cyclic AMP-dependent transcription factor ATF-4|cyclic AMP-responsive element-binding protein 2|tax-responsive enhancer element B67|tax-responsive enhancer element-binding protein 67 ATF4 OGG:3000000545 Bin Zhao, Yue Liu, Oliver He FCTCS FRP1 MEC1 SCKL SCKL1 WEB: http://www.ncbi.nlm.nih.gov/gene ATR ataxia telangiectasia and Rad3 related 545 3q23 9606 3 Official from a nomenclature committee GO_0000077 (EC: IDA, PMID: 14657349); GO_0001741 (EC: IEA); GO_0003677 (EC: IEA); GO_0004672 (EC: IDA, PMID: 14657349); GO_0004674 (EC: IDA, PMID: 9733515); GO_0005515 (EC: IPI, PMID: 14657349); GO_0005524 (EC: IEA); GO_0005654 (EC: TAS); GO_0005694 (EC: ISS); GO_0006260 (EC: TAS); GO_0006281 (EC: TAS); GO_0006974 (EC: TAS, PMID: 15538388); GO_0007049 (EC: TAS, PMID: 9590286); GO_0007275 (EC: TAS, PMID: 9590286); GO_0008156 (EC: IMP, PMID: 14657349); GO_0016605 (EC: IDA, PMID: 12814551); GO_0018105 (EC: IDA, PMID: 9733515); GO_0032405 (EC: IDA, PMID: 16713580); GO_0032407 (EC: IDA, PMID: 16713580); GO_0034644 (EC: IMP, PMID: 9925639); GO_0042493 (EC: IEA); GO_0043393 (EC: IEA); GO_0043517 (EC: IMP, PMID: 9925639); GO_0046777 (EC: IDA, PMID: 9733515); GO_0071480 (EC: IDA, PMID: 9925639); GO_0090399 (EC: IMP, PMID: 15149599) PMID: 8610130; 8843195; 8978690; 9427750; 9590286; 9636169; 9733515; 9765199; 9766667; 9857181; 9925639; 10435622; 10545197; 10597277; 10608806; 10673501; 10747897; 10749680; 10859164; 10889046; 10951572; 10973490; 11016625; 11114888; 11163154; 11252893; 11278964; 11390642; 11393670; 11418864; 11459832; 11470508; 11551930; 11673449; 11688760; 11709713; 11715017; 11721054; 11790298; 11799063; 11865061; 11883897; 11927575; 12011431; 12024051; 12147700; 12446774; 12493754; 12519769; 12526805; 12629512; 12640452; 12679521; 12738771; 12766152; 12773400; 12791699; 12791985; 12814551; 12915485; 12959929; 14657349; 14724280; 14729972; 14729973; 14742437; 14755251; 14871897; 14988723; 15050919; 15149599; 15159397; 15195100; 15210935; 15235112; 15279777; 15282542; 15302935; 15314022; 15374968; 15451423; 15456891; 15466211; 15485898; 15496423; 15527801; 15533933; 15538388; 15539948; 15616588; 15635413; 15640246; 15650165; 15650754; 15680327; 15707391; 15734998; 15743907; 15758953; 15775976; 15854902; 15933716; 15987455; 16009130; 16051665; 16086026; 16122425; 16122426; 16195237; 16260606; 16293623; 16306615; 16354571; 16431910; 16436511; 16461339; 16474843; 16488880; 16530042; 16540648; 16675950; 16705183; 16713580; 16738325; 16741947; 16757521; 16827800; 16872911; 16880517; 16909103; 16943440; 16951182; 16956949; 16968694; 17010193; 17015476; 17030982; 17035231; 17118963; 17124492; 17140287; 17148452; 17157788; 17210576; 17260016; 17272271; 17292679; 17376433; 17384638; 17384681; 17409144; 17478428; 17526493; 17616578; 17616665; 17620599; 17638878; 17686975; 17716975; 17879369; 17934520; 17976513; 18003706; 18025301; 18032786; 18160036; 18162465; 18202016; 18245444; 18283122; 18344416; 18357388; 18381943; 18434539; 18451105; 18451257; 18480045; 18495871; 18514189; 18519640; 18536714; 18550533; 18583959; 18625709; 18642075; 18664457; 18757420; 18931676; 18936170; 18950845; 18985806; 18995830; 19004803; 19064565; 19064572; 19074885; 19097996; 19109555; 19116388; 19119425; 19124506; 19146767; 19154794; 19197236; 19242509; 19244116; 19275579; 19275588; 19285939; 19330022; 19351817; 19372558; 19444312; 19470935; 19477925; 19527713; 19536649; 19570909; 19584262; 19586908; 19633697; 19690177; 19714462; 19798433; 19805520; 19828454; 19889979; 19903823; 20005840; 20008788; 20012529; 20029092; 20048340; 20060399; 20084458; 20103595; 20147462; 20233725; 20301772; 20347598; 20368801; 20424596; 20427275; 20427287; 20453000; 20469721; 20496165; 20513533; 20515729; 20566845; 20616048; 20634891; 20731661; 20798688; 20801936; 20810650; 20818375; 20847938; 20861269; 20930849; 21034966; 21139048; 21144835; 21224401; 21242293; 21270107; 21284603; 21285353; 21294646; 21308861; 21383502; 21502314; 21566061; 21659603; 21680529; 21705319; 21857991; 21859891; 21874023; 21890473; 21906983; 21908846; 21963094; 21976111; 21994772; 21995812; 21998596; 22053931; 22084169; 22123827; 22159421; 22174788; 22179839; 22184063; 22341969; 22435685; 22505724; 22535492; 22556425; 22621920; 22713662; 22735644; 22740051; 22797063; 22807682; 22842784; 22939629; 22948311; 23000965; 23029527; 23085754; 23135710; 23144622; 23176708; 23178497; 23255133; 23272087; 23284306; 23345434; 23401567; 23438602; 23447674; 23447702; 23451157; 23454212; 23548269; 23592782; 23592994; 23600770; 23684611; 23696651; 23698467; 23733185; 23807228; 23844225; 23861882; 23873943; 23874235; 23897887; 23901102; 23956138; 24005565; 24045107; 24267891 ataxia telangiectasia and Rad3 related Ensembl:ENSG00000175054 HGNC:882 HPRD:08369 MIM:601215 Vega:OTTHUMG00000159234 Other designations: FRAP-related protein 1|FRAP-related protein-1|MEC1, mitosis entry checkpoint 1, homolog|Rad3 related protein|ataxia telangiectasia and Rad3-related protein|protein kinase ATR|serine/threonine-protein kinase ATR ATR gene OGG:3000000572 Bin Zhao, Yue Liu, Oliver He BBC2 BCL2L8 WEB: http://www.ncbi.nlm.nih.gov/gene BAD BCL2-associated agonist of cell death 572 11q13.1 9606 11 Official from a nomenclature committee GO_0001836 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10949025); GO_0005543 (EC: IMP); GO_0005739 (EC: IDA); GO_0005741 (EC: IDA); GO_0005741 (EC: TAS); GO_0005829 (EC: IDA); GO_0005829 (EC: TAS); GO_0006007 (EC: IEA); GO_0006915 (EC: IDA, PMID: 19667065); GO_0006915 (EC: TAS, PMID: 7834748); GO_0006919 (EC: ISS); GO_0007173 (EC: TAS); GO_0008289 (EC: IDA, PMID: 19667065); GO_0008543 (EC: TAS); GO_0008625 (EC: IEA); GO_0008630 (EC: IEA); GO_0008656 (EC: IDA, PMID: 18402937); GO_0009749 (EC: IEA); GO_0010508 (EC: TAS, PMID: 18309324); GO_0010918 (EC: ISS); GO_0019050 (EC: IEA); GO_0019221 (EC: IEA); GO_0019901 (EC: IPI, PMID: 17270021); GO_0030346 (EC: IEA); GO_0032024 (EC: ISS); GO_0032355 (EC: IEA); GO_0032570 (EC: IEA); GO_0033133 (EC: ISS); GO_0033574 (EC: IEA); GO_0034201 (EC: IEA); GO_0035774 (EC: IEA); GO_0038095 (EC: TAS); GO_0042493 (EC: IEA); GO_0042542 (EC: IEA); GO_0042593 (EC: ISS); GO_0043065 (EC: IDA, PMID: 9388232); GO_0043065 (EC: IMP, PMID: 17289999); GO_0043065 (EC: TAS); GO_0043200 (EC: IEA); GO_0043280 (EC: IDA, PMID: 18402937); GO_0043422 (EC: IEA); GO_0044342 (EC: ISS); GO_0045087 (EC: TAS); GO_0045471 (EC: IEA); GO_0045579 (EC: IEA); GO_0045582 (EC: IEA); GO_0045862 (EC: IDA, PMID: 18387192); GO_0046031 (EC: ISS); GO_0046034 (EC: ISS); GO_0046902 (EC: IMP); GO_0046931 (EC: IDA, PMID: 19667065); GO_0046982 (EC: IEA); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0050679 (EC: IMP, PMID: 19593445); GO_0051384 (EC: IEA); GO_0051592 (EC: IEA); GO_0060139 (EC: IEA); GO_0060154 (EC: IEA); GO_0071247 (EC: IEA); GO_0071260 (EC: IEP, PMID: 19593445); GO_0071316 (EC: IDA, PMID: 18676776); GO_0071396 (EC: IEA); GO_0071456 (EC: IEP); GO_0090200 (EC: IMP, PMID: 17289999); GO_0097190 (EC: TAS); GO_0097191 (EC: IMP, PMID: 18852119); GO_0097192 (EC: IEA); GO_0097193 (EC: IMP, PMID: 18676776); GO_0097193 (EC: TAS); GO_0097202 (EC: IDA, PMID: 18387192); GO_1900740 (EC: TAS); GO_1901216 (EC: IEA); GO_2000078 (EC: ISS); GO_2001244 (EC: TAS) PMID: 7834748; 8929531; 8929532; 9130713; 9305851; 9369453; 9381178; 9388232; 9389483; 9463381; 9651683; 9824152; 9878060; 9973195; 10195903; 10381646; 10407019; 10521512; 10558990; 10579309; 10611223; 10620799; 10811615; 10837486; 10837489; 10880354; 10949025; 10949026; 11077446; 11206074; 11278245; 11410287; 11483855; 11494146; 11500364; 11544290; 11583631; 11689886; 11697890; 11717309; 11739707; 11742726; 11781193; 11839683; 11878929; 11908866; 11994280; 12084714; 12087097; 12115603; 12137781; 12239175; 12376548; 12477932; 12657644; 12754297; 12787561; 12842996; 12897128; 12931191; 12954615; 12965220; 14702039; 14767529; 14967141; 15033904; 15078178; 15131699; 15183529; 15226424; 15231831; 15280438; 15489334; 15574335; 15694340; 15705582; 15721256; 15731037; 15751984; 15767261; 15784622; 15849194; 15901741; 15978696; 15990872; 15998799; 16148027; 16189514; 16297499; 16403219; 16413544; 16445909; 16484005; 16603546; 16697956; 16710454; 16728406; 16767165; 16785131; 16843435; 16847055; 16908594; 16932738; 16949642; 16978419; 17011751; 17110373; 17270021; 17274640; 17287851; 17289999; 17393317; 17404594; 17420275; 17438366; 17446862; 17457084; 17474147; 17499381; 17541305; 17544220; 17557568; 17670745; 17696955; 17696989; 17900801; 17927446; 17979178; 18006502; 18029348; 18165867; 18246127; 18276761; 18309324; 18387192; 18391004; 18402774; 18402937; 18420586; 18449891; 18508762; 18508827; 18568448; 18593990; 18628207; 18636124; 18651163; 18651222; 18676776; 18775810; 18798227; 18832722; 18852119; 18973553; 19168699; 19171933; 19508210; 19587239; 19593445; 19624871; 19641507; 19667065; 19679565; 19730683; 19773546; 19882362; 19895838; 19913121; 20012528; 20043968; 20339252; 20596645; 20618440; 20628086; 20647330; 20691103; 20700721; 20810912; 20855536; 20877624; 20936779; 21076048; 21081150; 21187157; 21302807; 21317286; 21419810; 21444773; 21674599; 21849418; 21900206; 21918885; 21988832; 22011203; 22057915; 22096607; 22172950; 22214866; 22423221; 22464442; 22805310; 22837380; 23135712; 23383273; 23547889; 24255178 BCL2-associated agonist of cell death Ensembl:ENSG00000002330 HGNC:936 HPRD:04409 MIM:603167 Vega:OTTHUMG00000134302 Other designations: BCL-X/BCL-2 binding protein|BCL2-antagonist of cell death protein|BCL2-binding component 6|BCL2-binding protein|bcl-2-binding component 6|bcl-2-like protein 8|bcl-XL/Bcl-2-associated death promoter|bcl2 antagonist of cell death|bcl2-L-8 BAD OGG:3000000578 Bin Zhao, Yue Liu, Oliver He BAK BAK-LIKE BCL2L7 CDN1 WEB: http://www.ncbi.nlm.nih.gov/gene BAK1 BCL2-antagonist/killer 1 578 6p21.3 9606 6 Official from a nomenclature committee GO_0001782 (EC: IEA); GO_0001783 (EC: IEA); GO_0001836 (EC: IDA, PMID: 16199525); GO_0001836 (EC: IGI); GO_0001974 (EC: IEA); GO_0002262 (EC: IEA); GO_0002352 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10381623); GO_0005739 (EC: IDA, PMID: 9843949); GO_0005741 (EC: IBA); GO_0005741 (EC: TAS); GO_0005783 (EC: IEA); GO_0005829 (EC: IEA); GO_0006915 (EC: TAS); GO_0007420 (EC: IEA); GO_0007568 (EC: IEA); GO_0008053 (EC: IEA); GO_0008283 (EC: IEA); GO_0008285 (EC: IEA); GO_0008630 (EC: IBA); GO_0008635 (EC: IEA); GO_0009620 (EC: IEA); GO_0010046 (EC: IEA); GO_0010225 (EC: IEA); GO_0010248 (EC: IDA, PMID: 9843949); GO_0010332 (EC: IEA); GO_0010524 (EC: IEA); GO_0010629 (EC: IEA); GO_0014070 (EC: IEA); GO_0031018 (EC: IEA); GO_0031072 (EC: IEA); GO_0031100 (EC: IEA); GO_0031307 (EC: ISS); GO_0032469 (EC: TAS, PMID: 18309324); GO_0032471 (EC: IEA); GO_0033137 (EC: IEA); GO_0034644 (EC: IMP, PMID: 15901672); GO_0034644 (EC: ISS); GO_0035108 (EC: IEA); GO_0042493 (EC: IEA); GO_0042542 (EC: IEA); GO_0042802 (EC: IPI, PMID: 15901672); GO_0042803 (EC: IBA); GO_0043065 (EC: IMP, PMID: 17289999); GO_0043496 (EC: IDA, PMID: 9111042); GO_0043497 (EC: IDA, PMID: 9111042); GO_0044346 (EC: IEA); GO_0045471 (EC: IEA); GO_0045862 (EC: IDA, PMID: 18387192); GO_0046872 (EC: IEA); GO_0046902 (EC: IDA); GO_0046930 (EC: IDA, PMID: 9843949); GO_0046982 (EC: IPI, PMID: 10837489); GO_0048597 (EC: IEA); GO_0051087 (EC: IEA); GO_0051400 (EC: IEA); GO_0051726 (EC: IEA); GO_0051881 (EC: IDA, PMID: 9843949); GO_0060068 (EC: IEA); GO_0070059 (EC: IEA); GO_0070242 (EC: IEA); GO_0071260 (EC: IEP, PMID: 19593445); GO_0090200 (EC: IEA); GO_0097190 (EC: IMP, PMID: 15901672); GO_0097192 (EC: IBA); GO_0097193 (EC: TAS); GO_0097202 (EC: IDA, PMID: 18387192); GO_1900103 (EC: IMP, PMID: 16645094); GO_1901030 (EC: TAS); GO_1902262 (EC: IEA) PMID: 7715729; 7715730; 7715731; 8521816; 8887627; 9020082; 9111042; 9463381; 9573342; 9843949; 9878060; 10085290; 10365962; 10381623; 10381646; 10579309; 10639121; 10837489; 10950869; 11175750; 11206074; 11326099; 11571294; 11728179; 11795669; 11867266; 11908704; 11929871; 11932420; 11940658; 11964315; 12070120; 12137781; 12176904; 12297281; 12454021; 12477932; 12624108; 12624178; 12721291; 12808108; 12847083; 12881569; 14574404; 14596824; 14647456; 14702039; 14980220; 15003505; 15077116; 15124764; 15159409; 15194786; 15248898; 15292519; 15322047; 15351796; 15467752; 15478112; 15489334; 15637055; 15638360; 15638362; 15757910; 15846303; 15846589; 15901672; 16172118; 16199525; 16341674; 16376985; 16410245; 16436379; 16439990; 16529740; 16645094; 16712791; 16794010; 16847458; 16874066; 16978419; 16988840; 17015472; 17074758; 17188240; 17227835; 17235284; 17289999; 17353931; 17513609; 17686864; 17698840; 17699158; 17724463; 17879944; 17880809; 17927446; 17991745; 18056640; 18178565; 18251703; 18299329; 18309324; 18349538; 18362892; 18387192; 18413764; 18471982; 18472157; 18524770; 18593893; 18636124; 18665919; 18676680; 18715924; 18927073; 19041633; 19056676; 19060904; 19074885; 19135534; 19148187; 19168699; 19170196; 19255499; 19282307; 19343496; 19351886; 19381065; 19463775; 19481066; 19483681; 19514060; 19587033; 19593445; 19625176; 19692168; 19820697; 19875445; 19898928; 19913121; 19955184; 20034877; 20139978; 20308427; 20428767; 20453000; 20460378; 20503275; 20561923; 20618440; 20628086; 20629644; 20836993; 20855536; 20877624; 20930068; 20959805; 20978950; 21036904; 21041309; 21148306; 21158936; 21159883; 21196599; 21233848; 21613222; 21617256; 21656147; 21658363; 21712378; 21726118; 21727192; 21852253; 21900206; 21988832; 22024133; 22056880; 22065578; 22072546; 22139419; 22188816; 22253918; 22257632; 22297299; 22354970; 22378505; 22423221; 22440942; 22479585; 22493436; 22504646; 22515821; 22526391; 22686245; 22700719; 22719244; 22939629; 23140172; 23189150; 23192964; 23217248; 23229512; 23242420; 23251661; 23263863; 23283967; 23303126; 23389372; 23404709; 23480852; 23604079; 23666239; 23666240; 23770605; 23798675; 23928699; 23954442; 23954445; 23966164; 24026423; 24074954; 24097825; 24100034; 24265320 BCL2-antagonist/killer 1 Ensembl:ENSG00000030110 HGNC:949 HPRD:02744 MIM:600516 Vega:OTTHUMG00000014530 Other designations: BCL2-like 7 protein|apoptosis regulator BAK|bcl-2 homologous antagonist/killer|bcl-2-like protein 7|bcl2-L-7|pro-apoptotic protein BAK BAK1 gene OGG:3000000581 Bin Zhao, Yue Liu, Oliver He BCL2L4 WEB: http://www.ncbi.nlm.nih.gov/gene BAX BCL2-associated X protein 581 19q13.3-q13.4 9606 19 Official from a nomenclature committee GO_0001101 (EC: IEA); GO_0001541 (EC: IEA); GO_0001764 (EC: IEA); GO_0001777 (EC: IEA); GO_0001782 (EC: IEA); GO_0001783 (EC: IDA, PMID: 15214043); GO_0001822 (EC: IEA); GO_0001836 (EC: IDA, PMID: 16199525); GO_0001844 (EC: IEA); GO_0001974 (EC: IEA); GO_0002262 (EC: IEA); GO_0002352 (EC: IEA); GO_0002358 (EC: IEA); GO_0002904 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10753914); GO_0005634 (EC: IMP, PMID: 15102863); GO_0005739 (EC: IDA, PMID: 11912183); GO_0005741 (EC: IBA); GO_0005741 (EC: TAS); GO_0005757 (EC: IDA, PMID: 9843949); GO_0005783 (EC: IDA, PMID: 16424160); GO_0005789 (EC: IDA, PMID: 16424160); GO_0005829 (EC: IDA, PMID: 11912183); GO_0005829 (EC: TAS); GO_0006687 (EC: IEA); GO_0006808 (EC: IEA); GO_0006915 (EC: NAS, PMID: 9920818); GO_0006915 (EC: TAS); GO_0006919 (EC: IDA, PMID: 11912183); GO_0006919 (EC: IMP, PMID: 11350920); GO_0006927 (EC: IMP, PMID: 10739008); GO_0007281 (EC: IEA); GO_0008053 (EC: IDA, PMID: 14769861); GO_0008289 (EC: IDA, PMID: 14522999); GO_0008625 (EC: IC, PMID: 16199525); GO_0008630 (EC: IBA); GO_0008635 (EC: IDA, PMID: 15214043); GO_0008637 (EC: IDA, PMID: 9843949); GO_0009566 (EC: IEA); GO_0009636 (EC: IDA, PMID: 16307838); GO_0009651 (EC: IEA); GO_0010248 (EC: IDA, PMID: 9843949); GO_0010332 (EC: IEA); GO_0015267 (EC: IDA, PMID: 9219694); GO_0016032 (EC: IEA); GO_0021854 (EC: IEA); GO_0021987 (EC: IEA); GO_0030264 (EC: IEA); GO_0032091 (EC: IDA, PMID: 9388232); GO_0032461 (EC: IDA, PMID: 19805544); GO_0032469 (EC: TAS, PMID: 18309324); GO_0032471 (EC: IEA); GO_0032976 (EC: IDA, PMID: 9843949); GO_0033137 (EC: IEA); GO_0033599 (EC: IEA); GO_0034644 (EC: IEA); GO_0035234 (EC: IEA); GO_0042475 (EC: IEA); GO_0042802 (EC: IPI, PMID: 10620504); GO_0042803 (EC: IDA, PMID: 16608847); GO_0042803 (EC: IPI, PMID: 9111042); GO_0043065 (EC: IMP, PMID: 17289999); GO_0043496 (EC: IDA, PMID: 9111042); GO_0043497 (EC: IPI, PMID: 9111042); GO_0043524 (EC: IEA); GO_0043525 (EC: IDA, PMID: 15637643); GO_0043653 (EC: IDA, PMID: 12499352); GO_0045136 (EC: IEA); GO_0046666 (EC: IEA); GO_0046930 (EC: IDA, PMID: 9219694); GO_0046982 (EC: IPI, PMID: 9111042); GO_0048087 (EC: IEA); GO_0048147 (EC: IEA); GO_0048515 (EC: IEA); GO_0048597 (EC: IEA); GO_0048678 (EC: IEA); GO_0048873 (EC: IEA); GO_0051259 (EC: IDA, PMID: 19074440); GO_0051260 (EC: IDA, PMID: 14522999); GO_0051281 (EC: IEA); GO_0051402 (EC: IEA); GO_0051434 (EC: IDA); GO_0051434 (EC: IPI, PMID: 15705586); GO_0051726 (EC: IEA); GO_0051881 (EC: IDA, PMID: 9843949); GO_0060011 (EC: IEA); GO_0060041 (EC: IEA); GO_0060058 (EC: IEA); GO_0060068 (EC: IEA); GO_0070059 (EC: IMP, PMID: 16645094); GO_0070062 (EC: IDA); GO_0070242 (EC: IEA); GO_0071310 (EC: IEA); GO_0072332 (EC: IEA); GO_0090200 (EC: IDA, PMID: 14963330); GO_0097136 (EC: IDA); GO_0097144 (EC: IDA, PMID: 19767770); GO_0097190 (EC: IDA, PMID: 16424160); GO_0097191 (EC: IDA, PMID: 15214043); GO_0097192 (EC: IBA); GO_0097193 (EC: IDA, PMID: 16462759); GO_0097193 (EC: TAS); GO_0097296 (EC: IEA); GO_1900103 (EC: IMP, PMID: 16645094); GO_1901030 (EC: TAS); GO_1902262 (EC: IEA); GO_1902263 (EC: IEA); GO_1902512 (EC: IMP, PMID: 11350920); GO_1990009 (EC: IMP, PMID: 10702418); GO_1990117 (EC: IDA, PMID: 15214043); GO_2001234 (EC: IEA); GO_2001241 (EC: IEA); GO_2001244 (EC: IMP, PMID: 14963330) PMID: 7566098; 7607685; 7834749; 8358790; 8521816; 8580080; 8760290; 8889548; 8961277; 9020077; 9027312; 9111042; 9130713; 9153240; 9219694; 9372935; 9388232; 9449720; 9463381; 9531611; 9565621; 9742125; 9748162; 9824152; 9843949; 9920818; 9988273; 10200447; 10365962; 10381646; 10437917; 10620504; 10620603; 10620799; 10629050; 10702418; 10716992; 10739008; 10753914; 10772918; 10837489; 10854321; 10908576; 10942389; 11060313; 11106734; 11136736; 11161816; 11175251; 11175336; 11251969; 11259440; 11278245; 11283018; 11350920; 11437653; 11571294; 11574543; 11602639; 11642719; 11742726; 11759059; 11759062; 11782443; 11787859; 11839668; 11839683; 11842081; 11850803; 11850816; 11852106; 11867266; 11869962; 11875499; 11894116; 11899739; 11909872; 11911971; 11912124; 11912183; 11922616; 11929871; 11932420; 11943780; 11949842; 11992551; 11994280; 11997495; 12023951; 12025227; 12032841; 12036888; 12058280; 12070030; 12070120; 12082629; 12137781; 12151395; 12161031; 12165421; 12169275; 12176904; 12189556; 12193163; 12214154; 12215338; 12215842; 12270344; 12359369; 12388688; 12389125; 12393866; 12393884; 12408758; 12419244; 12426317; 12439925; 12445631; 12454021; 12477729; 12477932; 12481899; 12490315; 12496485; 12499352; 12510156; 12575534; 12579342; 12583439; 12592374; 12606781; 12732850; 12737446; 12743423; 12749011; 12767928; 12782632; 12808108; 12816867; 12837286; 12839682; 12853473; 12901880; 12907654; 12917444; 12963997; 12970744; 14522999; 14550297; 14559989; 14596892; 14606101; 14612448; 14612938; 14628086; 14631373; 14634023; 14647416; 14647455; 14661970; 14681224; 14698203; 14704000; 14714449; 14716828; 14719078; 14730312; 14752512; 14766748; 14767525; 14769861; 14963330; 14971737; 14980220; 15024076; 15033690; 15037603; 15073604; 15077116; 15096513; 15102863; 15131699; 15148411; 15149158; 15158440; 15214043; 15231068; 15254227; 15258908; 15262986; 15292938; 15298965; 15302859; 15304079; 15314639; 15322047; 15351796; 15375594; 15375604; 15383280; 15388581; 15459197; 15467752; 15484294; 15489334; 15516208; 15555592; 15574335; 15607964; 15613549; 15637055; 15637643; 15638363; 15642728; 15655830; 15657356; 15688029; 15694358; 15705586; 15710329; 15735127; 15735709; 15743033; 15743760; 15757910; 15764647; 15767261; 15770735; 15773546; 15782132; 15806163; 15830715; 15832769; 15843890; 15846375; 15889622; 15893728; 15901672; 15949439; 15962362; 16009130; 16010425; 16085058; 16113678; 16132718; 16139338; 16148027; 16151013; 16172114; 16172118; 16186627; 16199525; 16215676; 16229013; 16235026; 16246184; 16307023; 16307838; 16344548; 16380996; 16410245; 16424160; 16436379; 16443387; 16462759; 16472763; 16479009; 16485142; 16518869; 16538501; 16552754; 16568093; 16572399; 16575548; 16603637; 16608847; 16611260; 16642033; 16645094; 16709574; 16810067; 16830365; 16832704; 16855163; 16874066; 16946732; 16949642; 16987815; 17007374; 17015472; 17015762; 17052454; 17067385; 17074758; 17084966; 17091766; 17097560; 17107772; 17118768; 17140287; 17171827; 17203183; 17203211; 17213822; 17235284; 17274640; 17289842; 17289999; 17335847; 17346710; 17388661; 17390059; 17395004; 17404017; 17426704; 17438366; 17438390; 17486058; 17494694; 17496930; 17499214; 17509221; 17513609; 17519046; 17525161; 17534116; 17535899; 17556360; 17562177; 17575222; 17626754; 17634542; 17635522; 17635912; 17643375; 17666167; 17668322; 17676485; 17686764; 17693666; 17803695; 17823127; 17855051; 17880809; 17897954; 17900801; 17905238; 17911107; 17912641; 17927446; 17927572; 17978676; 17981213; 17990907; 17993285; 17996028; 17997990; 18006502; 18006817; 18006836; 18019411; 18023359; 18029348; 18034190; 18054155; 18059532; 18074738; 18089567; 18158779; 18160666; 18177350; 18178565; 18193434; 18195012; 18211414; 18214681; 18223689; 18240345; 18251703; 18258596; 18259190; 18259191; 18282575; 18299320; 18299329; 18307410; 18309324; 18331646; 18344566; 18362350; 18362892; 18375382; 18390829; 18395515; 18415681; 18415689; 18445700; 18449500; 18453545; 18454316; 18462830; 18472156; 18472157; 18474606; 18481805; 18494554; 18508723; 18511705; 18534994; 18546202; 18563851; 18568448; 18590739; 18590778; 18594472; 18636124; 18642056; 18644472; 18651163; 18651223; 18664350; 18665919; 18670882; 18676372; 18676680; 18692524; 18695676; 18705408; 18705844; 18718060; 18719392; 18727869; 18772168; 18793611; 18812638; 18813857; 18814044; 18818203; 18818304; 18835031; 18840646; 18925695; 18928586; 18928588; 18936968; 18941118; 18948948; 18973553; 18974096; 18979557; 19031258; 19035131; 19054058; 19056676; 19062087; 19074440; 19074885; 19101510; 19118032; 19125733; 19141860; 19148187; 19150424; 19157504; 19170196; 19177010; 19196429; 19221769; 19228953; 19237173; 19247369; 19265193; 19266703; 19278624; 19319745; 19336552; 19351510; 19360919; 19363595; 19376889; 19380879; 19429011; 19439449; 19439472; 19453261; 19463775; 19475409; 19481066; 19494020; 19541585; 19564333; 19573080; 19587033; 19625176; 19629483; 19636580; 19655415; 19657228; 19660860; 19680558; 19692168; 19692349; 19700502; 19723045; 19729672; 19737817; 19745831; 19767770; 19773279; 19801665; 19805544; 19809877; 19812265; 19846939; 19875445; 19880508; 19888426; 19895710; 19898928; 19913121; 19931389; 19937732; 19938958; 19955813; 19956635; 19968986; 20015862; 20034877; 20045442; 20075864; 20101465; 20114030; 20130137; 20140092; 20180421; 20200776; 20300062; 20308427; 20333643; 20340172; 20346360; 20360684; 20382739; 20404718; 20416158; 20423844; 20431057; 20453000; 20485298; 20490654; 20503275; 20561923; 20565851; 20584903; 20627094; 20628086; 20644561; 20652449; 20683843; 20683914; 20723294; 20723427; 20728382; 20732674; 20803149; 20819778; 20822926; 20850011; 20855536; 20877624; 20929130; 20929131; 20942963; 20959405; 20960177; 20966963; 21029589; 21041309; 21042904; 21048031; 21060336; 21067292; 21069436; 21070973; 21090097; 21104343; 21115898; 21122152; 21123558; 21138867; 21139048; 21148306; 21156403; 21159883; 21173168; 21196320; 21199865; 21223758; 21245196; 21289292; 21367852; 21414921; 21458670; 21483469; 21506333; 21521785; 21530645; 21565982; 21567405; 21597469; 21606679; 21642427; 21642428; 21674599; 21695182; 21706237; 21712378; 21717192; 21725926; 21729540; 21746927; 21751259; 21752397; 21778226; 21785112; 21810274; 21819468; 21847364; 21852238; 21861179; 21862870; 21883444; 21887277; 21890473; 21903925; 21906983; 21907236; 21936009; 21947543; 21949851; 21952639; 21953454; 21978892; 22014978; 22015607; 22037145; 22052011; 22053931; 22056880; 22065578; 22067154; 22072718; 22109662; 22141411; 22159712; 22189282; 22198199; 22201672; 22246181; 22262057; 22277657; 22278385; 22292626; 22297694; 22309278; 22366766; 22418443; 22440942; 22442678; 22479585; 22484496; 22524261; 22526391; 22544745; 22552851; 22560721; 22570867; 22590594; 22629415; 22645134; 22668011; 22675938; 22685558; 22707322; 22710714; 22719244; 22729748; 22732402; 22736223; 22745744; 22748563; 22761420; 22785534; 22852863; 22860893; 22892098; 22906710; 22910913; 22926545; 22949938; 22995373; 23000965; 23038985; 23049480; 23064052; 23088735; 23140172; 23151078; 23151600; 23170075; 23213219; 23220614; 23245210; 23283967; 23289213; 23291169; 23295106; 23297497; 23324193; 23329846; 23334076; 23383273; 23389372; 23392123; 23421021; 23421973; 23442864; 23479508; 23479509; 23487455; 23543151; 23553948; 23562578; 23658815; 23682076; 23744079; 23777485; 23788040; 23824909; 23900080; 23900644; 23907458; 23907941; 23908591; 23966164; 24055994; 24074954; 24100034; 24113173; 24161344; 24200861; 24379070 BCL2-associated X protein Ensembl:ENSG00000087088 HGNC:959 HPRD:02498 MIM:600040 Vega:OTTHUMG00000160476 Other designations: BCL2-associated X protein omega|BCL2-associated X protein transcript variant delta2|apoptosis regulator BAX|bcl-2-like protein 4|bcl2-L-4 BAX gene OGG:3000000595 Bin Zhao, Yue Liu, Oliver He BCL1 D11S287E PRAD1 U21B31 WEB: http://www.ncbi.nlm.nih.gov/gene CCND1 cyclin D1 595 11q13 9606 11 Official from a nomenclature committee GO_0000082 (EC: IDA, PMID: 19412162); GO_0000082 (EC: TAS, PMID: 18483258); GO_0000122 (EC: IDA, PMID: 16569215); GO_0000278 (EC: TAS); GO_0000307 (EC: IDA, PMID: 17420273); GO_0000320 (EC: IEA); GO_0001889 (EC: IEA); GO_0001934 (EC: IDA, PMID: 8114739); GO_0003714 (EC: IDA, PMID: 16569215); GO_0004672 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15232106); GO_0005622 (EC: IDA); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005829 (EC: TAS); GO_0005923 (EC: IEA); GO_0006351 (EC: IEA); GO_0006974 (EC: IDA, PMID: 19412162); GO_0007219 (EC: TAS); GO_0007595 (EC: IEA); GO_0008134 (EC: IPI, PMID: 16569215); GO_0010039 (EC: IEA); GO_0010165 (EC: IEA); GO_0010243 (EC: IEA); GO_0010971 (EC: IDA, PMID: 19124461); GO_0016020 (EC: IEA); GO_0016538 (EC: IEA); GO_0017053 (EC: IDA, PMID: 16569215); GO_0019899 (EC: IPI, PMID: 19412162); GO_0019901 (EC: IPI, PMID: 19124461); GO_0030178 (EC: IEA); GO_0030857 (EC: IEA); GO_0030968 (EC: IEA); GO_0031100 (EC: IEA); GO_0031571 (EC: IDA, PMID: 19412162); GO_0032026 (EC: IEA); GO_0032403 (EC: IEA); GO_0033197 (EC: IEA); GO_0033327 (EC: IEA); GO_0033598 (EC: IEA); GO_0033601 (EC: IEA); GO_0042493 (EC: IEP, PMID: 18291362); GO_0042826 (EC: IPI, PMID: 18417529); GO_0043627 (EC: IEA); GO_0045444 (EC: IEA); GO_0045471 (EC: IEA); GO_0045737 (EC: IDA, PMID: 8114739); GO_0051301 (EC: IEA); GO_0051412 (EC: IEA); GO_0051592 (EC: IEA); GO_0060070 (EC: IEA); GO_0060749 (EC: IEA); GO_0070064 (EC: IDA, PMID: 19124461); GO_0070141 (EC: IDA, PMID: 18483258); GO_0071157 (EC: IDA, PMID: 19124461) PMID: 1386335; 1532244; 1535701; 1682919; 1826542; 1827756; 1833066; 1833629; 6610211; 7478582; 7568034; 7665234; 7687458; 7733934; 7739547; 7903056; 7908906; 8058338; 8058751; 8101826; 8114739; 8134134; 8136159; 8159685; 8204893; 8208539; 8259215; 8302605; 8490963; 8643455; 8647086; 8657154; 8662825; 8756624; 8826947; 8867812; 8887674; 8978686; 8999999; 9003781; 9039267; 9050835; 9106657; 9139732; 9150368; 9178893; 9190208; 9228064; 9244350; 9311993; 9372967; 9380698; 9426067; 9626345; 9632134; 9661876; 9736735; 9832502; 9832503; 9837900; 9926939; 10066798; 10202152; 10318892; 10344732; 10353443; 10371345; 10486249; 10491434; 10500095; 10580009; 10581175; 10645009; 10764802; 10766840; 10801854; 10850422; 10908655; 10910956; 10952989; 11042687; 11073968; 11076863; 11126356; 11256614; 11279133; 11311237; 11360184; 11470749; 11593423; 11642719; 11696452; 11698342; 11698641; 11739785; 11739795; 11751903; 11788592; 11793365; 11805292; 11813305; 11815623; 11836555; 11838966; 11860939; 11870667; 11872630; 11884610; 11896626; 11902820; 11923474; 11935308; 11940657; 11948404; 11958128; 11986316; 11992406; 12002755; 12006580; 12007188; 12024041; 12036888; 12036906; 12036934; 12036951; 12048199; 12067972; 12096344; 12097293; 12101670; 12127555; 12138206; 12150453; 12151312; 12164325; 12203362; 12209953; 12231535; 12237776; 12241561; 12364325; 12376514; 12379776; 12383116; 12388769; 12391146; 12394763; 12439750; 12444551; 12455063; 12477932; 12480939; 12515730; 12519773; 12529437; 12539042; 12554669; 12557224; 12569141; 12582032; 12589056; 12594215; 12601350; 12606305; 12607604; 12634633; 12673692; 12676926; 12680219; 12692418; 12694349; 12707028; 12738746; 12743597; 12746453; 12759391; 12761882; 12778072; 12807740; 12808109; 12824903; 12825853; 12867429; 12883688; 12883749; 12894561; 12896908; 12899785; 12914697; 12917336; 12917338; 12921950; 12930597; 12937137; 12955092; 12965081; 12972956; 14530270; 14612904; 14641107; 14645506; 14645576; 14646596; 14657069; 14666635; 14666673; 14666699; 14679024; 14688016; 14689059; 14701845; 14703063; 14720512; 14754892; 14759115; 14764597; 14767060; 14966901; 14981950; 15059606; 15060836; 15063389; 15090460; 15128059; 15133490; 15138714; 15153436; 15172998; 15203873; 15225161; 15226187; 15232106; 15239347; 15245939; 15277517; 15282324; 15297421; 15350626; 15355984; 15375804; 15377668; 15378006; 15485920; 15489334; 15489336; 15498584; 15505422; 15513923; 15538282; 15539430; 15544931; 15545188; 15551329; 15557280; 15557752; 15558026; 15578074; 15580291; 15592430; 15621754; 15652748; 15655836; 15659654; 15668481; 15684604; 15688030; 15695117; 15695403; 15709184; 15713663; 15734847; 15735724; 15754315; 15755896; 15776189; 15791567; 15808510; 15809880; 15811121; 15824172; 15845652; 15856299; 15861516; 15862753; 15863141; 15870300; 15878868; 15893730; 15896460; 15897899; 15900590; 15914210; 15923181; 15943036; 15949570; 15950906; 15951302; 15951563; 15971196; 15981100; 16051426; 16061635; 16082198; 16115225; 16123218; 16131791; 16142313; 16155412; 16163549; 16163738; 16166625; 16172916; 16174239; 16207592; 16226824; 16258726; 16258756; 16273238; 16287839; 16322291; 16328437; 16334487; 16341674; 16343742; 16357142; 16381901; 16399423; 16406195; 16407831; 16436505; 16461912; 16488657; 16490596; 16495921; 16507767; 16508013; 16547504; 16552496; 16568089; 16569215; 16600870; 16601140; 16614707; 16614728; 16616093; 16638786; 16644723; 16645724; 16672066; 16690963; 16691558; 16691626; 16699726; 16705174; 16723714; 16732330; 16758952; 16776827; 16782892; 16783567; 16788380; 16804724; 16815198; 16820873; 16829689; 16832876; 16843438; 16860316; 16865250; 16870553; 16884382; 16912209; 16916940; 16924241; 16940298; 16942622; 16959222; 16980615; 16985050; 17011980; 17018901; 17022831; 17046823; 17053782; 17060721; 17067457; 17070615; 17080657; 17081987; 17090192; 17106256; 17116943; 17129455; 17139501; 17188136; 17198740; 17203162; 17203214; 17205132; 17207971; 17208333; 17240151; 17254966; 17274640; 17278098; 17284370; 17299095; 17308274; 17310991; 17316413; 17334399; 17344214; 17374178; 17393422; 17398034; 17409409; 17420273; 17427198; 17437044; 17438373; 17447856; 17482347; 17486065; 17499716; 17509221; 17517369; 17517622; 17524364; 17525627; 17549378; 17556661; 17561354; 17600882; 17605237; 17606477; 17606765; 17607588; 17616526; 17616699; 17626745; 17629555; 17634024; 17653856; 17684142; 17693985; 17695500; 17698033; 17720094; 17724472; 17804732; 17848143; 17855508; 17868090; 17881732; 17882269; 17901853; 17906980; 17908995; 17912028; 17916995; 17922974; 17923265; 17927591; 17927853; 17934069; 17935714; 17941827; 17960397; 18006686; 18006821; 18019405; 18024283; 18027856; 18043898; 18047954; 18056951; 18061526; 18063576; 18067636; 18079202; 18171527; 18174243; 18180298; 18182398; 18187454; 18194492; 18194538; 18196581; 18197291; 18205772; 18212742; 18226366; 18237245; 18239461; 18240019; 18251939; 18281541; 18284543; 18291362; 18301453; 18306932; 18327210; 18327303; 18341653; 18343791; 18347178; 18349267; 18349392; 18355450; 18355918; 18358634; 18361427; 18367547; 18373498; 18379871; 18381935; 18393977; 18398822; 18404250; 18406353; 18413612; 18413728; 18413773; 18413827; 18417529; 18431519; 18437417; 18445313; 18456656; 18459109; 18467434; 18483258; 18483394; 18484097; 18491248; 18507837; 18514338; 18537972; 18547262; 18548202; 18562319; 18598945; 18604165; 18609126; 18616527; 18618300; 18625744; 18632615; 18640142; 18644870; 18650423; 18665038; 18665077; 18676680; 18677114; 18695042; 18695676; 18703151; 18710938; 18710949; 18713830; 18715616; 18715870; 18753363; 18758380; 18769147; 18787961; 18794045; 18794151; 18798551; 18799029; 18819000; 18822177; 18823025; 18829570; 18839518; 18842998; 18843022; 18844221; 18925698; 18936968; 18942117; 18942709; 18949380; 18950845; 18983468; 18988190; 18991334; 19009649; 19020753; 19034659; 19040567; 19047108; 19055446; 19064572; 19070887; 19071090; 19074853; 19074885; 19075005; 19080374; 19084934; 19086036; 19091404; 19096232; 19106611; 19106744; 19116388; 19124461; 19124506; 19129688; 19134409; 19136653; 19139013; 19142864; 19143767; 19147768; 19152247; 19166930; 19170196; 19183483; 19187116; 19203829; 19237565; 19242061; 19258477; 19287456; 19289374; 19302219; 19303206; 19321861; 19322201; 19324500; 19330026; 19336552; 19373442; 19375306; 19379556; 19386349; 19412162; 19415719; 19430707; 19440933; 19443866; 19448414; 19453261; 19467018; 19470470; 19470724; 19474518; 19475398; 19477949; 19489683; 19499154; 19502783; 19505905; 19525979; 19536092; 19538740; 19549773; 19550124; 19554511; 19556892; 19558863; 19564413; 19572978; 19573080; 19575018; 19578796; 19585495; 19589865; 19602458; 19625176; 19633425; 19634112; 19636701; 19638577; 19666237; 19666944; 19670700; 19679881; 19687314; 19690970; 19692168; 19706803; 19723065; 19724860; 19728335; 19738611; 19750108; 19757306; 19760977; 19773279; 19774638; 19779113; 19780858; 19787783; 19789190; 19795398; 19800042; 19801633; 19801969; 19802676; 19806481; 19821490; 19822419; 19823025; 19823825; 19826048; 19850937; 19883431; 19885547; 19898427; 19900369; 19903334; 19904758; 19915615; 19915977; 19917254; 19919588; 19921577; 19923826; 19933579; 19935879; 19940156; 19941161; 19956635; 19956831; 19967453; 20028857; 20062011; 20067552; 20072652; 20087644; 20101207; 20103831; 20113529; 20137349; 20154722; 20160059; 20172376; 20179208; 20181625; 20204303; 20204402; 20231315; 20232305; 20301636; 20304954; 20306448; 20338923; 20347627; 20359085; 20359118; 20372799; 20373052; 20380574; 20389301; 20392877; 20397048; 20401451; 20404095; 20407865; 20418097; 20426528; 20429623; 20437058; 20443083; 20453000; 20453838; 20459741; 20460515; 20466633; 20473525; 20484017; 20485284; 20503270; 20512928; 20515940; 20540739; 20543468; 20564361; 20575692; 20577923; 20578819; 20581865; 20586028; 20616110; 20618968; 20628002; 20631636; 20631637; 20631638; 20644561; 20662834; 20680537; 20680693; 20683026; 20683061; 20683643; 20699365; 20701069; 20714998; 20723296; 20727381; 20737317; 20801098; 20809334; 20822933; 20837141; 20839920; 20844743; 20856207; 20857402; 20890425; 20924203; 20950152; 20951943; 20971731; 21036743; 21042715; 21044962; 21056029; 21062395; 21079973; 21098327; 21107342; 21116504; 21131888; 21135252; 21139048; 21148318; 21159451; 21161398; 21179427; 21185249; 21187402; 21193919; 21200149; 21212260; 21242960; 21242966; 21254295; 21268129; 21273603; 21281227; 21300445; 21315112; 21315488; 21326383; 21327470; 21331989; 21343394; 21347341; 21385053; 21401699; 21410931; 21438905; 21447152; 21454057; 21455311; 21487939; 21492065; 21497295; 21498736; 21503589; 21517236; 21526487; 21537090; 21537837; 21544737; 21547408; 21548803; 21569306; 21594903; 21606015; 21654808; 21738001; 21745168; 21746927; 21777578; 21778791; 21783402; 21789902; 21799732; 21830375; 21850541; 21867613; 21890746; 21892090; 21906983; 21912938; 21946890; 21952639; 21955753; 21956468; 21963094; 21965784; 21972713; 21987572; 21988832; 21989330; 21989926; 22002566; 22024187; 22037875; 22050898; 22052559; 22065993; 22072615; 22100494; 22102309; 22133292; 22135025; 22150974; 22158041; 22204713; 22231956; 22234583; 22260073; 22261253; 22266466; 22289525; 22296356; 22304571; 22306268; 22307325; 22318732; 22321253; 22322158; 22336657; 22357515; 22369110; 22387541; 22391566; 22399638; 22406359; 22406644; 22451658; 22456513; 22460364; 22467101; 22467868; 22475046; 22484283; 22490843; 22528945; 22534667; 22553812; 22565393; 22581837; 22590809; 22606291; 22629227; 22640743; 22647349; 22647378; 22706868; 22707287; 22711989; 22722256; 22747683; 22760121; 22770229; 22776845; 22790016; 22801439; 22812184; 22814742; 22819905; 22833568; 22853846; 22864797; 22884659; 22884800; 22893700; 22901215; 22905217; 22905260; 22922827; 22926658; 22967707; 22976805; 22982899; 23000965; 23001925; 23020291; 23031786; 23044415; 23060014; 23108396; 23111452; 23125009; 23126531; 23135283; 23144465; 23161911; 23163571; 23201130; 23217712; 23222716; 23226276; 23244103; 23255553; 23261678; 23270726; 23292829; 23300886; 23311506; 23315417; 23322406; 23327593; 23354584; 23383003; 23383271; 23388457; 23390492; 23396251; 23400686; 23455922; 23502783; 23515614; 23525507; 23529990; 23540573; 23543735; 23562784; 23566410; 23568005; 23568006; 23613410; 23625206; 23625573; 23648671; 23653001; 23661346; 23664541; 23670132; 23674142; 23696923; 23707388; 23718855; 23720779; 23731275; 23733133; 23737530; 23741361; 23795354; 23804702; 23852369; 23861098; 23864650; 23873109; 23893383; 23897809; 23898488; 23920145; 23936312; 23949314; 23975835; 23985254; 23991960; 23991964; 24019069; 24060591; 24085301; 24088803; 24119401; 24134204; 24145651; 24282282; 24324055; 24403468 cyclin D1 Ensembl:ENSG00000110092 HGNC:1582 HPRD:01346 MIM:168461 Vega:OTTHUMG00000167877 Other designations: B-cell CLL/lymphoma 1|B-cell lymphoma 1 protein|BCL-1 oncogene|G1/S-specific cyclin-D1|PRAD1 oncogene CCND1 gene OGG:3000000596 Bin Zhao, Yue Liu, Oliver He Bcl-2 PPP1R50 WEB: http://www.ncbi.nlm.nih.gov/gene BCL2 B-cell CLL/lymphoma 2 596 18q21.3 9606 18 Official from a nomenclature committee GO_0000209 (EC: IDA, PMID: 16717086); GO_0001101 (EC: IEA); GO_0001503 (EC: IEA); GO_0001541 (EC: IEA); GO_0001656 (EC: IEA); GO_0001658 (EC: IEA); GO_0001662 (EC: IEA); GO_0001782 (EC: IEA); GO_0001836 (EC: ISS, PMID: 9843949); GO_0001836 (EC: NAS, PMID: 9027314); GO_0001952 (EC: IEA); GO_0002020 (EC: IDA, PMID: 10620603); GO_0002320 (EC: IEA); GO_0002326 (EC: IEA); GO_0002931 (EC: IEA); GO_0003014 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10837489); GO_0005634 (EC: IDA, PMID: 7546744); GO_0005737 (EC: IDA, PMID: 11530860); GO_0005739 (EC: IDA, PMID: 7896880); GO_0005741 (EC: IDA, PMID: 8402648); GO_0005741 (EC: TAS); GO_0005783 (EC: IDA, PMID: 8402648); GO_0005789 (EC: IEA); GO_0005829 (EC: IEA); GO_0006470 (EC: IEA); GO_0006582 (EC: IEA); GO_0006808 (EC: IEA); GO_0006915 (EC: TAS); GO_0006959 (EC: TAS, PMID: 1908951); GO_0006974 (EC: IMP, PMID: 17875758); GO_0007015 (EC: IEA); GO_0007409 (EC: IEA); GO_0007565 (EC: NAS, PMID: 11530860); GO_0007569 (EC: IEA); GO_0008134 (EC: IEA); GO_0008219 (EC: IDA, PMID: 36599); GO_0008584 (EC: IEA); GO_0008625 (EC: IDA, PMID: 10597216); GO_0008630 (EC: IBA); GO_0008631 (EC: IEA); GO_0009314 (EC: NAS, PMID: 15799693); GO_0009636 (EC: IDA, PMID: 16307838); GO_0009791 (EC: IEA); GO_0010039 (EC: IDA, PMID: 11264898); GO_0010224 (EC: IEA); GO_0010332 (EC: IEA); GO_0010507 (EC: TAS, PMID: 18309324); GO_0010523 (EC: IEA); GO_0010559 (EC: IEA); GO_0014031 (EC: IEA); GO_0014042 (EC: IEA); GO_0014911 (EC: IEA); GO_0015267 (EC: IDA, PMID: 9219694); GO_0016020 (EC: IDA, PMID: 7896880); GO_0016049 (EC: IEA); GO_0016248 (EC: IDA, PMID: 9219694); GO_0016337 (EC: IEA); GO_0018105 (EC: IEA); GO_0018107 (EC: IEA); GO_0021747 (EC: IEA); GO_0022612 (EC: IEA); GO_0022898 (EC: IDA, PMID: 9219694); GO_0030279 (EC: IEA); GO_0030307 (EC: IDA, PMID: 8022822); GO_0030308 (EC: IEA); GO_0030318 (EC: IEA); GO_0030336 (EC: IEA); GO_0030890 (EC: IMP, PMID: 17875758); GO_0031069 (EC: IEA); GO_0031103 (EC: IEA); GO_0031625 (EC: IPI); GO_0031647 (EC: IEA); GO_0031965 (EC: IDA, PMID: 1502141); GO_0032469 (EC: TAS, PMID: 18309324); GO_0032835 (EC: IEA); GO_0032848 (EC: IDA, PMID: 10506221); GO_0033033 (EC: IEA); GO_0033077 (EC: IEA); GO_0033138 (EC: IEA); GO_0033689 (EC: IEA); GO_0034097 (EC: IDA, PMID: 9184696); GO_0035094 (EC: IDA, PMID: 12421819); GO_0035265 (EC: IEA); GO_0035872 (EC: TAS); GO_0040018 (EC: IEA); GO_0042100 (EC: IDA, PMID: 1373874); GO_0042149 (EC: IEA); GO_0042493 (EC: IDA, PMID: 36599); GO_0042493 (EC: IMP, PMID: 17875758); GO_0042542 (EC: IEA); GO_0042802 (EC: IPI, PMID: 18835031); GO_0042803 (EC: IPI, PMID: 9111042); GO_0043029 (EC: IEA); GO_0043066 (EC: IDA, PMID: 10506221); GO_0043066 (EC: IMP, PMID: 17289999); GO_0043085 (EC: IEA); GO_0043209 (EC: IEA); GO_0043375 (EC: IEA); GO_0043496 (EC: IDA, PMID: 9111042); GO_0043497 (EC: IDA, PMID: 9111042); GO_0043524 (EC: IDA, PMID: 7546744); GO_0043565 (EC: IDA, PMID: 12086670); GO_0043583 (EC: IEA); GO_0045069 (EC: IEA); GO_0045087 (EC: TAS); GO_0045636 (EC: IEA); GO_0045930 (EC: IEA); GO_0046671 (EC: IEA); GO_0046902 (EC: ISS, PMID: 9843949); GO_0046930 (EC: IDA, PMID: 9219694); GO_0046982 (EC: IPI, PMID: 9111042); GO_0048041 (EC: IEA); GO_0048536 (EC: IEA); GO_0048538 (EC: IEA); GO_0048546 (EC: IEA); GO_0048589 (EC: IEA); GO_0048599 (EC: IEA); GO_0048743 (EC: IEA); GO_0048753 (EC: IEA); GO_0048873 (EC: IEA); GO_0050853 (EC: IMP, PMID: 17875758); GO_0051384 (EC: IEA); GO_0051402 (EC: TAS, PMID: 16167175); GO_0051434 (EC: IPI, PMID: 9111042); GO_0051607 (EC: IDA, PMID: 10620603); GO_0051721 (EC: IEA); GO_0051881 (EC: ISS, PMID: 9843949); GO_0051902 (EC: TAS, PMID: 9027314); GO_0051924 (EC: IDA, PMID: 8022822); GO_0055085 (EC: IDA, PMID: 9219694); GO_0070059 (EC: IDA, PMID: 15776018); GO_0071310 (EC: IEA); GO_0071456 (EC: IEA); GO_0072593 (EC: IEA); GO_0097192 (EC: IEA); GO_0097193 (EC: TAS); GO_1900740 (EC: TAS); GO_2000134 (EC: IEA); GO_2000811 (EC: IMP, PMID: 15006356); GO_2001234 (EC: IMP); GO_2001240 (EC: IGI, PMID: 8358790); GO_2001243 (EC: IDA, PMID: 11684014); GO_2001244 (EC: TAS) PMID: 36599; 1339299; 1373874; 1453000; 1502141; 1508712; 1908951; 2250705; 2834197; 2875799; 3285301; 3523487; 3924412; 7546744; 7579350; 7593193; 7650367; 7753817; 7772249; 7834748; 7896880; 7929424; 7954800; 8022822; 8050499; 8080725; 8090743; 8183370; 8232588; 8358790; 8402618; 8402648; 8551385; 8668206; 8760290; 8790371; 8910675; 8929532; 8949945; 9027314; 9031086; 9070836; 9109491; 9111042; 9115213; 9119086; 9130713; 9184696; 9219694; 9226175; 9226228; 9305631; 9334338; 9389483; 9395403; 9430630; 9449720; 9463381; 9488477; 9525867; 9561195; 9660918; 9668078; 9727491; 9731710; 9738012; 9765397; 9788433; 9843949; 9852076; 9973195; 10072505; 10075695; 10198631; 10217402; 10329560; 10330179; 10354271; 10417825; 10467396; 10490827; 10506221; 10521466; 10567572; 10597216; 10620603; 10620799; 10622714; 10625696; 10669763; 10677502; 10679027; 10716992; 10807576; 10837489; 10848600; 10871848; 10949025; 11054413; 11060313; 11123279; 11126360; 11158204; 11175251; 11181702; 11206074; 11262395; 11264898; 11278245; 11323417; 11325850; 11326318; 11368354; 11390485; 11406564; 11437653; 11463391; 11463392; 11483855; 11495898; 11513873; 11527400; 11530860; 11546872; 11583631; 11642719; 11684014; 11728179; 11752215; 11759059; 11759062; 11774038; 11776759; 11787859; 11790116; 11804283; 11804688; 11815602; 11832478; 11839683; 11855781; 11856759; 11861644; 11864421; 11867266; 11871856; 11877091; 11877266; 11877309; 11877669; 11877670; 11908736; 11914580; 11929874; 11940482; 11948397; 11949842; 11949843; 11956602; 11959101; 11964319; 11971816; 11983915; 11986946; 11988841; 11994280; 11999565; 12000759; 12011972; 12019168; 12025227; 12031912; 12032828; 12032841; 12036852; 12036886; 12036888; 12039864; 12046064; 12054739; 12054916; 12070027; 12082633; 12086670; 12086875; 12095980; 12095993; 12096338; 12101183; 12112824; 12118096; 12133494; 12133517; 12137781; 12140755; 12151395; 12161031; 12162425; 12165497; 12167335; 12170763; 12171774; 12172977; 12174951; 12186923; 12189556; 12197229; 12197771; 12207028; 12209154; 12209955; 12214154; 12215338; 12217802; 12234263; 12270344; 12393707; 12400004; 12404120; 12420213; 12421819; 12431997; 12439925; 12440815; 12452037; 12477721; 12477729; 12477932; 12480939; 12481899; 12488548; 12490308; 12499093; 12510149; 12510191; 12513829; 12515824; 12530303; 12532420; 12533044; 12540563; 12575534; 12579337; 12581249; 12583439; 12613529; 12617962; 12624108; 12629413; 12637332; 12667443; 12670866; 12684626; 12686415; 12694817; 12698366; 12702730; 12720100; 12721288; 12721767; 12722479; 12729794; 12749011; 12751031; 12754350; 12756585; 12759537; 12815463; 12819863; 12821128; 12835724; 12839682; 12853473; 12879322; 12890751; 12890867; 12901880; 12937123; 12938158; 12939460; 12960134; 12960340; 12970736; 13130506; 14519627; 14529662; 14554083; 14555646; 14558950; 14572466; 14612291; 14627346; 14628086; 14631373; 14647416; 14647426; 14660675; 14679209; 14689061; 14698203; 14699151; 14714449; 14724650; 14737118; 14739602; 14754534; 14764541; 14767525; 14769789; 14964781; 14966123; 14971737; 14980220; 14999286; 15006356; 15024706; 15026553; 15033793; 15033825; 15033827; 15034060; 15051039; 15057274; 15061204; 15093750; 15115329; 15123638; 15124764; 15149157; 15149158; 15156398; 15179054; 15196944; 15203866; 15210690; 15225643; 15231068; 15231831; 15233914; 15235941; 15243561; 15245329; 15261486; 15263017; 15274378; 15280201; 15302859; 15303767; 15314290; 15314639; 15329319; 15339676; 15340216; 15344336; 15345651; 15351796; 15353294; 15367432; 15375594; 15467428; 15467450; 15478112; 15484294; 15489334; 15489891; 15492114; 15498929; 15520201; 15528355; 15541642; 15544840; 15545228; 15547950; 15561778; 15563082; 15572421; 15574335; 15577328; 15584904; 15593417; 15605273; 15613488; 15619620; 15633216; 15634885; 15638363; 15657349; 15657350; 15694340; 15716988; 15720412; 15720419; 15733859; 15735709; 15754411; 15757646; 15757977; 15763593; 15776018; 15799693; 15800682; 15803126; 15811121; 15817479; 15826766; 15830715; 15832179; 15832769; 15837573; 15840562; 15849194; 15876860; 15880952; 15889622; 15901672; 15907209; 15911345; 15929186; 15965276; 15981087; 15990872; 16007339; 16010987; 16120388; 16132718; 16133992; 16139338; 16148027; 16166262; 16167175; 16173075; 16181427; 16186627; 16186795; 16194898; 16195370; 16199534; 16204228; 16215670; 16215945; 16227396; 16228292; 16235026; 16243795; 16246184; 16273250; 16307838; 16308474; 16358373; 16434970; 16438077; 16443602; 16463650; 16469847; 16472763; 16479062; 16481323; 16520895; 16530191; 16533178; 16533807; 16538384; 16541314; 16545683; 16550596; 16554306; 16566921; 16568081; 16575548; 16636671; 16638854; 16638864; 16642033; 16648655; 16675913; 16690525; 16697956; 16707568; 16714000; 16717086; 16732934; 16733517; 16735440; 16750039; 16761743; 16777355; 16790527; 16799010; 16820876; 16832704; 16839413; 16840204; 16841088; 16850164; 16855163; 16874461; 16949642; 16950491; 16960146; 16980304; 16982461; 16984978; 16988783; 16998187; 17007374; 17015762; 17050165; 17074584; 17082179; 17090549; 17091766; 17097560; 17118768; 17145812; 17188136; 17191123; 17200714; 17203183; 17207023; 17241114; 17252199; 17259174; 17272502; 17274640; 17289999; 17290286; 17295204; 17301078; 17310847; 17325632; 17356300; 17360176; 17363905; 17372162; 17379544; 17379601; 17384650; 17404013; 17418785; 17426248; 17434928; 17438366; 17439414; 17464868; 17473827; 17507655; 17516030; 17516614; 17534194; 17536310; 17557568; 17561354; 17575222; 17588340; 17616686; 17626754; 17632732; 17652637; 17666167; 17670745; 17675494; 17692808; 17693666; 17701916; 17713095; 17727680; 17785366; 17785460; 17825790; 17848143; 17848408; 17852408; 17875758; 17880809; 17882791; 17893147; 17893875; 17905238; 17908970; 17909067; 17909078; 17912028; 17913397; 17916073; 17920946; 17936584; 17942410; 17957472; 17959858; 17960583; 17978676; 17981569; 17989874; 18006836; 18021997; 18023359; 18026954; 18037229; 18041310; 18046447; 18046449; 18046541; 18055344; 18059532; 18063429; 18069888; 18073527; 18079751; 18091321; 18156504; 18158619; 18160396; 18162459; 18174230; 18178565; 18182854; 18189268; 18199533; 18203018; 18215418; 18220834; 18228020; 18240345; 18248353; 18263880; 18279996; 18309324; 18313386; 18314333; 18327814; 18334006; 18342927; 18343029; 18357521; 18363112; 18367485; 18375822; 18382371; 18386458; 18398703; 18407350; 18410632; 18411730; 18415681; 18415689; 18426731; 18427947; 18428028; 18430249; 18438339; 18450493; 18458532; 18465329; 18468253; 18472157; 18474261; 18478476; 18493992; 18505729; 18508827; 18510726; 18516322; 18516673; 18534064; 18534994; 18538438; 18543286; 18561741; 18566606; 18568671; 18568776; 18568946; 18570871; 18572327; 18573594; 18594472; 18595518; 18622426; 18633450; 18636124; 18651163; 18652313; 18653721; 18657507; 18664350; 18675369; 18687309; 18692524; 18695675; 18695940; 18705844; 18712678; 18719108; 18727869; 18752503; 18758240; 18758641; 18769111; 18769121; 18788571; 18794804; 18806751; 18813857; 18818203; 18835031; 18838868; 18928586; 18928588; 18928590; 18929412; 18940474; 18949393; 18957415; 18983973; 18985814; 18998362; 19002577; 19020723; 19027288; 19035131; 19048366; 19050681; 19058789; 19060592; 19064571; 19074885; 19080514; 19107326; 19107575; 19107861; 19124070; 19138978; 19141121; 19141860; 19152170; 19157504; 19160418; 19168699; 19195736; 19196738; 19205434; 19228691; 19237173; 19238538; 19240654; 19250983; 19253527; 19260506; 19266703; 19269343; 19272801; 19276283; 19280241; 19287190; 19287965; 19298794; 19318089; 19336552; 19348791; 19351510; 19351886; 19360919; 19379569; 19380879; 19385591; 19390575; 19395874; 19398149; 19404232; 19417623; 19429088; 19448593; 19452318; 19453261; 19460716; 19473442; 19475409; 19477129; 19484260; 19495739; 19520430; 19520857; 19521340; 19535347; 19535901; 19537891; 19539330; 19540934; 19541585; 19549844; 19550126; 19556603; 19557638; 19560836; 19573080; 19576799; 19582475; 19585117; 19589501; 19597184; 19602458; 19605509; 19620938; 19625133; 19627536; 19634687; 19636371; 19655415; 19656156; 19664395; 19671677; 19676105; 19706527; 19717648; 19723039; 19723066; 19724860; 19725224; 19730103; 19737931; 19752028; 19762066; 19773279; 19774677; 19774948; 19783718; 19786087; 19789190; 19797069; 19798108; 19805519; 19813621; 19818125; 19823588; 19834492; 19838163; 19846939; 19854241; 19883311; 19890377; 19890662; 19895735; 19908860; 19913121; 19925052; 19931389; 19937732; 19938012; 19938958; 19940548; 19956635; 19968497; 19996270; 20001236; 20010526; 20010695; 20012528; 20023428; 20025478; 20032416; 20034411; 20036222; 20042890; 20045442; 20048149; 20068093; 20072652; 20082279; 20087644; 20090905; 20118770; 20128283; 20132430; 20139069; 20140889; 20142237; 20146885; 20157331; 20160358; 20177797; 20178647; 20180421; 20181625; 20189848; 20189983; 20193114; 20198332; 20200776; 20223826; 20233885; 20237496; 20307495; 20340172; 20350212; 20352431; 20352700; 20368071; 20368567; 20382751; 20392693; 20399529; 20400521; 20401641; 20404322; 20409521; 20411301; 20415745; 20416158; 20423464; 20423844; 20434805; 20442586; 20448381; 20453000; 20459572; 20459695; 20460269; 20468060; 20495005; 20503275; 20504155; 20514538; 20518070; 20530713; 20564216; 20571027; 20584903; 20594261; 20608924; 20610805; 20627094; 20628086; 20631638; 20644561; 20648653; 20652449; 20658730; 20664977; 20668314; 20668552; 20668868; 20683843; 20691103; 20699221; 20716276; 20716950; 20723294; 20723300; 20732674; 20822926; 20836993; 20841355; 20855536; 20865015; 20869096; 20877624; 20885445; 20889974; 20890735; 20929126; 20929130; 20929131; 20936988; 20951945; 20952062; 20959405; 20962079; 20969490; 20976415; 20981461; 21029589; 21060336; 21061795; 21067292; 21068757; 21072044; 21076048; 21090097; 21104343; 21107291; 21108607; 21110823; 21115898; 21117871; 21122152; 21130495; 21131755; 21148306; 21148799; 21151158; 21159314; 21167476; 21171016; 21174060; 21199860; 21203533; 21207420; 21212266; 21223758; 21233846; 21250804; 21258880; 21289092; 21317312; 21320251; 21320534; 21336967; 21358617; 21376256; 21380782; 21385902; 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22174682; 22174832; 22187149; 22189900; 22194596; 22194861; 22198673; 22199279; 22207524; 22219597; 22252757; 22262057; 22275372; 22275374; 22277792; 22278385; 22285729; 22293115; 22309998; 22320961; 22322190; 22366560; 22366766; 22367371; 22372356; 22393362; 22395507; 22395508; 22395515; 22406486; 22414090; 22418857; 22433870; 22446832; 22462654; 22464442; 22484426; 22504301; 22504646; 22506026; 22517702; 22523079; 22524261; 22532139; 22562364; 22562824; 22563025; 22582499; 22591684; 22619347; 22622204; 22623155; 22629415; 22647378; 22650021; 22666341; 22668011; 22675938; 22684875; 22710204; 22727345; 22732796; 22739157; 22748563; 22749322; 22797576; 22804688; 22842544; 22848417; 22851565; 22855608; 22895528; 22896703; 22926545; 22929980; 22933114; 22936014; 22949148; 22951829; 22953646; 22965228; 22967897; 22968395; 22971934; 22976527; 22990545; 22995373; 23018213; 23030583; 23038985; 23064052; 23065465; 23072837; 23076250; 23091012; 23095743; 23115005; 23119114; 23126236; 23135964; 23138847; 23151078; 23152059; 23153525; 23160675; 23170075; 23174100; 23207618; 23216071; 23235765; 23243017; 23245210; 23247143; 23261425; 23263985; 23272207; 23283967; 23295106; 23301386; 23316052; 23316280; 23324193; 23334076; 23335369; 23341456; 23352961; 23355004; 23358890; 23359021; 23359184; 23363601; 23364242; 23364875; 23369735; 23403511; 23417836; 23421973; 23422486; 23437205; 23449635; 23463292; 23471820; 23479508; 23479509; 23480852; 23494176; 23497522; 23504944; 23509938; 23511489; 23514940; 23527542; 23553948; 23564079; 23568006; 23573235; 23588221; 23610963; 23612742; 23613399; 23613627; 23624503; 23628417; 23637776; 23671559; 23673452; 23673926; 23674504; 23688426; 23708869; 23719266; 23722017; 23724505; 23733877; 23770605; 23784204; 23802633; 23812727; 23818364; 23822101; 23832737; 23846229; 23850692; 23851330; 23861345; 23880928; 23900644; 23906301; 23907579; 23939148; 23960074; 23975374; 23991978; 23991993; 23994555; 24048795; 24091677; 24097825; 24127568; 24141421; 24157866; 24240096; 24256571; 24288815; 24293274; 24299314; 24314632; 24395794 B-cell CLL/lymphoma 2 Ensembl:ENSG00000171791 HGNC:990 HPRD:01045 MIM:151430 Other designations: apoptosis regulator Bcl-2|protein phosphatase 1, regulatory subunit 50 BCL2 gene OGG:3000000597 Bin Zhao, Yue Liu, Oliver He ACC-1 ACC-2 BCL2L5 BFL1 GRS HBPA1 WEB: http://www.ncbi.nlm.nih.gov/gene BCL2A1 BCL2-related protein A1 597 15q24.3 20140408 9606 15 protein-coding Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 10753914); GO_0005741 (EC: IBA); GO_0008630 (EC: IBA); GO_0042803 (EC: IBA); GO_0043066 (EC: IBA); GO_0046982 (EC: IBA); GO_0051400 (EC: IEA); GO_0097192 (EC: IBA); GO_2001243 (EC: IBA) PMID: 7478596; 8345191; 8589678; 8605321; 8910286; 8952545; 9050999; 9321477; 9356461; 9670936; 9731710; 10049353; 10198631; 10381646; 10430908; 10454539; 10545479; 10753914; 10849436; 11329013; 11483855; 11696595; 11929871; 12477932; 12665576; 12692420; 12771180; 14747545; 14966372; 14981542; 15489334; 15499630; 15501771; 15592513; 15617521; 15694340; 15696550; 16164629; 16551634; 16572199; 16697956; 16873269; 17121585; 17666431; 17724464; 17726463; 17907802; 17942758; 18093280; 18206119; 18414982; 18512730; 18812174; 18835031; 19336552; 19573080; 19759007; 19773279; 19913121; 20185581; 20353833; 20628086; 20800603; 20855536; 21167304; 21491422; 21832049; 21843371; 22231730; 22292048; 22510878; 22553204; 22615379; 22720045; 22745672; 22865454; 23118966; 23152563; 23447565 BCL2-related protein A1 Ensembl:ENSG00000140379 HGNC:991 HPRD:03034 MIM:601056 Vega:OTTHUMG00000144173 Other designations: bcl-2-like protein 5|bcl-2-related protein A1|bcl2-L-5|hematopoietic BCL2-related protein A1|hemopoietic-specific early response protein|protein BFL-1 BCL2A1 OGG:3000000602 Bin Zhao, Yue Liu, Oliver He BCL4 D19S37 WEB: http://www.ncbi.nlm.nih.gov/gene BCL3 B-cell CLL/lymphoma 3 602 19q13.1-q13.2 9606 19 Official from a nomenclature committee GO_0000060 (EC: IMP, PMID: 16280327); GO_0002268 (EC: IEA); GO_0002315 (EC: IEA); GO_0002455 (EC: IEA); GO_0002467 (EC: IEA); GO_0003677 (EC: IEA); GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10362352); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0006351 (EC: IDA, PMID: 16306601); GO_0006974 (EC: IDA, PMID: 16384933); GO_0007249 (EC: IDA, PMID: 8196632); GO_0008134 (EC: IPI, PMID: 11387332); GO_0009615 (EC: IDA, PMID: 16306601); GO_0010225 (EC: IDA, PMID: 16384933); GO_0019730 (EC: IEA); GO_0030198 (EC: IEA); GO_0030330 (EC: IMP, PMID: 16384933); GO_0030674 (EC: TAS, PMID: 16306601); GO_0032729 (EC: IEA); GO_0032996 (EC: IDA, PMID: 16280327); GO_0033257 (EC: IDA, PMID: 9407099); GO_0042088 (EC: IEA); GO_0042345 (EC: IEP, PMID: 8196632); GO_0042536 (EC: IEA); GO_0042742 (EC: IEA); GO_0042771 (EC: IMP, PMID: 16384933); GO_0042832 (EC: IEA); GO_0042981 (EC: IDA, PMID: 16732314); GO_0043066 (EC: IDA, PMID: 16384933); GO_0043234 (EC: IDA, PMID: 16280327); GO_0045064 (EC: IEA); GO_0045082 (EC: IEA); GO_0045171 (EC: IDA); GO_0045415 (EC: IMP, PMID: 16306601); GO_0045727 (EC: IMP, PMID: 16384933); GO_0045892 (EC: IDA, PMID: 16306601); GO_0045893 (EC: IDA, PMID: 16384933); GO_0045944 (EC: IEA); GO_0048471 (EC: IEA); GO_0048536 (EC: IEA); GO_0051101 (EC: IEP, PMID: 9407099); GO_0051457 (EC: NAS, PMID: 8196632) PMID: 1406939; 1501714; 1923524; 2124350; 2180580; 7691160; 7896265; 8196632; 8330739; 8428580; 8453667; 8497270; 9218802; 9407099; 9576921; 9812988; 10362352; 10469655; 10497212; 10607713; 11387332; 11485202; 11707390; 12456498; 12477932; 12730195; 12808109; 14678988; 15105810; 15469820; 15489334; 15634875; 15829968; 16099425; 16108830; 16123212; 16280327; 16306601; 16311697; 16331275; 16384933; 16732314; 16940298; 17272867; 17495977; 17644518; 17881446; 17923499; 17962807; 17963943; 18025803; 18796561; 18940474; 19191868; 19229118; 19282837; 19383626; 19451226; 19494302; 19617629; 19806201; 19893491; 19913121; 20226764; 20414006; 20471052; 20547759; 20558726; 20572854; 20601676; 20634891; 20658525; 20672350; 20731879; 20737317; 20800578; 20974051; 21048031; 21912613; 21988832; 22580608; 22782967; 23115114; 23149915; 23494744; 23534762; 23565137; 23607276; 23669365; 23794716 B-cell CLL/lymphoma 3 Ensembl:ENSG00000069399 HGNC:998 HPRD:00179 MIM:109560 Vega:OTTHUMG00000151517 Other designations: B-cell leukemia/lymphoma 3|B-cell lymphoma 3 protein|B-cell lymphoma 3-encoded protein|BCL-3|chronic lymphatic leukemia protein|proto-oncogene BCL3 BCL3 OGG:3000000635 Bin Zhao, Yue Liu, Oliver He BHMT1 HEL-S-61p WEB: http://www.ncbi.nlm.nih.gov/gene BHMT betaine--homocysteine S-methyltransferase 635 5q14.1 9606 5 Official from a nomenclature committee GO_0000096 (EC: TAS); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006479 (EC: NAS, PMID: 10075673); GO_0006579 (EC: IEA); GO_0008270 (EC: IEA); GO_0008898 (EC: IEA); GO_0009086 (EC: IEA); GO_0010243 (EC: IEA); GO_0032403 (EC: IEA); GO_0034641 (EC: TAS); GO_0043234 (EC: IEA); GO_0044281 (EC: TAS); GO_0047150 (EC: NAS, PMID: 10075673); GO_0047150 (EC: TAS); GO_0050666 (EC: NAS, PMID: 10075673) PMID: 1657504; 8798461; 8889548; 9281325; 9681996; 10075673; 10529246; 11223523; 11516176; 11883905; 12071701; 12220488; 12475213; 12477932; 12749058; 12818402; 15122900; 15489334; 16189514; 16344560; 16816108; 16953798; 17035141; 17119116; 17376725; 17436311; 17705221; 17993766; 18000879; 18029348; 18230680; 18262489; 18427977; 18457970; 18498552; 18635682; 18676680; 18708404; 18830263; 18988749; 19048631; 19161160; 19170196; 19336437; 19493349; 19625176; 19635752; 19683694; 19692168; 19737740; 19777601; 19913121; 19936946; 19948975; 20031554; 20346360; 20453000; 20458436; 20628086; 20634891; 20662904; 20664391; 20737570; 21093336; 21349258; 21564312; 21565678; 21630102; 21988832; 22138536; 22339686; 22339736; 23378610; 23645037; 23720494 betaine--homocysteine S-methyltransferase Ensembl:ENSG00000145692 HGNC:1047 HPRD:04200 MIM:602888 Vega:OTTHUMG00000108157 Other designations: betaine--homocysteine S-methyltransferase 1|epididymis secretory sperm binding protein Li 61p BHMT OGG:3000000637 Bin Zhao, Yue Liu, Oliver He FP497 WEB: http://www.ncbi.nlm.nih.gov/gene BID BH3 interacting domain death agonist 637 22q11.1 9606 22 Official from a nomenclature committee GO_0001836 (EC: IDA, PMID: 17052454); GO_0005123 (EC: TAS, PMID: 8918887); GO_0005515 (EC: IPI, PMID: 12624108); GO_0005739 (EC: TAS, PMID: 9727491); GO_0005741 (EC: TAS); GO_0005829 (EC: TAS); GO_0006626 (EC: IEA); GO_0006915 (EC: TAS); GO_0006919 (EC: IEA); GO_0007420 (EC: IEA); GO_0008625 (EC: TAS, PMID: 9727491); GO_0008637 (EC: TAS, PMID: 9727492); GO_0016020 (EC: TAS, PMID: 8918887); GO_0031625 (EC: IEA); GO_0032355 (EC: IEA); GO_0032461 (EC: IDA, PMID: 19074440); GO_0032464 (EC: IDA); GO_0032592 (EC: IEA); GO_0034349 (EC: IEA); GO_0042127 (EC: IEA); GO_0042770 (EC: TAS, PMID: 18309324); GO_0043065 (EC: IMP, PMID: 17289999); GO_0051260 (EC: IEA); GO_0051402 (EC: TAS, PMID: 16167175); GO_0090150 (EC: IDA); GO_0090200 (EC: IGI); GO_0090200 (EC: IMP, PMID: 17289999); GO_0097193 (EC: TAS); GO_1900740 (EC: TAS); GO_1901030 (EC: TAS); GO_1902108 (EC: IEA); GO_2000045 (EC: IEA); GO_2001238 (EC: IMP); GO_2001244 (EC: TAS) PMID: 7774948; 7929347; 8918887; 9463381; 9721221; 9727491; 9727492; 9790773; 10089877; 10364179; 10629050; 10950869; 11085743; 11099414; 11114298; 11399776; 11544326; 11583622; 11583631; 11585909; 11741882; 11790791; 11805084; 11832478; 11929871; 11940658; 11971973; 12000759; 12061801; 12097160; 12193163; 12196516; 12404116; 12419244; 12477932; 12598529; 12624108; 12754217; 12766488; 12804595; 12808108; 12871587; 12934063; 14581476; 14583606; 14702039; 14716828; 14769944; 15024076; 15117953; 15123718; 15146197; 15173176; 15231831; 15323553; 15353804; 15461802; 15489334; 15501827; 15520201; 15574335; 15592455; 15615731; 15637055; 15659383; 15692567; 15694340; 15721256; 15772077; 15809076; 16077201; 16167175; 16172118; 16341674; 16344560; 16380381; 16475813; 16485030; 16697956; 16908521; 16964285; 16987815; 17052454; 17200714; 17226776; 17283187; 17289999; 17308307; 17431792; 17488272; 17534194; 17549073; 17635912; 17666167; 17762183; 17765974; 17855051; 18029348; 18089817; 18165867; 18166654; 18173728; 18195012; 18297401; 18309324; 18317451; 18373075; 18469004; 18593990; 18648372; 18665919; 18723680; 18838202; 18925930; 19029793; 19046991; 19052714; 19074440; 19074885; 19219602; 19233849; 19246452; 19381674; 19423537; 19454696; 19640637; 19641510; 19670908; 19711428; 19820711; 19890662; 19913121; 19918914; 19929986; 20140092; 20187936; 20356928; 20379614; 20392206; 20404718; 20453000; 20628086; 20801175; 20802294; 20855536; 20877624; 21041309; 21060336; 21072056; 21113148; 21139048; 21148306; 21178828; 21223573; 21367852; 21382479; 21613222; 21642428; 21751259; 21856753; 21859891; 21900206; 21906983; 22052011; 22115752; 22130162; 22189507; 22213163; 22246181; 22339673; 22354970; 22393005; 22416135; 22464442; 22860893; 22939629; 22964611; 23019260; 23192964; 23333919; 23352961; 23383273; 23418437; 23604079; 23744079; 23824909; 24074954; 24158446 BH3 interacting domain death agonist Ensembl:ENSG00000015475 HGNC:1050 HPRD:03590 MIM:601997 Vega:OTTHUMG00000150087 Other designations: BH3-interacting domain death agonist|BID isoform ES(1b)|BID isoform L(2)|BID isoform Si6|Human BID coding sequence|apoptic death agonist|desmocollin type 4|p22 BID BID OGG:3000000639 Bin Zhao, Yue Liu, Oliver He BLIMP1 PRDI-BF1 WEB: http://www.ncbi.nlm.nih.gov/gene PRDM1 PR domain containing 1, with ZNF domain 639 RP1-134E15.1 6q21 9606 6 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0001893 (EC: IEA); GO_0003700 (EC: TAS, PMID: 1851123); GO_0005515 (EC: IPI); GO_0005634 (EC: IEA); GO_0005737 (EC: IDA); GO_0006351 (EC: IEA); GO_0007281 (EC: IEA); GO_0008168 (EC: IEA); GO_0010628 (EC: IEA); GO_0030889 (EC: IEA); GO_0031665 (EC: IEA); GO_0042462 (EC: IEA); GO_0042826 (EC: IEA); GO_0043565 (EC: IEA); GO_0045165 (EC: IEA); GO_0045579 (EC: IEA); GO_0046872 (EC: IEA); GO_0060707 (EC: IEA) PMID: 1851123; 8033216; 8168136; 8921366; 9887105; 10713181; 11067898; 11342629; 11877292; 12150891; 12165517; 12453881; 12477932; 12626569; 14985713; 16002735; 16424392; 16492805; 16547239; 16585013; 16699504; 16713569; 16765445; 16849320; 17043021; 17213024; 17264218; 17379744; 17682124; 17877160; 18071884; 18089822; 18192112; 18235046; 18256039; 18354204; 18370921; 18400362; 18552212; 18583325; 18596541; 18604866; 18845144; 18992153; 19047678; 19124609; 19194464; 19234190; 19269192; 19322201; 19433448; 19460752; 19530237; 19563034; 19717648; 19735688; 19760754; 19788443; 19828629; 19828640; 19838193; 19838195; 19898481; 19915048; 20047096; 20379614; 20530581; 20800019; 20859709; 20944005; 20966935; 21102463; 21103670; 21216962; 21411757; 21622776; 21690554; 21722313; 21722636; 21785431; 22020966; 22040493; 22143801; 22278826; 22438909; 22555612; 22580854; 22585398; 22593617; 22634616; 22939624; 23028907; 23129528; 23273568; 23348703; 23624108; 23648065; 23911415; 24004669; 24009228 PR domain containing 1, with ZNF domain Ensembl:ENSG00000057657 HGNC:9346 HPRD:04572 MIM:603423 Vega:OTTHUMG00000015299 Other designations: B-lymphocyte-induced maturation protein 1|BLIMP-1|PR domain zinc finger protein 1|PRDI-binding factor-1|beta-interferon gene positive-regulatory domain I binding factor PRDM1 OGG:3000000708 Bin Zhao, Yue Liu, Oliver He GC1QBP HABP1 SF2p32 gC1Q-R gC1qR p32 WEB: http://www.ncbi.nlm.nih.gov/gene C1QBP complement component 1, q subcomponent binding protein 708 17p13.3 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 15243141); GO_0001849 (EC: IDA, PMID: 8195709); GO_0003714 (EC: IDA, PMID: 15243141); GO_0003729 (EC: ISS); GO_0005080 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10831594); GO_0005540 (EC: IDA, PMID: 8567680); GO_0005615 (EC: IEA); GO_0005634 (EC: IDA, PMID: 15243141); GO_0005730 (EC: IEA); GO_0005737 (EC: ISS); GO_0005739 (EC: IDA, PMID: 19164550); GO_0005759 (EC: IEA); GO_0005829 (EC: IDA, PMID: 15243141); GO_0005886 (EC: TAS); GO_0006351 (EC: IEA); GO_0006397 (EC: IEA); GO_0006915 (EC: IEA); GO_0006955 (EC: TAS, PMID: 8195709); GO_0006958 (EC: IEA); GO_0007596 (EC: TAS); GO_0007597 (EC: TAS); GO_0008134 (EC: IDA, PMID: 15243141); GO_0008380 (EC: IEA); GO_0009986 (EC: IDA, PMID: 17881511); GO_0014065 (EC: IMP, PMID: 16177118); GO_0016020 (EC: IDA, PMID: 11290596); GO_0016032 (EC: IEA); GO_0030449 (EC: IDA, PMID: 8195709); GO_0030984 (EC: IDA, PMID: 8662673); GO_0031690 (EC: ISS); GO_0032689 (EC: IDA, PMID: 17881511); GO_0032695 (EC: IDA, PMID: 16177118); GO_0039534 (EC: IDA, PMID: 19164550); GO_0039536 (EC: IDA, PMID: 19164550); GO_0042256 (EC: IMP); GO_0043065 (EC: IMP, PMID: 15031724); GO_0045087 (EC: IEA); GO_0045785 (EC: IMP); GO_0048025 (EC: IDA, PMID: 10022843); GO_0050687 (EC: IMP, PMID: 19164550); GO_0051897 (EC: IMP, PMID: 16177118); GO_0070131 (EC: ISS); GO_0090023 (EC: IDA, PMID: 9461517); GO_0097177 (EC: ISS); GO_1900026 (EC: IMP, PMID: 11859136); GO_1901165 (EC: IMP); GO_2000510 (EC: IMP, PMID: 16140380) PMID: 1830244; 2372546; 7778269; 8189522; 8195709; 8262387; 8567680; 8626563; 8662673; 8710908; 9284938; 9461517; 9721222; 10022843; 10097078; 10747014; 10823864; 10831594; 11278463; 11290596; 11350968; 11549288; 11773076; 11859136; 11866440; 11870091; 12220632; 12443542; 12477932; 12538033; 12574814; 12833064; 14559993; 14583623; 14667819; 15031724; 15163734; 15231747; 15243141; 15324660; 15467913; 15489334; 16039650; 16140380; 16164755; 16177118; 16196087; 16212417; 16455055; 16537587; 16641292; 16713569; 16721827; 16871385; 16893067; 17314511; 17620012; 17620599; 17676665; 17881511; 17892212; 17907801; 17979178; 18172692; 18358546; 18460468; 18538737; 18676636; 18757437; 18781797; 19004836; 19149558; 19164550; 19190731; 19423540; 19454010; 19473882; 19523114; 19565630; 19608861; 19710015; 19738201; 19828637; 19836239; 19913121; 20020773; 20100866; 20186120; 20360068; 20406964; 20438785; 20617170; 20628086; 20877624; 21081666; 21139048; 21145461; 21156793; 21205079; 21248045; 21536672; 21536856; 21559373; 21627988; 21725590; 21726808; 21890473; 21906983; 21988832; 22008525; 22101277; 22114354; 22118674; 22145905; 22268729; 22354994; 22451658; 22700724; 22771308; 22863883; 22904065; 22939629; 22952844; 22960332; 23246001; 23378602; 23402259; 23438482; 23455922; 23667531; 23692256; 23798571; 23929393; 24174616; 24244333; 24250222; 24255178; 24457600 complement component 1, q subcomponent binding protein Ensembl:ENSG00000108561 HGNC:1243 HPRD:03168 MIM:601269 Vega:OTTHUMG00000177875 C1QBP OGG:3000000721 Bin Zhao, Yue Liu, Oliver He C4B1 C4B12 C4B2 C4B3 C4B5 C4BD C4B_2 C4F CH CO4 CPAMD3 WEB: http://www.ncbi.nlm.nih.gov/gene C4B complement component 4B (Chido blood group) 721 DADB-112B14.11-001 6p21.3 20140408 9606 6 protein-coding Official from a nomenclature committee GO_0004866 (EC: IEA); GO_0005576 (EC: TAS); GO_0005886 (EC: TAS); GO_0006954 (EC: IEA); GO_0006956 (EC: TAS); GO_0006958 (EC: IEA); GO_0030449 (EC: TAS); GO_0045087 (EC: TAS); GO_0072562 (EC: IDA) PMID: 1088823; 1699796; 1717583; 1988494; 2295627; 2431902; 2883116; 3542363; 3696167; 3840370; 3944109; 6167582; 6546707; 6559257; 6832377; 6881182; 6950384; 6978711; 7391573; 7525470; 7545960; 7590866; 7642209; 7893437; 7911492; 8132574; 8575831; 8630395; 8660986; 8889548; 9759862; 10072631; 10207042; 10383431; 10528211; 10851272; 10946278; 11062289; 11168010; 11341920; 11367523; 11803045; 12224044; 12226794; 12477932; 12480675; 12754519; 12878586; 12893820; 12907438; 14574404; 14760718; 14989716; 15033778; 15096498; 15203218; 15456488; 15665772; 15787745; 15816885; 15998580; 16098595; 16344560; 16386506; 16504674; 16740002; 16889542; 16893076; 16908004; 16980082; 17015733; 17202363; 17212707; 17257223; 17318071; 17425651; 17503323; 17728371; 17915330; 17921792; 17971360; 17984207; 18032375; 18065805; 18085389; 18091514; 18179706; 18315707; 18347532; 18360261; 18365397; 18645500; 18682851; 18927458; 18929826; 19062096; 19135723; 19137635; 19150565; 19167759; 19505723; 19900552; 19913121; 20022265; 20139276; 20452682; 20506482; 20580617; 20628086; 20795316; 21085669; 21345967; 21620080; 21642539; 21857912; 21967755; 22076784; 22132894; 22151770; 22169613; 22387014; 22393059; 22737222; 22785613; 22841245; 22878256; 23006730; 23026593; 23199209; 23274969; 23447068; 23535732; 23698598; 23911397; 23918728 complement component 4B (Chido blood group) Ensembl:ENSG00000224389 HGNC:1324 HPRD:00402 HPRD:18631 MIM:120820 Vega:OTTHUMG00000031187 C4B OGG:3000000727 Bin Zhao, Yue Liu, Oliver He C5a C5b CPAMD4 WEB: http://www.ncbi.nlm.nih.gov/gene C5 complement component 5 727 9q33-q34 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0000187 (EC: TAS, PMID: 7649993); GO_0001701 (EC: IEA); GO_0002523 (EC: IEA); GO_0004866 (EC: IEA); GO_0005102 (EC: TAS, PMID: 10820279); GO_0005515 (EC: IPI); GO_0005576 (EC: TAS); GO_0005579 (EC: IEA); GO_0005615 (EC: IEA); GO_0006874 (EC: IEA); GO_0006935 (EC: TAS, PMID: 10820279); GO_0006950 (EC: TAS, PMID: 9590258); GO_0006954 (EC: TAS, PMID: 8759757); GO_0006956 (EC: TAS); GO_0006957 (EC: IEA); GO_0006958 (EC: IEA); GO_0007166 (EC: TAS, PMID: 10820279); GO_0007186 (EC: TAS, PMID: 8898085); GO_0008009 (EC: TAS, PMID: 10820279); GO_0010575 (EC: IDA, PMID: 14566334); GO_0010700 (EC: IEA); GO_0010760 (EC: IDA, PMID: 14566334); GO_0019835 (EC: IEA); GO_0030449 (EC: TAS); GO_0031714 (EC: IEA); GO_0033602 (EC: IEA); GO_0042593 (EC: IEA); GO_0045087 (EC: TAS); GO_0045766 (EC: IEA); GO_0050921 (EC: IEA); GO_0060326 (EC: TAS, PMID: 10820279); GO_0070062 (EC: IDA, PMID: 19056867); GO_0090197 (EC: IDA, PMID: 14566334) PMID: 106884; 690134; 1387399; 1847994; 1984448; 1996961; 2579066; 2730871; 2784981; 2808363; 3052276; 3365401; 3408713; 3624872; 7649993; 7661861; 7730648; 7835913; 7911492; 8175701; 8630395; 8702752; 8759757; 8889548; 8898085; 9007977; 9188742; 9218605; 9553099; 9590258; 10352266; 10820279; 11367533; 11752456; 11939578; 12477932; 12488432; 12878586; 12881318; 12937147; 14556080; 14566334; 14662858; 15278436; 15383587; 15488949; 15550394; 15585680; 15598652; 15768031; 15778377; 15879120; 15995705; 16335952; 16452172; 16670089; 16823297; 16879222; 17023413; 17322907; 17428459; 17482181; 17498719; 17505301; 17533009; 17634448; 17644516; 17703412; 17804836; 17880261; 18039528; 18240029; 18300128; 18411281; 18576341; 18644651; 18714034; 18759306; 18953960; 18974840; 19028820; 19056867; 19110536; 19116907; 19131662; 19162005; 19180477; 19225544; 19230171; 19247692; 19258923; 19263529; 19265162; 19324972; 19336421; 19344414; 19375167; 19401279; 19414197; 19416238; 19423540; 19479237; 19503088; 19559392; 19565500; 19674979; 19729601; 19741008; 19843088; 19864026; 19902201; 19909405; 19913121; 19918040; 19948975; 20022638; 20030635; 20049410; 20109314; 20124699; 20133685; 20143644; 20205706; 20219786; 20233754; 20237496; 20353580; 20406964; 20424189; 20438785; 20444755; 20453842; 20479942; 20498205; 20503287; 20536507; 20545943; 20591742; 20603037; 20628086; 20797713; 20813982; 20822712; 20880552; 20962850; 21393613; 21890473; 21926466; 22244896; 22258234; 22284611; 22308306; 22452399; 22496247; 22500023; 22528500; 22802338; 22812419; 22820624; 23028051; 23071133; 23321589; 23371790; 23401592; 23602531; 23662819; 23792503; 23833239; 24521109 complement component 5 Ensembl:ENSG00000106804 HGNC:1331 HPRD:00405 MIM:120900 Vega:OTTHUMG00000020579 C5 OGG:3000000760 Bin Zhao, Yue Liu, Oliver He CA-II CAC CAII Car2 HEL-76 WEB: http://www.ncbi.nlm.nih.gov/gene CA2 carbonic anhydrase II 760 8q22 9606 8 Official from a nomenclature committee GO_0001822 (EC: IEA); GO_0002009 (EC: IEA); GO_0004089 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15990874); GO_0005615 (EC: IEA); GO_0005737 (EC: IDA, PMID: 114507); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA, PMID: 15990874); GO_0005902 (EC: IEA); GO_0006730 (EC: IEA); GO_0008270 (EC: IDA, PMID: 3151020); GO_0009268 (EC: IEA); GO_0010043 (EC: IEA); GO_0015670 (EC: IEA); GO_0015701 (EC: TAS); GO_0016323 (EC: IEA); GO_0030424 (EC: IEA); GO_0032849 (EC: IEA); GO_0038166 (EC: IDA, PMID: 15990874); GO_0042475 (EC: IEA); GO_0043627 (EC: IEA); GO_0044070 (EC: IDA, PMID: 15990874); GO_0044281 (EC: TAS); GO_0045177 (EC: IDA, PMID: 14675051); GO_0045672 (EC: IEA); GO_0045780 (EC: IEA); GO_0046903 (EC: IEA); GO_0051453 (EC: ISS); GO_0070062 (EC: IDA, PMID: 19056867); GO_2001150 (EC: ISS) PMID: 114507; 823150; 1301935; 1542674; 1602151; 1925679; 1928091; 1977133; 2117271; 2121671; 2123360; 2850697; 3000449; 3081869; 3107918; 3108857; 3121496; 3151019; 3151020; 3221988; 3925334; 4207120; 4621826; 4624444; 6407977; 6817747; 7574487; 7627193; 7930522; 8127074; 8128957; 8460098; 8834238; 9143915; 9150731; 9205766; 9336790; 9453381; 9541386; 9774471; 9890926; 10231836; 10333352; 10423017; 10811634; 10820026; 10821857; 11063570; 11076507; 11264157; 11457932; 11606574; 11956656; 12056894; 12138085; 12171926; 12411514; 12477932; 12501217; 12566520; 12826902; 12933803; 14567693; 14578124; 14675051; 14675565; 14718574; 14736710; 14760703; 15049705; 15062553; 15218065; 15300855; 15453828; 15489334; 15667203; 15836783; 15837316; 15837325; 15952740; 15990874; 16106378; 16169070; 16196087; 16265785; 16344560; 16475831; 16687407; 16825953; 16996812; 17202139; 17319692; 17319695; 17363915; 17631639; 17881426; 18029348; 18060825; 18083150; 18189416; 18247480; 18323598; 18539591; 18580434; 18942852; 18976975; 19012038; 19034380; 19056867; 19269136; 19371798; 19407386; 19415900; 19520834; 19583303; 19615732; 19634894; 19686046; 20000378; 20025241; 20081808; 20170095; 20297840; 20360068; 20398423; 20445237; 20445238; 20509747; 20578724; 20634585; 20637176; 20693695; 20849852; 21139048; 21145461; 21145876; 21243755; 21282642; 21543742; 21680735; 21890473; 21988105; 22001224; 22192857; 22386980; 22416960; 22732064; 22878862; 23030313; 23098192; 23181366; 23215152; 23360090; 23674848; 23720494; 23727877; 23953824; 24036123 carbonic anhydrase II Ensembl:ENSG00000104267 HGNC:1373 HPRD:02023 MIM:611492 Vega:OTTHUMG00000164944 Other designations: carbonate dehydratase II|carbonic anhydrase 2|carbonic anhydrase B|carbonic anhydrase C|carbonic dehydratase|epididymis luminal protein 76 CA2 OGG:3000000771 Bin Zhao, Yue Liu, Oliver He CAXII HsT18816 WEB: http://www.ncbi.nlm.nih.gov/gene CA12 carbonic anhydrase XII 771 15q22 9606 15 Official from a nomenclature committee GO_0004089 (EC: IEA); GO_0005886 (EC: TAS); GO_0006730 (EC: IEA); GO_0008270 (EC: IEA); GO_0015701 (EC: TAS); GO_0016021 (EC: IEA); GO_0044281 (EC: TAS) PMID: 8524854; 9636197; 9770531; 10512682; 10611263; 10666387; 11083462; 11101628; 11238049; 11420383; 11493685; 11680594; 12477932; 12676895; 12854129; 12923247; 14578124; 14702039; 15489334; 15849821; 16169070; 16416108; 18029348; 18322268; 18336315; 18451179; 19291313; 20132413; 20215053; 20398423; 20434230; 20509747; 21035102; 21040567; 21139048; 21184099; 21278619; 21900206; 22172588; 22439015; 22944692; 23348702 carbonic anhydrase XII HGNC:1371 HPRD:04464 MIM:603263 Other designations: CA-XII|carbonate dehydratase XII|carbonic anhydrase 12|carbonic dehydratase|tumor antigen HOM-RCC-3.1.3 CA12 OGG:3000000782 Bin Zhao, Yue Liu, Oliver He CAB1 CACNLB1 CCHLB1 WEB: http://www.ncbi.nlm.nih.gov/gene CACNB1 calcium channel, voltage-dependent, beta 1 subunit 782 17q21-q22 9606 17 Official from a nomenclature committee GO_0005245 (EC: TAS, PMID: 1385409); GO_0005891 (EC: IEA); GO_0006612 (EC: IEA); GO_0006810 (EC: TAS, PMID: 1385409); GO_0007411 (EC: TAS); GO_0008331 (EC: IEA); GO_0016529 (EC: IEA); GO_0030315 (EC: IEA) PMID: 1309651; 1370480; 1385409; 1657644; 7916667; 8381767; 8395940; 8905728; 8943043; 10066897; 10465427; 10624822; 12477932; 14623965; 14760703; 14762176; 15342556; 16713569; 17081983; 19821165; 19953087; 21098446; 21832049; 21906983; 23382691; 23602568 calcium channel, voltage-dependent, beta 1 subunit Ensembl:ENSG00000067191 HGNC:1401 HPRD:11743 MIM:114207 Vega:OTTHUMG00000133217 Other designations: calcium channel voltage-dependent subunit beta 1|calcium channel, L type, beta 1 polypeptide|dihydropyridine-sensitive L-type, calcium channel beta-1 subunit|voltage-dependent L-type calcium channel subunit beta-1 CACNB1 OGG:3000000788 Bin Zhao, Yue Liu, Oliver He CAC CACT WEB: http://www.ncbi.nlm.nih.gov/gene SLC25A20 solute carrier family 25 (carnitine/acylcarnitine translocase), member 20 788 3p21.31 9606 3 Official from a nomenclature committee GO_0005739 (EC: IDA); GO_0005743 (EC: TAS); GO_0006853 (EC: TAS); GO_0016021 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS) PMID: 1598097; 9399886; 9533014; 9686371; 9733094; 9837782; 10384384; 10697964; 11257506; 11592821; 12477932; 12859414; 15057979; 15365988; 15489334; 15515015; 16054041; 16169070; 17508264; 18029348; 18307102; 19748481; 20877624; 21130740; 21890473; 22560224; 23178685; 23266187; 23322164 solute carrier family 25 (carnitine/acylcarnitine translocase), member 20 Ensembl:ENSG00000178537 HGNC:1421 HPRD:01953 MIM:613698 Vega:OTTHUMG00000133538 Other designations: mitochondrial carnitine/acylcarnitine carrier protein SLC25A20 OGG:3000000834 Bin Zhao, Yue Liu, Oliver He ICE IL1BC P45 WEB: http://www.ncbi.nlm.nih.gov/gene CASP1 caspase 1, apoptosis-related cysteine peptidase 834 11q23 9606 11 GO_0001666 (EC: IEA); GO_0004197 (EC: IBA); GO_0004197 (EC: TAS); GO_0005515 (EC: IPI, PMID:11374873); GO_0005576 (EC: IEA); GO_0005737 (EC: IBA); GO_0005829 (EC: TAS); GO_0006508 (EC: IDA, PMID:12888622); GO_0006915 (EC: TAS, PMID:7876192); GO_0006919 (EC: TAS, PMID:10799503); GO_0007165 (EC: TAS, PMID:1373520); GO_0008656 (EC: TAS, PMID:10799503); GO_0032496 (EC: IEA); GO_0032611 (EC: IEA); GO_0033198 (EC: IEA); GO_0035872 (EC: TAS); GO_0043123 (EC: IEP, PMID:12761501); GO_0045087 (EC: TAS); GO_0050717 (EC: IEA); GO_0050718 (EC: IEA); GO_0050727 (EC: IBA); GO_0051882 (EC: IEA); GO_0060081 (EC: IEA); GO_0070269 (EC: IEA); GO_0071260 (EC: IEP, PMID:19593445); GO_0071310 (EC: IDA, PMID:19158679); GO_0072557 (EC: IBA); GO_0072557 (EC: ISS); GO_0072558 (EC: IDA, PMID:12191486); GO_0072559 (EC: IDA, PMID:15030775); GO_0097169 (EC: IDA, PMID:19158676); GO_0097194 (EC: IBA) PMID:1321594; 1373520; 1574116; 1919001; 7642516; 7721861; 7797510; 7876192; 8034320; 8035875; 8044845; 8125298; 8861900; 8962078; 8978814; 8999548; 9002959; 9070648; 9115219; 9190289; 9219695; 9250871; 9334240; 9334338; 9435230; 9535906; 9548463; 9593687; 9632733; 9705209; 9705938; 9727491; 9792675; 9804161; 9830039; 9875225; 9894612; 9987822; 9990034; 10069390; 10329646; 10353249; 10438581; 10477277; 10510468; 10660263; 10708425; 10799503; 11085743; 11226410; 11374873; 11390368; 11432859; 11437653; 11438643; 11472070; 11536016; 11684016; 11821383; 11953316; 11967258; 11997061; 12019269; 12096920; 12170183; 12191486; 12215842; 12387869; 12459189; 12459463; 12477932; 12628757; 12692130; 12761501; 12888622; 14584052; 14669344; 15030775; 15039421; 15107016; 15296730; 15326478; 15383541; 15471361; 15489334; 15498465; 15561713; 15749123; 15809717; 16037825; 16087165; 16123779; 16260731; 16286016; 16405550; 16428475; 16575408; 16621994; 16778130; 16780720; 16785446; 16817903; 16903774; 16920334; 17036048; 17173859; 17196042; 17207965; 17303764; 17360653; 17418785; 17477815; 17597823; 17623017; 17703412; 17959595; 18029348; 18209072; 18263705; 18263805; 18304957; 18329368; 18523309; 18550243; 18577712; 18590738; 18799371; 18828051; 18981155; 19013323; 19074885; 19117953; 19141860; 19158676; 19158679; 19258923; 19269008; 19275586; 19382257; 19414860; 19439663; 19573080; 19593445; 19648107; 19737897; 19773279; 19779610; 19825518; 19833722; 19913121; 20038581; 20048342; 20060974; 20170165; 20184726; 20197547; 20402676; 20485444; 20503287; 20628086; 20808838; 20852925; 20855536; 20959405; 21037509; 21048031; 21052690; 21311905; 21320026; 21463955; 21757759; 21792841; 21832064; 21862576; 21862623; 22046355; 22046441; 22195745; 22227487; 22491736; 22537218; 22833538; 22837397; 23021143; 23209292; 23226468; 23236067; 23278288; 23386603; 23508996; 23590971; 23637985; 23703390; 23793845; 23839215; 23884363; 24022484; 24356306 caspase 1, apoptosis-related cysteine peptidase Ensembl:ENSG00000137752 HGNC:1499 HPRD:00977 MIM:147678 Vega:OTTHUMG00000048072 Other designations: CASP1 nirs variant 1|IL-1 beta-converting enzyme|IL1B-convertase|caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase)|caspase-1|interleukin 1, beta, convertase|interleukin 1-B converting enzyme CASP1 OGG:3000000835 Bin Zhao, Yue Liu, Oliver He CASP-2 ICH1 NEDD-2 NEDD2 PPP1R57 WEB: http://www.ncbi.nlm.nih.gov/gene CASP2 caspase 2, apoptosis-related cysteine peptidase 835 7q34-q35 9606 7 GO_0001554 (EC: IEA); GO_0003407 (EC: IEA); GO_0004197 (EC: IDA, PMID:10980123); GO_0005515 (EC: IPI, PMID:11076957); GO_0005634 (EC: TAS, PMID:18309324); GO_0005737 (EC: IBA); GO_0005739 (EC: IEA); GO_0005829 (EC: TAS); GO_0006915 (EC: NAS, PMID:11156409); GO_0006977 (EC: IMP); GO_0007420 (EC: IEA); GO_0007568 (EC: IEA); GO_0008630 (EC: IBA); GO_0008630 (EC: TAS, PMID:18309324); GO_0016020 (EC: IEA); GO_0016485 (EC: IDA, PMID:9044836); GO_0019899 (EC: ISS, PMID:11076957); GO_0019904 (EC: IPI, PMID:9044836); GO_0035234 (EC: IEA); GO_0043065 (EC: IDA, PMID:10980123); GO_0043281 (EC: TAS); GO_0043525 (EC: IEA); GO_0048011 (EC: TAS); GO_0071260 (EC: IEP, PMID:19593445); GO_0097153 (EC: IEA); GO_0097190 (EC: TAS, PMID:18309324); GO_0097192 (EC: IBA); GO_0097194 (EC: TAS, PMID:18309324); GO_2001235 (EC: IEA) PMID:7789948; 8044845; 8087842; 8780721; 8962078; 8985253; 9044836; 9228018; 9261102; 9560245; 9695946; 9792675; 9847074; 10079193; 10329646; 10791974; 10980123; 11076957; 11156409; 11278287; 11313953; 11350957; 11399776; 11425872; 11823470; 11830582; 11832478; 11972030; 12011445; 12065594; 12107826; 12145703; 12193789; 12477715; 12477932; 12584573; 12598307; 12787561; 12837286; 12853948; 12920126; 14584591; 14623896; 14647455; 14701762; 14702039; 14713958; 14716300; 15073321; 15173176; 15262979; 15297885; 15489334; 15500642; 15511269; 15555560; 15590671; 15735701; 15817479; 15843892; 15882978; 16172118; 16193064; 16227610; 16344560; 16360037; 16387548; 16652156; 16701639; 16777994; 16822901; 16843824; 17079734; 17159900; 17195089; 17627033; 17637755; 17902043; 17945178; 18166155; 18238895; 18309324; 18375382; 18413747; 18418048; 18723680; 18840686; 19074885; 19269008; 19322201; 19347032; 19414860; 19453261; 19573080; 19593445; 19604093; 19715609; 19730412; 19738422; 19773279; 19935698; 20143425; 20158568; 20187765; 20208132; 20402676; 20453000; 20819778; 20855536; 20978129; 21051981; 21332795; 21415862; 21475302; 21726810; 21828056; 21900206; 21903589; 21906983; 21940110; 21988832; 22002103; 22077397; 22174370; 22201672; 22396545; 22486813; 22505724; 22531785; 22825847; 23042294; 23404198; 23469978; 23553630; 23568547; 24250222; 24321384 caspase 2, apoptosis-related cysteine peptidase Ensembl:ENSG00000106144 HGNC:1503 HPRD:02800 MIM:600639 Vega:OTTHUMG00000023641 Other designations: caspase-2|neural precursor cell expressed developmentally down-regulated protein 2|protease ICH-1|protein phosphatase 1, regulatory subunit 57 CASP2 OGG:3000000836 Bin Zhao, Yue Liu, Oliver He CPP32 CPP32B SCA-1 WEB: http://www.ncbi.nlm.nih.gov/gene CASP3 caspase 3, apoptosis-related cysteine peptidase 836 4q34 9606 4 GO_0001782 (EC: IEA); GO_0001836 (EC: IEA); GO_0004190 (EC: EXP); GO_0004197 (EC: IDA, PMID:19240112); GO_0004197 (EC: TAS); GO_0004861 (EC: IEA); GO_0005515 (EC: IPI, PMID:16501604); GO_0005634 (EC: IDA, PMID:17167422); GO_0005654 (EC: TAS); GO_0005829 (EC: IDA, PMID:17167422); GO_0005829 (EC: TAS); GO_0005886 (EC: TAS); GO_0006309 (EC: TAS); GO_0006508 (EC: IDA, PMID:12888622); GO_0006915 (EC: TAS); GO_0006921 (EC: TAS); GO_0006974 (EC: IEA); GO_0007507 (EC: IEA); GO_0007605 (EC: IEA); GO_0008233 (EC: IDA, PMID:17167422); GO_0008625 (EC: IEA); GO_0008631 (EC: IEA); GO_0008635 (EC: TAS); GO_0009411 (EC: IEA); GO_0009611 (EC: IEA); GO_0022617 (EC: TAS); GO_0030182 (EC: IBA); GO_0030198 (EC: TAS); GO_0030216 (EC: IBA); GO_0030218 (EC: IDA, PMID:17167422); GO_0030218 (EC: TAS, PMID:18309324); GO_0030220 (EC: TAS, PMID:18309324); GO_0030889 (EC: IEA); GO_0034349 (EC: IEA); GO_0034612 (EC: TAS, PMID:10521396); GO_0035329 (EC: TAS); GO_0042981 (EC: TAS); GO_0043029 (EC: IEA); GO_0043065 (EC: TAS); GO_0043066 (EC: IGI, PMID:9353287); GO_0043281 (EC: TAS); GO_0043525 (EC: IEA); GO_0045165 (EC: IEA); GO_0045736 (EC: IEA); GO_0046007 (EC: IEA); GO_0048011 (EC: TAS); GO_0051402 (EC: IEA); GO_0097153 (EC: IMP, PMID:10921886); GO_0097190 (EC: TAS, PMID:10521396); GO_0097192 (EC: IEA); GO_0097193 (EC: TAS); GO_0097194 (EC: IDA, PMID:8689682); GO_0097194 (EC: IMP, PMID:11350920); GO_0097200 (EC: IMP, PMID:17559062) PMID:1067155; 7596430; 7774019; 7983002; 8044845; 8605870; 8626669; 8673606; 8689682; 8696339; 8755496; 8780721; 8804412; 8812467; 8900201; 8943232; 8962078; 8976194; 9021152; 9045680; 9108473; 9115219; 9206994; 9208847; 9219695; 9230442; 9233763; 9235961; 9252332; 9267021; 9278461; 9298992; 9323209; 9326610; 9334214; 9334240; 9334338; 9337844; 9348292; 9351817; 9353287; 9361003; 9367996; 9368003; 9384571; 9395403; 9422780; 9452471; 9525868; 9535906; 9545236; 9548463; 9593687; 9618490; 9624143; 9632733; 9660939; 9671712; 9685336; 9694885; 9705209; 9708895; 9736630; 9751706; 9786869; 9799125; 9811849; 9840926; 9850056; 9857079; 9875225; 9878167; 9894612; 9933635; 9990034; 10022118; 10066732; 10069390; 10082566; 10103059; 10200531; 10205158; 10205159; 10319819; 10364179; 10409750; 10430052; 10432301; 10435619; 10438581; 10454555; 10469173; 10479680; 10490026; 10510468; 10521396; 10556977; 10564664; 10579725; 10602493; 10602513; 10608812; 10611247; 10629060; 10671544; 10672017; 10675528; 10704341; 10708425; 10712510; 10713703; 10734073; 10748026; 10770929; 10777594; 10791974; 10799874; 10821855; 10823823; 10862606; 10896157; 10899937; 10921886; 10926122; 10942389; 10998058; 11002417; 11016947; 11024045; 11042212; 11053413; 11058115; 11076937; 11084335; 11098060; 11106668; 11123279; 11141237; 11149901; 11162250; 11162351; 11170436; 11175261; 11177389; 11222676; 11230124; 11242052; 11248093; 11257230; 11257232; 11261798; 11274152; 11278283; 11278287; 11278424; 11278572; 11278782; 11278797; 11283607; 11313965; 11331419; 11345898; 11350920; 11356849; 11359776; 11387340; 11399776; 11420704; 11423904; 11425872; 11437602; 11438643; 11447297; 11462036; 11470874; 11478781; 11479289; 11500511; 11509621; 11514563; 11517310; 11526478; 11550094; 11551979; 11555640; 11602184; 11675509; 11689006; 11696595; 11741893; 11748221; 11752060; 11752215; 11787859; 11788610; 11795487; 11802788; 11815631; 11825902; 11830582; 11832478; 11840332; 11854437; 11859414; 11866986; 11875078; 11901153; 11904443; 11927604; 11948397; 11960384; 11972398; 11981455; 11988074; 11989976; 11992386; 12004072; 12019321; 12032677; 12036886; 12044963; 12055227; 12070005; 12070657; 12080079; 12095993; 12107159; 12112012; 12118383; 12124386; 12145703; 12149654; 12150947; 12151338; 12169388; 12181128; 12181742; 12186978; 12190962; 12207967; 12210761; 12228224; 12235123; 12297281; 12390838; 12393901; 12397210; 12401855; 12404116; 12425945; 12438416; 12444137; 12477932; 12483536; 12490308; 12511568; 12515825; 12566444; 12576296; 12576443; 12579342; 12581734; 12598529; 12605885; 12606589; 12611892; 12621124; 12624662; 12643601; 12657644; 12677451; 12686427; 12700630; 12700660; 12707329; 12750393; 12750404; 12760639; 12787561; 12788227; 12788938; 12792782; 12804035; 12809603; 12821118; 12824190; 12833566; 12837287; 12854132; 12867600; 12874324; 12888622; 12897143; 14555204; 14570914; 14572611; 14612448; 14623896; 14657946; 14674699; 14678329; 14684629; 14710359; 14764700; 14960581; 14970175; 14971566; 14976035; 14982947; 14991812; 14993250; 15014070; 15015772; 15033720; 15033815; 15041704; 15087450; 15098015; 15153940; 15156398; 15178331; 15179054; 15186778; 15187159; 15200957; 15204919; 15205454; 15220451; 15241180; 15246206; 15254227; 15258591; 15280469; 15345747; 15375594; 15473998; 15489334; 15505416; 15507451; 15542841; 15564512; 15569669; 15569672; 15569692; 15578977; 15599395; 15617521; 15637055; 15638357; 15650747; 15657349; 15657356; 15670787; 15705385; 15706351; 15716280; 15725353; 15735701; 15748158; 15748808; 15767427; 15803189; 15806167; 15843892; 15848173; 15869582; 15935070; 15996160; 16009347; 16080782; 16083554; 16111829; 16120388; 16121124; 16179347; 16203739; 16204230; 16213496; 16227597; 16242324; 16286477; 16300929; 16320828; 16330530; 16337360; 16338743; 16344560; 16382148; 16455648; 16463650; 16480911; 16498457; 16501604; 16505307; 16511342; 16516911; 16520893; 16526059; 16529748; 16530181; 16530191; 16543147; 16567804; 16651613; 16689860; 16716256; 16781734; 16787777; 16791842; 16802364; 16808908; 16835231; 16869888; 16882668; 16884727; 16894574; 16897667; 16931214; 16935258; 16948902; 16949642; 16955788; 16977583; 16979168; 16983089; 17008916; 17013756; 17013758; 17023557; 17038954; 17065568; 17069460; 17071630; 17080552; 17114647; 17118559; 17121821; 17123522; 17124493; 17130234; 17140287; 17141888; 17143787; 17167422; 17172814; 17198755; 17217622; 17219053; 17235653; 17245643; 17261582; 17272816; 17283187; 17291493; 17301822; 17321792; 17324936; 17337451; 17340613; 17364171; 17379327; 17412564; 17413988; 17430778; 17436592; 17437405; 17462862; 17488272; 17495975; 17498346; 17505517; 17525639; 17534194; 17544405; 17559062; 17597071; 17606719; 17606900; 17616526; 17645689; 17653867; 17689858; 17698513; 17721932; 17724022; 17805550; 17823127; 17880920; 17908973; 17928446; 17936584; 17950632; 17967742; 17978580; 17981569; 17983802; 17989718; 18000616; 18029348; 18047842; 18054197; 18055116; 18058802; 18060501; 18074388; 18083346; 18086147; 18088367; 18092356; 18155705; 18155731; 18164959; 18171980; 18209072; 18211414; 18227733; 18256758; 18256791; 18266005; 18296636; 18297401; 18298948; 18300076; 18309324; 18330265; 18379198; 18381704; 18384375; 18415681; 18415689; 18427836; 18439040; 18441516; 18450750; 18473402; 18476631; 18521960; 18551626; 18561948; 18577580; 18585351; 18586680; 18623086; 18652315; 18658137; 18669646; 18676680; 18708163; 18712678; 18723680; 18727869; 18754867; 18759060; 18763039; 18768468; 18814044; 18818379; 18820371; 18821563; 18829519; 18838202; 18844072; 18946722; 18986328; 19013323; 19035131; 19043361; 19046417; 19052714; 19058789; 19074885; 19132366; 19141860; 19157504; 19157506; 19159073; 19170196; 19178812; 19200347; 19204086; 19219602; 19223905; 19236754; 19240112; 19241192; 19244543; 19258326; 19266703; 19269008; 19270727; 19272183; 19275584; 19275586; 19275587; 19281794; 19283487; 19289465; 19299722; 19319745; 19322201; 19351510; 19355923; 19379562; 19404232; 19414860; 19453261; 19458171; 19513559; 19519609; 19531679; 19544333; 19549685; 19550122; 19553679; 19557639; 19559790; 19567200; 19570417; 19573080; 19585117; 19598027; 19604093; 19610261; 19625176; 19626422; 19636556; 19655253; 19655254; 19655415; 19665028; 19692168; 19692467; 19698783; 19698994; 19715609; 19723039; 19724860; 19724907; 19730442; 19738422; 19759058; 19770576; 19770581; 19773279; 19774677; 19784808; 19788069; 19788411; 19807657; 19812265; 19826114; 19838207; 19840460; 19854241; 19878567; 19895210; 19913121; 19925402; 19937139; 19942343; 19956888; 19996122; 19996272; 19996275; 19996278; 20001963; 20012528; 20025478; 20038816; 20041182; 20042134; 20045442; 20060927; 20063052; 20068062; 20072652; 20085765; 20087649; 20101263; 20103643; 20104682; 20142237; 20150439; 20180022; 20198319; 20227371; 20299368; 20307198; 20340172; 20346214; 20383567; 20402676; 20404718; 20423928; 20424172; 20450729; 20453000; 20492341; 20512574; 20530714; 20566630; 20580881; 20598358; 20619728; 20628086; 20628645; 20632819; 20644561; 20661084; 20665667; 20667824; 20683021; 20683843; 20702410; 20722551; 20723300; 20738749; 20801175; 20814064; 20839416; 20855536; 20856198; 20862799; 20919853; 20929126; 20947770; 20950443; 20959405; 20962079; 20966960; 20981869; 21029675; 21048031; 21081164; 21098975; 21099290; 21099299; 21123175; 21123558; 21139048; 21142842; 21148072; 21151026; 21160486; 21178828; 21203962; 21216952; 21223758; 21237154; 21248767; 21255440; 21270757; 21307660; 21317880; 21319273; 21382445; 21441410; 21479362; 21483469; 21483669; 21484410; 21504623; 21506333; 21548803; 21555338; 21561870; 21624464; 21644054; 21644232; 21667042; 21668377; 21671484; 21682651; 21700414; 21706480; 21724551; 21725926; 21729540; 21756903; 21775054; 21785112; 21802116; 21819468; 21827945; 21859712; 21869592; 21875325; 21880013; 21890473; 21914347; 21926353; 21944661; 21959934; 21963094; 21987091; 21988832; 22013052; 22072751; 22094081; 22121772; 22136337; 22147199; 22184067; 22191568; 22216281; 22238643; 22242595; 22298410; 22302483; 22309278; 22320973; 22429811; 22429842; 22482362; 22496955; 22504224; 22541080; 22552851; 22568453; 22607239; 22629415; 22678593; 22683311; 22764223; 22796265; 22815893; 22832123; 22837201; 22844442; 22872644; 22885173; 22912727; 22926545; 22931643; 22939953; 22944165; 22949938; 22951837; 22952982; 22964638; 23000965; 23054082; 23103707; 23122728; 23152053; 23156805; 23170075; 23170789; 23220614; 23221544; 23271051; 23271418; 23295106; 23326121; 23345589; 23384723; 23386603; 23416147; 23421973; 23519117; 23531593; 23545262; 23555267; 23568731; 23591201; 23599180; 23650375; 23658722; 23686572; 23703388; 23708668; 23724505; 23765963; 23775301; 23781587; 23791066; 23846227; 23867824; 23892923; 23894522; 23900644; 23907941; 23949910; 23979166; 24009453; 24129493; 24161344; 24553140 caspase 3, apoptosis-related cysteine peptidase Ensembl:ENSG00000164305 HGNC:1504 HPRD:02799 MIM:600636 Vega:OTTHUMG00000133681 Other designations: CASP-3|CPP-32|PARP cleavage protease|SREBP cleavage activity 1|apopain|caspase 3, apoptosis-related cysteine protease|caspase-3|cysteine protease CPP32|procaspase3|protein Yama CASP3 OGG:3000000837 Bin Zhao, Yue Liu, Oliver He ICE(rel)II ICEREL-II ICH-2 Mih1/TX TX WEB: http://www.ncbi.nlm.nih.gov/gene CASP4 caspase 4, apoptosis-related cysteine peptidase 837 11q22.2-q22.3 9606 11 GO_0004197 (EC: IBA); GO_0005737 (EC: IBA); GO_0005739 (EC: IEA); GO_0005789 (EC: IEA); GO_0006508 (EC: TAS, PMID:7797510); GO_0006915 (EC: TAS, PMID:7743998); GO_0042981 (EC: IEA); GO_0050727 (EC: IBA); GO_0072557 (EC: IBA); GO_0072559 (EC: IBA); GO_0097169 (EC: IBA); GO_0097194 (EC: IBA) PMID:1919001; 7743998; 7797510; 7797592; 8125298; 8962078; 9233763; 9250871; 9539746; 9694885; 9792675; 9875225; 10069390; 10329646; 10477277; 10872455; 11927604; 12096920; 12477932; 14702039; 15123740; 15146197; 15326478; 15489334; 15500642; 15975932; 16920334; 17353931; 17942194; 18029041; 18056395; 19269008; 19414860; 19573080; 19705160; 19773279; 20237496; 20402676; 20453000; 20514521; 20816908; 20855536; 21282934; 21317160; 21479362; 21781452; 21832049; 21984918; 21988832; 22246630; 22733992; 23661706; 23684308 caspase 4, apoptosis-related cysteine peptidase Ensembl:ENSG00000196954 HGNC:1505 HPRD:04047 MIM:602664 Vega:OTTHUMG00000166078 Other designations: CASP-4|ICE(rel)-II|apoptotic cysteine protease Mih1/TX|caspase 4, apoptosis-related cysteine protease|caspase-4|protease ICH-2|protease TX CASP4 OGG:3000000838 Bin Zhao, Yue Liu, Oliver He ICE(rel)III ICEREL-III ICH-3 WEB: http://www.ncbi.nlm.nih.gov/gene CASP5 caspase 5, apoptosis-related cysteine peptidase 838 11q22.2-q22.3 9606 11 GO_0004197 (EC: IBA); GO_0005737 (EC: IBA); GO_0006508 (EC: TAS, PMID:7797592); GO_0006915 (EC: TAS, PMID:7797592); GO_0008234 (EC: TAS, PMID:7797592); GO_0021762 (EC: IEP); GO_0042981 (EC: IEA); GO_0050727 (EC: IBA); GO_0071260 (EC: IEP, PMID:19593445); GO_0072557 (EC: IBA, Qualifier: NOT); GO_0072558 (EC: IDA, PMID:12191486); GO_0072559 (EC: IBA, Qualifier: NOT); GO_0097169 (EC: IBA, Qualifier: NOT); GO_0097194 (EC: IBA) PMID:7797592; 8617266; 9250871; 9298992; 9894612; 10872455; 10986288; 11356849; 11535131; 12191486; 12477932; 12479849; 12853457; 12964016; 15886296; 16886895; 16893518; 17418785; 17676485; 18430458; 19074885; 19203830; 19269008; 19270026; 19414860; 19573080; 19593445; 19604093; 19773279; 20237496; 20379614; 20402676; 20434535; 20635389; 20855536; 21051981; 21191419; 21454616; 21668377; 21700414; 21969293; 22906436 caspase 5, apoptosis-related cysteine peptidase Ensembl:ENSG00000137757 HGNC:1506 HPRD:04048 MIM:602665 Vega:OTTHUMG00000048073 Other designations: CASP-5|ICE(rel)-III|TY protease|caspase 5, apoptosis-related cysteine protease|caspase-5|protease ICH-3|protease TY CASP5 OGG:3000000839 Bin Zhao, Yue Liu, Oliver He MCH2 WEB: http://www.ncbi.nlm.nih.gov/gene CASP6 caspase 6, apoptosis-related cysteine peptidase 839 4q25 9606 4 GO_0004197 (EC: IBA); GO_0004197 (EC: TAS); GO_0005515 (EC: IPI, PMID:12888622); GO_0005654 (EC: TAS); GO_0005829 (EC: IDA, PMID:17167422); GO_0005829 (EC: TAS); GO_0006508 (EC: IDA, PMID:12888622); GO_0006915 (EC: IBA); GO_0006915 (EC: TAS); GO_0006921 (EC: TAS); GO_0008234 (EC: TAS, PMID:7796396); GO_0030855 (EC: IEP); GO_0042802 (EC: IPI) PMID:7796396; 7983002; 8710882; 8780721; 8812467; 8900201; 8962078; 8978814; 9219695; 9228018; 9298992; 9337844; 9463409; 9593687; 9857079; 9933635; 9990034; 10069390; 10103059; 10205159; 10409650; 10432301; 10438520; 10469173; 10481058; 10655504; 10734073; 10770929; 11016947; 11098060; 11246070; 11262188; 11331782; 11356849; 11387340; 11423904; 11438643; 11463840; 11514563; 11802788; 11832478; 11859414; 11901153; 11953316; 12052891; 12089322; 12145703; 12232792; 12477932; 12888622; 14713958; 15103018; 15200957; 15273717; 15280469; 15321985; 15356202; 15489334; 15500642; 15511269; 15654952; 15735701; 16123779; 16135563; 16169070; 16341674; 16518869; 16948818; 16977583; 17167422; 17337451; 17392160; 18029348; 18155731; 18408014; 18497562; 18723680; 18762957; 18820706; 18946722; 19022247; 19052714; 19219602; 19269008; 19414860; 19573080; 19694615; 19773279; 19897582; 19915487; 20097875; 20332099; 20402676; 20427671; 20437871; 20606168; 20661084; 20682790; 20702410; 20801175; 20855536; 20890311; 21098228; 21111746; 21139048; 21317160; 21621544; 21900206; 21906983; 21918813; 21936563; 21963094; 21988832; 22094081; 22433863; 22505724; 22683611; 22858542; 22891250; 23402898 caspase 6, apoptosis-related cysteine peptidase Ensembl:ENSG00000138794 HGNC:1507 HPRD:03321 MIM:601532 Vega:OTTHUMG00000131914 Other designations: apoptotic protease MCH-2|caspase 6, apoptosis-related cysteine protease|caspase-6 CASP6 OGG:3000000840 Bin Zhao, Yue Liu, Oliver He CASP-7 CMH-1 ICE-LAP3 LICE2 MCH3 WEB: http://www.ncbi.nlm.nih.gov/gene CASP7 caspase 7, apoptosis-related cysteine peptidase 840 RP11-211N11.6 10q25 9606 10 GO_0001836 (EC: IEA); GO_0004190 (EC: IEA); GO_0004197 (EC: IBA); GO_0004197 (EC: TAS); GO_0005515 (EC: IPI, PMID:11084335); GO_0005634 (EC: IDA, PMID:17167422); GO_0005654 (EC: TAS); GO_0005737 (EC: TAS, PMID:8576161); GO_0005829 (EC: IDA, PMID:17167422); GO_0005829 (EC: TAS); GO_0006508 (EC: IDA, PMID:12888622); GO_0006915 (EC: TAS); GO_0006921 (EC: TAS); GO_0007507 (EC: IEA); GO_0007568 (EC: IEA); GO_0008234 (EC: TAS, PMID:8567622); GO_0008635 (EC: TAS); GO_0009411 (EC: IEA); GO_0043525 (EC: IEA); GO_0097153 (EC: IEA); GO_0097193 (EC: TAS); GO_0097194 (EC: IBA) PMID:1056466; 7983002; 8125298; 8521391; 8567622; 8576161; 8631895; 8755496; 8780721; 8812467; 8889548; 8962078; 9070923; 9219695; 9228018; 9230442; 9298992; 9323209; 9325343; 9337844; 9384571; 9525868; 9535906; 9593687; 9607320; 9671712; 9850056; 9875225; 9894612; 9922454; 9990034; 10069390; 10082581; 10103059; 10200531; 10318789; 10469173; 10564664; 10675528; 10731697; 10791974; 10862606; 10998058; 11016947; 11024045; 11058599; 11084335; 11170436; 11257230; 11257231; 11257232; 11278572; 11356849; 11359776; 11387340; 11399776; 11420704; 11423904; 11425872; 11448953; 11514563; 11535131; 11555640; 11752425; 11755217; 11802788; 11815631; 11829465; 11832478; 11859414; 11875078; 11904443; 11943137; 12107159; 12145703; 12181742; 12477932; 12586738; 12665508; 12804035; 12824163; 12888622; 12951057; 12970753; 14512414; 14583630; 14584591; 14623896; 14713958; 15033720; 15200957; 15254227; 15489334; 15500642; 15507451; 15511269; 15580265; 15650747; 15735701; 16123041; 16213496; 16339151; 16344560; 16385451; 16498457; 16918502; 17023557; 17094969; 17167422; 17283187; 17337451; 17504820; 17532763; 17697120; 17880920; 17978580; 18072206; 18086147; 18459962; 18521960; 18596415; 18708163; 18723680; 18785314; 19022247; 19052714; 19058873; 19141860; 19219602; 19241192; 19258326; 19269008; 19323650; 19414860; 19531679; 19573080; 19581639; 19604093; 19605487; 19617626; 19655253; 19655254; 19692467; 19698783; 19738422; 19759058; 19770576; 19773279; 19782763; 19826114; 19913121; 19996278; 20159985; 20379614; 20402676; 20404718; 20453000; 20468060; 20566630; 20567846; 20628086; 20661084; 20800603; 20819778; 20855536; 20950443; 20959405; 21044950; 21142842; 21157428; 21484410; 21555521; 21936563; 22184066; 22441531; 22451931; 22548721; 22561518; 22584050; 22863883; 22986525; 23000965; 23190606; 23383273; 23650375; 23765963; 23979166 caspase 7, apoptosis-related cysteine peptidase Ensembl:ENSG00000165806 HGNC:1508 HPRD:03457 MIM:601761 Vega:OTTHUMG00000019076 Other designations: ICE-like apoptotic protease 3|apoptotic protease MCH-3|caspase 7, apoptosis-related cysteine protease|caspase-7 CASP7 OGG:3000000841 Bin Zhao, Yue Liu, Oliver He ALPS2B CAP4 Casp-8 FLICE MACH MCH5 WEB: http://www.ncbi.nlm.nih.gov/gene CASP8 caspase 8, apoptosis-related cysteine peptidase 841 2q33-q34 9606 2 GO_0001525 (EC: IEA); GO_0001841 (EC: IEA); GO_0002020 (EC: IPI); GO_0002224 (EC: TAS); GO_0002756 (EC: TAS); GO_0004197 (EC: IDA, PMID:19240112); GO_0004197 (EC: TAS); GO_0005164 (EC: IEA); GO_0005515 (EC: IPI, PMID:10442631); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005739 (EC: IDA); GO_0005741 (EC: TAS); GO_0005815 (EC: IDA); GO_0005829 (EC: IDA, PMID:17167422); GO_0005829 (EC: TAS); GO_0005856 (EC: TAS, PMID:10891503); GO_0006508 (EC: IDA, PMID:12888622); GO_0006915 (EC: IGI, PMID:17599062); GO_0006915 (EC: IMP); GO_0006915 (EC: TAS); GO_0006919 (EC: TAS); GO_0006921 (EC: TAS); GO_0007507 (EC: IEA); GO_0008233 (EC: IMP, PMID:17047155); GO_0008234 (EC: TAS, PMID:8681376); GO_0008625 (EC: IBA); GO_0009409 (EC: IEA); GO_0016032 (EC: IEA); GO_0030101 (EC: TAS, PMID:18309324); GO_0030225 (EC: TAS, PMID:18309324); GO_0030690 (EC: IEA); GO_0031264 (EC: IDA, PMID:11101870); GO_0031265 (EC: IDA, PMID:11717445); GO_0031625 (EC: IPI, PMID:15069192); GO_0032025 (EC: IEA); GO_0032355 (EC: IEA); GO_0032496 (EC: IEA); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034612 (EC: IMP, PMID:10521396); GO_0035666 (EC: TAS); GO_0035872 (EC: TAS); GO_0035877 (EC: IPI, PMID:11717445); GO_0042110 (EC: TAS, PMID:18309324); GO_0042113 (EC: TAS, PMID:18309324); GO_0043005 (EC: IEA); GO_0043123 (EC: IEP, PMID:12761501); GO_0043123 (EC: IMP, PMID:12884866); GO_0043124 (EC: IMP, PMID:17047155); GO_0044297 (EC: IEA); GO_0045087 (EC: TAS); GO_0045121 (EC: IEA); GO_0045471 (EC: IEA); GO_0045651 (EC: IMP, PMID:17047155); GO_0045862 (EC: IDA, PMID:18387192); GO_0046677 (EC: IEA); GO_0051291 (EC: IEA); GO_0051603 (EC: IMP, PMID:10521396); GO_0060715 (EC: TAS, PMID:18309324); GO_0070243 (EC: IEA); GO_0070423 (EC: TAS); GO_0071260 (EC: IEP, PMID:19593445); GO_0071407 (EC: IEA); GO_0097153 (EC: IMP); GO_0097190 (EC: IMP, PMID:11101870); GO_0097190 (EC: TAS); GO_0097191 (EC: IDA); GO_0097193 (EC: TAS); GO_0097194 (EC: IMP); GO_0097199 (EC: IMP, PMID:11717445); GO_0097202 (EC: IDA, PMID:18387192); GO_0097284 (EC: IEA); GO_0097342 (EC: IDA); GO_1900740 (EC: TAS); GO_2001238 (EC: IEA); GO_2001239 (EC: TAS) PMID:170210; 3031469; 7983002; 8521391; 8681376; 8681377; 8755496; 8962078; 9006941; 9027312; 9184224; 9208847; 9219695; 9228018; 9271594; 9289491; 9325248; 9326610; 9334338; 9337844; 9380701; 9535906; 9539746; 9560245; 9575181; 9624166; 9632733; 9721089; 9727491; 9727492; 9763668; 9774341; 9792675; 9804161; 9875225; 9878167; 9931493; 9971775; 9990034; 10069390; 10235259; 10329646; 10432301; 10435619; 10438581; 10442631; 10469173; 10493725; 10508784; 10521396; 10616217; 10708425; 10716992; 10734073; 10860845; 10891503; 10894160; 10911620; 10926122; 10964557; 11000244; 11002417; 11016947; 11048727; 11085743; 11098060; 11101867; 11101870; 11102441; 11161814; 11177389; 11181075; 11260720; 11264300; 11340079; 11387340; 11395500; 11406564; 11420686; 11423904; 11431480; 11437602; 11479289; 11514563; 11555640; 11583996; 11683038; 11684016; 11717445; 11733517; 11734564; 11735112; 11741396; 11741985; 11751056; 11751897; 11752160; 11772515; 11788820; 11832478; 11865194; 11877293; 11917123; 11933563; 11940602; 11965497; 11992615; 12010809; 12021264; 12037669; 12041673; 12052891; 12065591; 12095993; 12096338; 12097160; 12107159; 12107169; 12122017; 12131184; 12170765; 12189238; 12191471; 12196516; 12198154; 12215447; 12218097; 12220669; 12232792; 12353035; 12393901; 12404116; 12438416; 12477932; 12496481; 12496482; 12507932; 12527898; 12598529; 12620239; 12646168; 12668660; 12692130; 12700635; 12700660; 12702723; 12707329; 12721308; 12738800; 12748179; 12750393; 12750404; 12753742; 12754217; 12761501; 12765336; 12804595; 12841868; 12884866; 12887920; 12888622; 12911633; 12912912; 12960156; 13679856; 14522966; 14560027; 14584591; 14625033; 14644092; 14644197; 14684825; 14688019; 14701762; 14713958; 14759258; 14970175; 14982875; 14982947; 14991747; 14993214; 15015772; 15024054; 15034549; 15067048; 15069192; 15111130; 15142380; 15159409; 15205454; 15210716; 15254227; 15262979; 15280356; 15289853; 15369772; 15383280; 15388581; 15389560; 15390286; 15473998; 15476874; 15489334; 15492869; 15507451; 15507484; 15509781; 15531912; 15578977; 15592455; 15592525; 15601643; 15611097; 15637055; 15640164; 15645452; 15650242; 15659383; 15701651; 15717329; 15735701; 15735742; 15746428; 15760909; 15782135; 15815621; 15849201; 15906362; 15956881; 15976052; 16036110; 16135563; 16169070; 16179347; 16179941; 16183855; 16186808; 16193064; 16225956; 16227629; 16242324; 16251207; 16344560; 16374545; 16397500; 16436380; 16446372; 16478725; 16497673; 16528386; 16538383; 16541419; 16556893; 16607283; 16619028; 16633737; 16636047; 16722146; 16733806; 16762833; 16886176; 16920630; 16936772; 16938569; 16951203; 17018785; 17030903; 17047155; 17064406; 17071630; 17159907; 17167422; 17170703; 17182797; 17224200; 17272309; 17283187; 17290218; 17293864; 17314102; 17337451; 17378240; 17436592; 17442709; 17450141; 17488272; 17525260; 17532763; 17534194; 17545522; 17572490; 17585337; 17599062; 17616526; 17623017; 17626072; 17627287; 17653867; 17666167; 17684142; 17726263; 17891485; 17911615; 17932347; 17940865; 18029348; 18045865; 18054197; 18076022; 18086677; 18089778; 18089800; 18097748; 18158779; 18161513; 18216014; 18245485; 18305469; 18309324; 18324486; 18328427; 18343995; 18362937; 18381704; 18387192; 18398042; 18431743; 18455983; 18458084; 18473402; 18483392; 18485876; 18516683; 18563783; 18570872; 18596409; 18603835; 18617900; 18625728; 18632964; 18675369; 18676680; 18676836; 18684943; 18691973; 18716417; 18725521; 18728974; 18776134; 18796435; 18823309; 18823701; 18840411; 18974049; 19001123; 19013323; 19048023; 19048627; 19060883; 19074885; 19094228; 19111387; 19112091; 19115040; 19122169; 19124506; 19125371; 19141860; 19152111; 19160091; 19166881; 19170196; 19176810; 19203830; 19214542; 19214744; 19219602; 19239323; 19240112; 19258216; 19260109; 19269008; 19275584; 19275586; 19276244; 19289465; 19318553; 19343040; 19345995; 19372376; 19373245; 19412632; 19414860; 19427028; 19432816; 19453261; 19470771; 19492233; 19493480; 19521670; 19528225; 19531679; 19542541; 19543235; 19550122; 19573080; 19593445; 19597472; 19617217; 19625176; 19629679; 19644511; 19665028; 19684859; 19692168; 19692467; 19698994; 19710364; 19738422; 19770581; 19773279; 19773432; 19778795; 19795398; 19801665; 19807657; 19812265; 19826114; 19843670; 19852930; 19854135; 19902255; 19913121; 19923319; 19954364; 19996275; 20005201; 20012528; 20013803; 20033750; 20033885; 20044137; 20080300; 20085538; 20086182; 20087649; 20132554; 20143425; 20145138; 20150972; 20176653; 20198319; 20237344; 20301425; 20308068; 20353946; 20356928; 20363033; 20379197; 20398055; 20402676; 20403046; 20404718; 20443055; 20448643; 20453000; 20471133; 20502973; 20554749; 20564345; 20565257; 20572163; 20605201; 20606168; 20613771; 20616437; 20628086; 20644561; 20652397; 20661084; 20671745; 20677014; 20702410; 20724831; 20799830; 20800603; 20802294; 20804486; 20808443; 20811726; 20817393; 20819778; 20825417; 20829884; 20855536; 20870287; 20877624; 20937773; 20951133; 20959405; 20972266; 20978129; 20978178; 21048031; 21072056; 21104989; 21107701; 21135236; 21139048; 21153367; 21157428; 21166494; 21178828; 21183680; 21183955; 21248767; 21282461; 21328377; 21380726; 21396853; 21419663; 21426305; 21436691; 21444671; 21454681; 21458669; 21461653; 21483669; 21487429; 21524651; 21525013; 21538054; 21548803; 21554547; 21569377; 21576355; 21620750; 21628531; 21633787; 21667042; 21669575; 21697465; 21704196; 21714991; 21724551; 21737329; 21751259; 21785112; 21785459; 21801448; 21803845; 21816816; 21819468; 21822306; 21865223; 21868312; 21900206; 21906983; 21979465; 21983787; 21988832; 22010212; 22027693; 22037414; 22056502; 22094081; 22120515; 22160860; 22179575; 22211869; 22253841; 22266862; 22267217; 22274400; 22297296; 22322857; 22339913; 22357491; 22383778; 22408249; 22421964; 22508042; 22513478; 22528489; 22585859; 22588838; 22632162; 22644571; 22659694; 22672670; 22683265; 22683266; 22691345; 22801217; 22806078; 22815944; 22820578; 22843554; 22860893; 22864571; 22922291; 22949938; 22971934; 23071110; 23081800; 23096115; 23142077; 23185580; 23230268; 23244104; 23255602; 23289213; 23306557; 23313206; 23418437; 23434145; 23618862; 23659359; 23751956; 23770605; 23844036; 23921907; 23972990; 23982205; 24021263; 24121507; 24391214 caspase 8, apoptosis-related cysteine peptidase Ensembl:ENSG00000064012 HGNC:1509 HPRD:03459 MIM:601763 Vega:OTTHUMG00000132821 Other designations: FADD-homologous ICE/CED-3-like protease|FADD-like ICE|ICE-like apoptotic protease 5|MACH-alpha-1/2/3 protein|MACH-beta-1/2/3/4 protein|MORT1-associated ced-3 homolog|apoptotic cysteine protease|apoptotic protease Mch-5|caspase 8, apoptosis-related cysteine protease|caspase-8 CASP8 OGG:3000000842 Bin Zhao, Yue Liu, Oliver He APAF-3 APAF3 ICE-LAP6 MCH6 PPP1R56 WEB: http://www.ncbi.nlm.nih.gov/gene CASP9 caspase 9, apoptosis-related cysteine peptidase 842 RP11-265F14.3 1p36.21 9606 1 GO_0004197 (EC: IBA); GO_0005515 (EC: IPI, PMID:10206961); GO_0005634 (EC: IEA); GO_0005739 (EC: IEA); GO_0005829 (EC: IDA, PMID:17167422); GO_0005829 (EC: TAS); GO_0006915 (EC: TAS, PMID:8663294); GO_0006974 (EC: IDA, PMID:15657060); GO_0007173 (EC: TAS); GO_0007568 (EC: IEA); GO_0008047 (EC: TAS, PMID:9390557); GO_0008233 (EC: IDA); GO_0008543 (EC: TAS); GO_0008630 (EC: IMP, PMID:15657060); GO_0008635 (EC: TAS); GO_0017124 (EC: IDA, PMID:15657060); GO_0019901 (EC: IDA, PMID:15657060); GO_0030220 (EC: TAS, PMID:18309324); GO_0032025 (EC: IEA); GO_0032355 (EC: IEA); GO_0032496 (EC: IEA); GO_0034349 (EC: IEA); GO_0034644 (EC: IDA, PMID:15657060); GO_0038095 (EC: TAS); GO_0042770 (EC: IDA, PMID:15657060); GO_0042981 (EC: TAS); GO_0043065 (EC: TAS); GO_0043293 (EC: IDA); GO_0043525 (EC: IEA); GO_0045087 (EC: TAS); GO_0046677 (EC: IEA); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0071549 (EC: IEA); GO_0097193 (EC: TAS); GO_2001020 (EC: IMP, PMID:15657060) PMID:1067155; 7983002; 8663294; 8900201; 8962078; 9323209; 9337844; 9390557; 9488720; 9539746; 9545235; 9651578; 9671712; 9812896; 9837928; 9878060; 9890966; 9922454; 9990849; 10070954; 10085063; 10187815; 10206961; 10329646; 10376594; 10384055; 10438581; 10469173; 10671558; 10708425; 11024045; 11069302; 11076957; 11084335; 11113115; 11230124; 11242052; 11248093; 11350957; 11387340; 11390657; 11393657; 11408476; 11423904; 11462036; 11514563; 11734640; 11801602; 11801603; 11803376; 11832478; 11870543; 11905052; 11919192; 11927604; 11948397; 12021264; 12055227; 12095993; 12096338; 12145703; 12147322; 12372609; 12393263; 12393884; 12404116; 12477932; 12566444; 12586738; 12620238; 12620239; 12637514; 12732844; 12749848; 12782307; 12792650; 12804035; 12914932; 12954616; 14512414; 14523016; 14566819; 14634335; 14684629; 14701803; 14747474; 14982875; 14991812; 14993223; 15200957; 15214043; 15220451; 15254227; 15262985; 15273730; 15280366; 15300255; 15473998; 15485395; 15485396; 15489334; 15500642; 15507451; 15578977; 15629764; 15657060; 15657349; 15674327; 15703181; 15725353; 15735701; 15749826; 15767427; 15811855; 15829969; 15935070; 16038259; 16120388; 16181301; 16242324; 16260615; 16287866; 16300929; 16322207; 16337360; 16339151; 16344560; 16480911; 16497673; 16505307; 16505493; 16511342; 16520893; 16687442; 16689829; 16701639; 16710414; 16716256; 16780893; 16895904; 16936772; 16979168; 17030903; 17071630; 17079734; 17140287; 17167422; 17179183; 17207965; 17285546; 17291493; 17299206; 17379327; 17409234; 17437405; 17466630; 17534194; 17626072; 17653867; 17893147; 17899380; 17967742; 18022362; 18054197; 18083711; 18086147; 18202770; 18297401; 18309324; 18381704; 18415681; 18632964; 18676680; 18723680; 18813792; 18814044; 18840411; 19013323; 19016842; 19052714; 19058789; 19074885; 19081073; 19141860; 19153467; 19159073; 19170196; 19183163; 19219602; 19238172; 19269008; 19275583; 19275584; 19275586; 19275587; 19359048; 19412632; 19414860; 19458171; 19465923; 19493480; 19550122; 19573080; 19625176; 19626422; 19655415; 19674438; 19692168; 19692467; 19698783; 19724860; 19741144; 19758996; 19770581; 19773279; 19789190; 19807657; 19826114; 19895210; 19906200; 19913121; 20012528; 20013803; 20022954; 20042134; 20060927; 20071584; 20227371; 20227384; 20340172; 20357690; 20379614; 20402676; 20404718; 20453000; 20490276; 20628086; 20644561; 20650551; 20661084; 20667824; 20800603; 20804486; 20855536; 20887385; 20959405; 20978129; 21045158; 21048031; 21091209; 21117896; 21142842; 21178828; 21266831; 21282934; 21284734; 21297999; 21382445; 21396853; 21461653; 21483669; 21538054; 21555338; 21565459; 21612408; 21622622; 21644232; 21659556; 21724551; 21757755; 21785112; 21827945; 21868008; 21869827; 21944661; 21957492; 21988832; 22086301; 22120515; 22191568; 22219640; 22306364; 22339913; 22552851; 22573662; 22616010; 22629415; 22679284; 22683311; 22926545; 22944165; 22974165; 22981751; 23038270; 23303631; 23383273; 23396972; 23424205; 23430060; 23443079; 23539542; 23566959; 23572523; 23615977; 23637769; 23645041; 23652278; 23678002; 23725396; 23867824; 24121507; 24161344; 24346702 caspase 9, apoptosis-related cysteine peptidase Ensembl:ENSG00000132906 HGNC:1511 HPRD:03756 MIM:602234 Vega:OTTHUMG00000002256 Other designations: ICE-like apoptotic protease 6|apoptotic protease MCH-6|apoptotic protease activating factor 3|caspase-9|protein phosphatase 1, regulatory subunit 56 CASP9 OGG:3000000843 Bin Zhao, Yue Liu, Oliver He ALPS2 FLICE2 MCH4 WEB: http://www.ncbi.nlm.nih.gov/gene CASP10 caspase 10, apoptosis-related cysteine peptidase 843 2q33-q34 9606 2 GO_0004197 (EC: TAS, PMID:10412980); GO_0005515 (EC: IPI, PMID:12884866); GO_0005737 (EC: IBA); GO_0005829 (EC: TAS); GO_0005886 (EC: TAS); GO_0006915 (EC: IBA); GO_0006915 (EC: TAS); GO_0031265 (EC: IDA, PMID:11717445); GO_0031625 (EC: IPI, PMID:15069192); GO_0035877 (EC: IPI, PMID:11717445); GO_0042981 (EC: IEA); GO_0043123 (EC: IMP, PMID:12884866); GO_0043123 (EC: RCA, PMID:19641626); GO_0045087 (EC: TAS); GO_0097190 (EC: TAS); GO_0097199 (EC: IMP, PMID:11717445); GO_0097342 (EC: IDA) PMID:170210; 1171445; 3031469; 8125298; 8521391; 8755496; 8962078; 9045686; 9153302; 9208847; 9228018; 9289491; 9325248; 9337844; 9792675; 10187817; 10412980; 10432301; 10716992; 10734073; 11002417; 11048727; 11098060; 11161814; 11395500; 11583996; 11717445; 11832478; 11973654; 12010812; 12037669; 12198154; 12388546; 12477932; 12527898; 12884866; 12887920; 14687710; 14688482; 14759258; 14761933; 15069192; 15280356; 15452117; 15500642; 15659383; 15735701; 15767684; 15772077; 16186808; 16251207; 16344560; 16446975; 16767158; 17071630; 17085968; 17159907; 17450141; 17479112; 17534194; 17623017; 17822854; 17999750; 18381704; 18563783; 18676680; 18716417; 18823309; 19074885; 19141860; 19166881; 19170196; 19219602; 19269008; 19380486; 19414860; 19423537; 19550122; 19604093; 19625176; 19641626; 19692168; 19773279; 19784808; 19826114; 19861680; 19900088; 19902255; 20025484; 20301287; 20402676; 20453000; 20467438; 20644561; 20661084; 20800603; 20802294; 20829884; 20855536; 20959405; 20978178; 21048031; 21139048; 21368896; 21454616; 21559821; 21911414; 21988832; 22683265; 22782902; 22843554; 22864571; 23212337; 23303631; 23541952; 23770605; 23921907 caspase 10, apoptosis-related cysteine peptidase Ensembl:ENSG00000003400 HGNC:1500 HPRD:03458 MIM:601762 Vega:OTTHUMG00000132818 Other designations: CASP-10|FADD-like ICE2|FAS-associated death domain protein interleukin-1B-converting enzyme 2|ICE-like apoptotic protease 4|apoptotic protease MCH-4|caspase 10, apoptosis-related cysteine protease|caspase-10|interleukin-1B-converting enzyme 2 CASP10 OGG:3000000846 Bin Zhao, Yue Liu, Oliver He CAR EIG8 FHH FIH GPRC2A HHC HHC1 HYPOC1 NSHPT PCAR1 WEB: http://www.ncbi.nlm.nih.gov/gene CASR calcium-sensing receptor 846 3q13 9606 3 Official from a nomenclature committee GO_0001503 (EC: TAS, PMID: 7874174); GO_0004435 (EC: TAS, PMID: 7874174); GO_0004930 (EC: IEA); GO_0005513 (EC: TAS, PMID: 7759551); GO_0005515 (EC: IPI); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 7759551); GO_0006874 (EC: TAS, PMID: 7874174); GO_0007186 (EC: TAS, PMID: 7759551); GO_0007635 (EC: TAS, PMID: 7759551); GO_0008152 (EC: TAS, PMID: 7874174); GO_0009653 (EC: TAS, PMID: 7916660); GO_0070509 (EC: IDA) PMID: 7673400; 7677761; 7726161; 7759551; 7874174; 7916660; 8597637; 8613532; 8675635; 8702647; 8733126; 8756555; 9168937; 9217223; 9298824; 9677383; 9694886; 9722601; 9852126; 9920108; 9920407; 10405337; 10487661; 11013439; 11095989; 11108243; 11161843; 11248745; 11390379; 11390380; 11589681; 11668634; 11762699; 11863123; 11889154; 11889203; 11907035; 11979955; 11984699; 12018449; 12036954; 12040821; 12050233; 12052452; 12095982; 12150336; 12239240; 12241879; 12356761; 12399473; 12409307; 12459170; 12469911; 12477932; 12517779; 12544508; 12574201; 12605346; 12656660; 12700051; 12773131; 12783889; 12890593; 12899245; 12914574; 14508624; 14660633; 14713274; 14729680; 14976203; 14985373; 15201280; 15219850; 15472173; 15489334; 15501733; 15531522; 15551332; 15572418; 15579475; 15591042; 15598778; 15613438; 15637145; 15657061; 15684428; 15718278; 15781005; 15805541; 15837785; 15864123; 15879434; 15888439; 15960151; 16109841; 16117875; 16147994; 16218047; 16278666; 16472767; 16497624; 16509534; 16513638; 16596260; 16598859; 16616098; 16622736; 16642557; 16735501; 16738533; 16740430; 16754659; 16854379; 16938272; 17018660; 17046587; 17054460; 17062884; 17097611; 17110864; 17122384; 17124506; 17132283; 17138967; 17284438; 17309124; 17310098; 17320849; 17331389; 17332735; 17372216; 17374704; 17374709; 17426287; 17463182; 17473068; 17478419; 17482347; 17513419; 17537980; 17555508; 17591780; 17623778; 17698911; 17853337; 17932932; 17962359; 17974568; 17979873; 18065418; 18240029; 18296474; 18322048; 18328986; 18348986; 18393231; 18410554; 18443236; 18497443; 18525093; 18577758; 18621740; 18622738; 18676680; 18680227; 18703641; 18712808; 18751724; 18756473; 18796518; 18843020; 18852253; 18938753; 18980667; 19011996; 19035514; 19038444; 19058262; 19066294; 19073830; 19088423; 19133942; 19151705; 19157541; 19170196; 19179454; 19237714; 19257819; 19285978; 19328421; 19350667; 19389809; 19397786; 19423559; 19432691; 19453261; 19471101; 19474519; 19580466; 19621386; 19625176; 19640368; 19690432; 19692168; 19695239; 19706842; 19716891; 19789209; 19839774; 19887834; 19912241; 19913121; 19915295; 20034274; 20067903; 20130845; 20164288; 20237496; 20361938; 20364112; 20421307; 20424473; 20457124; 20558521; 20558539; 20595056; 20602573; 20628086; 20631026; 20634891; 20648625; 20654748; 20661308; 20668040; 20697181; 20705733; 20798521; 20826781; 20846291; 21048031; 21082232; 21084311; 21130730; 21183554; 21187282; 21209619; 21240254; 21317879; 21340433; 21369680; 21393549; 21414629; 21441391; 21532883; 21566074; 21645025; 21667241; 21843504; 21965686; 21966463; 22010828; 22024717; 22094462; 22107799; 22144504; 22158862; 22187299; 22192860; 22210744; 22278364; 22315359; 22403735; 22422767; 22424352; 22449852; 22577108; 22730443; 22789683; 22798347; 23009664; 23103379; 23108190; 23125333; 23169696; 23228129; 23247143; 23269116; 23271661; 23287098; 23300272; 23334987; 23372019; 23533647; 23552627; 23555732; 23569134; 23639611; 23674327; 23756480; 23764372; 23817301; 23856265; 23860708; 23864702; 23913941; 23917029; 23946278; 24068962; 24120622; 24238055; 24336654; 24455835 calcium-sensing receptor Ensembl:ENSG00000036828 HGNC:1514 HPRD:03122 MIM:601199 Vega:OTTHUMG00000159491 Other designations: extracellular calcium-sensing receptor|parathyroid Ca(2+)-sensing receptor 1|parathyroid cell calcium-sensing receptor 1 CASR OGG:3000000900 Bin Zhao, Yue Liu, Oliver He CCNG WEB: http://www.ncbi.nlm.nih.gov/gene CCNG1 cyclin G1 900 5q32-q34 9606 5 Official from a nomenclature committee GO_0000079 (EC: TAS, PMID: 8626390); GO_0005515 (EC: IPI); GO_0005634 (EC: IEA); GO_0006949 (EC: IEA); GO_0007067 (EC: IEA); GO_0007095 (EC: IEA); GO_0007420 (EC: IEA); GO_0010243 (EC: IEA); GO_0016049 (EC: IEA); GO_0019904 (EC: IEA); GO_0030425 (EC: IEA); GO_0043025 (EC: IEA); GO_0043066 (EC: IEA); GO_0048471 (EC: IEA) PMID: 8626390; 8806701; 8887688; 8954786; 9013862; 10194136; 10196184; 11956189; 12214116; 12477932; 12556559; 12634633; 12642871; 12684677; 15077171; 15489334; 16322753; 17616664; 17868090; 18408012; 18632610; 18981217; 19584283; 19698214; 19738611; 21688120; 21832049; 21988832; 22105316; 22271581; 22649121; 22835824; 23589924 cyclin G1 Ensembl:ENSG00000113328 HGNC:1592 HPRD:03345 MIM:601578 Vega:OTTHUMG00000130380 Other designations: cyclin-G|cyclin-G1 CCNG1 OGG:3000000929 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CD14 CD14 molecule 929 5q31.1 20140408 9606 5 protein-coding Official from a nomenclature committee GO_0001530 (EC: IDA, PMID: 12594207); GO_0001847 (EC: TAS, PMID: 2402637); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0005515 (EC: IPI); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0005886 (EC: TAS); GO_0006909 (EC: TAS, PMID: 9548256); GO_0006915 (EC: TAS, PMID: 9548256); GO_0006954 (EC: IEA); GO_0007166 (EC: TAS, PMID: 8798531); GO_0007249 (EC: TAS); GO_0009408 (EC: IEA); GO_0009986 (EC: IEA); GO_0010008 (EC: TAS); GO_0016019 (EC: TAS, PMID: 8798531); GO_0031225 (EC: IEA); GO_0032026 (EC: IEA); GO_0032760 (EC: IDA, PMID: 12594207); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034612 (EC: IEA); GO_0035666 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0045087 (EC: TAS); GO_0045121 (EC: IEA); GO_0045471 (EC: IEA); GO_0045807 (EC: IEA); GO_0050715 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0070891 (EC: IDA, PMID: 12594207); GO_0071222 (EC: IDA, PMID: 12594207); GO_0071223 (EC: IDA, PMID: 12594207) PMID: 2402637; 2448876; 2453848; 2462937; 2472171; 2779588; 3385210; 7583357; 8798531; 9142045; 9548256; 9562334; 9655682; 9665271; 10395652; 10575214; 11062291; 11076863; 11083760; 11145656; 11199329; 11257272; 11282774; 11343243; 11489942; 11732288; 11745332; 11779220; 11810121; 11825494; 11841490; 11843056; 11854210; 11876746; 11932927; 11935032; 11985523; 12006789; 12011764; 12067299; 12075251; 12082592; 12101079; 12103253; 12106839; 12117913; 12126249; 12140663; 12171914; 12174084; 12185442; 12196527; 12207338; 12324469; 12404174; 12410798; 12414752; 12417309; 12438323; 12450609; 12477932; 12492251; 12566518; 12580907; 12594207; 12624278; 12663765; 12679473; 12700637; 12731067; 12754215; 12756848; 12757265; 12825176; 12832426; 12853157; 12885845; 12897754; 12911501; 12938192; 12940436; 12942028; 12960274; 14500479; 14508193; 14510720; 14517492; 14517520; 14587643; 14617510; 14624155; 14648231; 14672339; 14673018; 14706103; 14720421; 14739370; 14996480; 15034063; 15039096; 15069085; 15080833; 15081257; 15116260; 15120158; 15132789; 15143473; 15164100; 15166925; 15175649; 15190267; 15207785; 15257175; 15269840; 15273551; 15292769; 15342556; 15356557; 15358661; 15369724; 15373760; 15378299; 15489334; 15489336; 15491315; 15516360; 15520404; 15558232; 15591473; 15599151; 15602630; 15619435; 15640605; 15647432; 15655821; 15670766; 15686783; 15714129; 15741437; 15753758; 15764151; 15777548; 15778383; 15842262; 15854776; 15867866; 15879416; 15932345; 15940135; 15946916; 15966209; 15975149; 16038043; 16046876; 16051275; 16061600; 16085746; 16101942; 16109674; 16137548; 16142747; 16148556; 16159630; 16165702; 16174094; 16174099; 16194368; 16239565; 16246938; 16266379; 16273620; 16273622; 16275943; 16283111; 16290232; 16292464; 16331574; 16335952; 16337421; 16344560; 16368002; 16381901; 16385250; 16386288; 16387800; 16409569; 16427140; 16433727; 16437636; 16443672; 16444757; 16446545; 16467036; 16473828; 16492974; 16509825; 16512634; 16520888; 16538169; 16552356; 16611358; 16614348; 16625214; 16698680; 16706818; 16749413; 16751411; 16785528; 16815140; 16836908; 16848791; 16860318; 16873708; 16879054; 16890863; 16893989; 16916546; 16933467; 16950285; 16950521; 17003960; 17007028; 17030237; 17046070; 17052752; 17056323; 17062130; 17067484; 17075287; 17086894; 17087609; 17098305; 17126402; 17187267; 17196641; 17201240; 17205552; 17207357; 17217435; 17259806; 17264400; 17274987; 17304102; 17309585; 17436151; 17438094; 17448042; 17456337; 17471431; 17511783; 17515856; 17565650; 17600225; 17607003; 17617027; 17653770; 17703412; 17802898; 17846597; 17869646; 17877764; 17877801; 17900622; 17913858; 17916440; 17919709; 17925604; 17934216; 17943182; 17949800; 17982638; 18008256; 18040078; 18056918; 18057002; 18067042; 18157711; 18158110; 18174680; 18180316; 18180796; 18182917; 18288274; 18312481; 18315435; 18320914; 18354240; 18385826; 18414664; 18415752; 18417506; 18425216; 18426570; 18458151; 18495781; 18496988; 18497880; 18519568; 18565258; 18571004; 18580445; 18580477; 18596635; 18606699; 18634146; 18664531; 18666712; 18676680; 18691306; 18714537; 18728522; 18767926; 18774388; 18794053; 18810425; 18818748; 18931892; 18938271; 18951711; 18974840; 18974842; 18987746; 18991094; 19006850; 19010986; 19019335; 19027777; 19028820; 19037967; 19046305; 19056867; 19060757; 19096003; 19131662; 19148143; 19170196; 19189651; 19200604; 19210273; 19222419; 19225544; 19242719; 19247692; 19254290; 19258923; 19263529; 19264973; 19275920; 19318422; 19337058; 19346955; 19360901; 19361972; 19365146; 19390489; 19420105; 19423540; 19433913; 19447482; 19466271; 19468702; 19479237; 19500269; 19508433; 19522765; 19527514; 19536153; 19550115; 19559392; 19572148; 19578796; 19584052; 19595045; 19605672; 19625176; 19674346; 19692168; 19701968; 19729601; 19733948; 19741468; 19758335; 19761511; 19795323; 19799036; 19809507; 19824106; 19829130; 19830784; 19845895; 19847953; 19860589; 19892918; 19913121; 19928913; 19948975; 19997857; 20039305; 20085599; 20092898; 20109306; 20109750; 20113368; 20163933; 20179016; 20207250; 20219985; 20227257; 20302606; 20346360; 20363151; 20364047; 20377740; 20381257; 20384875; 20394509; 20395963; 20398919; 20406964; 20430603; 20430725; 20438785; 20452482; 20463618; 20472010; 20472613; 20485444; 20503287; 20532808; 20536280; 20536507; 20555320; 20579716; 20587312; 20603037; 20608916; 20618347; 20628086; 20636398; 20660791; 20673868; 20677014; 20703737; 20717070; 20723409; 20730440; 20826579; 20832340; 20865702; 20964518; 21039068; 21041645; 21048031; 21052690; 21062235; 21063024; 21079949; 21084593; 21118416; 21172039; 21178007; 21191073; 21209279; 21253969; 21257965; 21277522; 21278688; 21293259; 21303362; 21333644; 21361908; 21389010; 21476947; 21489615; 21498585; 21596674; 21633598; 21700881; 21705839; 21722015; 21740312; 21745379; 21799175; 21808991; 21842127; 21885391; 21905503; 21921097; 21948372; 21988832; 22014346; 22015088; 22056216; 22219617; 22232682; 22260507; 22265692; 22363790; 22376040; 22384567; 22445606; 22482418; 22564189; 22648004; 22697010; 22703766; 22737215; 22808111; 22812245; 22937756; 22961048; 22999728; 23000519; 23009036; 23036097; 23036271; 23046822; 23049772; 23079836; 23101184; 23107636; 23121673; 23146639; 23162014; 23162132; 23194293; 23201091; 23206327; 23264655; 23277403; 23338226; 23371544; 23430250; 23510625; 23537804; 23565226; 23582034; 23589304; 23679818; 23741383; 23762319; 23786414; 23824692; 23880187; 23936239; 24044964; 24077340; 24116867; 24172224 CD14 molecule CD14 OGG:3000000960 Bin Zhao, Yue Liu, Oliver He CDW44 CSPG8 ECMR-III HCELL HUTCH-I IN LHR MC56 MDU2 MDU3 MIC4 Pgp1 WEB: http://www.ncbi.nlm.nih.gov/gene CD44 CD44 molecule (Indian blood group) 960 AL133330.1 11p13 9606 11 Official from a nomenclature committee GO_0001658 (EC: IEA); GO_0002246 (EC: IEA); GO_0004415 (EC: IDA, PMID: 17170110); GO_0004888 (EC: IDA, Qualifier: contributes_to, PMID: 17045821); GO_0005515 (EC: IPI, PMID: 11207560); GO_0005518 (EC: NAS, PMID: 2471973); GO_0005540 (EC: IDA, PMID: 17170110); GO_0005540 (EC: NAS, PMID: 1991450); GO_0005737 (EC: IDA); GO_0005794 (EC: IDA); GO_0005886 (EC: IDA); GO_0005886 (EC: TAS); GO_0005887 (EC: NAS, PMID: 1991450); GO_0005975 (EC: TAS); GO_0007160 (EC: NAS, PMID: 1922057); GO_0007596 (EC: TAS); GO_0009897 (EC: IEA); GO_0009986 (EC: IDA, PMID: 16809613); GO_0010628 (EC: IEA); GO_0016055 (EC: IEA); GO_0016323 (EC: IEA); GO_0016337 (EC: NAS, PMID: 1922057); GO_0019221 (EC: TAS); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0030203 (EC: TAS); GO_0030212 (EC: TAS); GO_0030214 (EC: IDA, PMID: 17170110); GO_0030214 (EC: TAS); GO_0033138 (EC: IDA, PMID: 17045821); GO_0034116 (EC: IMP, PMID: 15100360); GO_0043066 (EC: IMP, PMID: 19047049); GO_0043154 (EC: IMP, PMID: 19047049); GO_0043518 (EC: IDA, PMID: 17045821); GO_0044281 (EC: TAS); GO_0044344 (EC: IDA, PMID: 19577615); GO_0050731 (EC: IDA, PMID: 17045821); GO_0050900 (EC: TAS); GO_0051216 (EC: IEP, PMID: 11944887); GO_0060333 (EC: TAS); GO_0060442 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19199708); GO_0070374 (EC: IDA, PMID: 17045821); GO_0070487 (EC: IMP, PMID: 15100360); GO_1900625 (EC: IMP); GO_1902166 (EC: IDA, PMID: 17045821) PMID: 1281868; 1465456; 1496383; 1537855; 1694723; 1717145; 1730778; 1734871; 1840487; 1922057; 1991450; 2007624; 2056274; 2454887; 2466575; 2466576; 2471973; 2474557; 7499241; 7505012; 7508842; 7516819; 7529574; 7532176; 7539755; 7542116; 7557500; 7591309; 7699015; 7821789; 7908632; 8148709; 8343954; 8352881; 8576267; 8599448; 8636151; 8640758; 8649806; 8858161; 8871928; 8986622; 9058761; 9334256; 9472040; 9519902; 9573028; 9580567; 9794764; 10636882; 10652271; 10657301; 10737800; 10933060; 10950950; 11084024; 11095749; 11129651; 11207560; 11381077; 11402070; 11463356; 11466334; 11606575; 11716065; 11727257; 11740562; 11759056; 11792412; 11825873; 11825898; 11839564; 11840273; 11935029; 11944887; 12032545; 12090473; 12093135; 12127836; 12145196; 12145287; 12168806; 12183053; 12198147; 12223485; 12226094; 12235127; 12297287; 12356905; 12370738; 12371152; 12377945; 12392323; 12393872; 12407110; 12411303; 12421945; 12439723; 12444143; 12452061; 12477932; 12479099; 12485845; 12506143; 12508241; 12511569; 12511867; 12574156; 12629514; 12635659; 12650924; 12702150; 12711360; 12714503; 12727228; 12730955; 12748184; 12767055; 12779084; 12801931; 12820426; 12826680; 12842543; 12883358; 12893366; 12901833; 12908752; 12909589; 12911725; 12928429; 12939665; 12949055; 14504094; 14525786; 14534711; 14534719; 14614016; 14623895; 14644158; 14669354; 14702039; 14981907; 14992719; 15009704; 15013310; 15017146; 15023889; 15040016; 15048167; 15051494; 15060082; 15070674; 15100360; 15123640; 15239258; 15292257; 15313120; 15361838; 15452148; 15489334; 15509527; 15516973; 15531362; 15558018; 15578568; 15638368; 15638386; 15641486; 15645378; 15652352; 15655247; 15688033; 15728517; 15736104; 15783086; 15809746; 15816636; 15851553; 15867228; 15923644; 15943035; 15962382; 15990174; 16002044; 16085055; 16166750; 16177123; 16208414; 16219515; 16229685; 16234326; 16248506; 16311123; 16325770; 16335952; 16352650; 16354706; 16390331; 16407205; 16415175; 16419149; 16478744; 16494036; 16504370; 16530165; 16533775; 16554035; 16565089; 16565092; 16620830; 16636662; 16652145; 16702221; 16713680; 16809345; 16809613; 16848180; 16868940; 16969488; 16998483; 16998484; 17045821; 17081983; 17085435; 17092940; 17135256; 17136494; 17170110; 17237445; 17265493; 17324121; 17332338; 17343740; 17381240; 17383158; 17392272; 17464868; 17479111; 17482182; 17516109; 17540049; 17579117; 17581168; 17589956; 17599831; 17611661; 17611662; 17627000; 17638891; 17657222; 17679465; 17702746; 17708612; 17726647; 17846873; 17849363; 17891137; 17911438; 17914409; 17919613; 17940137; 17945212; 17945213; 17975002; 17987038; 18005092; 18029348; 18048043; 18077444; 18092951; 18094716; 18155656; 18160820; 18162778; 18193058; 18199543; 18214619; 18227732; 18234849; 18246799; 18265895; 18276068; 18279620; 18326820; 18350162; 18372518; 18375392; 18387829; 18396641; 18414895; 18415803; 18438684; 18441325; 18450428; 18450824; 18476625; 18476632; 18495204; 18502033; 18502153; 18513329; 18516325; 18559090; 18577517; 18608209; 18612220; 18614011; 18632604; 18644869; 18651220; 18654930; 18662989; 18753140; 18757307; 18787423; 18804101; 18804988; 18835619; 18852874; 18952835; 18971959; 18980968; 18981124; 18997126; 19004834; 19009655; 19010227; 19017033; 19017937; 19023892; 19047049; 19073595; 19077409; 19088176; 19097357; 19100415; 19141242; 19148550; 19167378; 19176383; 19199708; 19200980; 19243022; 19254252; 19275586; 19277703; 19322201; 19331807; 19350388; 19351367; 19360323; 19385591; 19396460; 19415765; 19416960; 19432801; 19434087; 19488035; 19506034; 19563418; 19577615; 19580891; 19582779; 19598259; 19621595; 19626493; 19633292; 19635906; 19638429; 19698232; 19703720; 19724852; 19764564; 19773544; 19787202; 19787231; 19794081; 19794958; 19794964; 19799609; 19816074; 19826051; 19857547; 19906290; 19912362; 19913121; 19914206; 19937401; 19952968; 19955840; 19965872; 19996285; 20019840; 20042890; 20083228; 20093404; 20093489; 20098615; 20121756; 20127679; 20142144; 20157733; 20178130; 20193563; 20199686; 20200161; 20211062; 20212041; 20228222; 20237496; 20306693; 20357818; 20361869; 20374021; 20382854; 20403620; 20405247; 20416163; 20454640; 20491779; 20525896; 20526812; 20530438; 20552237; 20562647; 20588206; 20605145; 20606680; 20606732; 20628086; 20628624; 20663864; 20663884; 20670691; 20696077; 20698358; 20799279; 20806065; 20809185; 20819778; 20837694; 20843027; 20851866; 20856229; 20920234; 20956971; 20962267; 20969572; 20971508; 20974992; 21055388; 21078678; 21087933; 21098716; 21105049; 21124918; 21136024; 21139048; 21151997; 21179550; 21194677; 21215700; 21254647; 21257828; 21257905; 21258793; 21278261; 21279958; 21294926; 21299347; 21331451; 21356346; 21374592; 21376257; 21393860; 21397861; 21411116; 21424816; 21454519; 21471214; 21471434; 21473743; 21482826; 21489997; 21493336; 21546273; 21570715; 21617876; 21618131; 21618132; 21630198; 21632186; 21633165; 21645921; 21649540; 21668410; 21678082; 21680714; 21685938; 21694464; 21701559; 21708929; 21718681; 21731740; 21743962; 21749678; 21764578; 21768115; 21768350; 21802218; 21804359; 21813394; 21819617; 21824412; 21827751; 21829201; 21830016; 21833756; 21835433; 21849440; 21895545; 21898409; 21906983; 21912471; 21933023; 21935375; 21935404; 21953074; 21957977; 21963094; 21987572; 21993315; 22014860; 22021370; 22024057; 22048598; 22068886; 22069487; 22072421; 22076958; 22119814; 22119938; 22125838; 22130902; 22135720; 22152097; 22205660; 22213301; 22216242; 22218639; 22234250; 22237177; 22242150; 22266115; 22270319; 22271686; 22272243; 22278305; 22293754; 22304920; 22307465; 22321833; 22322379; 22335271; 22363471; 22386367; 22389315; 22429811; 22433859; 22437554; 22449225; 22456539; 22473523; 22491449; 22493711; 22499789; 22514625; 22525501; 22552294; 22552741; 22559040; 22561518; 22610405; 22610780; 22621373; 22637644; 22654106; 22673507; 22673910; 22706704; 22711991; 22726066; 22733437; 22740085; 22740326; 22753277; 22770970; 22784357; 22804494; 22807608; 22836803; 22839505; 22842095; 22843930; 22847005; 22855175; 22863883; 22865879; 22870202; 22895075; 22901285; 22922740; 22923071; 22923171; 22932199; 22939629; 22947857; 22966907; 22967445; 22969228; 22972620; 23000965; 23002207; 23028444; 23031255; 23039365; 23049743; 23056168; 23071680; 23089492; 23098472; 23112116; 23118219; 23138176; 23143465; 23151220; 23160198; 23170789; 23171677; 23182705; 23220849; 23221384; 23226410; 23238743; 23251004; 23252868; 23263849; 23265944; 23273568; 23326564; 23334333; 23342032; 23373240; 23400010; 23404221; 23419168; 23422486; 23426175; 23435135; 23444222; 23445749; 23449937; 23457460; 23476138; 23547049; 23549458; 23565227; 23589287; 23589310; 23600676; 23603511; 23609373; 23633482; 23645762; 23664487; 23667174; 23679813; 23685894; 23736812; 23744486; 23764310; 23768762; 23778530; 23797812; 23800986; 23848514; 23856463; 23883608; 23884413; 23888049; 23940692; 24005673; 24064218; 24084461; 24091662; 24099991; 24194636; 24333422; 24434386 CD44 molecule (Indian blood group) Ensembl:ENSG00000026508 HGNC:1681 HPRD:00115 MIM:107269 Vega:OTTHUMG00000044388 Other designations: CD44 antigen|GP90 lymphocyte homing/adhesion receptor|Hermes antigen|cell surface glycoprotein CD44|chondroitin sulfate proteoglycan 8|epican|extracellular matrix receptor III|hematopoietic cell E- and L-selectin ligand|heparan sulfate proteoglycan|homing function and Indian blood group system|hyaluronate receptor|phagocytic glycoprotein 1 CD44 OGG:3000000983 Bin Zhao, Yue Liu, Oliver He CDC2 CDC28A P34CDC2 WEB: http://www.ncbi.nlm.nih.gov/gene CDK1 cyclin-dependent kinase 1 983 10q21.1 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0000082 (EC: TAS); GO_0000083 (EC: TAS); GO_0000086 (EC: TAS); GO_0000165 (EC: TAS); GO_0000186 (EC: TAS); GO_0000187 (EC: TAS); GO_0000226 (EC: TAS); GO_0000278 (EC: TAS); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0004672 (EC: NAS, PMID: 9001210); GO_0004674 (EC: IDA, PMID: 19879842); GO_0004693 (EC: IDA, PMID: 11069302); GO_0004693 (EC: TAS); GO_0005515 (EC: IPI, PMID: 10373560); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005737 (EC: IDA); GO_0005739 (EC: TAS, PMID: 19917720); GO_0005815 (EC: IEA); GO_0005829 (EC: TAS); GO_0005876 (EC: IDA, PMID: 11069302); GO_0006260 (EC: TAS); GO_0006281 (EC: TAS); GO_0006461 (EC: IEA); GO_0006915 (EC: IEA); GO_0007067 (EC: IEA); GO_0007077 (EC: TAS); GO_0007095 (EC: IEA); GO_0007098 (EC: TAS, PMID: 19364923); GO_0007173 (EC: TAS); GO_0007264 (EC: TAS); GO_0007265 (EC: TAS); GO_0007344 (EC: TAS); GO_0007411 (EC: TAS); GO_0007569 (EC: IEA); GO_0008286 (EC: TAS); GO_0008353 (EC: IDA, PMID: 12721286); GO_0008543 (EC: TAS); GO_0009636 (EC: IEA); GO_0010628 (EC: IEA); GO_0014038 (EC: TAS, PMID: 17200138); GO_0014070 (EC: IEA); GO_0014075 (EC: IEA); GO_0014823 (EC: IEA); GO_0016477 (EC: TAS, PMID: 17200138); GO_0018105 (EC: IDA, PMID: 19879842); GO_0030261 (EC: IEA); GO_0030332 (EC: IEA); GO_0030496 (EC: IDA, PMID: 11069302); GO_0030544 (EC: IEA); GO_0030855 (EC: IEP); GO_0031100 (EC: IEA); GO_0031145 (EC: TAS); GO_0033160 (EC: IEA); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0034501 (EC: IDA, PMID: 18195732); GO_0035173 (EC: IEA); GO_0035666 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042493 (EC: IEA); GO_0043066 (EC: IDA, PMID: 11069302); GO_0045087 (EC: TAS); GO_0045471 (EC: IEA); GO_0045740 (EC: IEA); GO_0045931 (EC: IEA); GO_0045995 (EC: TAS); GO_0046686 (EC: IEA); GO_0046688 (EC: IEA); GO_0048011 (EC: TAS); GO_0048678 (EC: IEA); GO_0051403 (EC: TAS); GO_0051437 (EC: TAS); GO_0051439 (EC: TAS); GO_0055015 (EC: IEA); GO_0060045 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0070301 (EC: IEA) PMID: 914146; 1310466; 1318195; 1384126; 1388288; 1400350; 1406653; 1425574; 1628647; 1717476; 1748630; 1756735; 1828290; 1916766; 1939057; 2013279; 2183353; 2227411; 2344612; 2473839; 2538242; 2541912; 2570636; 2686978; 3289755; 3553962; 7474080; 7474100; 7494303; 7499230; 7578274; 7590285; 7592773; 7635160; 7666531; 7673335; 7716549; 7724583; 7737117; 7769006; 7790358; 7799941; 7822264; 7876309; 7902715; 7903056; 7925482; 7944411; 7949095; 7969176; 7983050; 8034666; 8051108; 8051175; 8070405; 8084605; 8087847; 8119945; 8125092; 8127873; 8242750; 8325880; 8376365; 8397206; 8397207; 8404858; 8423786; 8428596; 8440392; 8463339; 8475101; 8491187; 8524869; 8548803; 8565853; 8626512; 8626527; 8631817; 8652557; 8662825; 8663071; 8672508; 8806671; 8910336; 9001210; 9053846; 9069267; 9094673; 9109675; 9126608; 9130708; 9141461; 9188632; 9199321; 9235942; 9242535; 9244350; 9247342; 9258347; 9268380; 9271440; 9295339; 9315091; 9315635; 9398320; 9467962; 9515786; 9520381; 9524113; 9525956; 9560267; 9575153; 9585407; 9600099; 9614189; 9668078; 9725910; 9733650; 9753325; 9774639; 9885575; 9891079; 9926943; 9988268; 9990288; 10077596; 10339564; 10359664; 10362260; 10373560; 10383391; 10395539; 10403367; 10497277; 10502411; 10504341; 10524633; 10564259; 10602502; 10636877; 10656688; 10712923; 10716937; 10747892; 10764745; 10766737; 10767298; 10769027; 10793135; 10825186; 10864927; 10884347; 10924145; 10938080; 10958988; 10973963; 11034995; 11069302; 11076863; 11076968; 11113134; 11113184; 11135364; 11136719; 11259605; 11278541; 11278991; 11285280; 11310559; 11326318; 11327730; 11331587; 11395479; 11444800; 11470801; 11504921; 11516829; 11520933; 11531413; 11549262; 11559705; 11574543; 11584018; 11598127; 11683421; 11687586; 11774038; 11779217; 11782384; 11836499; 11861764; 11878934; 11895447; 11901153; 11953320; 11980914; 11986303; 12058066; 12077309; 12107172; 12124778; 12145207; 12151413; 12177195; 12186947; 12190313; 12200623; 12221128; 12361598; 12372621; 12397081; 12407107; 12411508; 12450396; 12468530; 12477932; 12525641; 12551973; 12556484; 12569090; 12569365; 12586835; 12604359; 12612056; 12612082; 12613668; 12648761; 12676926; 12721286; 12742823; 12771130; 12775724; 12791267; 12810701; 12832492; 12839990; 12852856; 12853968; 12881709; 12884029; 12912980; 14499622; 14551205; 14635192; 14645578; 14654553; 14697231; 14993212; 15014043; 15016823; 15024056; 15030318; 15050687; 15070733; 15073847; 15082718; 15125835; 15142377; 15145941; 15147269; 15175024; 15181148; 15215233; 15265780; 15276183; 15311285; 15317660; 15345747; 15367677; 15368451; 15474478; 15489334; 15489336; 15525513; 15525677; 15531913; 15541388; 15578977; 15582998; 15591787; 15592455; 15604258; 15635413; 15662526; 15674323; 15678101; 15725353; 15735702; 15735705; 15767402; 15780175; 15782160; 15790566; 15800651; 15817944; 15888452; 15951569; 15989971; 16009130; 16036217; 16109376; 16118207; 16142332; 16159883; 16192727; 16196087; 16198290; 16205633; 16226712; 16237118; 16247472; 16258277; 16344560; 16354571; 16371510; 16377132; 16381901; 16385451; 16407259; 16427064; 16458891; 16462731; 16465393; 16474839; 16478538; 16519687; 16533053; 16565220; 16629900; 16682949; 16760428; 16784539; 16807237; 16880735; 16880739; 16888198; 16998479; 17011204; 17012222; 17013563; 17043241; 17098733; 17159347; 17171635; 17172867; 17192257; 17200138; 17242184; 17274640; 17327911; 17349584; 17351640; 17359356; 17373700; 17386261; 17419986; 17431037; 17433108; 17466630; 17472438; 17474786; 17488622; 17498878; 17525531; 17540176; 17586317; 17636382; 17679094; 17681274; 17725712; 17906618; 17960875; 18003885; 18025303; 18029348; 18056802; 18069625; 18195732; 18201571; 18230152; 18245089; 18247328; 18271526; 18272572; 18272575; 18329369; 18337751; 18347064; 18356527; 18372919; 18408765; 18434602; 18445273; 18450493; 18457437; 18471975; 18477460; 18480403; 18490441; 18514189; 18550795; 18560763; 18568422; 18593881; 18615582; 18635963; 18655026; 18781797; 18799590; 18950845; 19048596; 19056867; 19061641; 19066288; 19134343; 19158392; 19162005; 19223178; 19275580; 19275583; 19275586; 19275588; 19303298; 19344781; 19364923; 19369249; 19375851; 19454010; 19458171; 19471022; 19473963; 19483727; 19509060; 19615732; 19664338; 19683496; 19687009; 19723060; 19725879; 19737929; 19738201; 19786724; 19789190; 19815027; 19837665; 19879842; 19884882; 19917720; 20062077; 20068230; 20068231; 20126263; 20169205; 20171170; 20181698; 20228808; 20360007; 20360068; 20367638; 20368335; 20368358; 20379221; 20395957; 20404109; 20412769; 20439461; 20444701; 20508983; 20526282; 20581839; 20711190; 20733055; 20739936; 20808790; 20810654; 20890132; 20935635; 20937773; 20956543; 20974803; 20974812; 21041660; 21059642; 21081492; 21081666; 21120602; 21123648; 21131960; 21135039; 21139048; 21148318; 21262764; 21308745; 21319273; 21325631; 21379580; 21406398; 21454540; 21488187; 21489275; 21498573; 21504622; 21522128; 21525341; 21569376; 21659531; 21693764; 21712819; 21743465; 21767532; 21813648; 21840486; 21871177; 21871181; 21875946; 21878504; 21878640; 21887332; 21890473; 21900237; 21900495; 21906983; 21907836; 21918813; 21924351; 21925791; 21951856; 21952639; 21963094; 21987572; 21987589; 21988832; 21998300; 22024133; 22053931; 22071694; 22101338; 22137483; 22158041; 22163316; 22266860; 22268729; 22407595; 22482362; 22496227; 22505724; 22552942; 22580043; 22623428; 22689984; 22718829; 22726437; 22768111; 22784093; 22814604; 22848730; 22863883; 22871736; 22907750; 22939629; 22949227; 22962268; 22965228; 23000965; 23045552; 23264621; 23330000; 23355470; 23383273; 23455152; 23471882; 23518499; 23525902; 23532886; 23543736; 23602568; 23619525; 23667531; 23720738; 23738518; 23775624; 23776131; 23814058; 23824909; 23901111; 23908594; 23921553; 23933584; 23956138; 23958962; 23966160; 23990466; 24101154; 24137814; 24248602; 24250222; 24457600 cyclin-dependent kinase 1 Ensembl:ENSG00000170312 HGNC:1722 HPRD:00302 MIM:116940 Vega:OTTHUMG00000018290 Other designations: cell cycle controller CDC2|cell division control protein 2 homolog|cell division cycle 2, G1 to S and G2 to M|cell division protein kinase 1|p34 protein kinase CDK1 gene OGG:3000000997 Bin Zhao, Yue Liu, Oliver He E2-CDC34 UBC3 UBCH3 UBE2R1 WEB: http://www.ncbi.nlm.nih.gov/gene CDC34 cell division cycle 34 997 19p13.3 9606 19 Official from a nomenclature committee GO_0000082 (EC: NAS, PMID: 8248134); GO_0000209 (EC: IDA); GO_0004842 (EC: IDA, PMID: 10373550); GO_0004842 (EC: NAS, PMID: 8248134); GO_0005515 (EC: IPI, PMID: 10373550); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005634 (EC: NAS, PMID: 8248134); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0006270 (EC: NAS, PMID: 8248134); GO_0006464 (EC: NAS, PMID: 8248134); GO_0016567 (EC: IDA, PMID: 10373550); GO_0016567 (EC: NAS, PMID: 8248134); GO_0043161 (EC: IDA, PMID: 10373550); GO_0043525 (EC: IEA); GO_0043951 (EC: IDA, PMID: 10373550); GO_0070848 (EC: IEA); GO_0070936 (EC: IDA); GO_0090261 (EC: IEA) PMID: 8248134; 8576261; 8939846; 9367342; 9430629; 9710583; 10329681; 10373550; 10385629; 10531035; 10713156; 10748083; 10769200; 10871850; 10918611; 11032804; 11054541; 11245432; 11463388; 11546811; 11566883; 11675391; 11689688; 12037680; 12060736; 12435635; 12477932; 12565873; 12813041; 12840033; 14532120; 14578910; 14645576; 14671314; 14690596; 14980219; 15327770; 15489334; 15611064; 15652359; 16123592; 16210246; 16322693; 16338364; 16472766; 16774918; 16861890; 16874460; 17274640; 17461777; 17597759; 17698585; 17785450; 17965458; 18029348; 18239684; 18458088; 18851830; 18950845; 19073596; 19084516; 19112177; 19123975; 19126550; 19240061; 19256485; 19471022; 19549727; 19581926; 19615732; 19875449; 19933270; 19945379; 20081843; 20160477; 20347421; 20353940; 20378537; 20379614; 20596027; 20638939; 20639865; 20663873; 20864041; 21098119; 21130766; 21139048; 21220517; 21296085; 21841822; 21890473; 21906983; 21963094; 22017877; 22053931; 22069333; 22087249; 22113614; 22145905; 22190037; 22210895; 22286100; 22334663; 22496338; 22669845; 22711876; 22748924; 22863883; 22959436; 23000965; 23250430; 23261596; 23297342; 23465077; 23478441; 23589337; 23604317; 23624912; 23910095; 23972993; 24129577; 24250222 cell division cycle 34 Ensembl:ENSG00000099804 HGNC:1734 HPRD:00306 MIM:116948 Vega:OTTHUMG00000180558 Other designations: cell division cycle 34 homolog|ubiquitin carrier protein|ubiquitin-conjugating enzyme E2 R1|ubiquitin-conjugating enzyme E2-32 KDA complementing|ubiquitin-conjugating enzyme E2-CDC34|ubiquitin-protein ligase R1 CDC34 OGG:3000001026 Bin Zhao, Yue Liu, Oliver He CAP20 CDKN1 CIP1 MDA-6 P21 SDI1 WAF1 p21CIP1 WEB: http://www.ncbi.nlm.nih.gov/gene CDKN1A cyclin-dependent kinase inhibitor 1A (p21, Cip1) 1026 6p21.2 9606 6 Official from a nomenclature committee GO_0000079 (EC: TAS, PMID: 8242751); GO_0000082 (EC: IDA, PMID: 10208428); GO_0000082 (EC: TAS); GO_0000086 (EC: IMP, PMID: 17553787); GO_0000278 (EC: TAS); GO_0000307 (EC: IDA, PMID: 17420273); GO_0004861 (EC: TAS, PMID: 7958916); GO_0005515 (EC: IPI, PMID: 15232106); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005829 (EC: TAS); GO_0006468 (EC: IDA, PMID: 9106657); GO_0006974 (EC: IMP); GO_0006977 (EC: IDA, PMID: 15149599); GO_0006977 (EC: TAS); GO_0007050 (EC: IDA, PMID: 15149599); GO_0007050 (EC: IMP, PMID: 17553787); GO_0007173 (EC: TAS); GO_0007265 (EC: IEP, PMID: 9054499); GO_0008285 (EC: IDA, PMID: 10208428); GO_0008285 (EC: IMP, PMID: 17553787); GO_0008543 (EC: TAS); GO_0009411 (EC: IEA); GO_0009636 (EC: IEA); GO_0010243 (EC: IEA); GO_0010629 (EC: IEA); GO_0019912 (EC: IDA, PMID: 9106657); GO_0030308 (EC: IDA, PMID: 10208428); GO_0030332 (EC: IEA); GO_0030890 (EC: IEA); GO_0031100 (EC: IEA); GO_0031668 (EC: IMP, PMID: 17553787); GO_0032403 (EC: IEA); GO_0033158 (EC: IEA); GO_0038095 (EC: TAS); GO_0042326 (EC: IDA, PMID: 10208428); GO_0042493 (EC: IEA); GO_0042771 (EC: IEA); GO_0043066 (EC: IEA); GO_0043068 (EC: IEA); GO_0043231 (EC: IDA); GO_0045087 (EC: TAS); GO_0045736 (EC: IEA); GO_0045860 (EC: IDA, PMID: 9106657); GO_0046685 (EC: IEA); GO_0046872 (EC: IEA); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0048146 (EC: IMP, PMID: 17420273); GO_0051412 (EC: IEA); GO_0055093 (EC: IEA); GO_0070557 (EC: IDA, PMID: 18794347); GO_0071479 (EC: IMP); GO_0071850 (EC: IEA); GO_0090398 (EC: IMP, PMID: 15149599); GO_0090400 (EC: TAS); GO_0097193 (EC: TAS, PMID: 9660939); GO_2000278 (EC: IEA); GO_2000379 (EC: IMP) PMID: 7478582; 7478594; 7655464; 7698009; 7753561; 7780738; 7911228; 7958916; 8084608; 8101826; 8125163; 8242751; 8242752; 8259214; 8560263; 8622677; 8641969; 8647134; 8657154; 8662825; 8700517; 8756624; 8807325; 8861913; 8861969; 8891332; 8999999; 9054499; 9106657; 9178907; 9190208; 9218599; 9372966; 9380407; 9396813; 9464540; 9465025; 9467962; 9472014; 9515786; 9545252; 9546435; 9632134; 9658399; 9660939; 9705499; 9716181; 9716736; 9736735; 9798959; 9799125; 9811456; 9822382; 9837900; 9840927; 9840943; 9858585; 9858587; 10022118; 10022926; 10208428; 10323868; 10337545; 10455148; 10486249; 10529385; 10581175; 10679299; 10692450; 10698951; 10710306; 10753973; 10764767; 10828884; 10837373; 10848585; 10858286; 10873631; 10874474; 10878006; 10891505; 10912791; 10918595; 10973963; 11022036; 11076863; 11084299; 11132966; 11175348; 11179504; 11231585; 11254741; 11255227; 11302688; 11313979; 11343236; 11350925; 11389691; 11463845; 11477082; 11498536; 11559705; 11642719; 11684722; 11695244; 11700040; 11733969; 11741909; 11748297; 11751405; 11751903; 11756412; 11762751; 11781193; 11809712; 11815410; 11842244; 11860939; 11872638; 11877274; 11877298; 11877436; 11882322; 11893252; 11896572; 11908736; 11911463; 11931757; 11943869; 11953864; 11956602; 11968052; 11989975; 12015083; 12025230; 12036888; 12046058; 12052868; 12054510; 12054572; 12054658; 12055678; 12058028; 12111504; 12123335; 12138103; 12145325; 12151346; 12151347; 12151395; 12168821; 12204872; 12205674; 12354776; 12359245; 12361598; 12370305; 12379120; 12383116; 12384701; 12388558; 12392301; 12393707; 12396717; 12400017; 12407107; 12412576; 12417334; 12417722; 12429910; 12431783; 12431987; 12434183; 12441075; 12457968; 12459877; 12474524; 12477932; 12485998; 12513833; 12517948; 12519780; 12522211; 12527941; 12531694; 12545156; 12573582; 12599217; 12612054; 12642873; 12644083; 12651158; 12665570; 12665584; 12680256; 12681289; 12690110; 12698196; 12699883; 12705898; 12706118; 12716906; 12727210; 12727815; 12748190; 12771291; 12781424; 12782595; 12800980; 12809883; 12810668; 12820963; 12825853; 12839982; 12841870; 12847090; 12853982; 12855666; 12867429; 12884030; 12885947; 12890637; 12897156; 12930830; 12930846; 12931225; 12936910; 12947099; 12949733; 12963997; 12964161; 12970742; 13678583; 14504476; 14572899; 14574404; 14580260; 14592451; 14597617; 14607331; 14607337; 14628083; 14633995; 14637149; 14642618; 14647439; 14677632; 14702288; 14712207; 14715257; 14719078; 14726710; 14738489; 14744793; 14751560; 14759525; 14761977; 14762439; 14764039; 14981901; 15001356; 15003515; 15014036; 15016552; 15024057; 15033443; 15036662; 15059516; 15060836; 15069711; 15081425; 15082782; 15084259; 15094066; 15107488; 15111320; 15122333; 15142382; 15149599; 15161699; 15169570; 15171713; 15173090; 15179054; 15181148; 15184045; 15184659; 15190207; 15201954; 15201979; 15226418; 15232106; 15240512; 15251435; 15286705; 15291355; 15297421; 15302882; 15309711; 15317660; 15321712; 15340083; 15342418; 15347670; 15367606; 15371422; 15371446; 15378017; 15386430; 15389598; 15456784; 15474507; 15475071; 15489334; 15489336; 15492264; 15497017; 15509808; 15510615; 15528212; 15546622; 15555546; 15557281; 15574338; 15576034; 15580267; 15582998; 15592362; 15598783; 15606307; 15609309; 15616584; 15623356; 15645120; 15647383; 15660129; 15664193; 15665589; 15665816; 15671036; 15674334; 15674341; 15690394; 15694358; 15694838; 15695403; 15708847; 15709169; 15710329; 15716956; 15735102; 15736438; 15738655; 15743033; 15743834; 15746092; 15750619; 15752352; 15753078; 15756520; 15763542; 15764647; 15765097; 15767448; 15776189; 15780936; 15780937; 15798220; 15807891; 15817070; 15819981; 15839202; 15840769; 15856024; 15866118; 15878916; 15880444; 15880942; 15890360; 15893728; 15905168; 15936816; 15942645; 15944261; 15960923; 15964852; 15964998; 15965232; 15972853; 15975933; 15989967; 16009130; 16012716; 16014176; 16054204; 16078010; 16080520; 16081043; 16082198; 16082224; 16091736; 16111738; 16122475; 16135801; 16142303; 16142340; 16149052; 16150942; 16169070; 16182613; 16189514; 16191374; 16199872; 16200730; 16214366; 16226712; 16243918; 16248979; 16254341; 16256947; 16262255; 16276353; 16280359; 16283431; 16287849; 16288006; 16289646; 16343435; 16344056; 16344560; 16364249; 16381901; 16394138; 16432835; 16434701; 16464125; 16474839; 16479163; 16480585; 16507767; 16510448; 16514663; 16533812; 16551699; 16554660; 16580634; 16581770; 16616141; 16678112; 16705171; 16712793; 16718778; 16723699; 16735508; 16765349; 16775840; 16777994; 16782892; 16803887; 16804724; 16804901; 16818630; 16831599; 16835890; 16837471; 16867219; 16951143; 16952553; 16953367; 16964243; 16982699; 17008550; 17014852; 17016640; 17050675; 17054950; 17055654; 17059853; 17062672; 17072949; 17074759; 17079232; 17079872; 17080297; 17080554; 17108107; 17109628; 17115032; 17130157; 17158927; 17172426; 17172832; 17188136; 17203174; 17214516; 17239344; 17273559; 17283049; 17284535; 17286201; 17292858; 17293600; 17293864; 17294043; 17300726; 17303651; 17317670; 17325029; 17337084; 17339230; 17351341; 17371838; 17373842; 17388661; 17409409; 17420273; 17431791; 17438369; 17443496; 17448597; 17460193; 17460194; 17465503; 17477906; 17498252; 17502456; 17513615; 17517622; 17536310; 17553787; 17556661; 17560543; 17585201; 17588519; 17592292; 17595776; 17606716; 17611661; 17616661; 17617120; 17619016; 17627285; 17634558; 17638911; 17641414; 17656367; 17662641; 17671089; 17671689; 17671727; 17679094; 17682292; 17684142; 17686574; 17692879; 17700068; 17721438; 17804869; 17855660; 17873065; 17885207; 17894409; 17911387; 17920036; 17925548; 17937105; 17941827; 17952758; 17972508; 18004740; 18024214; 18025091; 18035504; 18046503; 18049450; 18057010; 18067855; 18071305; 18086887; 18097575; 18156402; 18162471; 18162533; 18166158; 18172194; 18174230; 18174243; 18181833; 18202757; 18203777; 18205772; 18212054; 18215742; 18226366; 18230337; 18243530; 18251939; 18263614; 18278446; 18281511; 18281541; 18292944; 18298387; 18316600; 18334933; 18339845; 18348176; 18353898; 18358634; 18361427; 18374497; 18385383; 18385759; 18386236; 18400748; 18413741; 18427550; 18441278; 18451802; 18456456; 18458079; 18459109; 18463164; 18498065; 18507837; 18508827; 18509005; 18546941; 18559599; 18562088; 18563330; 18583941; 18593937; 18619950; 18632985; 18644983; 18655775; 18664350; 18694622; 18698027; 18703516; 18710616; 18713757; 18719376; 18765563; 18766473; 18782865; 18788572; 18790797; 18791688; 18794347; 18794348; 18798266; 18806827; 18818310; 18823025; 18829543; 18842998; 18850004; 18850315; 18852884; 18923142; 18941111; 18948188; 18949380; 18950845; 18979138; 18981726; 19001415; 19002614; 19033664; 19041685; 19058005; 19064572; 19091404; 19096232; 19102934; 19106607; 19122196; 19124506; 19125693; 19129183; 19134409; 19141585; 19159630; 19161984; 19176223; 19176530; 19177004; 19211566; 19211842; 19221506; 19223555; 19224585; 19237173; 19243472; 19249676; 19258477; 19262578; 19263441; 19269967; 19273588; 19275888; 19276188; 19276356; 19305381; 19321391; 19322021; 19322654; 19329556; 19330811; 19332548; 19339270; 19356250; 19364816; 19367277; 19383287; 19384944; 19407849; 19409758; 19435914; 19452712; 19453261; 19458054; 19465901; 19465904; 19481339; 19487575; 19491257; 19491398; 19502805; 19505915; 19513497; 19528229; 19536092; 19536131; 19538940; 19541625; 19550124; 19557639; 19560419; 19572978; 19578553; 19581932; 19609363; 19626602; 19628749; 19629483; 19635457; 19638413; 19643983; 19657064; 19657726; 19664338; 19667069; 19668373; 19670700; 19672706; 19686092; 19686743; 19692168; 19693773; 19704162; 19713748; 19723065; 19723093; 19723627; 19730150; 19732026; 19738611; 19750108; 19773351; 19789190; 19795398; 19798054; 19802676; 19818775; 19819988; 19820361; 19822666; 19840446; 19855935; 19860623; 19895794; 19910837; 19913121; 19914103; 19921577; 19923826; 19931389; 19935879; 19950226; 19955391; 19956635; 19956888; 19958256; 20006705; 20012529; 20018861; 20025780; 20039273; 20054616; 20062013; 20062063; 20067556; 20071335; 20079711; 20084294; 20086099; 20101223; 20102411; 20112071; 20126416; 20127253; 20139077; 20144199; 20154723; 20160708; 20164022; 20169278; 20179200; 20190802; 20190813; 20190815; 20193371; 20203690; 20204299; 20204303; 20211058; 20219912; 20301197; 20302655; 20303835; 20308078; 20331843; 20347598; 20349127; 20350217; 20351180; 20357201; 20363991; 20369488; 20370687; 20383190; 20388787; 20419447; 20428774; 20433229; 20444901; 20452353; 20453000; 20458559; 20466633; 20495378; 20504375; 20508865; 20510020; 20510146; 20524403; 20544840; 20583115; 20587660; 20598695; 20600642; 20605778; 20606006; 20622899; 20628086; 20644561; 20668328; 20701798; 20702488; 20732856; 20803550; 20813048; 20814747; 20818156; 20844987; 20858736; 20878079; 20890119; 20954283; 20955243; 20966541; 20979563; 21040707; 21046779; 21048031; 21054888; 21076409; 21087528; 21088000; 21098705; 21115898; 21124069; 21127431; 21139048; 21148311; 21165952; 21242961; 21245169; 21262772; 21288367; 21292770; 21308745; 21311948; 21325273; 21325288; 21325480; 21336720; 21342417; 21358637; 21368573; 21383005; 21402054; 21415438; 21415862; 21417953; 21419318; 21430453; 21437722; 21439247; 21443127; 21460037; 21475302; 21478095; 21511729; 21515331; 21526487; 21532626; 21546904; 21552210; 21554918; 21559393; 21561680; 21565979; 21567397; 21575583; 21608063; 21616632; 21628527; 21637851; 21637966; 21642427; 21652709; 21666704; 21677879; 21685936; 21704589; 21709715; 21725088; 21726628; 21729169; 21768776; 21769863; 21780161; 21791360; 21804532; 21820300; 21832049; 21858171; 21870644; 21875573; 21877955; 21887277; 21890473; 21900206; 21903579; 21906983; 21907315; 21918011; 21933447; 21933903; 21938741; 21956786; 21963094; 21976111; 21988832; 22001409; 22002313; 22009857; 22032898; 22101335; 22110135; 22117196; 22135025; 22147197; 22160829; 22172947; 22173494; 22190353; 22199295; 22206000; 22211246; 22214381; 22216119; 22217266; 22227369; 22244827; 22249270; 22262409; 22266309; 22277651; 22291954; 22296117; 22311974; 22320961; 22321971; 22371483; 22383522; 22392074; 22401965; 22427654; 22428663; 22446964; 22449259; 22469187; 22490020; 22503977; 22510560; 22511267; 22511763; 22514271; 22521293; 22547059; 22547681; 22555846; 22615960; 22634755; 22650359; 22662213; 22673765; 22675167; 22683204; 22684370; 22698403; 22711822; 22713239; 22732402; 22735451; 22751124; 22771799; 22797886; 22814028; 22814742; 22820403; 22828875; 22858377; 22859066; 22869584; 22956625; 22964432; 22980580; 22988851; 22995373; 22997714; 23000965; 23007394; 23007395; 23013131; 23026136; 23034899; 23037503; 23066038; 23085750; 23085987; 23128396; 23133524; 23146670; 23153928; 23158659; 23159636; 23160381; 23167335; 23167427; 23169665; 23178572; 23184467; 23187802; 23208500; 23210340; 23211592; 23213251; 23215027; 23219618; 23224600; 23231583; 23236067; 23238566; 23253087; 23255119; 23261596; 23261678; 23271730; 23275116; 23292332; 23306062; 23306186; 23318451; 23324739; 23329847; 23333058; 23349794; 23349842; 23359201; 23375502; 23376845; 23382584; 23383273; 23388456; 23399735; 23449391; 23455922; 23457546; 23458879; 23463857; 23536437; 23555284; 23577194; 23582783; 23590292; 23601845; 23602568; 23603558; 23618860; 23639631; 23645206; 23652278; 23665236; 23684928; 23715767; 23737759; 23745637; 23759594; 23780339; 23807750; 23832541; 23832542; 23856463; 23928864; 23949224; 24027428; 24074410; 24076166; 24082141; 24119401; 24123000; 24134839; 24217248; 24225749; 24244542; 24277930; 24291038; 24379070 cyclin-dependent kinase inhibitor 1A (p21, Cip1) Ensembl:ENSG00000124762 HGNC:1784 HPRD:00298 MIM:116899 Vega:OTTHUMG00000014603 Other designations: CDK-interacting protein 1|CDK-interaction protein 1|DNA synthesis inhibitor|cyclin-dependent kinase inhibitor 1|melanoma differentiation associated protein 6|wild-type p53-activated fragment 1 CDKN1A OGG:3000001052 Bin Zhao, Yue Liu, Oliver He C/EBP-delta CELF CRP3 NF-IL6-beta WEB: http://www.ncbi.nlm.nih.gov/gene CEBPD CCAAT/enhancer binding protein (C/EBP), delta 1052 8p11.2-p11.1 9606 8 Official from a nomenclature committee GO_0003700 (EC: IEA); GO_0005634 (EC: IEA); GO_0006366 (EC: TAS, PMID: 8314590); GO_0043565 (EC: IEA) PMID: 1638120; 1741402; 1840554; 1884998; 7594592; 7789168; 8314590; 8946919; 9570146; 11741938; 11851384; 12177065; 12477932; 12524424; 12554732; 12825852; 12857754; 12937035; 15212823; 15389878; 15389879; 15486993; 15588942; 15674331; 15718495; 15901830; 16195339; 16322893; 16397300; 16914534; 16997058; 17098861; 17234736; 17373909; 17562792; 17903252; 17910034; 18370833; 18477566; 18619497; 18660489; 18753137; 19471022; 19800021; 19806320; 19811452; 20385105; 20460359; 20467438; 20805509; 20829351; 20971808; 21072181; 21076392; 21112127; 21612582; 21666710; 21693764; 21980073; 22037769; 23028973; 23575666; 23603433; 23861541; 24128855; 24155666 CCAAT/enhancer binding protein (C/EBP), delta HGNC:1835 HPRD:00297 MIM:116898 Other designations: CCAAT/enhancer-binding protein delta|c/EBP delta|nuclear factor NF-IL6-beta CEBPD OGG:3000001062 Bin Zhao, Yue Liu, Oliver He CENP-E KIF10 PPP1R61 WEB: http://www.ncbi.nlm.nih.gov/gene CENPE centromere protein E, 312kDa 1062 4q24-q25 9606 4 Official from a nomenclature committee GO_0000089 (EC: TAS, PMID: 2022189); GO_0000278 (EC: TAS); GO_0000775 (EC: IDA, PMID: 11084331); GO_0000776 (EC: IDA, PMID: 11682612); GO_0000778 (EC: IEA); GO_0000779 (EC: IDA, PMID: 19465021); GO_0000940 (EC: TAS, Qualifier: colocalizes_with, PMID: 9763420); GO_0003777 (EC: IMP, PMID: 7889940); GO_0005515 (EC: IPI, PMID: 17535814); GO_0005524 (EC: IEA); GO_0005634 (EC: IMP, PMID: 9763420); GO_0005737 (EC: IDA); GO_0005819 (EC: IEA); GO_0005829 (EC: TAS); GO_0005871 (EC: IEA); GO_0005874 (EC: IDA, PMID: 7889940); GO_0007018 (EC: TAS); GO_0007079 (EC: TAS, PMID: 1406971); GO_0007080 (EC: TAS, PMID: 9363944); GO_0007275 (EC: IEA); GO_0007596 (EC: TAS); GO_0008017 (EC: IEA); GO_0008152 (EC: IMP, PMID: 7889940); GO_0015630 (EC: IDA); GO_0019886 (EC: TAS); GO_0043515 (EC: IDA, PMID: 9763420); GO_0045860 (EC: IMP, PMID: 12925705); GO_0051382 (EC: NAS, PMID: 9763420) PMID: 1406971; 2022189; 7851898; 7889940; 9363944; 9391217; 9744883; 9763420; 9914370; 10477750; 10852915; 11084331; 11337467; 11682612; 12686615; 12925705; 12938929; 14684825; 15146197; 15159587; 15181147; 15236970; 15297875; 16144904; 16196087; 16565220; 16682006; 16926026; 17081983; 17268814; 17370265; 17535814; 18029348; 18342609; 18374647; 18460473; 19389623; 19465021; 19525938; 19553660; 19625775; 19723035; 19733075; 19779646; 20021663; 20085233; 20237434; 20332099; 20354862; 20360068; 20691903; 21139048; 21282530; 22110139; 22307330; 22637578; 22801780; 22974711; 23236152; 23314748; 23666240; 23955301 centromere protein E, 312kDa Ensembl:ENSG00000138778 HGNC:1856 HPRD:00316 MIM:117143 Vega:OTTHUMG00000160980 Other designations: Centromere autoantigen E (312kD)|centromere-associated protein E|kinesin family member 10|kinesin-related protein CENPE|protein phosphatase 1, regulatory subunit 61 CENPE OGG:3000001158 Bin Zhao, Yue Liu, Oliver He CKMM M-CK WEB: http://www.ncbi.nlm.nih.gov/gene CKM creatine kinase, muscle 1158 19q13.32 20140408 9606 19 protein-coding Official from a nomenclature committee GO_0004111 (EC: IEA); GO_0005524 (EC: IEA); GO_0005829 (EC: TAS); GO_0006600 (EC: TAS); GO_0034641 (EC: TAS); GO_0044281 (EC: TAS); GO_0046314 (EC: IEA) PMID: 1690725; 2309701; 2331374; 2903158; 2914937; 3031982; 3778496; 7057800; 7805577; 7808454; 8524781; 9748661; 10089465; 10893433; 11922612; 12039490; 12432079; 12477932; 12601813; 12972258; 15057824; 15161933; 15489334; 15504039; 15967462; 16037885; 16079652; 16087811; 16092153; 16120572; 16289162; 16344560; 16373479; 16810680; 16981706; 17000714; 17303563; 17478608; 17885020; 18055044; 18222470; 18801770; 18810980; 18833644; 19039220; 19125286; 19337554; 19422651; 19523464; 19670037; 19913121; 20157874; 20525694; 20536908; 20558199; 20588136; 20588308; 20591515; 20628086; 20634891; 20669347; 20952631; 21139048; 21426302; 21448949; 21456469; 21516340; 21565611; 21706313; 21768101; 21873942; 21931810; 22592287; 23122801; 23274523; 23436474 creatine kinase, muscle Ensembl:ENSG00000104879 HGNC:1994 HPRD:00426 MIM:123310 Vega:OTTHUMG00000181782 CKM OGG:3000001174 Bin Zhao, Yue Liu, Oliver He AP19 CLAPS1 EKV3 MEDNIK SIGMA1A WUGSC:H_DJ0747G18.2 WEB: http://www.ncbi.nlm.nih.gov/gene AP1S1 adaptor-related protein complex 1, sigma 1 subunit 1174 7q22.1 9606 7 Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0005765 (EC: TAS); GO_0005829 (EC: TAS); GO_0005905 (EC: IEA); GO_0006886 (EC: IEA); GO_0006892 (EC: TAS); GO_0006898 (EC: TAS, PMID: 9733768); GO_0008565 (EC: IEA); GO_0009615 (EC: IEP, PMID: 16548883); GO_0016032 (EC: TAS); GO_0019886 (EC: TAS); GO_0030121 (EC: TAS, PMID: 9733768); GO_0030659 (EC: TAS); GO_0032588 (EC: TAS); GO_0050690 (EC: TAS); GO_0061024 (EC: TAS) PMID: 2040623; 7593184; 9653655; 9733768; 9736718; 9811606; 9811611; 9847074; 9882340; 10535737; 10747088; 10966473; 11031247; 11222723; 11252894; 11463741; 11694590; 11707398; 12215646; 12477932; 12486136; 12836198; 12853948; 15469849; 15489334; 15569716; 15681409; 16253302; 16548883; 17353931; 18336259; 18781797; 19057675; 19149577; 19895210; 20594957; 21139048; 21762802; 21906983; 21963094; 21987572; 22103831; 22939629; 23000965; 23423674; 23956138; 24250222 adaptor-related protein complex 1, sigma 1 subunit Ensembl:ENSG00000106367 HGNC:559 HPRD:04635 MIM:603531 Vega:OTTHUMG00000157103 Other designations: AP-1 complex subunit sigma-1A|HA1 19 kDa subunit|adapter-related protein complex 1 sigma-1A subunit|adapter-related protein complex 1 subunit sigma-1A|adaptor protein complex AP-1 subunit sigma-1A|clathrin assembly protein complex 1 sigma-1A small chain|clathrin coat assembly protein AP19|clathrin-associated/assembly/adaptor protein, small 1 (19kD)|erythrokeratodermia variabilis 3 (Kamouraska type)|golgi adaptor HA1/AP1 adaptin sigma-1A subunit|sigma1A subunit of AP-1 clathrin adaptor complex|sigma1A-adaptin AP1S1 OGG:3000001191 Bin Zhao, Yue Liu, Oliver He APO-J APOJ CLI CLU1 CLU2 KUB1 NA1/NA2 SGP-2 SGP2 SP-40 TRPM-2 TRPM2 WEB: http://www.ncbi.nlm.nih.gov/gene CLU clusterin 1191 AAG4 8p21-p12 9606 8 Official from a nomenclature committee GO_0001836 (EC: IC, PMID: 16113678); GO_0002576 (EC: TAS); GO_0005515 (EC: IPI, PMID: 16113678); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 11123922); GO_0005634 (EC: IEA); GO_0005739 (EC: IDA, PMID: 16113678); GO_0005783 (EC: IEA); GO_0005829 (EC: IEA); GO_0006629 (EC: NAS, PMID: 2387851); GO_0006956 (EC: TAS, PMID: 1585460); GO_0006958 (EC: IEA); GO_0007596 (EC: TAS); GO_0009615 (EC: IEP, PMID: 16548883); GO_0016887 (EC: IDA, Qualifier: NOT, PMID: 11123922); GO_0030168 (EC: TAS); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0031093 (EC: TAS); GO_0031625 (EC: IDA); GO_0031966 (EC: IEA); GO_0032436 (EC: IMP); GO_0032463 (EC: IMP, PMID: 16113678); GO_0034366 (EC: IDA, PMID: 16682745); GO_0042583 (EC: IEA); GO_0043065 (EC: IMP); GO_0043691 (EC: TAS, PMID: 16682745); GO_0045087 (EC: IEA); GO_0048471 (EC: IDA); GO_0050821 (EC: IDA, PMID: 11123922); GO_0051092 (EC: IMP); GO_0051787 (EC: IDA, PMID: 11123922); GO_0051787 (EC: IPI, PMID: 19996109); GO_0051788 (EC: IDA, PMID: 19996109); GO_0061077 (EC: IDA, PMID: 11123922); GO_0070062 (EC: IDA, PMID: 19056867); GO_0072562 (EC: IDA); GO_0097193 (EC: IDA); GO_1902230 (EC: IMP, PMID: 16113678); GO_2000060 (EC: IMP); GO_2001244 (EC: IMP) PMID: 1424805; 1491011; 1551440; 1585460; 1903064; 1924317; 1974459; 2185274; 2387851; 2454950; 2601725; 2721499; 2780565; 2780570; 3154963; 3167096; 7615015; 7626703; 7768901; 8181474; 8292612; 8314591; 8328966; 8345200; 8387101; 8555189; 8634259; 8752142; 8759347; 8843912; 8889548; 9228033; 9336835; 9537999; 10066740; 10219089; 10329371; 10694874; 11123922; 11186422; 11570883; 11714447; 11795992; 11813210; 11892985; 11904161; 11906815; 12082621; 12172907; 12176985; 12200037; 12393179; 12427144; 12429802; 12470829; 12477932; 12551933; 12679903; 12754519; 12824284; 12860995; 12867999; 12882985; 14618611; 14630798; 14702039; 14718574; 14760718; 15033782; 15133840; 15146195; 15158456; 15174051; 15247015; 15252304; 15304052; 15342556; 15389725; 15480429; 15489334; 15492264; 15499376; 15538973; 15591223; 15649646; 15689620; 15791650; 15809754; 15883054; 15925890; 15929184; 15955107; 16113678; 16179938; 16263699; 16331665; 16335952; 16421571; 16464517; 16490286; 16548883; 16675913; 16682745; 16709604; 16709934; 16740002; 16775601; 16806233; 16955214; 17043677; 17048076; 17056579; 17080454; 17148459; 17170699; 17203891; 17224269; 17260971; 17322305; 17407782; 17412999; 17420006; 17451556; 17512083; 17534116; 17535098; 17689225; 17855704; 17872975; 17974975; 18079682; 18082619; 18097679; 18239862; 18378577; 18458059; 18514801; 18542050; 18612545; 18624398; 18649357; 18709641; 18712185; 18714397; 18786636; 18806885; 18813793; 18842294; 19056867; 19118032; 19137541; 19165232; 19166932; 19177010; 19182256; 19220628; 19264665; 19289586; 19344414; 19353783; 19357365; 19391138; 19413638; 19446882; 19535339; 19542874; 19651157; 19664600; 19734902; 19734903; 19757199; 19793084; 19814590; 19878569; 19878770; 19878774; 19879420; 19879421; 19879422; 19879423; 19903339; 19903745; 19935703; 19940549; 19996109; 20000738; 20007348; 20009887; 20019877; 20028970; 20057494; 20058210; 20068069; 20096688; 20195357; 20209083; 20353268; 20360068; 20410100; 20460622; 20497247; 20534741; 20554627; 20570404; 20599866; 20603455; 20614220; 20674675; 20697030; 20738160; 20739100; 20842452; 20847305; 20850846; 20855565; 20873220; 20930273; 21042904; 21043527; 21059989; 21135756; 21163940; 21224044; 21240462; 21242307; 21280673; 21300948; 21347408; 21379329; 21397462; 21422520; 21447104; 21460841; 21460853; 21467232; 21467285; 21505792; 21508640; 21525168; 21527247; 21543606; 21567405; 21573492; 21627779; 21630085; 21633299; 21732348; 21761117; 21824521; 21892414; 21899841; 21900379; 21912625; 21953030; 21953454; 21980627; 21987172; 21988832; 21998749; 22012253; 22013110; 22015308; 22016805; 22068036; 22082661; 22122982; 22130675; 22145905; 22159129; 22166956; 22179788; 22232000; 22234156; 22236192; 22248099; 22258514; 22266332; 22268729; 22274961; 22296908; 22391565; 22402018; 22465014; 22506010; 22532874; 22539578; 22545109; 22569264; 22613415; 22617144; 22647452; 22689054; 22701550; 22795969; 22832520; 22863883; 22889670; 22896337; 22902018; 22906254; 22952074; 22975582; 22981431; 22990118; 23010347; 23051594; 23099883; 23174100; 23201481; 23208459; 23209684; 23276503; 23279642; 23411014; 23416242; 23455922; 23457489; 23538443; 23573206; 23589125; 23602568; 23621580; 23650005; 23673647; 23702390; 23769013; 23770713; 23786771; 23956692; 24073260 clusterin Ensembl:ENSG00000120885 HGNC:2095 HPRD:01706 MIM:185430 Vega:OTTHUMG00000102114 Other designations: aging-associated protein 4|apolipoprotein J|complement cytolysis inhibitor|complement lysis inhibitor|complement-associated protein SP-40,40|ku70-binding protein 1|sulfated glycoprotein 2|testosterone-repressed prostate message 2 CLU OGG:3000001230 Bin Zhao, Yue Liu, Oliver He CD191 CKR-1 CKR1 CMKBR1 HM145 MIP1aR SCYAR1 WEB: http://www.ncbi.nlm.nih.gov/gene CCR1 chemokine (C-C motif) receptor 1 1230 3p21 9606 3 GO_0002407 (EC: TAS, PMID:16621978); GO_0004435 (EC: IDA, PMID:10734056); GO_0004950 (EC: IDA, PMID:10660125); GO_0005515 (EC: IPI, PMID:15001559); GO_0005886 (EC: IDA, PMID:10660125); GO_0005886 (EC: IMP, PMID:15001559); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:7505609); GO_0006816 (EC: IDA, PMID:10734056); GO_0006874 (EC: IDA, PMID:10734056); GO_0006887 (EC: IDA, PMID:10734056); GO_0006935 (EC: NAS, PMID:15474493); GO_0006954 (EC: IEA); GO_0006955 (EC: IDA, PMID:10734056); GO_0007155 (EC: TAS, PMID:10910894); GO_0007166 (EC: TAS, PMID:10770925); GO_0007187 (EC: TAS, PMID:7505609); GO_0007204 (EC: IDA, PMID:10734056); GO_0007267 (EC: IDA, PMID:10734056); GO_0008152 (EC: IDA, PMID:10734056); GO_0009611 (EC: TAS, PMID:7505609); GO_0009897 (EC: IDA, PMID:10706735); GO_0010629 (EC: IMP); GO_0016493 (EC: IDA, PMID:10734056); GO_0019221 (EC: NAS, PMID:15474493); GO_0019957 (EC: IPI, PMID:10660125); GO_0030502 (EC: IMP); GO_0035717 (EC: IPI, PMID:10660125); GO_0045672 (EC: IMP); GO_0051928 (EC: IDA, PMID:15764707); GO_0070098 (EC: IDA); GO_0070374 (EC: IMP); GO_0071791 (EC: IPI, PMID:10660125); GO_0090026 (EC: IDA, PMID:18587271) PMID:2834384; 7505609; 7545673; 7594543; 7679328; 7683036; 8011297; 8530354; 8626727; 8631787; 8699119; 9115216; 9143512; 9289016; 9346309; 9558365; 9886417; 10094132; 10202040; 10583963; 10660125; 10702689; 10706735; 10734056; 10770925; 10910894; 11085751; 11110672; 11116158; 11449371; 11470772; 11804551; 11832479; 11920567; 12070001; 12085329; 12270118; 12477932; 12651617; 12763925; 12794150; 14530297; 14595653; 14637022; 14674010; 15001559; 15039444; 15053339; 15103513; 15265234; 15337751; 15474493; 15489334; 15548526; 15764707; 15927850; 15950672; 16182378; 16226254; 16323127; 16621978; 16837468; 16969502; 17135764; 17192849; 17298994; 17336272; 17389578; 17464174; 17558413; 17914560; 18178867; 18240029; 18311140; 18559339; 18577758; 18587271; 18972130; 19017998; 19423540; 19553544; 19603542; 19664396; 19687291; 19693089; 19913121; 20015385; 20056178; 20086017; 20154287; 20190752; 20406964; 20429924; 20438785; 20628086; 20634891; 20802378; 20921899; 21148810; 21942940; 22007486; 22104149; 22650026; 22727097; 22829007; 22842622; 23054685; 23125416; 23217400; 23219091; 23233369; 23276697; 23291587; 24056371 chemokine (C-C motif) receptor 1 Ensembl:ENSG00000163823 HGNC:1602 HPRD:03101 MIM:601159 Vega:OTTHUMG00000133451 Other designations: C-C CKR-1|C-C chemokine receptor type 1|CC-CKR-1|CCR-1|LD78 receptor|MIP-1alpha-R|RANTES receptor|RANTES-R|macrophage inflammatory protein 1-alpha receptor CCR1 OGG:3000001232 Bin Zhao, Yue Liu, Oliver He CC-CKR-3 CD193 CKR3 CMKBR3 WEB: http://www.ncbi.nlm.nih.gov/gene CCR3 chemokine (C-C motif) receptor 3 1232 3p21.3 9606 3 GO_0001938 (EC: IEA); GO_0004950 (EC: TAS, PMID:10415069); GO_0005515 (EC: IPI); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:9302298); GO_0006935 (EC: IEA); GO_0006954 (EC: IEA); GO_0006968 (EC: TAS, PMID:10713092); GO_0007155 (EC: TAS, PMID:10201960); GO_0007188 (EC: TAS, PMID:10201960); GO_0007204 (EC: TAS, PMID:9302298); GO_0016032 (EC: IEA); GO_0016493 (EC: IEA); GO_0045766 (EC: IMP, PMID:19525930); GO_0070098 (EC: TAS, PMID:10415069) PMID:7594543; 7622448; 8609214; 8631813; 8631926; 8642344; 8674119; 8676064; 8884276; 9005985; 9024664; 9143512; 9182688; 9252350; 9289016; 9302298; 9346309; 9359702; 9419219; 9573273; 9636210; 9653051; 9712872; 9736741; 9765440; 9789057; 10094132; 10201960; 10415069; 10488147; 10514402; 10527858; 10590105; 10642580; 10666479; 10713092; 10877489; 10900353; 10975800; 11001881; 11085751; 11110785; 11115360; 11120849; 11149986; 11196669; 11307756; 11396683; 11449371; 11832479; 11920572; 11991282; 11994538; 12023397; 12079287; 12149192; 12218106; 12393570; 12397598; 12477932; 12654630; 12794150; 12884299; 12902471; 14581140; 14647058; 14702039; 14733956; 15053339; 15086398; 15194768; 15219825; 15476879; 15489334; 15507393; 15580493; 15607028; 15807893; 15857508; 15992849; 16081847; 16174786; 16470129; 16631222; 16712896; 16904155; 16920975; 17041228; 17135764; 17146638; 17672867; 17703412; 17845580; 17983872; 18240029; 18244953; 18311140; 18379861; 18577758; 18636124; 18676680; 18805825; 18974840; 19017998; 19028820; 19131662; 19170196; 19218218; 19247692; 19258923; 19414538; 19423540; 19525930; 19526283; 19542083; 19553323; 19559392; 19625176; 19692168; 19693089; 19714638; 19731977; 20022477; 20056178; 20144207; 20190752; 20220260; 20237496; 20306659; 20364559; 20380698; 20406964; 20438785; 20503287; 20505746; 20603037; 20647273; 20659406; 20726325; 20734064; 20921899; 20923436; 21041734; 21077277; 21143381; 21280323; 21406396; 21660963; 21735070; 21917937; 22086059; 22217447; 22702503; 22829007; 22842622; 23017229; 23054685; 23183094; 23251661; 23291587; 23566847; 23636060; 23643185; 23702389; 23742077; 23955446 chemokine (C-C motif) receptor 3 Ensembl:ENSG00000183625 HGNC:1604 HPRD:03167 MIM:601268 Vega:OTTHUMG00000133484 Other designations: C-C CKR-3|C-C chemokine receptor type 3|CC chemokine receptor 3|CCR-3|b-chemokine receptor|eosinophil CC chemokine receptor 3|eosinophil eotaxin receptor CCR3 OGG:3000001233 Bin Zhao, Yue Liu, Oliver He CC-CKR-4 CD194 CKR4 CMKBR4 ChemR13 HGCN:14099 K5-5 WEB: http://www.ncbi.nlm.nih.gov/gene CCR4 chemokine (C-C motif) receptor 4 1233 3p24 9606 3 GO_0001764 (EC: IEA); GO_0002507 (EC: IEA); GO_0004950 (EC: TAS, PMID:7642634); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:7642634); GO_0006935 (EC: IEA); GO_0006954 (EC: IEA); GO_0006955 (EC: IEA); GO_0007204 (EC: TAS, PMID:7642634); GO_0009314 (EC: IEA); GO_0009617 (EC: IEA); GO_0009897 (EC: IEA); GO_0016493 (EC: IEA); GO_0043025 (EC: IEA); GO_0046677 (EC: IEA); GO_0050927 (EC: IEA); GO_0070098 (EC: TAS, PMID:7642634) PMID:7642634; 8573157; 8884276; 9169480; 9430724; 9743322; 9933589; 10036181; 10466728; 10754297; 11196669; 11861261; 12070001; 12270118; 12406880; 12429730; 12456591; 12477932; 12485447; 12778466; 14657875; 15187160; 15202833; 15328188; 15489334; 15569983; 15621800; 15857508; 15955100; 17071491; 17117949; 17546636; 18071306; 18240029; 18577758; 18782672; 19106589; 19239991; 19244125; 19261691; 19374191; 19423540; 19903885; 19913121; 19942450; 20148806; 20164417; 20190752; 20237293; 20237496; 20334681; 20364559; 20406964; 20412707; 20438785; 20628086; 20963786; 21443538; 21525208; 21739422; 22490506; 22842622; 23180648; 23644599; 23731651; 24127572 chemokine (C-C motif) receptor 4 HGNC:1605 HPRD:05324 MIM:604836 Other designations: C-C CKR-4|C-C chemokine receptor type 4|CCR-4|chemokine (C-C) receptor 4 CCR4 OGG:3000001234 Bin Zhao, Yue Liu, Oliver He CC-CKR-5 CCCKR5 CCR-5 CD195 CKR-5 CKR5 CMKBR5 IDDM22 WEB: http://www.ncbi.nlm.nih.gov/gene CCR5 chemokine (C-C motif) receptor 5 (gene/pseudogene) 1234 3p21.31 9606 3 GO_0000165 (EC: IEP, PMID:12032188); GO_0001974 (EC: IEA); GO_0002407 (EC: TAS, PMID:16621978); GO_0003779 (EC: IDA, PMID:12421915); GO_0004435 (EC: TAS, PMID:8663314); GO_0004950 (EC: TAS, PMID:10201901); GO_0005515 (EC: IPI, PMID:12421915); GO_0005737 (EC: TAS, PMID:10415069); GO_0005768 (EC: IDA, PMID:10679098); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:10393923); GO_0006816 (EC: IDA, PMID:8699119); GO_0006935 (EC: TAS, PMID:10741397); GO_0006954 (EC: IEA); GO_0006955 (EC: IEA); GO_0006968 (EC: TAS, PMID:10201901); GO_0007166 (EC: TAS, PMID:8639485); GO_0007186 (EC: IMP, PMID:19523456); GO_0007204 (EC: TAS, PMID:10201901); GO_0007267 (EC: IDA, PMID:10679098); GO_0009897 (EC: IDA, PMID:10679098); GO_0009986 (EC: IDA, PMID:10521508); GO_0014808 (EC: IDA, PMID:19523456); GO_0015026 (EC: TAS, PMID:10469138); GO_0016032 (EC: TAS); GO_0016493 (EC: IDA, PMID:11278962); GO_0016493 (EC: NAS, PMID:8639485); GO_0019722 (EC: IDA, PMID:10679098); GO_0019957 (EC: IPI, PMID:10679098); GO_0023052 (EC: IEP, PMID:12032188); GO_0030260 (EC: TAS); GO_0070098 (EC: IDA, PMID:11278962); GO_0070098 (EC: NAS, PMID:8639485); GO_0070098 (EC: TAS, PMID:10201901); GO_0070723 (EC: IMP, PMID:19523456); GO_0071222 (EC: IEP, PMID:10679098); GO_0071791 (EC: IPI, PMID:8699119); GO_0090026 (EC: IEA) PMID:2183196; 2564392; 2569467; 2834384; 3346208; 3512269; 3960725; 8639485; 8649511; 8649512; 8663314; 8674119; 8699119; 8751444; 8756719; 8805353; 8898753; 8906795; 8906796; 8976200; 8995603; 9020356; 9031325; 9143512; 9184207; 9188565; 9207783; 9256481; 9261346; 9261451; 9289016; 9334377; 9343222; 9353123; 9359654; 9359702; 9362541; 9388201; 9399903; 9420225; 9420238; 9445013; 9446638; 9468473; 9525683; 9576751; 9576954; 9632396; 9636210; 9653051; 9653130; 9765440; 9870313; 9882290; 9882373; 9890944; 9971818; 10029247; 10037796; 10085131; 10089882; 10200301; 10201901; 10229873; 10339592; 10357469; 10364178; 10370370; 10384144; 10393923; 10393974; 10413516; 10415069; 10438703; 10438870; 10446313; 10449282; 10453044; 10465086; 10469138; 10477567; 10477718; 10482561; 10482572; 10487781; 10497246; 10505675; 10521508; 10527688; 10544150; 10555208; 10559284; 10562492; 10574939; 10585143; 10590105; 10590121; 10602038; 10602409; 10606089; 10623731; 10640778; 10644351; 10679098; 10702689; 10725362; 10738970; 10741397; 10751368; 10758170; 10775626; 10801487; 10807185; 10816381; 10820198; 10823934; 10826481; 10872839; 10877489; 10882583; 10888615; 10888639; 10917742; 10938094; 10961858; 10970739; 10985308; 11005830; 11023492; 11023526; 11024154; 11069996; 11072599; 11085751; 11086073; 11115360; 11116158; 11118070; 11125885; 11125899; 11134270; 11141322; 11153675; 11162839; 11175286; 11177400; 11181160; 11188946; 11196681; 11196706; 11238869; 11263244; 11264152; 11264346; 11264367; 11265761; 11274729; 11278567; 11278738; 11278962; 11290759; 11312658; 11313374; 11334429; 11335892; 11336643; 11342415; 11350939; 11354628; 11356952; 11356961; 11356967; 11369664; 11377705; 11385319; 11390601; 11393656; 11397808; 11398114; 11403814; 11413305; 11414813; 11427892; 11429110; 11447384; 11448957; 11449371; 11464139; 11468147; 11470772; 11477473; 11484163; 11485305; 11485615; 11489906; 11500196; 11504955; 11511825; 11517394; 11529558; 11543895; 11559423; 11591716; 11595595; 11596075; 11602715; 11679153; 11679916; 11689632; 11693435; 11694103; 11696224; 11698270; 11698699; 11700073; 11703822; 11709091; 11709782; 11711617; 11727771; 11729511; 11733580; 11734558; 11751947; 11752157; 11756347; 11781692; 11803051; 11809184; 11856781; 11859127; 11860793; 11860823; 11861850; 11861874; 11873082; 11876757; 11877445; 11878912; 11901272; 11920312; 11920324; 11937056; 11958683; 11964548; 11966764; 11966770; 11988632; 11994442; 11994538; 12001056; 12010355; 12023175; 12032188; 12032878; 12036855; 12055576; 12056598; 12065593; 12070001; 12082592; 12085329; 12091904; 12093918; 12131184; 12136242; 12140749; 12163044; 12163614; 12166499; 12169668; 12176010; 12183462; 12200385; 12201365; 12202222; 12215252; 12239139; 12271718; 12355376; 12356205; 12368322; 12377943; 12378793; 12403355; 12403770; 12408990; 12412204; 12413885; 12421915; 12426392; 12426393; 12426633; 12427015; 12429730; 12437612; 12445801; 12447757; 12451219; 12461425; 12462338; 12477875; 12477932; 12490404; 12496074; 12509908; 12514416; 12522035; 12531905; 12532229; 12551992; 12552446; 12555203; 12556692; 12557141; 12571248; 12571520; 12579509; 12584049; 12586555; 12587636; 12599073; 12610055; 12610158; 12612298; 12612937; 12619446; 12634405; 12651900; 12667818; 12680626; 12688247; 12689409; 12692222; 12726730; 12745546; 12751031; 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18692212; 18706447; 18753930; 18763111; 18776933; 18781860; 18786994; 18814951; 18815295; 18820725; 18845960; 18846999; 18855658; 18923649; 18925934; 18928397; 18941536; 18949389; 18952441; 18972295; 18974840; 18977142; 18989363; 18991615; 19005677; 19017985; 19017998; 19018669; 19028820; 19032065; 19037908; 19050382; 19064579; 19064722; 19098363; 19116725; 19124913; 19129082; 19129457; 19131662; 19143484; 19149577; 19155524; 19170196; 19170639; 19172482; 19196047; 19200444; 19201454; 19212663; 19218218; 19225544; 19247692; 19250219; 19258923; 19260142; 19263529; 19289833; 19297481; 19321618; 19334035; 19339951; 19339953; 19357773; 19389855; 19402700; 19420105; 19433914; 19460331; 19474452; 19476483; 19479237; 19479371; 19506371; 19520154; 19523456; 19535121; 19538721; 19553544; 19559392; 19561149; 19578796; 19585516; 19603542; 19625176; 19625411; 19644155; 19644158; 19669591; 19679608; 19680536; 19692168; 19692476; 19692480; 19700905; 19706316; 19722264; 19729379; 19740335; 19744036; 19744740; 19769961; 19811270; 19811439; 19816596; 19841162; 19864932; 19874552; 19886839; 19894308; 19913121; 19917679; 19950235; 19956635; 19958843; 20018238; 20025530; 20025985; 20038229; 20050936; 20053336; 20068218; 20075058; 20087947; 20107582; 20130232; 20153665; 20169157; 20174557; 20182805; 20190752; 20203694; 20206716; 20220260; 20237496; 20331378; 20334567; 20364409; 20377425; 20378664; 20381825; 20411675; 20420684; 20442634; 20442662; 20453841; 20463745; 20465832; 20503287; 20507591; 20518834; 20530467; 20531015; 20536507; 20570309; 20594957; 20598754; 20603037; 20608170; 20628086; 20628649; 20682662; 20710056; 20729133; 20801883; 20811274; 20842205; 20855251; 20856130; 20861743; 20865789; 20875295; 20921899; 20923564; 20932773; 20969781; 21041313; 21068438; 21084992; 21091093; 21118814; 21132346; 21134114; 21148810; 21152581; 21155586; 21156032; 21188555; 21248683; 21258050; 21280323; 21284403; 21288812; 21288824; 21288827; 21295814; 21325401; 21330910; 21345957; 21349294; 21354457; 21356539; 21362450; 21381021; 21388649; 21396623; 21429204; 21454526; 21465943; 21473821; 21513481; 21525208; 21555814; 21569409; 21573951; 21592988; 21602126; 21634220; 21637819; 21647388; 21655330; 21663455; 21667221; 21671175; 21676905; 21680525; 21696586; 21703201; 21709449; 21715437; 21723943; 21731496; 21739422; 21741662; 21744265; 21760891; 21763489; 21775441; 21789236; 21814863; 21819370; 21820915; 21835796; 21846359; 21859712; 21860345; 21878623; 21886032; 21890375; 21926353; 21926633; 21944757; 21984373; 21984929; 21988832; 22011385; 22024519; 22026334; 22028271; 22044225; 22047989; 22050776; 22069466; 22079021; 22083068; 22085486; 22102307; 22103833; 22103834; 22157596; 22175768; 22218121; 22264071; 22265023; 22282138; 22285384; 22286874; 22292949; 22297516; 22313935; 22314435; 22325341; 22342838; 22348061; 22374185; 22380870; 22392992; 22403408; 22404213; 22416573; 22424737; 22479344; 22496149; 22496885; 22506069; 22537745; 22547820; 22554649; 22554651; 22583417; 22612293; 22637726; 22638733; 22657741; 22665517; 22701041; 22727097; 22728273; 22732432; 22787219; 22808111; 22811524; 22815758; 22818666; 22830600; 22852142; 22862553; 22875513; 22893032; 22908191; 22918850; 22924548; 22933279; 22954962; 22957026; 22957692; 22966075; 22988032; 22994752; 23041556; 23057571; 23077246; 23115275; 23152559; 23185351; 23217182; 23217400; 23235831; 23250822; 23289212; 23298254; 23312573; 23355876; 23454776; 23480650; 23490419; 23493400; 23515570; 23588722; 23594959; 23632061; 23632983; 23643185; 23691059; 23696662; 23753295; 23773920; 23852305; 23856897; 23880174; 23888779; 23903010; 23936229; 23954573; 24030490; 24078580; 24090135; 24128342; 24129241; 24405814 chemokine (C-C motif) receptor 5 (gene/pseudogene) Ensembl:ENSG00000160791 HGNC:1606 HPRD:03223 MIM:601373 Vega:OTTHUMG00000133481 Other designations: C-C chemokine receptor type 5|C-C motif chemokine receptor 5 A159A|HIV-1 fusion coreceptor|chemokine receptor CCR5|chemr13 CCR5 OGG:3000001235 Bin Zhao, Yue Liu, Oliver He BN-1 C-C CKR-6 CC-CKR-6 CCR-6 CD196 CKR-L3 CKRL3 CMKBR6 DCR2 DRY6 GPR29 GPRCY4 STRL22 WEB: http://www.ncbi.nlm.nih.gov/gene CCR6 chemokine (C-C motif) receptor 6 1235 6q27 9606 6 GO_0002407 (EC: TAS, PMID:16621978); GO_0004872 (EC: TAS, PMID:9186513); GO_0004950 (EC: TAS, PMID:11001880); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:9186513); GO_0006928 (EC: TAS, PMID:9186513); GO_0006935 (EC: TAS, PMID:11001880); GO_0006955 (EC: TAS, PMID:9223454); GO_0006959 (EC: TAS, PMID:11001880); GO_0006968 (EC: TAS, PMID:10521347); GO_0007165 (EC: TAS, PMID:9186513); GO_0007204 (EC: TAS, PMID:9223454); GO_0016493 (EC: IEA); GO_0045087 (EC: TAS); GO_0070098 (EC: TAS, PMID:11001880) PMID:2834384; 8125298; 8886020; 9070937; 9169459; 9186513; 9223454; 9294137; 9294138; 10521347; 11001880; 11164896; 11714836; 11751947; 11994436; 12067311; 12070001; 12081481; 12149255; 12193700; 12477932; 12514792; 12642342; 14574404; 15483227; 15489334; 15591779; 15701269; 15972662; 16095490; 16215992; 16344560; 16621978; 16622267; 16641550; 17075975; 17133360; 17171755; 17562763; 17615381; 18097022; 18218038; 18240029; 18465142; 18577758; 18587394; 18703490; 19233848; 19249008; 19305396; 19324905; 19423540; 19492413; 19539215; 19760754; 19811428; 20022113; 20023216; 20056178; 20068036; 20194631; 20220766; 20334681; 20379614; 20406964; 20438785; 20439195; 20453841; 20453842; 20459729; 20483750; 20511548; 20526339; 20526340; 20570966; 20634891; 20720211; 20872189; 21072187; 21092675; 21102463; 21228329; 21261017; 21300824; 21398606; 21624121; 21724701; 21763254; 21873313; 21912453; 21935436; 21937703; 21949768; 21984702; 22079021; 22092173; 22269120; 22490506; 22732549; 22796894; 22842622; 22859539; 22926920; 23128233; 23306142; 23599932; 23681234; 23758411; 23765988; 23790181; 23850713; 23935994; 23983073 chemokine (C-C motif) receptor 6 Ensembl:ENSG00000112486 HGNC:1607 HPRD:03498 MIM:601835 Vega:OTTHUMG00000016015 Other designations: C-C chemokine receptor type 6|G protein-coupled receptor 29|G-protein coupled receptor 29|LARC receptor|chemokine (C-C) receptor 6|chemokine receptor-like 3|seven-transmembrane receptor, lymphocyte, 22 CCR6 OGG:3000001236 Bin Zhao, Yue Liu, Oliver He BLR2 CD197 CDw197 CMKBR7 EBI1 WEB: http://www.ncbi.nlm.nih.gov/gene CCR7 chemokine (C-C motif) receptor 7 1236 17q12-q21.2 9606 17 GO_0001768 (EC: IC, PMID:12729902); GO_0001954 (EC: IC, PMID:15569314); GO_0002407 (EC: IC, PMID:15778365); GO_0002408 (EC: IC, PMID:14592837); GO_0002606 (EC: ISS); GO_0002885 (EC: ISS); GO_0002922 (EC: ISS); GO_0004930 (EC: TAS, PMID:16621978); GO_0005622 (EC: IDA); GO_0005886 (EC: IDA); GO_0005886 (EC: TAS); GO_0006954 (EC: NAS, PMID:14592837); GO_0006955 (EC: IEA); GO_0007186 (EC: TAS, PMID:16621978); GO_0007204 (EC: TAS, PMID:9153236); GO_0009897 (EC: IEA); GO_0016021 (EC: IEA); GO_0016493 (EC: ISS); GO_0030838 (EC: IC, PMID:11242036); GO_0031274 (EC: IC, PMID:11242036); GO_0031529 (EC: IC, PMID:15569314); GO_0032496 (EC: IEA); GO_0032649 (EC: ISS); GO_0032735 (EC: ISS); GO_0032862 (EC: IC, PMID:15778365); GO_0034695 (EC: IC, PMID:14592837); GO_0035757 (EC: IPI, PMID:9507024); GO_0035758 (EC: IPI, PMID:9507024); GO_0038115 (EC: IDA, PMID:9507024); GO_0038116 (EC: IDA, PMID:9507024); GO_0038117 (EC: IDA, PMID:9507024); GO_0038121 (EC: IDA, PMID:9507024); GO_0043123 (EC: IC, PMID:15059845); GO_0043552 (EC: IC, PMID:15059845); GO_0045060 (EC: IEA); GO_0045785 (EC: IC, PMID:15569314); GO_0045860 (EC: IC, PMID:14592837); GO_0046330 (EC: IC, PMID:15778365); GO_0050706 (EC: ISS); GO_0050862 (EC: IEA); GO_0051209 (EC: IC, PMID:14592837); GO_0051491 (EC: IC, PMID:15569314); GO_0051897 (EC: IC, PMID:15059845); GO_0070098 (EC: ISS); GO_0070374 (EC: IC, PMID:12729902); GO_0071731 (EC: IC, PMID:16249377); GO_0072610 (EC: ISS); GO_0090023 (EC: IDA); GO_0097022 (EC: TAS, PMID:18379575); GO_0097029 (EC: ISS); GO_2000107 (EC: IC, PMID:15059845); GO_2000147 (EC: IC, PMID:15778365); GO_2000510 (EC: ISS); GO_2000522 (EC: ISS); GO_2000525 (EC: ISS); GO_2000526 (EC: ISS); GO_2000547 (EC: ISS) PMID:2834384; 7488016; 7851893; 8383238; 8889548; 9153236; 9507024; 9585422; 9725259; 9743376; 10607681; 10706668; 10741397; 10861057; 11145663; 11242036; 11359797; 11507220; 11830455; 11861876; 11929789; 11970971; 12023337; 12070001; 12149218; 12477932; 12486098; 12642342; 12673677; 12729902; 12799021; 12851649; 14592837; 14990723; 15034011; 15040017; 15059845; 15073111; 15122702; 15247147; 15265234; 15284247; 15304089; 15489334; 15569314; 15674360; 15743472; 15753377; 15778365; 15867478; 15950936; 15972662; 16115904; 16223574; 16225771; 16249377; 16272303; 16278001; 16278374; 16278415; 16344560; 16494043; 16500130; 16621978; 16690519; 16786131; 16802356; 16857986; 16887149; 17006331; 17032700; 17178876; 17192395; 17431094; 17440035; 17587445; 17687340; 17890452; 18065728; 18166500; 18235009; 18240029; 18310327; 18319253; 18379575; 18437055; 18497951; 18544997; 18577758; 18623114; 18664492; 18696160; 18802075; 19068542; 19074885; 19087620; 19136936; 19196101; 19287948; 19423540; 19513547; 19536265; 19536742; 19540558; 19585516; 19615795; 19731977; 19749090; 19862774; 20029460; 20036791; 20056178; 20150960; 20237496; 20406964; 20438785; 20439195; 20651394; 20811680; 20855251; 20889506; 20889923; 21048031; 21071608; 21081040; 21092675; 21165563; 21165582; 21261017; 21347514; 21464944; 21548969; 21624121; 21680174; 21698152; 21731495; 21735098; 21739164; 21739671; 21953548; 22020953; 22043010; 22158872; 22163030; 22221265; 22251626; 22334704; 22350183; 22438908; 22498742; 22533989; 22619482; 22634622; 22659045; 22718198; 22797918; 22821963; 22842622; 22923218; 22990666; 23028633; 23290307; 23363813; 23449735; 23469143; 23498789; 23519840; 23747721; 23888080; 23922113; 24052640; 24136650; 24138884; 24311382 chemokine (C-C motif) receptor 7 Ensembl:ENSG00000126353 HGNC:1608 HPRD:02588 MIM:600242 Vega:OTTHUMG00000133375 Other designations: C-C CKR-7|C-C chemokine receptor type 7|CC chemokine receptor 7|CC-CKR-7|CCR-7|EBV-induced G protein-coupled receptor 1|EBV-induced G-protein coupled receptor 1|Epstein-Barr virus induced G-protein coupled receptor|Epstein-Barr virus induced gene 1|MIP-3 beta receptor|chemokine (C-C) receptor 7|epstein-Barr virus-induced G-protein coupled receptor 1|lymphocyte-specific G protein-coupled peptide receptor CCR7 OGG:3000001237 Bin Zhao, Yue Liu, Oliver He CC-CKR-8 CCR-8 CDw198 CKRL1 CMKBR8 CMKBRL2 CY6 GPRCY6 TER1 WEB: http://www.ncbi.nlm.nih.gov/gene CCR8 chemokine (C-C motif) receptor 8 1237 3p22 9606 3 GO_0004950 (EC: TAS, PMID:9417093); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:8816377); GO_0006935 (EC: IEA); GO_0006955 (EC: IEA); GO_0007155 (EC: TAS, PMID:10910894); GO_0007186 (EC: TAS, PMID:8816377); GO_0007204 (EC: IEA); GO_0015026 (EC: TAS, PMID:9417093); GO_0016493 (EC: IEA); GO_0070098 (EC: TAS, PMID:9417093) PMID:8816377; 8886020; 8977299; 9207005; 9211859; 9417093; 9469461; 9480837; 9521068; 9670926; 10469138; 10540332; 10888633; 10910894; 11007922; 11804551; 12163566; 12477932; 12525579; 12547701; 12551893; 12645948; 12832759; 12967681; 14576057; 15053339; 15489334; 15814739; 15992849; 16631222; 17023422; 17082609; 17558413; 17641040; 17693327; 18240029; 18577758; 19074885; 19423540; 20237496; 20406964; 20438785; 20455898; 21976223; 22479563; 22842622; 23043070; 23363815; 23999500 chemokine (C-C motif) receptor 8 Ensembl:ENSG00000179934 HGNC:1609 HPRD:03497 MIM:601834 Vega:OTTHUMG00000131290 Other designations: C-C chemokine receptor type 8|CC chemokine receptor 8|CC chemokine receptor CHEMR1|CC-chemokine receptor chemr1|chemokine (C-C) receptor 8|chemokine (C-C) receptor-like 2|chemokine receptor-like 1 CCR8 OGG:3000001284 Bin Zhao, Yue Liu, Oliver He ICH POREN2 WEB: http://www.ncbi.nlm.nih.gov/gene COL4A2 collagen, type IV, alpha 2 1284 RP11-90L1.2 13q34 9606 13 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0005201 (EC: TAS, PMID: 8317999); GO_0005515 (EC: IPI, PMID: 12011424); GO_0005576 (EC: TAS); GO_0005587 (EC: TAS, PMID: 2846280); GO_0005788 (EC: TAS); GO_0006351 (EC: IEA); GO_0007411 (EC: TAS); GO_0016525 (EC: IDA, PMID: 10625665); GO_0022617 (EC: TAS); GO_0030198 (EC: NAS, PMID: 8317999); GO_0030198 (EC: TAS); GO_0030574 (EC: TAS); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0031012 (EC: ISS, Qualifier: colocalizes_with); GO_0031012 (EC: TAS, Qualifier: colocalizes_with); GO_0043231 (EC: IDA); GO_0071560 (EC: IEA) PMID: 1377218; 1724753; 2211625; 2426947; 2439508; 2844531; 2846280; 3025878; 3089234; 3182844; 3198637; 3345760; 3582677; 3692475; 3997552; 6389236; 6811420; 6988303; 7495302; 7500359; 7827955; 8006028; 8317999; 8995276; 9136074; 9334230; 9409248; 9506531; 9673377; 9878537; 10382266; 10416788; 10625665; 10926178; 11259413; 11683410; 11711546; 11867580; 12011424; 12021518; 12180907; 12477932; 12878203; 15057823; 15146197; 15231748; 15489334; 15522229; 15743801; 16368877; 16712791; 17216253; 17339318; 17554254; 17557121; 18050191; 18706356; 19481338; 19913121; 20067797; 20080650; 20201926; 20452482; 20628086; 20673868; 20805453; 20889312; 21378990; 21527998; 21900206; 21942715; 22144573; 22209246; 22209247; 22268729; 22333902; 23818951 collagen, type IV, alpha 2 Ensembl:ENSG00000134871 HGNC:2203 HPRD:00355 MIM:120090 Vega:OTTHUMG00000017344 Other designations: canstatin|collagen alpha-2(IV) chain COL4A2 OGG:3000001316 Bin Zhao, Yue Liu, Oliver He BCD1 CBA1 COPEB CPBP GBF PAC1 ST12 ZF9 WEB: http://www.ncbi.nlm.nih.gov/gene KLF6 Kruppel-like factor 6 1316 RP11-184A2.1 10p15 9606 10 Official from a nomenclature committee GO_0003677 (EC: IEA); GO_0005634 (EC: TAS, PMID: 9689109); GO_0005737 (EC: IEA); GO_0006351 (EC: IEA); GO_0019221 (EC: IEA); GO_0030183 (EC: NAS, PMID: 9000136); GO_0045893 (EC: TAS, PMID: 9083102); GO_0046872 (EC: IEA) PMID: 8889548; 9000136; 9083102; 9503030; 9685731; 9689109; 10802067; 11752579; 12433697; 12477932; 12508640; 12590140; 12651597; 12651626; 12740910; 12794452; 15057748; 15064720; 15067324; 15131018; 15164054; 15172998; 15247715; 15342556; 15378003; 15486921; 15489334; 15735005; 15824733; 15917248; 15937668; 16044160; 16054710; 16169070; 16189514; 16385451; 16431954; 16500425; 16598737; 16702959; 16778100; 16856969; 16872311; 16972326; 16988269; 17071613; 17113081; 17125911; 17143513; 17207965; 17223258; 17347589; 17347668; 17514651; 17621627; 17636026; 17663506; 17893646; 18053161; 18174288; 18190240; 18250346; 18471523; 18515091; 18521079; 18596922; 18691883; 18719336; 18753303; 18755691; 18822210; 19020536; 19097929; 19101139; 19328586; 19333010; 19435908; 19808645; 19967571; 20014424; 20116377; 20126619; 20237496; 20453000; 20545576; 20660366; 20714872; 20801538; 20844588; 21056892; 21109018; 21154818; 21282102; 21309496; 21443094; 21470678; 21538018; 21799854; 21832049; 21849067; 21906983; 21928351; 21940380; 22095588; 22169644; 22277651; 22486562; 22535637; 22581522; 22653055; 22711891; 22782870; 22855058; 23048070; 23085750; 23219426; 23322324; 23345610; 23353867; 23508266; 23512538; 23831683; 23870195; 24130502 Kruppel-like factor 6 Ensembl:ENSG00000067082 HGNC:2235 HPRD:03632 MIM:602053 Vega:OTTHUMG00000017567 Other designations: B-cell-derived protein 1|GC-rich binding factor|GC-rich sites-binding factor GBF|Krueppel-like factor 6|Kruppel-like zinc finger protein Zf9|core promoter element binding protein|core promoter element-binding protein|proto-oncogene BCD1|protooncogene B-cell derived 1|suppression of tumorigenicity 12 (prostate)|suppressor of tumorigenicity 12 protein|transcription factor Zf9 KLF6 OGG:3000001340 Bin Zhao, Yue Liu, Oliver He COX6B COXG COXVIb1 WEB: http://www.ncbi.nlm.nih.gov/gene COX6B1 cytochrome c oxidase subunit VIb polypeptide 1 (ubiquitous) 1340 19q13.1 9606 19 Official from a nomenclature committee GO_0004129 (EC: NAS, PMID: 2172092); GO_0005739 (EC: IDA); GO_0005743 (EC: TAS); GO_0005758 (EC: IEA); GO_0021762 (EC: IEP); GO_0022904 (EC: TAS); GO_0044237 (EC: TAS); GO_0044281 (EC: TAS); GO_1902600 (EC: NAS, PMID: 2172092) PMID: 1647217; 1650756; 1651883; 2172092; 2537962; 7821789; 11943455; 12477932; 15057824; 15489334; 17353931; 17500595; 17516841; 18029348; 18499082; 19843159; 20877624; 21139048; 21890473; 21906983; 21963094; 22190034; 22419111; 22505724; 22939629; 23000965 cytochrome c oxidase subunit VIb polypeptide 1 (ubiquitous) Ensembl:ENSG00000126267 HGNC:2280 HPRD:00493 MIM:124089 Vega:OTTHUMG00000048112 Other designations: COX VIb-1|cytochrome c oxidase subunit 6B1 COX6B1 OGG:3000001374 Bin Zhao, Yue Liu, Oliver He CPT1-L CPTI L-CPT1 WEB: http://www.ncbi.nlm.nih.gov/gene CPT1A carnitine palmitoyltransferase 1A (liver) 1374 11q13.2 9606 22 Official from a nomenclature committee GO_0004095 (EC: IEA); GO_0005739 (EC: IDA); GO_0005741 (EC: TAS); GO_0006635 (EC: IEA); GO_0006853 (EC: TAS); GO_0016021 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS) PMID: 7892212; 9070836; 9070950; 9691089; 10408760; 11001805; 11095714; 11257506; 11350182; 11441142; 12111367; 12189492; 12464674; 12477932; 14517221; 14711372; 15489334; 15647998; 15669684; 15846373; 16054041; 16246309; 16271724; 16344560; 16697732; 16806233; 17089095; 17445541; 17452323; 18029348; 18253084; 18385088; 18996102; 19181627; 19217814; 19460752; 19913121; 20124555; 20301700; 20562859; 20602615; 20628086; 20638986; 20691246; 20696606; 20843525; 20877624; 20937660; 21139048; 21252943 carnitine palmitoyltransferase 1 Ensembl:ENSG00000110090 HGNC:2328 HPRD:02755 MIM:600528 Vega:OTTHUMG00000167892 CPT1A OGG:3000001376 Bin Zhao, Yue Liu, Oliver He CPT1 CPTASE IIAE4 WEB: http://www.ncbi.nlm.nih.gov/gene CPT2 carnitine palmitoyltransferase 2 1376 1p32 9606 1 Official from a nomenclature committee GO_0004095 (EC: NAS, PMID: 1988962); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005739 (EC: IDA); GO_0005743 (EC: NAS, PMID: 1988962); GO_0005743 (EC: TAS); GO_0006635 (EC: IEA); GO_0006853 (EC: TAS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS) PMID: 1528846; 1961767; 1988962; 2174799; 7711730; 7892212; 7896283; 8086471; 8125298; 8358442; 8499929; 8651281; 9600456; 9758712; 10090476; 10607472; 11001805; 11095714; 11257506; 11477613; 11855939; 11994355; 12408750; 12410208; 12477932; 12707442; 12971426; 14605500; 14615409; 15489334; 15622536; 15642848; 15647998; 15754283; 16054041; 16168441; 16670153; 16671104; 16710414; 16996287; 17179390; 17651973; 17709715; 17936304; 18024217; 18029348; 18306170; 18363739; 18550408; 18645163; 18996102; 19362304; 19762733; 19913121; 20186120; 20301431; 20370797; 20538056; 20602615; 20628086; 20810031; 20877624; 20934285; 20952238; 21277129; 21641254; 21697855; 21913903; 22493507; 23322164; 23475205; 23566841 carnitine palmitoyltransferase 2 Ensembl:ENSG00000157184 HGNC:2330 HPRD:02802 MIM:600650 Vega:OTTHUMG00000008942 Other designations: CPT II|carnitine O-palmitoyltransferase 2, mitochondrial|carnitine palmitoyltransferase II CPT2 OGG:3000001386 Bin Zhao, Yue Liu, Oliver He CRE-BP1 CREB-2 CREB2 HB16 TREB7 WEB: http://www.ncbi.nlm.nih.gov/gene ATF2 activating transcription factor 2 1386 2q32 9606 2 GO_0000980 (EC: IDA, PMID:19861239); GO_0001076 (EC: IC, PMID:19861239); GO_0001077 (EC: IEA); GO_0001102 (EC: IPI, PMID:19861239); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0003151 (EC: IEA); GO_0003682 (EC: IEA); GO_0003700 (EC: IDA, PMID:8798441); GO_0003705 (EC: IC, PMID:19861239); GO_0003713 (EC: TAS, PMID:2529117); GO_0004402 (EC: IDA, PMID:10821277); GO_0005515 (EC: IPI, PMID:10327051); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005741 (EC: IDA); GO_0006325 (EC: TAS); GO_0006355 (EC: IMP); GO_0006357 (EC: IC, PMID:19861239); GO_0006366 (EC: IC, PMID:19861239); GO_0006970 (EC: IDA); GO_0006974 (EC: IDA); GO_0006974 (EC: IMP, PMID:15916964); GO_0008140 (EC: IDA, PMID:19861239); GO_0016573 (EC: IDA, PMID:10821277); GO_0019901 (EC: IPI); GO_0031573 (EC: IMP, PMID:15916964); GO_0032915 (EC: IEA); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035497 (EC: IDA, PMID:19861239); GO_0035666 (EC: TAS); GO_0035861 (EC: IDA, PMID:15916964); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0045087 (EC: TAS); GO_0045444 (EC: IEA); GO_0046872 (EC: IEA); GO_0046982 (EC: IEA); GO_0051090 (EC: TAS); GO_0051091 (EC: IMP, PMID:10821277); GO_0051403 (EC: TAS); GO_0060612 (EC: IEA); GO_1902110 (EC: IMP) PMID:602896; 1641004; 1827203; 1828107; 1833307; 1838349; 2320002; 2521922; 2529117; 7535770; 7737129; 7737130; 7769693; 7774816; 8027667; 8440710; 8628277; 8654373; 8798441; 9030721; 9058782; 9110174; 9139739; 9155018; 9162092; 9207092; 9207191; 9235954; 9399639; 9405416; 9445037; 9488727; 9524124; 9628874; 9659924; 9671405; 9685505; 9748258; 9786917; 9873047; 9920921; 10066798; 10085140; 10207054; 10327051; 10357819; 10393177; 10567391; 10708586; 10821277; 10878576; 10909971; 11231009; 11259586; 11279118; 11302752; 11564156; 11566021; 11713276; 11836564; 11839738; 11932306; 12110590; 12200150; 12244047; 12270648; 12477932; 12592382; 12663670; 12697749; 12761180; 12788955; 12804775; 12805554; 12833146; 12874243; 12958075; 14499342; 14630918; 14678960; 14734562; 14988408; 15105425; 15276183; 15302935; 15304344; 15546613; 15691875; 15692053; 15878807; 15916964; 16049073; 16179804; 16303757; 16344560; 16418168; 16456540; 16511568; 16533805; 16869889; 16896160; 17036053; 17054722; 17081983; 17082618; 17244683; 17254968; 17258390; 17296604; 17337306; 17626013; 17681939; 17869487; 17875713; 18029348; 18077426; 18307971; 18348191; 18396163; 18397884; 18547788; 18671972; 18677098; 18700251; 19082758; 19135240; 19176525; 19184334; 19278424; 19331149; 19453261; 19487697; 19712049; 19822663; 19861239; 19913121; 19923798; 19944700; 20051382; 20068037; 20116378; 20195357; 20211142; 20213747; 20379614; 20398657; 20498639; 20507983; 20581861; 20619956; 20628086; 20675274; 20956942; 21098032; 21203491; 21278380; 21384452; 21444723; 21565167; 21832049; 21858082; 21890473; 21901137; 21988832; 21990224; 22275354; 22304920; 22351776; 22439931; 22685333; 22843696; 23000965; 23589174; 23591579; 23656735; 23661758; 23966864; 24289970 activating transcription factor 2 Ensembl:ENSG00000115966 HGNC:784 HPRD:00443 MIM:123811 Vega:OTTHUMG00000132424 Other designations: activating transcription factor 2 splice variant ATF2-var2|cAMP response element-binding protein CRE-BP1|cAMP responsive element binding protein 2, formerly|cAMP-dependent transcription factor ATF-2|cAMP-responsive element-binding protein 2|cyclic AMP-dependent transcription factor ATF-2|cyclic AMP-responsive element-binding protein 2|histone acetyltransferase ATF2 ATF2 OGG:3000001388 Bin Zhao, Yue Liu, Oliver He CREB-RP CREBL1 G13 WEB: http://www.ncbi.nlm.nih.gov/gene ATF6B activating transcription factor 6 beta 1388 DADB-220I18.4 6p21.3 9606 6 GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID:12445808); GO_0005622 (EC: IDA, PMID:8870652); GO_0005634 (EC: IEA); GO_0005789 (EC: IEA); GO_0006351 (EC: IEA); GO_0006986 (EC: IEA); GO_0007165 (EC: TAS, PMID:8586413); GO_0016021 (EC: IEA); GO_0043565 (EC: IEA) PMID:7686164; 8586413; 8870652; 8923003; 10644760; 11158310; 11163209; 11256944; 12445808; 12477932; 12782636; 14574404; 14656967; 14702039; 14973138; 18029348; 19693772; 19851445; 19913121; 20628086; 21139048; 21693764; 22094256; 23535732; 23577725; 23661758; 23886662; 24250222 activating transcription factor 6 beta Ensembl:ENSG00000213676 HGNC:2349 HPRD:02992 MIM:600984 Vega:OTTHUMG00000031296 Other designations: Creb-related protein|cAMP response element-binding protein-related protein|cAMP responsive element binding protein-like 1|cAMP-dependent transcription factor ATF-6 beta|cAMP-responsive element-binding protein-like 1|cyclic AMP-dependent transcription factor ATF-6 beta|protein G13 ATF6B OGG:3000001401 Bin Zhao, Yue Liu, Oliver He PTX1 WEB: http://www.ncbi.nlm.nih.gov/gene CRP C-reactive protein, pentraxin-related 1401 RP11-419N10.4 1q23.2 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0001666 (EC: IEA); GO_0005515 (EC: IPI, PMID: 17785206); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005615 (EC: IEA); GO_0006953 (EC: TAS, PMID: 2477488); GO_0006954 (EC: TAS, PMID: 10408362); GO_0006958 (EC: IEA); GO_0007568 (EC: IEA); GO_0008228 (EC: TAS, PMID: 2477488); GO_0010288 (EC: IEA); GO_0010745 (EC: IDA, PMID: 18322245); GO_0010888 (EC: IDA, PMID: 18322245); GO_0015485 (EC: IEA); GO_0030169 (EC: IDA, PMID: 18322245); GO_0030175 (EC: IEA); GO_0030426 (EC: IEA); GO_0033265 (EC: TAS, PMID: 2477488); GO_0042060 (EC: IEA); GO_0042803 (EC: IEA); GO_0045471 (EC: IEA); GO_0046872 (EC: IEA); GO_0050830 (EC: TAS, PMID: 2477488); GO_0051258 (EC: IEA); GO_0071277 (EC: IEA); GO_1900006 (EC: IEA) PMID: 265538; 403526; 762075; 1477104; 1989977; 2477447; 2477488; 2997165; 3759147; 3840479; 6427230; 6685157; 6693419; 6857266; 7881902; 8144569; 8482924; 8599761; 8613143; 10368284; 10408362; 10490997; 10675363; 11027634; 11739301; 11801683; 11857055; 11947917; 11964845; 11991668; 12033985; 12037301; 12055255; 12102655; 12104096; 12151853; 12186793; 12198121; 12213988; 12218140; 12234944; 12244213; 12351483; 12390313; 12393563; 12426217; 12426218; 12460042; 12471137; 12477932; 12529491; 12552583; 12563060; 12594844; 12616974; 12618085; 12637157; 12654086; 12663465; 12701054; 12716818; 12783932; 12819031; 12821545; 12835213; 12835218; 12842840; 12850811; 12869354; 12892901; 12934049; 12975260; 14500938; 14506615; 14508181; 14592848; 14634117; 14718574; 14744975; 14967730; 14967837; 14983228; 15044210; 15047644; 15078802; 15136507; 15271790; 15277326; 15286457; 15304023; 15306744; 15308783; 15337754; 15358216; 15380464; 15448085; 15456743; 15469865; 15472120; 15489334; 15517131; 15565375; 15579759; 15585208; 15585211; 15585215; 15585218; 15591095; 15653107; 15692104; 15735209; 15746456; 15766555; 15772777; 15777561; 15778807; 15795363; 15797975; 15798948; 15798966; 15808312; 15853546; 15859024; 15860734; 15866055; 15867284; 15878871; 15887860; 15894122; 15894827; 15897982; 15919817; 15920036; 15920065; 15920074; 15950309; 15955385; 15955391; 15993896; 15996056; 15997206; 16005364; 16005367; 16026589; 16051899; 16061741; 16087790; 16087807; 16109328; 16123325; 16131811; 16148535; 16151032; 16153429; 16170833; 16189249; 16213874; 16221209; 16257408; 16266402; 16306468; 16344720; 16352308; 16380821; 16405882; 16409458; 16417933; 16500582; 16501036; 16511556; 16534007; 16549465; 16550411; 16565153; 16580524; 16582918; 16603696; 16618976; 16643876; 16681424; 16682383; 16685271; 16698114; 16710414; 16719793; 16723442; 16731635; 16733231; 16751408; 16764962; 16765355; 16778366; 16803998; 16809555; 16809564; 16832147; 16832152; 16840032; 16847147; 16854501; 16858645; 16864904; 16879213; 16881737; 16908949; 16916777; 16963054; 16984505; 17003778; 17011566; 17044846; 17079491; 17082472; 17101857; 17110595; 17113035; 17113059; 17114654; 17126343; 17138933; 17141244; 17143564; 17148079; 17149558; 17157301; 17164456; 17185152; 17202380; 17211240; 17219082; 17220790; 17234298; 17261875; 17264952; 17279354; 17289011; 17292342; 17293598; 17325687; 17327459; 17335789; 17335903; 17343862; 17347578; 17350021; 17351284; 17355554; 17355643; 17369452; 17372148; 17380191; 17382928; 17383146; 17395501; 17400881; 17433639; 17449131; 17449922; 17452737; 17456635; 17459567; 17460724; 17477779; 17477815; 17498578; 17499233; 17511977; 17513778; 17519779; 17530289; 17531242; 17561469; 17573060; 17575367; 17581635; 17584642; 17588586; 17596285; 17597836; 17598370; 17600233; 17613401; 17615382; 17623721; 17623828; 17635239; 17641153; 17650829; 17652082; 17652155; 17653654; 17673235; 17676666; 17693973; 17697822; 17700210; 17702862; 17702963; 17706955; 17714716; 17714718; 17722225; 17763921; 17765290; 17785206; 17785926; 17806085; 17827818; 17845537; 17851127; 17851695; 17852082; 17852826; 17873311; 17878721; 17878753; 17880812; 17885262; 17888441; 17891599; 17900590; 17903293; 17909163; 17917609; 17920229; 17925606; 17934713; 17942113; 17943468; 17952446; 17956875; 17957146; 17981284; 17991470; 18000615; 18005189; 18023360; 18036188; 18054331; 18055473; 18055714; 18056120; 18060926; 18063701; 18071779; 18075240; 18078625; 18083122; 18096828; 18165866; 18167554; 18171282; 18172744; 18178503; 18182444; 18200582; 18206145; 18214695; 18216376; 18217154; 18218989; 18219371; 18219765; 18226363; 18226879; 18235049; 18241613; 18245530; 18250134; 18262272; 18263601; 18266777; 18279706; 18280482; 18285551; 18285696; 18288276; 18289549; 18296838; 18297417; 18305316; 18312679; 18316365; 18322245; 18327405; 18328265; 18332893; 18333373; 18344622; 18347271; 18347963; 18356846; 18359028; 18362454; 18365276; 18369665; 18372435; 18373721; 18378435; 18379563; 18383516; 18385179; 18385676; 18385743; 18385816; 18386294; 18388036; 18388037; 18389332; 18393253; 18394761; 18401567; 18403728; 18404970; 18412163; 18413218; 18414778; 18415802; 18418236; 18421029; 18422436; 18425592; 18428198; 18433460; 18436879; 18436884; 18439548; 18439552; 18443549; 18450770; 18458051; 18464913; 18476570; 18486609; 18489822; 18491455; 18493116; 18499652; 18500540; 18505467; 18508060; 18513241; 18513823; 18523031; 18541797; 18551710; 18556380; 18562472; 18566104; 18573122; 18573197; 18573495; 18577830; 18591402; 18605934; 18607165; 18609082; 18609102; 18616717; 18621860; 18622582; 18624398; 18632424; 18636307; 18650775; 18654020; 18654021; 18667998; 18675273; 18676680; 18685607; 18688084; 18695743; 18700811; 18702945; 18704199; 18704713; 18708524; 18710885; 18714381; 18714384; 18753723; 18753952; 18755462; 18757054; 18759279; 18764931; 18784972; 18785307; 18786923; 18790479; 18791482; 18793001; 18801352; 18805107; 18805592; 18810599; 18810717; 18818748; 18823889; 18829218; 18835219; 18836266; 18840622; 18841009; 18842294; 18842390; 18845301; 18852001; 18853099; 18853133; 18924263; 18937150; 18948966; 18952164; 18953261; 18957790; 18971492; 18974842; 18983663; 18996288; 18997194; 19004040; 19008293; 19010993; 19011614; 19019335; 19023151; 19025443; 19026696; 19029268; 19034331; 19040303; 19055599; 19060910; 19067532; 19072030; 19073362; 19074515; 19074985; 19075099; 19076828; 19077177; 19077918; 19078972; 19081678; 19084272; 19095725; 19096002; 19100387; 19101671; 19111610; 19117239; 19118119; 19122170; 19125286; 19128923; 19130414; 19136614; 19136826; 19138871; 19139603; 19139754; 19147740; 19155486; 19160050; 19168253; 19170196; 19170684; 19172699; 19178964; 19179966; 19188531; 19191811; 19193941; 19201044; 19201207; 19202332; 19203753; 19225207; 19228486; 19238141; 19240794; 19244088; 19248087; 19251259; 19252093; 19255512; 19262552; 19267250; 19267370; 19268605; 19268941; 19270348; 19272152; 19276622; 19281089; 19282426; 19282606; 19282863; 19297430; 19297456; 19322079; 19323703; 19328934; 19337791; 19343415; 19351632; 19358836; 19359657; 19360108; 19362308; 19369869; 19375128; 19377212; 19377253; 19387251; 19390179; 19394732; 19403254; 19410251; 19415164; 19415283; 19423540; 19426506; 19428053; 19433520; 19436122; 19436291; 19436676; 19436686; 19437230; 19439300; 19439303; 19461040; 19469014; 19473152; 19480860; 19482283; 19492468; 19494488; 19495883; 19499327; 19501581; 19501644; 19520972; 19521085; 19522741; 19523464; 19525580; 19527514; 19533498; 19534672; 19538326; 19545442; 19560102; 19565490; 19567438; 19568166; 19571581; 19576194; 19577754; 19578796; 19584180; 19594772; 19595394; 19602903; 19609738; 19614793; 19615354; 19617288; 19619902; 19620133; 19624831; 19625176; 19626399; 19631649; 19642908; 19643839; 19643942; 19644070; 19645035; 19667982; 19670170; 19680263; 19692124; 19692168; 19695857; 19706826; 19715516; 19719987; 19719993; 19728551; 19729797; 19736474; 19736479; 19751919; 19755616; 19760027; 19762396; 19762397; 19766699; 19783155; 19796676; 19800416; 19801321; 19806245; 19808368; 19816865; 19816870; 19818961; 19821022; 19833744; 19834334; 19850242; 19850925; 19851048; 19853918; 19855269; 19857655; 19857676; 19864399; 19874580; 19879773; 19900432; 19903811; 19906786; 19913121; 19914996; 19923014; 19929715; 19931932; 19942863; 19944144; 19946607; 19947988; 19948975; 19954777; 19956729; 19962488; 19965533; 20004425; 20005739; 20006362; 20017311; 20024640; 20031768; 20034371; 20036017; 20042240; 20047081; 20056225; 20056955; 20060752; 20068351; 20074254; 20075180; 20075509; 20075574; 20078870; 20078877; 20083961; 20131075; 20136960; 20138378; 20142117; 20145391; 20145925; 20170291; 20173307; 20179497; 20184510; 20184533; 20184536; 20186934; 20190687; 20200626; 20200627; 20211068; 20214668; 20215002; 20219150; 20220110; 20227257; 20227921; 20233980; 20237496; 20306065; 20333461; 20339115; 20339904; 20346360; 20346514; 20348053; 20359087; 20371432; 20386340; 20403997; 20406964; 20423474; 20423919; 20437055; 20438785; 20443669; 20453000; 20453690; 20465852; 20466978; 20485444; 20489166; 20494358; 20494378; 20502295; 20511616; 20522534; 20531240; 20537668; 20538124; 20538278; 20538960; 20539018; 20546810; 20552244; 20556836; 20573938; 20581772; 20587599; 20592333; 20596037; 20596713; 20599197; 20605213; 20610232; 20614004; 20618287; 20623261; 20626020; 20626239; 20626701; 20628086; 20638228; 20640440; 20651278; 20669343; 20670634; 20676960; 20679960; 20680929; 20683147; 20686879; 20690093; 20691829; 20703235; 20704541; 20706769; 20709501; 20722986; 20727736; 20730440; 20733302; 20734449; 20797493; 20805569; 20813565; 20819268; 20836727; 20843812; 20846522; 20846939; 20850446; 20852043; 20855282; 20855565; 20856253; 20874781; 20877716; 20881941; 20883364; 20929576; 20929699; 20930309; 20939118; 20949557; 20952358; 20967757; 20972697; 20974458; 20978825; 20979755; 21029360; 21029457; 21033124; 21034294; 21037097; 21037509; 21043803; 21044752; 21044781; 21054666; 21054877; 21059738; 21062467; 21067752; 21071964; 21080913; 21081932; 21086905; 21089116; 21094359; 21105323; 21108561; 21135979; 21136015; 21143859; 21143879; 21146168; 21149504; 21161711; 21162890; 21167068; 21172733; 21173097; 21173540; 21182750; 21190868; 21194909; 21195701; 21196492; 21203342; 21204606; 21215477; 21218608; 21226995; 21258804; 21270838; 21284020; 21287288; 21293934; 21294915; 21296145; 21296900; 21300955; 21305296; 21309051; 21309632; 21315565; 21323571; 21324310; 21325005; 21325757; 21357282; 21357824; 21360619; 21383176; 21402418; 21404895; 21406102; 21413847; 21414621; 21415385; 21444086; 21447704; 21455669; 21458205; 21465964; 21468168; 21476028; 21493089; 21508123; 21516340; 21519150; 21526633; 21536287; 21546857; 21553357; 21565862; 21570260; 21575917; 21592994; 21602602; 21617097; 21624120; 21625240; 21630214; 21640994; 21645137; 21647738; 21655904; 21658317; 21679689; 21685272; 21696613; 21697747; 21700090; 21714897; 21716910; 21719129; 21720757; 21729568; 21729973; 21730823; 21737650; 21740772; 21741099; 21757662; 21773944; 21794939; 21801245; 21804277; 21814873; 21816845; 21819975; 21821037; 21831326; 21832113; 21839826; 21843630; 21845926; 21856781; 21859817; 21868617; 21872279; 21883780; 21890096; 21901123; 21915265; 21923250; 21928234; 21931794; 21933586; 21934067; 21937998; 21951717; 21958326; 21970447; 21988832; 21993388; 22004660; 22014839; 22018511; 22019947; 22019953; 22025173; 22025360; 22038335; 22048011; 22055258; 22056216; 22079264; 22082888; 22095223; 22103876; 22104116; 22119118; 22134501; 22153152; 22158621; 22166506; 22178353; 22190020; 22192441; 22196954; 22203929; 22205174; 22208681; 22222005; 22241816; 22257305; 22260948; 22267327; 22267750; 22267767; 22277294; 22284830; 22291609; 22296194; 22297435; 22306563; 22311704; 22316266; 22316276; 22328138; 22329434; 22330622; 22357713; 22365588; 22392590; 22418747; 22418989; 22428468; 22430136; 22435454; 22437883; 22444955; 22446726; 22449109; 22457095; 22459389; 22464286; 22467322; 22474034; 22490475; 22492993; 22497530; 22529527; 22533665; 22545649; 22547903; 22552174; 22554299; 22556030; 22558327; 22562290; 22569431; 22569435; 22570140; 22576068; 22580582; 22588996; 22607374; 22614460; 22617158; 22641545; 22642594; 22645408; 22672862; 22676422; 22681496; 22683644; 22685243; 22685586; 22732721; 22748017; 22750226; 22763479; 22780440; 22783580; 22783989; 22796263; 22801596; 22813435; 22813921; 22816656; 22821639; 22828776; 22832641; 22836155; 22843654; 22847196; 22857740; 22867744; 22869540; 22875408; 22875596; 22884413; 22901456; 22906275; 22906998; 22911253; 22912790; 22914173; 22918393; 22939635; 22949303; 22957001; 22976070; 22982460; 22989605; 23013513; 23026925; 23046580; 23049543; 23066418; 23078984; 23087143; 23087294; 23104422; 23111890; 23116190; 23116196; 23124693; 23125484; 23126320; 23132698; 23139417; 23151748; 23158132; 23159256; 23166385; 23170819; 23182717; 23197238; 23197841; 23206444; 23212397; 23212764; 23220502; 23221172; 23224322; 23225486; 23228375; 23241067; 23254637; 23254959; 23257175; 23257395; 23263911; 23266263; 23270673; 23272049; 23274882; 23277135; 23285029; 23288467; 23306163; 23343124; 23361365; 23367494; 23375121; 23375154; 23379491; 23383155; 23393371; 23399387; 23401350; 23409097; 23425215; 23434327; 23440541; 23450030; 23463453; 23468212; 23484158; 23492986; 23516493; 23518675; 23527487; 23535585; 23547018; 23575330; 23576062; 23578742; 23579782; 23591413; 23592000; 23604041; 23618082; 23627410; 23635436; 23674518; 23692330; 23697277; 23702388; 23724031; 23724977; 23742758; 23766379; 23773138; 23784529; 23803251; 23808014; 23813138; 23813850; 23828261; 23835994; 23844046; 23852903; 23888317; 23910616; 23911413; 23935961; 23941472; 23968978; 24055729; 24072695; 24084772; 24097561; 24163955; 24206243; 24222149; 24222151; 24262327; 24347428; 24379064; 24403485; 24434384; 24440351 C-reactive protein, pentraxin-related Ensembl:ENSG00000132693 HGNC:2367 HPRD:00422 MIM:123260 Vega:OTTHUMG00000035344 Other designations: C-reactive protein|pentraxin 1 CRP OGG:3000001437 Bin Zhao, Yue Liu, Oliver He GMCSF WEB: http://www.ncbi.nlm.nih.gov/gene CSF2 colony stimulating factor 2 (granulocyte-macrophage) 1437 5q31.1 20140408 9606 5 protein-coding Official from a nomenclature committee GO_0001892 (EC: IEA); GO_0005125 (EC: IEA); GO_0005129 (EC: IEA); GO_0005515 (EC: IPI, PMID: 18692472); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0006955 (EC: IEA); GO_0008083 (EC: IEA); GO_0008284 (EC: IEA); GO_0010628 (EC: IDA, PMID: 10666185); GO_0010744 (EC: IDA, PMID: 19032770); GO_0032747 (EC: IDA); GO_0042045 (EC: IEA); GO_0042116 (EC: IEA); GO_0042523 (EC: IDA, PMID: 9722506); GO_0043011 (EC: IEA); GO_0045740 (EC: IDA, PMID: 9722506); GO_0045918 (EC: IDA, PMID: 10666185); GO_0071222 (EC: IEA); GO_0071803 (EC: IDA, PMID: 15220135); GO_0097028 (EC: IDA); GO_2001240 (EC: IDA, PMID: 10666185) PMID: 1569568; 1675789; 1702217; 1737041; 1837174; 1918997; 2645577; 2999978; 3083507; 3486413; 3876930; 3898082; 3923623; 3925454; 7642615; 7695626; 7727786; 7818827; 7957082; 8018916; 8278375; 8516290; 8910448; 9162089; 9211889; 9722506; 10477722; 10572088; 10666185; 10734053; 11289721; 11522597; 11763346; 11847009; 11855781; 11880043; 11883735; 11956032; 11963838; 12022701; 12031914; 12050184; 12144536; 12162871; 12171249; 12356579; 12356582; 12397015; 12421569; 12444058; 12477932; 12488507; 12496443; 12538575; 12548211; 12562384; 12565831; 12568301; 12615367; 12629028; 12637324; 12646185; 12663443; 12695562; 12743567; 12744771; 12759409; 12855588; 12926133; 12928384; 12935848; 12954601; 13679820; 14503968; 14512323; 14530365; 14564341; 14567558; 14628073; 14630612; 14662891; 14726527; 14730225; 15009203; 15078892; 15123671; 15129224; 15136573; 15201279; 15218949; 15220135; 15245433; 15269821; 15308671; 15340054; 15358207; 15372022; 15388258; 15388264; 15475489; 15479432; 15481145; 15489334; 15528381; 15541716; 15576295; 15621725; 15927668; 16027123; 16167889; 16211258; 16305336; 16380083; 16487109; 16491014; 16716376; 16783532; 16896315; 16912178; 16949316; 17142110; 17205286; 17273755; 17311927; 17342342; 17355643; 17362254; 17512774; 17533050; 17619839; 17681858; 17703412; 17713553; 17894541; 17914409; 17934321; 17938902; 18027871; 18089573; 18219369; 18254319; 18353856; 18434187; 18439101; 18441098; 18523302; 18676680; 18692472; 18701168; 18755511; 18804273; 18830265; 18926300; 18928604; 18945465; 18971287; 18974369; 18974840; 19028820; 19032770; 19050289; 19131452; 19131662; 19141860; 19158269; 19164476; 19170196; 19222422; 19225544; 19230854; 19247692; 19258923; 19263529; 19282464; 19324950; 19379606; 19453261; 19479237; 19494510; 19559392; 19560459; 19578876; 19625176; 19692168; 19699526; 19730683; 19773451; 19807655; 19913121; 20015396; 20056792; 20078425; 20233331; 20382843; 20452482; 20483917; 20485444; 20503287; 20527084; 20536507; 20603037; 20628086; 20673868; 20802406; 20811626; 20829438; 20956574; 20959405; 21052690; 21071541; 21123547; 21262803; 21324206; 21486701; 21506110; 21705618; 21724805; 21873076; 21931646; 22031867; 22200506; 22430742; 22446963; 22655069; 22698406; 22698407; 22837488; 22911897; 23069312; 23128233; 23520016; 23548906; 23585475; 23600834; 23696637; 24211252; 24275678 colony stimulating factor 2 (granulocyte-macrophage) Ensembl:ENSG00000164400 HGNC:2434 HPRD:00734 MIM:138960 Vega:OTTHUMG00000059637 Other designations: CSF|granulocyte-macrophage colony-stimulating factor|molgramostin|sargramostim CSF2 OGG:3000001440 Bin Zhao, Yue Liu, Oliver He C17orf33 CSF3OS GCSF WEB: http://www.ncbi.nlm.nih.gov/gene CSF3 colony stimulating factor 3 (granulocyte) 1440 17q11.2-q12 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0005125 (EC: IDA); GO_0005125 (EC: NAS, PMID: 15664994); GO_0005130 (EC: TAS, PMID: 2420009); GO_0005615 (EC: IEA); GO_0006955 (EC: IEA); GO_0007275 (EC: TAS, PMID: 2420009); GO_0008083 (EC: IEA); GO_0008284 (EC: IEA); GO_0014068 (EC: IDA); GO_0019221 (EC: NAS, PMID: 15664994); GO_0019899 (EC: IPI, PMID: 12393522); GO_0030838 (EC: IDA); GO_0030851 (EC: NAS, PMID: 15664994); GO_0032092 (EC: IDA); GO_0033138 (EC: IDA); GO_0042993 (EC: IDA); GO_0045944 (EC: IDA); GO_0050731 (EC: IDA); GO_0051897 (EC: IDA); GO_0071222 (EC: IEA); GO_0071345 (EC: IDA); GO_1901215 (EC: IEA); GO_2000251 (EC: IDA) PMID: 1281454; 1281794; 1692828; 2420009; 2423327; 2448221; 2453015; 2456256; 3034599; 3484805; 3494801; 3499671; 3501046; 7518249; 7522243; 7524894; 7685117; 8554326; 8708536; 8794774; 10364174; 10473051; 10584986; 10617744; 11436203; 11795665; 11861308; 11877288; 11920209; 12009905; 12027409; 12034575; 12152985; 12393522; 12393561; 12397015; 12456601; 12477932; 12548211; 12562880; 12568301; 12627849; 12636092; 12676791; 12717025; 12946100; 12954601; 14587040; 14751388; 14769149; 15019810; 15028279; 15214947; 15218949; 15576295; 15616013; 15622763; 15664994; 16037394; 16051386; 16211258; 16230423; 16492764; 16498082; 16712791; 16735597; 16822885; 16912178; 16980970; 17047971; 17115186; 17176065; 17342342; 17572226; 17703412; 17852446; 17879956; 17894541; 18029348; 18095095; 18196568; 18219369; 18297540; 18353856; 18358673; 18484240; 18515229; 18537187; 18597629; 18633131; 18675273; 18676680; 18785976; 18806347; 18952897; 19141860; 19151252; 19170196; 19172109; 19258923; 19453261; 19526310; 19539215; 19625176; 19640182; 19692168; 19789190; 19913121; 20012635; 20021260; 20139978; 20172861; 20179985; 20237318; 20237496; 20361316; 20435882; 20452482; 20485444; 20503287; 20523065; 20557950; 20628086; 20673868; 20680910; 20810026; 20957751; 20959405; 21039040; 21079612; 21092001; 21224471; 21262770; 21273924; 21334074; 21335665; 21524920; 21539498; 21645282; 21738478; 21738480; 21844566; 21935680; 21981141; 21999467; 22045733; 22120987; 22171570; 22313638; 22336152; 22440005; 22443081; 22465760; 22528488; 22751169; 22788528; 22829643; 22944463; 23063381; 23087180; 23244154; 23319418; 23530240; 23548906 colony stimulating factor 3 (granulocyte) Ensembl:ENSG00000108342 HGNC:2438 HPRD:00736 MIM:138970 Vega:OTTHUMG00000133247 Other designations: filgrastim|granulocyte colony-stimulating factor|lenograstim|pluripoietin CSF3 OGG:3000001508 Bin Zhao, Yue Liu, Oliver He APPS CPSB WEB: http://www.ncbi.nlm.nih.gov/gene CTSB cathepsin B 1508 8p22 20140408 9606 8 protein-coding Official from a nomenclature committee GO_0002224 (EC: TAS); GO_0004197 (EC: IDA); GO_0005515 (EC: IPI, PMID: 16364318); GO_0005518 (EC: IDA); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA); GO_0005615 (EC: ISS); GO_0005622 (EC: TAS, PMID: 1645961); GO_0005730 (EC: IDA); GO_0005739 (EC: IEA); GO_0005764 (EC: IDA, PMID: 1837142); GO_0006508 (EC: IDA, PMID: 7890620); GO_0008233 (EC: IDA, PMID: 7890620); GO_0008234 (EC: IDA, PMID: 8811434); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0030574 (EC: IDA); GO_0030574 (EC: TAS); GO_0030855 (EC: IEP); GO_0036021 (EC: TAS); GO_0042470 (EC: IEA); GO_0042981 (EC: TAS, PMID: 16130169); GO_0043231 (EC: IDA); GO_0043394 (EC: IPI); GO_0045087 (EC: TAS); GO_0048471 (EC: IDA, PMID: 15614436); GO_0050790 (EC: IEA); GO_0051603 (EC: IDA); GO_0070062 (EC: IDA, PMID: 19199708); GO_0097067 (EC: IEP) PMID: 417724; 1326552; 1577456; 1597471; 1637335; 1645961; 1837142; 1868826; 1900515; 1984484; 1996959; 2061332; 2476070; 3010323; 3463996; 3542996; 3972105; 6203523; 6351842; 7509303; 7622042; 7718586; 7890620; 8014475; 8083219; 8112600; 8617355; 8635854; 8811434; 9076588; 9295331; 9299326; 9360997; 9412840; 9539769; 9582368; 9585570; 9632704; 9733783; 9770500; 9776083; 9928950; 10353845; 10395917; 10512713; 10777578; 10849756; 10876156; 11016923; 11115496; 11134363; 11139332; 11162551; 11228542; 11241311; 11435427; 11513559; 11514663; 11536009; 11746262; 11815600; 11932257; 12057992; 12072442; 12086583; 12102727; 12185082; 12186841; 12189154; 12201820; 12437117; 12437120; 12477932; 12581740; 12589965; 12643545; 12677446; 12726991; 12887051; 12893746; 12926111; 14503883; 14702039; 14729603; 14730346; 14984956; 15016552; 15100281; 15122332; 15231747; 15255544; 15262981; 15274632; 15489334; 15512772; 15614436; 15679122; 15710602; 15799821; 15807897; 15816632; 15831716; 15832773; 16034129; 16051222; 16077201; 16130169; 16169070; 16303743; 16315320; 16364318; 16381007; 16492714; 16534247; 16709808; 16733801; 16894574; 16913838; 16914553; 17064696; 17081065; 17504810; 17507477; 17519890; 17724614; 17726009; 17982689; 17990360; 17991740; 18029348; 18163891; 18296264; 18314113; 18472965; 18515357; 18543249; 18566385; 18566436; 18598236; 18616803; 18706099; 18714186; 18718938; 18760860; 18949742; 19004543; 19040356; 19199708; 19331819; 19414800; 19434518; 19454696; 19615732; 19661440; 19692168; 19700239; 19774387; 19811804; 19913121; 19915865; 19930869; 20008285; 20042316; 20180636; 20302512; 20424577; 20536394; 20563251; 20567828; 20584670; 20627011; 20628086; 20661471; 20699092; 20706999; 20833970; 20880494; 20930303; 21060833; 21092200; 21112096; 21139048; 21199580; 21250859; 21323990; 21508263; 21541353; 21562164; 21585286; 21600167; 21742978; 21832049; 21835790; 21840777; 21850018; 21880013; 21890473; 21900206; 21925292; 21945151; 21948970; 21967108; 22066471; 22118674; 22127599; 22138708; 22190034; 22209964; 22222211; 22262857; 22266111; 22268729; 22278224; 22287159; 22322590; 22384200; 22464443; 22467319; 22571763; 22693552; 22695494; 22732093; 22745374; 22782900; 22851129; 22939629; 22949512; 23024364; 23063511; 23189279; 23195957; 23219593; 23222509; 23222817; 23292187; 23349634; 23362198; 23466190; 23591598; 23602568; 23603447; 23633927; 23667900; 23677785; 23708264; 23867824 cathepsin B Ensembl:ENSG00000164733 HGNC:2527 HPRD:00287 MIM:116810 Vega:OTTHUMG00000090799 Other designations: APP secretase|amyloid precursor protein secretase|cathepsin B1|cysteine protease CTSB OGG:3000001509 Bin Zhao, Yue Liu, Oliver He CLN10 CPSD HEL-S-130P WEB: http://www.ncbi.nlm.nih.gov/gene CTSD cathepsin D 1509 11p15.5 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0000045 (EC: IEA); GO_0004190 (EC: IEA); GO_0005515 (EC: IPI, PMID: 17112520); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA); GO_0005615 (EC: ISS); GO_0005739 (EC: IEA); GO_0005764 (EC: IDA, PMID: 1837142); GO_0008219 (EC: IEA); GO_0019886 (EC: TAS); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0030574 (EC: TAS); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0042470 (EC: IEA); GO_0043202 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 938470; 1522590; 1734961; 1837142; 1883350; 1939080; 2013314; 2069717; 2180427; 2736531; 3261170; 3588310; 3665421; 3927292; 3988746; 6236213; 7523115; 7547509; 7657720; 7935485; 8106429; 8262386; 8393577; 8419924; 8467789; 8671230; 8889548; 8930981; 8943232; 9076588; 9275067; 9731700; 10504270; 10508159; 10605825; 10623764; 10716266; 10748089; 10849758; 10876156; 10931940; 10986284; 11095076; 11198280; 11258665; 11264868; 11304834; 11341921; 11436125; 11581410; 11687971; 11779865; 11780226; 11786931; 11840502; 11906282; 12011767; 12083803; 12140763; 12147324; 12151789; 12185597; 12477932; 12556904; 12643545; 12651610; 12754519; 12782337; 12782632; 12811635; 12826741; 12970159; 14702039; 14718574; 14767531; 15003956; 15081423; 15158911; 15168727; 15192082; 15211064; 15211070; 15258139; 15318816; 15489334; 15668295; 15739123; 15843343; 15862967; 15896324; 15989967; 16046058; 16081416; 16127101; 16263699; 16263712; 16331270; 16335952; 16341674; 16354654; 16396496; 16417614; 16543533; 16608402; 16652347; 16685649; 16709808; 16784755; 16850161; 17032648; 17081065; 17112520; 17176069; 17188016; 17284061; 17289576; 17340625; 17395004; 17532541; 17601350; 17670831; 17875703; 18177262; 18202773; 18248894; 18296260; 18307033; 18367545; 18387691; 18396902; 18426579; 18431031; 18494001; 18559512; 18566016; 18566385; 18624398; 18702517; 18830724; 18977241; 19056867; 19061927; 19109932; 19115690; 19203374; 19221643; 19383337; 19487283; 19494521; 19571726; 19723497; 19802014; 19828951; 19854241; 19913121; 19919557; 19926167; 19939935; 19950226; 20000738; 20071328; 20083556; 20125193; 20301601; 20385381; 20399529; 20430722; 20597865; 20628086; 20666480; 20666745; 20826454; 20855565; 20926008; 21139048; 21145461; 21148553; 21298030; 21311773; 21315176; 21470957; 21533003; 21632707; 21674799; 21709160; 21789704; 21800051; 21890473; 21906983; 21909273; 21948970; 22081071; 22118674; 22190034; 22244896; 22268729; 22302483; 22388353; 22399610; 22439866; 22476353; 22528489; 22542809; 22623531; 22627201; 22816225; 22824147; 22898924; 22939629; 22949512; 22964611; 22990118; 22996917; 23042275; 23065739; 23107604; 23219593; 23250759; 23415546; 23455922; 23466190; 23483898; 23499937; 23840360; 23868063; 24198402; 24250222; 24511668 cathepsin D Ensembl:ENSG00000117984 HGNC:2529 HPRD:00291 MIM:116840 Vega:OTTHUMG00000044760 CTSD OGG:3000001514 Bin Zhao, Yue Liu, Oliver He CATL CTSL1 MEP WEB: http://www.ncbi.nlm.nih.gov/gene CTSL cathepsin L 1514 RP11-65B23.1 9q21.33 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0001968 (EC: IPI); GO_0002224 (EC: TAS); GO_0002250 (EC: IEP, PMID: 15196205); GO_0004197 (EC: IDA, PMID: 14511383); GO_0005515 (EC: IPI, PMID: 17889653); GO_0005518 (EC: IDA); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA); GO_0005634 (EC: TAS); GO_0005764 (EC: IDA, PMID: 15196205); GO_0006508 (EC: IDA); GO_0008234 (EC: IDA, PMID: 8811434); GO_0019882 (EC: TAS, PMID: 15196205); GO_0019886 (EC: TAS); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0030574 (EC: IDA); GO_0030574 (EC: TAS); GO_0036021 (EC: TAS); GO_0042393 (EC: IDA); GO_0043202 (EC: TAS); GO_0043394 (EC: IPI); GO_0045087 (EC: TAS); GO_0051603 (EC: IDA); GO_0071888 (EC: NAS, PMID: 18495127); GO_0097067 (EC: IEP) PMID: 116880; 1551416; 1837142; 1939080; 2275556; 2835398; 3342889; 3421948; 3490478; 3545185; 3550705; 7340337; 8419312; 8666891; 8811434; 8889548; 8896443; 9076588; 9141479; 9468501; 9548757; 9585570; 9632704; 9733783; 9837884; 9918848; 10022822; 10218831; 10395917; 10428479; 10716919; 10849756; 11278902; 11327826; 11435427; 11514663; 11517935; 11767948; 11771045; 11777924; 11801256; 11978977; 12137950; 12437117; 12437119; 12477932; 12492488; 12504904; 12748383; 12754519; 12809493; 12818188; 12921779; 12926111; 12941783; 12949073; 14511383; 14702039; 14718574; 15099520; 15100281; 15174051; 15196205; 15255544; 15318816; 15454886; 15489334; 15498563; 15512772; 15665831; 15816632; 15832773; 15982660; 16303743; 16335952; 16354158; 16433682; 16565075; 16740135; 16913838; 16918298; 17192395; 17227755; 17519890; 17561110; 17574778; 17643114; 17889653; 17928356; 18163891; 18221013; 18366346; 18450756; 18495127; 18616803; 18619973; 18624398; 18658137; 18971274; 19005484; 19096818; 19270352; 19291794; 19550400; 19663777; 19915865; 19924101; 19939935; 19958782; 19959474; 20075068; 20302512; 20347002; 20497254; 20524145; 20567828; 20837372; 20881085; 20926012; 21029616; 21134415; 21226994; 21308479; 21382349; 21395501; 21484410; 21496199; 21501115; 21555518; 21562164; 21585286; 21700710; 21715684; 21742978; 21750527; 21756348; 21769426; 21775114; 21880013; 21896479; 21898833; 21900206; 21906983; 21925292; 21965756; 21967108; 21988832; 22031933; 22222211; 22281037; 22365146; 22451661; 22571763; 22674323; 22695494; 22871890; 22963824; 23009386; 23063511; 23229094; 23337117; 23536651; 23603447; 23677785; 23915070 cathepsin L Ensembl:ENSG00000135047 HGNC:2537 HPRD:00293 MIM:116880 Vega:OTTHUMG00000020149 CTSL OGG:3000001522 Bin Zhao, Yue Liu, Oliver He CTSX WEB: http://www.ncbi.nlm.nih.gov/gene CTSZ cathepsin Z 1522 20q13.32 20140408 9606 20 protein-coding Official from a nomenclature committee GO_0002003 (EC: TAS); GO_0005615 (EC: IDA); GO_0005764 (EC: IEA); GO_0005783 (EC: IDA); GO_0005886 (EC: TAS); GO_0006508 (EC: TAS, PMID: 9642240); GO_0008234 (EC: IEA); GO_0043231 (EC: IDA); GO_0044267 (EC: TAS); GO_0060441 (EC: IEA) PMID: 9642240; 9738465; 10653162; 10653163; 10656802; 10745011; 10760573; 11030415; 11076863; 11256614; 11780052; 12477932; 15489334; 15489336; 15680921; 16381901; 17065156; 17601350; 18420963; 18976975; 18977241; 21139048; 21310951; 21354459; 21368909; 21454358; 21616554; 21963094; 21966391; 22139419; 22268729; 22451661; 22632162; 23128233; 23827504; 24026423 cathepsin Z Ensembl:ENSG00000101160 HGNC:2547 HPRD:04410 MIM:603169 Vega:OTTHUMG00000032858 CTSZ OGG:3000001543 Bin Zhao, Yue Liu, Oliver He AHH AHRR CP11 CYP1 P1-450 P450-C P450DX WEB: http://www.ncbi.nlm.nih.gov/gene CYP1A1 cytochrome P450, family 1, subfamily A, polypeptide 1 1543 15q24.1 9606 15 GO_0001666 (EC: IEA); GO_0005506 (EC: IEA); GO_0005739 (EC: IEA); GO_0005789 (EC: TAS); GO_0006778 (EC: IEA); GO_0006805 (EC: TAS); GO_0007568 (EC: IEA); GO_0008283 (EC: IEA); GO_0008395 (EC: IEA); GO_0009308 (EC: IEA); GO_0009611 (EC: IEA); GO_0009615 (EC: IEA); GO_0009624 (EC: IEA); GO_0009635 (EC: IEA); GO_0009792 (EC: IEA); GO_0009804 (EC: IEA); GO_0009812 (EC: IEA); GO_0010041 (EC: IEA); GO_0014070 (EC: IEA); GO_0016491 (EC: IDA, PMID:19219744); GO_0016679 (EC: IEA); GO_0016711 (EC: IEA); GO_0017143 (EC: IEA); GO_0017144 (EC: IDA, PMID:19219744); GO_0019341 (EC: IEA); GO_0019369 (EC: TAS); GO_0019373 (EC: TAS); GO_0019825 (EC: TAS, PMID:1691986); GO_0019899 (EC: IEA); GO_0020037 (EC: IEA); GO_0032094 (EC: IEA); GO_0032451 (EC: IEA); GO_0032496 (EC: IEA); GO_0033189 (EC: IEA); GO_0042359 (EC: IC, PMID:15546903); GO_0042493 (EC: IEA); GO_0042904 (EC: IEA); GO_0043010 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0046677 (EC: IEA); GO_0046685 (EC: IEA); GO_0048565 (EC: IEA); GO_0050665 (EC: IEA); GO_0055093 (EC: IEA); GO_0055114 (EC: IDA, PMID:19219744); GO_0060137 (EC: IEA); GO_0070330 (EC: IEA); GO_0070365 (EC: IEA); GO_0070576 (EC: IDA, PMID:15546903); GO_0097267 (EC: TAS); GO_1900087 (EC: IEA) PMID:1691986; 1722803; 1761516; 2989797; 3000715; 3019683; 3714481; 3838385; 4000952; 6102994; 8095225; 8125298; 8313840; 8442765; 8548778; 8895751; 9500998; 9890157; 10493257; 10612842; 10739168; 11037802; 11037803; 11045797; 11052546; 11124296; 11159735; 11162685; 11172643; 11191882; 11207026; 11236859; 11246217; 11259393; 11275366; 11279306; 11291049; 11295132; 11295847; 11325850; 11330960; 11389067; 11393538; 11396202; 11406420; 11406608; 11408349; 11408954; 11410321; 11418090; 11422615; 11434510; 11436564; 11459424; 11470760; 11470992; 11470996; 11471167; 11484167; 11485833; 11487538; 11488937; 11500195; 11501853; 11503278; 11507974; 11511301; 11520401; 11525595; 11535253; 11551408; 11564581; 11641039; 11675150; 11675474; 11689007; 11698341; 11719088; 11751440; 11752233; 11779261; 11792676; 11793160; 11798822; 11833070; 11854392; 11859435; 11860825; 11860900; 11872636; 11895912; 11934439; 11952781; 11955671; 11967624; 11996959; 12018173; 12030651; 12034316; 12036913; 12063626; 12071517; 12100112; 12110344; 12139735; 12144816; 12147246; 12163326; 12170467; 12171760; 12175533; 12183419; 12189551; 12210502; 12210751; 12237110; 12269988; 12297440; 12351530; 12354067; 12365037; 12378791; 12397416; 12419832; 12435115; 12464257; 12468438; 12477932; 12484238; 12490585; 12496044; 12527337; 12548461; 12569554; 12574216; 12579334; 12590982; 12594823; 12602902; 12620480; 12631667; 12646505; 12670526; 12680328; 12690010; 12713578; 12718576; 12729704; 12732844; 12738724; 12746631; 12748560; 12760253; 12767509; 12767526; 12771031; 12772461; 12777964; 12824892; 12827651; 12845676; 12846365; 12854128; 12879168; 12880680; 12883749; 12903034; 12919721; 12925969; 12934333; 12949934; 14510941; 14534704; 14560034; 14582397; 14602139; 14602525; 14611903; 14634838; 14639127; 14646291; 14656945; 14665706; 14675315; 14687717; 14693745; 14695173; 14719475; 14724908; 14734460; 14758730; 14991750; 15013696; 15037607; 15039299; 15052670; 15059326; 15061915; 15064998; 15069692; 15088300; 15093273; 15111988; 15124938; 15127181; 15127559; 15128046; 15136237; 15152552; 15176217; 15177667; 15180167; 15184245; 15185560; 15194533; 15195126; 15206494; 15215328; 15217514; 15241822; 15279831; 15298956; 15298960; 15299091; 15319333; 15327835; 15333250; 15333597; 15341023; 15352038; 15355699; 15363546; 15375499; 15376230; 15381379; 15382051; 15382273; 15386428; 15459023; 15469410; 15478298; 15489334; 15491310; 15496536; 15521013; 15526353; 15528152; 15546903; 15547760; 15552037; 15579657; 15583370; 15591802; 15596250; 15605089; 15618738; 15640066; 15642161; 15643613; 15646021; 15647817; 15648054; 15653213; 15671210; 15712341; 15725614; 15731166; 15734083; 15734958; 15756908; 15764294; 15765281; 15769360; 15774541; 15774926; 15801491; 15849806; 15856430; 15861041; 15867368; 15870154; 15914211; 15914277; 15920291; 15928955; 15931768; 15938845; 15941966; 15952134; 15953982; 15981231; 15986113; 15991278; 16009381; 16012082; 16037119; 16043197; 16051642; 16084889; 16099114; 16103451; 16130011; 16142442; 16153604; 16202920; 16227674; 16228113; 16235998; 16254684; 16260521; 16270381; 16273625; 16284375; 16284498; 16318816; 16319265; 16337337; 16357593; 16357600; 16360200; 16367916; 16393248; 16402077; 16402549; 16403567; 16407087; 16414014; 16416283; 16424825; 16426572; 16466991; 16471212; 16481407; 16484137; 16488179; 16492926; 16493615; 16505155; 16527884; 16580705; 16598069; 16599372; 16608396; 16609368; 16614107; 16614120; 16620591; 16625286; 16638864; 16676594; 16697254; 16721740; 16763966; 16767678; 16771603; 16788090; 16792888; 16803538; 16807674; 16823842; 16834659; 16835796; 16837240; 16864595; 16882880; 16914185; 16926176; 16947004; 16949388; 16956909; 16971197; 16977255; 16985026; 16985033; 16985250; 16998606; 17022435; 17035385; 17053541; 17063266; 17078101; 17081983; 17083362; 17113562; 17118447; 17119063; 17158763; 17160265; 17160896; 17164366; 17167268; 17171211; 17174438; 17191090; 17192049; 17220347; 17307802; 17307803; 17311112; 17316563; 17361553; 17363580; 17367411; 17372239; 17372243; 17372252; 17403528; 17408703; 17412371; 17427032; 17428572; 17429172; 17429315; 17449539; 17461521; 17477782; 17479406; 17496311; 17498780; 17507624; 17512722; 17512776; 17526865; 17531965; 17548691; 17549424; 17566695; 17577786; 17588204; 17589376; 17590289; 17603290; 17610937; 17611777; 17620151; 17623765; 17630984; 17640999; 17642299; 17646057; 17651397; 17695473; 17706398; 17711714; 17717632; 17728147; 17786624; 17823232; 17852022; 17873299; 17896209; 17900751; 17908297; 17919073; 17919675; 17959138; 17980001; 17980933; 17981384; 17982751; 17996038; 18061941; 18065768; 18070799; 18074679; 18078203; 18082227; 18090121; 18159984; 18180754; 18200441; 18203021; 18203634; 18224491; 18241825; 18247309; 18261353; 18268125; 18285692; 18287863; 18287869; 18304461; 18317771; 18318428; 18320229; 18339256; 18351133; 18389617; 18409146; 18409147; 18414197; 18415690; 18415801; 18437510; 18447907; 18449058; 18463401; 18493746; 18495522; 18496222; 18497059; 18507050; 18507060; 18510611; 18550589; 18569591; 18577398; 18589596; 18590468; 18593984; 18601742; 18618215; 18628428; 18632753; 18636124; 18642288; 18676680; 18691756; 18698632; 18700132; 18706519; 18763031; 18767181; 18768509; 18774560; 18779756; 18784359; 18798002; 18800292; 18818748; 18819424; 18824009; 18849443; 18936436; 18941913; 18979064; 18980759; 18990008; 18990750; 18992263; 19009239; 19012698; 19013013; 19019335; 19022366; 19024313; 19031960; 19064581; 19070657; 19074885; 19110417; 19126602; 19127255; 19138996; 19143007; 19147266; 19160101; 19170196; 19174490; 19178087; 19219744; 19222528; 19229255; 19246429; 19252926; 19264525; 19267064; 19276377; 19285097; 19287966; 19290787; 19303595; 19307236; 19317600; 19336370; 19338043; 19339270; 19343046; 19346634; 19351467; 19356113; 19387820; 19412423; 19414505; 19415745; 19424633; 19424794; 19427967; 19430483; 19443378; 19452301; 19453261; 19456854; 19469619; 19472123; 19479063; 19505920; 19507017; 19507064; 19521675; 19526463; 19527514; 19537956; 19538838; 19561157; 19563927; 19574343; 19575027; 19576320; 19582785; 19598235; 19608585; 19625176; 19627379; 19630952; 19632247; 19639480; 19643819; 19650794; 19666078; 19679043; 19682433; 19692168; 19718946; 19750329; 19751749; 19776291; 19786002; 19789190; 19789301; 19797843; 19799358; 19822571; 19826048; 19827888; 19860743; 19863350; 19892789; 19899130; 19903800; 19913121; 19947517; 19948975; 19954068; 19954069; 19963114; 19963139; 19995559; 20009880; 20012094; 20027111; 20029944; 20032816; 20035380; 20047124; 20052535; 20054510; 20080081; 20088379; 20088394; 20094781; 20095411; 20131310; 20136364; 20177288; 20193595; 20214802; 20226777; 20297661; 20345875; 20373852; 20375710; 20377136; 20381444; 20428802; 20437850; 20453000; 20462615; 20491576; 20511665; 20529763; 20534171; 20544687; 20554493; 20559649; 20579990; 20584197; 20596254; 20602615; 20628086; 20628863; 20634197; 20634891; 20638923; 20644561; 20661821; 20664892; 20700368; 20701904; 20704749; 20723587; 20734064; 20734807; 20804547; 20817259; 20845989; 20846153; 20850372; 20855412; 20878561; 20878621; 20883830; 20884258; 20886582; 20887941; 20937634; 20957336; 20962519; 20965504; 20970553; 21081473; 21086258; 21130723; 21211368; 21246002; 21254355; 21254556; 21262253; 21270613; 21304969; 21329749; 21357676; 21385088; 21402622; 21418988; 21438753; 21490707; 21508386; 21545198; 21545219; 21586621; 21590276; 21709011; 21710246; 21718208; 21775774; 21848428; 21859547; 21869479; 21870186; 21876539; 21909115; 21977969; 22000673; 22018952; 22025136; 22086975; 22088806; 22109568; 22154617; 22183307; 22213191; 22217397; 22236719; 22273851; 22277800; 22292665; 22294106; 22296350; 22297691; 22304463; 22311486; 22312901; 22359202; 22365406; 22374940; 22384629; 22392998; 22395499; 22422552; 22442665; 22448487; 22470100; 22579698; 22594779; 22611936; 22660220; 22664944; 22707145; 22733497; 22752755; 22754477; 22782580; 22837390; 22846179; 22847262; 22854411; 22855999; 22876118; 22893352; 22901117; 22909097; 22918668; 22948778; 22949628; 22951721; 22952673; 22964275; 22994769; 22997752; 23000097; 23013535; 23033491; 23046808; 23055196; 23056546; 23065259; 23065291; 23098461; 23111888; 23124075; 23152866; 23174221; 23178447; 23229202; 23259321; 23288144; 23293967; 23350368; 23353840; 23369756; 23381648; 23411129; 23419638; 23424205; 23471717; 23475304; 23492908; 23508959; 23528250; 23548414; 23619522; 23661361; 23707957; 23785672; 23816456; 23832578; 23840148; 23842721; 23860774; 23870476; 23886179; 23918309; 24091107; 24316127; 24355420 cytochrome P450, family 1, subfamily A, polypeptide 1 Ensembl:ENSG00000140465 HGNC:2595 HPRD:00148 MIM:108330 Vega:OTTHUMG00000142812 Other designations: CYPIA1|aryl hydrocarbon hydroxylase|cytochrome P1-450, dioxin-inducible|cytochrome P450 1A1|cytochrome P450 form 6|cytochrome P450, subfamily I (aromatic compound-inducible), polypeptide 1|cytochrome P450-C|cytochrome P450-P1|flavoprotein-linked monooxygenase|xenobiotic monooxygenase CYP1A1 OGG:3000001544 Bin Zhao, Yue Liu, Oliver He CP12 P3-450 P450(PA) WEB: http://www.ncbi.nlm.nih.gov/gene CYP1A2 cytochrome P450, family 1, subfamily A, polypeptide 2 1544 15q24.1 9606 15 GO_0004497 (EC: IDA, PMID:15327587); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006706 (EC: IMP, PMID:18356043); GO_0006778 (EC: IEA); GO_0006805 (EC: TAS); GO_0009055 (EC: TAS, PMID:2813353); GO_0009403 (EC: IDA, PMID:11511187); GO_0009791 (EC: IEA); GO_0009820 (EC: IDA, PMID:11511187); GO_0010468 (EC: IEA); GO_0016098 (EC: IDA, PMID:16401082); GO_0016491 (EC: IDA, PMID:16401082); GO_0016712 (EC: IMP, PMID:2813353); GO_0017144 (EC: IDA, PMID:15327587); GO_0018894 (EC: IEA); GO_0019369 (EC: TAS); GO_0019373 (EC: TAS); GO_0019899 (EC: IPI, PMID:15680923); GO_0020037 (EC: IDA, PMID:17311915); GO_0030324 (EC: IEA); GO_0032259 (EC: TAS); GO_0032355 (EC: IEA); GO_0032451 (EC: IDA, PMID:2813353); GO_0032496 (EC: IEA); GO_0032787 (EC: IDA, PMID:19651758); GO_0034875 (EC: IDA, PMID:18619574); GO_0042737 (EC: IMP, PMID:18356043); GO_0042738 (EC: IDA, PMID:18619574); GO_0043231 (EC: IDA, PMID:2813353); GO_0044281 (EC: TAS); GO_0045333 (EC: IEA); GO_0046483 (EC: IDA, PMID:15327587); GO_0050665 (EC: IEA); GO_0055114 (EC: IDA, PMID:16401082); GO_0070330 (EC: IEA); GO_0070989 (EC: IDA, PMID:18619574); GO_0071276 (EC: IEA); GO_0071615 (EC: IDA, PMID:19029318); GO_0097267 (EC: TAS) PMID:2575218; 2813353; 3000715; 3462722; 3517618; 3681487; 3755823; 8095225; 8287062; 8553685; 8573198; 8694864; 9398194; 9598815; 9797707; 9884316; 9890157; 10463577; 10493258; 10791558; 11153915; 11186132; 11207026; 11275366; 11393588; 11470995; 11496364; 11501059; 11507974; 11511187; 11749050; 11763009; 11782366; 11791895; 11817502; 11943609; 12067576; 12147246; 12181774; 12419832; 12445029; 12445035; 12477932; 12484238; 12534642; 12566081; 12569554; 12618594; 12630986; 12663508; 12692107; 12732846; 12790158; 12851801; 12900870; 12920202; 12925300; 12943470; 14563787; 14640293; 14648207; 14695651; 14714565; 14723376; 14976127; 15039299; 15110095; 15128046; 15241822; 15299091; 15319333; 15327587; 15349722; 15363478; 15382051; 15387446; 15466009; 15469410; 15489334; 15505641; 15519301; 15564895; 15643613; 15680923; 15734958; 15763632; 15770072; 15774926; 15849225; 15890241; 15901993; 15941966; 15949157; 15987714; 15996939; 16006997; 16048566; 16103451; 16130011; 16153396; 16157215; 16172230; 16188490; 16204462; 16307269; 16324277; 16385402; 16401082; 16402077; 16402549; 16406813; 16426572; 16471212; 16495781; 16505155; 16522833; 16538170; 16538176; 16609368; 16636061; 16740387; 16772608; 16775389; 16782969; 16800822; 16864595; 16882880; 16933202; 16969362; 16985026; 16985250; 17065585; 17164366; 17178267; 17191090; 17259654; 17295924; 17311915; 17345072; 17363580; 17370067; 17372239; 17418993; 17429315; 17477782; 17498780; 17503978; 17507615; 17507624; 17509724; 17564586; 17603224; 17603900; 17611010; 17615053; 17616786; 17627011; 17635176; 17688403; 17695473; 17823232; 17823234; 17852022; 17900275; 18052847; 18075470; 18077912; 18159984; 18180754; 18187423; 18200441; 18223460; 18231117; 18268115; 18318428; 18356043; 18389617; 18398030; 18455494; 18466106; 18490497; 18493746; 18496682; 18497059; 18499698; 18510611; 18544563; 18551037; 18569587; 18619574; 18628519; 18632753; 18690546; 18703023; 18751408; 18759349; 18784359; 18798002; 18801337; 18813311; 18825963; 18840375; 18850169; 18936436; 18941913; 18990750; 18992148; 18996102; 19000940; 19026171; 19029318; 19095219; 19106084; 19219744; 19229255; 19273964; 19274061; 19276377; 19285097; 19290787; 19307236; 19332078; 19336370; 19338043; 19339270; 19343046; 19356113; 19414633; 19415745; 19424794; 19430483; 19442564; 19450128; 19451835; 19452301; 19453261; 19479063; 19507017; 19534587; 19569730; 19571439; 19574343; 19575027; 19576320; 19583676; 19593158; 19593168; 19605743; 19636338; 19643819; 19651758; 19666078; 19682433; 19692168; 19751749; 19776291; 19789190; 19806921; 19822571; 19823875; 19843669; 19860743; 19913121; 19926050; 19956635; 19961320; 20029944; 20043572; 20047124; 20054636; 20080081; 20118554; 20125119; 20131310; 20136364; 20147896; 20163457; 20173083; 20175915; 20213484; 20214802; 20218903; 20304699; 20375710; 20381444; 20389299; 20390257; 20403997; 20437850; 20453000; 20505544; 20529763; 20559687; 20583967; 20602612; 20602615; 20628086; 20634197; 20634891; 20641098; 20652353; 20656072; 20663043; 20691427; 20701904; 20734064; 20797314; 20806393; 20829355; 20853468; 20881513; 20930417; 20933493; 20957336; 20970553; 21071160; 21072184; 21081473; 21086794; 21148426; 21210738; 21262253; 21281405; 21329464; 21357676; 21480221; 21490707; 21505853; 21598960; 21825116; 21876539; 21929532; 21977969; 22072123; 22086975; 22141270; 22228482; 22246422; 22258279; 22336631; 22426036; 22448362; 22466345; 22492992; 22628494; 22648710; 22673010; 22749033; 22785257; 22854411; 22855999; 22948892; 22949628; 23081704; 23128882; 23133610; 23138776; 23157985; 23167834; 23278694; 23292087; 23353840; 23492908; 23492909; 23601795; 23603339; 23628800; 23859573 cytochrome P450, family 1, subfamily A, polypeptide 2 Ensembl:ENSG00000140505 HGNC:2596 HPRD:00489 MIM:124060 Vega:OTTHUMG00000172901 Other designations: CYPIA2|P450 form 4|aryl hydrocarbon hydroxylase|cytochrome P(3)450|cytochrome P450 1A2|cytochrome P450 4|cytochrome P450, subfamily I (aromatic compound-inducible), polypeptide 2|cytochrome P450-P3|dioxin-inducible P3-450|flavoprotein-linked monooxygenase|microsomal monooxygenase|xenobiotic monooxygenase CYP1A2 OGG:3000001545 Bin Zhao, Yue Liu, Oliver He CP1B CYPIB1 GLC3A P4501B1 WEB: http://www.ncbi.nlm.nih.gov/gene CYP1B1 cytochrome P450, family 1, subfamily B, polypeptide 1 1545 2p22.2 9606 2 GO_0001525 (EC: IEA); GO_0004497 (EC: TAS, PMID:9097971); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006725 (EC: IEA); GO_0006805 (EC: IDA); GO_0006805 (EC: TAS); GO_0007601 (EC: TAS, PMID:9097971); GO_0008202 (EC: IDA); GO_0009404 (EC: IEA); GO_0009636 (EC: IEA); GO_0016125 (EC: TAS); GO_0016712 (EC: IDA, PMID:10871058); GO_0019369 (EC: TAS); GO_0019373 (EC: TAS); GO_0019825 (EC: TAS, PMID:9097971); GO_0020037 (EC: IDA); GO_0020037 (EC: TAS, PMID:9097971); GO_0043542 (EC: IEA); GO_0044281 (EC: TAS); GO_0055114 (EC: TAS, PMID:9097971); GO_0061298 (EC: IEA); GO_0070330 (EC: IEA); GO_0071603 (EC: IEA); GO_0097267 (EC: TAS) PMID:1925598; 8175734; 8910454; 9097971; 9463332; 9497261; 9823305; 9890157; 10227395; 10614688; 10871058; 11221602; 11303589; 11389067; 11403040; 11452143; 11555828; 11558822; 11749050; 11774072; 11854439; 11955671; 12010864; 12183407; 12200121; 12372064; 12385014; 12415427; 12419832; 12477932; 12520071; 12525557; 12567107; 12598442; 12602902; 12618873; 12692107; 12718576; 12770747; 12807732; 12837283; 12844487; 12873984; 14507861; 14520706; 14562027; 14634838; 14656940; 14729846; 14734460; 14744739; 14961553; 15041720; 15072827; 15075793; 15102677; 15122594; 15128046; 15177664; 15199113; 15255109; 15255550; 15285606; 15297370; 15299091; 15333708; 15342454; 15342556; 15342693; 15382051; 15386537; 15475877; 15489334; 15596250; 15636228; 15654505; 15723004; 15733270; 15734954; 15734958; 15774541; 15777990; 15808404; 15861043; 15896461; 15905203; 15941966; 15958554; 15987428; 16006997; 16051642; 16103451; 16115918; 16172228; 16172230; 16202920; 16207128; 16260521; 16284375; 16319265; 16319821; 16344560; 16384942; 16490498; 16569655; 16598069; 16638984; 16688110; 16716118; 16730930; 16735991; 16735994; 16766147; 16808847; 16847423; 16850246; 16862072; 16864595; 16896040; 16949388; 16963504; 16977255; 16978616; 16985026; 16985250; 17035385; 17053044; 17063266; 17077994; 17157584; 17164573; 17174438; 17187946; 17200336; 17220347; 17224759; 17224914; 17301257; 17311112; 17321191; 17353931; 17363580; 17372239; 17372243; 17403528; 17429315; 17449539; 17449559; 17458695; 17496311; 17498780; 17507616; 17507624; 17548691; 17562158; 17563717; 17575219; 17588204; 17589376; 17591938; 17603900; 17615053; 17627011; 17642299; 17687619; 17704407; 17718864; 17893647; 17914928; 17919675; 17922187; 17925548; 17980933; 18055790; 18059014; 18067928; 18070520; 18187806; 18227148; 18258609; 18268125; 18318428; 18347981; 18385784; 18414103; 18415014; 18425393; 18470941; 18483560; 18486761; 18497059; 18510611; 18537981; 18544568; 18569579; 18569591; 18573508; 18575334; 18616618; 18622259; 18628428; 18632753; 18676680; 18763031; 18779756; 18784359; 18794456; 18820009; 18829176; 18841557; 18852424; 18922394; 18936436; 18977467; 18980759; 18989382; 18990750; 18992148; 19015200; 19031960; 19064581; 19074885; 19083124; 19094228; 19096718; 19116217; 19126602; 19127255; 19138946; 19138996; 19170196; 19174490; 19179758; 19195637; 19199255; 19208203; 19214745; 19229255; 19234632; 19247456; 19274671; 19287966; 19290787; 19293312; 19324859; 19331196; 19338043; 19343046; 19349377; 19357154; 19383894; 19414505; 19415745; 19424633; 19424794; 19443378; 19453261; 19479063; 19505920; 19514368; 19528825; 19536304; 19574343; 19575027; 19582785; 19597567; 19598235; 19622003; 19625176; 19630952; 19643970; 19666078; 19668563; 19668597; 19690133; 19692168; 19730035; 19736056; 19744731; 19751749; 19754948; 19776291; 19789190; 19789301; 19793111; 19820397; 19822571; 19857456; 19860743; 19895167; 19898482; 19908239; 19913121; 19956635; 19963139; 19995559; 20027111; 20029944; 20033481; 20037207; 20051892; 20054638; 20057908; 20088394; 20131310; 20137445; 20151268; 20184498; 20198857; 20198978; 20212917; 20214802; 20301314; 20357201; 20375710; 20391138; 20395011; 20403997; 20453000; 20461808; 20462226; 20492382; 20505544; 20529763; 20559649; 20568895; 20628086; 20632082; 20634197; 20634891; 20660114; 20664688; 20678202; 20683028; 20701755; 20734064; 20830506; 20845989; 20875115; 20878130; 20884258; 20887769; 21072184; 21081473; 21081970; 21139974; 21147782; 21168818; 21191305; 21303932; 21306220; 21409489; 21438753; 21458313; 21596299; 21600657; 21614911; 21655360; 21674184; 21683070; 21707071; 21742528; 21850185; 21854771; 21890473; 21963094; 21987572; 22004014; 22011756; 22114726; 22128238; 22138065; 22177211; 22190224; 22232929; 22272893; 22296381; 22327650; 22374940; 22459615; 22466345; 22504876; 22509109; 22594779; 22840970; 22859684; 22878448; 22942166; 23028769; 23032576; 23087145; 23215915; 23218183; 23218701; 23283740; 23325794; 23350153; 23350368; 23353840; 23370603; 23757320; 23785672; 23794133; 23861929; 23922489; 24227805 cytochrome P450, family 1, subfamily B, polypeptide 1 Ensembl:ENSG00000138061 HGNC:2597 HPRD:03464 MIM:601771 Vega:OTTHUMG00000100970 Other designations: aryl hydrocarbon hydroxylase|cytochrome P450 1B1|cytochrome P450, subfamily I (dioxin-inducible), polypeptide 1 (glaucoma 3, primary infantile)|flavoprotein-linked monooxygenase|microsomal monooxygenase|xenobiotic monooxygenase CYP1B1 OGG:3000001548 Bin Zhao, Yue Liu, Oliver He CPA6 CYP2A CYP2A3 CYPIIA6 P450C2A P450PB WEB: http://www.ncbi.nlm.nih.gov/gene CYP2A6 cytochrome P450, family 2, subfamily A, polypeptide 6 1548 19q13.2 9606 19 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0005881 (EC: IDA); GO_0006805 (EC: TAS); GO_0008202 (EC: IMP, PMID:18356043); GO_0008389 (EC: IDA, PMID:16086027); GO_0009804 (EC: IDA, PMID:19651758); GO_0016712 (EC: IEA); GO_0017144 (EC: IDA, PMID:19651758); GO_0017144 (EC: IMP, PMID:18356043); GO_0019899 (EC: IPI, PMID:15680923); GO_0020037 (EC: IDA, PMID:16086027); GO_0042738 (EC: IDA, PMID:15680923); GO_0044281 (EC: TAS); GO_0046226 (EC: IDA, PMID:19029318) PMID:1889415; 1944238; 2322567; 2726448; 2748347; 3856261; 4011450; 7581481; 7668294; 7864805; 8587134; 9409631; 9827545; 9890157; 10544257; 10781881; 11054771; 11207029; 11237731; 11241319; 11259349; 11278503; 11434509; 11684323; 11725533; 11805739; 11927498; 11927840; 11960911; 11960914; 12115524; 12162851; 12164325; 12172220; 12223434; 12325023; 12406643; 12419832; 12445030; 12477932; 12708602; 12721789; 12749606; 12844137; 12883749; 14568264; 14583682; 14981342; 15039299; 15128046; 15203795; 15225612; 15308589; 15327835; 15370155; 15454735; 15469410; 15475735; 15489334; 15534625; 15564629; 15592323; 15618701; 15660270; 15665333; 15671201; 15680923; 15861035; 15861044; 15900015; 15940289; 15993850; 16006997; 16041240; 16048566; 16086027; 16126166; 16176798; 16207711; 16272956; 16344560; 16372023; 16377082; 16378601; 16402086; 16402128; 16452582; 16470306; 16636685; 16720336; 16758265; 16857725; 16891249; 16952495; 17015050; 17036930; 17112802; 17130279; 17156750; 17207267; 17220563; 17259654; 17267622; 17454707; 17522595; 17540336; 17549345; 17646279; 17683511; 17916905; 17927692; 17934923; 17979512; 18004205; 18188752; 18212800; 18216723; 18356043; 18360915; 18380793; 18425152; 18510611; 18666753; 18698229; 18715882; 18936436; 18941913; 18976031; 18979093; 19012698; 19029318; 19040121; 19082995; 19104915; 19225447; 19251454; 19279561; 19290787; 19300303; 19303722; 19339270; 19343046; 19361454; 19365400; 19371316; 19387893; 19406142; 19415821; 19454817; 19479063; 19533856; 19537956; 19604090; 19643819; 19651758; 19659438; 19702528; 19703308; 19751749; 19779319; 19789190; 19845430; 19921195; 19956635; 20012030; 20061389; 20089352; 20136358; 20139165; 20155256; 20173083; 20177288; 20336063; 20418888; 20418890; 20437850; 20438369; 20506136; 20596643; 20647221; 20656072; 20701904; 20717551; 20719908; 20734048; 20734064; 20860463; 20887713; 21205058; 21265876; 21326246; 21410749; 21418183; 21473878; 21521021; 21685187; 21745589; 21747048; 21765098; 21791872; 21964962; 22073590; 22080838; 22160797; 22217675; 22271297; 22322240; 22342802; 22465937; 22497566; 22498344; 22547082; 22614024; 22696418; 22706231; 22847926; 22854688; 22890016; 23049750; 23178447; 23203414; 23292114; 23371292; 23462429; 23471717; 23528144; 23585826; 23649654; 23733493; 23813797 cytochrome P450, family 2, subfamily A, polypeptide 6 Ensembl:ENSG00000255974 HGNC:2610 HPRD:00420 MIM:122720 Vega:OTTHUMG00000182713 Other designations: 1,4-cineole 2-exo-monooxygenase|coumarin 7-hydroxylase|cytochrome P450 2A6|cytochrome P450 IIA3|cytochrome P450(I)|cytochrome P450, subfamily IIA (phenobarbital-inducible), polypeptide 6|flavoprotein-linked monooxygenase|xenobiotic monooxygenase CYP2A6 OGG:3000001549 Bin Zhao, Yue Liu, Oliver He CPA7 CPAD CYP2A CYPIIA7 P450-IIA4 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2A7 cytochrome P450, family 2, subfamily A, polypeptide 7 1549 19q13.2 9606 19 GO_0005506 (EC: IEA); GO_0005789 (EC: IEA); GO_0019825 (EC: TAS, PMID:7864805); GO_0020037 (EC: IEA); GO_0070330 (EC: IEA) PMID:2322567; 7668294; 7864805; 8043031; 8587134; 9890157; 10353262; 10493259; 11960914; 12325023; 12477932; 15128046; 16636685; 22890016 cytochrome P450, family 2, subfamily A, polypeptide 7 Ensembl:ENSG00000198077 HGNC:2611 HPRD:07453 MIM:608054 Vega:OTTHUMG00000182715 Other designations: cytochrome P450 2A7|cytochrome P450 IIA4|cytochrome P450, subfamily IIA (phenobarbital-inducible), polypeptide 7|cytochrome P450IIA4 CYP2A7 OGG:3000001551 Bin Zhao, Yue Liu, Oliver He CP37 CYPIIIA7 P450-HFLA WEB: http://www.ncbi.nlm.nih.gov/gene CYP3A7 cytochrome P450, family 3, subfamily A, polypeptide 7 1551 7q21-q22.1 9606 7 GO_0004497 (EC: ISS); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0019825 (EC: TAS, PMID:2722762); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA) PMID:1562592; 2492179; 2722762; 2786707; 7894497; 8694864; 9644715; 9890157; 10950848; 11093772; 11137287; 11266076; 11940601; 12406645; 12477932; 12485945; 12690205; 12865317; 14569421; 15128046; 15319333; 15489334; 15698577; 15937338; 15985487; 16041241; 16314882; 16430309; 16635807; 17334880; 17559345; 17582393; 17604264; 17885626; 17936930; 18406467; 18445661; 18537580; 18676680; 18978522; 19064572; 19170196; 19275551; 19343046; 19424794; 19585271; 19593168; 19625176; 19692168; 19801957; 19842932; 20118548; 20147896; 20345875; 20529763; 20615193; 20621111; 20634891; 20637317; 22253426; 22277676; 23143891 cytochrome P450, family 3, subfamily A, polypeptide 7 Ensembl:ENSG00000160870 HGNC:2640 HPRD:05630 MIM:605340 Vega:OTTHUMG00000156726 Other designations: aryl hydrocarbon hydroxylase|cytochrome P450 3A7|cytochrome P450, subfamily IIIA, polypeptide 7|cytochrome P450-HFLA|flavoprotein-linked monooxygenase|microsomal monooxygenase|xenobiotic monooxygenase CYP3A7 OGG:3000001553 Bin Zhao, Yue Liu, Oliver He CPAD CYP2A CYPIIA13 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2A13 cytochrome P450, family 2, subfamily A, polypeptide 13 1553 19q13.2 9606 19 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0020037 (EC: IDA, PMID:17428784); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA) PMID:7581481; 7668294; 8587134; 8889548; 9890157; 10353262; 11016631; 12130698; 12721789; 12920161; 14633739; 15063809; 15115698; 15128046; 15196988; 15222883; 15333516; 15618722; 16316926; 16835796; 17428784; 18669584; 19290787; 19303722; 19343046; 19414505; 19789190; 19812523; 20431511; 20534012; 20568895; 20798279; 20846153; 21473878; 22315333; 22397853; 22696418; 22700965; 22798551; 22890016; 23463547; 23583631; 23602888; 23752126; 23917075 cytochrome P450, family 2, subfamily A, polypeptide 13 Ensembl:ENSG00000197838 HGNC:2608 HPRD:07454 MIM:608055 Vega:OTTHUMG00000182762 Other designations: cytochrome P450 2A13|cytochrome P450, subfamily IIA (phenobarbital-inducible), polypeptide 13 CYP2A13 OGG:3000001555 Bin Zhao, Yue Liu, Oliver He CPB6 CYP2B CYP2B7 CYP2B7P CYPIIB6 EFVM IIB1 P450 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2B6 cytochrome P450, family 2, subfamily B, polypeptide 6 1555 19q13.2 9606 19 GO_0004497 (EC: IDA, PMID:19651758); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: IDA); GO_0006805 (EC: TAS); GO_0008202 (EC: IMP, PMID:18356043); GO_0016712 (EC: IEA); GO_0017144 (EC: IDA, PMID:19651758); GO_0017144 (EC: IMP, PMID:18356043); GO_0020037 (EC: IDA); GO_0042180 (EC: IDA, PMID:19651758); GO_0042738 (EC: IDA, PMID:19029318); GO_0044281 (EC: TAS); GO_0055114 (EC: IDA, PMID:19651758) PMID:2308828; 2573390; 2813061; 2899870; 7668294; 8432525; 8587134; 9179987; 9890157; 10037683; 10471061; 10768437; 11243870; 11298076; 11353758; 11470993; 11602525; 11991950; 12207635; 12242601; 12439223; 12477932; 12490624; 12571232; 12629583; 12642465; 12721789; 12738724; 12814665; 14515060; 14977870; 15039299; 15057824; 15128046; 15178651; 15190123; 15194512; 15248218; 15284537; 15319333; 15383491; 15469410; 15563456; 15572372; 15622315; 15825040; 15864119; 16116487; 16125881; 16183265; 16267764; 16338275; 16392089; 16433869; 16495778; 16506047; 16538176; 16623664; 16772608; 16815693; 16912957; 16951995; 17015050; 17047492; 17054410; 17178267; 17223085; 17235330; 17329992; 17352764; 17356468; 17391322; 17407229; 17455229; 17465455; 17502835; 17559344; 17638512; 17654295; 17682072; 17885627; 17900275; 17918089; 18004205; 18024866; 18057928; 18090046; 18171905; 18223457; 18281305; 18287571; 18303024; 18332083; 18356043; 18496131; 18621926; 18728241; 18784455; 18839779; 18854779; 18978480; 18979093; 18989234; 19005482; 19029318; 19074885; 19076156; 19106084; 19124658; 19144407; 19218571; 19225447; 19228205; 19239339; 19282874; 19290787; 19343046; 19371316; 19376514; 19414633; 19425200; 19433561; 19464434; 19467232; 19474465; 19474786; 19486190; 19531981; 19593168; 19651758; 19659438; 19682083; 19693007; 19696793; 19702527; 19704172; 19779319; 19797611; 19812066; 19833192; 19916993; 19926050; 19944064; 20017669; 20079471; 20089352; 20096935; 20136364; 20137387; 20173083; 20179710; 20307138; 20338069; 20350955; 20361990; 20418888; 20459744; 20517174; 20529763; 20583967; 20602615; 20610889; 20622021; 20624854; 20625352; 20639527; 20642445; 20662624; 20668445; 20677014; 20696882; 20720517; 20723261; 20734064; 20841522; 20860463; 20861742; 20876786; 20878158; 20881953; 20952238; 20952418; 20966044; 20970553; 21108329; 21156812; 21158011; 21169260; 21486104; 21694616; 21715435; 21741706; 21746968; 21790905; 21821736; 21886015; 22232427; 22281205; 22397853; 22462748; 22471906; 22519658; 22680342; 22685215; 22815312; 22909231; 22936314; 22942317; 22950382; 23238783; 23249875; 23254426; 23288240; 23298916; 23344581; 23418033; 23524664; 23539296; 23550066; 23615745; 23687222; 23746185; 23837472; 24128861 cytochrome P450, family 2, subfamily B, polypeptide 6 Ensembl:ENSG00000197408 HGNC:2615 HPRD:00477 MIM:123930 Vega:OTTHUMG00000182714 Other designations: 1,4-cineole 2-exo-monooxygenase|cytochrome P450 2B6|cytochrome P450 IIB1|cytochrome P450, subfamily IIB (phenobarbital-inducible), polypeptide 6 CYP2B6 OGG:3000001557 Bin Zhao, Yue Liu, Oliver He CPCJ CYP2C P450C2C P450IIC19 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2C19 cytochrome P450, family 2, subfamily C, polypeptide 19 1557 RP11-400G3.4 10q24 9606 10 GO_0004497 (EC: IDA, PMID:19651758); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0008202 (EC: IMP, PMID:18356043); GO_0008395 (EC: IMP, PMID:18356043); GO_0016098 (EC: IDA, PMID:16401082); GO_0016491 (EC: IDA, PMID:16401082); GO_0017144 (EC: IDA, PMID:19219744); GO_0018675 (EC: IEA); GO_0018676 (EC: IEA); GO_0019369 (EC: TAS); GO_0019373 (EC: TAS); GO_0019825 (EC: TAS, PMID:3442670); GO_0019899 (EC: IPI, PMID:15680923); GO_0020037 (EC: IDA); GO_0042738 (EC: IDA, PMID:19029318); GO_0043231 (EC: TAS, PMID:3442670); GO_0044281 (EC: TAS); GO_0046483 (EC: IDA, PMID:19651758); GO_0052741 (EC: IEA); GO_0055114 (EC: IDA, PMID:16401082); GO_0097267 (EC: TAS) PMID:2009263; 3442670; 7704034; 7969038; 8095407; 8110777; 8195181; 8530044; 8647857; 8894508; 9103550; 9398194; 9435198; 9732415; 9890157; 10022751; 10233205; 10411572; 11037802; 11076863; 11207032; 11240980; 11263781; 11372584; 11474773; 11686476; 11713950; 11763000; 11773867; 11785712; 11791894; 11829201; 11836688; 11865668; 11908757; 11927837; 11950794; 11956668; 12047484; 12121503; 12130704; 12142727; 12171978; 12172336; 12222750; 12235924; 12360109; 12386647; 12419832; 12445035; 12464799; 12468438; 12477932; 12496751; 12534411; 12623762; 12642692; 12656699; 12698310; 12732844; 12809821; 12823155; 12835613; 12879168; 12900870; 12900872; 12919183; 12950145; 12963435; 12975335; 13680037; 14520122; 14583683; 14616425; 14634042; 14634838; 14636465; 14653835; 14659971; 14695703; 14990013; 14998561; 15017629; 15025747; 15039299; 15068562; 15090156; 15119530; 15128046; 15145965; 15164054; 15171646; 15177309; 15205367; 15222046; 15248218; 15284537; 15285851; 15301728; 15319333; 15327595; 15349706; 15371981; 15385836; 15385837; 15447734; 15448955; 15469410; 15496639; 15499191; 15569425; 15590749; 15608563; 15612662; 15639978; 15651900; 15660966; 15662508; 15680923; 15691303; 15691505; 15715938; 15752376; 15776277; 15813658; 15842554; 15855721; 15856433; 15903128; 15932363; 15952098; 15963082; 15963095; 15976989; 16006997; 16012079; 16021435; 16024198; 16025294; 16048566; 16116487; 16133961; 16141610; 16183265; 16198656; 16220110; 16231968; 16232205; 16236141; 16239354; 16261363; 16267764; 16268979; 16307177; 16338275; 16338278; 16338280; 16401082; 16413245; 16487224; 16487225; 16595916; 16638864; 16641871; 16740190; 16771603; 16772608; 16783561; 16789993; 16812949; 16815315; 16815316; 16855453; 16862439; 16863547; 16873909; 16890574; 16890578; 16908943; 16911688; 16912869; 16924387; 16937451; 16946555; 16960452; 17003844; 17047431; 17047492; 17048007; 17052843; 17112810; 17178267; 17201743; 17203292; 17215846; 17269966; 17279092; 17290075; 17295875; 17298483; 17304159; 17357148; 17358097; 17377957; 17407229; 17410461; 17417917; 17418993; 17424941; 17433262; 17439410; 17450472; 17455109; 17487889; 17502835; 17504998; 17559380; 17562299; 17623107; 17625515; 17635176; 17635181; 17666363; 17667801; 17667959; 17680025; 17681590; 17697139; 17697203; 17827141; 17868191; 17875119; 17900275; 17909762; 17922881; 17924835; 17934830; 17966194; 17978853; 17992535; 18004210; 18021343; 18024866; 18057705; 18061941; 18154472; 18205890; 18211619; 18214455; 18223462; 18224311; 18231117; 18240903; 18240905; 18241283; 18241287; 18294333; 18312490; 18319058; 18323861; 18346178; 18356043; 18382661; 18394438; 18399167; 18423013; 18425152; 18466100; 18482659; 18496131; 18496682; 18510611; 18511451; 18518848; 18520596; 18520598; 18521743; 18532997; 18551037; 18577829; 18581106; 18637061; 18641551; 18644391; 18654768; 18676680; 18677622; 18702650; 18751689; 18765869; 18781853; 18823430; 18854779; 18854824; 18936436; 18957504; 18979093; 18982321; 18996102; 19002442; 19025845; 19029318; 19033450; 19038035; 19069365; 19074885; 19102714; 19106083; 19106084; 19108880; 19129087; 19136640; 19139162; 19151603; 19156902; 19164093; 19166419; 19169185; 19170196; 19172254; 19176055; 19192051; 19193675; 19193970; 19199010; 19219744; 19220726; 19236548; 19238367; 19246508; 19259653; 19261446; 19268736; 19290787; 19299322; 19336370; 19337788; 19343046; 19348299; 19350405; 19398604; 19404631; 19407662; 19414633; 19415745; 19415824; 19424794; 19429918; 19430176; 19474452; 19496924; 19499406; 19516253; 19531897; 19534586; 19546880; 19552744; 19576320; 19578179; 19583677; 19593158; 19593168; 19617466; 19621685; 19624462; 19625176; 19636337; 19638460; 19651758; 19661214; 19692168; 19693007; 19696793; 19702490; 19706858; 19712984; 19745563; 19751749; 19761366; 19773541; 19817997; 19821196; 19823875; 19840783; 19841156; 19847408; 19881258; 19884907; 19890215; 19891553; 19904250; 19907421; 19926050; 19928008; 19932784; 19933691; 19934793; 19940233; 19942749; 19954515; 19954746; 19956635; 19961004; 19968574; 20002085; 20015960; 20040040; 20064729; 20078610; 20083681; 20088379; 20113968; 20147896; 20163283; 20173083; 20179710; 20206639; 20207952; 20223877; 20235787; 20236133; 20297661; 20309015; 20349052; 20350051; 20350136; 20351750; 20356512; 20358205; 20360782; 20373852; 20376628; 20390258; 20414645; 20430047; 20457439; 20460345; 20468063; 20492431; 20492467; 20492469; 20499227; 20510210; 20528170; 20529763; 20531370; 20533108; 20549256; 20549497; 20559522; 20565970; 20573087; 20581929; 20602612; 20602615; 20620727; 20633187; 20637959; 20650435; 20665013; 20669013; 20673183; 20679960; 20684753; 20708365; 20716239; 20716514; 20724801; 20801494; 20801498; 20804307; 20823393; 20826260; 20831535; 20831536; 20831548; 20833683; 20838991; 20845077; 20845310; 20857895; 20863179; 20885015; 20890775; 20924183; 20926021; 20941486; 20965456; 20970553; 20976881; 20978260; 20979470; 21038076; 21047200; 21054462; 21054464; 21071160; 21075428; 21079055; 21099121; 21108329; 21108610; 21132257; 21152987; 21160212; 21173785; 21192344; 21212520; 21215696; 21237322; 21247447; 21299635; 21302482; 21315147; 21332417; 21358751; 21380557; 21473286; 21497341; 21507170; 21511217; 21511219; 21527445; 21627593; 21628721; 21689142; 21692828; 21741706; 21766908; 21777277; 21778720; 21786436; 21794898; 21795468; 21798861; 21803320; 21806387; 21826689; 21831410; 21861665; 21862109; 21887904; 21913914; 21913948; 21916910; 21971440; 21972404; 21977947; 22007612; 22028352; 22030270; 22045970; 22070512; 22071359; 22088240; 22116003; 22118006; 22122271; 22123356; 22154242; 22180071; 22183943; 22228204; 22281205; 22304323; 22318618; 22324425; 22374717; 22377481; 22418828; 22425806; 22450429; 22469723; 22476388; 22491019; 22552318; 22585284; 22589111; 22591668; 22612904; 22624833; 22641027; 22648560; 22704413; 22747643; 22785462; 22839512; 22855348; 22873740; 22875498; 22875511; 22913530; 22929815; 22955794; 22971905; 22974728; 22984423; 23001453; 23016454; 23074110; 23081704; 23118231; 23148634; 23175667; 23179471; 23193974; 23257377; 23267857; 23337798; 23340030; 23364775; 23412869; 23413279; 23429358; 23469989; 23470885; 23474843; 23506580; 23517020; 23551241; 23555019; 23556336; 23588332; 23607088; 23618682; 23623526; 23640828; 23645039; 23646118; 23700873; 23736997; 23754447; 23755828; 23793025; 23872648; 23874401; 23886632; 23895809; 24015291; 24088005; 24169346; 24501942 cytochrome P450, family 2, subfamily C, polypeptide 19 HGNC:2621 HPRD:00486 MIM:124020 Other designations: (R)-limonene 6-monooxygenase|(S)-limonene 6-monooxygenase|(S)-limonene 7-monooxygenase|CYPIIC17|CYPIIC19|S-mephenytoin 4-hydroxylase|cytochrome P-450 II C|cytochrome P450 2C19|cytochrome P450, subfamily IIC (mephenytoin 4-hydroxylase), polypeptide 19|cytochrome P450-11A|cytochrome P450-254C|flavoprotein-linked monooxygenase|mephenytoin 4'-hydroxylase|mephenytoin 4-hydroxylase|microsomal monooxygenase|xenobiotic monooxygenase CYP2C19 OGG:3000001558 Bin Zhao, Yue Liu, Oliver He CPC8 CYPIIC8 MP-12/MP-20 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2C8 cytochrome P450, family 2, subfamily C, polypeptide 8 1558 10q23.33 9606 10 GO_0004497 (EC: IDA, PMID:19651758); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006082 (EC: IDA, PMID:19651758); GO_0006805 (EC: TAS); GO_0017144 (EC: IDA, PMID:19651758); GO_0019369 (EC: TAS); GO_0019373 (EC: TAS); GO_0020037 (EC: IEA); GO_0034875 (EC: IDA, PMID:18619574); GO_0042738 (EC: IDA, PMID:18619574); GO_0044281 (EC: TAS); GO_0055114 (EC: IDA, PMID:19651758); GO_0070330 (EC: IEA); GO_0070989 (EC: IDA, PMID:18619574); GO_0097267 (EC: TAS) PMID:1707679; 2009263; 2216732; 2729895; 3196692; 3500169; 3697070; 7574697; 7704034; 7841444; 8530044; 8870687; 9586955; 9797707; 9842986; 9890157; 10487415; 10704292; 10768437; 10874126; 11668219; 12429347; 12435384; 12477932; 12756196; 12756206; 12920163; 12936704; 14534525; 14646690; 14676196; 15028279; 15039299; 15074466; 15128046; 15289789; 15319333; 15469410; 15469873; 15606441; 15716363; 15785959; 15864120; 15901749; 15933212; 15961978; 16025294; 16141797; 16164496; 16202848; 16253141; 16299241; 16359408; 16372821; 16385451; 16390351; 16475901; 16538176; 16646575; 16856883; 16957870; 17048007; 17175891; 17178266; 17224914; 17241877; 17373732; 17429317; 17558302; 17627038; 17635176; 17670841; 17701008; 17913794; 17923851; 17925548; 17975119; 18216720; 18303964; 18413310; 18496133; 18548238; 18574320; 18594024; 18619574; 18694831; 18769365; 18779360; 18992346; 19023099; 19064572; 19074885; 19129086; 19143748; 19290787; 19339270; 19343046; 19381162; 19415824; 19460752; 19470925; 19480553; 19504558; 19651758; 19706858; 19761371; 19773535; 19833260; 19913121; 19935798; 19954515; 20013305; 20031551; 20136364; 20173083; 20190184; 20212519; 20214592; 20368717; 20375710; 20379614; 20389299; 20436375; 20437850; 20523106; 20529763; 20602612; 20602615; 20628086; 20665013; 20808793; 20848147; 20857895; 20890775; 20970553; 21047199; 21054465; 21059750; 21081644; 21163940; 21173785; 21214863; 21245287; 21270106; 21375401; 21685474; 21697463; 21697548; 21778352; 21791871; 21798861; 21838784; 21977947; 22027337; 22028317; 22028915; 22242967; 22313047; 22339777; 22491019; 22527101; 22542470; 22625877; 22723340; 23118231; 23171856; 23307233; 23336573; 23413280; 23426382; 23755828 cytochrome P450, family 2, subfamily C, polypeptide 8 Ensembl:ENSG00000138115 HGNC:2622 HPRD:03083 MIM:601129 Vega:OTTHUMG00000018804 Other designations: P450 form 1|cytochrome P450 2C8|cytochrome P450 IIC2|cytochrome P450 MP-12|cytochrome P450 MP-20|cytochrome P450 form 1|cytochrome P450, subfamily IIC (mephenytoin 4-hydroxylase), polypeptide 8|flavoprotein-linked monooxygenase|microsomal monooxygenase|s-mephenytoin 4-hydroxylase|xenobiotic monooxygenase CYP2C8 OGG:3000001559 Bin Zhao, Yue Liu, Oliver He CPC9 CYP2C CYP2C10 CYPIIC9 P450IIC9 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2C9 cytochrome P450, family 2, subfamily C, polypeptide 9 1559 RP11-208C17.6 10q24 9606 10 GO_0004497 (EC: IDA, PMID:19651758); GO_0004497 (EC: NAS, PMID:2827463); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0008144 (EC: IDA, PMID:19448135); GO_0008202 (EC: IMP, PMID:18356043); GO_0008395 (EC: IMP, PMID:18356043); GO_0016098 (EC: IDA, PMID:16401082); GO_0016491 (EC: IDA, PMID:16401082); GO_0017144 (EC: IDA, PMID:19219744); GO_0017144 (EC: IMP); GO_0018675 (EC: IEA); GO_0018676 (EC: IEA); GO_0019369 (EC: TAS); GO_0019373 (EC: TAS); GO_0019627 (EC: IDA, PMID:19029318); GO_0020037 (EC: IEA); GO_0032787 (EC: IDA, PMID:19651758); GO_0034875 (EC: IDA, PMID:18619574); GO_0042737 (EC: IMP, PMID:18356043); GO_0042738 (EC: IDA, PMID:18619574); GO_0043231 (EC: IDA, PMID:9618440); GO_0043231 (EC: TAS, PMID:2827463); GO_0043603 (EC: IDA, PMID:19651758); GO_0044281 (EC: TAS); GO_0052741 (EC: IEA); GO_0055114 (EC: IDA, PMID:16401082); GO_0070989 (EC: IDA, PMID:18619574); GO_0097267 (EC: TAS) PMID:1445376; 1857342; 2009263; 2025243; 2827463; 2963808; 3032244; 3079764; 3196692; 3243766; 3697070; 7704034; 7841444; 8095407; 8215449; 8333835; 8530044; 8809086; 8946475; 9110362; 9398194; 9618440; 9663807; 9890157; 10073515; 10704292; 10739176; 11127854; 11186133; 11298075; 11325819; 11372590; 11397381; 11422024; 11434505; 11455026; 11503012; 11588061; 11678789; 11697742; 11740344; 11833786; 11876753; 11893129; 11908757; 11911968; 11926893; 11950794; 11956512; 11960920; 11991950; 12010835; 12047484; 12152005; 12181452; 12207635; 12235454; 12359989; 12360109; 12406644; 12414349; 12419832; 12426520; 12435384; 12445031; 12451434; 12464247; 12477932; 12496751; 12509498; 12534640; 12559973; 12603175; 12621390; 12634980; 12668916; 12682803; 12698304; 12728288; 12732844; 12734606; 12800253; 12803577; 12805007; 12844136; 12861225; 12879168; 12891229; 12900870; 12913403; 12950145; 14500040; 14504850; 14520122; 14583800; 14614357; 14616425; 14634042; 14634838; 14646690; 14656880; 14661864; 14676821; 14691573; 14691574; 14707031; 14726986; 14739630; 15001971; 15001972; 15005635; 15024534; 15039299; 15048614; 15050794; 15061384; 15066644; 15070684; 15090156; 15100169; 15102864; 15116052; 15116053; 15128046; 15128048; 15145963; 15175798; 15177309; 15197523; 15199455; 15213846; 15222661; 15226678; 15229460; 15248218; 15260906; 15284535; 15284536; 15289788; 15290664; 15369736; 15370961; 15371982; 15385837; 15452553; 15469410; 15536456; 15569425; 15569819; 15588114; 15592327; 15606435; 15606441; 15608560; 15617742; 15632378; 15660966; 15691505; 15714076; 15742978; 15776277; 15790782; 15795654; 15813658; 15824753; 15841315; 15842554; 15855721; 15888487; 15889670; 15896241; 15900281; 15900282; 15919766; 15924351; 15940194; 15947090; 15961979; 15963101; 15970795; 16006997; 16025294; 16082538; 16094537; 16099926; 16111713; 16116487; 16141794; 16141797; 16160068; 16183265; 16187974; 16198655; 16198656; 16202848; 16220110; 16232205; 16236141; 16253141; 16268502; 16297214; 16303885; 16305586; 16305587; 16321620; 16325295; 16338275; 16342679; 16372821; 16385451; 16401082; 16413010; 16424822; 16432637; 16538176; 16541193; 16552506; 16580898; 16595916; 16611750; 16627267; 16630605; 16635054; 16638864; 16639745; 16646575; 16676068; 16699986; 16708125; 16740353; 16749864; 16771603; 16784736; 16797247; 16815313; 16847429; 16847664; 16863464; 16873909; 16878445; 16882880; 16890578; 16924387; 16957870; 16969365; 16985026; 16985032; 17015052; 17048007; 17049586; 17085674; 17110455; 17111199; 17157122; 17167248; 17178267; 17192772; 17201743; 17226852; 17269966; 17279092; 17298483; 17301738; 17304159; 17324110; 17325732; 17329986; 17332144; 17368604; 17391071; 17397249; 17413769; 17418993; 17419358; 17446262; 17460547; 17479200; 17504998; 17510308; 17558303; 17562299; 17572144; 17577464; 17596133; 17596671; 17597710; 17603219; 17627011; 17627038; 17635176; 17635181; 17635185; 17653141; 17681167; 17686967; 17721328; 17764537; 17827141; 17827526; 17849045; 17851566; 17868191; 17895500; 17899045; 17900275; 17955230; 17989110; 18021343; 18024866; 18030307; 18034618; 18034619; 18061941; 18154472; 18183038; 18204476; 18211048; 18216720; 18231117; 18240903; 18240905; 18252229; 18281915; 18303964; 18305455; 18310303; 18315785; 18322281; 18340006; 18356043; 18370846; 18375260; 18378563; 18399713; 18419640; 18425152; 18429757; 18466099; 18480003; 18485885; 18496131; 18496133; 18496682; 18510611; 18511451; 18516070; 18535201; 18542936; 18548238; 18552123; 18559094; 18570163; 18574025; 18597650; 18619574; 18629445; 18662264; 18669935; 18680736; 18681789; 18690342; 18694831; 18698879; 18754001; 18754597; 18756910; 18781852; 18793590; 18816302; 18836275; 18854779; 18855533; 18922023; 18936436; 18950464; 18971529; 18990750; 18992148; 18992263; 18992346; 18996102; 19005461; 19010418; 19018719; 19026171; 19029318; 19031075; 19053752; 19064572; 19074728; 19074885; 19077919; 19082874; 19099951; 19106084; 19117406; 19135231; 19136640; 19139476; 19151603; 19164093; 19177029; 19181737; 19192051; 19199010; 19202563; 19207028; 19219744; 19221727; 19223558; 19225451; 19233181; 19233910; 19258521; 19280158; 19290787; 19297219; 19300499; 19319511; 19324988; 19336370; 19337788; 19339270; 19343046; 19350405; 19369937; 19381162; 19381164; 19387626; 19414633; 19415745; 19415824; 19420105; 19424794; 19448135; 19450127; 19474452; 19480553; 19495518; 19534586; 19538716; 19538885; 19541511; 19541829; 19545555; 19546880; 19567378; 19578179; 19581657; 19593158; 19593168; 19593208; 19604036; 19605743; 19615687; 19617466; 19651758; 19652664; 19663669; 19663817; 19669737; 19692168; 19696793; 19706858; 19736056; 19745563; 19761366; 19794411; 19822571; 19823875; 19833260; 19847408; 19874474; 19881396; 19891553; 19891554; 19899329; 19903527; 19913121; 19925388; 19926050; 19934028; 19934793; 19935798; 19941044; 19942260; 19952982; 19954515; 19956635; 19958090; 19995889; 20020283; 20029944; 20031551; 20043560; 20064729; 20072124; 20073138; 20075209; 20088379; 20089352; 20102361; 20117066; 20121287; 20131310; 20136364; 20147896; 20149073; 20150829; 20167002; 20173083; 20179710; 20204461; 20207952; 20210733; 20226775; 20228265; 20235787; 20297661; 20339191; 20339978; 20351714; 20354686; 20359257; 20373852; 20375710; 20375999; 20376629; 20381283; 20386359; 20390258; 20403997; 20421126; 20430047; 20434758; 20436375; 20437850; 20442691; 20445534; 20453000; 20458343; 20459419; 20459744; 20488169; 20499136; 20504253; 20529763; 20553802; 20555338; 20569971; 20585445; 20585834; 20597268; 20602612; 20602615; 20602621; 20615525; 20628086; 20637959; 20653674; 20653676; 20656072; 20665013; 20677151; 20679960; 20709439; 20716240; 20722625; 20733952; 20808793; 20811787; 20815369; 20831047; 20831536; 20833655; 20833683; 20833980; 20842355; 20845310; 20852447; 20854800; 20857895; 20884456; 20885015; 20930419; 20937634; 20941486; 20946155; 20962433; 20970553; 21044367; 21047199; 21057703; 21063236; 21068649; 21071160; 21108610; 21110192; 21148049; 21160360; 21163940; 21167292; 21173785; 21213107; 21215088; 21248432; 21292004; 21334530; 21371265; 21375401; 21451434; 21493749; 21533175; 21537551; 21544933; 21597400; 21605066; 21638223; 21639946; 21651319; 21691805; 21692828; 21725053; 21757329; 21766908; 21768671; 21786578; 21798861; 21852944; 21861665; 21883387; 21977947; 21985811; 21988832; 22023024; 22075408; 22075505; 22108774; 22188360; 22198820; 22252093; 22272893; 22288731; 22289258; 22290467; 22294058; 22378156; 22393834; 22409277; 22452429; 22528326; 22533669; 22534826; 22542470; 22547083; 22571356; 22589111; 22641027; 22735459; 22808915; 22842957; 22854539; 22855348; 22918969; 22941809; 22952875; 23065265; 23081681; 23081704; 23089473; 23099353; 23113310; 23118231; 23145098; 23159358; 23159639; 23171336; 23183958; 23201087; 23279643; 23376925; 23446815; 23469989; 23473641; 23481074; 23556337; 23563037; 23577132; 23582453; 23586031; 23615745; 23651023; 23726967; 23732294; 23755828; 23774101; 23863877; 23930675 cytochrome P450, family 2, subfamily C, polypeptide 9 Ensembl:ENSG00000138109 HGNC:2623 HPRD:03084 MIM:601130 Vega:OTTHUMG00000018805 Other designations: cytochrome P-450 S-mephenytoin 4-hydroxylase|cytochrome P-450MP|cytochrome P450 2C9|cytochrome P450 PB-1|flavoprotein-linked monooxygenase|microsomal monooxygenase|xenobiotic monooxygenase CYP2C9 OGG:3000001562 Bin Zhao, Yue Liu, Oliver He CPCI CYP2C CYP2C17 P450-6B/29C P450IIC17 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2C18 cytochrome P450, family 2, subfamily C, polypeptide 18 1562 RP11-466J14.4 10q24 9606 10 GO_0004497 (EC: TAS, PMID:8110777); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0019825 (EC: TAS, PMID:8110777); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA) PMID:1306110; 1896026; 2009263; 7704034; 8095407; 8110777; 8125298; 8333835; 9028867; 9154796; 9797707; 9890157; 10487415; 10704292; 10768437; 11093772; 12378636; 12477932; 12694732; 15128046; 15164054; 15302935; 15319333; 15489334; 16359177; 16385451; 17048007; 17207965; 19038035; 19074885; 19204726; 19290787; 19578179; 19706858; 19751749; 19958090; 20045989; 20453000; 20529763; 21163940; 21798861; 21988832; 23755828 cytochrome P450, family 2, subfamily C, polypeptide 18 Ensembl:ENSG00000108242 HGNC:2620 HPRD:03085 MIM:601131 Vega:OTTHUMG00000018796 Other designations: (S)-mephenytoin hydroxylase associated cytochrome P450|CYPIIC18|cytochrome P450 2C18|cytochrome P450, subfamily IIC (mephenytoin 4-hydroxylase), polypeptide 17|cytochrome P450, subfamily IIC (mephenytoin 4-hydroxylase), polypeptide 18|cytochrome P450-6B/29C|flavoprotein-linked monooxygenase|microsomal monooxygenase|unspecific monooxygenase CYP2C18 OGG:3000001565 Bin Zhao, Yue Liu, Oliver He CPD6 CYP2D CYP2D7AP CYP2D7BP CYP2D7P2 CYP2D8P2 CYP2DL1 CYPIID6 P450-DB1 P450C2D P450DB1 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2D6 cytochrome P450, family 2, subfamily D, polypeptide 6 1565 RP4-669P10.2 22q13.1 9606 22 GO_0004497 (EC: IDA, PMID:15327587); GO_0005506 (EC: IEA); GO_0005739 (EC: IDA, PMID:19438707); GO_0005783 (EC: TAS, PMID:19438707); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS, PMID:19438707); GO_0008144 (EC: IDA, PMID:19448135); GO_0008202 (EC: IMP, PMID:18356043); GO_0009804 (EC: IDA, PMID:19438707); GO_0009820 (EC: IDA, PMID:19651758); GO_0009822 (EC: IDA, PMID:15039299); GO_0016098 (EC: IDA, PMID:16401082); GO_0016491 (EC: IDA, PMID:15039299); GO_0017144 (EC: IDA, PMID:19219744); GO_0017144 (EC: IMP, PMID:18356043); GO_0020037 (EC: IDA, PMID:16352597); GO_0033076 (EC: IDA, PMID:19448135); GO_0042737 (EC: IDA, PMID:15039299); GO_0044281 (EC: TAS); GO_0046483 (EC: IDA, PMID:15327587); GO_0051100 (EC: IDA, PMID:19448135); GO_0055114 (EC: IDA, PMID:16401082); GO_0070330 (EC: IEA); GO_0070989 (EC: IDA, PMID:15039299); GO_0090350 (EC: IDA, PMID:19448135) PMID:1673290; 1844820; 1978251; 1978565; 2211621; 2466049; 2574001; 3123997; 3410476; 7845481; 7868129; 7903454; 7927337; 7951238; 8287064; 8449513; 8530011; 8634695; 8655150; 8971426; 9241659; 9264312; 9890157; 10064570; 10233205; 10493260; 10675100; 11037800; 11037802; 11055624; 11097351; 11097352; 11147929; 11204351; 11207030; 11207032; 11214775; 11266079; 11285084; 11291049; 11294012; 11295783; 11303596; 11372584; 11376189; 11422605; 11422615; 11442888; 11470994; 11477317; 11505218; 11505219; 11520401; 11549206; 11560558; 11668217; 11682257; 11702057; 11735606; 11741249; 11750286; 11751440; 11753271; 11753272; 11763000; 11778144; 11791895; 11809184; 11816009; 11829201; 11895912; 11901361; 11927839; 11940091; 12006905; 12063626; 12065557; 12077255; 12089164; 12106691; 12107620; 12142727; 12152006; 12171760; 12171978; 12172215; 12172336; 12175908; 12177686; 12187002; 12191703; 12206675; 12207635; 12210290; 12360109; 12386645; 12386646; 12392820; 12404686; 12419832; 12421483; 12422998; 12426523; 12438554; 12439227; 12446689; 12459840; 12468438; 12477932; 12486288; 12490310; 12503836; 12536989; 12548461; 12569554; 12579870; 12589966; 12610741; 12616663; 12622923; 12629505; 12651805; 12657030; 12691769; 12728976; 12734765; 12743673; 12748560; 12756206; 12756210; 12766554; 12782969; 12784098; 12861292; 12879168; 12879776; 12883230; 12893130; 12900870; 12900872; 12911679; 12915955; 12919180; 12942225; 12950145; 12960748; 12963435; 13680033; 14499311; 14499440; 14514498; 14515061; 14520122; 14557687; 14571354; 14602525; 14624403; 14635107; 14639062; 14640293; 14652703; 14653957; 14658041; 14716707; 14726620; 14726986; 14748763; 14985156; 14991823; 15005635; 15039299; 15048614; 15051713; 15061826; 15068562; 15090156; 15108188; 15115913; 15116051; 15118351; 15128046; 15149890; 15177309; 15205367; 15237854; 15256524; 15260906; 15289790; 15313161; 15319333; 15327587; 15330195; 15349705; 15349706; 15382273; 15461802; 15469410; 15469888; 15470329; 15484318; 15489334; 15499201; 15538128; 15584944; 15588859; 15590749; 15592325; 15618665; 15625333; 15632378; 15646732; 15648054; 15651900; 15669884; 15680923; 15690482; 15691505; 15708542; 15726636; 15729081; 15731591; 15764408; 15768052; 15769360; 15770075; 15774926; 15813658; 15817819; 15820320; 15843230; 15855722; 15861039; 15914211; 15932952; 15952058; 15970126; 15987423; 16006997; 16024198; 16025294; 16037945; 16048566; 16079496; 16130179; 16141609; 16160620; 16162505; 16189709; 16198657; 16205777; 16220080; 16236141; 16239355; 16249913; 16272752; 16283274; 16294366; 16315032; 16337409; 16352597; 16361630; 16401082; 16415111; 16423440; 16459354; 16466686; 16476126; 16478753; 16490169; 16493615; 16534507; 16537246; 16544144; 16550211; 16551910; 16584388; 16595916; 16611538; 16633140; 16633141; 16638736; 16638864; 16642541; 16679388; 16712791; 16716118; 16771603; 16775389; 16778723; 16812949; 16815318; 16819548; 16833023; 16835697; 16845507; 16849011; 16855473; 16858124; 16864175; 16880622; 16924387; 16960721; 17038884; 17089107; 17102541; 17113562; 17115111; 17178267; 17186005; 17194620; 17224713; 17225875; 17234366; 17241532; 17242628; 17244352; 17250723; 17259947; 17270484; 17289397; 17297618; 17301689; 17304721; 17311358; 17324244; 17325735; 17329852; 17361124; 17374963; 17392730; 17418993; 17431033; 17442289; 17449559; 17450472; 17454842; 17460029; 17470523; 17479406; 17503978; 17517247; 17530572; 17536768; 17541883; 17547692; 17554527; 17568504; 17570739; 17573783; 17581325; 17609736; 17610534; 17624022; 17635181; 17635183; 17667795; 17667959; 17697394; 17700359; 17701031; 17713466; 17714084; 17715206; 17725248; 17761971; 17764479; 17803873; 17828532; 17882159; 17908053; 17909762; 17921051; 17947222; 17957765; 17965519; 17965522; 17966194; 17971818; 17992535; 18024866; 18034624; 18048313; 18061941; 18070221; 18075468; 18086475; 18165569; 18167502; 18183034; 18197300; 18202841; 18204346; 18211048; 18214456; 18214849; 18223460; 18231117; 18240905; 18258609; 18261353; 18280655; 18287869; 18294285; 18300942; 18304900; 18317231; 18327668; 18346175; 18346782; 18356043; 18372530; 18382661; 18384443; 18401578; 18407954; 18414197; 18423013; 18425152; 18425996; 18429752; 18433425; 18445827; 18474629; 18474679; 18480698; 18520596; 18520597; 18543297; 18545991; 18547414; 18551040; 18553077; 18583979; 18597648; 18618215; 18625943; 18632250; 18641553; 18648788; 18663559; 18666237; 18676680; 18681789; 18690546; 18698000; 18708991; 18713907; 18719619; 18725510; 18728242; 18754843; 18784265; 18784654; 18794098; 18794105; 18797858; 18818748; 18827765; 18834373; 18840375; 18927241; 18958918; 18978520; 18979093; 18996102; 19000552; 19000940; 19001559; 19019335; 19024387; 19025845; 19032724; 19033450; 19037197; 19047159; 19071885; 19082882; 19094446; 19095219; 19142106; 19151603; 19153830; 19156902; 19162321; 19164093; 19169185; 19170196; 19189210; 19189212; 19192051; 19194367; 19219744; 19219857; 19225771; 19242697; 19284319; 19290787; 19296901; 19303860; 19308365; 19320528; 19330589; 19336370; 19343046; 19350405; 19356055; 19357842; 19364831; 19365402; 19374513; 19387424; 19387994; 19395173; 19405050; 19421167; 19429471; 19437119; 19438707; 19444434; 19448135; 19470220; 19474452; 19512959; 19521114; 19523031; 19527514; 19537956; 19575027; 19593158; 19593168; 19593180; 19593802; 19596663; 19597703; 19604081; 19604084; 19604091; 19625176; 19636337; 19651758; 19652678; 19656108; 19660006; 19692168; 19694742; 19702490; 19710640; 19710642; 19715474; 19719813; 19738170; 19761369; 19781968; 19797609; 19809024; 19823875; 19833260; 19840783; 19866496; 19887477; 19891553; 19892789; 19902987; 19907421; 19910717; 19937844; 19940985; 19946748; 19947517; 19953095; 19954080; 19954746; 19956635; 19995332; 19997080; 20007670; 20009880; 20031551; 20041956; 20075642; 20081063; 20118554; 20124171; 20133509; 20136364; 20137387; 20147896; 20173083; 20174590; 20185366; 20195825; 20201714; 20205348; 20206139; 20225176; 20297661; 20305604; 20309015; 20332423; 20335142; 20350136; 20364044; 20368706; 20373852; 20375710; 20385997; 20421845; 20430047; 20432045; 20435235; 20454926; 20456744; 20459744; 20461808; 20467479; 20473659; 20489028; 20492431; 20515869; 20520586; 20530222; 20531370; 20547595; 20563569; 20565970; 20574415; 20588073; 20590587; 20590588; 20597905; 20599499; 20602615; 20628863; 20634891; 20643254; 20656020; 20656072; 20679960; 20684753; 20686235; 20700584; 20701904; 20727252; 20731819; 20799519; 20809362; 20814331; 20827267; 20828547; 20846929; 20849243; 20851451; 20857895; 20859244; 20863179; 20877299; 20877302; 20878561; 20881950; 20925579; 20970553; 21063774; 21071160; 21072184; 21108610; 21135868; 21140323; 21173786; 21241245; 21248727; 21321564; 21391885; 21430657; 21433154; 21437611; 21449914; 21456632; 21485696; 21486104; 21518482; 21527579; 21543662; 21589866; 21596874; 21599570; 21605066; 21631295; 21677335; 21728792; 21743374; 21749835; 21787170; 21797939; 21803659; 21821735; 21823108; 21826689; 21835244; 21840870; 21860550; 21861665; 21880792; 21907728; 21913948; 21918425; 21956465; 21958961; 21971440; 21989258; 22039821; 22092298; 22109568; 22141351; 22159753; 22180068; 22180372; 22198443; 22216145; 22245658; 22277677; 22281720; 22301406; 22303032; 22308038; 22324840; 22355045; 22398969; 22399238; 22428763; 22459173; 22497725; 22531512; 22623212; 22623266; 22661184; 22688624; 22700965; 22735900; 22775532; 22777153; 22803153; 22905959; 22913530; 22929407; 22948856; 22986607; 22994728; 23167378; 23207012; 23212934; 23213055; 23258538; 23277250; 23280482; 23289191; 23292115; 23350374; 23357843; 23394389; 23469064; 23471717; 23503455; 23552177; 23555934; 23558964; 23570465; 23609392; 23644254; 23664723; 23686417; 23691026; 23700791; 23712329; 23733622; 23734807; 23737191; 23781139; 23803265; 23809878; 23842856; 23851570; 23855716; 23870808; 23872830; 23893861 cytochrome P450, family 2, subfamily D, polypeptide 6 Ensembl:ENSG00000100197 HGNC:2625 HPRD:00487 MIM:124030 Vega:OTTHUMG00000150918 Other designations: cytochrome P450 2D6|cytochrome P450, family 2, subfamily D, polypeptide 7 pseudogene 2|cytochrome P450, family 2, subfamily D, polypeptide 8 pseudogene 2|cytochrome P450, subfamily II (debrisoquine, sparteine, etc., -metabolising), polypeptide 7 pseudogene 2|cytochrome P450, subfamily IID (debrisoquine, sparteine, etc., -metabolising), polypeptide 8 pseudogene 2|cytochrome P450, subfamily IID (debrisoquine, sparteine, etc., -metabolizing), polypeptide 6|cytochrome P450, subfamily IID (debrisoquine, sparteine, etc., -metabolizing)-like 1|cytochrome P450-DB1|debrisoquine 4-hydroxylase|flavoprotein-linked monooxygenase|microsomal monooxygenase|xenobiotic monooxygenase CYP2D6 OGG:3000001571 Bin Zhao, Yue Liu, Oliver He CPE1 CYP2E P450-J P450C2E WEB: http://www.ncbi.nlm.nih.gov/gene CYP2E1 cytochrome P450, family 2, subfamily E, polypeptide 1 1571 10q26.3 9606 10 GO_0000139 (EC: IEA); GO_0004497 (EC: IDA, PMID:19651758); GO_0005506 (EC: IEA); GO_0005739 (EC: IEA); GO_0005789 (EC: TAS); GO_0006641 (EC: IEA); GO_0006805 (EC: TAS); GO_0008202 (EC: IMP, PMID:18356043); GO_0010193 (EC: IEA); GO_0010243 (EC: IEA); GO_0016098 (EC: IDA, PMID:16401082); GO_0016491 (EC: IDA, PMID:16401082); GO_0016709 (EC: TAS, PMID:18818195); GO_0016712 (EC: IEA); GO_0017144 (EC: IDA, PMID:19219744); GO_0017144 (EC: IMP, PMID:18356043); GO_0019825 (EC: TAS, PMID:3233219); GO_0019899 (EC: IPI, PMID:15680923); GO_0020037 (EC: IDA, PMID:18818195); GO_0031227 (EC: IEA); GO_0042493 (EC: IEA); GO_0044281 (EC: TAS); GO_0045471 (EC: IEA); GO_0046483 (EC: IDA, PMID:19651758); GO_0055114 (EC: IDA, PMID:16401082) PMID:1719479; 1778977; 2587619; 3233219; 3675576; 3782137; 7529759; 7733943; 7773503; 8031147; 8307581; 8809087; 9058590; 9129165; 9398194; 9834965; 9890157; 9918138; 10620320; 10731522; 10741631; 11051375; 11104220; 11191882; 11198676; 11207032; 11236836; 11259352; 11263781; 11275366; 11305777; 11331106; 11377232; 11389775; 11406608; 11410713; 11422615; 11503278; 11520401; 11535247; 11535253; 11641039; 11675150; 11696658; 11697456; 11700262; 11701230; 11719088; 11746208; 11748356; 11751440; 11756225; 11766168; 11774269; 11776598; 11782477; 11798822; 11802217; 11815398; 11854903; 11869835; 11895912; 11907164; 11911601; 11960914; 11964928; 11966948; 12010862; 12047484; 12055050; 12063626; 12080432; 12115524; 12172927; 12198369; 12211622; 12351530; 12355548; 12365037; 12376502; 12376511; 12397416; 12403788; 12452057; 12454736; 12460800; 12469218; 12477932; 12490624; 12540498; 12548461; 12552594; 12554615; 12561466; 12563175; 12569554; 12579334; 12601351; 12668988; 12705718; 12707490; 12710951; 12718576; 12718671; 12721789; 12732844; 12738724; 12739102; 12759747; 12760253; 12767509; 12771559; 12774019; 12777398; 12777962; 12777965; 12813050; 12824748; 12824892; 12851035; 12860273; 12883487; 12883749; 12915519; 12939804; 12940444; 12960506; 14499622; 14500779; 14510941; 14527082; 14535982; 14578150; 14606109; 14634838; 14646291; 14661969; 14669323; 14681495; 14691069; 14695651; 14695664; 14696128; 14751678; 14757192; 14991750; 15036355; 15039299; 15061915; 15064998; 15066574; 15112335; 15125228; 15128046; 15138035; 15162526; 15177663; 15182482; 15215328; 15220553; 15226677; 15289170; 15318112; 15327835; 15349722; 15355699; 15370874; 15469410; 15491310; 15519646; 15532721; 15536330; 15632182; 15633127; 15640066; 15646021; 15660387; 15680923; 15712341; 15714076; 15734972; 15753073; 15763499; 15769360; 15774926; 15780023; 15793883; 15849806; 15899651; 15902904; 15914211; 15914277; 15928955; 15938845; 15952134; 15961886; 15968714; 15991278; 16006997; 16019049; 16039674; 16043197; 16052683; 16125881; 16126235; 16137184; 16142352; 16172237; 16235983; 16235992; 16253141; 16311924; 16324524; 16337880; 16365683; 16372174; 16380384; 16385451; 16393248; 16401082; 16424825; 16425414; 16440362; 16459354; 16470306; 16471212; 16484137; 16488179; 16497268; 16535827; 16551616; 16600530; 16634857; 16679316; 16720291; 16721740; 16758119; 16770646; 16834659; 16837478; 16841220; 16962935; 16985026; 16985032; 17007050; 17016589; 17022435; 17034788; 17059334; 17078101; 17118447; 17119198; 17119944; 17134659; 17146594; 17156750; 17176083; 17178637; 17219769; 17264406; 17284772; 17292341; 17331164; 17361553; 17367411; 17373732; 17380320; 17384900; 17427487; 17440116; 17442289; 17486761; 17498780; 17559142; 17564586; 17577619; 17584020; 17603900; 17611777; 17617119; 17627011; 17659824; 17695473; 17885617; 17916905; 17935737; 17950035; 17963298; 17996038; 18025800; 18028774; 18034693; 18056994; 18211048; 18218609; 18231117; 18258609; 18261353; 18304215; 18322963; 18327668; 18356043; 18369917; 18418580; 18420361; 18423013; 18446064; 18460770; 18466102; 18472009; 18473182; 18497573; 18507060; 18510611; 18544910; 18550589; 18569579; 18569587; 18569591; 18628434; 18636124; 18642288; 18645668; 18663376; 18676680; 18698632; 18713495; 18715838; 18726416; 18769766; 18773092; 18798002; 18798003; 18801337; 18818195; 18936436; 18990750; 18992148; 19012698; 19058336; 19064572; 19074885; 19096130; 19115622; 19124503; 19131562; 19157621; 19157724; 19170196; 19190172; 19219744; 19230487; 19250143; 19267064; 19288740; 19290787; 19334053; 19336370; 19339548; 19343046; 19351467; 19357030; 19381774; 19382518; 19390575; 19428381; 19442564; 19481674; 19484729; 19489076; 19492240; 19506726; 19521675; 19528831; 19537956; 19575027; 19625176; 19643819; 19651758; 19655364; 19686770; 19692168; 19706845; 19751749; 19761367; 19786980; 19789190; 19796841; 19805575; 19822571; 19826048; 19860798; 19874574; 19887496; 19891553; 19913121; 19927646; 19948975; 19956635; 19958676; 19963114; 19963139; 20026093; 20029944; 20031389; 20093049; 20095411; 20100563; 20100738; 20101753; 20102722; 20117323; 20131310; 20171022; 20173083; 20180013; 20195803; 20364586; 20392357; 20394984; 20401433; 20404016; 20406102; 20426969; 20437058; 20453000; 20463018; 20511665; 20529763; 20554493; 20556843; 20576306; 20598484; 20602615; 20628086; 20634891; 20637790; 20661821; 20663217; 20675267; 20692331; 20715111; 20819434; 20932821; 20939108; 20941486; 20957336; 20958328; 20969746; 21072184; 21076874; 21209460; 21228414; 21261721; 21265876; 21281483; 21295098; 21360299; 21385088; 21553050; 21557999; 21590276; 21705789; 21729529; 21745589; 21856753; 21869556; 21895718; 21988832; 22012226; 22077825; 22088806; 22109568; 22126492; 22155602; 22156006; 22222162; 22228187; 22230367; 22238121; 22249978; 22251540; 22335459; 22342293; 22384697; 22392284; 22436864; 22442693; 22485222; 22506592; 22589738; 22591346; 22606226; 22613106; 22614694; 22761909; 22788240; 22807108; 22815852; 22954124; 22957075; 22997752; 23007992; 23066397; 23077626; 23104821; 23124075; 23131254; 23139769; 23186213; 23193974; 23193996; 23244081; 23251661; 23335995; 23355335; 23363738; 23394127; 23404349; 23418369; 23454624; 23460870; 23471973; 23530020; 23534720; 23583009; 23595220; 23628324; 23632049; 23636797; 23660503; 23707663; 23875638; 23886179; 23934444; 24113184; 24333271 cytochrome P450, family 2, subfamily E, polypeptide 1 Ensembl:ENSG00000130649 HGNC:2631 HPRD:11813 MIM:124040 Vega:OTTHUMG00000019322 Other designations: 4-nitrophenol 2-hydroxylase|CYPIIE1|cytochrome P450 2E1|cytochrome P450, subfamily IIE (ethanol-inducible), polypeptide 1|cytochrome P450-J|flavoprotein-linked monooxygenase|microsomal monooxygenase|xenobiotic monooxygenase CYP2E1 OGG:3000001572 Bin Zhao, Yue Liu, Oliver He C2F1 CYP2F WEB: http://www.ncbi.nlm.nih.gov/gene CYP2F1 cytochrome P450, family 2, subfamily F, polypeptide 1 1572 19q13.2 9606 19 GO_0004497 (EC: TAS, PMID:1974816); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0009636 (EC: IEA); GO_0016712 (EC: IDA, PMID:10383923); GO_0018931 (EC: IDA, PMID:10383923); GO_0018979 (EC: IEA); GO_0019825 (EC: IEA); GO_0020037 (EC: IEA); GO_0043231 (EC: IDA, PMID:10383923); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA) PMID:1974816; 2045106; 8432525; 8587134; 8619884; 9539103; 10383923; 11827709; 12477932; 12598524; 15128046; 16883522; 17327131; 17943660; 19343046; 20198857; 22232929; 22397853 cytochrome P450, family 2, subfamily F, polypeptide 1 Ensembl:ENSG00000197446 HGNC:2632 HPRD:00490 MIM:124070 Vega:OTTHUMG00000167412 Other designations: CYPIIF1|cytochrome P450 2F1|cytochrome P450, subfamily IIF, polypeptide 1|flavoprotein-linked monooxygenase|microsomal monooxygenase|xenobiotic monooxygenase CYP2F1 OGG:3000001573 Bin Zhao, Yue Liu, Oliver He CPJ2 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2J2 cytochrome P450, family 2, subfamily J, polypeptide 2 1573 1p31.3-p31.2 9606 1 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006690 (EC: TAS, PMID:8631948); GO_0006805 (EC: TAS, PMID:11901223); GO_0008016 (EC: TAS, PMID:8631948); GO_0008392 (EC: IDA, PMID:11901223); GO_0008404 (EC: IDA, PMID:11901223); GO_0008405 (EC: IDA, PMID:11901223); GO_0019369 (EC: TAS); GO_0019373 (EC: IDA, PMID:11901223); GO_0019373 (EC: TAS); GO_0020037 (EC: IEA); GO_0043651 (EC: IDA, PMID:11901223); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA); GO_0071614 (EC: IDA, PMID:11901223) PMID:8631948; 8913342; 9048644; 9187259; 9570962; 10065373; 10405341; 10681399; 10828211; 11901223; 12386130; 12477932; 12737630; 14575523; 14702039; 15128046; 15256482; 15361551; 15466638; 15489334; 15861034; 15864120; 16008525; 16182271; 16202848; 16842392; 16957870; 17126841; 17162467; 17286575; 17327508; 17429317; 17470359; 17475630; 17638876; 17705402; 17979511; 18004755; 18216721; 18219097; 18303964; 18496133; 18675280; 18729130; 18769365; 19105833; 19290787; 19420105; 19448409; 19550113; 19576320; 19578796; 19615687; 19823578; 19851119; 19913121; 19923256; 20140850; 20173083; 20379614; 20480811; 20597138; 20628086; 21030485; 21059750; 21642892; 21988832; 22028915; 22232929; 22731644; 22761738; 23155181; 23647230; 23661295; 23684773; 23696562 cytochrome P450, family 2, subfamily J, polypeptide 2 Ensembl:ENSG00000134716 HGNC:2634 HPRD:03159 MIM:601258 Vega:OTTHUMG00000008991 Other designations: CYPIIJ2|arachidonic acid epoxygenase|cytochrome P450 2J2|cytochrome P450, subfamily IIJ (arachidonic acid epoxygenase) polypeptide 2|flavoprotein-linked monooxygenase|microsomal monooxygenase CYP2J2 OGG:3000001576 Bin Zhao, Yue Liu, Oliver He CP33 CP34 CYP3A CYP3A3 CYPIIIA3 CYPIIIA4 HLP NF-25 P450C3 P450PCN1 WEB: http://www.ncbi.nlm.nih.gov/gene CYP3A4 cytochrome P450, family 3, subfamily A, polypeptide 4 1576 7q21.1 9606 7 GO_0004497 (EC: IDA, PMID:15327587); GO_0004497 (EC: ISS); GO_0005496 (EC: IDA, PMID:15256616); GO_0005506 (EC: IDA, PMID:15256616); GO_0005737 (EC: IDA, PMID:18446064); GO_0005789 (EC: TAS); GO_0006629 (EC: TAS, PMID:2492107); GO_0006706 (EC: IMP, PMID:18356043); GO_0006805 (EC: TAS); GO_0008202 (EC: IMP, PMID:3259858); GO_0008209 (EC: TAS, PMID:19651758); GO_0008395 (EC: IMP, PMID:18356043); GO_0009822 (EC: IDA, PMID:15039299); GO_0016021 (EC: IEA); GO_0016098 (EC: IDA, PMID:16401082); GO_0016491 (EC: IDA, PMID:15039299); GO_0016712 (EC: IEA); GO_0017144 (EC: IDA, PMID:15327587); GO_0019825 (EC: TAS, PMID:2492107); GO_0019899 (EC: IPI, PMID:15680923); GO_0020037 (EC: IEA); GO_0030343 (EC: IDA, PMID:15546903); GO_0033780 (EC: IEA); GO_0034875 (EC: IDA, PMID:18619574); GO_0036378 (EC: IDA, PMID:15546903); GO_0042359 (EC: IC, PMID:15546903); GO_0042737 (EC: IDA, PMID:15039299); GO_0042737 (EC: IMP, PMID:18356043); GO_0042738 (EC: IDA, PMID:18619574); GO_0043231 (EC: TAS, PMID:3460094); GO_0044281 (EC: TAS); GO_0046483 (EC: IDA, PMID:15327587); GO_0047638 (EC: IEA); GO_0050591 (EC: IEA); GO_0050649 (EC: IMP, PMID:3259858); GO_0055114 (EC: IDA, PMID:16401082); GO_0070576 (EC: IDA, PMID:15546903); GO_0070989 (EC: IDA, PMID:15039299) PMID:1391968; 2463251; 2492107; 3243766; 3259858; 3267210; 3460094; 3464943; 3898085; 8269949; 9088578; 9394023; 9456308; 9890157; 10222036; 10322772; 10668853; 10933049; 11051261; 11067821; 11137287; 11161840; 11181494; 11266076; 11470997; 11549683; 11714865; 11726664; 11745731; 11749050; 11782366; 11809184; 11875366; 11876753; 11890939; 11907494; 11940601; 11956645; 11991950; 12072427; 12107441; 12130689; 12142725; 12147248; 12151999; 12202670; 12419838; 12439220; 12446983; 12464248; 12477932; 12485945; 12493773; 12532467; 12569554; 12623762; 12644831; 12690205; 12692107; 12695546; 12732844; 12738724; 12747609; 12756206; 12756210; 12809821; 12867495; 12900870; 12900872; 12960109; 12966368; 12969965; 12975335; 14504207; 14515058; 14515059; 14580164; 14640293; 14643022; 14660173; 14681232; 14690448; 14693733; 14697480; 14742674; 15039299; 15114431; 15128046; 15256616; 15258162; 15260917; 15277015; 15307840; 15319333; 15327587; 15334674; 15365656; 15370963; 15379787; 15454728; 15459178; 15462611; 15469410; 15475069; 15496535; 15496639; 15523087; 15540736; 15546903; 15548719; 15592326; 15611481; 15618745; 15622315; 15634941; 15650881; 15680923; 15684873; 15698606; 15707415; 15708356; 15708542; 15713537; 15731117; 15770073; 15770075; 15778453; 15801936; 15817670; 15820320; 15882469; 15896485; 15900215; 15900284; 15901749; 15931768; 15932952; 15981231; 16004554; 16006997; 16059671; 16079101; 16103451; 16109480; 16130011; 16146556; 16172230; 16207150; 16243813; 16267764; 16299241; 16306861; 16314882; 16321621; 16324277; 16338276; 16344560; 16401082; 16414488; 16434211; 16467307; 16507515; 16538176; 16580902; 16608838; 16633141; 16645157; 16684709; 16711396; 16758258; 16765145; 16771603; 16842392; 16862439; 16890574; 16890579; 16906020; 16909599; 16924387; 16954191; 16981844; 16985250; 17007050; 17014074; 17015051; 17042920; 17047492; 17065585; 17083953; 17118447; 17119944; 17162468; 17178267; 17200113; 17220347; 17224914; 17270371; 17279585; 17296590; 17352764; 17357589; 17363580; 17364054; 17367411; 17372239; 17373732; 17392393; 17409981; 17418993; 17429319; 17433262; 17434921; 17460031; 17460547; 17465708; 17495874; 17495878; 17495880; 17498886; 17502835; 17526062; 17526937; 17545536; 17548528; 17548691; 17555301; 17582393; 17601520; 17605821; 17609736; 17615053; 17622974; 17624028; 17634410; 17635182; 17691855; 17697139; 17701008; 17704997; 17724065; 17764444; 17766366; 17827338; 17827444; 17854673; 17880367; 17900275; 17912464; 17918187; 17919092; 17919884; 17922881; 17925385; 17925548; 17952011; 17965521; 17974099; 17985934; 17992531; 18004209; 18004210; 18021343; 18028890; 18052847; 18058330; 18092806; 18097620; 18163429; 18192894; 18211048; 18217151; 18223457; 18231117; 18240903; 18258609; 18268015; 18294295; 18294936; 18309947; 18332045; 18348473; 18356043; 18364084; 18382661; 18385010; 18394438; 18408564; 18431572; 18433425; 18446064; 18496131; 18509327; 18518855; 18528690; 18551040; 18566991; 18569587; 18619574; 18632753; 18636247; 18669585; 18688081; 18704002; 18768784; 18781853; 18784074; 18794335; 18825162; 18854779; 18936436; 18957504; 18976975; 18978522; 18979093; 18981009; 18981011; 18989234; 18996102; 19005401; 19020497; 19027952; 19064572; 19070657; 19074750; 19076156; 19077426; 19103148; 19127255; 19143748; 19206087; 19214745; 19219744; 19225447; 19228205; 19228751; 19232333; 19239339; 19242060; 19258929; 19282874; 19332043; 19337788; 19339270; 19343046; 19343062; 19343327; 19349540; 19350405; 19356113; 19376514; 19395426; 19406954; 19414505; 19420105; 19424794; 19433561; 19451401; 19453261; 19460945; 19470925; 19474452; 19480557; 19505920; 19506580; 19538885; 19546880; 19560436; 19571438; 19574343; 19575027; 19576320; 19591893; 19626470; 19636001; 19651758; 19659438; 19667110; 19692168; 19696793; 19712670; 19727863; 19752211; 19761365; 19762492; 19773538; 19784640; 19797609; 19801957; 19802823; 19812066; 19823875; 19833260; 19842932; 19846565; 19865079; 19907160; 19913121; 19921206; 19926050; 19934400; 19934793; 19937844; 19956635; 19963139; 20007670; 20012430; 20017669; 20027111; 20031551; 20038391; 20068078; 20088394; 20118548; 20136364; 20147837; 20147896; 20171174; 20173083; 20212519; 20213484; 20214802; 20218903; 20235787; 20338069; 20350051; 20350136; 20354687; 20361990; 20386561; 20389299; 20395213; 20403997; 20437850; 20453000; 20459744; 20490798; 20505544; 20523106; 20526235; 20529763; 20530282; 20538049; 20538721; 20578904; 20583967; 20588308; 20602612; 20602615; 20604570; 20615193; 20617557; 20621111; 20625352; 20628086; 20630055; 20634197; 20642445; 20654748; 20656072; 20679960; 20682687; 20697309; 20715157; 20734064; 20809279; 20812728; 20833683; 20841961; 20847137; 20849814; 20861742; 20863320; 20879989; 20884258; 20931330; 20951982; 20959500; 20970553; 21047202; 21063236; 21071160; 21072155; 21072184; 21081028; 21081644; 21114969; 21169260; 21177853; 21186373; 21199372; 21207936; 21209460; 21223952; 21292004; 21342487; 21380731; 21402137; 21402692; 21412247; 21433154; 21471209; 21493872; 21513075; 21566342; 21605066; 21692828; 21750466; 21767526; 21798277; 21835977; 21838784; 21863748; 21886157; 21902501; 21902502; 21903774; 21916909; 21925256; 21940338; 21952236; 21963990; 21964586; 21988832; 21992114; 21996064; 21998292; 22050110; 22076448; 22094027; 22096084; 22101235; 22106171; 22108774; 22157006; 22194603; 22277676; 22292071; 22333269; 22369694; 22388796; 22472546; 22510778; 22517972; 22562045; 22617232; 22621802; 22645092; 22677141; 22696420; 22699155; 22728071; 22741198; 22763214; 22773874; 22885098; 22906825; 22945461; 22971138; 22985909; 22990330; 22993851; 23090875; 23107770; 23129512; 23143891; 23146479; 23160340; 23162896; 23179402; 23212742; 23217392; 23223499; 23252948; 23264496; 23277250; 23290512; 23295386; 23313934; 23320986; 23334403; 23361102; 23400261; 23436703; 23459029; 23469989; 23491640; 23510058; 23527115; 23530020; 23557865; 23574760; 23640974; 23665933; 23715232; 23732298; 23746300; 23780963; 23837477; 23965431; 23977680; 24256945; 24273886 cytochrome P450, family 3, subfamily A, polypeptide 4 HGNC:2637 HPRD:00484 MIM:124010 Other designations: 1,8-cineole 2-exo-monooxygenase|P450-III, steroid inducible|albendazole monooxygenase|albendazole sulfoxidase|cytochrome P450 3A3|cytochrome P450 3A4|cytochrome P450 HLp|cytochrome P450 NF-25|cytochrome P450, subfamily IIIA (niphedipine oxidase), polypeptide 3|cytochrome P450, subfamily IIIA (niphedipine oxidase), polypeptide 4|cytochrome P450-PCN1|glucocorticoid-inducible P450|nifedipine oxidase|quinine 3-monooxygenase|taurochenodeoxycholate 6-alpha-hydroxylase CYP3A4 OGG:3000001577 Bin Zhao, Yue Liu, Oliver He CP35 CYPIIIA5 P450PCN3 PCN3 WEB: http://www.ncbi.nlm.nih.gov/gene CYP3A5 cytochrome P450, family 3, subfamily A, polypeptide 5 1577 7q21.1 9606 7 GO_0004497 (EC: ISS); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0008202 (EC: TAS, PMID:2732228); GO_0009822 (EC: IDA, PMID:15039299); GO_0016491 (EC: IDA, PMID:15039299); GO_0019825 (EC: TAS, PMID:2732228); GO_0020037 (EC: IEA); GO_0042737 (EC: IDA, PMID:15039299); GO_0043231 (EC: TAS, PMID:2732228); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA); GO_0070989 (EC: IDA, PMID:15039299) PMID:2732228; 2802615; 7750548; 7811260; 7883227; 7894497; 7895614; 8004129; 8125298; 8569713; 8619878; 8619884; 8694864; 8869826; 8877031; 8889549; 8946469; 9070608; 9364212; 9797707; 9890157; 10069460; 10403825; 11137287; 11266076; 11279519; 11502729; 11726664; 11740341; 11809184; 11836601; 12042671; 12202670; 12242601; 12324482; 12433824; 12439220; 12477932; 12690205; 12692107; 12694732; 12754175; 12756511; 12814460; 12822676; 12853948; 12893984; 12960109; 12966368; 12969965; 12975492; 14504207; 14515058; 14515059; 14647405; 14676821; 14702039; 14747421; 14961555; 15039299; 15114431; 15116055; 15128046; 15167702; 15226679; 15248218; 15252010; 15284534; 15289787; 15319333; 15385835; 15454734; 15469410; 15489334; 15502717; 15548719; 15592326; 15596297; 15596575; 15622315; 15632378; 15634941; 15698606; 15707415; 15708542; 15729180; 15801936; 15808586; 15814280; 15833928; 15876487; 15882469; 15900215; 15900284; 15919447; 15931768; 15952872; 15961978; 15978331; 15981231; 16004554; 16024008; 16086282; 16116487; 16141800; 16160620; 16168193; 16172230; 16188140; 16207150; 16243813; 16249748; 16253141; 16267764; 16272171; 16272955; 16299241; 16306861; 16314882; 16321621; 16338276; 16361630; 16421475; 16424824; 16442753; 16513443; 16584389; 16595916; 16612255; 16612333; 16614106; 16628701; 16638864; 16684709; 16765145; 16765147; 16769602; 16771603; 16772608; 16791115; 16815317; 16822233; 16827636; 16842392; 16847425; 16906018; 16906020; 17015051; 17032130; 17042920; 17047492; 17048977; 17049058; 17049128; 17162466; 17178265; 17178267; 17192506; 17192769; 17198275; 17224914; 17244352; 17264302; 17286792; 17296590; 17329995; 17339868; 17352764; 17358097; 17363580; 17372036; 17373732; 17377957; 17391324; 17395652; 17425754; 17430486; 17443134; 17450472; 17460031; 17495880; 17495881; 17502835; 17510208; 17517050; 17545536; 17554244; 17568575; 17582393; 17605821; 17615053; 17635176; 17635181; 17635182; 17691921; 17700595; 17701008; 17761709; 17827141; 17851225; 17875118; 17885626; 17900275; 17914095; 17922881; 17925548; 17941052; 17979504; 17979523; 17992026; 18021343; 18024866; 18028890; 18058330; 18192894; 18211618; 18212618; 18214455; 18221820; 18223457; 18240903; 18248681; 18294295; 18300941; 18306354; 18309947; 18315786; 18315894; 18319058; 18322448; 18334918; 18382661; 18385010; 18385991; 18394438; 18408564; 18414696; 18429967; 18443548; 18490434; 18496128; 18496131; 18502461; 18509327; 18509328; 18509645; 18518855; 18551040; 18566991; 18582803; 18587567; 18589174; 18597650; 18603015; 18628519; 18636247; 18641551; 18650247; 18688081; 18704002; 18708991; 18727922; 18752284; 18930278; 18936931; 18978522; 18979093; 18981009; 18989234; 18996102; 19005401; 19005461; 19010156; 19033450; 19034006; 19040121; 19064572; 19067682; 19074750; 19076156; 19106083; 19106084; 19114346; 19125240; 19139162; 19141860; 19205682; 19225447; 19228205; 19228751; 19229255; 19239339; 19258929; 19289993; 19290787; 19290795; 19332043; 19337788; 19343046; 19343327; 19349540; 19350405; 19376366; 19376514; 19384171; 19384264; 19414505; 19414633; 19424794; 19470925; 19474452; 19506580; 19516253; 19523815; 19538885; 19545678; 19546880; 19576320; 19584153; 19591893; 19593168; 19636001; 19644155; 19650988; 19659438; 19663817; 19667110; 19693007; 19696793; 19710077; 19730841; 19744012; 19761365; 19762492; 19801957; 19812606; 19817997; 19823770; 19842932; 19855314; 19865079; 19881258; 19904021; 19907160; 19913121; 19916993; 19925383; 19934793; 19946748; 20010459; 20017669; 20030680; 20031551; 20038391; 20040338; 20041908; 20118548; 20133509; 20136364; 20147896; 20160155; 20172323; 20173083; 20179710; 20207952; 20212519; 20214802; 20218903; 20231858; 20235787; 20332423; 20345875; 20354687; 20357698; 20368718; 20383212; 20389299; 20393454; 20395213; 20403997; 20415563; 20430047; 20453000; 20459744; 20479955; 20490798; 20514078; 20526235; 20529763; 20530282; 20565970; 20588203; 20596503; 20602615; 20615193; 20617557; 20621111; 20625352; 20628086; 20630055; 20662624; 20679960; 20696882; 20716514; 20720558; 20818295; 20833683; 20846929; 20860463; 20873239; 20881953; 20931330; 20959405; 20959500; 20970553; 20970601; 20970628; 20970643; 21039054; 21047202; 21072155; 21072184; 21076384; 21081028; 21094057; 21094796; 21094797; 21148251; 21153923; 21165655; 21173786; 21206424; 21209234; 21225912; 21237140; 21265876; 21380731; 21389905; 21418106; 21434577; 21436775; 21493872; 21513075; 21519338; 21544031; 21644845; 21677300; 21698374; 21711429; 21743379; 21770725; 21806386; 21814220; 21839244; 21851254; 21896346; 21916909; 21950641; 21988832; 22007612; 22022918; 22096084; 22210422; 22214815; 22277678; 22292071; 22304537; 22369694; 22511346; 22610055; 22645092; 22696420; 22704849; 22819265; 22875663; 22889968; 22923690; 22993851; 23023417; 23073208; 23107770; 23131698; 23143606; 23143891; 23146466; 23146479; 23149441; 23223499; 23320986; 23354298; 23364483; 23385102; 23432535; 23459029; 23491640; 23557865; 23584898; 23633119; 23700791; 23715232; 23723360; 23734777; 23780963; 23837476; 23845965; 23873120; 23984379 cytochrome P450, family 3, subfamily A, polypeptide 5 Ensembl:ENSG00000106258 HGNC:2638 HPRD:05617 MIM:605325 Vega:OTTHUMG00000156724 Other designations: aryl hydrocarbon hydroxylase|cytochrome P450 3A5|cytochrome P450 HLp2|cytochrome P450, subfamily IIIA (niphedipine oxidase), polypeptide 5|cytochrome P450-PCN3|flavoprotein-linked monooxygenase|microsomal monooxygenase|xenobiotic monooxygenase CYP3A5 OGG:3000001579 Bin Zhao, Yue Liu, Oliver He CP4Y CYP4A2 CYP4AII WEB: http://www.ncbi.nlm.nih.gov/gene CYP4A11 cytochrome P450, family 4, subfamily A, polypeptide 11 1579 1p33 9606 1 GO_0001676 (EC: IDA, PMID:18433732); GO_0003091 (EC: IEP, PMID:10660572); GO_0003095 (EC: IEP, PMID:10660572); GO_0005506 (EC: IEA); GO_0005737 (EC: IDA, PMID:10660572); GO_0005789 (EC: TAS); GO_0006631 (EC: TAS, PMID:7679927); GO_0006691 (EC: IDA, PMID:9799565); GO_0006805 (EC: TAS); GO_0008392 (EC: IDA, PMID:9618440); GO_0016324 (EC: IDA, PMID:10660572); GO_0018685 (EC: IDA, PMID:18433732); GO_0019369 (EC: IDA, PMID:10660572); GO_0019369 (EC: TAS); GO_0019373 (EC: IDA, PMID:9618440); GO_0020037 (EC: IEA); GO_0032305 (EC: IMP, PMID:18391101); GO_0036101 (EC: IDA, PMID:9799565); GO_0043231 (EC: IDA, PMID:10660572); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0050051 (EC: IDA, PMID:9799565); GO_0052869 (EC: IEA); GO_0055078 (EC: IEP, PMID:10660572); GO_0055114 (EC: IDA, PMID:18433732); GO_0097267 (EC: TAS) PMID:1739747; 7679927; 7798189; 8274222; 8363569; 8914854; 9618440; 9799565; 10024026; 10660572; 10860550; 11139583; 11736898; 11821421; 12464261; 12464262; 12477932; 15028279; 15128046; 15319333; 15611369; 16144986; 16957555; 18227405; 18300855; 18385420; 18391101; 18433732; 18484194; 18574070; 18624398; 18660489; 18936345; 19343046; 19366684; 19615687; 19898482; 20130494; 21326303; 21617944; 21820496; 21873888; 21886157; 21912424; 22327816; 22804341; 23085321 cytochrome P450, family 4, subfamily A, polypeptide 11 Ensembl:ENSG00000187048 HGNC:2642 HPRD:03201 MIM:601310 Vega:OTTHUMG00000008020 Other designations: 20-HETE synthase|20-hydroxyeicosatetraenoic acid synthase|CYPIVA11|P450HL-omega|alkane-1 monooxygenase|cytochrome P-450HK-omega|cytochrome P450 4A11|cytochrome P450, subfamily IVA, polypeptide 11|cytochrome P450HL-omega|fatty acid omega-hydroxylase|lauric acid omega-hydroxylase CYP4A11 OGG:3000001580 Bin Zhao, Yue Liu, Oliver He CYPIVB1 P-450HP WEB: http://www.ncbi.nlm.nih.gov/gene CYP4B1 cytochrome P450, family 4, subfamily B, polypeptide 1 1580 RP4-732G19.1 1p33 9606 1 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0008144 (EC: IEA); GO_0018585 (EC: IEA); GO_0018879 (EC: IEA); GO_0018917 (EC: IEA); GO_0019825 (EC: TAS, PMID:2574990); GO_0020037 (EC: IEA); GO_0042738 (EC: IEA); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA) PMID:2298205; 2574990; 7894498; 8125298; 8313365; 8694864; 8889548; 9202751; 9364212; 9493761; 9498238; 10768437; 11062028; 11669629; 11737226; 11767004; 12142726; 12477932; 12837283; 15006160; 15128046; 15499177; 16344560; 18660489; 18713828; 19040121; 19074885; 19343046; 19898482; 19913121; 20379614; 20628086; 22675492 cytochrome P450, family 4, subfamily B, polypeptide 1 Ensembl:ENSG00000142973 HGNC:2644 HPRD:00491 MIM:124075 Vega:OTTHUMG00000007984 Other designations: cytochrome P450 4B1|cytochrome P450, subfamily IVB, polypeptide 1|cytochrome P450-HP|microsomal monooxygenase CYP4B1 OGG:3000001581 CP7A CYP7 CYPVII WEB: http://www.ncbi.nlm.nih.gov/gene CYP7A1 cytochrome P450, family 7, subfamily A, polypeptide 1 1581 8q11-q12 9606 8 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006699 (EC: IDA, PMID:19965590); GO_0006699 (EC: IEA); GO_0006699 (EC: ISS); GO_0006699 (EC: TAS); GO_0006707 (EC: ISS); GO_0006805 (EC: TAS); GO_0008123 (EC: ISS); GO_0008206 (EC: TAS); GO_0016125 (EC: TAS); GO_0020037 (EC: IEA); GO_0042632 (EC: ISS); GO_0043231 (EC: ISS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0070857 (EC: IDA, PMID:19965590); GO_0070857 (EC: ISS); GO_0071333 (EC: IDA, PMID:19965590); GO_0071397 (EC: ISS) PMID:1312351; 1358792; 1610352; 2384150; 7288293; 8020987; 8439551; 8504159; 9559267; 10359768; 10882719; 11257258; 11907135; 12011083; 12093884; 12093894; 12116231; 12202481; 12213890; 12477932; 12554795; 12721789; 12810154; 12815072; 12865425; 14515446; 14522988; 14592954; 14762172; 15128046; 15133863; 15205472; 15241483; 15262185; 15333704; 15489334; 15640003; 15707388; 15736936; 15752749; 15796896; 15805302; 15910869; 16115473; 16630139; 16709249; 16763159; 16892178; 16917677; 16937432; 17680536; 17920062; 18078817; 18178499; 18270374; 18307386; 18385139; 18660489; 18665040; 18728123; 18728290; 18996102; 19018779; 19185005; 19343046; 19448895; 19463968; 19537927; 19558216; 19598235; 19850125; 19956635; 19965590; 20005541; 20031551; 20235787; 20351063; 20403997; 20578904; 20602615; 20686565; 20717043; 20857261; 20872969; 20884100; 21039385; 21147774; 21346769; 21813643; 21902813; 22058145; 22235657; 22607622; 22713451; 23038264; 23458092; 23626788 cytochrome P450, family 7, subfamily A, polypeptide 1 Ensembl:ENSG00000167910 HGNC:2651 HPRD:00324 MIM:118455 Vega:OTTHUMG00000164301 Other designations: cholesterol 7-alpha-hydroxylase|cholesterol 7-alpha-monooxygenase|cytochrome P450 7A1|cytochrome P450, subfamily VIIA polypeptide 1 CYP7A1 OGG:3000001582 Bin Zhao, Yue Liu, Oliver He CP8B CYP12 WEB: http://www.ncbi.nlm.nih.gov/gene CYP8B1 cytochrome P450, family 8, subfamily B, polypeptide 1 1582 3p22.1 9606 3 GO_0005506 (EC: IEA); GO_0005783 (EC: IBA); GO_0005789 (EC: TAS); GO_0006629 (EC: IBA); GO_0006699 (EC: TAS); GO_0006805 (EC: TAS); GO_0008206 (EC: TAS); GO_0008397 (EC: IBA); GO_0016021 (EC: IEA); GO_0016125 (EC: TAS); GO_0019825 (EC: TAS, PMID:10051404); GO_0020037 (EC: IBA); GO_0033778 (EC: IEA); GO_0044281 (EC: TAS) PMID:10051404; 11535594; 12477932; 15128046; 15249218; 15489334; 15891895; 16937432; 17585019; 18660489; 19898482; 22093981; 23216301; 24226095 cytochrome P450, family 8, subfamily B, polypeptide 1 Ensembl:ENSG00000180432 HGNC:2653 HPRD:03705 MIM:602172 Vega:OTTHUMG00000133047 Other designations: 7 alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase|7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase|7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase|CYPVIIIB1|cytochrome P450 8B1|cytochrome P450, subfamily VIIIB (sterol 12-alpha-hydroxylase), polypeptide 1|sterol 12-alpha-hydroxylase CYP8B1 OGG:3000001583 Bin Zhao, Yue Liu, Oliver He CYP11A CYPXIA1 P450SCC WEB: http://www.ncbi.nlm.nih.gov/gene CYP11A1 cytochrome P450, family 11, subfamily A, polypeptide 1 1583 15q23-q24 9606 15 GO_0005506 (EC: IEA); GO_0005739 (EC: ISS); GO_0005759 (EC: TAS); GO_0006700 (EC: IDA, PMID:11502818); GO_0006700 (EC: TAS); GO_0006701 (EC: IEA); GO_0006703 (EC: IEA); GO_0006805 (EC: TAS); GO_0007617 (EC: IEA); GO_0008202 (EC: TAS); GO_0008203 (EC: IDA); GO_0008203 (EC: IMP, PMID:18182448); GO_0008203 (EC: ISS); GO_0008386 (EC: IDA, PMID:11502818); GO_0008386 (EC: ISS); GO_0009651 (EC: IEA); GO_0010332 (EC: IEA); GO_0014037 (EC: IEA); GO_0015485 (EC: IEA); GO_0016125 (EC: TAS); GO_0017085 (EC: IEA); GO_0018879 (EC: IEA); GO_0018894 (EC: IEA); GO_0018958 (EC: IEA); GO_0018963 (EC: IEA); GO_0020037 (EC: IDA); GO_0021549 (EC: IEA); GO_0021766 (EC: IEA); GO_0030061 (EC: IEA); GO_0033197 (EC: IEA); GO_0033327 (EC: IEA); GO_0033591 (EC: IEA); GO_0033595 (EC: IEA); GO_0042359 (EC: ISS); GO_0042493 (EC: IEA); GO_0042542 (EC: IEA); GO_0043204 (EC: IEA); GO_0043279 (EC: IEA); GO_0044281 (EC: TAS); GO_0044344 (EC: IEA); GO_0050756 (EC: IEA); GO_0051412 (EC: IEA); GO_0060014 (EC: IEA); GO_0060135 (EC: IEA); GO_0060992 (EC: IEA); GO_0061370 (EC: IEA); GO_0071222 (EC: IEA); GO_0071236 (EC: IEA); GO_0071276 (EC: IEA); GO_0071320 (EC: IEA); GO_0071347 (EC: IEA); GO_0071356 (EC: IEA); GO_0071372 (EC: IEA); GO_0071375 (EC: IEA); GO_0071560 (EC: IEA) PMID:1429635; 1849407; 1863359; 1917982; 2419119; 3024157; 3038854; 8125298; 8372604; 9029710; 9147642; 9498238; 9685215; 10391209; 10411633; 10416690; 10644752; 10856721; 11008920; 11062177; 11137199; 11238527; 11502818; 11535251; 11701663; 11864972; 11997174; 12101186; 12137805; 12145340; 12161514; 12242026; 12385014; 12477932; 12517592; 12530663; 12530676; 14644808; 14702039; 15054879; 15126571; 15128046; 15159300; 15231748; 15323426; 15471945; 15489334; 15583024; 15613430; 15793791; 15927889; 16103457; 16116976; 16172228; 16195240; 16344560; 16391898; 16409859; 16764871; 16798289; 17065579; 17110639; 17178901; 17507624; 17575134; 17594537; 17615053; 18004979; 18182448; 18191841; 18307388; 18368131; 18437511; 18483327; 18490834; 18499961; 18505908; 18665078; 18725155; 18992638; 19064571; 19116240; 19197249; 19240061; 19300392; 19336370; 19342447; 19453261; 19543524; 19574343; 19598235; 19846611; 20066577; 20199803; 20200332; 20214802; 20381444; 20450755; 20634197; 20734064; 20877624; 21159840; 21164259; 21195129; 21391350; 21520051; 21557918; 21636783; 21771722; 21880796; 22199361; 22227097; 22585829; 22673022; 22699877; 22877869; 23158025; 23330251; 23337730; 23555723; 23756599 cytochrome P450, family 11, subfamily A, polypeptide 1 Ensembl:ENSG00000140459 HGNC:2590 HPRD:00326 MIM:118485 Vega:OTTHUMG00000150716 Other designations: cholesterol 20-22 desmolase|cholesterol monooxygenase (side-chain cleaving)|cholesterol side-chain cleavage enzyme, mitochondrial|cytochrome P450 11A1|cytochrome P450(scc)|cytochrome P450, subfamily XIA (cholesterol side chain cleavage)|cytochrome P450C11A1|steroid 20-22-lyase CYP11A1 OGG:3000001584 Bin Zhao, Yue Liu, Oliver He CPN1 CYP11B FHI P450C11 WEB: http://www.ncbi.nlm.nih.gov/gene CYP11B1 cytochrome P450, family 11, subfamily B, polypeptide 1 1584 8q21 9606 8 GO_0004507 (EC: IDA, PMID:2256920); GO_0004507 (EC: IMP, PMID:2022736); GO_0005506 (EC: IEA); GO_0005739 (EC: IDA, PMID:2256920); GO_0005743 (EC: IC, PMID:8506298); GO_0005743 (EC: TAS, PMID:15026188); GO_0006700 (EC: IDA, PMID:2256920); GO_0006704 (EC: TAS); GO_0006705 (EC: TAS); GO_0006805 (EC: TAS); GO_0006955 (EC: TAS, PMID:12452430); GO_0008202 (EC: TAS); GO_0008217 (EC: IMP, PMID:2022736); GO_0016125 (EC: TAS); GO_0020037 (EC: IC, PMID:2256920); GO_0032342 (EC: IDA, PMID:2256920); GO_0032342 (EC: IMP, PMID:19342457); GO_0032870 (EC: IEP, PMID:19342457); GO_0034651 (EC: IDA, PMID:8506298); GO_0034651 (EC: IMP, PMID:19342457); GO_0035865 (EC: IEP, PMID:19342457); GO_0042593 (EC: TAS, PMID:16114325); GO_0044281 (EC: TAS) PMID:1303253; 1430088; 1518866; 1741400; 2022736; 2256920; 2401360; 2592361; 3499608; 7903314; 8372604; 8506298; 9302260; 10391209; 10391210; 10411633; 10599751; 11095433; 11549669; 11549691; 11675945; 11903322; 11932209; 12452430; 12477932; 14682466; 14702039; 15026188; 15062555; 15128046; 15324322; 15507509; 15522937; 15583024; 15699546; 15751602; 15755848; 15793791; 16030166; 16110193; 16114325; 16396990; 16984984; 17075029; 17121536; 17296872; 17556864; 17651452; 17980006; 18215163; 18294861; 18397978; 18636124; 18661760; 18663314; 18974272; 19082699; 19336370; 19342457; 19453261; 19567537; 19598235; 19820005; 19844114; 19913121; 20089618; 20214802; 20331679; 20339375; 20486282; 20523022; 20529578; 20628086; 20634641; 20708777; 20808686; 20877624; 20947076; 21164264; 21625068; 21848792; 22083159; 22217843; 22921894; 22964742; 23146819; 23150505; 23345044; 23825130 cytochrome P450, family 11, subfamily B, polypeptide 1 Ensembl:ENSG00000160882 HGNC:2591 HPRD:01943 MIM:610613 Vega:OTTHUMG00000164637 Other designations: CYPXIB1|cytochrome P-450c11|cytochrome P450 11B1, mitochondrial|cytochrome P450, subfamily XIB (steroid 11-beta-hydroxylase), polypeptide 1|cytochrome P450C11|cytochrome p450 XIB1|steroid 11-beta-hydroxylase|steroid 11-beta-monooxygenase CYP11B1 OGG:3000001585 Bin Zhao, Yue Liu, Oliver He ALDOS CPN2 CYP11B CYP11BL CYPXIB2 P-450C18 P450C18 P450aldo WEB: http://www.ncbi.nlm.nih.gov/gene CYP11B2 cytochrome P450, family 11, subfamily B, polypeptide 2 1585 8q21-q22 9606 8 GO_0002017 (EC: IMP, PMID:14614232); GO_0003091 (EC: IC, PMID:2256920); GO_0004507 (EC: IDA, PMID:1741400); GO_0005506 (EC: IEA); GO_0005739 (EC: IDA, PMID:1741400); GO_0005743 (EC: IC, PMID:2256920); GO_0005743 (EC: TAS); GO_0006700 (EC: IDA, PMID:2256920); GO_0006705 (EC: TAS); GO_0006805 (EC: TAS); GO_0008202 (EC: TAS); GO_0016125 (EC: TAS); GO_0020037 (EC: IC, PMID:2256920); GO_0020037 (EC: IDA); GO_0032342 (EC: IDA, PMID:1741400); GO_0032342 (EC: IMP, PMID:19342457); GO_0032870 (EC: IEP, PMID:19342457); GO_0034651 (EC: IMP, PMID:19342457); GO_0034651 (EC: IMP, Qualifier: NOT, PMID:9703385); GO_0035865 (EC: IEP, PMID:19342457); GO_0044281 (EC: TAS); GO_0047783 (EC: IEA); GO_0055075 (EC: IMP, PMID:9838244); GO_0055078 (EC: IMP, PMID:9838244) PMID:1303253; 1346492; 1518866; 1594605; 1741400; 1775135; 2256920; 2592361; 3872685; 7792802; 8372604; 8439335; 8954040; 9177280; 9360501; 9506770; 9625333; 9703385; 9814506; 9838244; 9931115; 10371693; 10391209; 10391210; 10411633; 10902803; 11076863; 11116113; 11238478; 11245725; 11288810; 11325068; 11422106; 11422735; 11447495; 11518842; 11587161; 11696658; 11696688; 11711521; 11711524; 11725161; 11728005; 11728946; 11841224; 11856349; 11903322; 11910301; 11923700; 11932209; 11967817; 12022239; 12031704; 12065207; 12107246; 12133420; 12137808; 12161536; 12172317; 12193581; 12195120; 12205735; 12213905; 12376254; 12391843; 12444540; 12446192; 12446468; 12477932; 12544440; 12544508; 12611423; 12624609; 12627873; 12746403; 12783697; 12788845; 12788848; 12817181; 12832734; 14508191; 14530292; 14614232; 14643573; 14704730; 14736447; 15055249; 15062555; 15097233; 15102677; 15128046; 15135254; 15223724; 15230231; 15238568; 15272911; 15361760; 15378162; 15479186; 15505931; 15507509; 15522937; 15532370; 15545843; 15569322; 15573760; 15583024; 15583997; 15600184; 15611122; 15614025; 15643128; 15662219; 15699546; 15824464; 15882548; 15894890; 15894891; 15914614; 16078594; 16080804; 16080805; 16110193; 16126185; 16207322; 16208140; 16303227; 16396990; 16468060; 16485730; 16580565; 16615274; 16638864; 16672053; 16714246; 16759311; 16765146; 16767667; 16780672; 16796847; 16893516; 16979018; 16984984; 17003099; 17075029; 17143166; 17190732; 17261471; 17273158; 17296872; 17318792; 17334527; 17334644; 17383306; 17407071; 17519002; 17531119; 17546276; 17631084; 17633457; 17651452; 17664852; 17698557; 17762647; 17851694; 17980006; 17984617; 17987391; 18192839; 18202594; 18260840; 18260994; 18397978; 18413308; 18446309; 18636124; 18638595; 18660489; 18710464; 18771471; 18773126; 18855530; 18856058; 18974272; 19026620; 19093739; 19112833; 19116236; 19117407; 19151144; 19158234; 19166692; 19243623; 19253715; 19254215; 19262476; 19332265; 19342457; 19343046; 19407459; 19418629; 19609286; 19729965; 19776632; 19779464; 19786005; 19820005; 19853701; 19913121; 19948975; 19956635; 20094057; 20097716; 20123934; 20176774; 20182453; 20193236; 20193392; 20214802; 20224556; 20300066; 20339375; 20381197; 20413672; 20416077; 20486282; 20494601; 20535141; 20537417; 20560800; 20598712; 20628086; 20634641; 20659024; 20662731; 20708777; 20808686; 20831027; 20877624; 20878543; 20966514; 21092623; 21106862; 21125974; 21127960; 21163122; 21164264; 21228735; 21239432; 21269059; 21357309; 21476902; 21625068; 21682760; 21777344; 21846681; 22083159; 22134143; 22156739; 22217843; 22311496; 22331364; 22508051; 22652909; 22801770; 22885098; 23023242; 23133610; 23135028; 23150505; 23209837; 23257735; 23275203; 23322723; 23443813; 23479071; 23535359; 23701507; 23936266; 24015270 cytochrome P450, family 11, subfamily B, polypeptide 2 Ensembl:ENSG00000179142 HGNC:2592 HPRD:00492 MIM:124080 Vega:OTTHUMG00000160254 Other designations: aldosterone synthase|aldosterone-synthesizing enzyme|cytochrome P-450Aldo|cytochrome P-450C18|cytochrome P450 11B2, mitochondrial|cytochrome P450, subfamily XIB (steroid 11-beta-hydroxylase), polypeptide 2|mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2|steroid 11-beta-monooxygenase|steroid 11-beta/18-hydroxylase|steroid 18-hydroxylase, aldosterone synthase, P450C18, P450aldo CYP11B2 OGG:3000001586 Bin Zhao, Yue Liu, Oliver He CPT7 CYP17 P450C17 S17AH WEB: http://www.ncbi.nlm.nih.gov/gene CYP17A1 cytochrome P450, family 17, subfamily A, polypeptide 1 1586 RP11-753C18.1 10q24.3 9606 10 GO_0004508 (EC: IDA); GO_0005506 (EC: IEA); GO_0005739 (EC: IEA); GO_0005783 (EC: NAS, PMID:9326943); GO_0005789 (EC: TAS); GO_0006694 (EC: TAS, PMID:3500022); GO_0006702 (EC: TAS); GO_0006704 (EC: TAS); GO_0006805 (EC: TAS); GO_0007548 (EC: TAS, PMID:9326943); GO_0008202 (EC: IDA); GO_0008202 (EC: TAS); GO_0009635 (EC: IEA); GO_0010034 (EC: IEA); GO_0010212 (EC: IEA); GO_0016125 (EC: TAS); GO_0017085 (EC: IEA); GO_0018879 (EC: IEA); GO_0018894 (EC: IEA); GO_0018958 (EC: IEA); GO_0018963 (EC: IEA); GO_0019825 (EC: TAS, PMID:2808364); GO_0020037 (EC: IDA); GO_0021766 (EC: IEA); GO_0030325 (EC: IEA); GO_0030424 (EC: IEA); GO_0030728 (EC: IEA); GO_0031667 (EC: IEA); GO_0032526 (EC: IEA); GO_0033327 (EC: IEA); GO_0034097 (EC: IEA); GO_0042446 (EC: IDA); GO_0042448 (EC: IDA); GO_0042493 (EC: IEA); GO_0043025 (EC: IEA); GO_0044281 (EC: TAS); GO_0047442 (EC: IEA); GO_0048545 (EC: IEA); GO_0051591 (EC: IEA); GO_0051597 (EC: IEA); GO_0060992 (EC: IEA); GO_0071222 (EC: IEA); GO_0071236 (EC: IEA); GO_0071371 (EC: IEA); GO_0090031 (EC: IEA) PMID:1347802; 1478654; 1515452; 1577471; 1621662; 1665206; 1714904; 1740503; 1964490; 2335573; 2466376; 2786493; 2808364; 2843762; 3025870; 3274893; 3488328; 3500022; 6976525; 7629254; 8027220; 8245018; 8345056; 8396144; 8550762; 8675607; 8855840; 9177409; 9326943; 9360545; 9435441; 9601054; 9888582; 10406467; 10720067; 11036113; 11059764; 11094312; 11142420; 11145739; 11212283; 11221867; 11232039; 11248649; 11303586; 11341336; 11358812; 11379008; 11440959; 11470993; 11535545; 11549685; 11571725; 11668516; 11749050; 11834432; 11836339; 11839369; 11847524; 11867265; 11880540; 11888844; 11895872; 11897684; 11911969; 11925378; 11956159; 12036913; 12036914; 12164325; 12368392; 12370109; 12385014; 12444089; 12446594; 12464252; 12466376; 12477932; 12506119; 12517592; 12530262; 12530647; 12530662; 12530676; 12574216; 12582021; 12584742; 12602902; 12631293; 12631398; 12644832; 12645864; 12652520; 12692107; 12718576; 12719950; 12949806; 12954495; 12971967; 14504283; 14512432; 14552332; 14552333; 14561815; 14575568; 14634838; 14644808; 14665706; 14671162; 14684846; 14693733; 14702039; 14714492; 14715870; 14744739; 14985252; 14995917; 15072828; 15128046; 15129369; 15164054; 15195127; 15199113; 15235815; 15241822; 15341023; 15364798; 15372520; 15382051; 15466495; 15477877; 15482786; 15489334; 15536258; 15538743; 15539439; 15555906; 15583024; 15591802; 15598676; 15604994; 15609124; 15654505; 15663233; 15686129; 15687493; 15706422; 15711606; 15749482; 15761247; 15774541; 15799583; 15823822; 15824149; 15865082; 15878919; 15886251; 15916684; 15927351; 15941966; 15953542; 15987450; 15987458; 15999490; 16045239; 16202920; 16214922; 16232327; 16244490; 16260521; 16280037; 16306078; 16319265; 16344560; 16354159; 16381022; 16385451; 16411751; 16424004; 16515644; 16519145; 16527884; 16595228; 16595705; 16603433; 16604478; 16608396; 16616104; 16638864; 16702327; 16707883; 16716118; 16720291; 16730930; 16739881; 16782804; 16783967; 16850246; 16859836; 16875543; 16885156; 16887917; 16890174; 16896040; 16909599; 16969494; 16971197; 16977255; 17077994; 17108148; 17110639; 17119038; 17167982; 17218734; 17235448; 17307805; 17328668; 17359589; 17386955; 17484509; 17507624; 17588204; 17589376; 17606708; 17615053; 17664281; 17669147; 17704407; 17760252; 17765230; 17785571; 17786540; 17826473; 17875358; 17895316; 17961073; 17975119; 17986287; 18000308; 18006912; 18163429; 18172694; 18184656; 18187541; 18262808; 18281250; 18299473; 18305346; 18318428; 18411914; 18415690; 18422032; 18437511; 18483327; 18491956; 18495332; 18496127; 18499961; 18501301; 18503826; 18505908; 18510611; 18560445; 18593984; 18601603; 18618215; 18619494; 18629629; 18636124; 18636181; 18645709; 18676680; 18682255; 18707589; 18722876; 18725155; 18767927; 18781485; 18820009; 18930188; 18957719; 18980759; 19013303; 19015200; 19023099; 19064572; 19064581; 19127255; 19170196; 19174490; 19267349; 19330259; 19336370; 19379515; 19387820; 19415745; 19430479; 19430483; 19443382; 19453261; 19454579; 19469636; 19505920; 19508587; 19574343; 19598235; 19625176; 19627379; 19636199; 19642097; 19672705; 19692168; 19789190; 19805543; 19850690; 19863350; 19913121; 19915575; 19954068; 19956635; 20013047; 20033766; 20043206; 20043997; 20069306; 20072949; 20086173; 20099974; 20113968; 20133979; 20171624; 20173016; 20184498; 20193327; 20197673; 20200332; 20207836; 20214802; 20379614; 20381444; 20414254; 20432167; 20453000; 20479155; 20503394; 20534731; 20539301; 20595043; 20619364; 20628086; 20628746; 20634197; 20650774; 20677014; 20716560; 20720262; 20728566; 20729390; 20729792; 20734064; 20798986; 20852445; 20884100; 20886547; 21045733; 21094112; 21193363; 21300759; 21307141; 21338212; 21378990; 21420394; 21511288; 21572416; 21644229; 21656827; 21676446; 21848792; 21868758; 21896988; 21909110; 21909115; 21919858; 21948762; 21963141; 21966534; 21988832; 22001566; 22048715; 22057025; 22066265; 22071413; 22072737; 22103881; 22174412; 22217842; 22237020; 22238371; 22266943; 22309630; 22331461; 22419734; 22434081; 22456087; 22528335; 22653668; 22714708; 22873692; 22951291; 22954317; 22959498; 23015357; 23036723; 23129512; 23133444; 23229009; 23257735; 23291414; 23350368; 23467202; 23535732; 23551929; 23586722; 23609033; 23620596; 23649771; 23775394; 23809139; 23836902; 23974872; 24001895; 24140098; 24140493 cytochrome P450, family 17, subfamily A, polypeptide 1 Ensembl:ENSG00000148795 HGNC:2593 HPRD:01944 MIM:609300 Vega:OTTHUMG00000018969 Other designations: 17-alpha-hydroxyprogesterone aldolase|CYPXVII|cytochrome P450 17A1|cytochrome P450, subfamily XVII (steroid 17-alpha-hydroxylase), adrenal hyperplasia|cytochrome P450-C17|cytochrome P450c17|cytochrome p450 XVIIA1|steroid 17-alpha-hydroxylase/17,20 lyase|steroid 17-alpha-monooxygenase CYP17A1 OGG:3000001588 Bin Zhao, Yue Liu, Oliver He ARO ARO1 CPV1 CYAR CYP19 CYPXIX P-450AROM WEB: http://www.ncbi.nlm.nih.gov/gene CYP19A1 cytochrome P450, family 19, subfamily A, polypeptide 1 1588 15q21.1 9606 15 GO_0005506 (EC: IEA); GO_0005783 (EC: IDA); GO_0005789 (EC: TAS); GO_0006694 (EC: TAS, PMID:2848247); GO_0006703 (EC: TAS); GO_0006805 (EC: TAS); GO_0008202 (EC: TAS); GO_0008209 (EC: IEA); GO_0009055 (EC: TAS, PMID:2848247); GO_0016020 (EC: TAS, PMID:2848247); GO_0016125 (EC: TAS); GO_0016712 (EC: TAS, PMID:1371509); GO_0019825 (EC: TAS, PMID:2848247); GO_0020037 (EC: IDA, PMID:19129847); GO_0044281 (EC: TAS); GO_0060736 (EC: IEA); GO_0070330 (EC: IDA, PMID:19129847) PMID:1371509; 1472013; 1724289; 1825497; 2040633; 2171939; 2541021; 2691883; 2808431; 2848247; 2973313; 3018730; 3390233; 3653507; 3964273; 7690033; 8090165; 8117272; 8265607; 8477708; 8530621; 9177373; 9211678; 9696881; 10566648; 10837748; 11076863; 11140838; 11181459; 11216915; 11232039; 11256614; 11344237; 11469726; 11571725; 11595700; 11756225; 11826265; 11850203; 11850205; 11850206; 11850208; 11850209; 11850210; 11850219; 11850220; 11850221; 11850222; 11850224; 11850225; 11850230; 11850233; 11850235; 11897504; 11903314; 11904449; 11925378; 11927588; 11935306; 11997208; 12036913; 12053085; 12154211; 12160997; 12161013; 12161505; 12164325; 12204674; 12213901; 12351690; 12370109; 12385014; 12428207; 12451990; 12462076; 12462077; 12466340; 12477932; 12489562; 12517592; 12592380; 12602902; 12606587; 12618873; 12620480; 12639945; 12690088; 12705475; 12720534; 12734209; 12736278; 12759877; 12768436; 12788892; 12839940; 12843146; 12846271; 12864794; 12914527; 12917334; 12944421; 14508827; 14517714; 14580722; 14593077; 14602139; 14631363; 14634838; 14714492; 14715870; 14744739; 14747179; 14973387; 14981949; 14990865; 15046111; 15072827; 15072828; 15074077; 15079018; 15083376; 15083377; 15083380; 15083381; 15126575; 15128046; 15132727; 15177662; 15181061; 15183689; 15199113; 15207764; 15229337; 15241822; 15298966; 15319333; 15330195; 15358790; 15364411; 15449726; 15489336; 15582747; 15583024; 15613678; 15640252; 15668497; 15677755; 15688015; 15695318; 15748828; 15774541; 15788666; 15794932; 15800924; 15802318; 15840311; 15862960; 15862961; 15862962; 15955695; 16019206; 16020944; 16024248; 16039845; 16045239; 16086586; 16103457; 16128984; 16146740; 16199862; 16202920; 16213843; 16232327; 16244490; 16251630; 16251760; 16260521; 16269961; 16287071; 16302261; 16303757; 16306085; 16322405; 16344016; 16344560; 16381901; 16392624; 16395678; 16402077; 16406421; 16418790; 16424004; 16426763; 16467490; 16473000; 16498360; 16498361; 16498363; 16498364; 16541304; 16556483; 16566930; 16595205; 16604491; 16608396; 16621515; 16634644; 16641167; 16648498; 16684355; 16691199; 16723309; 16730930; 16733710; 16739881; 16741831; 16767510; 16782804; 16793950; 16798289; 16850246; 16875543; 16882736; 16894362; 16895991; 16896040; 16930994; 16949385; 16949391; 16964243; 16977255; 16997132; 17004113; 17065579; 17066438; 17118999; 17119036; 17158756; 17167982; 17176215; 17187946; 17216495; 17219197; 17325027; 17331471; 17336977; 17359589; 17372263; 17391072; 17400043; 17404019; 17405842; 17415442; 17482958; 17507620; 17507624; 17517397; 17562079; 17574328; 17584767; 17588204; 17589376; 17595315; 17615053; 17646720; 17657731; 17661084; 17662285; 17678915; 17681675; 17682677; 17687621; 17704407; 17766065; 17827443; 17893373; 17953943; 17962916; 17975727; 17979523; 17989043; 17989068; 18030614; 18048499; 18049890; 18083712; 18086758; 18157729; 18159088; 18163429; 18181018; 18182446; 18199708; 18201819; 18245543; 18274619; 18281655; 18299793; 18305346; 18426832; 18437511; 18445666; 18467089; 18483177; 18483761; 18491956; 18497059; 18501301; 18505907; 18510611; 18512790; 18559914; 18568448; 18593984; 18595017; 18601603; 18614276; 18614591; 18617186; 18622258; 18629629; 18636124; 18667686; 18676680; 18767927; 18817841; 18818748; 18820009; 18822378; 18847535; 18930188; 18941892; 18941913; 18955734; 18962445; 18980759; 19015200; 19019335; 19022561; 19064562; 19064572; 19064581; 19083124; 19093296; 19107851; 19116238; 19124504; 19124506; 19129847; 19137777; 19152063; 19158807; 19159688; 19170196; 19172223; 19174490; 19185610; 19194457; 19240151; 19282383; 19299445; 19324338; 19340622; 19366906; 19389254; 19415745; 19419293; 19438456; 19445691; 19453261; 19469636; 19470632; 19478482; 19491387; 19493871; 19500729; 19505920; 19514368; 19527514; 19549443; 19551860; 19555469; 19556341; 19558171; 19570444; 19573564; 19574343; 19589174; 19591804; 19598235; 19604497; 19625176; 19630952; 19639193; 19692168; 19776291; 19782135; 19789370; 19800002; 19800101; 19805543; 19808095; 19815003; 19818337; 19879925; 19883757; 19896534; 19906189; 19906814; 19913121; 19921206; 19933466; 19952760; 19956635; 19969081; 20004389; 20015405; 20026603; 20030115; 20048079; 20052540; 20053928; 20060879; 20064870; 20072949; 20133979; 20140262; 20144226; 20148360; 20164038; 20164294; 20173016; 20184498; 20186154; 20189936; 20193327; 20200332; 20211687; 20214802; 20231365; 20300828; 20305046; 20346360; 20351196; 20381444; 20385561; 20417295; 20430378; 20432167; 20453000; 20505544; 20526739; 20539301; 20546829; 20586553; 20588246; 20588308; 20628086; 20628746; 20634197; 20655525; 20668023; 20688833; 20716560; 20729390; 20734064; 20797716; 20819792; 20881004; 20881960; 20932310; 20937744; 20960227; 21125383; 21154336; 21170323; 21188138; 21198743; 21217768; 21251330; 21269619; 21282199; 21296134; 21300759; 21319151; 21319995; 21320735; 21356374; 21377485; 21392518; 21392519; 21392520; 21414724; 21479914; 21511357; 21622727; 21676395; 21757507; 21771722; 21807013; 21939764; 21948762; 21952832; 21972004; 22057025; 22079757; 22089263; 22104650; 22106445; 22119029; 22130322; 22160249; 22185650; 22217837; 22237979; 22300440; 22315456; 22320986; 22331461; 22335023; 22384274; 22407818; 22426781; 22448795; 22492871; 22508516; 22511967; 22578533; 22633539; 22634420; 22638611; 22675492; 22731640; 22759564; 22773874; 22843875; 22848710; 22887836; 22889864; 22902617; 22915343; 22982181; 23001776; 23029457; 23085504; 23090135; 23110082; 23116507; 23122578; 23129173; 23178495; 23229009; 23239821; 23253631; 23340254; 23342035; 23350368; 23400010; 23438603; 23456168; 23461365; 23518928; 23540392; 23584792; 23599027; 23625281; 23635391; 23643682; 23661022; 23669293; 23700878; 23727336; 23729401; 23747729; 23748068; 23809139; 23846226; 23873111; 24049095 cytochrome P450, family 19, subfamily A, polypeptide 1 Ensembl:ENSG00000137869 HGNC:2594 HPRD:00488 MIM:107910 Vega:OTTHUMG00000131747 Other designations: aromatase|cytochrome P-450AROM|cytochrome P450 19A1|cytochrome P450, subfamily XIX (aromatization of androgens)|estrogen synthase|estrogen synthetase|flavoprotein-linked monooxygenase|microsomal monooxygenase CYP19A1 OGG:3000001589 Bin Zhao, Yue Liu, Oliver He CA21H CAH1 CPS1 CYP21 CYP21B P450c21B WEB: http://www.ncbi.nlm.nih.gov/gene CYP21A2 cytochrome P450, family 21, subfamily A, polypeptide 2 1589 DADB-112B14.10-001 6p21.3 9606 6 GO_0004509 (EC: IEA); GO_0005496 (EC: IEA); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006704 (EC: TAS); GO_0006705 (EC: TAS); GO_0006805 (EC: TAS); GO_0008202 (EC: TAS); GO_0008395 (EC: TAS, PMID:1406709); GO_0016125 (EC: TAS); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS) PMID:1351548; 1406699; 1406709; 1496017; 1605859; 1644925; 1864962; 1937474; 1985465; 2072928; 2249999; 2303461; 2325662; 2788081; 2827462; 2845408; 3038528; 3137812; 3257825; 3260007; 3260033; 3267225; 3486422; 3487786; 3497399; 3500473; 3871526; 5804199; 7096533; 7629224; 7635470; 7749410; 8081391; 8175971; 8372604; 8478006; 8485582; 8518786; 8675607; 8731325; 8968761; 8989258; 9067760; 9099896; 9187661; 9215318; 9497336; 9580109; 9661649; 10051010; 10072631; 10094562; 10198222; 10207042; 10229037; 10343159; 10364682; 10391209; 10408778; 10408786; 10443693; 10496074; 10720040; 11073721; 11093272; 11232002; 11287026; 11457572; 11581476; 11598371; 11600539; 11692155; 11739456; 11746135; 11836313; 12028996; 12038604; 12050231; 12050257; 12121677; 12213672; 12213891; 12220458; 12222711; 12370110; 12384784; 12464252; 12477932; 12746407; 12788866; 12788880; 12788889; 12855227; 12876419; 12887291; 12915679; 12966197; 14502362; 14514162; 14671153; 14676460; 14676461; 14702039; 14715874; 14733808; 15004406; 15027205; 15028279; 15110320; 15126570; 15128046; 15342556; 15493145; 15572419; 15583024; 15598692; 15608154; 15627780; 15705377; 15751603; 15761541; 15775714; 15793784; 15818055; 15830218; 15858147; 15988383; 16046588; 16238926; 16344560; 16427797; 16487445; 16500637; 16541276; 16648810; 16712666; 16728546; 16788163; 16984992; 17033937; 17047018; 17119906; 17275379; 17466088; 17505149; 17526939; 17551464; 17573904; 17666484; 17803691; 17878254; 18028896; 18039588; 18042312; 18179706; 18204270; 18319307; 18381579; 18392095; 18397975; 18445671; 18478071; 18505908; 18589890; 18636124; 18702679; 18787377; 18825878; 18973462; 19039234; 19058224; 19062540; 19085698; 19116923; 19135723; 19137635; 19158234; 19201236; 19208730; 19226270; 19272182; 19347184; 19420818; 19423540; 19449670; 19453261; 19501079; 19505723; 19531083; 19598235; 19624807; 19773403; 19799922; 19844122; 19856253; 19890026; 19925038; 19930153; 20029944; 20059433; 20070950; 20080860; 20110635; 20132843; 20201644; 20233785; 20301350; 20406964; 20423741; 20438785; 20587039; 20587610; 20617557; 20661889; 20671415; 20818501; 20838032; 20926536; 20970527; 21117955; 21134444; 21164261; 21164262; 21169732; 21175091; 21198393; 21264314; 21274396; 21446712; 21521936; 21534945; 21570420; 21609351; 21646284; 21750395; 21912141; 22001566; 22014889; 22017335; 22020670; 22127631; 22217838; 22308849; 22313422; 22497080; 22561756; 22802425; 22841790; 22873692; 22885098; 22886582; 23027774; 23044877; 23045419; 23073904; 23142378; 23155693; 23211577; 23298233; 23313747; 23322511; 23329749; 23342490; 23359706; 23370425; 23376085; 23386413; 23535732; 23586722; 23692712 cytochrome P450, family 21, subfamily A, polypeptide 2 Ensembl:ENSG00000231852 HGNC:2600 HPRD:01942 MIM:613815 Vega:OTTHUMG00000031069 Other designations: 21-OHase|cytochrome P450 XXI|cytochrome P450, subfamily XXIA (steroid 21-hydroxylase, congenital adrenal hyperplasia), polypeptide 2|cytochrome P450-C21B|steroid 21-hydroxylase|steroid 21-monooxygenase CYP21A2 OGG:3000001591 Bin Zhao, Yue Liu, Oliver He CP24 CYP24 HCAI P450-CC24 WEB: http://www.ncbi.nlm.nih.gov/gene CYP24A1 cytochrome P450, family 24, subfamily A, polypeptide 1 1591 20q13 9606 20 GO_0001649 (EC: IEP, PMID:17023519); GO_0005506 (EC: IEA); GO_0005743 (EC: TAS); GO_0006766 (EC: TAS); GO_0006805 (EC: TAS); GO_0008202 (EC: TAS); GO_0008403 (EC: IEA); GO_0016491 (EC: NAS, PMID:7632726); GO_0020037 (EC: TAS, PMID:8506296); GO_0030342 (EC: IDA, PMID:8506296); GO_0033280 (EC: IDA, PMID:16720713); GO_0042359 (EC: TAS); GO_0042369 (EC: NAS, PMID:16720713); GO_0044281 (EC: TAS); GO_0055114 (EC: IDA, PMID:8506296); GO_0070561 (EC: NAS, PMID:16720713) PMID:7595086; 7632726; 7829101; 7938037; 8266831; 8440135; 8506296; 10218951; 11149490; 11780052; 12477932; 12485911; 12641633; 12855575; 14665637; 14760115; 15078099; 15128046; 15146197; 15358094; 15583024; 15630458; 15788398; 15919092; 15951480; 16457885; 16516540; 16600026; 16617161; 16691293; 16708384; 16720713; 17023519; 17079137; 17223345; 17244366; 17254772; 17368180; 17426122; 17475215; 17585873; 17606874; 17646648; 17875655; 17932346; 18467787; 18676680; 18824104; 18843020; 19097033; 19170196; 19237542; 19255064; 19343046; 19393625; 19453261; 19454612; 19505920; 19625176; 19667160; 19692168; 19706847; 19852851; 19891555; 19901270; 19913121; 19922790; 20007432; 20304053; 20304056; 20304059; 20394945; 20398751; 20450955; 20453000; 20460683; 20467438; 20541252; 20587525; 20591973; 20628086; 20654748; 20687218; 20809279; 20831823; 20847308; 20877624; 21169243; 21385079; 21440908; 21441443; 21675912; 21697097; 21725204; 21828234; 21833088; 21906983; 22213328; 22285938; 22511602; 22612324; 22648713; 22649517; 22690899; 22841393; 22871965; 22940288; 22984610; 23042114; 23059474; 23155244; 23169318; 23293122; 23377224; 23393347; 23423976; 23435876; 23456391; 23463632; 23485543; 23674869; 23826131; 24068962 cytochrome P450, family 24, subfamily A, polypeptide 1 Ensembl:ENSG00000019186 HGNC:2602 HPRD:00522 MIM:126065 Vega:OTTHUMG00000032773 Other designations: 1,25-@dihydroxyvitamin D3 24-hydroxylase|1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial|24-OHase|cytochrome P450 24A1|cytochrome P450, subfamily XXIV (vitamin D 24-hydroxylase)|cytochrome P450-CC24|exo-mitochondrial protein|vitamin D 24-hydroxylase|vitamin D(3) 24-hydroxylase CYP24A1 OGG:3000001592 Bin Zhao, Yue Liu, Oliver He CP26 CYP26 P450RAI P450RAI1 WEB: http://www.ncbi.nlm.nih.gov/gene CYP26A1 cytochrome P450, family 26, subfamily A, polypeptide 1 1592 RP11-348J12.1 10q23-q24 9606 10 GO_0001972 (EC: IDA, PMID:10823918); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006766 (EC: TAS); GO_0006805 (EC: TAS); GO_0007417 (EC: IEA); GO_0008152 (EC: TAS, PMID:9228017); GO_0008401 (EC: IDA, PMID:10823918); GO_0009952 (EC: IEA); GO_0014032 (EC: IEA); GO_0019825 (EC: TAS, PMID:9228017); GO_0020037 (EC: NAS, PMID:9228017); GO_0034653 (EC: IDA, PMID:10823918); GO_0044281 (EC: TAS); GO_0048384 (EC: IEA); GO_0048387 (EC: TAS, PMID:14532297); GO_0071300 (EC: IEA) PMID:8601734; 9228017; 9228041; 9521883; 9716180; 9826557; 10583049; 10823918; 10874126; 10976925; 12727970; 14532297; 14702039; 15128046; 15281009; 16053444; 16194896; 16463413; 16778795; 16933217; 17059167; 17218384; 17460545; 18059332; 18992717; 19519282; 19553612; 19703508; 20167577; 20375987; 20513361; 20682464; 20686565; 20693622; 21521770; 21850183; 21975512; 22020119; 22179182; 23396134; 24043786 cytochrome P450, family 26, subfamily A, polypeptide 1 Ensembl:ENSG00000095596 HGNC:2603 HPRD:03759 MIM:602239 Vega:OTTHUMG00000018765 Other designations: P450, retinoic acid-inactivating, 1|cytochrome P450 26A1|cytochrome P450 retinoic acid-inactivating 1|cytochrome P450, subfamily XXVIA, polypeptide 1|cytochrome P450RAI|hP450RAI|retinoic acid 4-hydroxylase|retinoic acid-metabolizing cytochrome CYP26A1 OGG:3000001593 Bin Zhao, Yue Liu, Oliver He CP27 CTX CYP27 WEB: http://www.ncbi.nlm.nih.gov/gene CYP27A1 cytochrome P450, family 27, subfamily A, polypeptide 1 1593 2q35 9606 2 GO_0005506 (EC: IEA); GO_0005743 (EC: IEA); GO_0005759 (EC: TAS); GO_0006699 (EC: TAS); GO_0006805 (EC: TAS); GO_0008203 (EC: IEA); GO_0008206 (EC: TAS); GO_0008395 (EC: TAS, PMID:9790667); GO_0016125 (EC: TAS); GO_0020037 (EC: IEA); GO_0030343 (EC: IEA); GO_0031073 (EC: IEA); GO_0044281 (EC: TAS); GO_0047749 (EC: IEA) PMID:1708392; 2019602; 7690968; 7915755; 8125298; 8514861; 9186905; 9215552; 9790667; 10519880; 11167933; 11604260; 11903362; 12000359; 12011083; 12117727; 12119285; 12242561; 12477932; 12777473; 14672608; 14741198; 15128046; 15340076; 15489334; 15533057; 15708352; 16157755; 16372260; 16584175; 16930540; 17088262; 17292862; 17482558; 17697869; 17875655; 18227423; 18791760; 19255064; 19343046; 19671838; 19852851; 19913121; 20149624; 20301583; 20402754; 20450308; 20558929; 20628086; 20654748; 20809279; 20855565; 20877624; 21049985; 21134350; 21258856; 21411718; 21498512; 21958693; 21988832; 22018287; 22185844; 22227097; 22509407; 24096962 cytochrome P450, family 27, subfamily A, polypeptide 1 Ensembl:ENSG00000135929 HGNC:2605 HPRD:05939 MIM:606530 Vega:OTTHUMG00000048238 Other designations: 5-beta-cholestane-3-alpha, 7-alpha, 12-alpha-triol 26-hydroxylase|5-beta-cholestane-3-alpha, 7-alpha, 12-alpha-triol 27-hydroxylase|5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase|cholestanetriol 26-monooxygenase|cytochrome P-450C27/25|cytochrome P450 27|cytochrome P450, subfamily XXVIIA (steroid 27-hydroxylase, cerebrotendinous xanthomatosis), polypeptide 1|sterol 26-hydroxylase, mitochondrial|sterol 27-hydroxylase|vitamin D(3) 25-hydroxylase CYP27A1 OGG:3000001594 Bin Zhao, Yue Liu, Oliver He CP2B CYP1 CYP1alpha CYP27B P450c1 PDDR VDD1 VDDR VDDRI VDR WEB: http://www.ncbi.nlm.nih.gov/gene CYP27B1 cytochrome P450, family 27, subfamily B, polypeptide 1 1594 12q14.1 9606 12 GO_0004498 (EC: IDA, PMID:15795327); GO_0005506 (EC: IEA); GO_0005737 (EC: IDA, PMID:15589699); GO_0005739 (EC: ISS); GO_0005739 (EC: TAS, PMID:9333115); GO_0005741 (EC: TAS); GO_0006766 (EC: TAS); GO_0006805 (EC: TAS); GO_0006816 (EC: ISS); GO_0008202 (EC: TAS); GO_0008285 (EC: IDA, PMID:16549446); GO_0010956 (EC: IDA, PMID:16549446); GO_0010980 (EC: IDA, PMID:16549446); GO_0020037 (EC: IEA); GO_0030282 (EC: IEP, PMID:17023519); GO_0030308 (EC: IMP, PMID:12496369); GO_0030500 (EC: IMP, PMID:9415400); GO_0032496 (EC: IDA, PMID:12855575); GO_0033280 (EC: IDA, PMID:16549446); GO_0034341 (EC: IDA, PMID:9282826); GO_0036378 (EC: IDA, PMID:15795327); GO_0042359 (EC: IDA, PMID:9415400); GO_0042359 (EC: TAS); GO_0042369 (EC: IEA); GO_0043627 (EC: IEP, PMID:15795327); GO_0044281 (EC: TAS); GO_0045618 (EC: IMP, PMID:12496369); GO_0046697 (EC: IEP, PMID:16720713); GO_0055074 (EC: IMP, PMID:9415400); GO_0070314 (EC: IMP, PMID:12496369); GO_0070564 (EC: IDA, PMID:16549446) PMID:1662663; 1690216; 1971995; 9282826; 9295274; 9333115; 9344864; 9415400; 9428799; 9486994; 9837822; 10320521; 10359826; 10566658; 11799066; 12039697; 12050193; 12050281; 12107095; 12137802; 12161526; 12386916; 12457456; 12477932; 12496369; 12520522; 12746631; 12855575; 14671156; 15225751; 15243130; 15296474; 15331405; 15342556; 15583024; 15589699; 15795327; 15934135; 15947108; 15951480; 15956353; 16061850; 16549446; 16720713; 17023519; 17079137; 17207990; 17207994; 17223345; 17236759; 17250953; 17254772; 17267208; 17287116; 17368179; 17395559; 17395703; 17426122; 17488797; 17606874; 17878529; 17932346; 18476984; 18495603; 18676680; 18689381; 18767073; 18767934; 18768522; 18843020; 19064572; 19154546; 19170196; 19219539; 19255064; 19343046; 19453261; 19454612; 19505920; 19524013; 19525955; 19625176; 19667158; 19706847; 19783860; 19852851; 19891555; 19913121; 19951419; 19966181; 19998245; 20007432; 20082271; 20152900; 20304056; 20453000; 20518841; 20534770; 20619365; 20628086; 20648053; 20654748; 20687218; 20701904; 20809279; 20831823; 20847308; 20877624; 21107545; 21145801; 21440908; 21441443; 21542014; 21833088; 21869486; 22190362; 22326730; 22443290; 22446158; 22511602; 22516854; 22547098; 22588163; 22612324; 22963605; 22995334; 23045480; 23063903; 23149444; 23286944; 23334593; 23423976; 23444327; 23483640; 23614044; 23894780; 24308945 cytochrome P450, family 27, subfamily B, polypeptide 1 Ensembl:ENSG00000111012 HGNC:2606 HPRD:02031 MIM:609506 Vega:OTTHUMG00000170457 Other designations: 1alpha(OH)ase|25 hydroxyvitamin D3-1-alpha hydroxylase|25-OHD-1 alpha-hydroxylase|25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial|VD3 1A hydroxylase|calcidiol 1-monooxygenase|cytochrome P450 subfamily XXVIIB polypeptide 1|cytochrome P450C1 alpha|cytochrome P450VD1-alpha|cytochrome p450 27B1 CYP27B1 OGG:3000001595 Bin Zhao, Yue Liu, Oliver He CP51 CYP51 CYPL1 LDM P450-14DM P450L1 WEB: http://www.ncbi.nlm.nih.gov/gene CYP51A1 cytochrome P450, family 51, subfamily A, polypeptide 1 1595 7q21.2 9606 7 GO_0005506 (EC: IEA); GO_0005783 (EC: IDA); GO_0005789 (EC: TAS); GO_0006694 (EC: IDA); GO_0006695 (EC: TAS); GO_0006805 (EC: TAS); GO_0008398 (EC: IDA); GO_0016021 (EC: IEA); GO_0016125 (EC: TAS); GO_0020037 (EC: IDA); GO_0033488 (EC: IEA); GO_0044281 (EC: TAS); GO_0070988 (EC: IDA) PMID:8024575; 8619637; 8797093; 8809088; 8845856; 8975714; 11678326; 12145339; 12477932; 12690205; 12824470; 12853948; 14702039; 15128046; 15489334; 15611056; 16344560; 18660489; 18676367; 19322201; 20149798; 20547249; 21139048; 21890473; 21906983; 21963094; 21987572; 21988832; 22053931; 22180046; 23000965; 24362992; 24502137 cytochrome P450, family 51, subfamily A, polypeptide 1 Ensembl:ENSG00000001630 HGNC:2649 HPRD:03381 MIM:601637 Vega:OTTHUMG00000131131 Other designations: CYPLI|cytochrome P450 51A1|cytochrome P450, 51 (lanosterol 14-alpha-demethylase)|cytochrome P450-14DM|cytochrome P45014DM|cytochrome P450LI|lanosterol 14-alpha demethylase|lanosterol 14-alpha-demethylase|sterol 14-alpha demethylase CYP51A1 OGG:3000001601 Bin Zhao, Yue Liu, Oliver He DOC-2 DOC2 WEB: http://www.ncbi.nlm.nih.gov/gene DAB2 Dab, mitogen-responsive phosphoprotein, homolog 2 (Drosophila) 1601 5p13.1 20140408 9606 5 protein-coding Official from a nomenclature committee GO_0000904 (EC: IEA); GO_0001701 (EC: IEA); GO_0001921 (EC: IEA); GO_0001934 (EC: IMP, PMID: 12805222); GO_0005178 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11387212); GO_0005546 (EC: IEA); GO_0005730 (EC: IDA); GO_0005765 (EC: TAS); GO_0005886 (EC: IDA); GO_0005886 (EC: TAS); GO_0005905 (EC: IDA, PMID: 12857860); GO_0006907 (EC: IEA); GO_0006915 (EC: IEA); GO_0007257 (EC: IEA); GO_0007492 (EC: IEA); GO_0007588 (EC: IEA); GO_0008022 (EC: IPI, PMID: 15837803); GO_0008283 (EC: TAS, PMID: 9620555); GO_0010718 (EC: IDA, PMID: 15734730); GO_0010862 (EC: IDA, PMID: 11387212); GO_0015031 (EC: IEA); GO_0016055 (EC: IEA); GO_0016324 (EC: IEA); GO_0030099 (EC: IEA); GO_0030132 (EC: IEA); GO_0030335 (EC: IEA); GO_0030511 (EC: IDA, PMID: 11387212); GO_0030665 (EC: IEA); GO_0032091 (EC: IMP, PMID: 12805222); GO_0032436 (EC: IMP, PMID: 12805222); GO_0032968 (EC: IEA); GO_0035612 (EC: IEA); GO_0035615 (EC: IMP, PMID: 16984970); GO_0038024 (EC: IMP, PMID: 16984970); GO_0043066 (EC: IDA, PMID: 15734730); GO_0043231 (EC: IDA); GO_0045807 (EC: IMP); GO_0045892 (EC: IMP, PMID: 12805222); GO_0045893 (EC: IMP, PMID: 12805222); GO_0046332 (EC: IDA, PMID: 11387212); GO_0048268 (EC: IEA); GO_0060391 (EC: IDA, PMID: 11387212); GO_0060766 (EC: IMP, PMID: 16267015); GO_0061024 (EC: TAS); GO_0070022 (EC: IDA, Qualifier: colocalizes_with, PMID: 11387212); GO_0071560 (EC: IEA); GO_0090090 (EC: IMP, PMID: 12805222); GO_1900026 (EC: IEA); GO_2000096 (EC: IMP, PMID: 12805222); GO_2000370 (EC: IMP, PMID: 16984970); GO_2000643 (EC: IMP); GO_2001046 (EC: IEA); GO_2001237 (EC: IEA) PMID: 8314147; 8660969; 8889548; 9569023; 9620555; 10340382; 10542228; 10769163; 11039902; 11161789; 11247302; 11371563; 11387212; 11812785; 11906161; 11927540; 11967127; 12473651; 12477932; 12606711; 12805222; 12853125; 12857860; 12881709; 14596919; 14669280; 15134832; 15231748; 15247260; 15280374; 15302935; 15489334; 15734730; 15837803; 15894542; 16061224; 16267015; 16713569; 16870701; 16964243; 16984970; 17009406; 17081983; 17110338; 17115114; 17187061; 17474147; 17671122; 18070591; 18354201; 18429820; 18582465; 19204726; 19423540; 19531213; 19581412; 19738201; 19767570; 19855435; 19956625; 20379614; 20383146; 20406964; 20438785; 20448150; 20525238; 20592473; 20628624; 20936779; 21063401; 21097498; 21139048; 21496867; 21573318; 21725366; 21963094; 21987572; 21988832; 21995445; 22158540; 22218591; 22265793; 22323290; 22399289; 22558309; 22648170; 22705885; 22898784; 22977233; 23005040; 23263486; 23817569; 23909735; 24186266 Dab, mitogen-responsive phosphoprotein, homolog 2 (Drosophila) Ensembl:ENSG00000153071 HGNC:2662 HPRD:03139 MIM:601236 Vega:OTTHUMG00000162043 Other designations: differentially-expressed protein 2|disabled homolog 2|disabled homolog 2, mitogen-responsive phosphoprotein DAB2 OGG:3000001647 Bin Zhao, Yue Liu, Oliver He DDIT1 GADD45 WEB: http://www.ncbi.nlm.nih.gov/gene GADD45A growth arrest and DNA-damage-inducible, alpha 1647 RP5-975D15.1 1p31.2 9606 1 Official from a nomenclature committee GO_0000079 (EC: TAS, PMID: 10747892); GO_0000185 (EC: IDA, PMID: 9827804); GO_0001047 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12716909); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA, PMID: 9827804); GO_0006281 (EC: TAS, PMID: 7973727); GO_0006469 (EC: IEA); GO_0006915 (EC: TAS, PMID: 10828065); GO_0007050 (EC: IEA); GO_0007098 (EC: IEA); GO_0042770 (EC: IMP); GO_0043065 (EC: IDA, PMID: 9827804); GO_0046330 (EC: IDA, PMID: 9827804); GO_0071260 (EC: IEP, PMID: 19593445); GO_0071479 (EC: IMP); GO_1900745 (EC: IDA, PMID: 9827804); GO_2000379 (EC: IMP) PMID: 1990262; 7478510; 7478594; 7784094; 7798274; 7973727; 8226988; 9178907; 9705499; 9827804; 10022855; 10362260; 10747892; 10828065; 10872826; 10912791; 10973963; 11076863; 11256614; 11498536; 11777930; 11893252; 12124778; 12168790; 12171872; 12477932; 12483522; 12716909; 12748288; 14506229; 14517299; 14586402; 14635187; 14647444; 15203190; 15328371; 15353598; 15489334; 15489336; 15616591; 15623356; 15642443; 15644315; 15650754; 15735726; 15736438; 15899854; 16157202; 16169070; 16189514; 16353139; 16381901; 16421274; 16772293; 16827157; 16951143; 16997058; 17140287; 17178890; 17230496; 17436581; 17474084; 17599061; 17616671; 17703175; 18243530; 18296737; 18350249; 18369439; 18413758; 18472964; 18480060; 18611122; 18760377; 18950845; 19048389; 19052873; 19064572; 19128509; 19190346; 19298651; 19452502; 19459735; 19536092; 19550118; 19593445; 19596022; 19728081; 19789190; 20012529; 20131288; 20444249; 20460379; 20639865; 20652500; 20932473; 21048031; 21120602; 21139048; 21211282; 21368893; 21739277; 21813510; 21890473; 21900206; 21906983; 21931671; 21963094; 21986581; 21988832; 22135303; 22313682; 22430142; 22521726; 22718299; 22825327; 22970179; 23000965; 23071284; 23114628; 23158659; 23187294; 23227140; 23478041; 23485469; 23563151; 23603344; 23616123; 23706118; 24104470; 24104471; 24104476 growth arrest and DNA-damage-inducible, alpha Ensembl:ENSG00000116717 HGNC:4095 HPRD:00528 MIM:126335 Vega:OTTHUMG00000009374 Other designations: DDIT-1|DNA damage-inducible transcript 1 protein|DNA damage-inducible transcript-1|DNA-damage-inducible transcript 1|growth arrest and DNA damage-inducible protein GADD45 alpha|growth arrest and DNA-damage-inducible 45 alpha GADD45A OGG:3000001649 Other designations: C/EBP zeta|CCAAT/enhancer-binding protein homologous protein|DDIT-3|DNA damage-inducible transcript 3 protein|c/EBP-homologous protein 10|growth arrest and DNA damage-inducible protein GADD153 DDIT3 DNA-damage-inducible transcript 3 Ensembl:ENSG00000175197 HGNC:2726 HPRD:00529 MIM:126337 NCBI-Human-GeneID:1649 CEBPZ CHOP CHOP-10 CHOP10 GAD153 DDIT3 NCBI-Human-GeneID:1649 http://www.ncbi.nlm.nih.gov/gene/1649 OGG:3000001656 Bin Zhao, Yue Liu, Oliver He HLR2 P54 RCK WEB: http://www.ncbi.nlm.nih.gov/gene DDX6 DEAD (Asp-Glu-Ala-Asp) box helicase 6 1656 11q23.3 9606 11 Official from a nomenclature committee GO_0000288 (EC: TAS); GO_0000932 (EC: IDA, PMID: 16699599); GO_0003724 (EC: TAS, PMID: 1579499); GO_0004386 (EC: TAS, PMID: 1394235); GO_0005515 (EC: IPI, PMID: 16364915); GO_0005524 (EC: IEA); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0008026 (EC: IEA); GO_0010467 (EC: TAS); GO_0010494 (EC: IDA, PMID: 17392519); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016442 (EC: IDA); GO_0033962 (EC: IDA); GO_0043231 (EC: IDA); GO_0043928 (EC: TAS); GO_0044822 (EC: IDA) PMID: 1394235; 1579499; 7614484; 8816452; 10319407; 10360675; 10737800; 11839790; 12477932; 12823589; 14684915; 14702039; 15489334; 16147992; 16344560; 16364915; 16611246; 16699599; 16756390; 17207965; 17353931; 17392519; 17898068; 18378046; 18769115; 19285948; 19297524; 19380743; 19542561; 19560422; 19738201; 20020773; 20158304; 20360068; 20392846; 20884783; 21030982; 21110914; 21139048; 21145461; 21383967; 21906983; 21957497; 22022269; 22190034; 22203041; 22268729; 22505724; 22797925; 22836354; 22851315; 22939629; 22951725; 22965301; 23293030; 23455922; 23535175; 23602568; 23826300; 23932921; 24130170; 24255178; 24457600 DEAD (Asp-Glu-Ala-Asp) box helicase 6 HGNC:2747 HPRD:02638 MIM:600326 Other designations: ATP-dependent RNA helicase p54|DEAD (Asp-Glu-Ala-Asp) box polypeptide 6|DEAD box protein 6|DEAD box-6|DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 6 (RNA helicase, 54kD)|oncogene RCK|probable ATP-dependent RNA helicase DDX6 DDX6 OGG:3000001719 Bin Zhao, Yue Liu, Oliver He DHFRP1 DYR WEB: http://www.ncbi.nlm.nih.gov/gene DHFR dihydrofolate reductase 1719 5q11.2-q13.2 20140408 9606 5 protein-coding Official from a nomenclature committee PMID: 1731871; 1935897; 2248959; 2592384; 2859520; 3185016; 3383852; 6235374; 6306253; 6323448; 6504041; 6687716; 6750132; 8527095; 8559246; 8976559; 9119086; 9374868; 10749676; 10898545; 11448909; 11779239; 11964483; 11996001; 12084458; 12096917; 12384595; 12477932; 12588981; 12612070; 12788094; 12812497; 14664697; 14679136; 14735580; 15039552; 15489334; 15755837; 15817466; 16116078; 16124424; 16196087; 16467096; 16735474; 16969375; 17237763; 17336564; 17413111; 17449906; 17486595; 17597297; 17683969; 17917571; 18045573; 18056255; 18093916; 18247058; 18451149; 18498051; 18636124; 18676680; 18682947; 18785313; 18799873; 18818748; 18988749; 19019335; 19022952; 19048631; 19055622; 19064572; 19064578; 19161160; 19170196; 19196009; 19336370; 19353223; 19360472; 19461557; 19471022; 19493349; 19527514; 19533788; 19536847; 19578876; 19625176; 19666584; 19683694; 19692168; 19706381; 19727391; 19776634; 19861437; 19898482; 19913121; 20031554; 20237949; 20347265; 20472929; 20544798; 20615890; 20628086; 20634891; 20639865; 20670920; 20737570; 20834190; 20948192; 21120433; 21310276; 21310277; 21857842; 21890473; 21906983; 21963094; 22005284; 22024482; 22324981; 22505724; 22797925; 22954684; 22994778; 23000965; 23053953; 23197646; 23421317; 23707606; 23726796; 23733948; 23838799; 24053334; 24077226 dihydrofolate reductase Ensembl:ENSG00000228716 HGNC:2861 HPRD:00519 MIM:126060 Vega:OTTHUMG00000162529 DHFR OGG:3000001728 Bin Zhao, Yue Liu, Oliver He DHQU DIA4 DTD NMOR1 NMORI QR1 WEB: http://www.ncbi.nlm.nih.gov/gene NQO1 NAD(P)H dehydrogenase, quinone 1 1728 16q22.1 9606 16 Official from a nomenclature committee GO_0003955 (EC: IEA); GO_0004128 (EC: TAS, PMID: 9579781); GO_0004784 (EC: IEA); GO_0005515 (EC: IPI, PMID: 18388957); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006521 (EC: TAS); GO_0006801 (EC: IEA); GO_0006805 (EC: TAS, PMID: 10393963); GO_0006809 (EC: TAS, PMID: 9579781); GO_0006979 (EC: IEA); GO_0007271 (EC: TAS, PMID: 9579781); GO_0007568 (EC: IEA); GO_0007584 (EC: IEA); GO_0009636 (EC: TAS, PMID: 10393963); GO_0032355 (EC: IEA); GO_0034641 (EC: TAS); GO_0043025 (EC: IEA); GO_0043086 (EC: IEA); GO_0043525 (EC: IEA); GO_0044281 (EC: TAS); GO_0044822 (EC: IDA); GO_0045471 (EC: IEA) PMID: 1340765; 1657151; 1737339; 2071140; 2843525; 8125298; 9230185; 9579781; 10393963; 10447260; 10487530; 10543876; 10706635; 11051261; 11219774; 11319169; 11520401; 11551408; 11679176; 11688992; 11701227; 11722480; 11766168; 11773862; 11774269; 11810042; 11821413; 11840286; 11888914; 11894133; 11895912; 11943609; 11948402; 11956078; 11967624; 12018106; 12036913; 12037698; 12163326; 12164325; 12171070; 12171760; 12172217; 12232053; 12370194; 12383707; 12393447; 12393620; 12397416; 12417987; 12419832; 12439220; 12460800; 12468438; 12477932; 12480594; 12529318; 12694753; 12711112; 12713578; 12718576; 12718704; 12771035; 12777965; 12834817; 12854127; 12867492; 12960511; 13130177; 14506737; 14568289; 14592434; 14634213; 14634838; 14669229; 14675732; 14688016; 14694720; 14716779; 14720419; 14729580; 14985350; 15028279; 15061915; 15079792; 15111988; 15116053; 15138483; 15151706; 15184245; 15196853; 15219943; 15226677; 15279067; 15280903; 15298951; 15312971; 15334552; 15352038; 15355699; 15365958; 15370874; 15382274; 15385560; 15466980; 15489334; 15498787; 15590400; 15618957; 15640066; 15661231; 15694256; 15714076; 15727169; 15731166; 15734732; 15746160; 15747169; 15748501; 15749015; 15763338; 15767364; 15781212; 15808404; 15829318; 15838728; 15938845; 16003741; 16006997; 16038261; 16039674; 16054862; 16079101; 16157195; 16170238; 16172237; 16235982; 16235998; 16266898; 16284498; 16297214; 16321221; 16341674; 16343742; 16369108; 16385446; 16413497; 16520888; 16532285; 16595077; 16598069; 16610002; 16620556; 16702380; 16775388; 16818284; 16978807; 16985026; 17011189; 17027152; 17082176; 17113562; 17118447; 17119198; 17164365; 17166422; 17178637; 17179690; 17188257; 17332305; 17332311; 17337051; 17363580; 17367411; 17372252; 17378176; 17395013; 17400324; 17405841; 17424838; 17428572; 17449559; 17469025; 17476281; 17496311; 17507624; 17541156; 17575500; 17581325; 17603928; 17619904; 17644186; 17652311; 17669387; 17726138; 17869325; 17885617; 17901563; 18024413; 18029348; 18034618; 18061666; 18061941; 18074351; 18091324; 18098117; 18156703; 18203021; 18214807; 18218609; 18225579; 18253865; 18388957; 18393254; 18404535; 18407955; 18413200; 18416817; 18444152; 18444911; 18457324; 18510611; 18511948; 18569591; 18587252; 18601742; 18632753; 18636124; 18676018; 18676680; 18720901; 18784359; 18798003; 18813798; 18820947; 18836923; 18936436; 18945694; 18950733; 18977034; 18981090; 18986377; 18992148; 19012493; 19012698; 19017358; 19027876; 19027952; 19059883; 19074885; 19096102; 19138946; 19151739; 19162321; 19170196; 19174490; 19179423; 19214744; 19229058; 19251446; 19330589; 19336370; 19339270; 19360290; 19362588; 19382518; 19415745; 19456854; 19494791; 19549356; 19591959; 19593802; 19596483; 19625176; 19628038; 19651439; 19652895; 19657853; 19661089; 19671875; 19688691; 19692168; 19705749; 19715479; 19736056; 19738201; 19759547; 19778569; 19789190; 19808663; 19822020; 19899130; 19913121; 19952119; 20026093; 20027111; 20028737; 20049130; 20049212; 20056632; 20085630; 20091863; 20100551; 20110814; 20193673; 20194081; 20198579; 20200430; 20204281; 20214802; 20226854; 20331656; 20371868; 20373852; 20375710; 20391128; 20437850; 20453000; 20461808; 20480521; 20480816; 20511665; 20526719; 20526805; 20534171; 20568895; 20593958; 20599494; 20613985; 20628086; 20634891; 20663217; 20701904; 20819778; 20824655; 20851451; 20878130; 20935060; 20951227; 20962519; 20966810; 21041608; 21073132; 21117316; 21133623; 21139048; 21176850; 21211285; 21220432; 21253823; 21294640; 21329464; 21351093; 21479364; 21480392; 21502369; 21518531; 21524888; 21531452; 21577322; 21602889; 21605663; 21706157; 21718050; 21755707; 21756955; 21800014; 21861350; 21906983; 21946896; 21963094; 21964527; 21989715; 22016051; 22017531; 22021338; 22116627; 22215148; 22249251; 22272361; 22306249; 22387672; 22393995; 22483869; 22586705; 22623428; 22736108; 22770696; 22793692; 22853296; 22911602; 22925602; 22939629; 22960073; 22972504; 22976839; 22984577; 23000965; 23054000; 23065291; 23066387; 23066397; 23086932; 23110137; 23215885; 23249637; 23275341; 23276910; 23360829; 23390006; 23458878; 23468244; 23497461; 23643325; 23648480; 23651475; 23725139; 23749485; 23803694; 23824909; 23840148; 23852860; 23860519; 23873104; 23893397; 23918565; 24053646; 24140708 NAD(P)H dehydrogenase, quinone 1 Ensembl:ENSG00000181019 HGNC:2874 HPRD:00518 MIM:125860 Vega:OTTHUMG00000137575 Other designations: DT-diaphorase|NAD(P)H dehydrogenase [quinone] 1|NAD(P)H:Quinone acceptor oxidoreductase type 1|NAD(P)H:menadione oxidoreductase 1|NAD(P)H:quinone oxidoreductase 1|NAD(P)H:quinone oxireductase|azoreductase|diaphorase (NADH/NADPH) (cytochrome b-5 reductase)|diaphorase-4|dioxin-inducible 1|menadione reductase|phylloquinone reductase|quinone reductase 1 NQO1 OGG:3000001803 Bin Zhao, Yue Liu, Oliver He ADABP ADCP2 CD26 DPPIV TP103 WEB: http://www.ncbi.nlm.nih.gov/gene DPP4 dipeptidyl-peptidase 4 1803 2q24.3 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0001666 (EC: IDA, PMID: 16670267); GO_0002020 (EC: IPI, PMID: 16651416); GO_0004177 (EC: IEA); GO_0004252 (EC: IEA); GO_0005102 (EC: IPI, PMID: 10900005); GO_0005515 (EC: IPI, PMID: 14684150); GO_0005765 (EC: IDA, PMID: 17897319); GO_0005886 (EC: IDA, PMID: 16670267); GO_0007155 (EC: IEA); GO_0008236 (EC: IDA, PMID: 14684150); GO_0008239 (EC: IDA, PMID: 14684150); GO_0008284 (EC: IDA, PMID: 17549790); GO_0009986 (EC: IDA, PMID: 10900005); GO_0010716 (EC: IDA, PMID: 16651416); GO_0016021 (EC: IEA); GO_0016324 (EC: IDA, PMID: 15052268); GO_0030027 (EC: IDA, PMID: 16651416); GO_0030139 (EC: IDA, PMID: 10900005); GO_0031258 (EC: IEA); GO_0031295 (EC: IDA, PMID: 10900005); GO_0033632 (EC: IDA, PMID: 11772392); GO_0042110 (EC: IDA, PMID: 7594462); GO_0042802 (EC: IPI); GO_0042803 (EC: IPI, PMID: 14684150); GO_0043542 (EC: IDA, PMID: 16651416); GO_0045121 (EC: IEA); GO_0046581 (EC: IEA); GO_0070062 (EC: IDA, PMID: 11487543); GO_0071438 (EC: IDA, PMID: 16651416) PMID: 1347043; 1352530; 1352704; 1362202; 1677636; 1680916; 1975616; 1977364; 7487939; 7522442; 7539755; 7585218; 7594462; 7833626; 7903479; 7911242; 7912830; 7927537; 8094732; 8095514; 8096237; 8101391; 8635502; 8763423; 8806567; 8852605; 8925885; 9103436; 9185130; 9252108; 9263011; 9330689; 9330696; 9330699; 9374514; 9516414; 9537773; 9645485; 9671214; 9685737; 9710254; 9933589; 10880264; 10899322; 10900005; 10961862; 11278278; 11390394; 11487543; 11549856; 11696365; 11739156; 11739489; 11772392; 11773049; 11831694; 11882590; 11901152; 12023964; 12031601; 12047913; 12095981; 12112826; 12175726; 12176563; 12213886; 12239451; 12437097; 12471135; 12477932; 12483204; 12529175; 12579300; 12595736; 12634639; 12646248; 12675218; 12675220; 12675229; 12675231; 12675232; 12675233; 12675238; 12675243; 12675245; 12675246; 12675247; 12675248; 12675253; 12675254; 12690074; 12727530; 12752434; 12767062; 12790770; 12820316; 12832764; 12906826; 14525771; 14630704; 14684150; 14684825; 14691230; 14718659; 15002062; 15016824; 15027119; 15052268; 15146553; 15175333; 15213224; 15215186; 15292258; 15323360; 15353589; 15375776; 15448155; 15489334; 15490304; 15540901; 15681827; 15695814; 15797249; 15819895; 15864535; 15866709; 15911629; 15985311; 16335952; 16611738; 16621928; 16651416; 16670267; 16700508; 16700520; 16700525; 16704418; 16778789; 16781669; 16829852; 17071493; 17091451; 17244786; 17270095; 17287217; 17492130; 17525828; 17549790; 17610364; 17786309; 17846797; 17897319; 17904681; 17944883; 17949241; 18007554; 18189200; 18496701; 18520029; 18538760; 18563594; 18595667; 18606664; 18682883; 18708048; 18820218; 18940185; 18976975; 18983807; 19024603; 19061927; 19153055; 19247978; 19327104; 19358731; 19459926; 19469710; 19632987; 19654580; 19687096; 19734982; 19762327; 19811413; 19817894; 19913121; 19917055; 20008019; 20043068; 20075514; 20155839; 20185737; 20198559; 20361950; 20455069; 20459800; 20468064; 20495958; 20520837; 20534982; 20569697; 20572019; 20584285; 20628086; 20628624; 20805868; 20828536; 20841351; 20847730; 20878214; 20942971; 21108831; 21198750; 21281985; 21284881; 21334743; 21526345; 21558160; 21593202; 21614532; 21656024; 21672052; 21674250; 21785903; 21856036; 21894438; 21917073; 21951552; 21988832; 22001206; 22062893; 22086610; 22153807; 22167343; 22179204; 22185679; 22261805; 22369943; 22382050; 22388283; 22406180; 22504421; 22539793; 22561447; 22648548; 22674411; 22806538; 22846168; 22908963; 22949266; 22982114; 23035207; 23113658; 23122333; 23160239; 23184393; 23197976; 23219738; 23327927; 23382843; 23437290; 23486063; 23544270; 23548652; 23575259; 23586735; 23603488; 23608773; 23638030; 23654079; 23677473; 23894014; 24067970 dipeptidyl-peptidase 4 Ensembl:ENSG00000197635 HGNC:3009 HPRD:02187 MIM:102720 Vega:OTTHUMG00000132056 Other designations: ADCP-2|DPP IV|T-cell activation antigen CD26|adenosine deaminase complexing protein 2|dipeptidyl peptidase 4|dipeptidyl peptidase IV|dipeptidylpeptidase 4|dipeptidylpeptidase IV (CD26, adenosine deaminase complexing protein 2) DPP4 OGG:3000001806 Bin Zhao, Yue Liu, Oliver He DHP DHPDHASE DPD WEB: http://www.ncbi.nlm.nih.gov/gene DPYD dihydropyrimidine dehydrogenase 1806 1p22 9606 1 Official from a nomenclature committee GO_0004158 (EC: IEA); GO_0005737 (EC: IDA, PMID: 1512248); GO_0005829 (EC: IDA, PMID: 9348115); GO_0005829 (EC: TAS); GO_0006145 (EC: IMP, PMID: 11988088); GO_0006206 (EC: TAS); GO_0006208 (EC: IMP, PMID: 11988088); GO_0006208 (EC: ISS); GO_0006210 (EC: IDA, PMID: 10410956); GO_0006212 (EC: IDA, PMID: 1512248); GO_0006214 (EC: IDA, PMID: 1512248); GO_0006222 (EC: IEA); GO_0017113 (EC: IDA, PMID: 10410956); GO_0017113 (EC: IMP, PMID: 11988088); GO_0017113 (EC: ISS); GO_0017113 (EC: TAS); GO_0019483 (EC: IEA); GO_0042803 (EC: IDA, PMID: 1512248); GO_0042803 (EC: ISS); GO_0044281 (EC: TAS); GO_0046135 (EC: TAS); GO_0046872 (EC: IEA); GO_0050660 (EC: ISS); GO_0050661 (EC: ISS); GO_0051539 (EC: IEA); GO_0055086 (EC: TAS) PMID: 1512248; 1544906; 1901022; 2319593; 2528450; 3335642; 7713523; 8083224; 8221682; 8892022; 9135003; 9170156; 9266349; 9348115; 9439663; 9464498; 10410956; 10606257; 10923099; 11072080; 11267945; 11555601; 11862480; 11895907; 11988088; 11992400; 12025228; 12047484; 12209976; 12360106; 12477932; 12576451; 12822071; 12844478; 12851836; 14519634; 14562021; 14654904; 14702180; 15017333; 15025795; 15069545; 15102667; 15132136; 15254700; 15316940; 15709212; 15939134; 15993511; 15999119; 16021908; 16132996; 16328315; 16344560; 16361556; 16771603; 16786143; 16806531; 16820886; 16969493; 17000685; 17046731; 17121937; 17165084; 17203168; 17335544; 17375478; 17377791; 17397246; 17417073; 17445431; 17582309; 17582310; 17612628; 17699798; 17828463; 17848752; 17876700; 17905396; 18004243; 18075467; 18225548; 18299612; 18347391; 18443386; 18452418; 18537153; 18619742; 18705276; 18937829; 19020767; 19104657; 19154585; 19178088; 19288105; 19295264; 19296131; 19343046; 19473056; 19530960; 19546880; 19571608; 19636001; 19724871; 19795123; 19822137; 19858398; 19898482; 19956635; 20037211; 20157331; 20379614; 20385995; 20407238; 20453000; 20507294; 20530282; 20544545; 20570913; 20647221; 20647710; 20653680; 20665215; 20714149; 20714877; 20803296; 20809970; 20819423; 20837458; 21057378; 21111509; 21114665; 21498394; 21507922; 21612699; 21822266; 21919605; 21963094; 21965773; 21987572; 22003227; 22006578; 22143355; 22199347; 22270332; 22306127; 22339448; 22490566; 22505724; 22510597; 22593457; 22641663; 22688191; 22939629; 23313143; 23401991; 23453885; 23588312; 23603345; 23736036; 23781135; 23930673; 23960437; 23974872; 24104963 dihydropyrimidine dehydrogenase Ensembl:ENSG00000188641 HGNC:3012 HPRD:02036 MIM:612779 Vega:OTTHUMG00000039683 Other designations: dihydropyrimidine dehydrogenase [NADP(+)]|dihydrothymine dehydrogenase|dihydrouracil dehydrogenase DPYD OGG:3000001831 Bin Zhao, Yue Liu, Oliver He DIP DSIPI GILZ TSC-22R hDIP WEB: http://www.ncbi.nlm.nih.gov/gene TSC22D3 TSC22 domain family, member 3 1831 RP13-364K23.1 Xq22.3 9606 X Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0003700 (EC: IEA); GO_0005634 (EC: IEA); GO_0005829 (EC: TAS); GO_0006355 (EC: TAS, PMID: 8982256); GO_0006970 (EC: IEA); GO_0007589 (EC: IEA); GO_0034220 (EC: TAS); GO_0043426 (EC: IEA); GO_0048642 (EC: IEA); GO_0055085 (EC: TAS); GO_0070236 (EC: IEA) PMID: 8619474; 8982256; 9110174; 11230166; 11313722; 11397794; 11468175; 11688842; 12391160; 12393603; 12477932; 12671681; 14702039; 15031210; 15489334; 15705665; 16189514; 16196087; 16216878; 17356131; 17956870; 18468809; 18499442; 19260870; 19322201; 19380724; 19814803; 19875485; 20018851; 20124407; 20671745; 20947508; 20970683; 21512757; 21556028; 21726808; 21750716; 21804606; 21906983; 21988832; 22137507; 22539300; 22832853; 23440419; 23494955; 23573276; 23650723; 23729444 TSC22 domain family, member 3 Ensembl:ENSG00000157514 HGNC:3051 HPRD:04266 MIM:300506 Vega:OTTHUMG00000022168 Other designations: DSIP-immunoreactive leucine zipper protein|DSIP-immunoreactive peptide|TSC-22 related protein|TSC-22-like protein|TSC-22-related protein|TSC22 domain family protein 3|delta sleep inducing peptide, immunoreactor|delta sleep-inducing peptide immunoreactor|glucocorticoid-induced leucine zipper protein TSC22D3 OGG:3000001842 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene ECM2 extracellular matrix protein 2, female organ and adipocyte specific 1842 RP11-77D6.2 9q22.3 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0005178 (EC: TAS, PMID: 9790758); GO_0005578 (EC: TAS, PMID: 9790758); GO_0005614 (EC: IEA); GO_0007160 (EC: TAS, PMID: 9790758); GO_0008201 (EC: IEA); GO_0010811 (EC: IEA); GO_0030198 (EC: IEA); GO_0070052 (EC: IEA) PMID: 8889548; 9345023; 9790758; 11076863; 11230166; 12477932; 15164053; 15489334; 15489336; 16381901 extracellular matrix protein 2, female organ and adipocyte specific Other designations: extracellular matrix protein 2|matrix glycoprotein SC1/ECM2 ECM2 OGG:3000001891 Bin Zhao, Yue Liu, Oliver He HPXEL WEB: http://www.ncbi.nlm.nih.gov/gene ECH1 enoyl CoA hydratase 1, peroxisomal 1891 19q13.1 9606 19 Official from a nomenclature committee GO_0005102 (EC: IPI); GO_0005515 (EC: IPI, PMID: 15383276); GO_0005739 (EC: IEA); GO_0005777 (EC: NAS, PMID: 7558027); GO_0006635 (EC: IEA); GO_0016853 (EC: IEA); GO_0070062 (EC: IDA) PMID: 7558027; 9417087; 12477932; 14500732; 15383276; 15489334; 16169070; 16482509; 16615866; 17081983; 17676665; 18029348; 20178365; 20186120; 20877624; 21081666; 21139048; 21565611; 21832049; 21890473; 21906983; 21988832; 22002062; 22939629; 24255178 enoyl CoA hydratase 1, peroxisomal Ensembl:ENSG00000104823 HGNC:3149 HPRD:02825 MIM:600696 Vega:OTTHUMG00000182609 Other designations: delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial|delta3,5-delta2,4-dienoyl-CoA isomerase|dienoyl-CoA isomerase|enoyl Coenzyme A hydratase 1, peroxisomal|peroxisomal enoyl-CoA hydratase 1 ECH1 OGG:3000001906 Bin Zhao, Yue Liu, Oliver He ARCND3 ET1 HDLCQ7 PPET1 QME WEB: http://www.ncbi.nlm.nih.gov/gene EDN1 endothelin 1 1906 6p24.1 9606 6 Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 19767294); GO_0001516 (EC: IDA, PMID: 9492062); GO_0001569 (EC: IEA); GO_0001666 (EC: IEA); GO_0001701 (EC: IEA); GO_0001821 (EC: IEA); GO_0003100 (EC: IDA, PMID: 2649896); GO_0005125 (EC: IDA, PMID: 19767294); GO_0005179 (EC: IDA, PMID: 10770212); GO_0005515 (EC: IPI); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 10770212); GO_0005737 (EC: IDA, PMID: 12379507); GO_0006885 (EC: IEA); GO_0007166 (EC: IDA, PMID: 1713452); GO_0007186 (EC: IDA, PMID: 17078114); GO_0007204 (EC: IDA, PMID: 1917960); GO_0007205 (EC: IEA); GO_0007267 (EC: IDA, PMID: 12379507); GO_0007507 (EC: IEA); GO_0007585 (EC: IEA); GO_0007589 (EC: IEA); GO_0008284 (EC: IDA, PMID: 17078114); GO_0009953 (EC: IEA); GO_0010259 (EC: IEA); GO_0010460 (EC: IDA, PMID: 2649896); GO_0010595 (EC: TAS, PMID: 8999856); GO_0010613 (EC: IDA, PMID: 12847114); GO_0010870 (EC: IDA, PMID: 17178876); GO_0014032 (EC: IEA); GO_0014065 (EC: IDA, PMID: 17078114); GO_0014824 (EC: IDA, PMID: 8982507); GO_0014824 (EC: TAS, PMID: 1725334); GO_0014826 (EC: IDA, PMID: 9422810); GO_0015758 (EC: IEA); GO_0016049 (EC: IEA); GO_0019229 (EC: IEA); GO_0019233 (EC: IEA); GO_0019722 (EC: IDA, PMID: 10770212); GO_0030072 (EC: IDA, PMID: 10770212); GO_0030185 (EC: IDA, PMID: 16820593); GO_0030195 (EC: TAS, PMID: 16820593); GO_0030335 (EC: IDA, PMID: 9696419); GO_0030593 (EC: IDA, Qualifier: NOT, PMID: 9696419); GO_0030818 (EC: IEA); GO_0031583 (EC: IEA); GO_0031707 (EC: IDA, PMID: 10770212); GO_0031708 (EC: IDA, PMID: 10770212); GO_0032269 (EC: IDA, PMID: 19767294); GO_0032496 (EC: IEA); GO_0033574 (EC: IEA); GO_0034392 (EC: IEA); GO_0035094 (EC: IEA); GO_0035810 (EC: IEA); GO_0035815 (EC: IEA); GO_0042045 (EC: IEA); GO_0042310 (EC: IDA, PMID: 11410113); GO_0042313 (EC: IDA, PMID: 16820593); GO_0042474 (EC: IEA); GO_0042482 (EC: IEA); GO_0042554 (EC: IEA); GO_0043179 (EC: IEA); GO_0043200 (EC: IEA); GO_0043406 (EC: IDA, PMID: 10770212); GO_0043507 (EC: IDA, PMID: 12847114); GO_0045321 (EC: TAS, PMID: 16820593); GO_0045429 (EC: TAS, PMID: 8999856); GO_0045793 (EC: IDA, PMID: 12847114); GO_0045840 (EC: IDA, PMID: 10770212); GO_0045987 (EC: IEA); GO_0046887 (EC: IDA, PMID: 10770212); GO_0046888 (EC: IEA); GO_0048016 (EC: IDA, PMID: 1917960); GO_0048661 (EC: IDA, PMID: 10393673); GO_0051216 (EC: IEA); GO_0051482 (EC: IEA); GO_0051771 (EC: IDA, PMID: 16820593); GO_0051899 (EC: IEA); GO_0051930 (EC: IEA); GO_0060137 (EC: IEA); GO_0060298 (EC: IMP, PMID: 12847114); GO_0060585 (EC: IMP, PMID: 9492062); GO_0070101 (EC: IC, PMID: 17178876); GO_0071347 (EC: IEA); GO_0071356 (EC: IEA); GO_0090023 (EC: IEA) PMID: 1280264; 1422154; 1515112; 1713452; 1725334; 1736987; 1859417; 1864385; 1917960; 2005113; 2018043; 2201681; 2649896; 2659594; 2670930; 2678110; 3282927; 7509919; 7664037; 7773179; 8125160; 8144511; 8450044; 8482849; 8889548; 8982507; 8999856; 9257865; 9284755; 9324057; 9422810; 9453574; 9492062; 9595387; 9696419; 10220569; 10231710; 10334806; 10391210; 10393673; 10438732; 10620363; 10770212; 11179511; 11210078; 11399938; 11410113; 11448123; 11593097; 11601839; 11693192; 11742499; 11751711; 11795667; 11831453; 11858185; 11866544; 11932487; 11934840; 11991554; 11991733; 12009599; 12011762; 12013496; 12068797; 12077518; 12082592; 12087564; 12107733; 12117726; 12137974; 12144123; 12151765; 12189238; 12230494; 12379507; 12446192; 12459174; 12477932; 12508654; 12511547; 12529269; 12557940; 12565798; 12588850; 12620701; 12629276; 12657945; 12695528; 12721154; 12746758; 12750312; 12847114; 12855940; 12861161; 12887757; 12907686; 12941866; 12963677; 12972292; 13680553; 14514737; 14519635; 14523636; 14558091; 14574404; 14578413; 14587645; 14602502; 14634722; 14636060; 14639018; 14660616; 14685288; 14692644; 14733410; 14735061; 14736087; 14763917; 14769714; 15009217; 15041798; 15044479; 15047866; 15073116; 15093707; 15126915; 15139053; 15161426; 15188945; 15194301; 15198485; 15213100; 15224360; 15240857; 15269821; 15319532; 15347673; 15369130; 15466627; 15481145; 15489334; 15505112; 15518541; 15558022; 15568807; 15610525; 15621731; 15623376; 15643502; 15646831; 15652492; 15691296; 15699938; 15702240; 15743480; 15817494; 15818445; 15838269; 15838299; 15838323; 15838328; 15838333; 15838334; 15838336; 15838337; 15838340; 15838344; 15838351; 15838357; 15838368; 15838369; 15838370; 15864745; 15946241; 15946919; 15979050; 15988412; 16002759; 16021085; 16026642; 16076689; 16095497; 16097909; 16098041; 16169070; 16217751; 16234608; 16291872; 16320159; 16336267; 16357176; 16452160; 16466695; 16521405; 16526196; 16531800; 16582543; 16597412; 16648553; 16713569; 16720059; 16754659; 16769575; 16778329; 16809784; 16815566; 16820593; 16864942; 16931893; 16943682; 16947775; 16956834; 16971893; 16982943; 16986361; 17016610; 17016617; 17020466; 17078114; 17122448; 17123690; 17148661; 17178876; 17197385; 17203161; 17221318; 17222082; 17264805; 17274718; 17291632; 17328840; 17335511; 17340622; 17345061; 17353514; 17357073; 17357519; 17395629; 17404040; 17438153; 17444275; 17460393; 17470272; 17497038; 17497041; 17497362; 17505299; 17525706; 17535295; 17549358; 17556493; 17569300; 17575543; 17576235; 17664075; 17664854; 17681742; 17693542; 17701914; 17703412; 17850909; 17855483; 17875064; 17884295; 17893002; 17913962; 17938376; 17960156; 17967707; 17969585; 17996929; 18005077; 18023202; 18025413; 18031458; 18050250; 18063846; 18080871; 18212505; 18260253; 18288492; 18326921; 18346810; 18378042; 18379872; 18390205; 18395679; 18398338; 18401297; 18411415; 18436890; 18441204; 18442814; 18447854; 18463805; 18484695; 18489822; 18550016; 18568290; 18579320; 18579652; 18580062; 18603063; 18623111; 18660489; 18663623; 18676680; 18752143; 18764935; 18772174; 18794727; 18806884; 18809573; 18814847; 18822124; 18923236; 18945274; 18945538; 18953265; 18974277; 18991099; 18991188; 19012521; 19014602; 19046960; 19056482; 19057845; 19073831; 19074885; 19077312; 19086031; 19086263; 19087492; 19103606; 19116719; 19150882; 19170196; 19171135; 19188658; 19188660; 19212702; 19217622; 19225824; 19247692; 19254215; 19258923; 19264973; 19336370; 19358249; 19367425; 19369451; 19371341; 19391127; 19415232; 19416273; 19420105; 19446279; 19460784; 19475602; 19479828; 19520685; 19520754; 19526396; 19527488; 19536618; 19543207; 19558538; 19564455; 19578796; 19592490; 19625176; 19626996; 19634784; 19640695; 19661472; 19672034; 19687345; 19692168; 19717811; 19729965; 19730395; 19764340; 19767294; 19808370; 19862540; 19887561; 19899414; 19907721; 19913121; 19927348; 19948975; 19996987; 20015663; 20016521; 20028935; 20031624; 20051644; 20055532; 20055806; 20082271; 20083228; 20083432; 20091488; 20150570; 20188614; 20204072; 20217138; 20308035; 20339975; 20346360; 20368210; 20370579; 20416077; 20437399; 20452482; 20452970; 20485444; 20495015; 20497976; 20503287; 20537417; 20538124; 20538960; 20559285; 20562228; 20565774; 20572854; 20587610; 20588001; 20594474; 20594999; 20602615; 20608808; 20628086; 20628425; 20628428; 20634595; 20634796; 20634891; 20652766; 20663522; 20664700; 20670842; 20672350; 20673868; 20678167; 20685405; 20707291; 20725135; 20725137; 20725140; 20725141; 20725143; 20728421; 20837776; 20837906; 20873151; 20952631; 20952681; 20971496; 20974279; 21045115; 21059990; 21087804; 21129745; 21169360; 21174590; 21183790; 21208707; 21214096; 21217075; 21219832; 21251377; 21334758; 21356562; 21406182; 21418087; 21445967; 21490504; 21498707; 21498912; 21499502; 21515378; 21531894; 21557930; 21601190; 21637825; 21638248; 21656314; 21659661; 21666117; 21673044; 21677436; 21681744; 21701170; 21701423; 21712053; 21730058; 21741393; 21767690; 21773759; 21777246; 21786569; 21801587; 21801592; 21813388; 21826669; 21851036; 21896842; 21908890; 21932697; 21952518; 21959927; 22006997; 22045428; 22082020; 22113444; 22165675; 22175913; 22232246; 22265324; 22299030; 22321643; 22330820; 22341591; 22377253; 22406080; 22412088; 22415226; 22483689; 22483692; 22503784; 22504006; 22520393; 22525370; 22527528; 22545467; 22552325; 22553998; 22569256; 22580289; 22666926; 22675930; 22727793; 22759779; 22770822; 22796455; 22856221; 22856224; 22869459; 22907118; 22960172; 22965194; 22971991; 22994522; 23002189; 23018104; 23103494; 23142694; 23163519; 23208497; 23227981; 23233754; 23255664; 23273644; 23290569; 23329136; 23344160; 23372172; 23381795; 23401650; 23436272; 23436727; 23457411; 23523690; 23565184; 23643051; 23683481; 23713736; 23720837; 23815989; 23828677; 23832707; 23887640; 23902937; 24015303; 24056654; 24088894; 24184161; 24196534; 24268655 endothelin 1 Ensembl:ENSG00000078401 HGNC:3176 HPRD:07030 MIM:131240 Vega:OTTHUMG00000014266 Other designations: endothelin-1|preproendothelin-1 EDN1 OGG:3000001939 Bin Zhao, Yue Liu, Oliver He HCA56 LGTN WEB: http://www.ncbi.nlm.nih.gov/gene EIF2D eukaryotic translation initiation factor 2D 1939 RP11-534L20.3 1q32.1 9606 1 GO_0003743 (EC: IDA); GO_0004872 (EC: TAS, PMID:2482295); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA); GO_0006886 (EC: TAS, PMID:2482295) PMID:2482295; 7085778; 7299841; 8125298; 12097419; 12477932; 14702039; 15302935; 17353931; 20566627; 21145461; 22939629; 23277564; 24250222 eukaryotic translation initiation factor 2D Ensembl:ENSG00000143486 HGNC:6583 HPRD:01057 MIM:613709 Vega:OTTHUMG00000036344 Other designations: hepatocellular carcinoma-associated antigen 56|ligatin EIF2D OGG:3000001950 Bin Zhao, Yue Liu, Oliver He HOMG4 URG WEB: http://www.ncbi.nlm.nih.gov/gene EGF epidermal growth factor 1950 4q25 9606 4 GO_0000186 (EC: IEA); GO_0001525 (EC: IDA, PMID:15611079); GO_0002576 (EC: TAS); GO_0005154 (EC: TAS, PMID:15611079); GO_0005509 (EC: IEA); GO_0005515 (EC: IPI, PMID:12297050); GO_0005576 (EC: IC, PMID:9712850); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0005765 (EC: IDA, PMID:17897319); GO_0005886 (EC: IEA); GO_0006260 (EC: TAS, PMID:9482941); GO_0007165 (EC: TAS); GO_0007171 (EC: TAS, PMID:9712850); GO_0007173 (EC: TAS); GO_0007262 (EC: ISS); GO_0007596 (EC: TAS); GO_0008083 (EC: IDA, PMID:15611079); GO_0008284 (EC: IDA, PMID:15611079); GO_0008543 (EC: TAS); GO_0010800 (EC: IDA, PMID:16314496); GO_0016021 (EC: IEA); GO_0018108 (EC: IEA); GO_0021940 (EC: IEA); GO_0030168 (EC: TAS); GO_0030297 (EC: TAS, PMID:9712850); GO_0031093 (EC: TAS); GO_0035413 (EC: IDA); GO_0038095 (EC: TAS); GO_0042059 (EC: TAS); GO_0042327 (EC: IDA, PMID:15611079); GO_0043388 (EC: ISS); GO_0043406 (EC: IDA, PMID:15611079); GO_0045087 (EC: TAS); GO_0045741 (EC: IDA, PMID:15611079); GO_0045741 (EC: TAS, PMID:9712850); GO_0045840 (EC: IDA, PMID:15611079); GO_0045893 (EC: IDA, PMID:16314496); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0048754 (EC: IEA); GO_0051048 (EC: IDA, PMID:10559227); GO_0060749 (EC: IEA); GO_0070062 (EC: IDA, PMID:19056867); GO_0070371 (EC: IDA, PMID:16314496); GO_0090279 (EC: IDA, PMID:19996314); GO_0090370 (EC: IEA); GO_1900127 (EC: IDA, PMID:17324121); GO_2000008 (EC: IDA, PMID:19996314); GO_2000060 (EC: IEA) PMID:300079; 1281549; 1334406; 1501243; 1522591; 1639032; 2789514; 2790960; 3486749; 3491360; 6290982; 6382023; 6603475; 7540053; 7558411; 7615511; 7640657; 7730382; 7736574; 8077234; 8123596; 8413296; 8419140; 8639530; 8796265; 8845374; 9188692; 9356464; 9482941; 9544989; 9661876; 9687510; 9712850; 9925763; 10085134; 10199559; 10436156; 10559227; 10567358; 10579352; 10648629; 10734310; 10748174; 10788520; 10913131; 10973965; 11438527; 11751923; 11786904; 11796824; 11823423; 11844511; 11894095; 11896055; 11903419; 11914075; 11925427; 11950840; 11971908; 11994282; 12009575; 12093292; 12138086; 12141529; 12163055; 12163506; 12192610; 12202942; 12218189; 12297050; 12368284; 12388817; 12397374; 12425525; 12477932; 12508124; 12531699; 12540376; 12593796; 12620237; 12637502; 12643788; 12667326; 12672817; 12722480; 12768436; 12788694; 12795334; 12879019; 12954631; 12960147; 14507446; 14520709; 14523024; 14560030; 14614718; 14651960; 14662770; 14665621; 14676838; 15003992; 15063762; 15081423; 15087376; 15129177; 15175028; 15180992; 15183666; 15192046; 15194442; 15252009; 15256384; 15260478; 15272014; 15329330; 15373781; 15373782; 15373802; 15475003; 15481560; 15485655; 15485674; 15488707; 15489334; 15491342; 15509542; 15536154; 15574420; 15611079; 15613483; 15620700; 15622242; 15659382; 15663953; 15675968; 15729146; 15735691; 15748906; 15798095; 15802268; 15837620; 15860930; 15886816; 15901830; 15913871; 15950078; 15950906; 15962011; 15982634; 16019439; 16033767; 16115648; 16134968; 16210470; 16214932; 16248985; 16274239; 16274250; 16282324; 16314496; 16316319; 16332692; 16344560; 16407418; 16407834; 16413767; 16428382; 16436184; 16584205; 16636672; 16691190; 16728406; 16762922; 16788380; 16820871; 16837648; 16847055; 16872636; 16885506; 16939220; 16946702; 16969495; 16979250; 17123472; 17175377; 17204151; 17223314; 17227756; 17311928; 17316357; 17324121; 17334773; 17392355; 17397984; 17433039; 17453000; 17473192; 17479438; 17545148; 17562024; 17567965; 17573555; 17578349; 17612563; 17617058; 17626784; 17634901; 17661145; 17673689; 17762162; 17851837; 17852426; 17897319; 17898861; 17912028; 17940864; 17943082; 17950068; 17962208; 17968796; 17986122; 17991726; 17991733; 18006148; 18036246; 18080773; 18088275; 18094008; 18096367; 18156174; 18167406; 18187620; 18212060; 18271526; 18271972; 18276761; 18292095; 18325497; 18349392; 18365874; 18382118; 18398039; 18434322; 18441095; 18463167; 18467441; 18483390; 18485152; 18487214; 18490463; 18511414; 18519765; 18543351; 18571008; 18583979; 18632979; 18676680; 18722874; 18757521; 18773861; 18813355; 18831963; 18844210; 18990689; 19010984; 19011936; 19014905; 19020743; 19032382; 19056867; 19064572; 19073827; 19074885; 19081071; 19086053; 19087984; 19110611; 19124506; 19127217; 19141999; 19144868; 19167371; 19170196; 19172394; 19179548; 19203995; 19236842; 19319135; 19336395; 19380191; 19388850; 19403524; 19415484; 19453261; 19460345; 19470771; 19484147; 19488063; 19491269; 19492417; 19520791; 19531499; 19544388; 19549686; 19549816; 19592671; 19604397; 19608641; 19619867; 19624835; 19625176; 19634110; 19670348; 19692168; 19708171; 19727227; 19749156; 19817957; 19823871; 19834535; 19840254; 19840943; 19853299; 19880507; 19887603; 19895983; 19896111; 19900104; 19913121; 19920151; 19921131; 19951549; 19953086; 19996314; 20033794; 20036812; 20092031; 20101173; 20108217; 20126978; 20127414; 20157331; 20158379; 20164030; 20169434; 20197289; 20201065; 20201926; 20203692; 20207214; 20303009; 20332099; 20351270; 20362419; 20364107; 20375273; 20379614; 20398806; 20412119; 20418097; 20423485; 20424473; 20429940; 20430735; 20444693; 20453000; 20466569; 20472833; 20482449; 20487573; 20498653; 20514023; 20564212; 20587610; 20598233; 20606012; 20621058; 20628086; 20628624; 20631636; 20634891; 20644561; 20674545; 20690902; 20714325; 20727496; 20727996; 20800603; 20818748; 20819124; 20830310; 20832399; 20851879; 20854793; 20889718; 20963824; 20969541; 21029725; 21048224; 21062739; 21087604; 21099256; 21123997; 21186997; 21187523; 21209099; 21212517; 21224998; 21236296; 21247755; 21273531; 21274378; 21309478; 21358296; 21376205; 21436680; 21439278; 21533003; 21567271; 21678081; 21752154; 21868386; 21872446; 21971700; 21982438; 22022452; 22033246; 22070650; 22087246; 22106858; 22122913; 22129558; 22236006; 22279551; 22293333; 22308022; 22401280; 22403631; 22404757; 22413835; 22416276; 22433566; 22457050; 22479527; 22479638; 22481252; 22493503; 22503865; 22504456; 22505024; 22532606; 22534548; 22574813; 22578596; 22621366; 22668508; 22677173; 22701712; 22721997; 22727668; 22745586; 22773267; 22782629; 22797360; 22829589; 22829952; 22852842; 22914212; 22925500; 22951723; 22990108; 23007402; 23090954; 23188118; 23201894; 23219876; 23229345; 23382691; 23403233; 23419149; 23457387; 23466131; 23542467; 23577098; 23608378; 23631828; 23645212; 23689072; 23711349; 23731208; 23790025; 23843455; 23869217; 23869762; 23899513; 23902938; 23936413; 23963773; 24036907; 24043306; 24045955 epidermal growth factor Ensembl:ENSG00000138798 HGNC:3229 HPRD:00578 MIM:131530 Vega:OTTHUMG00000132044 Other designations: beta-urogastrone|pro-epidermal growth factor EGF OGG:3000001956 Bin Zhao, Yue Liu, Oliver He ERBB ERBB1 HER1 PIG61 mENA WEB: http://www.ncbi.nlm.nih.gov/gene EGFR epidermal growth factor receptor 1956 7p12 9606 7 GO_0000139 (EC: IEA); GO_0000165 (EC: NAS, PMID:15542601); GO_0001503 (EC: NAS, PMID:12925580); GO_0001889 (EC: IEA); GO_0001892 (EC: IEA); GO_0001934 (EC: IDA); GO_0001942 (EC: IEA); GO_0001948 (EC: IEA); GO_0003682 (EC: IDA); GO_0003690 (EC: NAS, PMID:6325948); GO_0004709 (EC: NAS, PMID:15542601); GO_0004713 (EC: IDA, PMID:17115032); GO_0004713 (EC: IMP, PMID:14702346); GO_0004713 (EC: TAS, PMID:16076471); GO_0004714 (EC: TAS); GO_0004716 (EC: IEA); GO_0004888 (EC: IDA, PMID:7736574); GO_0005006 (EC: IDA, PMID:12435727); GO_0005006 (EC: NAS, PMID:2790960); GO_0005178 (EC: IEA); GO_0005515 (EC: IPI, PMID:10026169); GO_0005524 (EC: IEA); GO_0005615 (EC: NAS, PMID:9103388); GO_0005634 (EC: IDA, PMID:12828935); GO_0005737 (EC: IDA); GO_0005768 (EC: IDA, PMID:14702346); GO_0005789 (EC: IEA); GO_0005886 (EC: IDA); GO_0005886 (EC: TAS); GO_0005976 (EC: IEA); GO_0006412 (EC: IEA); GO_0006950 (EC: NAS, PMID:12828935); GO_0006970 (EC: IEA); GO_0006979 (EC: IEA); GO_0007165 (EC: IDA, PMID:10572067); GO_0007165 (EC: TAS); GO_0007166 (EC: IDA, PMID:7736574); GO_0007173 (EC: IDA, PMID:12435727); GO_0007173 (EC: TAS); GO_0007202 (EC: TAS, PMID:12435727); GO_0007411 (EC: TAS); GO_0007435 (EC: IEA); GO_0007611 (EC: ISS); GO_0007623 (EC: IEA); GO_0008283 (EC: IDA, PMID:17115032); GO_0008284 (EC: IDA, PMID:7736574); GO_0008543 (EC: TAS); GO_0009986 (EC: IEA); GO_0010008 (EC: IEA); GO_0010960 (EC: IEA); GO_0016020 (EC: IDA, PMID:12435727); GO_0016021 (EC: IEA); GO_0016101 (EC: IEA); GO_0016323 (EC: IDA, PMID:12646923); GO_0016324 (EC: IEA); GO_0016337 (EC: IMP, PMID:12435727); GO_0018108 (EC: IDA, PMID:17115032); GO_0018108 (EC: IMP, PMID:14702346); GO_0018108 (EC: TAS, PMID:16076471); GO_0019694 (EC: IEA); GO_0019899 (EC: IPI, PMID:12009895); GO_0019901 (EC: IEA); GO_0019903 (EC: IPI, PMID:15899872); GO_0021795 (EC: IEA); GO_0030122 (EC: TAS, Qualifier: colocalizes_with, PMID:14702346); GO_0030235 (EC: IDA, Qualifier: contributes_to, PMID:12828935); GO_0030324 (EC: IEA); GO_0030335 (EC: IMP, PMID:12435727); GO_0031659 (EC: IDA, PMID:18483258); GO_0031965 (EC: IEA); GO_0032930 (EC: IEA); GO_0033590 (EC: IEA); GO_0033594 (EC: IEA); GO_0035413 (EC: IMP); GO_0035690 (EC: IEA); GO_0038095 (EC: TAS); GO_0042059 (EC: TAS); GO_0042177 (EC: IDA, PMID:17115032); GO_0042327 (EC: IDA, PMID:15082764); GO_0042698 (EC: IEA); GO_0042743 (EC: IEA); GO_0042802 (EC: IPI, PMID:16777603); GO_0043006 (EC: TAS, PMID:12435727); GO_0043066 (EC: IMP, PMID:18070883); GO_0043235 (EC: IDA); GO_0043406 (EC: IDA, PMID:10572067); GO_0043586 (EC: IEA); GO_0045087 (EC: TAS); GO_0045121 (EC: IDA, PMID:12009895); GO_0045429 (EC: IDA, PMID:12828935); GO_0045739 (EC: IDA, PMID:17115032); GO_0045740 (EC: IDA, PMID:17115032); GO_0045907 (EC: IEA); GO_0045909 (EC: IEA); GO_0045930 (EC: IEA); GO_0045944 (EC: IDA); GO_0046777 (EC: IMP, PMID:18070883); GO_0046982 (EC: IDA, PMID:10572067); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0048143 (EC: IEA); GO_0048146 (EC: IEA); GO_0048408 (EC: IEA); GO_0048471 (EC: IEA); GO_0048546 (EC: IEA); GO_0048661 (EC: IEA); GO_0050679 (EC: IDA, PMID:10572067); GO_0050729 (EC: IEA); GO_0050730 (EC: IMP, PMID:12435727); GO_0050999 (EC: IDA, PMID:12828935); GO_0051015 (EC: IDA, PMID:14702346); GO_0051205 (EC: TAS, PMID:12435727); GO_0051592 (EC: IEA); GO_0051897 (EC: IMP, PMID:17655843); GO_0051968 (EC: IEA); GO_0060571 (EC: IEA); GO_0070141 (EC: IDA, PMID:18483258); GO_0070374 (EC: IDA); GO_0070435 (EC: ISS); GO_0071260 (EC: IEA); GO_0071364 (EC: ISS); GO_0071392 (EC: IDA); GO_0071549 (EC: IEA) PMID:1281549; 1301150; 1309762; 1322798; 1333047; 1372092; 1382070; 1383230; 1385407; 1501243; 1505215; 1623525; 1633149; 1647028; 1651322; 1689310; 1706616; 1808202; 1850098; 1988448; 2173144; 2176151; 2434500; 2543678; 2543683; 2790960; 2810532; 2984676; 2985580; 2987962; 2991749; 2991899; 3039909; 3138233; 3329716; 6093780; 6297856; 6324343; 6325948; 6326261; 6328312; 6330563; 7506413; 7510700; 7518560; 7527043; 7532293; 7535770; 7540771; 7543024; 7588596; 7592693; 7623846; 7640657; 7654368; 7657591; 7657660; 7673163; 7682059; 7690989; 7730382; 7736574; 7761838; 7782294; 7880396; 7903710; 8125298; 8305738; 8375396; 8413296; 8493579; 8497321; 8577769; 8596488; 8610109; 8610433; 8621392; 8638121; 8639530; 8647288; 8647858; 8650580; 8657103; 8662998; 8702572; 8729040; 8798643; 8810325; 8845374; 8875975; 8885868; 8887653; 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23349873; 23350658; 23352033; 23358982; 23359207; 23359693; 23361279; 23363301; 23364874; 23370527; 23371026; 23371856; 23374155; 23374349; 23374350; 23378269; 23384599; 23384673; 23387315; 23387505; 23392229; 23397762; 23399900; 23404504; 23404538; 23407558; 23408463; 23410174; 23411345; 23413122; 23416450; 23418353; 23418425; 23419507; 23423768; 23425899; 23429996; 23435217; 23441167; 23443279; 23449277; 23456637; 23457600; 23461856; 23464964; 23465277; 23468578; 23468851; 23470965; 23472148; 23472669; 23477725; 23485129; 23486266; 23486275; 23486338; 23491080; 23494210; 23495083; 23499740; 23513863; 23514946; 23517177; 23520442; 23520446; 23521519; 23525704; 23532252; 23536719; 23540867; 23546020; 23548265; 23548963; 23555046; 23555641; 23558893; 23559009; 23563092; 23564810; 23564819; 23565769; 23569038; 23575413; 23575414; 23581229; 23583406; 23589287; 23590575; 23594562; 23595626; 23599147; 23601297; 23602387; 23608326; 23614656; 23617883; 23620765; 23620784; 23625205; 23628526; 23633480; 23635774; 23636329; 23638794; 23643362; 23644172; 23650389; 23651790; 23653350; 23661635; 23665199; 23668355; 23675485; 23677180; 23685782; 23686431; 23690991; 23693078; 23698466; 23700486; 23704979; 23707073; 23707413; 23710458; 23720781; 23721103; 23722667; 23729361; 23729401; 23731208; 23736812; 23744486; 23744832; 23746767; 23749785; 23754287; 23754386; 23757022; 23758840; 23763474; 23764002; 23764753; 23765179; 23765574; 23771370; 23774213; 23774386; 23780873; 23786162; 23786997; 23787814; 23790025; 23791006; 23791944; 23792604; 23799367; 23799848; 23806066; 23817698; 23822636; 23827764; 23841084; 23844533; 23850692; 23861540; 23866081; 23867504; 23871709; 23880166; 23886169; 23888049; 23892415; 23897813; 23897956; 23903906; 23908594; 23909080; 23909081; 23916913; 23921085; 23927961; 23932319; 23932718; 23938604; 23940030; 23945382; 23945384; 23945389; 23945392; 23948418; 23956138; 23966299; 23966300; 23972990; 23974272; 23986462; 23990774; 23991943; 23991992; 23994953; 23999497; 24002608; 24007863; 24012640; 24014028; 24015256; 24019463; 24034250; 24038070; 24043629; 24046058; 24053674; 24055032; 24058967; 24063894; 24067727; 24075601; 24076656; 24082147; 24091658; 24113009; 24120917; 24135280; 24142702; 24145651; 24170107; 24189400; 24200637; 24211838; 24216759; 24222141; 24222150; 24222153; 24240702; 24253040; 24278442; 24304721; 24369725; 24391216; 24404585; 24413169; 24439929; 24457318; 24510991 epidermal growth factor receptor Ensembl:ENSG00000146648 HGNC:3236 HPRD:00579 MIM:131550 Vega:OTTHUMG00000023661 Other designations: avian erythroblastic leukemia viral (v-erb-b) oncogene homolog|cell growth inhibiting protein 40|cell proliferation-inducing protein 61|proto-oncogene c-ErbB-1|receptor tyrosine-protein kinase erbB-1 EGFR OGG:3000001958 Bin Zhao, Yue Liu, Oliver He AT225 G0S30 KROX-24 NGFI-A TIS8 ZIF-268 ZNF225 WEB: http://www.ncbi.nlm.nih.gov/gene EGR1 early growth response 1 1958 5q31.1 9606 5 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0000976 (EC: IDA, PMID: 18718911); GO_0000979 (EC: IEA); GO_0001077 (EC: IEA); GO_0001975 (EC: IEA); GO_0003677 (EC: IDA, PMID: 12560508); GO_0003690 (EC: IEA); GO_0003700 (EC: IDA, PMID: 12560508); GO_0005515 (EC: IPI, PMID: 14979875); GO_0005634 (EC: IDA); GO_0005634 (EC: ISS); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA, PMID: 19057511); GO_0005737 (EC: ISS); GO_0006366 (EC: IDA, PMID: 19057511); GO_0007611 (EC: IEA); GO_0007623 (EC: IEA); GO_0008134 (EC: IEA); GO_0009749 (EC: IEA); GO_0019221 (EC: TAS); GO_0030217 (EC: IEA); GO_0030509 (EC: IEA); GO_0031667 (EC: IEA); GO_0032869 (EC: IEA); GO_0033233 (EC: IDA, PMID: 19057511); GO_0034465 (EC: IEA); GO_0035035 (EC: IPI); GO_0035690 (EC: IEA); GO_0035914 (EC: IBA); GO_0042220 (EC: IEA); GO_0043066 (EC: IBA); GO_0043525 (EC: IEA); GO_0043565 (EC: IDA, PMID: 1662794); GO_0045471 (EC: IEA); GO_0045893 (EC: IDA, PMID: 12560508); GO_0045944 (EC: IDA, PMID: 19057511); GO_0045944 (EC: IMP); GO_0046872 (EC: IEA); GO_0048169 (EC: IBA); GO_0048709 (EC: IEA); GO_0051602 (EC: IEA); GO_0060291 (EC: IEA); GO_0060337 (EC: TAS); GO_0070498 (EC: IMP); GO_0071236 (EC: IEA); GO_0071260 (EC: IEA); GO_0071317 (EC: IEA); GO_0071320 (EC: IBA); GO_0071363 (EC: IEA); GO_0071371 (EC: IBA); GO_0071372 (EC: IEA); GO_0071383 (EC: IEA); GO_0071455 (EC: IEA); GO_0071456 (EC: IEA); GO_0071480 (EC: IEA); GO_0071504 (EC: ISS); GO_0071506 (EC: ISS); GO_0071873 (EC: IEA); GO_0072110 (EC: ISS); GO_0072303 (EC: ISS); GO_0090090 (EC: IEA) PMID: 1090709; 1383501; 1411083; 1569051; 1662794; 1702972; 2109185; 2110381; 2377485; 3127059; 3839394; 7624335; 8662759; 8668170; 9806899; 10049687; 10051405; 10079243; 10082522; 10409428; 10575214; 10671503; 10806043; 10849212; 11124866; 11251186; 11278640; 11795984; 11819815; 11830539; 11909874; 11925592; 11956220; 11978801; 12011097; 12065847; 12165491; 12235180; 12379479; 12384223; 12393577; 12433834; 12439908; 12456801; 12457461; 12470865; 12477932; 12507899; 12517959; 12543866; 12553019; 12553721; 12560487; 12560508; 12566441; 12569082; 12571843; 12618431; 12637574; 12690110; 12706485; 12729460; 12840049; 12872165; 12890669; 12947119; 12958075; 14522979; 14662774; 14722058; 14744935; 14966901; 14979875; 14985468; 15003938; 15023995; 15155664; 15211096; 15225550; 15231681; 15449318; 15486985; 15489334; 15517593; 15523672; 15545275; 15548700; 15611055; 15616591; 15640148; 15689620; 15709168; 15875316; 15910736; 15923644; 15999367; 16007175; 16079301; 16091742; 16093249; 16260776; 16382041; 16393964; 16464174; 16552541; 16702209; 16741963; 16831524; 16858414; 16995904; 17099140; 17257596; 17420284; 17448597; 17494953; 17502875; 17516844; 17559061; 17581316; 17599039; 17631285; 17631291; 17671831; 17932312; 17967787; 17975260; 17986608; 18027854; 18067864; 18068676; 18088351; 18171299; 18174470; 18204200; 18215136; 18247371; 18281035; 18281687; 18303024; 18316600; 18324520; 18434015; 18434089; 18435749; 18460021; 18469860; 18489490; 18507785; 18515748; 18525291; 18583706; 18604866; 18636116; 18675783; 18682391; 18704310; 18711316; 18718911; 18772333; 18780286; 18830406; 18842581; 18989526; 19032775; 19050264; 19057511; 19067769; 19074480; 19074849; 19112164; 19115247; 19131339; 19152168; 19245972; 19261809; 19276347; 19307156; 19307576; 19374776; 19426596; 19432968; 19435811; 19446747; 19467232; 19526316; 19724854; 19747485; 19765320; 19781349; 19786090; 19822898; 19833116; 19837667; 19837979; 19878561; 19885607; 19888474; 19913601; 19915002; 19940138; 20009530; 20016208; 20018936; 20053757; 20087343; 20121949; 20144677; 20190820; 20204305; 20348948; 20363028; 20372793; 20398657; 20403028; 20414733; 20448047; 20489156; 20506119; 20507991; 20578042; 20585888; 20621662; 20690147; 20811575; 20862322; 20864524; 20936779; 20945384; 21118966; 21160498; 21189327; 21212994; 21224049; 21297666; 21321112; 21325822; 21336263; 21354100; 21354147; 21365018; 21368226; 21419860; 21436631; 21479245; 21489990; 21506108; 21551235; 21596316; 21617851; 21688838; 21725089; 21743491; 21743958; 21791614; 21931594; 21968973; 21995436; 21998680; 22053691; 22095683; 22115966; 22127986; 22140445; 22198386; 22260630; 22316125; 22344601; 22354777; 22428032; 22431919; 22433566; 22455954; 22508482; 22531302; 22634339; 22659570; 22713211; 22721276; 22832523; 22878149; 22912725; 22918686; 23029358; 23103837; 23121767; 23127556; 23142458; 23152075; 23178451; 23363221; 23409769; 23416169; 23433111; 23468057; 23478574; 23592216; 23632636; 23696025; 23715767; 23718776; 23755764; 23857582; 23874821; 24076422; 24098051; 24106272 early growth response 1 Ensembl:ENSG00000120738 HGNC:3238 HPRD:00549 MIM:128990 Vega:OTTHUMG00000129197 Other designations: EGR-1|early growth response protein 1|nerve growth factor-induced protein A|transcription factor ETR103|transcription factor Zif268|zinc finger protein 225|zinc finger protein Krox-24 EGR1 OGG:3000001962 Bin Zhao, Yue Liu, Oliver He ECHD FRTS3 L-PBE LBFP LBP PBFE WEB: http://www.ncbi.nlm.nih.gov/gene EHHADH enoyl-CoA, hydratase/3-hydroxyacyl CoA dehydrogenase 1962 3q26.3-q28 9606 3 Official from a nomenclature committee GO_0003857 (EC: NAS, PMID: 8188243); GO_0004165 (EC: IEA); GO_0004300 (EC: NAS, PMID: 8188243); GO_0005102 (EC: IPI); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005739 (EC: IEA); GO_0005777 (EC: IDA, PMID: 1651711); GO_0005777 (EC: NAS, PMID: 8188243); GO_0005829 (EC: IEA); GO_0006475 (EC: IDA); GO_0006635 (EC: IEA); GO_0006635 (EC: NAS, PMID: 8188243); GO_0019899 (EC: IPI, PMID: 16781659); GO_0043231 (EC: IDA); GO_0050662 (EC: IEA) PMID: 1651711; 2895531; 8125298; 8188243; 9053548; 10856712; 12477932; 16781659; 18029348; 18660489; 19240061; 19734545; 20178365; 20877624; 21042317; 22002062; 24401050 enoyl-CoA, hydratase/3-hydroxyacyl CoA dehydrogenase Ensembl:ENSG00000113790 HGNC:3247 HPRD:06125 MIM:607037 Vega:OTTHUMG00000156698 Other designations: 3,2-trans-enoyl-CoA isomerase|L-3-hydroxyacyl-CoA dehydrogenase|L-bifunctional protein, peroxisomal|PBE|enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase|peroxisomal bifunctional enzyme|peroxisomal enoyl-CoA hydratase EHHADH OGG:3000001964 Bin Zhao, Yue Liu, Oliver He EIF1A EIF1AP1 EIF4C eIF-1A eIF-4C WEB: http://www.ncbi.nlm.nih.gov/gene EIF1AX eukaryotic translation initiation factor 1A, X-linked 1964 RP11-393H10.1 Xp22.12 9606 X GO_0003743 (EC: IEA); GO_0005829 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0008135 (EC: TAS, PMID:8106356); GO_0010467 (EC: TAS); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:8106356; 9381176; 10678173; 10982835; 11447110; 11699879; 12426392; 12477932; 12514125; 12569173; 12588972; 14660691; 15489334; 15772651; 16710414; 17784828; 18029348; 19322201; 20060839; 20098747; 20434207; 21832049; 21890473; 21906983; 22505724; 22863883; 22939629; 23000965; 23293029; 23793026; 24250222 eukaryotic translation initiation factor 1A, X-linked Ensembl:ENSG00000173674 HGNC:3250 HPRD:02174 MIM:300186 Vega:OTTHUMG00000022704 Other designations: Putative eukaryotic translation initiation factor 1A|eIF-1A X isoform|eukaryotic translation initiation factor 1A, X chromosome|eukaryotic translation initiation factor 1A, X-chromosomal|eukaryotic translation initiation factor 4C EIF1AX OGG:3000001965 Bin Zhao, Yue Liu, Oliver He EIF-2 EIF-2A EIF-2alpha EIF2 EIF2A WEB: http://www.ncbi.nlm.nih.gov/gene EIF2S1 eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa 1965 14q23.3 9606 14 GO_0003743 (EC: IDA, PMID:16289705); GO_0005515 (EC: IPI, PMID:11500362); GO_0005634 (EC: IEA); GO_0005829 (EC: TAS); GO_0005844 (EC: TAS, PMID:2948954); GO_0005850 (EC: IEA); GO_0005851 (EC: IDA, Qualifier: colocalizes_with, PMID:11323413); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0006987 (EC: TAS); GO_0010467 (EC: TAS); GO_0010494 (EC: ISS); GO_0030968 (EC: TAS); GO_0043022 (EC: IDA, PMID:17894550); GO_0043558 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0046777 (EC: IEA); GO_0070062 (EC: IDA) PMID:1104615; 1400363; 1677563; 1748310; 1883206; 2116318; 2948954; 7821789; 8098621; 8099443; 8099444; 8645159; 8887689; 9079663; 9442054; 9446619; 9819435; 10432301; 10504407; 10542257; 10620360; 10648795; 10734073; 11323413; 11331597; 11500362; 11555640; 11739746; 11859078; 11985496; 12186496; 12370288; 12447867; 12477932; 12499843; 12514125; 12556489; 12588972; 12601012; 12686399; 12687390; 14747531; 15060162; 15207627; 15330758; 15341733; 15476887; 15489334; 15635413; 15650164; 16210351; 16216881; 16288713; 16289705; 16289913; 16418533; 16500424; 16720581; 16982605; 17113348; 17210633; 17274640; 17290288; 17353931; 17361185; 17393484; 17488873; 17894550; 18082745; 18234281; 18423202; 18457437; 18604219; 18639529; 18664456; 18781797; 19009018; 19017641; 19188486; 19189853; 19244104; 19322201; 19364808; 19369421; 19470760; 19559055; 19733181; 19738201; 19754954; 19800319; 19846675; 20154146; 20361218; 20428777; 20457808; 20467438; 20521618; 20660158; 21139048; 21145461; 21385877; 21556050; 21575865; 21699776; 21715487; 21787283; 21853274; 21890473; 21906983; 21907836; 21963094; 21987572; 22053000; 22053931; 22102852; 22113938; 22145905; 22306812; 22623428; 22652449; 22678362; 22705549; 22833567; 22863883; 22939629; 23000965; 23293029; 23402259; 23405127; 23455922; 23741361; 24250222; 24457600 eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa Ensembl:ENSG00000134001 HGNC:3265 HPRD:04881 MIM:603907 Vega:OTTHUMG00000029800 Other designations: eIF-2-alpha|eukaryotic translation initiation factor 2 subunit 1|eukaryotic translation initiation factor 2 subunit alpha EIF2S1 OGG:3000001967 Bin Zhao, Yue Liu, Oliver He EIF2B EIF2BA WEB: http://www.ncbi.nlm.nih.gov/gene EIF2B1 eukaryotic translation initiation factor 2B, subunit 1 alpha, 26kDa 1967 12q24.31 9606 12 GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:16289705); GO_0005085 (EC: IDA, Qualifier: contributes_to, PMID:11323413); GO_0005515 (EC: IPI, PMID:9235896); GO_0005525 (EC: IEA); GO_0005737 (EC: IDA, PMID:11323413); GO_0005829 (EC: TAS); GO_0005851 (EC: IDA, PMID:11323413); GO_0005886 (EC: IDA, PMID:9235896); GO_0006412 (EC: TAS); GO_0006413 (EC: IDA, PMID:16289705); GO_0006413 (EC: TAS); GO_0006446 (EC: IBA); GO_0009408 (EC: ISS); GO_0009408 (EC: TAS, PMID:12499492); GO_0009749 (EC: ISS); GO_0010467 (EC: TAS); GO_0014003 (EC: IMP, PMID:15217090); GO_0016020 (EC: IDA, PMID:9235896); GO_0019003 (EC: IEA); GO_0019509 (EC: IBA, Qualifier: NOT); GO_0030234 (EC: IEA); GO_0032057 (EC: IEA); GO_0043087 (EC: IDA, PMID:11323413); GO_0043434 (EC: ISS); GO_0044267 (EC: TAS); GO_0046523 (EC: IBA, Qualifier: NOT); GO_0051716 (EC: IDA, PMID:8626696) PMID:1883206; 7495858; 8626696; 8887689; 9235896; 9446619; 10805739; 10858531; 11323413; 11835386; 12477932; 12499492; 12707859; 14566705; 14993275; 15060152; 15217090; 15489334; 15752756; 15776425; 16169070; 16289705; 16344560; 17353931; 18263758; 18330844; 18632786; 19631657; 19913121; 20301435; 20368287; 20434207; 20628086; 21139048; 21795329; 21890473; 21906983 eukaryotic translation initiation factor 2B, subunit 1 alpha, 26kDa HGNC:3257 HPRD:09458 MIM:606686 Other designations: eIF-2B GDP-GTP exchange factor subunit alpha|translation initiation factor eIF-2B subunit alpha EIF2B1 OGG:3000001968 Bin Zhao, Yue Liu, Oliver He EIF2 EIF2G EIF2gamma eIF-2gA WEB: http://www.ncbi.nlm.nih.gov/gene EIF2S3 eukaryotic translation initiation factor 2, subunit 3 gamma, 52kDa 1968 Xp22.2-p22.1 9606 X GO_0003743 (EC: IDA, PMID:10900014); GO_0003924 (EC: IEA); GO_0005515 (EC: IPI, PMID:16288713); GO_0005525 (EC: IEA); GO_0005829 (EC: TAS); GO_0006184 (EC: TAS, PMID:8106381); GO_0006412 (EC: TAS); GO_0006413 (EC: IDA, PMID:10900014); GO_0006413 (EC: TAS); GO_0008135 (EC: IDA, PMID:10900014); GO_0010467 (EC: TAS); GO_0044267 (EC: TAS); GO_0070062 (EC: IDA) PMID:1104615; 8098621; 8106381; 8125298; 9079663; 9736774; 10620360; 10648795; 10900014; 12477932; 12588972; 12665801; 15489334; 15635413; 15669143; 16196087; 16201836; 16288713; 16289705; 16712791; 17220478; 17353931; 18781797; 19322201; 19723899; 19738201; 20020773; 20434207; 21110914; 21139048; 21145461; 21252943; 21319273; 21693764; 21853274; 21890473; 21906983; 21907836; 21963094; 21987572; 22145905; 22174317; 22505724; 22797925; 22863883; 22939629; 22952844; 23000965; 23063529; 23455922; 23602568; 24457600 eukaryotic translation initiation factor 2, subunit 3 gamma, 52kDa HGNC:3267 HPRD:02155 MIM:300161 Other designations: eIF-2-gamma X|eIF-2gX|eukaryotic translation initiation factor 2 subunit 3|eukaryotic translation initiation factor 2 subunit gamma X|eukaryotic translation initiation factor 2G EIF2S3 OGG:3000001973 Bin Zhao, Yue Liu, Oliver He DDX2A EIF-4A EIF4A eIF-4A-I eIF4A-I WEB: http://www.ncbi.nlm.nih.gov/gene EIF4A1 eukaryotic translation initiation factor 4A1 1973 17p13 9606 17 GO_0000288 (EC: TAS); GO_0000289 (EC: TAS); GO_0000339 (EC: TAS, PMID:3215517); GO_0003725 (EC: IDA); GO_0003729 (EC: TAS, PMID:3215517); GO_0003743 (EC: IEA); GO_0004386 (EC: TAS, PMID:3215517); GO_0005515 (EC: IPI, PMID:16166382); GO_0005524 (EC: IEA); GO_0005829 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0008026 (EC: IEA); GO_0008135 (EC: TAS, PMID:10880459); GO_0010467 (EC: TAS); GO_0016032 (EC: IEA); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016281 (EC: TAS, PMID:9168945); GO_0019221 (EC: TAS); GO_0031100 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0070062 (EC: IDA) PMID:3215517; 8449919; 8493113; 8619474; 9110174; 9168945; 9372926; 9418880; 9548260; 9790779; 10611228; 10644445; 10880459; 11073994; 11408474; 11903057; 12426392; 12477932; 12588972; 15082783; 15282546; 15489334; 16027165; 16159877; 16166382; 16169070; 16196087; 16541103; 16648488; 17053147; 17130132; 17284590; 17314511; 17353931; 17361185; 17643375; 18034160; 18296639; 18700728; 18719248; 18781797; 19135240; 19203580; 19661379; 19738201; 19805454; 20000738; 20080577; 20156963; 20360068; 20639865; 20927385; 20972266; 21081666; 21110914; 21139048; 21145461; 21182205; 21252943; 21319273; 21377182; 21427765; 21454508; 21800051; 21840318; 21853274; 21890473; 21900206; 21906983; 21963094; 21987572; 22053931; 22076380; 22118674; 22145905; 22268729; 22505724; 22586265; 22586326; 22589333; 22623428; 22689062; 22797925; 22939629; 22990118; 23000965; 23077236; 23402259; 23463506; 23747307; 23798571; 24113185; 24130170; 24248602 eukaryotic translation initiation factor 4A1 Ensembl:ENSG00000161960 HGNC:3282 HPRD:04030 MIM:602641 Vega:OTTHUMG00000108149 Other designations: ATP-dependent RNA helicase eIF4A-1|eukaryotic initiation factor 4A-I|eukaryotic initiation factor 4AI|eukaryotic translation initiation factor 4A EIF4A1 OGG:3000001974 Bin Zhao, Yue Liu, Oliver He BM-010 DDX2B EIF4A EIF4F eIF-4A-II eIF4A-II WEB: http://www.ncbi.nlm.nih.gov/gene EIF4A2 eukaryotic translation initiation factor 4A2 1974 3q28 9606 3 GO_0000288 (EC: TAS); GO_0000289 (EC: TAS); GO_0003743 (EC: IEA); GO_0004386 (EC: TAS, PMID:8521730); GO_0005524 (EC: IEA); GO_0005829 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0006446 (EC: TAS, PMID:8521730); GO_0008026 (EC: IEA); GO_0010467 (EC: TAS); GO_0016032 (EC: IEA); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016281 (EC: TAS, PMID:8521730); GO_0019221 (EC: TAS); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:8125298; 8449919; 8521730; 11172724; 11408474; 11922617; 12477932; 12588972; 15047060; 15489334; 15946665; 16014927; 16169070; 16567544; 17353931; 17643375; 18250159; 18593934; 18976975; 19034380; 19596686; 19615732; 20360068; 20639865; 20972266; 21110914; 21139048; 21427765; 21890473; 21900206; 21906983; 21963094; 21987572; 22053931; 22360420; 22505724; 22589333; 22759308; 22939629; 22944692; 22990118; 23000965; 23383273; 23463506; 23559250; 23824909 eukaryotic translation initiation factor 4A2 Ensembl:ENSG00000156976 HGNC:3284 HPRD:03062 MIM:601102 Vega:OTTHUMG00000156564 Other designations: ATP-dependent RNA helicase eIF4A-2|eukaryotic initiation factor 4A-II|eukaryotic translation initiation factor 4A EIF4A2 OGG:3000001975 Bin Zhao, Yue Liu, Oliver He EIF-4B PRO1843 WEB: http://www.ncbi.nlm.nih.gov/gene EIF4B eukaryotic translation initiation factor 4B 1975 12q13.13 9606 12 GO_0000166 (EC: IEA); GO_0000288 (EC: TAS); GO_0000289 (EC: TAS); GO_0003723 (EC: TAS, PMID:2390971); GO_0003743 (EC: IEA); GO_0005515 (EC: IPI); GO_0005829 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0006446 (EC: TAS, PMID:2390971); GO_0008286 (EC: TAS); GO_0010467 (EC: TAS); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016281 (EC: TAS, PMID:2390971); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:2016328; 2390971; 6722878; 8125298; 8139536; 8182051; 8816444; 10585411; 10672017; 11274152; 12477932; 12489981; 12588972; 12885229; 14702039; 14968112; 15071500; 15078951; 15302935; 15314020; 15342556; 16281055; 16286006; 16763566; 17081983; 17361185; 17620599; 18719248; 19167051; 19322201; 19369421; 19542561; 19615732; 20360068; 20462248; 20562859; 21044950; 21139048; 21145461; 21427765; 21743057; 21840318; 21906983; 21987572; 21994950; 22113938; 22268729; 22863883; 22939629; 23000965; 23084401; 23184937; 23398456; 23749639; 23813671; 24244333; 24250222 eukaryotic translation initiation factor 4B Ensembl:ENSG00000063046 HGNC:3285 HPRD:04892 MIM:603928 Vega:OTTHUMG00000169570 EIF4B OGG:3000001977 Bin Zhao, Yue Liu, Oliver He AUTS19 CBP EIF4E1 EIF4EL1 EIF4F WEB: http://www.ncbi.nlm.nih.gov/gene EIF4E eukaryotic translation initiation factor 4E 1977 4q21-q25 9606 4 GO_0000082 (EC: IMP, PMID:14673156); GO_0000288 (EC: TAS); GO_0000289 (EC: TAS); GO_0000339 (EC: TAS, PMID:3469651); GO_0000932 (EC: IDA); GO_0003743 (EC: IDA); GO_0003743 (EC: ISS); GO_0005515 (EC: IPI, PMID:10772338); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005845 (EC: IDA, PMID:16271312); GO_0006406 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0006417 (EC: IDA); GO_0008286 (EC: TAS); GO_0010467 (EC: TAS); GO_0010494 (EC: IDA); GO_0016032 (EC: IEA); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016281 (EC: IDA); GO_0016442 (EC: IDA); GO_0019221 (EC: TAS); GO_0030324 (EC: IEA); GO_0031370 (EC: IEA); GO_0033391 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0045931 (EC: IMP, PMID:14673156); GO_0070062 (EC: IDA) PMID:1384058; 1672854; 1674733; 1736299; 1916814; 1993647; 2016328; 3112145; 3469651; 7590282; 7651417; 7665584; 7782323; 7935836; 8449919; 8505316; 8521827; 8662663; 8816458; 8939971; 9155017; 9330633; 9372926; 9418880; 9593750; 9607624; 9628874; 9873047; 9878069; 10022874; 10364159; 10394359; 10405182; 10600798; 10648556; 10698949; 10753870; 10772338; 10856257; 10870064; 10880459; 10910074; 11072066; 11154262; 11401917; 11408474; 11500381; 11553333; 11575918; 11605658; 11771728; 11847216; 11879179; 11959093; 12071973; 12089333; 12105188; 12138083; 12151318; 12167712; 12169454; 12186496; 12189553; 12239292; 12374671; 12477932; 12482586; 12554669; 12588972; 12588975; 12691746; 12775419; 12781867; 12897141; 12918105; 12975586; 14558943; 14645512; 14673156; 14732354; 14990584; 15094042; 15122903; 15153109; 15220445; 15247416; 15355912; 15361857; 15371741; 15375804; 15487973; 15489334; 15542544; 15767663; 15809305; 15840819; 15878868; 15897904; 15956551; 15961545; 16023599; 16112647; 16124648; 16242075; 16271312; 16281055; 16332685; 16341674; 16540463; 16541103; 16648488; 16699599; 16720573; 16739988; 16756390; 16798736; 16824195; 17010208; 17074885; 17203162; 17245113; 17254965; 17316564; 17353931; 17357517; 17524464; 17601486; 17631896; 17638893; 17667941; 17689990; 17724079; 17786246; 17855553; 18234281; 18250159; 18343217; 18479935; 18593934; 18614538; 18719964; 18789325; 18805096; 18957614; 19020722; 19060904; 19114552; 19122207; 19134194; 19188486; 19244480; 19261348; 19262567; 19289374; 19367274; 19383915; 19440045; 19483468; 19556253; 19560264; 19603014; 19615732; 19776122; 19850923; 19850929; 20053821; 20101233; 20224576; 20359850; 20360068; 20379614; 20421305; 20427534; 20434207; 20499137; 20537983; 20652449; 20655307; 20686366; 21047768; 21088106; 21139048; 21145089; 21159249; 21238947; 21320304; 21334199; 21389327; 21415224; 21661078; 21750861; 21832049; 21876152; 21883093; 21890473; 21913890; 21941146; 21963094; 21964297; 21987572; 21988832; 21995271; 22216185; 22397984; 22456335; 22457629; 22505724; 22509910; 22556409; 22586265; 22614784; 22623428; 22684010; 22748716; 22759308; 22797067; 22851180; 22863883; 22872150; 22902403; 22939629; 23000965; 23100465; 23277284; 23359369; 23410891; 23467026; 23471078; 23472659; 23547259; 23588929; 23665580; 23665581; 23667251; 23737503; 23831578; 23883783; 23901100; 24211447; 24250222 eukaryotic translation initiation factor 4E HGNC:3287 HPRD:00591 MIM:133440 Other designations: eIF-4E|eIF-4F 25 kDa subunit|eukaryotic translation initiation factor 4E-like 1|mRNA cap-binding protein EIF4E OGG:3000001978 Bin Zhao, Yue Liu, Oliver He 4E-BP1 4EBP1 BP-1 PHAS-I WEB: http://www.ncbi.nlm.nih.gov/gene EIF4EBP1 eukaryotic translation initiation factor 4E binding protein 1 1978 8p12 9606 8 GO_0000082 (EC: IMP, PMID:14673156); GO_0002931 (EC: IEA); GO_0005515 (EC: IPI, PMID:10772338); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0008190 (EC: IEA); GO_0008286 (EC: TAS); GO_0010467 (EC: TAS); GO_0030324 (EC: IEA); GO_0030371 (EC: IDA); GO_0031333 (EC: IEA); GO_0031929 (EC: IDA, PMID:12150926); GO_0043234 (EC: IEA); GO_0044267 (EC: TAS); GO_0045471 (EC: IEA); GO_0045931 (EC: IMP, PMID:14673156); GO_0045947 (EC: IDA) PMID:7651417; 7935836; 8083223; 8521827; 8816458; 8957083; 8975712; 9092573; 9344920; 9405468; 9465032; 9628874; 9806882; 10022874; 10092805; 10198256; 10364159; 10405182; 10608806; 10698949; 10713094; 10753870; 10772338; 10779345; 10942774; 10971657; 11069026; 11114166; 11146653; 11280764; 11438723; 11553333; 11605658; 11691836; 11777913; 11847216; 11865047; 11909977; 12071973; 12080086; 12105188; 12150925; 12150926; 12151318; 12271141; 12477932; 12588975; 12604610; 12618431; 12665511; 12665801; 12747827; 12759354; 12820960; 12912989; 14507920; 14673156; 15066126; 15094042; 15153109; 15178440; 15459249; 15467718; 15489334; 15542544; 15767663; 15809305; 15854902; 15927069; 16098202; 16098514; 16109716; 16169070; 16189514; 16242075; 16271312; 16648488; 16652388; 16715128; 16798736; 16824195; 16837165; 16873412; 16899564; 16983702; 17081983; 17114181; 17200342; 17254965; 17316564; 17353931; 17386266; 17502379; 17601486; 17604271; 17653084; 17693255; 17699757; 17724476; 18029348; 18051367; 18280804; 18337562; 18337751; 18384376; 18439897; 18442140; 18660489; 18668138; 18701920; 18708753; 18722121; 18810319; 18922789; 18957614; 19036825; 19107520; 19211763; 19244480; 19271249; 19336517; 19360336; 19367274; 19428047; 19429661; 19533653; 19541645; 19574449; 19603014; 19648884; 19834456; 19850923; 20090955; 20133758; 20304964; 20372058; 20532202; 20609351; 20621385; 20671708; 21046149; 21067588; 21071439; 21366462; 21460630; 21576371; 21661078; 21750861; 21784851; 21841310; 21900206; 21913890; 21914810; 21922152; 21964297; 22110663; 22142830; 22178476; 22184107; 22216185; 22248270; 22457629; 22493283; 22578813; 22586265; 22641346; 22652449; 22690797; 22918237; 22977662; 23082216; 23100465; 23175522; 23340172; 23451476; 23547259; 23640516; 23707523; 23814053; 24030155; 24211447; 24255178 eukaryotic translation initiation factor 4E binding protein 1 Ensembl:ENSG00000187840 HGNC:3288 HPRD:03746 MIM:602223 Vega:OTTHUMG00000164012 Other designations: eIF4E-binding protein 1|eukaryotic translation initiation factor 4E-binding protein 1|phosphorylated heat- and acid-stable protein regulated by insulin 1 EIF4EBP1 OGG:3000001979 Bin Zhao, Yue Liu, Oliver He 4EBP2 PHASII WEB: http://www.ncbi.nlm.nih.gov/gene EIF4EBP2 eukaryotic translation initiation factor 4E binding protein 2 1979 10q21-q22 9606 10 GO_0005515 (EC: IPI, PMID:16271312); GO_0006412 (EC: TAS, PMID:7935836); GO_0008190 (EC: IEA); GO_0008286 (EC: IEA); GO_0019933 (EC: IEA); GO_0045947 (EC: IEA) PMID:7651417; 7935836; 8939971; 8975712; 9344920; 9381973; 9465032; 9531283; 10092805; 11069026; 11847216; 11865047; 12151318; 12477932; 14507920; 14702039; 15153109; 15489334; 16271312; 16385451; 16751776; 16798736; 17316564; 18789325; 19244480; 19322201; 19913121; 20424163; 20628086; 20628624; 21661078; 23824909 eukaryotic translation initiation factor 4E binding protein 2 Ensembl:ENSG00000148730 HGNC:3289 HPRD:03747 MIM:602224 Vega:OTTHUMG00000018409 Other designations: 4E-BP2|eIF4E-binding protein 2|eukaryotic translation initiation factor 4E-binding protein 2|phosphorylated, heat and acid stable regulated by insulin protein II EIF4EBP2 OGG:3000001981 Bin Zhao, Yue Liu, Oliver He EIF-4G1 EIF4F EIF4G EIF4GI P220 PARK18 WEB: http://www.ncbi.nlm.nih.gov/gene EIF4G1 eukaryotic translation initiation factor 4 gamma, 1 1981 3q27.1 9606 3 GO_0000184 (EC: TAS); GO_0000288 (EC: TAS); GO_0000289 (EC: TAS); GO_0003743 (EC: TAS, PMID:8961935); GO_0005515 (EC: IPI, PMID:10523622); GO_0005829 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0006446 (EC: IMP, PMID:19648179); GO_0006446 (EC: NAS, PMID:8961935); GO_0008135 (EC: TAS, PMID:10880459); GO_0008219 (EC: IEA); GO_0008286 (EC: TAS); GO_0010467 (EC: TAS); GO_0016032 (EC: IEA); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016281 (EC: TAS, PMID:9857202); GO_0019221 (EC: TAS); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:1429670; 7601469; 7651417; 7935836; 8396129; 8449919; 8521827; 8889548; 8961935; 9002667; 9139875; 9372926; 9418880; 9755181; 9857202; 9878069; 10205060; 10523622; 10600798; 10753870; 10859165; 10872469; 10880459; 10970864; 10996799; 11154262; 11331597; 11340157; 11408474; 11606767; 11821405; 11866104; 12052860; 12054647; 12054764; 12071973; 12086624; 12149653; 12239292; 12477932; 12505164; 12581158; 12682023; 12897141; 14592777; 14610163; 14701818; 14702039; 15047801; 15128869; 15153109; 15193258; 15220445; 15231748; 15234964; 15302935; 15314020; 15314025; 15361857; 15452223; 15592455; 15713657; 15743837; 15755734; 15885108; 15897904; 15961545; 16009940; 16010989; 16156639; 16169070; 16236269; 16281055; 16344560; 16412378; 16513844; 16541103; 16556936; 16648488; 16698552; 16720573; 16766523; 16964243; 16982693; 17053147; 17081983; 17130132; 17195095; 17266347; 17290396; 17353931; 17361185; 17601486; 18250159; 18296639; 18426977; 18508616; 18573886; 18593934; 18614538; 18631141; 18799579; 19114555; 19203580; 19525934; 19596686; 19615732; 19648179; 19716330; 19738201; 19769989; 19850929; 19956697; 20020773; 20028737; 20053821; 20360068; 20398343; 21139048; 21145461; 21182205; 21252943; 21377182; 21454508; 21576361; 21840318; 21890473; 21900206; 21906983; 21907011; 21964297; 21988832; 22108332; 22145905; 22178476; 22280895; 22431630; 22505724; 22509910; 22561553; 22586265; 22586326; 22623428; 22658323; 22707335; 22759308; 22772876; 22863883; 22909319; 22939629; 23000965; 23041282; 23092605; 23112151; 23124435; 23261770; 23263986; 23408866; 23409027; 23455922; 23490116; 23562511; 23617574; 23726718; 23805307; 23862649; 23901100; 24092755; 24248602; 24250222 eukaryotic translation initiation factor 4 gamma, 1 Ensembl:ENSG00000114867 HGNC:3296 HPRD:06774 MIM:600495 Vega:OTTHUMG00000156784 Other designations: EIF4-gamma|eIF-4-gamma 1|eucaryotic translation initiation factor 4G|eukaryotic translation initiation factor 4 gamma 1 EIF4G1 OGG:3000001982 Bin Zhao, Yue Liu, Oliver He AAG1 DAP5 NAT1 P97 WEB: http://www.ncbi.nlm.nih.gov/gene EIF4G2 eukaryotic translation initiation factor 4 gamma, 2 1982 OK/SW-cl.75 11p15 9606 11 GO_0003743 (EC: IDA, PMID:11943866); GO_0005515 (EC: IPI, PMID:16166382); GO_0005829 (EC: TAS); GO_0006446 (EC: IDA, PMID:11943866); GO_0007050 (EC: TAS, PMID:9032289); GO_0008135 (EC: IDA, PMID:16289705); GO_0008219 (EC: TAS, PMID:9032289); GO_0016281 (EC: IDA, PMID:11943866); GO_0019221 (EC: TAS); GO_0044822 (EC: IDA) PMID:8125298; 9027506; 9032289; 9049310; 9372926; 9418880; 9878069; 10394359; 10611228; 11172724; 11175261; 11331597; 11511540; 11943866; 12477932; 12505164; 12665801; 12703993; 14507913; 14702039; 15016848; 15231748; 15302935; 15361857; 15489334; 15718103; 16166382; 16289705; 16344560; 16410684; 16751776; 16932749; 17195095; 17237356; 17353931; 18450493; 18491231; 18722383; 19615732; 19738201; 19769989; 20057060; 20467438; 20544972; 21139048; 21145461; 21890473; 21906983; 21963094; 21988832; 22505724; 22555068; 22623428; 22909319; 22939629; 23000965; 23318444 eukaryotic translation initiation factor 4 gamma, 2 Ensembl:ENSG00000110321 HGNC:3297 HPRD:09084 MIM:602325 Vega:OTTHUMG00000165823 Other designations: DAP-5|aging-associated protein 1|death-associated protein 5|eIF-4-gamma 2|eIF-4G 2|eIF4G 2|eukaryotic translation initiation factor 4 gamma 2|eukaryotic translation initiation factor 4G-like 1 EIF4G2 OGG:3000001983 Bin Zhao, Yue Liu, Oliver He EIF-5 EIF-5A WEB: http://www.ncbi.nlm.nih.gov/gene EIF5 eukaryotic translation initiation factor 5 1983 14q32.32 9606 14 GO_0003743 (EC: NAS, PMID:8663286); GO_0003924 (EC: TAS, PMID:8663286); GO_0005525 (EC: IEA); GO_0005737 (EC: IDA); GO_0005829 (EC: NAS, PMID:8663286); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA); GO_0006184 (EC: TAS, PMID:8663286); GO_0006412 (EC: TAS); GO_0006413 (EC: NAS, PMID:8663286); GO_0006413 (EC: TAS); GO_0006446 (EC: TAS, PMID:8663286); GO_0008135 (EC: TAS, PMID:8663286); GO_0010467 (EC: TAS); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:8663286; 9395514; 9973622; 10805737; 10982835; 11092890; 11230166; 11331597; 11861906; 12477932; 12569173; 14702039; 15489334; 16227438; 16584190; 16781736; 17081983; 17207965; 18029348; 19738201; 19953087; 20562859; 21139048; 21832049; 21890473; 21906983; 21963094; 21988832; 22062548; 22412018; 22813744; 22863883; 22939629; 23222517; 23293029; 24319994 eukaryotic translation initiation factor 5 Ensembl:ENSG00000100664 HGNC:3299 HPRD:03417 MIM:601710 Vega:OTTHUMG00000171839 EIF5 OGG:3000001984 Bin Zhao, Yue Liu, Oliver He EIF-5A EIF5A1 eIF5AI WEB: http://www.ncbi.nlm.nih.gov/gene EIF5A eukaryotic translation initiation factor 5A 1984 17p13-p12 9606 17 GO_0003723 (EC: IDA, PMID:15303967); GO_0003746 (EC: ISS); GO_0005515 (EC: IPI, PMID:10381392); GO_0005634 (EC: IDA, PMID:12210765); GO_0005642 (EC: IDA, PMID:12210765); GO_0005643 (EC: IDA, PMID:10381392); GO_0005737 (EC: IDA, PMID:12210765); GO_0005789 (EC: IEA); GO_0005829 (EC: TAS); GO_0006406 (EC: IMP, PMID:9465063); GO_0006452 (EC: IEA); GO_0006611 (EC: IMP, PMID:8596953); GO_0006913 (EC: IDA, Qualifier: NOT, PMID:12210765); GO_0006913 (EC: IMP, PMID:10381392); GO_0006915 (EC: IDA, PMID:15371445); GO_0008284 (EC: IGI, PMID:14622290); GO_0008612 (EC: TAS); GO_0017070 (EC: IDA, PMID:9285100); GO_0043022 (EC: IEA); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0045901 (EC: ISS); GO_0045905 (EC: IEA); GO_0047485 (EC: IPI, PMID:15371445) PMID:1286667; 1850732; 1900436; 2492279; 3095320; 7545941; 7578077; 7622067; 7759117; 7929297; 7971969; 8125298; 8253832; 8596953; 9285095; 9285100; 9442029; 9465063; 10229683; 10381392; 10944119; 11161802; 11238447; 11742107; 11790298; 11870779; 12210765; 12477932; 12562768; 12687616; 12788913; 12894223; 14622290; 15231747; 15303967; 15371445; 15489334; 16354571; 16371467; 16452303; 16515720; 16519677; 16522190; 16712791; 16842744; 16916647; 16987817; 17008552; 17187778; 17213197; 17578650; 18067580; 18781797; 19149558; 19160416; 19322201; 19379712; 19471022; 19825182; 19998337; 20232312; 20360068; 20639865; 20830705; 20942800; 21139048; 21145461; 21224998; 21360055; 21565611; 21693764; 21778671; 21890473; 21906983; 21942715; 21963094; 22053931; 22304920; 22354994; 22505724; 22771473; 22863883; 22908221; 22927971; 22939629; 22944692; 23000965; 23132580; 23322277; 23383273; 23402259; 23539416; 23733422; 23862649; 24220243; 24250222; 24509416 eukaryotic translation initiation factor 5A Ensembl:ENSG00000132507 HGNC:3300 HPRD:02555 MIM:600187 Vega:OTTHUMG00000102197 Other designations: eIF-4D|eIF-5A-1|eIF-5A1|eukaryotic initiation factor 5A|eukaryotic translation initiation factor 5A-1|rev-binding factor EIF5A OGG:3000001996 Bin Zhao, Yue Liu, Oliver He HUD PNEM WEB: http://www.ncbi.nlm.nih.gov/gene ELAVL4 ELAV like neuron-specific RNA binding protein 4 1996 1p34 9606 1 Official from a nomenclature committee GO_0000166 (EC: IEA); GO_0003723 (EC: TAS, PMID: 1655278); GO_0003730 (EC: TAS, PMID: 10848602); GO_0006396 (EC: TAS, PMID: 1655278); GO_0006397 (EC: TAS, PMID: 10348344); GO_0017091 (EC: IDA, PMID: 10710437) PMID: 1415481; 1655278; 2166930; 8069866; 8222755; 9065557; 10348344; 10710437; 10848602; 11175903; 11803489; 12034726; 12209604; 12235292; 12384599; 12388589; 12468554; 12477932; 14512168; 15358174; 15735910; 15827745; 16189514; 16278682; 16508003; 16710414; 17230446; 17234598; 17577668; 18218628; 18493953; 18587682; 18607064; 19252764; 19410329; 21110914; 21282516; 21491091; 21890473; 21988832; 22387028; 22965691; 23251661; 23618873 ELAV like neuron-specific RNA binding protein 4 Ensembl:ENSG00000162374 HGNC:3315 HPRD:01343 MIM:168360 Vega:OTTHUMG00000007877 Other designations: ELAV (embryonic lethal, abnormal vision, Drosophila)-like 4 (Hu antigen D)|ELAV-like protein 4|Embryonic lethal, abnormal vision, Drosophila, homolog of, like-4|Hu antigen D|hu-antigen D|paraneoplastic encephalomyelitis antigen HuD ELAVL4 OGG:3000002081 Bin Zhao, Yue Liu, Oliver He IRE1 IRE1P IRE1a hIRE1p WEB: http://www.ncbi.nlm.nih.gov/gene ERN1 endoplasmic reticulum to nucleus signaling 1 2081 17q24.2 9606 17 Official from a nomenclature committee GO_0000287 (EC: IDA, PMID: 9637683); GO_0004521 (EC: IDA, PMID: 11779465); GO_0004521 (EC: TAS); GO_0004674 (EC: IDA, PMID: 9637683); GO_0004674 (EC: TAS); GO_0005515 (EC: IPI, PMID: 11278723); GO_0005524 (EC: IDA, PMID: 9637683); GO_0005637 (EC: IEA); GO_0005739 (EC: IEA); GO_0005789 (EC: TAS); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0006468 (EC: IDA, PMID: 9637683); GO_0006987 (EC: IDA, PMID: 9637683); GO_0006987 (EC: TAS); GO_0007050 (EC: ISS); GO_0019899 (EC: IPI); GO_0030176 (EC: IDA, PMID: 9637683); GO_0030968 (EC: TAS); GO_0042802 (EC: IPI, PMID: 12637535); GO_0044267 (EC: TAS); GO_0046777 (EC: IEA); GO_0070055 (EC: IDA, PMID: 11779465); GO_0070059 (EC: IEA); GO_0090502 (EC: IDA, PMID: 11779465); GO_0090502 (EC: TAS); GO_1900103 (EC: IMP, PMID: 16645094) PMID: 9637683; 10587643; 10650002; 10737800; 11175748; 11278723; 11779465; 11850408; 11897784; 12050113; 12446770; 12477932; 12637535; 12843613; 14702039; 15063770; 15234121; 16107700; 16344560; 16645094; 16680093; 17585877; 17638880; 17951406; 17991856; 18065414; 18242182; 18369366; 18840095; 19135427; 19913121; 20007910; 20013084; 20103773; 20379614; 20447464; 20625543; 20628086; 20702765; 20798350; 20819778; 20965234; 21118962; 21385877; 21482118; 21525936; 21680894; 21954231; 22194594; 22199355; 22219383; 22314839; 22315414; 22419015; 22446326; 22718352; 22787145; 22917505; 23001845; 23041190; 23042294; 23103912; 23110043; 23363253; 23575540; 23598528; 23602568; 23684307; 23748775; 23752693; 23942232; 23950715; 24330607 endoplasmic reticulum to nucleus signaling 1 Ensembl:ENSG00000178607 HGNC:3449 HPRD:04943 MIM:604033 Vega:OTTHUMG00000178879 Other designations: ER to nucleus signalling 1|endoplasmic reticulum-to-nucleus signaling 1|inositol-requiring 1|inositol-requiring enzyme 1|inositol-requiring protein 1|ire1-alpha|protein kinase/endoribonuclease|serine/threonine-protein kinase/endoribonuclease IRE1 ERN1 OGG:3000002114 Bin Zhao, Yue Liu, Oliver He ETS2IT1 WEB: http://www.ncbi.nlm.nih.gov/gene ETS2 v-ets avian erythroblastosis virus E26 oncogene homolog 2 2114 21q22.2 9606 21 Official from a nomenclature committee GO_0000977 (EC: IEA); GO_0000981 (EC: IBA); GO_0001501 (EC: TAS, PMID: 8596630); GO_0003677 (EC: TAS, PMID: 10918595); GO_0003700 (EC: IDA, PMID: 11909962); GO_0005515 (EC: IPI, PMID: 11909962); GO_0005634 (EC: IDA, PMID: 16780588); GO_0005654 (EC: TAS); GO_0006357 (EC: IBA); GO_0006366 (EC: IBA); GO_0030154 (EC: IBA); GO_0035259 (EC: IEA); GO_0045893 (EC: IDA, PMID: 11909962); GO_0045944 (EC: IEA) PMID: 2186967; 2250910; 2847145; 2997781; 3021321; 3285299; 8596630; 9334186; 9681824; 10212281; 10358095; 10377039; 10815800; 10830953; 10918595; 10942770; 11027273; 11279115; 11313931; 11689681; 11752456; 11909962; 12095911; 12174931; 12477932; 12511603; 12532432; 12637547; 12646185; 12743594; 12860972; 12894593; 14507917; 14702039; 14722092; 15231748; 15489334; 15572696; 15788656; 15806151; 15900611; 16263717; 16780588; 16953216; 17703088; 17921261; 17975022; 17986575; 18059336; 18094719; 18242510; 18374905; 18586674; 18598946; 18801734; 18848526; 18854154; 18942749; 19318269; 19407855; 19453261; 19939245; 20145133; 20379614; 20398657; 20554528; 20671229; 21079520; 21241890; 21526717; 21562315; 21693764; 21700929; 21763315; 21963094; 21987572; 22048266; 22128184; 22221250; 22298639; 22354960; 22446105; 22505724; 22615925; 22819965; 22826236; 22922762; 23343470; 23416888; 23530240; 23542016; 23589550; 23659968; 24024966 v-ets avian erythroblastosis virus E26 oncogene homolog 2 Ensembl:ENSG00000157557 HGNC:3489 HPRD:01263 MIM:164740 Vega:OTTHUMG00000090769 Other designations: oncogene ETS-2|protein C-ets-2|v-ets avian erythroblastosis virus E2 oncogene homolog 2|v-ets erythroblastosis virus E26 oncogene homolog 2 ETS2 gene OGG:3000002152 Bin Zhao, Yue Liu, Oliver He CD142 TF TFA WEB: http://www.ncbi.nlm.nih.gov/gene F3 coagulation factor III (thromboplastin, tissue factor) 2152 1p22-p21 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0001938 (EC: IDA, PMID: 17898544); GO_0002020 (EC: IPI, PMID: 3455766); GO_0002541 (EC: IDA, PMID: 17469850); GO_0002543 (EC: IC, PMID: 17469850); GO_0005515 (EC: IPI, PMID: 15522303); GO_0005543 (EC: IDA, PMID: 17469850); GO_0005615 (EC: IDA, PMID: 19065458); GO_0005886 (EC: TAS); GO_0006919 (EC: IDA, PMID: 17898544); GO_0007596 (EC: TAS); GO_0007598 (EC: TAS); GO_0009986 (EC: IDA, PMID: 17898544); GO_0010641 (EC: IDA, PMID: 17991872); GO_0016021 (EC: IEA); GO_0030335 (EC: TAS, PMID: 18612547); GO_0031012 (EC: IDA, PMID: 2704749); GO_0031233 (EC: IC, PMID: 17469850); GO_0045766 (EC: IDA, PMID: 17898544); GO_0050927 (EC: IC, PMID: 17991872); GO_0051897 (EC: IMP, PMID: 18612547) PMID: 392457; 1740409; 2271516; 2315317; 2704749; 2719077; 2719931; 2823875; 3037536; 3166978; 3297348; 3399965; 3424286; 3455766; 3527261; 4023720; 7598447; 7615158; 8086403; 8598903; 8609606; 8702971; 8889548; 9192667; 9480775; 9490681; 9490735; 9925787; 10856975; 10896200; 11307801; 11583305; 11601848; 11744662; 11776298; 11816707; 11816709; 11858183; 11858185; 11858480; 11876644; 11882315; 11921018; 11929768; 11943929; 11973337; 11994566; 12008961; 12019261; 12028585; 12036889; 12070020; 12083487; 12083501; 12095134; 12149215; 12152652; 12152682; 12172458; 12189027; 12192302; 12270558; 12353085; 12356487; 12408769; 12426405; 12477932; 12514112; 12529356; 12540946; 12544727; 12603864; 12652293; 12654807; 12787023; 12871349; 12883669; 12903530; 12920028; 12941032; 14597990; 14610342; 14675092; 14675093; 14678810; 14738565; 14750502; 14756558; 14961150; 15016732; 15034795; 15034796; 15041276; 15117736; 15154603; 15161741; 15182581; 15213840; 15213854; 15242552; 15252050; 15304041; 15328160; 15467908; 15489334; 15494427; 15522303; 15562024; 15604222; 15630487; 15814630; 15835921; 15842359; 15860742; 15865421; 15869604; 15892865; 15905465; 15935832; 15996056; 16020745; 16113798; 16113838; 16182846; 16215234; 16217771; 16236262; 16239598; 16324758; 16341674; 16344560; 16363246; 16453151; 16473535; 16488980; 16490369; 16493499; 16507316; 16510984; 16516912; 16529959; 16531802; 16634740; 16697385; 16710414; 16794185; 16820938; 16835245; 16839353; 16894464; 16930953; 16937466; 16949034; 16959886; 17008590; 17060476; 17066404; 17137581; 17157899; 17196206; 17200119; 17200762; 17200764; 17234207; 17237436; 17314141; 17323935; 17324918; 17331567; 17334638; 17347408; 17384202; 17401435; 17459125; 17469034; 17469850; 17470200; 17483700; 17536017; 17549302; 17577783; 17586694; 17597988; 17598015; 17663729; 17675290; 17721619; 17724132; 17726162; 17848177; 17852460; 17883594; 17883595; 17898544; 17900273; 17901245; 17920661; 17922809; 17938822; 17939398; 17947506; 17977694; 17982314; 17991872; 18000605; 18005233; 18019946; 18023707; 18029910; 18031796; 18091328; 18180609; 18217146; 18278195; 18278454; 18284603; 18292391; 18297283; 18308368; 18310227; 18315555; 18327399; 18363812; 18449421; 18490736; 18495150; 18508060; 18612547; 18641355; 18642055; 18645927; 18665396; 18665928; 18677291; 18802362; 18835104; 18846330; 18848323; 18983479; 18983492; 18983503; 18983524; 18989544; 19002040; 19012190; 19027114; 19056482; 19065458; 19091315; 19095643; 19099647; 19105796; 19132232; 19149969; 19167313; 19167713; 19168442; 19203804; 19219655; 19234141; 19249541; 19276228; 19290852; 19322201; 19350119; 19356953; 19359592; 19424642; 19428056; 19483295; 19492160; 19500510; 19515372; 19541671; 19545871; 19558505; 19561489; 19572083; 19578796; 19583819; 19592470; 19597299; 19604541; 19628788; 19631649; 19661141; 19698254; 19750223; 19795460; 19806259; 19817993; 19828697; 19829668; 19843576; 19856410; 19861441; 19880163; 19904262; 19913121; 19914247; 19923558; 19954621; 19958818; 19966052; 19995406; 20034913; 20061396; 20062929; 20103969; 20113254; 20133705; 20138335; 20140262; 20142117; 20149415; 20149924; 20150920; 20153879; 20156644; 20163832; 20171716; 20185792; 20189224; 20224254; 20227257; 20237315; 20237496; 20338779; 20388709; 20434002; 20434004; 20434015; 20451919; 20452482; 20524980; 20546120; 20553947; 20589316; 20601186; 20605795; 20616308; 20628086; 20628259; 20656331; 20673868; 20688968; 20708219; 20708733; 20810696; 20830515; 20846886; 20930172; 20933205; 20978007; 21037076; 21042291; 21059650; 21091668; 21129276; 21149441; 21160057; 21182229; 21186047; 21236471; 21245964; 21248061; 21293108; 21310953; 21344386; 21367569; 21404058; 21458031; 21464728; 21467727; 21474669; 21483174; 21488215; 21500176; 21502573; 21518473; 21531894; 21535396; 21543928; 21592524; 21605334; 21617868; 21619686; 21621407; 21625939; 21652710; 21690060; 21693061; 21694469; 21737126; 21762960; 21800004; 21868706; 21906983; 21934552; 21963094; 21987572; 22022598; 22066736; 22076613; 22099707; 22115773; 22119392; 22156911; 22178066; 22187432; 22196362; 22212466; 22214850; 22237453; 22238593; 22340074; 22437887; 22461171; 22547577; 22672593; 22682123; 22682138; 22683021; 22705067; 22771387; 22784289; 22828416; 22964479; 23000965; 23007470; 23029002; 23029190; 23038262; 23065128; 23118232; 23152142; 23223577; 23294934; 23325480; 23373413; 23381943; 23409769; 23434438; 23524311; 23539451; 23578769; 23585459; 23604472; 23621622; 23623171; 23640483; 23666757; 23754313; 23798713; 23801760; 23803674; 24021283 coagulation factor III (thromboplastin, tissue factor) Ensembl:ENSG00000117525 HGNC:3541 HPRD:00603 MIM:134390 Vega:OTTHUMG00000010716 Other designations: tissue factor F3 OGG:3000002166 Bin Zhao, Yue Liu, Oliver He FAAH-1 PSAB WEB: http://www.ncbi.nlm.nih.gov/gene FAAH fatty acid amide hydrolase 2166 1p35-p34 9606 1 Official from a nomenclature committee GO_0005737 (EC: IEA); GO_0005856 (EC: IEA); GO_0009062 (EC: IDA, PMID: 9122178); GO_0012505 (EC: IEA); GO_0016021 (EC: IEA); GO_0016884 (EC: IEA); GO_0017064 (EC: IDA, PMID: 9122178); GO_0031090 (EC: ISS); GO_0047372 (EC: IEA) PMID: 9122178; 9790682; 9822713; 9871570; 9878243; 10036136; 10431820; 10788462; 10806398; 11352748; 11390466; 11818522; 12008024; 12060782; 12153574; 12477932; 12556536; 12665801; 12799380; 14657172; 15219977; 15254019; 15489334; 15721218; 15809662; 16710414; 16972078; 17065342; 17216208; 17290447; 17342744; 17449448; 17553686; 17621164; 17712725; 17962356; 17991615; 18029348; 18068305; 18295974; 18493729; 18497731; 18566995; 18705688; 18805581; 18819056; 19002671; 19014633; 19053981; 19086053; 19095868; 19103437; 19165169; 19193342; 19419760; 19659925; 19801960; 19859057; 19874574; 19890266; 19913121; 19958092; 20010552; 20010914; 20015515; 20044928; 20054193; 20056290; 20065978; 20080186; 20098695; 20099163; 20102775; 20189896; 20369362; 20628086; 20631561; 20716455; 20808855; 20870184; 20976246; 21037510; 21118518; 21442624; 21477106; 21519771; 21930339; 22035053; 22068813; 22442717; 22609216; 22701012; 22776995; 22826533; 22827915; 22832737; 23122699; 23211960; 23333123; 23372171; 23556448; 23616186 fatty acid amide hydrolase Ensembl:ENSG00000117480 HGNC:3553 HPRD:04244 MIM:602935 Vega:OTTHUMG00000007811 Other designations: anandamide amidohydrolase 1|fatty-acid amide hydrolase 1|oleamide hydrolase 1 FAAH OGG:3000002168 Bin Zhao, Yue Liu, Oliver He FABPL L-FABP WEB: http://www.ncbi.nlm.nih.gov/gene FABP1 fatty acid binding protein 1, liver 2168 2p11 9606 2 Official from a nomenclature committee GO_0003682 (EC: IEA); GO_0005324 (EC: IEA); GO_0005504 (EC: IEA); GO_0005543 (EC: IEA); GO_0005654 (EC: TAS); GO_0005782 (EC: ISS); GO_0005829 (EC: IEA); GO_0008144 (EC: IEA); GO_0008284 (EC: IEA); GO_0016209 (EC: IDA, PMID: 16175609); GO_0032000 (EC: IEA); GO_0032052 (EC: IEA); GO_0043066 (EC: IDA, PMID: 16175609); GO_0043154 (EC: IDA, PMID: 16175609); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0045179 (EC: IEA); GO_0050892 (EC: IEA); GO_0051345 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0070301 (EC: IDA, PMID: 16175609); GO_0071456 (EC: IDA, PMID: 16175609) PMID: 1699834; 2824476; 3012800; 3838309; 3838313; 7566098; 7784447; 8232272; 9070383; 9250612; 9688651; 10684629; 11226238; 11354243; 11461829; 12121132; 12477932; 12646418; 14563446; 15123239; 15249972; 15308127; 15342556; 15489334; 15547295; 16175609; 16249547; 16772708; 16945373; 17003471; 17428383; 17485234; 17526850; 17605029; 17698986; 17826730; 18094680; 18506375; 18624398; 18660489; 18838948; 18854154; 19019918; 19056867; 19217864; 19330863; 19435794; 19441025; 19499240; 19622156; 19913121; 20185732; 20416077; 20550918; 20575163; 20628086; 20721681; 21153750; 21356355; 21504508; 21757748; 21767383; 21856370; 21996226; 22396741; 22465531; 22515481; 22525507; 22640736; 23144966; 23167703; 23223350; 23291381; 23349979; 23599408; 23893635; 24299557 fatty acid binding protein 1, liver Ensembl:ENSG00000163586 HGNC:3555 HPRD:00612 MIM:134650 Vega:OTTHUMG00000130312 Other designations: fatty acid-binding protein 1|fatty acid-binding protein, liver|liver-type fatty acid-binding protein FABP1 OGG:3000002171 Bin Zhao, Yue Liu, Oliver He E-FABP EFABP KFABP PA-FABP PAFABP WEB: http://www.ncbi.nlm.nih.gov/gene FABP5 fatty acid binding protein 5 (psoriasis-associated) 2171 8q21.13 9606 8 Official from a nomenclature committee GO_0005215 (EC: IEA); GO_0005504 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12839573); GO_0005737 (EC: TAS, PMID: 16130169); GO_0006006 (EC: IEA); GO_0006629 (EC: TAS, PMID: 8092987); GO_0006656 (EC: IEA); GO_0008289 (EC: TAS, PMID: 1512466); GO_0008544 (EC: TAS, PMID: 1512466); GO_0009611 (EC: IEA); GO_0015758 (EC: IEA); GO_0070062 (EC: IDA) PMID: 1286667; 1512466; 8092987; 8125298; 8427590; 8726632; 8947466; 9285630; 9438903; 10191275; 10331666; 10493790; 11113456; 12049637; 12477932; 12665801; 12839573; 15146197; 15335354; 15489334; 15592455; 16130169; 16759896; 16806233; 17353931; 17428383; 18360704; 18729184; 19156129; 19337991; 19339807; 19434059; 19554614; 19861119; 20040021; 20057506; 20424164; 20452069; 20563994; 20833513; 21139048; 21288588; 21356353; 21492859; 21890473; 21906983; 22010213; 22505724; 22761399; 22825302; 23000965; 23039948; 23327868; 23528210; 23535730; 23722546; 24457600 fatty acid binding protein 5 (psoriasis-associated) Ensembl:ENSG00000164687 HGNC:3560 HPRD:05524 MIM:605168 Vega:OTTHUMG00000134313 Other designations: epidermal-type fatty acid-binding protein|fatty acid-binding protein, epidermal|psoriasis-associated fatty acid-binding protein homolog FABP5 OGG:3000002195 Bin Zhao, Yue Liu, Oliver He CDHF7 CDHR8 FAT ME5 hFat1 WEB: http://www.ncbi.nlm.nih.gov/gene FAT1 FAT atypical cadherin 1 2195 4q35 9606 4 Official from a nomenclature committee GO_0005509 (EC: IEA); GO_0005515 (EC: IPI, PMID: 16979624); GO_0005634 (EC: IDA, PMID: 15922730); GO_0005886 (EC: IDA, PMID: 15922730); GO_0005887 (EC: TAS, PMID: 8586420); GO_0005911 (EC: IDA, PMID: 15148305); GO_0007015 (EC: ISS); GO_0007155 (EC: TAS, PMID: 8586420); GO_0007156 (EC: IEA); GO_0007163 (EC: ISS); GO_0007267 (EC: TAS, PMID: 8586420); GO_0009653 (EC: TAS, PMID: 8586420); GO_0016337 (EC: ISS); GO_0016477 (EC: ISS); GO_0030027 (EC: IEA); GO_0030175 (EC: IEA); GO_0048471 (EC: IDA, PMID: 15922730); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 8586420; 8889548; 9182820; 9199196; 10737800; 12477932; 15146197; 15148305; 15342556; 15744052; 15922730; 16402135; 16979624; 17081983; 17325662; 17500054; 17895925; 17938632; 19033385; 19056867; 19126244; 19131340; 19328558; 19893579; 21139048; 21552555; 21617878; 21680732; 21890473; 21906983; 21963094; 22116550; 22194967; 22347407; 22505724; 22959770; 22986533; 23314748; 23354438; 23438482; 23785297 FAT atypical cadherin 1 Ensembl:ENSG00000083857 HGNC:3595 HPRD:02986 MIM:600976 Vega:OTTHUMG00000160320 Other designations: FAT tumor suppressor 1|FAT tumor suppressor homolog 1|cadherin ME5|cadherin family member 7|cadherin-related family member 8|cadherin-related tumor suppressor homolog|protein fat homolog|protocadherin Fat 1 FAT1 OGG:3000002206 Bin Zhao, Yue Liu, Oliver He APY ATOPY FCER1B FCERI IGEL IGER IGHER MS4A1 WEB: http://www.ncbi.nlm.nih.gov/gene MS4A2 membrane-spanning 4-domains, subfamily A, member 2 2206 11q12-q13 9606 11 Official from a nomenclature committee GO_0005768 (EC: IEA); GO_0005886 (EC: TAS); GO_0005887 (EC: NAS, PMID: 1535625); GO_0006954 (EC: IEA); GO_0006955 (EC: IMP, PMID: 7920628); GO_0007202 (EC: IEA); GO_0007205 (EC: IEA); GO_0009897 (EC: IEA); GO_0019863 (EC: IEA); GO_0019901 (EC: IEA); GO_0032998 (EC: IEA); GO_0038095 (EC: TAS); GO_0042169 (EC: IEA); GO_0043306 (EC: IEA); GO_0045087 (EC: TAS); GO_0045121 (EC: IEA); GO_0050663 (EC: IEA); GO_0051219 (EC: IEA); GO_0051279 (EC: IEA) PMID: 1386024; 1533242; 1535625; 2146219; 2448768; 7528770; 7612892; 7920628; 8071371; 8094113; 8188278; 8805698; 8817330; 8842731; 8968765; 8995445; 9169438; 9341761; 9379041; 11134951; 11142503; 11150000; 11245344; 11368631; 11447385; 11702205; 11758232; 12047428; 12082592; 12217393; 12393595; 12422339; 12477932; 12697656; 12753743; 12903039; 12919239; 14687477; 15087090; 15316148; 15453830; 15479187; 15489334; 15528387; 15953854; 16002993; 16344560; 16750991; 16839401; 16839402; 16867043; 17014622; 17088130; 17121586; 17178032; 17430357; 17686114; 17703412; 18269668; 18379861; 18534082; 18579528; 18691306; 18931892; 18949059; 18974840; 19028820; 19131662; 19218813; 19247692; 19258923; 19264973; 19288130; 19356729; 19416867; 19479237; 19514647; 19559392; 19796196; 19824886; 19862939; 19913121; 19948975; 20028371; 20085599; 20358027; 20395963; 20503287; 20536507; 20554927; 20628086; 20703737; 20716621; 21061265; 21832049; 22150093; 22845063; 23643722 membrane-spanning 4-domains, subfamily A, member 2 HGNC:7316 HPRD:00915 MIM:147138 Other designations: Fc fragment of IgE, high affinity I, receptor for; beta polypeptide|High affinity immunoglobulin epsilon receptor beta-subunit (FcERI) (IgE Fc receptor, beta-subunit) (Fc epsilon receptor I beta-chain)|high affinity IgE receptor beta subunit|high affinity immunoglobulin epsilon receptor subunit beta|igE Fc receptor subunit beta|immunoglobulin E receptor, high affinity, beta polypeptide MS4A2 OGG:3000002237 Bin Zhao, Yue Liu, Oliver He FEN-1 MF1 RAD2 WEB: http://www.ncbi.nlm.nih.gov/gene FEN1 flap structure-specific endonuclease 1 2237 11q12 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0000278 (EC: TAS); GO_0000287 (EC: IEA); GO_0000722 (EC: TAS); GO_0000723 (EC: TAS); GO_0000737 (EC: IDA, PMID: 18995831); GO_0000737 (EC: IMP, PMID: 11986308); GO_0000738 (EC: TAS, PMID: 8131753); GO_0003677 (EC: IMP, PMID: 11986308); GO_0003684 (EC: TAS, PMID: 8007985); GO_0003690 (EC: TAS, PMID: 8131753); GO_0004519 (EC: TAS, PMID: 8131753); GO_0004523 (EC: IDA, PMID: 7961795); GO_0004527 (EC: TAS, PMID: 9778254); GO_0005515 (EC: IPI, PMID: 11430825); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA); GO_0005739 (EC: IDA, PMID: 18995831); GO_0006260 (EC: NAS, PMID: 15504738); GO_0006271 (EC: TAS); GO_0006281 (EC: NAS, PMID: 15504738); GO_0006281 (EC: TAS); GO_0006284 (EC: TAS); GO_0006302 (EC: TAS, PMID: 8131753); GO_0007613 (EC: IEA); GO_0008309 (EC: TAS, PMID: 8131753); GO_0008409 (EC: IDA, PMID: 7961795); GO_0009650 (EC: TAS, PMID: 8007985); GO_0017108 (EC: IDA, PMID: 18995831); GO_0017108 (EC: IMP, PMID: 11986308); GO_0030145 (EC: IEA); GO_0032201 (EC: TAS); GO_0043137 (EC: IDA, PMID: 18995831); GO_0048015 (EC: NAS, PMID: 15504738); GO_0090305 (EC: IDA, PMID: 7961795); GO_0090305 (EC: TAS, PMID: 8131753); GO_0090502 (EC: IDA, PMID: 7961795) PMID: 1477073; 7673186; 7774922; 7961795; 8007985; 8131753; 8621570; 8668533; 8876181; 9178907; 9214649; 9305916; 9445487; 9545252; 9705499; 9778254; 10460157; 10545607; 10559261; 10635332; 11260214; 11313979; 11430825; 11598021; 11601988; 11948189; 11986308; 12065902; 12171929; 12200445; 12356323; 12411510; 12427278; 12453426; 12477932; 12494477; 12515398; 12554738; 12683998; 12853968; 12856420; 12917330; 14562054; 14657243; 14688284; 14690413; 15037610; 15131255; 15146197; 15342556; 15489334; 15504738; 15556996; 15561706; 15576034; 15579905; 15592449; 15616578; 15635413; 15758026; 16133872; 16169070; 16216273; 16326861; 16543152; 16554811; 16582103; 16914748; 17115032; 17176113; 17488975; 18029348; 18097100; 18291413; 18394896; 18417526; 18443037; 18499658; 18541666; 18662981; 18669164; 18692475; 18781797; 18786645; 18995831; 19010819; 19068479; 19208620; 19218431; 19329428; 19471022; 19525235; 19595719; 19618370; 19674974; 19738201; 20019387; 20126648; 20226869; 20444887; 20496165; 20522537; 20551483; 20574454; 20643645; 20729856; 20802161; 20819778; 21044950; 21139048; 21252943; 21345332; 21454907; 21496641; 21829377; 21832049; 21890473; 21900206; 21906983; 21963094; 21987572; 22011247; 22072618; 22139419; 22145905; 22244820; 22505724; 22556262; 22586102; 22592530; 22606318; 22749529; 22751659; 22787431; 22863883; 22918592; 22939629; 22990118; 23000965; 23128233; 23184144; 23277564; 23362303; 23378610; 23382697; 23675412; 23975198; 24126913; 24515614 flap structure-specific endonuclease 1 Ensembl:ENSG00000168496 HGNC:3650 HPRD:02670 MIM:600393 Vega:OTTHUMG00000168162 Other designations: DNase IV|flap endonuclease 1|maturation factor 1|maturation factor-1 FEN1 OGG:3000002247 Bin Zhao, Yue Liu, Oliver He BFGF FGF-2 FGFB HBGF-2 WEB: http://www.ncbi.nlm.nih.gov/gene FGF2 fibroblast growth factor 2 (basic) 2247 4q26 9606 4 Official from a nomenclature committee GO_0000186 (EC: IEA); GO_0000187 (EC: TAS, PMID: 9712850); GO_0000189 (EC: IEA); GO_0001658 (EC: IDA, PMID: 12631064); GO_0001759 (EC: IEA); GO_0001938 (EC: IMP, PMID: 18059339); GO_0002042 (EC: IDA, PMID: 18059339); GO_0002042 (EC: IGI, PMID: 19351956); GO_0005104 (EC: IPI, PMID: 10830168); GO_0005125 (EC: IDA, PMID: 18059339); GO_0005515 (EC: IPI, PMID: 10490103); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0005634 (EC: IEA); GO_0005829 (EC: IEA); GO_0006661 (EC: IDA); GO_0006700 (EC: IEA); GO_0006935 (EC: TAS, PMID: 10848592); GO_0007165 (EC: NAS, PMID: 9712850); GO_0007173 (EC: TAS); GO_0007265 (EC: TAS, PMID: 10848592); GO_0007399 (EC: TAS, PMID: 9576942); GO_0008083 (EC: IDA, PMID: 18059339); GO_0008201 (EC: IEA); GO_0008284 (EC: IGI, PMID: 8663044); GO_0008285 (EC: IEA); GO_0008286 (EC: TAS); GO_0008543 (EC: IDA, PMID: 17500071); GO_0008543 (EC: IGI, PMID: 8663044); GO_0008543 (EC: IPI, PMID: 10830168); GO_0008543 (EC: TAS); GO_0009887 (EC: TAS, PMID: 10903182); GO_0010001 (EC: IEA); GO_0010764 (EC: IDA, PMID: 19577615); GO_0010863 (EC: IDA); GO_0017134 (EC: IEA); GO_0021762 (EC: IEA); GO_0021940 (EC: IEA); GO_0030198 (EC: TAS); GO_0030214 (EC: IDA, PMID: 19577615); GO_0030308 (EC: IEA); GO_0030324 (EC: IEA); GO_0030374 (EC: IDA, PMID: 17500071); GO_0032958 (EC: IDA); GO_0038095 (EC: TAS); GO_0042056 (EC: IDA, PMID: 18059339); GO_0042060 (EC: TAS); GO_0042660 (EC: IDA, PMID: 18635606); GO_0043536 (EC: IDA, PMID: 18555217); GO_0043537 (EC: IDA, PMID: 18555217); GO_0043552 (EC: IDA); GO_0045087 (EC: TAS); GO_0045669 (EC: IEA); GO_0045765 (EC: TAS); GO_0045766 (EC: IDA); GO_0045892 (EC: IEA); GO_0045893 (EC: IDA, PMID: 17500071); GO_0045944 (EC: IDA, PMID: 18059339); GO_0046668 (EC: IEA); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0048598 (EC: TAS); GO_0048678 (EC: IEA); GO_0048864 (EC: IEA); GO_0050918 (EC: IDA, PMID: 18059339); GO_0051209 (EC: IDA); GO_0051726 (EC: IEA); GO_0051781 (EC: IEA); GO_0060045 (EC: IDA, PMID: 9553078); GO_0060128 (EC: IEA); GO_0060129 (EC: IEA); GO_0060548 (EC: IDA, PMID: 12631064); GO_0060591 (EC: IDA, PMID: 17167778); GO_0060644 (EC: IEA); GO_0061045 (EC: IDA, PMID: 19577615); GO_0070374 (EC: IDA, PMID: 17167778) PMID: 1417798; 1697263; 1702556; 1707542; 1769963; 1785797; 1849658; 1885605; 2265560; 2320377; 2435284; 2435575; 2538817; 2726761; 3472745; 3579930; 3732516; 3780670; 3964259; 7532176; 7691311; 7735329; 7935812; 7999082; 8344959; 8530375; 8622701; 8663044; 8885834; 9139660; 9266968; 9342064; 9553078; 9558385; 9576942; 9712850; 9826564; 9858574; 9925931; 10358027; 10397733; 10438928; 10490103; 10574949; 10579907; 10652299; 10830168; 10848592; 10903182; 10950949; 11030354; 11053263; 11066092; 11075807; 11141237; 11276432; 11294897; 11390973; 11418238; 11509569; 11598182; 11708770; 11716516; 11742492; 11796824; 11815602; 11847221; 11864711; 11891198; 11891801; 11928807; 11940567; 11960370; 11964307; 11976347; 11985797; 11986954; 11999550; 12000311; 12006402; 12008951; 12020352; 12032827; 12054499; 12057924; 12080186; 12087465; 12145206; 12168799; 12172783; 12209593; 12235165; 12369790; 12393937; 12403780; 12428103; 12477932; 12478660; 12496364; 12509902; 12517814; 12538477; 12545206; 12571252; 12574959; 12590983; 12607599; 12623787; 12631064; 12631070; 12651930; 12659634; 12660731; 12676798; 12682649; 12717444; 12727994; 12746216; 12755687; 12799459; 12815619; 12823444; 12857600; 12857733; 12871330; 12871334; 12872165; 13680247; 14523006; 14630795; 14669345; 14672345; 14680499; 14699503; 14706681; 15033176; 15096041; 15117822; 15120936; 15146197; 15166228; 15199049; 15208265; 15243127; 15247002; 15247275; 15249224; 15293454; 15297314; 15302993; 15316024; 15342556; 15464234; 15481452; 15496150; 15525641; 15573376; 15603823; 15610530; 15631865; 15680705; 15689238; 15695515; 15703886; 15713745; 15725477; 15726914; 15731686; 15737206; 15756443; 15769511; 15769981; 15780951; 15809086; 15817123; 15825079; 15875316; 15875782; 15879597; 15906377; 15924676; 15942693; 15947088; 15985216; 15996482; 16020751; 16077964; 16077988; 16080018; 16095497; 16103882; 16135988; 16160009; 16210019; 16222707; 16227592; 16257968; 16278388; 16304044; 16320338; 16436505; 16463783; 16490198; 16495214; 16521228; 16597610; 16597617; 16631837; 16638370; 16685268; 16709186; 16723715; 16739027; 16769728; 16807244; 16816927; 16820871; 16822883; 16840552; 16867222; 16876430; 16905765; 16949906; 16982797; 16996573; 17133345; 17157157; 17166351; 17167778; 17169545; 17204151; 17217840; 17234579; 17285972; 17298206; 17381064; 17466952; 17478553; 17487982; 17497037; 17500071; 17503459; 17505261; 17522998; 17532297; 17537644; 17537668; 17543283; 17556598; 17562265; 17578349; 17605857; 17637743; 17651425; 17653045; 17676480; 17699594; 17706726; 17724016; 17726742; 17762899; 17825301; 17929017; 17942638; 17949478; 17968311; 17968943; 17981115; 17996481; 17997184; 18006148; 18025790; 18031768; 18036796; 18042549; 18051571; 18052595; 18055262; 18059339; 18088275; 18093228; 18094712; 18164591; 18164704; 18171671; 18179408; 18187129; 18253936; 18258238; 18279437; 18281281; 18298475; 18329368; 18332228; 18347025; 18364383; 18419755; 18420995; 18438927; 18452581; 18476630; 18481005; 18511454; 18519946; 18549879; 18555217; 18570917; 18592007; 18635606; 18639416; 18680389; 18698254; 18705695; 18773427; 18783914; 18802039; 18803285; 18819464; 18829480; 18930044; 18974971; 18979395; 19056764; 19059221; 19061884; 19086919; 19096229; 19096867; 19100714; 19107653; 19147956; 19160106; 19196427; 19197140; 19217457; 19235591; 19245795; 19279131; 19287993; 19301256; 19308772; 19318994; 19319189; 19351956; 19386985; 19423540; 19453261; 19456219; 19477940; 19478386; 19489096; 19495899; 19533745; 19541589; 19556344; 19577615; 19586755; 19587357; 19608737; 19614919; 19617559; 19631775; 19631914; 19651147; 19670348; 19696444; 19710942; 19713533; 19781633; 19802384; 19822079; 19828453; 19885553; 19890880; 19892399; 19913121; 19919531; 19930868; 19933269; 19950605; 19952401; 20001221; 20016498; 20053757; 20056600; 20116383; 20122687; 20127022; 20128380; 20150555; 20197313; 20202860; 20206949; 20224347; 20230531; 20335309; 20339243; 20362567; 20363749; 20371606; 20406964; 20438785; 20452482; 20504760; 20504870; 20514456; 20526813; 20571834; 20628086; 20628269; 20628624; 20634891; 20641033; 20644561; 20645833; 20646480; 20672350; 20673868; 20681019; 20713592; 20817637; 20819778; 20850693; 20857427; 20886037; 20926602; 20945415; 21029699; 21037114; 21041608; 21041986; 21048031; 21139048; 21161264; 21209880; 21224050; 21266348; 21350328; 21381082; 21382096; 21460777; 21471211; 21501244; 21506108; 21506113; 21515689; 21528671; 21539890; 21572099; 21678127; 21695795; 21699503; 21720547; 21733164; 21761458; 21766497; 21771176; 21830216; 21832283; 21835001; 21855631; 21894939; 21919032; 21923031; 21942441; 21996542; 21997191; 21998584; 22009965; 22016523; 22102278; 22125837; 22158871; 22174424; 22193058; 22228819; 22233184; 22237711; 22260074; 22267482; 22335910; 22393273; 22493287; 22506349; 22508498; 22542539; 22546563; 22577248; 22599586; 22680042; 22730382; 22732006; 22804708; 22836867; 22895562; 22927437; 22932066; 22962037; 22967508; 23053181; 23071632; 23086340; 23122986; 23154434; 23236888; 23239497; 23243019; 23264596; 23265436; 23290762; 23322705; 23331079; 23335070; 23352645; 23385422; 23435034; 23448571; 23457216; 23485603; 23620752; 23630597; 23677479; 23861152; 23869761; 23998120; 24014875; 24063890; 24089521; 24216509 fibroblast growth factor 2 (basic) Ensembl:ENSG00000138685 HGNC:3676 HPRD:00622 MIM:134920 Vega:OTTHUMG00000039506 Other designations: basic fibroblast growth factor bFGF|fibroblast growth factor 2|heparin-binding growth factor 2|prostatropin FGF2 OGG:3000002259 Bin Zhao, Yue Liu, Oliver He FGF-14 FHF-4 FHF4 SCA27 WEB: http://www.ncbi.nlm.nih.gov/gene FGF14 fibroblast growth factor 14 2259 RP11-397O8.6 13q34 9606 13 Official from a nomenclature committee GO_0005104 (EC: IDA, Qualifier: NOT, PMID: 12815063); GO_0005576 (EC: IEA); GO_0005634 (EC: IEA); GO_0007165 (EC: TAS, PMID: 8790420); GO_0007254 (EC: IPI, PMID: 12815063); GO_0007267 (EC: TAS, PMID: 8790420); GO_0007268 (EC: IEA); GO_0007399 (EC: IEA); GO_0008083 (EC: IEA); GO_0008201 (EC: IDA, PMID: 12815063); GO_0008219 (EC: IEA); GO_0008344 (EC: IEA); GO_0008543 (EC: IDA, Qualifier: NOT, PMID: 12815063); GO_0010765 (EC: IEA); GO_0050905 (EC: IEA) PMID: 8790420; 12123606; 12364586; 12477932; 12489043; 12815063; 15057823; 15148151; 15199049; 15365159; 15470364; 16166153; 16211615; 17221845; 17236779; 20379614; 22579694; 23166209; 23509962; 23551011; 23640885 fibroblast growth factor 14 HGNC:3671 HPRD:03305 MIM:601515 Other designations: bA397O8.2|fibroblast growth factor homologous factor 4 FGF14 OGG:3000002272 Bin Zhao, Yue Liu, Oliver He AP3Aase FRA3B WEB: http://www.ncbi.nlm.nih.gov/gene FHIT fragile histidine triad 2272 3p14.2 9606 3 Official from a nomenclature committee GO_0000166 (EC: IEA); GO_0003824 (EC: TAS, PMID: 8598045); GO_0005515 (EC: IPI, PMID: 18319262); GO_0005737 (EC: IDA, PMID: 15007172); GO_0005829 (EC: IDA, PMID: 15313915); GO_0006163 (EC: IDA, PMID: 9323207); GO_0006260 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0009117 (EC: TAS, PMID: 8794732); GO_0016787 (EC: IDA, PMID: 8794732); GO_0031625 (EC: IPI, PMID: 15313915); GO_0032435 (EC: IMP, PMID: 15313915); GO_0042802 (EC: IPI, PMID: 16189514); GO_0047710 (EC: IDA, PMID: 8794732); GO_0072332 (EC: IMP, PMID: 15313915) PMID: 3864602; 8598045; 8640789; 8661111; 8794732; 8824874; 9012482; 9261067; 9290949; 9323207; 9366528; 9537583; 9576908; 9583683; 9671749; 9824201; 10706123; 11085938; 11731438; 11768238; 11788890; 11809703; 11891319; 11902576; 11915181; 12007194; 12048684; 12057912; 12067991; 12090476; 12119013; 12169206; 12177781; 12231533; 12353263; 12362975; 12419158; 12452072; 12477932; 12483524; 12529969; 12627509; 12697969; 12698186; 12800227; 12833632; 12839965; 12890991; 12893195; 12926121; 12964015; 12969785; 14566838; 14569398; 14630947; 14660280; 14675322; 14702039; 14719066; 14719099; 14760383; 14991669; 15007172; 15026336; 15044096; 15060557; 15073846; 15080495; 15080505; 15182206; 15219888; 15231689; 15246872; 15313915; 15328196; 15361849; 15384174; 15480422; 15489334; 15489891; 15569992; 15633221; 15674328; 15798093; 15835917; 15902282; 15906520; 15929169; 15935551; 15949315; 15998374; 16115913; 16189514; 16217683; 16231322; 16242161; 16344560; 16359767; 16513840; 16533421; 16570269; 16698048; 16699861; 16733051; 16739375; 16740775; 16763940; 16773697; 16864578; 16963412; 16990010; 17029211; 17037022; 17119051; 17137614; 17142325; 17143956; 17164758; 17328863; 17348444; 17359554; 17373735; 17374991; 17380463; 17382535; 17393360; 17548701; 17562266; 17596760; 17609851; 17671701; 17694439; 17712558; 17846126; 18006149; 18029348; 18038314; 18077326; 18091387; 18097574; 18162546; 18221322; 18247301; 18299890; 18319262; 18338496; 18338497; 18367246; 18378390; 18426086; 18476633; 18494825; 18517280; 18567082; 18595145; 18608185; 18618300; 18690840; 18821565; 18953408; 18985481; 19004824; 19096006; 19130459; 19240061; 19267103; 19286306; 19339270; 19401904; 19414370; 19418484; 19419937; 19434452; 19452299; 19502167; 19620087; 19621594; 19622739; 19728916; 19730990; 19751438; 19760177; 19913121; 19931269; 20060354; 20060399; 20082323; 20083852; 20083853; 20095356; 20125088; 20306291; 20379614; 20399571; 20417865; 20435627; 20458975; 20510001; 20552362; 20606729; 20622329; 20628086; 20689140; 20690795; 20814237; 20864173; 20864512; 21095196; 21182207; 21223598; 21241597; 21258320; 21404710; 21557333; 21617227; 21668571; 21679157; 21685375; 21711110; 21830375; 21870644; 21928112; 21988832; 22315171; 22379998; 22393963; 22419666; 22425911; 22578181; 22613411; 22747683; 22760553; 22766745; 22843886; 22932087; 22952603; 23019410; 23049088; 23102829; 23131390; 23209436; 23404381; 23470693; 23724516; 23736021; 23780737; 23797051; 23897914; 23929738; 23947369 fragile histidine triad Ensembl:ENSG00000189283 HGNC:3701 HPRD:03096 MIM:601153 Vega:OTTHUMG00000158591 Other designations: AP3A hydrolase|bis(5'-adenosyl)-triphosphatase|diadenosine 5',5'''-P1,P3-triphosphate hydrolase|dinucleosidetriphosphatase|tumor suppressor protein FHIT OGG:3000002308 Bin Zhao, Yue Liu, Oliver He FKH1 FKHR FOXO1A WEB: http://www.ncbi.nlm.nih.gov/gene FOXO1 forkhead box O1 2308 13q14.1 9606 13 Official from a nomenclature committee GO_0001078 (EC: IEA); GO_0001568 (EC: IBA); GO_0001659 (EC: ISS); GO_0001678 (EC: ISS); GO_0003682 (EC: ISS); GO_0005515 (EC: IPI, PMID: 11237865); GO_0005634 (EC: IDA, PMID: 11311120); GO_0005654 (EC: TAS); GO_0005737 (EC: IDA, PMID: 11237865); GO_0005739 (EC: ISS); GO_0005829 (EC: ISS); GO_0005829 (EC: TAS); GO_0006473 (EC: ISS); GO_0006915 (EC: IEA); GO_0006974 (EC: ISS); GO_0007173 (EC: TAS); GO_0007389 (EC: IBA); GO_0008286 (EC: ISS); GO_0008301 (EC: IBA); GO_0008543 (EC: TAS); GO_0009267 (EC: ISS); GO_0009790 (EC: IBA); GO_0009888 (EC: IBA); GO_0031018 (EC: TAS); GO_0032873 (EC: IDA, PMID: 19696738); GO_0034599 (EC: ISS); GO_0035947 (EC: IEA); GO_0038095 (EC: TAS); GO_0042127 (EC: IEA); GO_0043066 (EC: IDA, PMID: 10871843); GO_0043565 (EC: IDA, PMID: 12228231); GO_0045087 (EC: TAS); GO_0045444 (EC: ISS); GO_0045599 (EC: ISS); GO_0045722 (EC: IEA); GO_0045892 (EC: ISS); GO_0045893 (EC: IDA, PMID: 10871843); GO_0045944 (EC: IDA, PMID: 10871843); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0051721 (EC: ISS); GO_0070417 (EC: ISS); GO_0071732 (EC: ISS); GO_2000505 (EC: ISS) PMID: 7630639; 7862145; 8275086; 8634710; 8790412; 9479491; 10358014; 10358075; 10783894; 10871843; 10973497; 11030146; 11237865; 11311120; 11353774; 11435445; 11672436; 11735247; 11893744; 11980723; 12039929; 12150827; 12163409; 12228231; 12242297; 12477932; 12482965; 12493691; 12519792; 12560069; 12606503; 12921955; 12960271; 12966085; 13679577; 14664696; 14726521; 15047604; 15057823; 15084259; 15109499; 15140004; 15184910; 15220471; 15342912; 15489334; 15582274; 15613482; 15632117; 15668399; 15688035; 15688409; 15692560; 15778376; 15890677; 15905404; 15987820; 16076959; 16100571; 16123151; 16133873; 16154098; 16282329; 16485043; 16492665; 16497530; 16571842; 16670089; 16690806; 16709600; 16849544; 16885156; 16916907; 16943287; 16950602; 16952014; 16952980; 16964289; 16973122; 16979636; 17030088; 17038621; 17050673; 17077083; 17202144; 17210752; 17218607; 17258205; 17285543; 17404186; 17442120; 17478621; 17490646; 17491598; 17525748; 17555999; 17556536; 17597184; 17599040; 17609436; 17613043; 17638879; 17873969; 17986608; 17993506; 18006475; 18022385; 18029348; 18096667; 18280254; 18301748; 18303411; 18316359; 18356527; 18408765; 18420577; 18483260; 18497882; 18497885; 18612045; 18660489; 18692812; 18713968; 18718910; 18786403; 18787186; 18788887; 18805788; 18815134; 18844239; 18951090; 18988640; 19049975; 19058789; 19075016; 19086408; 19103600; 19141580; 19150739; 19221179; 19233123; 19244250; 19254690; 19281796; 19293131; 19308286; 19321440; 19442434; 19463968; 19483080; 19503105; 19513505; 19535741; 19549905; 19563779; 19574223; 19584310; 19633686; 19675556; 19686743; 19696738; 19727442; 19740748; 19757185; 19772960; 19787258; 19793722; 19887561; 19893043; 19948975; 19953635; 19956688; 20018872; 20033803; 20061393; 20095040; 20125105; 20151947; 20351326; 20353756; 20357092; 20406953; 20412774; 20485516; 20543840; 20682687; 20719862; 20819778; 20868688; 20874444; 20884733; 20933505; 21069157; 21075101; 21116854; 21177767; 21177856; 21179458; 21185807; 21238503; 21298325; 21320536; 21321994; 21373837; 21388494; 21396404; 21423212; 21440011; 21440577; 21442235; 21505104; 21510935; 21539865; 21541992; 21613825; 21655267; 21666686; 21670150; 21696576; 21697492; 21708191; 21747041; 21775495; 21804543; 21993163; 22013015; 22072736; 22089931; 22159921; 22180177; 22197543; 22213032; 22266855; 22315317; 22343918; 22374423; 22389493; 22400069; 22411791; 22417654; 22454413; 22489460; 22515357; 22538365; 22552808; 22569260; 22622204; 22653055; 22675169; 22761423; 22761592; 22821817; 22865884; 22931788; 22992773; 23002242; 23025577; 23029264; 23035900; 23041154; 23059127; 23077062; 23105097; 23142810; 23160481; 23255113; 23263330; 23277279; 23291589; 23381604; 23389878; 23401241; 23460611; 23469153; 23532851; 23574718; 23603247; 23614736; 23615915; 23640897; 23686362; 23721824; 23733015; 23733882; 23748164; 23778262; 23799156; 23803610; 23814486; 23855308; 23865345; 23874926; 23995837; 24145170; 24268349; 24334454; 24374340 forkhead box O1 Ensembl:ENSG00000150907 HGNC:3819 HPRD:00645 MIM:136533 Vega:OTTHUMG00000016775 Other designations: forkhead box protein O1|forkhead box protein O1A|forkhead, Drosophila, homolog of, in rhabdomyosarcoma FOXO1 gene OGG:3000002335 Bin Zhao, Yue Liu, Oliver He CIG ED-B FINC FN FNZ GFND GFND2 LETS MSF WEB: http://www.ncbi.nlm.nih.gov/gene FN1 fibronectin 1 2335 2q34 9606 2 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0002020 (EC: IPI); GO_0002576 (EC: TAS); GO_0005178 (EC: IDA, PMID: 19738201); GO_0005515 (EC: IPI, PMID: 10627046); GO_0005518 (EC: NAS, PMID: 3024962); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005576 (EC: TAS); GO_0005577 (EC: IDA, PMID: 3997886); GO_0005604 (EC: IEA); GO_0005615 (EC: IDA); GO_0005793 (EC: IDA, PMID: 15308636); GO_0006953 (EC: IEA); GO_0007044 (EC: IEA); GO_0007155 (EC: NAS, PMID: 1423622); GO_0007161 (EC: IEA); GO_0007596 (EC: TAS); GO_0008201 (EC: NAS, PMID: 10075919); GO_0008360 (EC: IEA); GO_0009611 (EC: NAS, PMID: 7989369); GO_0016324 (EC: IEA); GO_0016504 (EC: IEA); GO_0018149 (EC: IDA, PMID: 3997886); GO_0022617 (EC: TAS); GO_0030168 (EC: TAS); GO_0030198 (EC: TAS); GO_0031012 (EC: IDA, PMID: 16157329); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0031012 (EC: ISS, Qualifier: colocalizes_with); GO_0031093 (EC: TAS); GO_0034446 (EC: IDA, PMID: 16236823); GO_0050900 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867); GO_0072562 (EC: IDA) PMID: 444675; 1311202; 1372909; 1400330; 1409674; 1423622; 1468447; 1532572; 1632457; 1694173; 1730778; 1875953; 1959621; 2012601; 2138612; 2229073; 2414772; 2531657; 2745554; 2822387; 2867902; 2989004; 2992573; 2992939; 3003095; 3021206; 3024962; 3031656; 3375063; 3478690; 3593230; 3770189; 3770201; 3900070; 3943369; 3988746; 3997552; 3997886; 4019516; 6092370; 6200322; 6304699; 6462919; 6630202; 6688418; 6693419; 6981115; 7050098; 7493623; 7499434; 7500359; 7519849; 7559467; 7583666; 7690138; 7963647; 7989369; 8063866; 8120056; 8120888; 8168508; 8173552; 8308892; 8360181; 8449034; 8468356; 8548820; 8599839; 8663002; 8756760; 8798654; 8905624; 8952048; 8997243; 8997639; 9016396; 9117345; 9169408; 9211865; 9334230; 9339851; 9361795; 9443108; 9501082; 9514732; 9626063; 9636140; 9651579; 9733622; 9751722; 9837825; 10075919; 10196121; 10451539; 10464263; 10470078; 10470109; 10627046; 10647176; 10706716; 10772816; 10783396; 10823831; 10848816; 11010812; 11023498; 11024059; 11134254; 11149921; 11157741; 11180285; 11276204; 11285119; 11285216; 11311202; 11342427; 11344214; 11419941; 11423128; 11423542; 11493006; 11500098; 11605051; 11686302; 11737888; 11751853; 11752017; 11768240; 11773026; 11775745; 11795204; 11801638; 11801679; 11829448; 11832485; 11847210; 11864705; 11867580; 11867643; 11891225; 11928812; 11937267; 11956183; 11960984; 11981027; 11997396; 12034705; 12069579; 12091360; 12100475; 12105189; 12119020; 12119179; 12127832; 12127836; 12149247; 12180907; 12225805; 12225811; 12270980; 12388756; 12401883; 12468382; 12477932; 12486316; 12497612; 12527107; 12535082; 12538453; 12538576; 12621118; 12631068; 12736686; 12761244; 12802498; 12810082; 12902636; 12917446; 14558920; 14602715; 14645245; 14662883; 14695199; 14702039; 14709558; 14718574; 14737076; 14760718; 15060148; 15161923; 15165854; 15174051; 15213410; 15231748; 15247227; 15265957; 15308636; 15331608; 15331737; 15384859; 15456495; 15456743; 15467744; 15485890; 15609325; 15645125; 15652337; 15699160; 15717924; 15721303; 15799029; 15806100; 15835821; 15855153; 15890670; 15912204; 15961545; 16005629; 16055535; 16083879; 16091757; 16106752; 16150826; 16157329; 16159961; 16236823; 16277979; 16322219; 16335952; 16336961; 16375583; 16378831; 16463680; 16495290; 16498633; 16581250; 16621928; 16757476; 16839338; 16928957; 16933105; 16978691; 16982604; 16984808; 16986166; 17003032; 17015452; 17027088; 17081983; 17136547; 17187346; 17266699; 17273763; 17416372; 17425334; 17459242; 17468934; 17490871; 17512904; 17526550; 17554369; 17596138; 17636193; 17704536; 17879163; 17929131; 17949711; 18006840; 18042364; 18064631; 18083324; 18268355; 18276110; 18313373; 18323857; 18332212; 18334936; 18340378; 18343220; 18348696; 18451110; 18451144; 18474427; 18499669; 18577581; 18624398; 18633626; 18690341; 18713862; 18716775; 18776591; 18801363; 18810851; 18824166; 18829569; 18957516; 18958156; 19020673; 19031824; 19037100; 19056867; 19094228; 19160003; 19161998; 19212764; 19224684; 19251642; 19342448; 19345424; 19391127; 19404402; 19417080; 19460753; 19471022; 19541353; 19542224; 19553700; 19564406; 19581300; 19616291; 19617627; 19701604; 19701759; 19730683; 19738201; 19760097; 19821053; 19834535; 19847669; 19880379; 19893244; 19893454; 19903114; 19913121; 19914350; 19935699; 20007695; 20012564; 20029029; 20043904; 20097172; 20097751; 20145126; 20161770; 20201928; 20210243; 20232238; 20357207; 20359090; 20364278; 20403349; 20419094; 20452482; 20463177; 20470202; 20484935; 20489157; 20495339; 20505078; 20506163; 20530259; 20552237; 20600851; 20628086; 20628340; 20628624; 20638438; 20643357; 20670094; 20671107; 20672308; 20672350; 20673868; 20686611; 20708078; 20725648; 20811396; 20814177; 20819642; 20851879; 20860816; 20939933; 21036168; 21036738; 21078624; 21098633; 21131589; 21138686; 21139048; 21148425; 21150319; 21160032; 21178109; 21190414; 21224775; 21311138; 21325030; 21330459; 21347378; 21429937; 21472136; 21508391; 21573010; 21630266; 21691075; 21768108; 21824169; 21840989; 21861843; 21876142; 21890473; 21924268; 21942715; 21961600; 21969082; 21980357; 21988832; 22009740; 22048274; 22219202; 22241990; 22319020; 22339947; 22351755; 22378065; 22496919; 22514602; 22523280; 22531343; 22586326; 22641031; 22674303; 22699679; 22705941; 22716248; 22782528; 22837202; 22848537; 22896658; 22918248; 22919069; 22936677; 23029023; 23056244; 23098431; 23116545; 23142796; 23170788; 23201264; 23201304; 23217101; 23238252; 23251222; 23288153; 23315067; 23341464; 23485472; 23509360; 23593224; 23612019; 23622001; 23643164; 23653350; 23653354; 23684510; 23740248; 23750785; 23763354; 23765377; 23791940; 23811340; 23872359; 23884219; 23908593; 23921871; 24030464; 24070235 fibronectin 1 Ensembl:ENSG00000115414 HGNC:3778 HPRD:00626 MIM:135600 Vega:OTTHUMG00000133054 Other designations: cold-insoluble globulin|fibronectin|migration-stimulating factor FN1 OGG:3000002339 Bin Zhao, Yue Liu, Oliver He FPTA PGGT1A PTAR2 WEB: http://www.ncbi.nlm.nih.gov/gene FNTA farnesyltransferase, CAAX box, alpha 2339 8p11 9606 8 Official from a nomenclature committee GO_0004660 (EC: IDA, PMID: 16893176); GO_0004660 (EC: IDA, Qualifier: contributes_to, PMID: 19228685); GO_0004661 (EC: IDA, PMID: 16893176); GO_0004662 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11687658); GO_0005737 (EC: TAS, PMID: 8599089); GO_0005829 (EC: TAS); GO_0005875 (EC: IDA, PMID: 19228685); GO_0005953 (EC: IDA, PMID: 16893176); GO_0005965 (EC: IDA, PMID: 16893176); GO_0006915 (EC: TAS); GO_0006921 (EC: TAS); GO_0007179 (EC: TAS, PMID: 8599089); GO_0007603 (EC: TAS); GO_0008017 (EC: IDA, PMID: 19228685); GO_0016056 (EC: TAS); GO_0018343 (EC: IDA, PMID: 16893176); GO_0018344 (EC: IDA, PMID: 16893176); GO_0022400 (EC: TAS); GO_0043014 (EC: IDA, PMID: 19228685); GO_0090044 (EC: IDA, PMID: 19228685); GO_0090045 (EC: IDA, PMID: 19228685) PMID: 1400319; 2217184; 7713879; 8106351; 8175923; 8276393; 8419339; 8494894; 8530343; 8599089; 8830800; 8889548; 8910345; 10676968; 10747914; 10852915; 11313965; 11598000; 11687658; 12036349; 12374986; 12477932; 12825937; 14702039; 15170324; 15451670; 15489334; 16893176; 17192483; 17353931; 18187620; 18406652; 18654987; 19228685; 19841875; 20403997; 21139048; 21906983; 21988832; 22160308; 22863883; 23602568 farnesyltransferase, CAAX box, alpha Ensembl:ENSG00000168522 HGNC:3782 HPRD:00607 MIM:134635 Vega:OTTHUMG00000165279 Other designations: FTase-alpha|GGTase-I-alpha|farnesyl-protein transferase alpha-subunit|protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha|protein prenyltransferase alpha subunit repeat containing 2|ras proteins prenyltransferase subunit alpha|type I protein geranyl-geranyltransferase alpha subunit FNTA OGG:3000002494 Bin Zhao, Yue Liu, Oliver He B1F B1F2 CPF FTF FTZ-F1 FTZ-F1beta LRH-1 LRH1 hB1F-2 WEB: http://www.ncbi.nlm.nih.gov/gene NR5A2 nuclear receptor subfamily 5, group A, member 2 2494 1q32.1 9606 1 Official from a nomenclature committee GO_0003677 (EC: IDA, PMID: 16289203); GO_0003700 (EC: IDA, PMID: 15205472); GO_0003705 (EC: TAS, PMID: 9786908); GO_0003707 (EC: IEA); GO_0004879 (EC: TAS, PMID: 16271724); GO_0005515 (EC: IPI, PMID: 12040021); GO_0005543 (EC: IDA, PMID: 15723037); GO_0005634 (EC: IDA, PMID: 15143342); GO_0005654 (EC: TAS); GO_0005737 (EC: IDA, PMID: 15205472); GO_0006355 (EC: IDA, PMID: 15723037); GO_0006355 (EC: TAS, PMID: 16289203); GO_0006367 (EC: TAS); GO_0008206 (EC: IEA); GO_0008270 (EC: IEA); GO_0009790 (EC: TAS, PMID: 16289203); GO_0010467 (EC: TAS); GO_0030522 (EC: TAS, PMID: 16271724); GO_0031018 (EC: TAS); GO_0042127 (EC: IEA); GO_0042592 (EC: NAS, PMID: 16289203); GO_0042632 (EC: IEA); GO_0043565 (EC: IDA, PMID: 16289203); GO_0044212 (EC: IDA, PMID: 15205472); GO_0045070 (EC: IDA, PMID: 19264593); GO_0045893 (EC: IDA, PMID: 15143342); GO_0045893 (EC: TAS, PMID: 15205472); GO_0045944 (EC: IEA) PMID: 7680097; 8938589; 9786908; 9858833; 10359768; 11030332; 11564608; 11595170; 11668176; 11927588; 12040021; 12198243; 12208674; 12477932; 12820970; 12852843; 12853459; 12972592; 14671206; 14701856; 14728801; 14963109; 15117876; 15121760; 15143151; 15143342; 15181096; 15205472; 15218078; 15327767; 15604093; 15613430; 15707893; 15723037; 15897460; 15923626; 15963945; 16091743; 16271724; 16282330; 16289203; 16439367; 16450584; 16469397; 16712791; 17036045; 17095585; 17522048; 17664281; 17895379; 17910058; 17952562; 17977826; 18029348; 18191017; 18270374; 18385139; 18410128; 18508634; 18665078; 19015525; 19022561; 19264593; 19359379; 19629617; 19692572; 19913121; 20101243; 20133449; 20159957; 20375098; 20379614; 20516075; 20607599; 20628086; 20811994; 20817789; 21129436; 21258413; 21262773; 21392518; 21536586; 21554248; 21566081; 21614002; 21949357; 21990348; 22048972; 22125638; 22187462; 22359603; 22504882; 23000165; 23038264; 23128233; 23471216; 23537609; 23637637; 23667258; 23737522; 23817023 nuclear receptor subfamily 5, group A, member 2 Ensembl:ENSG00000116833 HGNC:7984 HPRD:06830 MIM:604453 Vega:OTTHUMG00000035635 Other designations: CYP7A promoter-binding factor|alpha-1-fetoprotein transcription factor|b1-binding factor, hepatocyte transcription factor which activates enhancer II of hepatitis B virus|fetoprotein-alpha 1 (AFP) transcription factor|hepatocytic transcription factor hB1F-3|liver nuclear receptor homolog-1 variant 2|liver receptor homolog 1|liver receptor homolog-1|nuclear receptor NR5A2|nuclear receptor subfamily 5 group A member 2 NR5A2 OGG:3000002538 Bin Zhao, Yue Liu, Oliver He G6PC1 G6PT GSD1 GSD1a WEB: http://www.ncbi.nlm.nih.gov/gene G6PC glucose-6-phosphatase, catalytic subunit 2538 17q21 9606 17 Official from a nomenclature committee GO_0004346 (EC: IDA, PMID: 10318794); GO_0005789 (EC: TAS); GO_0005975 (EC: TAS); GO_0005977 (EC: TAS, PMID: 8211187); GO_0005980 (EC: IEA); GO_0006094 (EC: IEA); GO_0006094 (EC: IMP, PMID: 8211187); GO_0006641 (EC: IEA); GO_0008202 (EC: IEA); GO_0008645 (EC: TAS); GO_0010468 (EC: IEA); GO_0015758 (EC: TAS); GO_0015760 (EC: IEA); GO_0016021 (EC: IDA, PMID: 10318794); GO_0016311 (EC: IDA, PMID: 10318794); GO_0016773 (EC: IEA); GO_0030176 (EC: TAS, PMID: 10318794); GO_0035264 (EC: IEA); GO_0042301 (EC: IMP, PMID: 12093795); GO_0042593 (EC: IMP, PMID: 8211187); GO_0042632 (EC: IEA); GO_0044281 (EC: TAS); GO_0046415 (EC: IEA); GO_0051156 (EC: IEA); GO_0055085 (EC: TAS) PMID: 175958; 212064; 2172641; 2547044; 2986020; 7573034; 7623438; 7655466; 7668282; 7774924; 8182131; 8211187; 8612793; 8640227; 8733042; 9001800; 9332655; 9428641; 9675154; 9705299; 10023055; 10024523; 10026167; 10094563; 10318794; 10447271; 10452914; 10612834; 10748407; 10960498; 11672436; 11739393; 12093795; 12189168; 12373566; 12444104; 12477932; 12556524; 12560945; 13129915; 14718531; 14759518; 15316959; 15661744; 15696478; 15918042; 16892178; 16893891; 17354259; 18008183; 18449899; 18660489; 18805788; 18847435; 19082990; 19587243; 19832742; 20004937; 20301489; 20509832; 21109326; 21328436; 21733854; 21983240; 21988832; 23465595; 23755305 glucose-6-phosphatase, catalytic subunit HGNC:4056 HPRD:01983 MIM:613742 Other designations: G-6-Pase|G6Pase|G6Pase-alpha|glucose-6-phosphatase|glucose-6-phosphatase alpha G6PC OGG:3000002539 Bin Zhao, Yue Liu, Oliver He G6PD1 WEB: http://www.ncbi.nlm.nih.gov/gene G6PD glucose-6-phosphate dehydrogenase 2539 Xq28 9606 X Official from a nomenclature committee GO_0001816 (EC: IMP, PMID: 17361089); GO_0004345 (EC: IDA, PMID: 15858258); GO_0004345 (EC: IMP, PMID: 2420826); GO_0005515 (EC: IPI); GO_0005536 (EC: IDA, PMID: 15858258); GO_0005536 (EC: IMP, PMID: 5643703); GO_0005634 (EC: IEA); GO_0005737 (EC: IDA); GO_0005829 (EC: IDA, PMID: 743300); GO_0005829 (EC: TAS); GO_0005975 (EC: TAS); GO_0006098 (EC: IDA, PMID: 2297768); GO_0006098 (EC: TAS); GO_0006629 (EC: TAS, PMID: 17361089); GO_0006695 (EC: IMP, PMID: 12027950); GO_0006739 (EC: IDA, PMID: 15858258); GO_0006740 (EC: IMP, PMID: 17516514); GO_0006749 (EC: IMP, PMID: 17516514); GO_0009051 (EC: IMP, PMID: 2420826); GO_0009898 (EC: IDA, PMID: 743300); GO_0010734 (EC: IMP, PMID: 17516514); GO_0014070 (EC: IEA); GO_0019322 (EC: IDA, PMID: 5643703); GO_0021762 (EC: IEP); GO_0032094 (EC: IEA); GO_0034599 (EC: IMP, PMID: 17516514); GO_0042803 (EC: IPI, PMID: 15858258); GO_0043249 (EC: IMP, PMID: 5643703); GO_0043523 (EC: IEA); GO_0044281 (EC: TAS); GO_0045471 (EC: IEA); GO_0046390 (EC: IMP, PMID: 2420826); GO_0050661 (EC: IDA, PMID: 15858258); GO_0051156 (EC: IDA, PMID: 15858258); GO_0051156 (EC: IMP, PMID: 5643703); GO_0055114 (EC: IMP, PMID: 2420826); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 743300; 1303180; 1303182; 1536798; 1611091; 1874446; 1889820; 1945893; 2297768; 2420826; 2428611; 2758468; 2836867; 2910917; 2912069; 3012556; 3126064; 3393536; 3446582; 3515319; 5643703; 5666113; 6696761; 7825590; 7857286; 7858267; 7959695; 8193373; 8356804; 8364584; 8466644; 8490627; 8533762; 8733135; 8826878; 9233561; 10087986; 10089300; 10627140; 10698963; 10745013; 11024211; 11042039; 11112389; 11237690; 11256614; 11440553; 11499668; 11793482; 11852882; 11857737; 11874436; 11876979; 11877026; 11920200; 12027950; 12130518; 12135480; 12378426; 12380870; 12439228; 12477932; 12497642; 12524354; 12588050; 12616531; 12641410; 12665801; 12680285; 12696079; 12737938; 12737940; 12737943; 12768444; 12850494; 12921788; 12972027; 14614139; 14757424; 14757426; 15223006; 15282679; 15307413; 15315792; 15330559; 15466166; 15476167; 15489334; 15506519; 15558953; 15592455; 15598086; 15622766; 15659240; 15718915; 15727905; 15748456; 15766741; 15772651; 15858258; 15864125; 15906717; 15906719; 15914531; 15951569; 15957246; 16020776; 16059744; 16088936; 16136268; 16137669; 16143877; 16155737; 16236267; 16255851; 16272653; 16331553; 16335966; 16356170; 16461316; 16483869; 16532971; 16569302; 16607506; 16637741; 16792831; 16859949; 16927025; 16934959; 16944148; 17007653; 17018380; 17077204; 17264545; 17361089; 17499234; 17516514; 17524386; 17557555; 17587269; 17611006; 17623298; 17637841; 17653668; 17660836; 17877203; 17959407; 18029348; 18043863; 18046504; 18056001; 18066402; 18086567; 18164966; 18173836; 18215251; 18226470; 18302154; 18376107; 18458302; 18493020; 18494377; 18558634; 18660489; 18677765; 18781797; 18985093; 19056867; 19219640; 19223928; 19224086; 19272180; 19317913; 19323016; 19336475; 19359662; 19419973; 19422023; 19465117; 19497363; 19589177; 19594365; 19632868; 19640310; 19738201; 19811411; 19858149; 19896395; 19913121; 19941843; 19996424; 20007901; 20017397; 20032314; 20113600; 20118060; 20200584; 20203002; 20236109; 20447239; 20459687; 20507315; 20514852; 20520804; 20528626; 20582980; 20602793; 20621077; 20628086; 20684792; 20713184; 20927393; 20949590; 21125776; 21139048; 21157431; 21180140; 21205543; 21302115; 21376116; 21376267; 21397531; 21507164; 21507207; 21549219; 21853274; 21890473; 21906983; 21963094; 21987572; 22012600; 22117603; 22139979; 22165289; 22307442; 22364808; 22431005; 22505724; 22537951; 22552160; 22768742; 22770933; 22848499; 22863883; 22906047; 22906837; 22939629; 22958163; 22963789; 23000965; 23023104; 23065279; 23146719; 23185302; 23233666; 23275194; 23389243; 23446634; 23631859; 23640907; 23696099; 23742107; 23824909 glucose-6-phosphate dehydrogenase Ensembl:ENSG00000160211 HGNC:4057 HPRD:02377 MIM:305900 Vega:OTTHUMG00000024237 Other designations: glucose-6-phosphate 1-dehydrogenase G6PD OGG:3000002549 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene GAB1 GRB2-associated binding protein 1 2549 4q31.21 9606 4 Official from a nomenclature committee GO_0004871 (EC: IEA); GO_0005070 (EC: TAS, PMID: 8596638); GO_0005515 (EC: IPI, PMID: 10978177); GO_0005829 (EC: TAS); GO_0006979 (EC: IEA); GO_0007173 (EC: TAS); GO_0007257 (EC: IEA); GO_0007507 (EC: IEA); GO_0008283 (EC: TAS, PMID: 8596638); GO_0008286 (EC: TAS); GO_0008543 (EC: TAS); GO_0008544 (EC: IEA); GO_0030334 (EC: IEA); GO_0038095 (EC: TAS); GO_0045087 (EC: TAS); GO_0048008 (EC: IEA); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0060711 (EC: IEA); GO_0070102 (EC: IEA) PMID: 8596638; 9045692; 9242692; 9252406; 9356464; 9658397; 9804835; 9878555; 9890893; 9891995; 10022866; 10068651; 10455108; 10648629; 10734310; 10747014; 10753869; 10871282; 10913131; 10978177; 10995442; 11134009; 11278704; 11314042; 11323411; 11353842; 11360177; 11402314; 11432805; 11507676; 11606067; 11701952; 11707404; 11894096; 11896055; 11940581; 11960376; 12008033; 12065326; 12138161; 12176364; 12370245; 12477932; 12486104; 12522270; 12582165; 12748184; 12766170; 12773374; 12808090; 12819203; 12855672; 14560030; 14660651; 14665621; 14701753; 14702039; 14973141; 14982882; 15010462; 15351743; 15379552; 15489334; 15574420; 15665327; 15815621; 15940252; 15952937; 16344560; 16638574; 16687399; 16787925; 16849525; 17145761; 17178724; 17211494; 17625596; 18003605; 18192688; 18271526; 18577518; 19167335; 19233262; 19380743; 19665053; 19881549; 19913121; 20005866; 20237496; 20467438; 20602450; 20628086; 20677014; 20723025; 20936779; 21282639; 21706016; 21782801; 21804548; 22366451; 22536782; 22751113; 22851227; 22865653; 22883624; 22915589; 23334917; 23612964; 23824909 GRB2-associated binding protein 1 Other designations: GRB2-associated binder 1|GRB2-associated-binding protein 1|growth factor receptor bound protein 2-associated protein 1 GAB1 OGG:3000002551 Bin Zhao, Yue Liu, Oliver He E4TF1-60 E4TF1A NFT2 NRF2 NRF2A RCH04A07 WEB: http://www.ncbi.nlm.nih.gov/gene GABPA GA binding protein transcription factor, alpha subunit 60kDa 2551 21q21.3 9606 21 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0000790 (EC: IDA); GO_0000978 (EC: IDA); GO_0001228 (EC: IDA); GO_0001701 (EC: IEA); GO_0003677 (EC: TAS, PMID: 8441384); GO_0003682 (EC: IEA); GO_0003700 (EC: TAS, PMID: 7590737); GO_0003713 (EC: TAS, PMID: 8441384); GO_0005515 (EC: IPI, PMID: 10675337); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0006366 (EC: TAS, PMID: 8441384); GO_0030154 (EC: IBA); GO_0044212 (EC: IDA, PMID: 9857059); GO_0045653 (EC: IEA); GO_0045944 (EC: IDA); GO_0046982 (EC: IDA, PMID: 9857059) PMID: 7590737; 7737900; 7799916; 8125298; 8441384; 8543189; 8889548; 9016666; 9461436; 9792629; 9857059; 9990060; 10585419; 10660899; 10675337; 10830953; 11237613; 11953439; 12107413; 12477932; 15361867; 15928042; 16574658; 16581781; 16712791; 17161026; 17304221; 17357964; 17439941; 18020712; 18029348; 18378679; 18660489; 18852034; 19116932; 19187944; 19324871; 19409485; 19424503; 19471022; 19687146; 19951946; 20028934; 20127517; 21624509; 21693764; 21774808; 21832049; 21890473; 21906983; 21988832; 22480519; 22505724; 22749526; 22863883; 22939629; 23000965; 23099293; 23284628; 23684612; 23856623; 24076158 GA binding protein transcription factor, alpha subunit 60kDa Ensembl:ENSG00000154727 HGNC:4071 HPRD:11793 MIM:600609 Vega:OTTHUMG00000078443 Other designations: GA binding protein transcription factor alpha subunit 60kDa|GA-binding protein alpha chain|GABP subunit alpha|human nuclear respiratory factor-2 subunit alpha|nuclear respiratory factor 2 alpha subunit|nuclear respiratory factor 2 subunit alpha|transcription factor E4TF1-60 GABPA OGG:3000002619 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene GAS1 growth arrest-specific 1 2619 9q21.3-q22 9606 9 Official from a nomenclature committee GO_0002053 (EC: IEA); GO_0005515 (EC: IPI); GO_0005886 (EC: IDA, PMID: 8127893); GO_0007050 (EC: IEA); GO_0007411 (EC: IEA); GO_0008589 (EC: ISS); GO_0010955 (EC: IMP); GO_0012501 (EC: IEA); GO_0016021 (EC: NAS, PMID: 8127893); GO_0021587 (EC: IEA); GO_0021904 (EC: IEA); GO_0030308 (EC: IEA); GO_0035924 (EC: IEP, PMID: 15070677); GO_0042473 (EC: IEA); GO_0042474 (EC: IEA); GO_0042476 (EC: IEA); GO_0042733 (EC: IEA); GO_0042981 (EC: ISS); GO_0043010 (EC: IEA); GO_0043066 (EC: IEA); GO_0045165 (EC: ISS); GO_0045879 (EC: IEA); GO_0045880 (EC: IEA); GO_0045930 (EC: IDA, PMID: 8127893); GO_0045930 (EC: IGI, PMID: 11356029); GO_0046658 (EC: ISS); GO_0048589 (EC: ISS); GO_0048592 (EC: IEA); GO_0048701 (EC: IEA); GO_0050679 (EC: IEA); GO_0050680 (EC: IEA); GO_0060021 (EC: IEA); GO_0060628 (EC: IMP); GO_2001240 (EC: IEA) PMID: 1505026; 7956349; 8127893; 8307588; 8889548; 9466658; 10996315; 11356029; 11572986; 11846389; 11906213; 12477932; 15070677; 15103018; 16551639; 17726382; 18394855; 18981472; 19322201; 19460624; 19638344; 20050020; 20583177; 20628624; 21111449; 21357679; 21842183; 21890473; 21901158; 21971401; 22311470; 22846196; 23254899 growth arrest-specific 1 Other designations: GAS-1|Growth arrest-specific gene-1|growth arrest-specific protein 1 GAS1 OGG:3000002673 Bin Zhao, Yue Liu, Oliver He CMSTA1 GFA GFAT GFAT 1 GFAT1 GFAT1m GFPT GFPT1L MSLG WEB: http://www.ncbi.nlm.nih.gov/gene GFPT1 glutamine--fructose-6-phosphate transaminase 1 2673 2p13 9606 2 Official from a nomenclature committee GO_0004360 (EC: IEA); GO_0005829 (EC: TAS); GO_0006002 (EC: IEA); GO_0006042 (EC: IEA); GO_0006048 (EC: IEA); GO_0006048 (EC: TAS); GO_0006112 (EC: TAS, PMID: 1460020); GO_0006488 (EC: TAS); GO_0006541 (EC: IEA); GO_0006987 (EC: TAS); GO_0009744 (EC: IEA); GO_0016051 (EC: IEA); GO_0016597 (EC: IEA); GO_0018279 (EC: TAS); GO_0030246 (EC: IEA); GO_0030968 (EC: TAS); GO_0032869 (EC: IEA); GO_0032922 (EC: ISS); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS); GO_0045719 (EC: IEA); GO_0051289 (EC: IEA); GO_0070062 (EC: IDA) PMID: 1460020; 2037571; 7601477; 7607664; 8144040; 8619474; 9110174; 9519709; 10198162; 10806197; 10997685; 11587069; 11679416; 12477932; 12802498; 14988277; 15308130; 15489334; 15595739; 15613432; 15878746; 16341674; 16344560; 16964243; 17024311; 17081983; 17542649; 17941647; 18781797; 19059404; 19170765; 19322201; 20301347; 20562859; 20845477; 21139048; 21310273; 21890473; 21906983; 21988832; 22053931; 22505724; 22586326; 22863883; 22987706; 23000965; 23569079; 23794683; 24250222 glutamine--fructose-6-phosphate transaminase 1 Ensembl:ENSG00000198380 HGNC:4241 HPRD:00702 MIM:138292 Vega:OTTHUMG00000152666 Other designations: D-fructose-6-phosphate amidotransferase 1|glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1|glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1|glutamine:fructose-6-phosphate amidotransferase 1|hexosephosphate aminotransferase 1 GFPT1 OGG:3000002674 Bin Zhao, Yue Liu, Oliver He GDNFR GDNFRA GFR-ALPHA-1 RET1L RETL1 TRNR1 WEB: http://www.ncbi.nlm.nih.gov/gene GFRA1 GDNF family receptor alpha 1 2674 10q26.11 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0005102 (EC: TAS, PMID: 9545641); GO_0005886 (EC: IEA); GO_0007166 (EC: NAS, PMID: 8674117); GO_0007411 (EC: TAS); GO_0016167 (EC: TAS, PMID: 10829012); GO_0019898 (EC: TAS, PMID: 10829012); GO_0031225 (EC: IEA); GO_0035860 (EC: TAS, PMID: 10829012); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 7829101; 8657309; 8674117; 8889548; 9108413; 9177201; 9182803; 9192898; 9407096; 9465905; 9482105; 9545641; 9600247; 9697851; 9740802; 10774729; 10821644; 10829012; 11182089; 11360200; 11932334; 12065680; 12477932; 12490080; 12624147; 12837245; 14514671; 14566559; 14702039; 14759258; 15310755; 15489334; 16175604; 16344560; 16385451; 16551639; 16644101; 16813162; 17298301; 17825269; 18089803; 18353777; 18394855; 18845535; 19019765; 19056867; 19188437; 19282698; 19896648; 20116071; 20347960; 20350599; 20379614; 20424473; 20669561; 21133924; 21988832; 22729463; 23351331; 23382691; 23793025; 23824909 GDNF family receptor alpha 1 Ensembl:ENSG00000151892 HGNC:4243 HPRD:03291 MIM:601496 Other designations: GDNF family receptor alpha-1|GDNF receptor alpha-1|GDNFR-alpha-1|GPI-linked anchor protein|Glial cell line-derived neurotrophic factor receptor alpha|PI-linked cell-surface accessory protein|RET ligand 1|TGF-beta related neurotrophic factor receptor 1|TGF-beta-related neurotrophic factor receptor 1 GFRA1 OGG:3000002729 2729 GO_0000096 (EC: TAS); GO_0000287 (EC: IDA, PMID: 24639); GO_0004357 (EC: IDA, PMID: 11972604); GO_0004357 (EC: IMP, PMID: 16183645); GO_0005524 (EC: IEA); GO_0005737 (EC: IBA); GO_0005829 (EC: TAS); GO_0006534 (EC: IDA, PMID: 2294991); GO_0006536 (EC: IDA, PMID: 12663448); GO_0006750 (EC: IDA, PMID: 10395918); GO_0006750 (EC: IEA); GO_0006750 (EC: IMP, PMID: 12663448); GO_0006750 (EC: TAS); GO_0006805 (EC: TAS); GO_0006979 (EC: IDA, PMID: 10395918); GO_0008637 (EC: IEA); GO_0009408 (EC: IDA, PMID: 8104187); GO_0009725 (EC: IDA, PMID: 8104187); GO_0016595 (EC: IDA, PMID: 9841880); GO_0017109 (EC: IEA); ... (Note: Only 20 GO IDs shown. See more from web page source or RDF output.)" PMID: 24639; 1350904; 2294991; 5058793; 7726839; 7789189; 8104187; 8825659; 8995480; 9675072; 9841880; 10395918; 10439045; 10515893; 10733484; 11820781; 11844594; 11972604; 12070177; 12477932; 12500194; 12598062; 12663448; 14574404; 14676828; 14702039; 15451055; 15485876; 15489334; 16183645; 16322067; 16403949; 16491484; 16599007; 16690975; 16766924; 17109620; 17207022; 17333241; 17344309; 17479437; 17601350; 17643973; 17921251; 17961430; 18035085; 18066575; 18276794; 18420959; 18549827; glutamate-cysteine ligase catalytic subunit Ensembl:ENSG00000001084 HGNC:4311 HPRD:06032 MIM:606857 Vega:OTTHUMG00000160220 GCLC OGG:3000002730 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene glutamate-cysteine ligase, modifier subunit 2730 9606 Official from a nomenclature committee GO_0000096 (EC: TAS); GO_0004357 (EC: IDA, Qualifier: contributes_to, PMID: 9841880); GO_0004357 (EC: IMP, Qualifier: contributes_to, PMID: 16183645); GO_0005829 (EC: NAS, PMID: 9895302); GO_0005829 (EC: TAS); GO_0006534 (EC: IEA); GO_0006536 (EC: IDA, PMID: 9841880); GO_0006750 (EC: IDA, PMID: 10395918); GO_0006750 (EC: IEA); GO_0006750 (EC: IMP, PMID: 12081989); GO_0006750 (EC: TAS); GO_0006805 (EC: TAS); GO_0006979 (EC: IDA, PMID: 10395918); GO_0008637 (EC: IEA); GO_0017109 (EC: IEA); GO_0034641 (EC: TAS); GO_0035226 (EC: IPI, PMID: 9675072); GO_0035229 (EC: IEA); GO_0042493 (EC: IDA, PMID: 9895302); GO_0043524 (EC: IEA); ... (Note: Only 20 GO IDs shown. " PMID: 7826375; 7829101; 8825659; 8978789; 9675072; 9841137; 9841880; 9895302; 10395918; 10674357; 12081989; 12477932; 12975258; 14532974; 15451055; 15489334; 15946948; 16081425; 16183645; 16599007; 16677451; 16710414; 16712791; 16766924; 16909399; 17333241; 17344309; 17353931; 17548779; 17643973; 17924854; 17961430; 18066575; 18449862; 18560528; 18614560; 18991850; 19056482; 19126404; 19153097; 19420105; 19455074; 19460752; 19578796; 19584774; 19808663; 19896490; 19913121; 20061124; 20200426 glutamate-cysteine ligase, modifier subunit HGNC:4312 HPRD:03106 MIM:601176 GCLM OGG:3000002805 Bin Zhao, Yue Liu, Oliver He ASTQTL1 GIG18 cAspAT cCAT WEB: http://www.ncbi.nlm.nih.gov/gene GOT1 glutamic-oxaloacetic transaminase 1, soluble 2805 10q24.1-q25.1 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0000096 (EC: TAS); GO_0004069 (EC: IDA, PMID: 2182221); GO_0004069 (EC: ISS); GO_0004069 (EC: TAS); GO_0004609 (EC: IEA); GO_0005737 (EC: IDA, PMID: 7060339); GO_0005764 (EC: IEA); GO_0005829 (EC: TAS); GO_0005975 (EC: TAS); GO_0006006 (EC: TAS); GO_0006094 (EC: TAS); GO_0006103 (EC: ISS); GO_0006107 (EC: IEA); GO_0006114 (EC: ISS); GO_0006531 (EC: ISS); GO_0006532 (EC: IEA); GO_0006533 (EC: IDA, PMID: 2241899); GO_0006536 (EC: ISS); GO_0006595 (EC: TAS); GO_0008483 (EC: TAS); GO_0008652 (EC: TAS); GO_0019509 (EC: TAS); GO_0019550 (EC: IEA); GO_0019551 (EC: IEA); GO_0030170 (EC: IEA); GO_0031406 (EC: IEA); GO_0032869 (EC: IEP, PMID: 8396422); GO_0034641 (EC: TAS); GO_0043679 (EC: IEA); GO_0044281 (EC: TAS); GO_0047801 (EC: ISS); GO_0051384 (EC: IEP, PMID: 8396422); GO_0055089 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0080130 (EC: IEA) PMID: 225064; 1974457; 2182221; 2225456; 2241899; 2731362; 2777255; 3207426; 6391741; 6397370; 7060339; 8349677; 8396422; 8619474; 9110174; 10360399; 12477932; 12480555; 15164054; 15306699; 15489334; 16169070; 16344560; 16681433; 17623298; 17877759; 17907318; 18242760; 18752324; 19012630; 19056867; 19370784; 19393479; 20029029; 20201926; 20205615; 20499337; 20972737; 21139048; 21750724; 21900944; 21906983; 21963094; 21988832; 22132177; 22242166; 22352690; 22412388; 22863883; 23667618; 24124411 glutamic-oxaloacetic transaminase 1, soluble Ensembl:ENSG00000120053 HGNC:4432 HPRD:00687 MIM:138180 Vega:OTTHUMG00000018882 GOT1 OGG:3000002806 Bin Zhao, Yue Liu, Oliver He KAT4 KATIV mitAAT WEB: http://www.ncbi.nlm.nih.gov/gene GOT2 glutamic-oxaloacetic transaminase 2, mitochondrial 2806 16q21 20140408 9606 16 protein-coding Official from a nomenclature committee GO_0004069 (EC: EXP); GO_0004069 (EC: IDA, PMID: 2182221); GO_0004069 (EC: ISS); GO_0005739 (EC: IDA); GO_0005739 (EC: ISS); GO_0005743 (EC: IEA); GO_0005759 (EC: TAS); GO_0005886 (EC: IDA, PMID: 9537447); GO_0005975 (EC: TAS); GO_0006006 (EC: TAS); GO_0006094 (EC: TAS); GO_0006103 (EC: ISS); GO_0006107 (EC: IEA); GO_0006531 (EC: ISS); GO_0006532 (EC: IEA); GO_0006533 (EC: IDA, PMID: 2567216); GO_0006536 (EC: ISS); GO_0008652 (EC: TAS); GO_0015908 (EC: IEP, PMID: 9537447); GO_0016212 (EC: IEA); GO_0019470 (EC: TAS); GO_0019550 (EC: IEA); GO_0019551 (EC: IEA); GO_0030170 (EC: IEA); GO_0034641 (EC: TAS); GO_0044281 (EC: TAS); GO_0044822 (EC: IDA); GO_0045471 (EC: IDA, PMID: 9537447); GO_0070062 (EC: IDA); GO_0080130 (EC: IEA) PMID: 376500; 752471; 2182221; 2567216; 2731362; 2777255; 2899080; 3207426; 3997814; 4052435; 5450376; 6397370; 6930651; 7114792; 7225087; 7559589; 8125298; 8349677; 9537447; 12477932; 12601813; 14702039; 15489334; 16169070; 16212419; 17353931; 17442055; 17728674; 17877759; 18781797; 19305408; 19834535; 20360068; 20877624; 21081666; 21139048; 21223598; 21319273; 21890473; 21900206; 21906983; 21963094; 22713574; 23000965 glutamic-oxaloacetic transaminase 2, mitochondrial Ensembl:ENSG00000125166 HGNC:4433 HPRD:00684 MIM:138150 Vega:OTTHUMG00000133769 GOT2 OGG:3000002817 Bin Zhao, Yue Liu, Oliver He glypican WEB: http://www.ncbi.nlm.nih.gov/gene GPC1 glypican 1 2817 2q35-q37 9606 2 Official from a nomenclature committee GO_0001523 (EC: TAS); GO_0005507 (EC: IDA, PMID: 12732622); GO_0005578 (EC: ISS); GO_0005615 (EC: IEA); GO_0005768 (EC: IEA); GO_0005796 (EC: TAS); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 2148568); GO_0005975 (EC: TAS); GO_0006024 (EC: TAS); GO_0006027 (EC: TAS); GO_0007411 (EC: TAS); GO_0007603 (EC: TAS); GO_0014037 (EC: ISS); GO_0017134 (EC: ISS); GO_0030200 (EC: IDA, PMID: 12732622); GO_0030203 (EC: TAS); GO_0030204 (EC: TAS); GO_0031225 (EC: IEA); GO_0032288 (EC: ISS); GO_0040037 (EC: ISS); GO_0043202 (EC: TAS); GO_0043236 (EC: ISS); GO_0043395 (EC: IEA); GO_0044281 (EC: TAS); GO_0045121 (EC: IDA, Qualifier: colocalizes_with, PMID: 12732622); GO_0045121 (EC: ISS); GO_0070062 (EC: IDA, PMID: 19199708); GO_2001016 (EC: ISS) PMID: 1417860; 2148568; 7774946; 8125298; 9802880; 10196157; 10364234; 10527946; 10892742; 11336704; 11375980; 11454708; 11968010; 12084716; 12477932; 12732622; 12972423; 14702039; 15084524; 15249209; 15297422; 15489334; 15547662; 16723715; 17016645; 18064304; 18536657; 18634034; 19023125; 19166823; 19199708; 19479373; 21139048; 21265098; 21932778; 22351761; 22863883; 23624389; 23736812; 24019070 glypican 1 Ensembl:ENSG00000063660 HGNC:4449 HPRD:02671 MIM:600395 Vega:OTTHUMG00000133349 Other designations: glypican proteoglycan 1|glypican-1 GPC1 OGG:3000002826 Bin Zhao, Yue Liu, Oliver He GPR2 WEB: http://www.ncbi.nlm.nih.gov/gene CCR10 chemokine (C-C motif) receptor 10 2826 17q21.1-q21.3 9606 17 GO_0004930 (EC: TAS, PMID:7851889); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:7851889); GO_0006935 (EC: IEA); GO_0006955 (EC: IEA); GO_0007186 (EC: TAS, PMID:7851889); GO_0007204 (EC: IEA); GO_0016493 (EC: IEA) PMID:7851889; 8889548; 9364936; 10706668; 10725696; 10725697; 10781587; 10975800; 11298490; 11821900; 12477932; 14667819; 15489334; 15700309; 16460738; 16675558; 16785557; 17071491; 17474147; 18240029; 18577758; 18782672; 20237496; 20947433; 21075690; 21937703; 22350183; 22526457; 22944692 chemokine (C-C motif) receptor 10 HGNC:4474 HPRD:02586 MIM:600240 Other designations: C-C CKR-10|C-C chemokine receptor type 10|CC chemokine receptor 10|CC-CKR-10|CCR-10|G protein-coupled receptor 2|G-protein coupled receptor 2 CCR10 OGG:3000002833 Bin Zhao, Yue Liu, Oliver He CD182 CD183 CKR-L2 CMKAR3 GPR9 IP10-R Mig-R MigR WEB: http://www.ncbi.nlm.nih.gov/gene CXCR3 chemokine (C-X-C motif) receptor 3 2833 Xq13 9606 X Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0001937 (EC: IDA, PMID: 12782716); GO_0002685 (EC: IEA); GO_0004872 (EC: IDA, PMID: 12782716); GO_0004950 (EC: TAS, PMID: 9064356); GO_0005737 (EC: TAS, PMID: 10903743); GO_0005886 (EC: IDA, PMID: 12782716); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 9064356); GO_0006915 (EC: IEA); GO_0006928 (EC: TAS, PMID: 10741397); GO_0006935 (EC: TAS, PMID: 10903763); GO_0006954 (EC: IEA); GO_0007155 (EC: TAS, PMID: 10942362); GO_0007166 (EC: IDA, PMID: 11554781); GO_0007186 (EC: IMP, PMID: 12782716); GO_0007204 (EC: IEA); GO_0008284 (EC: IDA, PMID: 12782716); GO_0009897 (EC: IEA); GO_0010818 (EC: IEA); GO_0016494 (EC: IEA); GO_0016525 (EC: IDA, PMID: 12782716); GO_0019722 (EC: IEA); GO_0019956 (EC: IPI, PMID: 11554781); GO_0019958 (EC: IDA, PMID: 12782716); GO_0030816 (EC: IDA, PMID: 12782716); GO_0043950 (EC: IDA, PMID: 12782716); GO_0045766 (EC: IDA, PMID: 12782716); GO_0045944 (EC: IDA, PMID: 12782716); GO_0050921 (EC: IDA, PMID: 12782716); GO_0051281 (EC: IMP, PMID: 12782716); GO_0071954 (EC: IDA, PMID: 12782716); GO_1900118 (EC: IDA, PMID: 12782716); GO_1900119 (EC: IDA, PMID: 12782716) PMID: 2834384; 8666380; 9064356; 9419219; 9466968; 9625760; 9660793; 10233762; 10393705; 10627472; 10666479; 10741397; 10900358; 10903743; 10903763; 10942362; 11083865; 11134180; 11160352; 11196695; 11554781; 11559369; 11714650; 11739530; 11966764; 11990865; 12016104; 12055238; 12070001; 12097412; 12270371; 12356205; 12425561; 12444109; 12445801; 12477932; 12517959; 12571234; 12688353; 12750173; 12782716; 12819030; 12884299; 12919091; 12953097; 12960247; 12960302; 14578618; 14618028; 14630801; 14657006; 14742268; 15126579; 15150261; 15155273; 15181567; 15254596; 15265234; 15273303; 15328188; 15489334; 15501397; 15518810; 15528361; 15578697; 15687242; 15713799; 15725351; 15808644; 15843529; 15856455; 15879427; 15885315; 16033640; 16034118; 16043121; 16127166; 16243485; 16339779; 16368892; 16455991; 16456020; 16679918; 16733654; 16787707; 16806233; 16847335; 16861617; 16930533; 16934957; 17018607; 17142783; 17142784; 17251291; 17339184; 17363734; 17457216; 17560677; 17615381; 17666357; 17703412; 17912012; 17947699; 18037659; 18174362; 18240029; 18280341; 18291705; 18375741; 18453591; 18485912; 18497951; 18616679; 18689270; 18729739; 18761554; 18798334; 18832436; 18962861; 19017998; 19106589; 19134328; 19232748; 19258923; 19344719; 19380511; 19539215; 19641142; 19703720; 19734217; 19735481; 19758167; 19767105; 19800124; 20041963; 20047517; 20059481; 20079227; 20096889; 20164417; 20185576; 20203286; 20228225; 20237496; 20377416; 20379873; 20429924; 20485444; 20503287; 20529825; 20733031; 20848514; 20855888; 20856926; 20980681; 21051441; 21087446; 21091908; 21148743; 21255008; 21274647; 21303425; 21303517; 21357438; 21426802; 21538345; 21645215; 21739422; 21811993; 21962843; 22079021; 22111598; 22236567; 22262158; 22369302; 22392992; 22401929; 22675496; 22685032; 22689289; 22792160; 22796894; 22798340; 22936405; 23121557; 23158864; 23179902; 23298254; 23600831; 23643635; 24129241; 24135023 chemokine (C-X-C motif) receptor 3 Ensembl:ENSG00000186810 HGNC:4540 HPRD:02936 MIM:300574 Vega:OTTHUMG00000033326 Other designations: C-X-C chemokine receptor type 3|CXC-R3|CXCR-3|G protein-coupled receptor 9|IP-10 receptor|IP10 receptor|Mig receptor|chemokine (C-X-C) receptor 3|interferon-inducible protein 10 receptor CXCR3 OGG:3000002863 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene GPR39 G protein-coupled receptor 39 2863 2q21-q22 9606 2 Official from a nomenclature committee GO_0004930 (EC: IEA); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 9441746); GO_0007186 (EC: TAS, PMID: 9441746); GO_0046872 (EC: IEA) PMID: 8889548; 9441746; 12477932; 14702039; 15383539; 15489334; 15815621; 16344560; 16959833; 17054911; 17488974; 17885920; 18180304; 18588883; 18815158; 19920139; 20379614; 20424473; 20522546; 21352519; 21900206; 22545109; 22879599; 23485550 G protein-coupled receptor 39 Other designations: G-protein coupled receptor 39 GPR39 OGG:3000002875 Bin Zhao, Yue Liu, Oliver He AAT1 ALT1 GPT1 WEB: http://www.ncbi.nlm.nih.gov/gene GPT glutamic-pyruvate transaminase (alanine aminotransferase) 2875 8q24.3 20140408 9606 8 protein-coding Official from a nomenclature committee GO_0004021 (EC: EXP); GO_0004021 (EC: NAS, PMID: 1931970); GO_0005829 (EC: TAS); GO_0008652 (EC: TAS); GO_0030170 (EC: IEA); GO_0034641 (EC: TAS); GO_0042853 (EC: IEA); GO_0044281 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 49232; 1931970; 3192219; 5581908; 7114790; 7114791; 7361762; 8125298; 9119391; 11863375; 12358155; 12477932; 12480555; 12774006; 14506613; 15306699; 15342556; 15489334; 16652026; 17134955; 17378732; 17405346; 17570354; 17764776; 17766001; 17877759; 17907292; 17907318; 17934148; 18090161; 18178283; 18242760; 18315552; 18432999; 18473412; 18508279; 18708042; 18763311; 18774966; 19012630; 19056867; 19065605; 19100265; 19159884; 19217453; 19232448; 19303161; 19360321; 19370784; 19393479; 19687577; 19938201; 20032584; 20190678; 20205615; 20387481; 20433554; 20872970; 20961180; 20972737; 21040936; 21199427; 21692932; 21715038; 21720553; 21987480; 21988832; 22132177; 22140488; 22158663; 22177542; 22242166; 22293393; 22352690; 22357454; 22389715; 22954960; 22975640; 23119080; 23384374; 23403445; 23667618; 23794308; 23880909 glutamic-pyruvate transaminase (alanine aminotransferase) Ensembl:ENSG00000167701 HGNC:4552 HPRD:00689 MIM:138200 Vega:OTTHUMG00000165176 GPT OGG:3000002877 Bin Zhao, Yue Liu, Oliver He GI-GPx GPRP GPRP-2 GPx-2 GPx-GI GSHPX-GI GSHPx-2 WEB: http://www.ncbi.nlm.nih.gov/gene GPX2 glutathione peroxidase 2 (gastrointestinal) 2877 14q24.1 9606 14 Official from a nomenclature committee GO_0001659 (EC: IEA); GO_0002862 (EC: IEA); GO_0004602 (EC: TAS); GO_0005737 (EC: TAS, PMID: 8428933); GO_0005829 (EC: TAS); GO_0006979 (EC: IEA); GO_0009055 (EC: TAS, PMID: 8428933); GO_0009609 (EC: IEA); GO_0051702 (EC: IEA) PMID: 2388849; 8125298; 8287691; 8428933; 8833155; 9501919; 10652368; 10806356; 11368344; 11373322; 11811519; 12477932; 12674495; 12751789; 15489334; 15910762; 15923610; 16446369; 16794261; 17277236; 17937616; 18029348; 18056462; 18479189; 18483336; 18676680; 19047153; 19161995; 19170196; 19573080; 19625176; 19692168; 19773279; 19884766; 19913121; 20200426; 20628086; 20813000; 21988832; 22683372; 22758632 glutathione peroxidase 2 (gastrointestinal) Ensembl:ENSG00000176153 HGNC:4554 HPRD:11818 MIM:138319 Vega:OTTHUMG00000171677 Other designations: gastrointestinal glutathione peroxidase|glutathione peroxidase 2|glutathione peroxidase-related protein 2 GPX2 OGG:3000002908 Bin Zhao, Yue Liu, Oliver He GCCR GCR GR GRL WEB: http://www.ncbi.nlm.nih.gov/gene NR3C1 nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) 2908 5q31.3 9606 5 Official from a nomenclature committee GO_0003700 (EC: IEA); GO_0004883 (EC: IEA); GO_0005496 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10364267); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005759 (EC: TAS, PMID: 10887960); GO_0005829 (EC: IEA); GO_0006111 (EC: IEA); GO_0006351 (EC: TAS, PMID: 10887960); GO_0006355 (EC: IDA, PMID: 19141540); GO_0006366 (EC: TAS, PMID: 8621628); GO_0006367 (EC: TAS); GO_0007165 (EC: TAS, PMID: 7769088); GO_0008211 (EC: IEA); GO_0008270 (EC: IEA); GO_0010467 (EC: TAS); GO_0016020 (EC: IEA); GO_0016568 (EC: IEA); GO_0030325 (EC: IEA); GO_0031946 (EC: IEA); GO_0043525 (EC: IEA); GO_0043565 (EC: IEA); GO_0046983 (EC: IEA); GO_0060603 (EC: IEA) PMID: 1152650; 1469072; 1562545; 1612132; 1704018; 1707881; 1865905; 1958537; 2019585; 2026589; 2793174; 2867473; 3597702; 3841189; 6261922; 6266631; 6509026; 6621034; 7254211; 7264103; 7295795; 7491111; 7621901; 7659084; 7683692; 7724608; 7769088; 7796394; 7823959; 7873448; 7877627; 7887964; 8051160; 8089152; 8107808; 8125298; 8157642; 8223438; 8269959; 8288028; 8290595; 8316249; 8341706; 8349631; 8358712; 8358735; 8445027; 8449898; 8530516; 8621522; 8621628; 8645634; 8733011; 8800208; 8863343; 8878484; 8898375; 9038175; 9079630; 9089287; 9115274; 9128241; 9148915; 9150737; 9154805; 9162033; 9195923; 9199329; 9215863; 9261129; 9334248; 9334723; 9348235; 9353307; 9388192; 9426156; 9435432; 9482670; 9528750; 9584182; 9590696; 9603979; 9637764; 9649342; 9671457; 9703718; 9742105; 9817600; 9873044; 9874563; 9915858; 9920895; 9928932; 10066374; 10085091; 10187825; 10359081; 10364267; 10391209; 10430878; 10477749; 10480874; 10490647; 10508170; 10517667; 10518526; 10566686; 10567404; 10601862; 10639135; 10659697; 10688647; 10691735; 10713165; 10713182; 10731636; 10784585; 10848625; 10866662; 10887960; 10898924; 10902803; 10903152; 10903900; 10933727; 10958685; 10995388; 11005817; 11027313; 11080152; 11096094; 11101523; 11117529; 11119758; 11146632; 11152650; 11154266; 11158330; 11162542; 11229437; 11238589; 11250851; 11266503; 11279115; 11287026; 11344238; 11358809; 11358960; 11435610; 11463861; 11555652; 11562347; 11571596; 11589680; 11591700; 11673782; 11689055; 11701741; 11704662; 11708406; 11710540; 11711524; 11739747; 11751894; 11792840; 11812797; 11818365; 11873873; 11932321; 11971959; 11983486; 11996936; 12000743; 12011091; 12039077; 12039962; 12050230; 12093808; 12099703; 12114257; 12114309; 12118039; 12144530; 12145329; 12151000; 12193561; 12208951; 12225995; 12237016; 12237292; 12351458; 12351702; 12361945; 12379213; 12430185; 12444143; 12466272; 12477485; 12477932; 12487626; 12490527; 12552091; 12569182; 12581885; 12595526; 12612067; 12623935; 12634356; 12637494; 12642036; 12686538; 12711001; 12730237; 12738786; 12748280; 12754700; 12773562; 12773573; 12787894; 12805402; 12807506; 12810720; 12843156; 12864802; 12874288; 12902338; 12903052; 12917342; 12920235; 12933681; 12974633; 14521715; 14522952; 14616881; 14617768; 14634838; 14715855; 14733805; 14739255; 14749509; 14764763; 14764810; 14966297; 15016838; 15044598; 15062560; 15142377; 15159550; 15171715; 15212141; 15265776; 15265780; 15276593; 15289446; 15292341; 15372022; 15380361; 15459252; 15462611; 15489334; 15497438; 15501915; 15511603; 15521959; 15531761; 15545613; 15550679; 15557560; 15576061; 15576464; 15590693; 15591061; 15604093; 15611350; 15638722; 15657031; 15698551; 15713213; 15725353; 15746190; 15755863; 15761032; 15769988; 15770078; 15774500; 15784617; 15797250; 15826950; 15832179; 15862824; 15866175; 15870285; 15879558; 15895983; 15916966; 15919839; 15933212; 15941832; 15955845; 15956716; 16083972; 16087666; 16131566; 16134770; 16143103; 16150697; 16189295; 16192984; 16204701; 16216909; 16222046; 16236267; 16239257; 16263717; 16319314; 16362036; 16380507; 16387802; 16423881; 16429131; 16446173; 16450310; 16458268; 16469772; 16523501; 16580345; 16610949; 16610957; 16615046; 16619302; 16621324; 16624805; 16636127; 16638864; 16648810; 16676134; 16684836; 16725041; 16728546; 16740143; 16759008; 16762839; 16806572; 16806906; 16809634; 16849409; 16855182; 16888650; 16890204; 16895953; 16914312; 16971495; 16973758; 16980656; 17003263; 17043312; 17065567; 17070695; 17081986; 17116691; 17133261; 17167179; 17184882; 17185395; 17186943; 17236775; 17239375; 17242171; 17242172; 17291258; 17382897; 17387179; 17392827; 17395275; 17404046; 17407502; 17438138; 17442162; 17455211; 17460547; 17490654; 17496926; 17512111; 17517920; 17522428; 17532759; 17535992; 17540466; 17552871; 17556642; 17559307; 17563720; 17572486; 17592773; 17602195; 17633252; 17633260; 17635946; 17641689; 17681029; 17682054; 17703412; 17704997; 17716631; 17848410; 17853270; 17884810; 17937535; 17951535; 17952860; 17989362; 18028994; 18029348; 18047640; 18079322; 18086889; 18096310; 18156379; 18160712; 18165172; 18182467; 18194492; 18195193; 18219286; 18246526; 18248637; 18269582; 18286599; 18295813; 18331827; 18337589; 18343955; 18362306; 18385010; 18396779; 18398271; 18407829; 18408151; 18417736; 18468809; 18483179; 18502562; 18510611; 18511904; 18515658; 18536531; 18562626; 18583474; 18595687; 18636124; 18660489; 18663733; 18668364; 18728163; 18772142; 18789525; 18801933; 18812484; 18818748; 18822299; 18827003; 18830906; 18838498; 18838540; 18854398; 18945813; 18952539; 18958157; 18983327; 18996102; 19005987; 19007848; 19007849; 19008334; 19019335; 19051288; 19074285; 19086053; 19089807; 19095219; 19100874; 19133972; 19141540; 19146914; 19174530; 19177170; 19183974; 19188741; 19207316; 19222494; 19230884; 19234455; 19234457; 19241242; 19248771; 19258923; 19275580; 19275583; 19275585; 19282465; 19318444; 19322201; 19336230; 19336370; 19339282; 19365399; 19372434; 19373457; 19375647; 19413563; 19429432; 19435830; 19450127; 19450611; 19453261; 19458171; 19463884; 19466222; 19471022; 19484926; 19491387; 19527514; 19545546; 19548263; 19562035; 19564704; 19570036; 19578796; 19586900; 19595997; 19605973; 19621425; 19628874; 19633971; 19646928; 19673019; 19683543; 19691529; 19692572; 19723618; 19758697; 19778524; 19779205; 19782477; 19783104; 19797430; 19801529; 19805480; 19818358; 19841061; 19874574; 19875381; 19875955; 19913032; 19913121; 19940520; 19948975; 20012529; 20015838; 20015871; 20018896; 20032106; 20035271; 20036846; 20093418; 20124551; 20137628; 20140262; 20156337; 20156759; 20170710; 20195357; 20199670; 20211142; 20219685; 20308989; 20335448; 20347598; 20351714; 20371666; 20376328; 20398657; 20399565; 20403506; 20419394; 20438742; 20440229; 20446002; 20448266; 20450542; 20472303; 20484466; 20485444; 20488636; 20503287; 20543003; 20545708; 20547006; 20561560; 20584071; 20602615; 20619282; 20628086; 20634891; 20660302; 20661446; 20680430; 20697295; 20712049; 20716560; 20727199; 20731635; 20733583; 20734064; 20841450; 20843780; 20850457; 20855522; 20861124; 20885351; 21050724; 21078539; 21084380; 21093928; 21113676; 21127044; 21146942; 21147850; 21148795; 21164266; 21169818; 21190962; 21234764; 21354648; 21355091; 21419342; 21438141; 21438768; 21473041; 21474440; 21477816; 21489275; 21511880; 21521257; 21521940; 21527497; 21531081; 21633323; 21641918; 21646426; 21664385; 21693764; 21730049; 21742609; 21750107; 21760925; 21764460; 21788965; 21789663; 21803757; 21853119; 21868756; 21881570; 21883217; 21900206; 21912096; 21930780; 21945289; 21963094; 21971518; 21980503; 21984896; 21988832; 21995950; 22003412; 22008062; 22015776; 22018181; 22032841; 22048965; 22068557; 22083731; 22085474; 22088926; 22174376; 22177699; 22185489; 22205602; 22227972; 22295073; 22357529; 22366879; 22371499; 22425674; 22427805; 22441538; 22444201; 22457708; 22469783; 22487832; 22507373; 22516378; 22516993; 22533504; 22570980; 22576823; 22587663; 22587831; 22592921; 22698871; 22728713; 22771494; 22773829; 22781842; 22798432; 22801563; 22810058; 22812453; 22832351; 22846929; 22848740; 22851186; 22855579; 22863883; 22879541; 22922069; 23028665; 23033538; 23033539; 23046934; 23055001; 23055525; 23068076; 23072594; 23073785; 23123359; 23124618; 23125313; 23127816; 23132854; 23148886; 23151527; 23176645; 23178279; 23196783; 23204024; 23209664; 23212335; 23219223; 23222642; 23228967; 23239753; 23239757; 23290588; 23297131; 23307810; 23325854; 23329746; 23334186; 23355259; 23391271; 23392094; 23393177; 23426617; 23428870; 23435844; 23440419; 23449091; 23493285; 23506845; 23548248; 23566423; 23603102; 23778418; 23814048; 23820903; 23892712; 24097989; 24128430; 24186266; 24316275 nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) Ensembl:ENSG00000113580 HGNC:7978 HPRD:00679 MIM:138040 Vega:OTTHUMG00000129677 Other designations: glucocorticoid nuclear receptor variant 1|glucocorticoid receptor NR3C1 OGG:3000002918 Bin Zhao, Yue Liu, Oliver He GLUR8 GPRC1H MGLUR8 mGlu8 WEB: http://www.ncbi.nlm.nih.gov/gene GRM8 glutamate receptor, metabotropic 8 2918 7q31.3-q32.1 9606 7 Official from a nomenclature committee GO_0001642 (EC: IEA); GO_0004930 (EC: IMP, PMID: 9473604); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 9473604); GO_0007196 (EC: IMP, PMID: 9473604); GO_0007601 (EC: TAS, PMID: 9473604); GO_0007608 (EC: IEA); GO_0008066 (EC: IMP, PMID: 9473604); GO_0030818 (EC: IDA, PMID: 11166323) PMID: 8824806; 9299241; 9473604; 10216218; 11166323; 11329013; 11912074; 11943148; 12477932; 15211621; 15452121; 15489334; 16144832; 17167337; 17684544; 17955477; 17975119; 18195715; 18618593; 19023099; 19058789; 19156168; 19268276; 20009918; 20201926; 20237162; 20379614; 20398908; 20560679; 20800221; 21493956; 23420844 glutamate receptor, metabotropic 8 Ensembl:ENSG00000179603 HGNC:4600 HPRD:03071 MIM:601116 Vega:OTTHUMG00000022888 Other designations: metabotropic glutamate receptor 8 GRM8 OGG:3000002937 glutathione synthetase GSS 2729 GO_0000287 (EC: IDA, PMID: 10369661); GO_0004363 (EC: TAS); GO_0005524 (EC: IDA, PMID: 10369661); GO_0005829 (EC: TAS); GO_0006520 (EC: TAS, PMID: 8896573); GO_0006750 (EC: TAS); GO_0006805 (EC: TAS); GO_0006979 (EC: TAS, PMID: 465367); GO_0007399 (EC: TAS, PMID: 8896573); GO_0007568 (EC: IEA); GO_0016594 (EC: IEA); GO_0031667 (EC: IEA); GO_0034612 (EC: IEA); GO_0042803 (EC: IDA, PMID: 10369661); GO_0043200 (EC: IEA); GO_0043295 (EC: IDA, PMID: 10369661); GO_0044281 (EC: TAS); GO_0046686 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_1901687 (EC: TAS) PMID: 465367; 1518371; 6112263; 6137189; 7646467; 8825653; 8896573; 9215686; 9501919; 10369661; 10450861; 10652368; 10861239; 11167850; 11780052; 12477932; 12638941; 14990577; 15173170; 15489334; 15890065; 17206463; 17234469; 17503480; 17601350; 18977241; 19056867; 19111905; 19672693; 19913121; 20200426; 20413906; 20439344; 20485444; 20628086; 20800579; 20802163; 21044950; 21105962; 21139048; 21683691; 21771585; 21890473; 21906983; 21963094; 21988832; 22505724; 22863883; 22939629; 23000965; 24030972; 24250222 GSS OGG:3000002940 Bin Zhao, Yue Liu, Oliver He GSTA3-3 GTA3 WEB: http://www.ncbi.nlm.nih.gov/gene GSTA3 glutathione S-transferase alpha 3 2940 RP1-214M20.2 6p12.1 9606 6 Official from a nomenclature committee GO_0004364 (EC: ISS); GO_0005829 (EC: TAS); GO_0006749 (EC: ISS); GO_0006805 (EC: TAS); GO_0044281 (EC: TAS); GO_1901687 (EC: TAS) PMID: 8307579; 9480897; 11418619; 11872752; 12477932; 14574404; 15454730; 15489334; 15595823; 16876319; 17601350; 18426392; 18977241; 19343046; 20083122; 20200426; 20237496; 21832049; 23650189; 23824909 glutathione S-transferase alpha 3 Ensembl:ENSG00000174156 HGNC:4628 HPRD:07290 MIM:605449 Vega:OTTHUMG00000014865 Other designations: GST class-alpha member 3|S-(hydroxyalkyl)glutathione lyase A3|glutathione S-alkyltransferase A3|glutathione S-aralkyltransferase A3|glutathione S-aryltransferase A3|glutathione S-transferase A3|glutathione S-transferase A3-3 GSTA3 OGG:3000002947 Bin Zhao, Yue Liu, Oliver He GST5 GSTB GSTM3-3 GTM3 WEB: http://www.ncbi.nlm.nih.gov/gene GSTM3 glutathione S-transferase mu 3 (brain) 2947 RP4-735C1.2 1p13.3 9606 1 Official from a nomenclature committee GO_0004364 (EC: IDA, PMID: 10587441); GO_0005737 (EC: IDA, PMID: 8373352); GO_0005829 (EC: TAS); GO_0006749 (EC: IDA, PMID: 10587441); GO_0006805 (EC: TAS); GO_0008065 (EC: TAS, PMID: 2345169); GO_0018916 (EC: IDA, PMID: 8373352); GO_0019899 (EC: IPI, PMID: 8373352); GO_0042178 (EC: IDA, PMID: 8373352); GO_0042802 (EC: IPI, PMID: 16189514); GO_0042803 (EC: IDA, PMID: 9545290); GO_0042803 (EC: IPI, PMID: 8373352); GO_0043295 (EC: IDA, PMID: 8373352); GO_0043627 (EC: IEP, PMID: 10037815); GO_0044281 (EC: TAS); GO_0070458 (EC: IDA, PMID: 8373352); GO_1901687 (EC: TAS) PMID: 1530570; 2345169; 8218382; 8242618; 8317488; 8373352; 8404061; 8473333; 8824514; 9230131; 9545290; 9797707; 9882431; 10037815; 10587441; 11040079; 11081456; 11173863; 11289100; 11303592; 11408349; 11511301; 11535247; 11692073; 11740339; 11927838; 12016153; 12063626; 12359356; 12477932; 12548461; 14634838; 14735473; 14968442; 15069685; 15115915; 15338373; 15459020; 15489334; 15525789; 15621212; 15654505; 15665284; 15829318; 15914277; 16006997; 16112301; 16172217; 16189514; 16328000; 16488179; 16509765; 16598069; 16760134; 16765145; 16886896; 16985026; 17034008; 17083362; 17220350; 17259654; 17290392; 17353931; 17372252; 17449559; 17565746; 17601350; 17617661; 17716224; 17904251; 17922434; 18065725; 18177825; 18204928; 18258609; 18423940; 18447907; 18510611; 18551009; 18569590; 18668224; 18676680; 18850183; 18977241; 18990750; 18992148; 19060904; 19062541; 19074885; 19151192; 19170196; 19336475; 19339270; 19343046; 19407363; 19424794; 19486347; 19521675; 19692168; 19696791; 19751749; 19786980; 19789190; 19822571; 19856098; 19860743; 19898482; 19913121; 19922706; 20029944; 20032816; 20131310; 20136364; 20200426; 20237496; 20391138; 20391338; 20437850; 20461808; 20485444; 20549140; 20577141; 20628086; 20634891; 20661821; 20819778; 20847076; 20970553; 21072184; 21139048; 21513434; 21800051; 21890473; 21900206; 21963094; 21987572; 22178446; 22360420; 22505724; 22976281; 23000965; 23036584; 23077236; 23167362; 23576398; 23824909; 24250222 glutathione S-transferase mu 3 (brain) Ensembl:ENSG00000134202 HGNC:4635 HPRD:00712 MIM:138390 Other designations: GST class-mu 3|S-(hydroxyalkyl)glutathione lyase M3|brain GST|brain type mu-glutathione S-transferase|glutathione S-alkyltransferase M3|glutathione S-aralkyltransferase M3|glutathione S-aryltransferase M3|glutathione S-transferase M3 (brain)|glutathione S-transferase Mu 3|glutathione S-transferase, Mu-3|hGSTM3-3 GSTM3 OGG:3000003021 Bin Zhao, Yue Liu, Oliver He H3.3B WEB: http://www.ncbi.nlm.nih.gov/gene H3F3B H3 histone, family 3B (H3.3B) 3021 17q25.1 9606 17 Official from a nomenclature committee GO_0000786 (EC: IEA); GO_0003677 (EC: IEA); GO_0005515 (EC: IPI, PMID: 19494831); GO_0005576 (EC: TAS); GO_0005654 (EC: TAS); GO_0006334 (EC: IEA); GO_0007420 (EC: IEA); GO_0007596 (EC: TAS); GO_0009725 (EC: IEA); GO_0046982 (EC: IEA); GO_0070062 (EC: IDA) PMID: 1748304; 7557364; 8586426; 8889548; 9188772; 9334241; 9566873; 9731536; 10096020; 11076863; 11080476; 11230166; 11278789; 11591653; 11689053; 11751582; 12477932; 12909349; 14527345; 14657027; 14702039; 15489336; 15616580; 15664198; 15674325; 16189514; 16381901; 16728976; 17620599; 18029348; 18760861; 19494831; 20110566; 20504901; 22174317; 22505724; 22623428; 23463506; 24162739 H3 histone, family 3B (H3.3B) Ensembl:ENSG00000132475 HGNC:4765 HPRD:03036 MIM:601058 Vega:OTTHUMG00000179842 Other designations: H3 histone, family 3A|histone H3.3 H3F3B OGG:3000003032 Bin Zhao, Yue Liu, Oliver He ECHB MTPB TP-BETA WEB: http://www.ncbi.nlm.nih.gov/gene HADHB hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), beta subunit 3032 MSTP029 2p23 9606 2 Official from a nomenclature committee GO_0000062 (EC: IEA); GO_0003857 (EC: TAS, PMID: 1550553); GO_0003988 (EC: IEA); GO_0004300 (EC: IEA); GO_0005515 (EC: IPI); GO_0005739 (EC: NAS, PMID: 7958339); GO_0005740 (EC: TAS, PMID: 1550553); GO_0005741 (EC: IDA); GO_0005743 (EC: IDA); GO_0005743 (EC: TAS); GO_0005783 (EC: IDA); GO_0006635 (EC: IEA); GO_0006635 (EC: TAS); GO_0006644 (EC: TAS); GO_0016507 (EC: IEA); GO_0016508 (EC: IEA); GO_0016509 (EC: IEA); GO_0032403 (EC: IEA); GO_0035965 (EC: TAS); GO_0042645 (EC: IDA, PMID: 18063578); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0044822 (EC: IDA); GO_0046474 (EC: TAS); GO_0051287 (EC: IEA) PMID: 1550553; 7958339; 8135828; 8163672; 8651282; 8921383; 9259266; 9605857; 9739053; 10075708; 11430884; 12477932; 12665801; 12721663; 12754706; 12933794; 14630990; 14702039; 15242332; 15489334; 15815621; 16196087; 16344560; 17199921; 17314511; 18063578; 19699128; 20305087; 20360068; 20562859; 20825197; 20877624; 21139048; 21319273; 21549624; 21565611; 21853274; 21890473; 21900206; 21988832; 22000755; 22079093; 22190034; 22268729; 22304920; 22375075; 22939629; 22952844; 23000159; 23398456; 23455922; 23798571; 24244333; 24255178 hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), beta subunit Ensembl:ENSG00000138029 HGNC:4803 HPRD:00887 MIM:143450 Vega:OTTHUMG00000096978 Other designations: 2-enoyl-Coenzyme A (CoA) hydratase, beta subunit|3-ketoacyl-Coenzyme A (CoA) thiolase of mitochondrial trifunctional protein, beta subunit|acetyl-CoA acyltransferase|beta-ketothiolase|hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional protein), beta subunit|trifunctional enzyme subunit beta, mitochondrial HADHB OGG:3000003055 Bin Zhao, Yue Liu, Oliver He JTK9 p59Hck p61Hck WEB: http://www.ncbi.nlm.nih.gov/gene HCK hemopoietic cell kinase 3055 RP5-836N17.3 20q11-q12 9606 20 Official from a nomenclature committee GO_0002522 (EC: TAS, PMID: 18538446); GO_0002758 (EC: TAS, PMID: 18538446); GO_0004713 (EC: IMP, PMID: 10092522); GO_0004715 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11278465); GO_0005524 (EC: IEA); GO_0005634 (EC: IEA); GO_0005764 (EC: IDA, PMID: 15998323); GO_0005794 (EC: IEA); GO_0005829 (EC: TAS); GO_0005884 (EC: IDA, Qualifier: colocalizes_with, PMID: 15998323); GO_0005901 (EC: IDA, PMID: 7791757); GO_0005925 (EC: IMP, PMID: 11904303); GO_0006468 (EC: TAS, PMID: 3496523); GO_0006954 (EC: IEA); GO_0007155 (EC: TAS, PMID: 18538446); GO_0007229 (EC: TAS, PMID: 18538446); GO_0007498 (EC: TAS, PMID: 3453117); GO_0008284 (EC: IMP, PMID: 10092522); GO_0008360 (EC: IMP, PMID: 10092522); GO_0016032 (EC: TAS); GO_0018108 (EC: IMP, PMID: 10092522); GO_0019221 (EC: TAS, PMID: 18538446); GO_0030133 (EC: IEA); GO_0030838 (EC: TAS, PMID: 18538446); GO_0031234 (EC: IMP, PMID: 11904303); GO_0031663 (EC: TAS, PMID: 18538446); GO_0038096 (EC: TAS); GO_0042995 (EC: IEA); GO_0043066 (EC: IMP, PMID: 17535448); GO_0043299 (EC: TAS, PMID: 18538446); GO_0045087 (EC: TAS); GO_0045728 (EC: TAS, PMID: 18538446); GO_0046777 (EC: IMP, PMID: 10092522); GO_0050690 (EC: TAS); GO_0050727 (EC: TAS, PMID: 18538446); GO_0050764 (EC: IMP, PMID: 11904303); GO_0051090 (EC: IMP, PMID: 17535448); GO_0060333 (EC: TAS, PMID: 18538446); GO_0071801 (EC: IDA, PMID: 15998323); GO_2000251 (EC: IDA, PMID: 15998323); GO_2000251 (EC: IMP, PMID: 11904303) PMID: 1373873; 1572549; 1689310; 1720539; 1875927; 3453117; 3496523; 7588629; 7682059; 7782336; 7791757; 7859737; 8058772; 8064233; 8125298; 8599760; 8626374; 8657103; 8885868; 8955135; 8995358; 9020138; 9024658; 9109402; 9178913; 9195918; 9218412; 9268059; 9400828; 9407116; 9571048; 9656992; 9705913; 9742969; 9778343; 9790917; 9837776; 9890970; 10068673; 10092522; 10318861; 10364375; 10388555; 10428862; 10527858; 10544125; 10547288; 10574946; 10586033; 10642173; 10749872; 10799548; 10849448; 10858437; 10918587; 10934191; 10967098; 10973280; 11071635; 11097855; 11239464; 11278465; 11294897; 11328823; 11350938; 11448168; 11463741; 11500821; 11533201; 11689697; 11741929; 11780052; 11896602; 11904303; 11940572; 11976726; 11994282; 12029088; 12033791; 12076760; 12138090; 12181444; 12235133; 12244095; 12477932; 12496276; 12522270; 12538589; 12576423; 12592324; 12600646; 12626508; 12734187; 12734410; 12748290; 12769846; 12900520; 14506255; 14551197; 14551213; 14702039; 14969582; 14993658; 15010462; 15078178; 15144186; 15263807; 15489334; 15491611; 15595833; 15626739; 15638726; 15707590; 15784897; 15952790; 15998323; 16169070; 16210316; 16271895; 16273093; 16344560; 16374509; 16454711; 16849330; 16964398; 17024369; 17081983; 17141806; 17535448; 17668209; 17868192; 17893228; 18005690; 18042718; 18067320; 18538446; 18794796; 19149577; 19211505; 19234535; 19585521; 19807124; 19807924; 20056178; 20181660; 20488787; 20670214; 20702582; 20798061; 20810664; 20936779; 21309750; 21365684; 21477083; 21567396; 21625496; 21696586; 21738584; 21763503; 21832049; 21878628; 21886773; 21890473; 21988832; 21993313; 22021612; 22110726; 22185326; 22345475; 22364282; 22393415; 22537596; 22623531; 22641034; 22651890; 22745667; 22939624; 22974441; 23128233; 23439650; 23896410; 24051604 hemopoietic cell kinase Ensembl:ENSG00000101336 HGNC:4840 HPRD:00796 MIM:142370 Vega:OTTHUMG00000032204 Other designations: hematopoietic cell kinase|p59-HCK/p60-HCK|tyrosine-protein kinase HCK HCK OGG:3000003084 Bin Zhao, Yue Liu, Oliver He ARIA GGF GGF2 HGL HRG HRG1 HRGA MST131 NDF SMDF WEB: http://www.ncbi.nlm.nih.gov/gene NRG1 neuregulin 1 3084 8p12 9606 8 Official from a nomenclature committee GO_0000165 (EC: IEA); GO_0000902 (EC: IEA); GO_0003161 (EC: IEA); GO_0003222 (EC: IDA, PMID: 17336907); GO_0003712 (EC: IDA, PMID: 15073182); GO_0005102 (EC: IPI, PMID: 7514177); GO_0005125 (EC: TAS, PMID: 10372964); GO_0005176 (EC: IEA); GO_0005515 (EC: IPI, PMID: 7592681); GO_0005576 (EC: NAS, PMID: 1348215); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 11389077); GO_0005634 (EC: IEA); GO_0005737 (EC: IEA); GO_0005887 (EC: IEA); GO_0007154 (EC: TAS, PMID: 17432114); GO_0007169 (EC: IDA, PMID: 7514177); GO_0007171 (EC: IDA, PMID: 9553078); GO_0007171 (EC: NAS, PMID: 1348215); GO_0007173 (EC: TAS); GO_0007399 (EC: TAS, PMID: 17432114); GO_0007416 (EC: IEA); GO_0007422 (EC: IEA); GO_0007626 (EC: IEA); GO_0008083 (EC: IDA, PMID: 11389077); GO_0008083 (EC: NAS, PMID: 8096067); GO_0008283 (EC: IDA, PMID: 11389077); GO_0008543 (EC: TAS); GO_0009790 (EC: IEA); GO_0010667 (EC: IDA, PMID: 9553078); GO_0014032 (EC: TAS, PMID: 17432114); GO_0016020 (EC: NAS, PMID: 8096067); GO_0016324 (EC: IDA, PMID: 12646923); GO_0016477 (EC: IEA); GO_0021781 (EC: IEA); GO_0030296 (EC: IDA, PMID: 7556068); GO_0030297 (EC: IC, PMID: 9553078); GO_0030297 (EC: NAS, PMID: 1348215); GO_0030307 (EC: IDA, PMID: 9553078); GO_0030424 (EC: IEA); GO_0030879 (EC: TAS, PMID: 17432114); GO_0030971 (EC: NAS, PMID: 1348215); GO_0031594 (EC: IEA); GO_0038095 (EC: TAS); GO_0038127 (EC: IDA, PMID: 11389077); GO_0042060 (EC: IDA, PMID: 12646923); GO_0042060 (EC: TAS, PMID: 16412517); GO_0042177 (EC: IEA); GO_0043125 (EC: IDA, PMID: 7556068); GO_0043125 (EC: IPI, PMID: 11389077); GO_0043496 (EC: TAS, PMID: 16412517); GO_0043497 (EC: IDA, PMID: 10559227); GO_0043624 (EC: IGI, PMID: 15155732); GO_0045087 (EC: TAS); GO_0045213 (EC: IEA); GO_0045785 (EC: IDA, PMID: 7556068); GO_0045892 (EC: IDA, PMID: 15073182); GO_0046579 (EC: IEA); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0048663 (EC: IEA); GO_0051048 (EC: IDA, PMID: 10559227); GO_0051155 (EC: ISS); GO_0051897 (EC: IEA); GO_0055007 (EC: ISS); GO_0055012 (EC: IDA, PMID: 9553078); GO_0060045 (EC: IDA, PMID: 9553078); GO_0060379 (EC: IDA, PMID: 17336907); GO_0060956 (EC: IDA, PMID: 17336907); GO_0061098 (EC: IDA, PMID: 7556068); GO_2001240 (EC: IDA, PMID: 9553078) PMID: 1348215; 1350381; 7509448; 7514177; 7556068; 7592681; 7689552; 7721889; 7730382; 7782315; 7876250; 7903175; 8062828; 8095334; 8096067; 8125298; 8325659; 8702572; 9168114; 9168115; 9333014; 9342050; 9553078; 9565587; 9685409; 10372964; 10523851; 10537356; 10559227; 10585499; 10597312; 11116142; 11389077; 11555649; 11896060; 12082616; 12145742; 12204892; 12471041; 12477932; 12478479; 12509456; 12528817; 12556556; 12600989; 12646923; 12768307; 12800145; 12808428; 12874607; 14569272; 14632199; 14647391; 14699424; 14702039; 14729827; 14966480; 15007393; 15073182; 15155732; 15159416; 15162166; 15197397; 15219675; 15248869; 15276238; 15303101; 15326116; 15466169; 15489334; 15494726; 15498868; 15527969; 15538186; 15545978; 15584912; 15609326; 15645137; 15703820; 15897877; 15939841; 16082692; 16155362; 16158055; 16189508; 16219117; 16219118; 16249994; 16287046; 16326006; 16344560; 16412517; 16428439; 16442083; 16446404; 16470843; 16483744; 16520822; 16526041; 16618933; 16638076; 16687441; 16690615; 16730337; 16767099; 16825199; 16867224; 16868568; 16891421; 16940976; 17033632; 17072305; 17214955; 17275115; 17300918; 17336907; 17336946; 17366345; 17405926; 17408693; 17432114; 17447867; 17499242; 17503451; 17519028; 17562386; 17565985; 17598910; 17602072; 17631867; 17652086; 17884806; 17901998; 17903296; 17925794; 17941827; 17962208; 18032396; 18159252; 18180429; 18193072; 18198266; 18234478; 18255317; 18282690; 18286587; 18291420; 18395550; 18455303; 18455369; 18466879; 18466881; 18470533; 18494263; 18494554; 18497096; 18516516; 18543275; 18571900; 18583979; 18584117; 18585932; 18606232; 18668031; 18704261; 18714568; 18728681; 18798975; 18799465; 18806920; 19054571; 19058791; 19086053; 19127563; 19148499; 19150438; 19156152; 19184335; 19196962; 19199244; 19229203; 19269083; 19306381; 19328558; 19339916; 19350564; 19367581; 19367584; 19394386; 19439994; 19448847; 19449332; 19497323; 19521112; 19545856; 19556605; 19569180; 19573260; 19575259; 19594860; 19597049; 19626024; 19644050; 19652122; 19659570; 19733651; 19736351; 19782967; 19797898; 19801490; 19802002; 19913121; 19913623; 19937977; 19965935; 19967439; 20036336; 20061032; 20102668; 20182055; 20215529; 20218976; 20227043; 20371257; 20374152; 20379614; 20427670; 20435087; 20472376; 20497232; 20520724; 20526724; 20580130; 20582876; 20625696; 20628086; 20638435; 20671236; 20682778; 20736300; 20800603; 20921115; 20926259; 20927045; 20978455; 21035784; 21041608; 21057508; 21127983; 21234898; 21239627; 21246584; 21247898; 21283760; 21368034; 21371516; 21437657; 21467033; 21512575; 21546767; 21555713; 21576249; 21653853; 21706185; 21716252; 21745728; 21792199; 21840482; 21858616; 21865659; 21965611; 22019858; 22027878; 22042562; 22052506; 22158511; 22183611; 22200588; 22209534; 22216327; 22226049; 22226548; 22249266; 22249457; 22267200; 22350758; 22377709; 22378022; 22378872; 22414959; 22425775; 22467496; 22494484; 22504067; 22520967; 22563075; 22574178; 22590542; 22613991; 22739235; 22790889; 22832904; 22886427; 22891299; 22944276; 22968213; 22974608; 22999558; 23032943; 23035098; 23104879; 23148218; 23213231; 23247143; 23253390; 23301017; 23308187; 23328545; 23360725; 23399902; 23400839; 23408906; 23468880; 23480537; 23489597; 23524320; 23572145; 23590603; 23625463; 23632455; 23739962; 23870195; 23934736; 23937725; 24097984; 24112719 neuregulin 1 Ensembl:ENSG00000157168 HGNC:7997 HPRD:00802 MIM:142445 Vega:OTTHUMG00000163918 Other designations: MSTP131|glial growth factor|heregulin, alpha (45kD, ERBB2 p185-activator)|neu differentiation factor|neuregulin 1 type IV beta 1a|neuregulin 1 type IV beta 3|pro-NRG1|pro-neuregulin-1, membrane-bound isoform|sensory and motor neuron derived factor NRG1 OGG:3000003091 Bin Zhao, Yue Liu, Oliver He HIF-1A HIF-1alpha HIF1 HIF1-ALPHA MOP1 PASD8 bHLHe78 WEB: http://www.ncbi.nlm.nih.gov/gene HIF1A hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor) 3091 14q23.2 20140408 9606 14 protein-coding Official from a nomenclature committee GO_0000989 (EC: IDA); GO_0001076 (EC: IEA); GO_0001077 (EC: IEA); GO_0001525 (EC: IEA); GO_0001666 (EC: IDA, PMID: 11782478); GO_0001666 (EC: IMP, PMID: 12411310); GO_0001755 (EC: IEA); GO_0001837 (EC: ISS, PMID: 18037992); GO_0001892 (EC: IEA); GO_0001922 (EC: IEA); GO_0001938 (EC: IC, PMID: 8756616); GO_0001947 (EC: IEA); GO_0002052 (EC: IEA); GO_0002248 (EC: ISS, PMID: 18037992); GO_0003151 (EC: IEA); GO_0003208 (EC: IEA); GO_0003700 (EC: IDA, PMID: 11782478); GO_0003700 (EC: TAS, PMID: 15261140); GO_0003705 (EC: IDA, PMID: 8387214); GO_0003705 (EC: IDA, Qualifier: contributes_to, PMID: 7539918); GO_0004871 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12004076); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005667 (EC: IPI, PMID: 9576906); GO_0005730 (EC: IDA); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006089 (EC: IEA); GO_0006355 (EC: IDA, PMID: 11782478); GO_0006879 (EC: IEA); GO_0007165 (EC: IMP, PMID: 12411310); GO_0007219 (EC: TAS); GO_0007595 (EC: IEA); GO_0008134 (EC: IPI, PMID: 7539918); GO_0008542 (EC: IEA); GO_0010468 (EC: IDA, PMID: 18419598); GO_0010573 (EC: IDA, PMID: 12958148); GO_0010575 (EC: IDA, PMID: 8756616); GO_0010575 (EC: IMP, PMID: 18658046); GO_0010634 (EC: ISS, PMID: 18037992); GO_0010870 (EC: IMP, PMID: 17178876); GO_0014850 (EC: IEA); GO_0019896 (EC: IMP, PMID: 19528298); GO_0019899 (EC: IPI, PMID: 11641274); GO_0019901 (EC: IPI); GO_0021502 (EC: IEA); GO_0021987 (EC: IEA); GO_0030502 (EC: IEA); GO_0030949 (EC: IC, PMID: 12958148); GO_0031514 (EC: IEA); GO_0031625 (EC: IPI, PMID: 11641274); GO_0032007 (EC: IEA); GO_0032364 (EC: IDA, PMID: 16956324); GO_0032722 (EC: TAS, PMID: 18370914); GO_0032909 (EC: IMP, PMID: 12411310); GO_0032963 (EC: ISS, PMID: 18037992); GO_0035035 (EC: IPI, PMID: 15261140); GO_0035162 (EC: IEA); GO_0035257 (EC: IPI, PMID: 18658046); GO_0035774 (EC: IEA); GO_0042541 (EC: IEA); GO_0042593 (EC: IEA); GO_0042789 (EC: IC, PMID: 7539918); GO_0042826 (EC: IEA); GO_0043524 (EC: IEA); GO_0043565 (EC: IDA, Qualifier: contributes_to, PMID: 7539918); GO_0043619 (EC: IDA, PMID: 8089148); GO_0044212 (EC: IDA); GO_0045648 (EC: IC, PMID: 1448077); GO_0045766 (EC: IC, PMID: 8756616); GO_0045821 (EC: IC, PMID: 8089148); GO_0045893 (EC: IDA, PMID: 8089148); GO_0045893 (EC: IMP); GO_0045926 (EC: IEA); GO_0045944 (EC: IDA, PMID: 11573933); GO_0045944 (EC: IGI, PMID: 17981124); GO_0046716 (EC: IEA); GO_0046886 (EC: IDA, PMID: 1448077); GO_0046982 (EC: IPI, PMID: 12239177); GO_0046982 (EC: TAS, PMID: 15261140); GO_0048546 (EC: IEA); GO_0051000 (EC: TAS, PMID: 18254728); GO_0051216 (EC: IEA); GO_0051541 (EC: ISS, PMID: 18037992); GO_0051879 (EC: IDA, PMID: 9079689); GO_0060574 (EC: IEA); GO_0061030 (EC: IEA); GO_0061298 (EC: IEA); GO_0061418 (EC: TAS); GO_0061419 (EC: IDA); GO_0061419 (EC: IMP, PMID: 19652095); GO_0070101 (EC: IC, PMID: 17178876); GO_0070244 (EC: IEA); GO_0071347 (EC: IEP, PMID: 12958148); GO_0071456 (EC: IDA, PMID: 11573933); GO_0071456 (EC: IEP); GO_0071456 (EC: TAS); GO_0071542 (EC: IEA); GO_2001054 (EC: IEA) PMID: 1448077; 7539918; 7836384; 8089148; 8107114; 8387214; 8663540; 8753788; 8756616; 8786149; 8816435; 8927054; 9079689; 9235919; 9537326; 9576906; 9653127; 9704006; 9782081; 9822602; 9828130; 9887100; 9923855; 10202154; 10353251; 10425220; 10551817; 10594042; 10640274; 10702253; 10758161; 10777486; 10823831; 10878807; 10903152; 10906065; 10944113; 10950862; 10961998; 10973499; 11006129; 11024059; 11089639; 11226425; 11278891; 11292861; 11292862; 11331613; 11358837; 11382768; 11389899; 11486006; 11504942; 11566883; 11573933; 11593383; 11598268; 11641274; 11707426; 11726537; 11734856; 11739718; 11782478; 11823643; 11852072; 11861398; 11865071; 11868612; 11886167; 11940656; 11943784; 11959977; 11959990; 11971899; 11980639; 11986208; 11992540; 12004076; 12016145; 12042299; 12050673; 12062197; 12080085; 12084725; 12086861; 12099689; 12114320; 12123724; 12124396; 12136249; 12149254; 12154057; 12202863; 12205091; 12207089; 12209691; 12213597; 12213806; 12215445; 12228247; 12237125; 12239177; 12242281; 12296651; 12351678; 12376345; 12401798; 12411310; 12446723; 12451989; 12464182; 12468553; 12477932; 12482756; 12482858; 12485908; 12485909; 12488445; 12538644; 12560087; 12586627; 12586829; 12588875; 12606543; 12606552; 12632503; 12651620; 12670503; 12673675; 12682018; 12697836; 12727858; 12743597; 12761217; 12764143; 12778114; 12781449; 12808024; 12810083; 12821113; 12823854; 12855680; 12858534; 12865501; 12871382; 12876287; 12883692; 12885785; 12900407; 12912907; 12914933; 12914934; 12919954; 12925778; 12937141; 12944107; 12958148; 12966423; 14512791; 14521712; 14523474; 14556007; 14559790; 14600153; 14636255; 14638687; 14645546; 14657004; 14662854; 14671307; 14672622; 14680803; 14680833; 14681237; 14691445; 14699081; 14702039; 14712484; 14726529; 14729605; 14734545; 14742449; 14744756; 14744852; 14757845; 14981919; 15024076; 15024078; 15031145; 15060148; 15062033; 15064771; 15071503; 15082527; 15082785; 15084243; 15084514; 15111179; 15135259; 15135470; 15146197; 15147973; 15154850; 15155569; 15156561; 15160341; 15169887; 15170665; 15175080; 15191555; 15199114; 15199132; 15199161; 15217953; 15240510; 15240563; 15247232; 15252039; 15261140; 15280364; 15280370; 15319539; 15322093; 15328163; 15331549; 15342390; 15342781; 15347669; 15350301; 15374877; 15382039; 15385570; 15388333; 15465032; 15466858; 15474027; 15474452; 15475194; 15479785; 15485863; 15489334; 15489637; 15492789; 15538748; 15543236; 15556623; 15561954; 15598682; 15598882; 15611046; 15611064; 15615775; 15623945; 15629713; 15652751; 15656883; 15665520; 15669079; 15674338; 15696961; 15709180; 15718424; 15721254; 15735682; 15741220; 15750626; 15770733; 15776016; 15780936; 15805230; 15805242; 15809750; 15811877; 15814637; 15831177; 15832512; 15838297; 15838334; 15850830; 15862159; 15862307; 15864753; 15876874; 15878343; 15897903; 15902299; 15935515; 15947089; 15962286; 15964822; 15967109; 15970466; 15978586; 15983061; 15987493; 15987702; 15994306; 16005427; 16007214; 16011198; 16035955; 16046581; 16100168; 16109785; 16110315; 16136272; 16136514; 16139409; 16140212; 16142350; 16144691; 16149050; 16157596; 16161047; 16168127; 16170370; 16189514; 16195397; 16205110; 16208522; 16227395; 16229017; 16229182; 16242072; 16246222; 16253768; 16261165; 16263938; 16278378; 16278385; 16284786; 16288478; 16288748; 16304044; 16331995; 16337862; 16338068; 16341243; 16344560; 16396931; 16407130; 16407835; 16408279; 16421254; 16424018; 16438736; 16452478; 16482104; 16490744; 16506055; 16507982; 16511565; 16515634; 16516166; 16516853; 16533170; 16543236; 16543242; 16543245; 16552335; 16554418; 16555123; 16579968; 16596228; 16611863; 16612574; 16627691; 16629644; 16631533; 16638120; 16682946; 16721291; 16735500; 16736613; 16738327; 16756955; 16760477; 16768548; 16769565; 16775626; 16775835; 16777103; 16779673; 16815840; 16826425; 16826581; 16828081; 16837101; 16847054; 16849522; 16854377; 16865676; 16871792; 16873253; 16883594; 16885164; 16890383; 16899596; 16899602; 16901993; 16920734; 16937436; 16951198; 16951228; 16954218; 16956324; 16969516; 16970912; 16979927; 16998808; 17010341; 17015263; 17015745; 17024177; 17043658; 17045016; 17047048; 17055760; 17060326; 17060462; 17066447; 17067582; 17075581; 17077301; 17097563; 17097641; 17102128; 17102633; 17132228; 17135241; 17143338; 17178876; 17179985; 17189520; 17220880; 17236590; 17237281; 17244529; 17245699; 17268888; 17273746; 17289019; 17289897; 17290185; 17292638; 17294729; 17307335; 17310851; 17320759; 17325032; 17335808; 17336340; 17339318; 17343848; 17360382; 17362638; 17376295; 17382205; 17382325; 17387384; 17400550; 17403672; 17404022; 17407091; 17418410; 17418790; 17418979; 17426247; 17426252; 17437013; 17438103; 17439941; 17442277; 17442736; 17445471; 17451682; 17452775; 17458899; 17461470; 17473988; 17474992; 17477366; 17482131; 17487356; 17488873; 17490410; 17495954; 17502379; 17507435; 17511040; 17519536; 17519789; 17525282; 17532031; 17536453; 17544543; 17545054; 17555795; 17558023; 17562539; 17562866; 17563752; 17568584; 17570486; 17591803; 17592963; 17595907; 17597020; 17606258; 17617866; 17624927; 17634230; 17637739; 17640715; 17650819; 17653093; 17662481; 17666400; 17674038; 17676480; 17684492; 17713282; 17714861; 17718430; 17721610; 17725546; 17726031; 17785433; 17805961; 17822384; 17826745; 17828303; 17848618; 17852557; 17875644; 17881647; 17889387; 17891484; 17893997; 17898080; 17903293; 17916562; 17927572; 17932327; 17938407; 17942596; 17947829; 17956732; 17965024; 17967865; 17967866; 17967880; 17973296; 17978497; 17981124; 17982282; 17984117; 17986458; 17989922; 17990984; 17999410; 18000826; 18006690; 18021370; 18024476; 18024825; 18025805; 18029348; 18030615; 18031949; 18035072; 18037992; 18047470; 18050215; 18050252; 18055454; 18060642; 18062281; 18065728; 18081507; 18083891; 18094421; 18097583; 18154573; 18159247; 18160046; 18163427; 18166158; 18172210; 18172309; 18172354; 18178340; 18184809; 18184961; 18199003; 18209490; 18221327; 18222538; 18225753; 18239067; 18240292; 18246800; 18250065; 18254728; 18256363; 18258605; 18264140; 18269201; 18279708; 18290322; 18292935; 18294451; 18295594; 18297062; 18299578; 18305400; 18307947; 18307948; 18309031; 18313384; 18314489; 18315897; 18323857; 18325389; 18339685; 18342368; 18347341; 18351386; 18354193; 18362831; 18365547; 18370914; 18370960; 18376310; 18381294; 18381358; 18384112; 18385176; 18393939; 18398039; 18411415; 18413745; 18418234; 18419598; 18422279; 18422749; 18424433; 18424783; 18426857; 18440561; 18447926; 18452596; 18459144; 18462799; 18465238; 18473128; 18476562; 18476629; 18476949; 18484090; 18493321; 18506785; 18521687; 18528739; 18533565; 18538669; 18546529; 18551130; 18554951; 18561315; 18563339; 18563715; 18570733; 18574470; 18588890; 18592007; 18593917; 18595517; 18606657; 18617693; 18619649; 18621534; 18630523; 18632605; 18638657; 18641302; 18644974; 18648372; 18655183; 18658046; 18687685; 18694926; 18703592; 18704463; 18713068; 18713836; 18718909; 18720385; 18727515; 18728026; 18762723; 18763582; 18772337; 18775313; 18779379; 18780286; 18781797; 18784753; 18785001; 18787502; 18790175; 18790176; 18792019; 18799519; 18813785; 18832593; 18834862; 18835464; 18835792; 18838541; 18841476; 18842833; 18844219; 18922940; 18927085; 18936210; 18936945; 18945681; 18945963; 18949419; 18950958; 18979225; 18980686; 18983642; 18984585; 18985005; 18987249; 18996102; 18996491; 18998488; 19007879; 19016246; 19016766; 19018165; 19018560; 19021062; 19028277; 19028544; 19028566; 19030186; 19030229; 19046997; 19048182; 19054610; 19057015; 19061835; 19071119; 19074848; 19077164; 19077391; 19080330; 19091459; 19096126; 19096962; 19097132; 19097995; 19098000; 19105964; 19106642; 19107364; 19109240; 19121088; 19123465; 19123984; 19128456; 19130303; 19132225; 19141292; 19142800; 19147576; 19147752; 19147754; 19151763; 19165496; 19168635; 19172095; 19176596; 19179292; 19179443; 19180921; 19183269; 19184477; 19188659; 19188818; 19204000; 19211554; 19211927; 19212630; 19212642; 19223463; 19223895; 19235921; 19238077; 19240858; 19244104; 19251694; 19252526; 19254160; 19254710; 19255431; 19265035; 19266161; 19268443; 19279559; 19287200; 19287962; 19293442; 19302703; 19303436; 19303878; 19304911; 19306159; 19307182; 19321184; 19335985; 19336661; 19347037; 19359588; 19360424; 19362550; 19381167; 19383558; 19386601; 19390242; 19401150; 19403384; 19406746; 19411751; 19414801; 19417024; 19419319; 19423615; 19435875; 19436307; 19445542; 19447872; 19449077; 19456861; 19458911; 19470762; 19484260; 19484991; 19487287; 19489936; 19491109; 19492421; 19502554; 19504235; 19524065; 19528298; 19529947; 19541609; 19546348; 19549358; 19549898; 19549990; 19552765; 19558170; 19558833; 19563493; 19575963; 19580347; 19580810; 19589398; 19589782; 19590529; 19602039; 19602254; 19602906; 19604478; 19620043; 19637235; 19640849; 19648120; 19651758; 19652095; 19657231; 19660915; 19668230; 19671674; 19671685; 19671876; 19676145; 19680224; 19691832; 19694616; 19696166; 19707816; 19712049; 19714248; 19717330; 19720740; 19723043; 19724277; 19724845; 19726677; 19727403; 19738058; 19742344; 19760195; 19763399; 19766100; 19768395; 19768695; 19779103; 19779281; 19782034; 19782666; 19786016; 19788888; 19789263; 19790048; 19790065; 19801454; 19801684; 19802003; 19802386; 19804771; 19808899; 19813243; 19819950; 19828020; 19834107; 19837381; 19838207; 19841637; 19841638; 19845827; 19846525; 19858293; 19880520; 19880525; 19887373; 19892848; 19893619; 19898961; 19901273; 19903792; 19913121; 19914104; 19915370; 19919679; 19919690; 19934275; 19940151; 19940550; 19948069; 19949104; 19954019; 19957875; 19958256; 19962963; 19995553; 19996311; 20001745; 20001759; 20003271; 20005538; 20007689; 20011601; 20018172; 20019845; 20020496; 20021862; 20021945; 20026589; 20026874; 20028790; 20028863; 20032301; 20032376; 20035632; 20036816; 20037203; 20039880; 20042684; 20049704; 20059631; 20075985; 20078552; 20097172; 20104680; 20105288; 20109337; 20110409; 20117921; 20123452; 20127031; 20136501; 20137122; 20139176; 20140681; 20145132; 20149310; 20150769; 20154717; 20154724; 20158574; 20164027; 20165885; 20166137; 20169663; 20174965; 20184881; 20194722; 20194889; 20197612; 20198320; 20204822; 20206160; 20217131; 20228066; 20232298; 20232316; 20237132; 20299614; 20300531; 20303950; 20307196; 20308562; 20346360; 20347035; 20347817; 20348876; 20363910; 20368331; 20374513; 20380593; 20383692; 20388348; 20389299; 20392253; 20392254; 20393480; 20398057; 20398289; 20403915; 20407014; 20412701; 20414936; 20416395; 20427288; 20427344; 20427574; 20427666; 20429620; 20453000; 20453713; 20459575; 20470445; 20473281; 20478051; 20496369; 20498255; 20501388; 20501419; 20509143; 20513003; 20514449; 20514457; 20515450; 20525878; 20526373; 20526721; 20538960; 20540786; 20544685; 20556580; 20556833; 20559021; 20559438; 20561442; 20562128; 20562859; 20569445; 20572162; 20574527; 20581113; 20596750; 20596845; 20599538; 20602615; 20603076; 20603618; 20620956; 20624301; 20624928; 20627616; 20628086; 20628624; 20631377; 20631454; 20634891; 20635169; 20644561; 20644645; 20648588; 20651398; 20651983; 20656543; 20659427; 20661221; 20661259; 20661931; 20663134; 20667978; 20668552; 20669661; 20675386; 20678440; 20691219; 20706634; 20711226; 20713124; 20716529; 20723413; 20724477; 20727020; 20729179; 20800603; 20807755; 20811474; 20813154; 20827750; 20832699; 20838824; 20844082; 20845004; 20848794; 20857420; 20864819; 20871160; 20876310; 20885442; 20888814; 20888838; 20889502; 20924188; 20924210; 20926496; 20931543; 20932296; 20932347; 20937289; 20938207; 20943999; 20952631; 20952681; 20953377; 20962622; 20964835; 20965423; 20970309; 20972335; 20977846; 20977930; 20978319; 21037926; 21042279; 21042761; 21042786; 21050481; 21057546; 21059659; 21059928; 21061787; 21069452; 21073615; 21073737; 21075472; 21085474; 21090098; 21092233; 21095582; 21109953; 21118962; 21124777; 21139048; 21143841; 21148070; 21156006; 21162194; 21163055; 21167768; 21176961; 21179202; 21182205; 21185840; 21187066; 21193390; 21193393; 21207956; 21209911; 21213129; 21220510; 21224490; 21227008; 21239473; 21242594; 21248371; 21249310; 21251377; 21254648; 21256111; 21257819; 21258402; 21264265; 21266576; 21266827; 21269972; 21278237; 21303984; 21320746; 21329466; 21330458; 21330825; 21332579; 21335603; 21338575; 21343371; 21344271; 21345792; 21350119; 21357506; 21358672; 21360641; 21362301; 21378341; 21386837; 21392092; 21397863; 21401309; 21412054; 21413014; 21415706; 21420913; 21421125; 21426663; 21426805; 21435097; 21435239; 21437769; 21438910; 21448281; 21448921; 21454812; 21458421; 21460102; 21473672; 21481907; 21483406; 21512126; 21514280; 21515475; 21517260; 21517900; 21519196; 21533547; 21538185; 21538273; 21540178; 21544845; 21547579; 21555452; 21557766; 21559457; 21559462; 21571835; 21574962; 21576240; 21586227; 21602890; 21610325; 21612401; 21613675; 21617216; 21620138; 21625218; 21629773; 21633368; 21637285; 21640852; 21647551; 21649463; 21651746; 21658608; 21666710; 21671140; 21672245; 21674552; 21685944; 21693763; 21698228; 21703345; 21709439; 21712445; 21732131; 21733372; 21746877; 21751260; 21763962; 21765619; 21773947; 21775632; 21778301; 21778785; 21779800; 21796840; 21799876; 21802218; 21807114; 21807897; 21813166; 21813290; 21818118; 21819559; 21822544; 21824245; 21824412; 21840486; 21841824; 21843314; 21846590; 21856910; 21859818; 21860410; 21875287; 21876459; 21880716; 21881486; 21887310; 21890473; 21896985; 21897117; 21906983; 21908555; 21910893; 21911388; 21917920; 21922131; 21922147; 21925591; 21926263; 21938405; 21944175; 21945026; 21945343; 21949677; 21959110; 21959987; 21963094; 21964756; 21966417; 21970364; 21979130; 21980400; 21985026; 21987572; 22004076; 22006996; 22009797; 22020939; 22023789; 22036844; 22037464; 22037472; 22041818; 22050843; 22053931; 22058032; 22073864; 22086003; 22086197; 22087807; 22090111; 22093255; 22094081; 22104200; 22114151; 22126773; 22128162; 22128293; 22132102; 22135724; 22144179; 22151618; 22152691; 22153809; 22157238; 22170854; 22172637; 22178822; 22186139; 22190738; 22192476; 22193962; 22194599; 22199311; 22199327; 22209974; 22214699; 22216344; 22219185; 22252496; 22258474; 22258630; 22266372; 22277676; 22277691; 22286099; 22287060; 22297543; 22302938; 22306363; 22308027; 22318330; 22320429; 22320863; 22323302; 22340517; 22341926; 22345328; 22349311; 22350022; 22351759; 22367210; 22376255; 22399808; 22406644; 22406979; 22409847; 22411794; 22415309; 22426121; 22432008; 22435731; 22441426; 22444690; 22450315; 22455137; 22467238; 22470047; 22470546; 22474076; 22475487; 22476163; 22477004; 22479397; 22490291; 22504483; 22505354; 22505724; 22510688; 22516347; 22537386; 22558480; 22569265; 22571395; 22581642; 22593272; 22613607; 22614004; 22614155; 22615960; 22622799; 22628316; 22632108; 22644784; 22645302; 22647679; 22659133; 22673574; 22684029; 22707412; 22728164; 22736026; 22738198; 22745382; 22749322; 22753248; 22781303; 22800355; 22801492; 22820662; 22823210; 22825513; 22831955; 22843691; 22843905; 22848707; 22860423; 22865452; 22865883; 22869720; 22872060; 22873764; 22883454; 22894905; 22908229; 22910906; 22914908; 22918951; 22924580; 22924616; 22925504; 22926560; 22926943; 22927657; 22931643; 22932900; 22936443; 22937154; 22945272; 22946054; 22946320; 22948784; 22952674; 22960198; 22964004; 22970168; 22971010; 22977270; 22977664; 22986049; 22991450; 22992985; 23008060; 23013270; 23020605; 23023480; 23028863; 23028920; 23029528; 23030583; 23034156; 23038967; 23042279; 23042446; 23047702; 23052192; 23053140; 23059773; 23059786; 23060442; 23063455; 23065176; 23065205; 23082126; 23084780; 23087365; 23093058; 23097160; 23123196; 23131565; 23142284; 23144021; 23160040; 23160373; 23161568; 23181555; 23185316; 23185562; 23194660; 23196386; 23220088; 23221556; 23225420; 23228635; 23237807; 23246962; 23248117; 23263636; 23266008; 23269488; 23275444; 23303559; 23326384; 23328582; 23331791; 23333658; 23334958; 23335846; 23336375; 23339102; 23342109; 23344526; 23358852; 23368766; 23372804; 23375385; 23375698; 23381944; 23387829; 23388440; 23389731; 23398456; 23401859; 23404377; 23405012; 23409121; 23409769; 23410250; 23413029; 23421024; 23423382; 23445622; 23449350; 23454212; 23456821; 23457305; 23462604; 23467940; 23474946; 23475391; 23476056; 23481058; 23485997; 23492195; 23496980; 23513056; 23517877; 23523960; 23526216; 23526365; 23526997; 23529663; 23530034; 23530843; 23538299; 23541582; 23545606; 23549681; 23550771; 23551342; 23562913; 23563312; 23567513; 23580587; 23581228; 23583797; 23587905; 23588703; 23593116; 23601303; 23611775; 23615397; 23618863; 23623921; 23639975; 23645672; 23649089; 23661177; 23667251; 23671189; 23671581; 23695013; 23704921; 23711352; 23722539; 23723982; 23746844; 23747271; 23749907; 23750001; 23760768; 23764844; 23767832; 23778527; 23785417; 23787140; 23791554; 23792163; 23799043; 23811286; 23836663; 23840432; 23840602; 23857282; 23862672; 23869589; 23870462; 23872148; 23872956; 23879962; 23880665; 23880760; 23886153; 23886154; 23886195; 23886708; 23897427; 23900566; 23911400; 23912593; 23916472; 23924606; 23928864; 23930677; 23935399; 23936170; 23946285; 23950980; 23959876; 23966163; 23979441; 23991975; 23992143; 23999440; 24015760; 24016866; 24033233; 24042437; 24067372; 24071737; 24090974; 24096035; 24127318; 24164895; 24176785; 24195510; 24197448; 24220190; 24232601; 24316222; 24324133; 24333432; 24344197; 24344305; 24374034; 24374892; 24391213; 24434214 hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor) Ensembl:ENSG00000100644 HGNC:4910 HPRD:04517 MIM:603348 Vega:OTTHUMG00000140344 Other designations: ARNT interacting protein|ARNT-interacting protein|HIF-1-alpha|PAS domain-containing protein 8|basic-helix-loop-helix-PAS protein MOP1|class E basic helix-loop-helix protein 78|hypoxia-inducible factor 1 alpha isoform I.3|hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)|hypoxia-inducible factor 1-alpha|hypoxia-inducible factor1alpha|member of PAS protein 1|member of PAS superfamily 1 HIF1A OGG:3000003116 Bin Zhao, Yue Liu, Oliver He DP2B DPB2 DPbeta2 HLA-DP2B WEB: http://www.ncbi.nlm.nih.gov/gene HLA-DPB2 major histocompatibility complex, class II, DP beta 2 (pseudogene) 3116 6p21.3 9606 6 Official from a nomenclature committee PMID: 3036829; 12477932; 18682748; 19950302; 20031603; 20587610; 21399633; 23482656; 23740775; 23817570 major histocompatibility complex, class II, DP beta 2 (pseudogene) Ensembl:ENSG00000224557 HGNC:4941 HLA-DPB2 OGG:3000003157 Bin Zhao, Yue Liu, Oliver He HMGCS WEB: http://www.ncbi.nlm.nih.gov/gene HMGCS1 3-hydroxy-3-methylglutaryl-CoA synthase 1 (soluble) 3157 5p14-p13 9606 5 Official from a nomenclature committee GO_0001101 (EC: IEA); GO_0001889 (EC: IEA); GO_0004421 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA); GO_0006629 (EC: NAS, PMID: 7913309); GO_0006695 (EC: TAS); GO_0007420 (EC: IEA); GO_0008144 (EC: IEA); GO_0008299 (EC: IEA); GO_0008584 (EC: IEA); GO_0009645 (EC: IEA); GO_0014074 (EC: IEA); GO_0016853 (EC: IEA); GO_0033197 (EC: IEA); GO_0042493 (EC: IEA); GO_0042803 (EC: IEA); GO_0043177 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0046690 (EC: IEA); GO_0055094 (EC: IEA); GO_0071372 (EC: IEA); GO_0071397 (EC: IEA) PMID: 1358203; 1971108; 2870496; 2877984; 3470763; 7913309; 12477932; 14702039; 15489334; 16344560; 17081983; 18029348; 18636124; 18660489; 18854154; 19088433; 20346956; 21139048; 21890473; 21906983; 21963094; 22053931; 22505724; 22939629; 23000965; 23464991 3-hydroxy-3-methylglutaryl-CoA synthase 1 (soluble) Ensembl:ENSG00000112972 HGNC:5007 HPRD:07515 MIM:142940 Vega:OTTHUMG00000162231 Other designations: 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase|3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (soluble)|hydroxymethylglutaryl-CoA synthase, cytoplasmic HMGCS1 OGG:3000003158 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene HMGCS2 3-hydroxy-3-methylglutaryl-CoA synthase 2 (mitochondrial) 3158 1p13-p12 9606 1 Official from a nomenclature committee GO_0004421 (EC: IEA); GO_0005739 (EC: TAS, PMID: 7851882); GO_0005743 (EC: IEA); GO_0005759 (EC: TAS); GO_0006695 (EC: IEA); GO_0008299 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0046950 (EC: TAS); GO_0046951 (EC: TAS) PMID: 6986618; 7851882; 7893153; 9305755; 11228257; 11479731; 12477932; 12647205; 15489334; 16940161; 17387528; 18636124; 18660489; 19913121; 20346956; 20549515; 20618440; 20628086; 20877624; 21502324; 21832049; 21890473; 21906983; 21952825; 22505724 3-hydroxy-3-methylglutaryl-CoA synthase 2 (mitochondrial) Other designations: 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 (mitochondrial)|HMG-CoA synthase|hydroxymethylglutaryl-CoA synthase, mitochondrial HMGCS2 OGG:3000003159 Bin Zhao, Yue Liu, Oliver He HMG-R HMGA1A HMGIY WEB: http://www.ncbi.nlm.nih.gov/gene HMGA1 high mobility group AT-hook 1 3159 RP11-513I15.2 6p21 9606 6 Official from a nomenclature committee GO_0000737 (EC: IDA, PMID: 19465398); GO_0003677 (EC: TAS, PMID: 10871404); GO_0003680 (EC: TAS, PMID: 10428834); GO_0003700 (EC: IMP, PMID: 10428834); GO_0003906 (EC: IDA, PMID: 19465398); GO_0005515 (EC: IPI, PMID: 10428834); GO_0005634 (EC: IDA, PMID: 16901784); GO_0005654 (EC: TAS); GO_0005667 (EC: TAS, PMID: 10428834); GO_0005829 (EC: TAS); GO_0006268 (EC: NAS, PMID: 10428834); GO_0006284 (EC: IDA, PMID: 19465398); GO_0006337 (EC: TAS, PMID: 10428834); GO_0006351 (EC: IEA); GO_0006355 (EC: TAS, PMID: 10871404); GO_0006461 (EC: TAS, PMID: 10428834); GO_0008134 (EC: IDA, PMID: 10428834); GO_0008285 (EC: IMP, PMID: 16901784); GO_0009615 (EC: IEP, PMID: 17005673); GO_0016032 (EC: TAS); GO_0019899 (EC: IPI, PMID: 16157300); GO_0030374 (EC: IMP, PMID: 10428834); GO_0031936 (EC: TAS, PMID: 10428834); GO_0035985 (EC: IDA, PMID: 16901784); GO_0035986 (EC: IDA, PMID: 16901784); GO_0042974 (EC: IDA, PMID: 10428834); GO_0042975 (EC: IDA, PMID: 10428834); GO_0045892 (EC: IMP, PMID: 16901784); GO_0045893 (EC: IMP, PMID: 10428834); GO_0046965 (EC: IDA, PMID: 10428834); GO_0051575 (EC: IDA, PMID: 19465398); GO_0075713 (EC: TAS); GO_0090402 (EC: IDA, PMID: 16901784); GO_2000774 (EC: IMP, PMID: 16901784) PMID: 1692833; 1939057; 2505228; 2701943; 2806554; 2920035; 3619901; 7791781; 7862168; 8414980; 9038339; 9188609; 9253416; 9388234; 9545312; 9751634; 9809067; 9823775; 10074149; 10357819; 10428834; 10428835; 10428836; 10428837; 10713105; 10871404; 10889043; 10891489; 11034995; 11069991; 11076660; 11279116; 11406267; 11498590; 11593421; 11834421; 11978964; 12002338; 12091904; 12097287; 12228227; 12477932; 12653562; 12665574; 12700639; 12761578; 13680222; 14611647; 14702039; 14729942; 14960313; 15213251; 15231747; 15247513; 15302935; 15350136; 15378028; 15479846; 15489334; 15569996; 15591590; 15609325; 15631895; 15835918; 15875659; 15893306; 15901130; 15924147; 16033759; 16075307; 16157300; 16166307; 16189514; 16204234; 16256199; 16291214; 16293633; 16344560; 16403635; 16901784; 17005673; 17045586; 17081983; 17178855; 17434141; 17550233; 17616660; 17654722; 17723105; 17877762; 17903177; 17935122; 17960875; 18202751; 18234858; 18279675; 18310298; 18316571; 18391951; 18473350; 18670638; 18817785; 18850631; 19060921; 19074878; 19223528; 19250063; 19266077; 19343178; 19396169; 19454010; 19465398; 19609535; 19687300; 19729480; 19738201; 19739099; 19750561; 19759913; 19820691; 19848064; 19893584; 19903768; 19913121; 19956671; 20004941; 20189936; 20194618; 20201926; 20335021; 20347905; 20360068; 20379614; 20397748; 20530667; 20546612; 20628086; 20881960; 20935630; 20975707; 21087998; 21089648; 21138859; 21139048; 21156240; 21282977; 21300033; 21319273; 21329653; 21364139; 21573994; 21656127; 21906983; 21957495; 21984063; 21998595; 22106824; 22113938; 22139073; 22156211; 22199144; 22210315; 22214847; 22221703; 22249617; 22332738; 22379092; 22392906; 22411136; 22503056; 22505724; 22564666; 22745191; 22898640; 22932725; 22939624; 22939629; 22961697; 23000965; 23149213; 23166588; 23201162; 23275563; 23302499; 23311322; 23394223; 23398456; 23508853; 23530587; 23545254; 23563607; 23658826; 23796420; 23798998; 23935884; 24122990 high mobility group AT-hook 1 Ensembl:ENSG00000137309 HGNC:5010 HPRD:02829 MIM:600701 Vega:OTTHUMG00000014539 Other designations: HMG-I(Y)|high mobility group protein A1|high mobility group protein HMG-I/HMG-Y|high mobility group protein R|high-mobility group (nonhistone chromosomal) protein isoforms I and Y|nonhistone chromosomal high-mobility group protein HMG-I/HMG-Y HMGA1 gene OGG:3000003161 Bin Zhao, Yue Liu, Oliver He CD168 IHABP RHAMM WEB: http://www.ncbi.nlm.nih.gov/gene HMMR hyaluronan-mediated motility receptor (RHAMM) 3161 5q34 20140408 9606 5 protein-coding Official from a nomenclature committee GO_0005540 (EC: IEA); GO_0005737 (EC: IEA); GO_0005886 (EC: TAS); GO_0005975 (EC: TAS); GO_0009986 (EC: IEA); GO_0030203 (EC: TAS); GO_0030212 (EC: TAS); GO_0030214 (EC: TAS); GO_0044281 (EC: TAS) PMID: 1602151; 7541721; 7683315; 8595891; 8890751; 9601098; 10216086; 10547355; 10882722; 11403955; 11433424; 11448954; 11716065; 12225794; 12477932; 12712331; 12808028; 12939665; 15705883; 15809329; 16112646; 16344560; 16565220; 17157168; 17392272; 17395888; 17872502; 17922014; 17978170; 18174258; 18354082; 18425326; 18559599; 18971636; 19001852; 19011633; 19064580; 19092852; 19148505; 19212667; 19424574; 19580345; 19724689; 19826009; 19857547; 20301425; 20309963; 20360068; 20619784; 20849445; 20956971; 21139048; 21274712; 21435222; 21903422; 21914806; 22095138; 22110403; 22371883; 22532518; 22610405; 23166824; 23328114; 23382057; 23455922; 24250222; 24367099 hyaluronan-mediated motility receptor (RHAMM) Ensembl:ENSG00000072571 HGNC:5012 HPRD:02963 MIM:600936 Vega:OTTHUMG00000130381 Other designations: hyaluronan mediated motility receptor|intracellular hyaluronic acid-binding protein|receptor for hyaluronan-mediated motility HMMR OGG:3000003162 Bin Zhao, Yue Liu, Oliver He HMOX1D HO-1 HSP32 bK286B10 WEB: http://www.ncbi.nlm.nih.gov/gene HMOX1 heme oxygenase (decycling) 1 3162 CTA-286B10.6 22q13.1 9606 22 Official from a nomenclature committee GO_0001525 (EC: TAS, PMID: 12239590); GO_0001935 (EC: TAS, PMID: 12239590); GO_0002246 (EC: IMP, PMID: 9884342); GO_0002686 (EC: TAS, PMID: 14525760); GO_0004392 (EC: IDA, PMID: 17915953); GO_0004392 (EC: IMP, PMID: 19556236); GO_0004630 (EC: IEA); GO_0004871 (EC: IMP, PMID: 12761501); GO_0005615 (EC: TAS, PMID: 18307065); GO_0005634 (EC: ISS); GO_0005730 (EC: IEA); GO_0005783 (EC: IDA, PMID: 19556236); GO_0005783 (EC: ISS); GO_0005789 (EC: TAS); GO_0005829 (EC: IEA); GO_0005901 (EC: IEA); GO_0006778 (EC: TAS); GO_0006788 (EC: IDA, PMID: 17915953); GO_0006879 (EC: TAS); GO_0006979 (EC: IMP, PMID: 9884342); GO_0007264 (EC: IEA); GO_0007588 (EC: IC, PMID: 17915953); GO_0008217 (EC: IEA); GO_0008219 (EC: ISS); GO_0008630 (EC: IEA); GO_0010656 (EC: IEA); GO_0014806 (EC: TAS, PMID: 18289072); GO_0016020 (EC: TAS, PMID: 3345742); GO_0019899 (EC: ISS, PMID: 15516695); GO_0020037 (EC: IDA, PMID: 17915953); GO_0031670 (EC: IEA); GO_0032764 (EC: IEA); GO_0034101 (EC: IMP, PMID: 9884342); GO_0034383 (EC: TAS, PMID: 9884342); GO_0035094 (EC: IDA, PMID: 18205746); GO_0035556 (EC: TAS, PMID: 17652371); GO_0042167 (EC: IDA, PMID: 17915953); GO_0042167 (EC: TAS); GO_0042542 (EC: ISS); GO_0042803 (EC: IDA, PMID: 19556236); GO_0043123 (EC: IMP, PMID: 12761501); GO_0043305 (EC: IEA); GO_0043392 (EC: IEA); GO_0043433 (EC: IEA); GO_0043524 (EC: IEA); GO_0043619 (EC: ISS); GO_0043627 (EC: IEA); GO_0044281 (EC: TAS); GO_0045080 (EC: TAS, PMID: 17652371); GO_0045765 (EC: TAS, PMID: 17652371); GO_0045766 (EC: IEA); GO_0045909 (EC: IC, PMID: 17915953); GO_0046872 (EC: IEA); GO_0048661 (EC: IDA, PMID: 17600318); GO_0048662 (EC: IDA, PMID: 17600318); GO_0051090 (EC: ISS); GO_0051260 (EC: IDA, PMID: 19556236); GO_0055072 (EC: IDA, PMID: 17915953); GO_0055072 (EC: IMP, PMID: 9884342); GO_0055085 (EC: TAS); GO_0071243 (EC: IEA); GO_0071276 (EC: IEA); GO_0071456 (EC: IEP, PMID: 12511571); GO_1902042 (EC: IMP, PMID: 18202225) PMID: 2537723; 2911585; 3345742; 7778849; 8034330; 8146161; 8650873; 9884342; 9890653; 10082382; 10467099; 10591208; 10631150; 10952020; 11385506; 11718398; 11727267; 11786534; 11820797; 11829463; 11849436; 11986386; 12086318; 12091240; 12099373; 12117910; 12118938; 12130498; 12133007; 12136229; 12151344; 12153964; 12182912; 12202863; 12207883; 12222997; 12239590; 12376298; 12376363; 12376366; 12377749; 12379283; 12396617; 12397597; 12431619; 12433915; 12469218; 12477932; 12480749; 12493432; 12500973; 12511571; 12566526; 12579334; 12585963; 12626517; 12649161; 12679469; 12690112; 12709566; 12709568; 12709569; 12709590; 12709592; 12716475; 12730098; 12736395; 12761501; 12777398; 12783778; 12805077; 12810075; 12832044; 12842469; 12865654; 12872043; 12891549; 12909459; 12927812; 12927819; 12933701; 12941774; 12947311; 12969148; 13678532; 14521259; 14523007; 14525760; 14529548; 14587309; 14615405; 14635185; 14647439; 14660632; 14683741; 14691581; 14715242; 14726403; 14733911; 14981149; 14988408; 14992466; 15004156; 15024026; 15028349; 15049686; 15064108; 15084931; 15140586; 15161530; 15166181; 15184199; 15233805; 15284058; 15285018; 15297453; 15316927; 15319861; 15336443; 15337692; 15342556; 15365571; 15451051; 15461802; 15465821; 15470195; 15474356; 15516695; 15519649; 15522396; 15525643; 15544924; 15547665; 15581622; 15611319; 15618017; 15629867; 15652505; 15661856; 15688187; 15690204; 15741166; 15763346; 15797262; 15797755; 15805230; 15817713; 15833736; 15834587; 15849554; 15875813; 15878918; 15885363; 15897578; 15899048; 15964514; 16020495; 16100019; 16117883; 16123320; 16154535; 16181102; 16189191; 16210136; 16232329; 16234431; 16249618; 16271489; 16309585; 16309586; 16309588; 16313248; 16319139; 16374439; 16387424; 16399210; 16455537; 16462769; 16474202; 16485041; 16495813; 16530877; 16540907; 16545694; 16582079; 16596642; 16609364; 16620829; 16697692; 16712795; 16724942; 16771696; 16772700; 16783602; 16804400; 16840713; 16849502; 16882737; 16887359; 16923960; 16945925; 16950787; 16951197; 16971418; 16999951; 17003650; 17018578; 17018862; 17020887; 17064313; 17065227; 17079780; 17081983; 17095719; 17203192; 17204476; 17211576; 17216339; 17219054; 17229906; 17244614; 17254481; 17277740; 17295091; 17389623; 17391133; 17400606; 17413033; 17452746; 17467999; 17511591; 17520317; 17526019; 17526500; 17531161; 17541213; 17558910; 17567933; 17600318; 17601350; 17603281; 17620093; 17652371; 17657593; 17667816; 17721824; 17726138; 17823375; 17853070; 17873285; 17883332; 17886034; 17896171; 17915953; 17919491; 17919492; 17927807; 17953374; 17964723; 17971338; 17991645; 18007994; 18042465; 18045827; 18048809; 18050210; 18077487; 18093274; 18174022; 18195184; 18200441; 18201862; 18202225; 18205746; 18216050; 18234118; 18261117; 18272347; 18274635; 18275848; 18289072; 18307065; 18312299; 18332044; 18344023; 18381758; 18390757; 18404535; 18443197; 18459998; 18460015; 18461097; 18483307; 18502573; 18508827; 18515325; 18524839; 18544348; 18550526; 18560362; 18566988; 18576916; 18582925; 18586007; 18587252; 18596041; 18597895; 18620357; 18640487; 18651163; 18665050; 18689604; 18692581; 18757839; 18769149; 18774956; 18786476; 18787101; 18799519; 18804049; 18811919; 18841019; 18845641; 18923065; 18930811; 18957281; 18975324; 18977241; 18981090; 18983509; 19056482; 19120903; 19122175; 19129475; 19133325; 19165391; 19194559; 19236506; 19238116; 19243019; 19243105; 19246912; 19250338; 19255063; 19255829; 19282863; 19289500; 19303319; 19322201; 19325051; 19336475; 19360326; 19371606; 19389234; 19399816; 19422386; 19428335; 19445907; 19457084; 19457866; 19475336; 19484149; 19487598; 19508729; 19522732; 19526221; 19526463; 19536150; 19548360; 19556236; 19578796; 19586801; 19587144; 19590927; 19604147; 19625608; 19669099; 19676145; 19696228; 19777608; 19785642; 19797297; 19808663; 19808972; 19822148; 19850937; 19853072; 19874887; 19879747; 19884647; 19886851; 19895178; 19903700; 19903769; 19910578; 19913121; 19924377; 19925812; 19965783; 20013271; 20020468; 20021945; 20039940; 20049130; 20064636; 20110814; 20121710; 20127796; 20155807; 20170613; 20175935; 20188821; 20190330; 20193368; 20194081; 20223113; 20229611; 20232486; 20299368; 20345481; 20345975; 20346360; 20351094; 20386498; 20395442; 20404253; 20416077; 20430037; 20446774; 20482362; 20485444; 20504881; 20508205; 20509889; 20518850; 20526373; 20580464; 20585394; 20587610; 20597111; 20599261; 20628086; 20633528; 20667089; 20682519; 20689807; 20705711; 20706680; 20708634; 20733275; 20796278; 20811623; 20832528; 20838751; 20846452; 20868356; 20869265; 20934533; 20938987; 21037234; 21044950; 21079975; 21080099; 21081499; 21091076; 21102410; 21113640; 21136273; 21144518; 21148661; 21157922; 21172416; 21174817; 21191307; 21198350; 21206978; 21211285; 21216973; 21233593; 21236443; 21275653; 21296438; 21307400; 21321939; 21354100; 21366594; 21389316; 21412259; 21425334; 21426408; 21454555; 21495030; 21497776; 21502755; 21506927; 21518986; 21525764; 21531452; 21545264; 21552291; 21555518; 21556890; 21576421; 21598088; 21620964; 21646819; 21647550; 21725851; 21729576; 21737788; 21741353; 21742584; 21756955; 21765894; 21781496; 21808062; 21827279; 21833623; 21861350; 21868703; 21889036; 21898994; 21902835; 21906983; 21911884; 21911919; 21945498; 21963094; 21982894; 21987660; 21988832; 21992109; 22048453; 22078849; 22088544; 22095074; 22123460; 22137262; 22138245; 22142473; 22147556; 22155307; 22158875; 22200625; 22203790; 22212955; 22264017; 22271370; 22276118; 22290142; 22302482; 22323644; 22330859; 22338608; 22418244; 22427825; 22438807; 22461696; 22490514; 22503972; 22541814; 22542718; 22545110; 22549002; 22559824; 22573121; 22578468; 22578957; 22579918; 22580187; 22583702; 22587389; 22594519; 22613607; 22630328; 22666428; 22670665; 22682876; 22689053; 22698995; 22750196; 22776971; 22842631; 22843690; 22849380; 22875919; 22879597; 22881289; 22901690; 22939811; 22945906; 22959128; 22966170; 22989377; 23010497; 23046979; 23051580; 23052192; 23055342; 23074199; 23087099; 23090292; 23092328; 23103292; 23114386; 23123430; 23139759; 23150184; 23158494; 23221079; 23226098; 23238643; 23251661; 23255485; 23288142; 23293173; 23324179; 23345623; 23403148; 23403272; 23406266; 23406650; 23412940; 23423194; 23430116; 23437133; 23454680; 23521418; 23526997; 23536693; 23569422; 23571756; 23580430; 23583371; 23602216; 23606537; 23615401; 23617628; 23660665; 23665328; 23671274; 23714423; 23720344; 23725037; 23737527; 23792437; 23840483; 24038461; 24053646; 24109237; 24211270; 24239896 heme oxygenase (decycling) 1 Ensembl:ENSG00000100292 HGNC:5013 HPRD:00782 MIM:141250 Vega:OTTHUMG00000150960 Other designations: heat shock protein, 32-kD|heme oxygenase 1 HMOX1 OGG:3000003177 Bin Zhao, Yue Liu, Oliver He DER12 ENT2 HNP36 WEB: http://www.ncbi.nlm.nih.gov/gene SLC29A2 solute carrier family 29 (equilibrative nucleoside transporter), member 2 3177 11q13 9606 11 Official from a nomenclature committee GO_0005337 (EC: IEA); GO_0005730 (EC: TAS, PMID: 7639753); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 7639753); GO_0006139 (EC: TAS, PMID: 9396714); GO_0008283 (EC: TAS, PMID: 7639753); GO_0015858 (EC: IDA, PMID: 12527552); GO_0016323 (EC: IDA, PMID: 12527552); GO_0031965 (EC: IEA); GO_0055085 (EC: TAS); GO_1901642 (EC: TAS, PMID: 9396714) PMID: 7639753; 9192854; 9396714; 9478986; 12006583; 12411296; 12477932; 12527552; 12590919; 12820662; 12838422; 14612157; 14702039; 15386342; 15489334; 15644498; 15649894; 16214850; 16924660; 17921321; 17926640; 18635603; 18703227; 18945750; 19105964; 19297449; 20392501; 21156465; 21822668; 21906983; 21926972; 21963094; 21987572; 23590299; 23639800 solute carrier family 29 (equilibrative nucleoside transporter), member 2 Ensembl:ENSG00000174669 HGNC:11004 HPRD:03662 MIM:602110 Vega:OTTHUMG00000169056 Other designations: 36 kDa nucleolar protein HNP36|delayed-early response protein 12|equilibrative NBMPR-insensitive nucleoside transporter|equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter|equilibrative nucleoside transporter 2|hydrophobic nucleolar protein, 36 kDa|hydrophobic nucleolar protein, 36kD|nucleoside transporter, ei-type|solute carrier family 29 (nucleoside transporters), member 2|solute carrier family 29 member 2 SLC29A2 OGG:3000003182 Bin Zhao, Yue Liu, Oliver He ABBP1 HNRPAB WEB: http://www.ncbi.nlm.nih.gov/gene HNRNPAB heterogeneous nuclear ribonucleoprotein A/B 3182 5q35.3 9606 5 Official from a nomenclature committee GO_0000166 (EC: IEA); GO_0001837 (EC: ISS); GO_0003700 (EC: ISS, Qualifier: contributes_to); GO_0003723 (EC: TAS, PMID: 1717314); GO_0003729 (EC: TAS, PMID: 8999813); GO_0005634 (EC: ISS); GO_0005737 (EC: ISS); GO_0030529 (EC: IDA, PMID: 17289661); GO_0043565 (EC: ISS, Qualifier: contributes_to); GO_0044822 (EC: IDA); GO_0045893 (EC: ISS) PMID: 1717314; 8125298; 8895530; 8999813; 11313474; 11790298; 11937625; 12388589; 12477932; 12692135; 14702039; 14704337; 14722087; 15324660; 15489334; 15782174; 16964243; 17289661; 17332742; 17353931; 17643375; 18029348; 18457437; 18850631; 19738201; 20000738; 20020773; 20085233; 20211142; 20360068; 21110914; 21139048; 21145461; 21182205; 21642987; 21853274; 21890473; 21906983; 21942715; 22053931; 22174317; 22178446; 22365833; 22505724; 22623428; 22751105; 22863883; 22939629; 23000965; 23077236; 23151878; 23184937; 23246001; 23398456; 23455922; 23500468; 24457600 heterogeneous nuclear ribonucleoprotein A/B Ensembl:ENSG00000197451 HGNC:5034 HPRD:04067 MIM:602688 Vega:OTTHUMG00000163452 Other designations: ABBP-1|APOBEC1-binding protein 1|apobec-1 binding protein 1|apolipoprotein B mRNA editing enzyme, catalytic polypeptide 1-binding protein 1|hnRNP A/B|hnRNP type A/B protein HNRNPAB OGG:3000003190 Bin Zhao, Yue Liu, Oliver He CSBP HNRPK TUNP WEB: http://www.ncbi.nlm.nih.gov/gene HNRNPK heterogeneous nuclear ribonucleoprotein K 3190 RP11-575L7.1 9q21.32-q21.33 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0000398 (EC: IC, PMID: 11991638); GO_0000398 (EC: TAS); GO_0000790 (EC: IDA); GO_0000978 (EC: IMP); GO_0001077 (EC: IMP); GO_0002102 (EC: IEA); GO_0003697 (EC: TAS); GO_0003723 (EC: TAS, PMID: 8107114); GO_0005515 (EC: IPI, PMID: 12183465); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IEA); GO_0006396 (EC: TAS, PMID: 8107114); GO_0007165 (EC: TAS, PMID: 16130169); GO_0008380 (EC: TAS); GO_0010467 (EC: TAS); GO_0010988 (EC: IMP); GO_0016032 (EC: IEA); GO_0030054 (EC: IEA); GO_0042995 (EC: IEA); GO_0044822 (EC: IDA); GO_0045716 (EC: IMP); GO_0045944 (EC: IMP); GO_0048260 (EC: IMP); GO_0070062 (EC: IDA); GO_0071013 (EC: IDA, PMID: 11991638); GO_0072369 (EC: IMP) PMID: 1729596; 7516469; 7862126; 8051112; 8107114; 8152927; 8398153; 8628302; 8810341; 8833161; 8889548; 9185665; 9399639; 9553145; 9651361; 10329716; 10369774; 10506147; 10749975; 10772858; 10809782; 11231586; 11259409; 11557983; 11741984; 11748221; 11790298; 11840567; 11867641; 11991638; 12029088; 12052863; 12093748; 12183049; 12183465; 12226669; 12370808; 12388589; 12411317; 12477932; 12529443; 12574161; 12951515; 14559993; 14562022; 14702039; 15039586; 15161933; 15161980; 15170860; 15302935; 15303970; 15486205; 15489334; 15514164; 15635413; 15671036; 15782174; 15848144; 15860232; 16004877; 16009940; 16055720; 16130169; 16189514; 16196087; 16230076; 16236267; 16293596; 16344560; 16360036; 16404425; 16492668; 16496041; 16564677; 16713569; 16964243; 17081983; 17191129; 17314511; 17332742; 17361185; 17403666; 17483488; 17561226; 17573780; 17620012; 17620599; 17623298; 17643375; 17667925; 17672864; 18029348; 18377426; 18441016; 18457437; 18472002; 18559600; 18655026; 18854243; 18854308; 19015635; 19059912; 19101556; 19135240; 19165527; 19170760; 19174163; 19249676; 19258514; 19330019; 19380743; 19394292; 19401687; 19520842; 19531213; 19548310; 19596686; 19609950; 19653139; 19738201; 19747914; 19805454; 19808671; 19880579; 20085233; 20224598; 20360068; 20371611; 20408130; 20467438; 20499280; 20548952; 20623123; 20697350; 20888333; 20936779; 20972266; 21044950; 21139048; 21145461; 21151833; 21182205; 21184736; 21233203; 21252943; 21319273; 21321982; 21466159; 21549307; 21821029; 21853274; 21890473; 21900255; 21906983; 21942715; 21963094; 21987572; 21988832; 22053931; 22178446; 22268729; 22321252; 22335908; 22365833; 22379092; 22446626; 22457825; 22505724; 22542455; 22558309; 22582387; 22623428; 22751105; 22760167; 22797925; 22825850; 22863883; 22879910; 22939629; 22960638; 23000965; 23084401; 23092970; 23099853; 23184937; 23246001; 23343766; 23455382; 23455922; 23463506; 23503679; 23519117; 23564449; 23798440; 23798571; 23824909; 23825951; 23843646; 23857582; 23862649; 23974796; 24244333; 24457600 heterogeneous nuclear ribonucleoprotein K Ensembl:ENSG00000165119 HGNC:5044 HPRD:02834 MIM:600712 Vega:OTTHUMG00000020107 Other designations: dC-stretch binding protein|transformation upregulated nuclear protein HNRNPK OGG:3000003300 Bin Zhao, Yue Liu, Oliver He DSMA5 HSJ-1 HSJ1 HSPF3 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2 3300 2q32-q34 9606 2 GO_0000502 (EC: IDA, Qualifier: colocalizes_with, PMID:15936278); GO_0005515 (EC: IPI, PMID:15936278); GO_0006457 (EC: TAS, PMID:1599432); GO_0006986 (EC: TAS, PMID:1599432); GO_0008219 (EC: IEA); GO_0008285 (EC: IGI, PMID:9553041); GO_0016234 (EC: IDA, PMID:15936278); GO_0030308 (EC: IGI, PMID:9553041); GO_0030433 (EC: IDA, PMID:15936278); GO_0030544 (EC: IPI, PMID:15936278); GO_0031398 (EC: IDA, PMID:15936278); GO_0031593 (EC: IDA, PMID:15936278); GO_0032436 (EC: IDA, PMID:15936278); GO_0051082 (EC: TAS, PMID:1599432); GO_0070628 (EC: IDA, PMID:15936278); GO_0090084 (EC: IDA, PMID:15936278); GO_0090086 (EC: IDA, PMID:15936278) PMID:1599432; 8889548; 9553041; 10516435; 11147971; 12107410; 12477932; 12754272; 14751250; 14759258; 15231748; 15489334; 15936278; 16604191; 17082820; 17207965; 17601350; 17847007; 18321953; 18977241; 19285159; 20395441; 21139048; 21625540; 21890473; 21906983; 21963094; 21987572; 22190034; 22522442; 23000965; 23752268; 23940030; 24023695; 24250222 DnaJ (Hsp40) homolog, subfamily B, member 2 Ensembl:ENSG00000135924 HGNC:5228 HPRD:07249 MIM:604139 Vega:OTTHUMG00000133134 Other designations: dnaJ homolog subfamily B member 2|dnaJ protein homolog 1|heat shock 40 kDa protein 3|heat shock protein J1|heat shock protein, neuronal DNAJ-like 1 DNAJB2 OGG:3000003309 Bin Zhao, Yue Liu, Oliver He BIP GRP78 HEL-S-89n MIF2 WEB: http://www.ncbi.nlm.nih.gov/gene HSPA5 heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa) 3309 9q33.3 9606 9 Official from a nomenclature committee GO_0002576 (EC: TAS); GO_0005509 (EC: TAS, PMID: 16130169); GO_0005515 (EC: IPI, PMID: 11907036); GO_0005524 (EC: IEA); GO_0005634 (EC: IMP, PMID: 11943137); GO_0005783 (EC: IDA, PMID: 16223484); GO_0005783 (EC: IMP, PMID: 11943137); GO_0005783 (EC: TAS, PMID: 16130169); GO_0005788 (EC: TAS); GO_0005789 (EC: TAS); GO_0005793 (EC: IDA, PMID: 15308636); GO_0006200 (EC: ISS); GO_0006983 (EC: IEA); GO_0006987 (EC: TAS); GO_0007596 (EC: TAS); GO_0008180 (EC: IDA, Qualifier: colocalizes_with, PMID: 18850735); GO_0009986 (EC: IEA); GO_0016887 (EC: ISS); GO_0019904 (EC: IPI, PMID: 12411443); GO_0021589 (EC: IEA); GO_0021680 (EC: IEA); GO_0021762 (EC: IEP); GO_0030168 (EC: TAS); GO_0030176 (EC: IDA, PMID: 11181571); GO_0030335 (EC: IMP); GO_0030433 (EC: TAS, PMID: 19816510); GO_0030496 (EC: IDA, PMID: 15166316); GO_0030512 (EC: IEA); GO_0030968 (EC: TAS, PMID: 19816510); GO_0031398 (EC: IEA); GO_0031625 (EC: IPI, PMID: 8666824); GO_0034663 (EC: IDA, PMID: 18400946); GO_0035437 (EC: IMP); GO_0042149 (EC: IDA, PMID: 10085239); GO_0042470 (EC: IEA); GO_0043022 (EC: IEA); GO_0043066 (EC: IMP, PMID: 10760948); GO_0043066 (EC: TAS, PMID: 16130169); GO_0044267 (EC: TAS); GO_0051082 (EC: TAS, PMID: 16130169); GO_0051087 (EC: TAS, PMID: 19816510); GO_0051787 (EC: IDA, PMID: 18400946); GO_0060904 (EC: TAS, PMID: 19816510); GO_0070062 (EC: IDA, PMID: 19056867); GO_0071236 (EC: IEA); GO_0071353 (EC: IEA) PMID: 1480470; 1602151; 1649196; 1900540; 2294010; 2840249; 3087629; 3122216; 7724523; 7878056; 7906708; 7957306; 8020977; 8666824; 9006956; 9150946; 9150948; 9305856; 9409741; 9492298; 9885241; 10049727; 10085239; 10197448; 10397760; 10461883; 10514465; 10588643; 10617616; 10708769; 10760948; 10777498; 10887119; 10906332; 10964507; 10964928; 10970892; 11013075; 11160188; 11162507; 11162551; 11181571; 11294872; 11476899; 11719466; 11751874; 11752154; 11765911; 11790298; 11907036; 11932435; 11943137; 12076252; 12097557; 12194978; 12356756; 12359150; 12383251; 12397072; 12411443; 12471035; 12475965; 12477932; 12480769; 12493773; 12514190; 12516782; 12552023; 12621026; 12637535; 12643545; 12665508; 12713871; 12832005; 12840015; 15009096; 15077298; 15146195; 15150263; 15166316; 15280358; 15308636; 15324660; 15456888; 15489334; 15514946; 15525676; 15618547; 15635413; 15657421; 15664986; 15778089; 15817150; 15899857; 15908432; 15949590; 15952740; 16027165; 16051665; 16130169; 16168956; 16169070; 16182273; 16196087; 16212417; 16223484; 16236267; 16257961; 16282978; 16329989; 16344560; 16400691; 16428306; 16472112; 16488447; 16497268; 16522924; 16543232; 16731524; 16912156; 16912197; 17002502; 17062670; 17081065; 17139257; 17184779; 17215244; 17220478; 17337485; 17380188; 17431395; 17601350; 17620599; 17640713; 17643375; 17670764; 17683050; 17721549; 17725712; 17728248; 17765891; 17805346; 17848573; 17906960; 17931354; 17932454; 17936241; 17942541; 17979178; 17991893; 18022401; 18064632; 18083346; 18192872; 18264092; 18268478; 18278507; 18331622; 18343577; 18400946; 18403493; 18411300; 18457437; 18482745; 18502753; 18556570; 18654987; 18708056; 18708359; 18720263; 18757373; 18776923; 18781276; 18781797; 18790759; 18840615; 18842681; 18850735; 18977241; 19014922; 19017364; 19056867; 19097122; 19103594; 19107326; 19128512; 19135240; 19151922; 19164805; 19165527; 19167051; 19188365; 19193609; 19212831; 19228285; 19236758; 19275587; 19287380; 19296942; 19309398; 19343720; 19380743; 19386345; 19411306; 19421146; 19470730; 19471022; 19482905; 19533686; 19546472; 19596686; 19616278; 19626590; 19632185; 19659607; 19671925; 19674193; 19713465; 19718440; 19722195; 19738201; 19741001; 19765186; 19776128; 19786088; 19815544; 19815549; 19816510; 19823030; 19838160; 19838163; 19842229; 19845896; 19850743; 19875381; 19950238; 20017148; 20020773; 20028516; 20072656; 20082722; 20085233; 20145413; 20171186; 20176102; 20204278; 20208072; 20213805; 20360535; 20371724; 20457808; 20473863; 20473970; 20484513; 20492754; 20497865; 20506407; 20508642; 20525207; 20605795; 20628775; 20651985; 20664690; 20672702; 20720212; 20735358; 20739513; 20936779; 20979610; 21056970; 21080038; 21081666; 21112319; 21118962; 21137052; 21139048; 21145461; 21156321; 21189163; 21199322; 21203488; 21221131; 21252943; 21319273; 21343306; 21374734; 21382870; 21389343; 21418596; 21467168; 21472681; 21479362; 21503958; 21516372; 21565611; 21597391; 21622563; 21642380; 21673190; 21738476; 21745816; 21763498; 21779363; 21800051; 21825151; 21840908; 21853274; 21890413; 21890473; 21903092; 21906983; 21940774; 21947079; 21947694; 21963094; 21965664; 21987572; 21988832; 22004425; 22076227; 22079093; 22146569; 22178446; 22215138; 22234250; 22268729; 22297694; 22306319; 22425662; 22427667; 22430489; 22438978; 22446326; 22460328; 22472071; 22495374; 22505724; 22527697; 22528773; 22536838; 22543280; 22546345; 22564965; 22581315; 22613557; 22627132; 22689054; 22735594; 22751133; 22752300; 22796945; 22801219; 22810585; 22851173; 22855534; 22863883; 22889453; 22912664; 22939629; 22945507; 22963397; 22996014; 23000965; 23056589; 23085757; 23089287; 23097496; 23123197; 23161089; 23182705; 23184937; 23200913; 23220234; 23233672; 23246001; 23277564; 23280503; 23314748; 23318453; 23322163; 23349634; 23363602; 23378021; 23383273; 23398456; 23402259; 23402331; 23416888; 23428871; 23438482; 23455922; 23456958; 23457489; 23470966; 23485528; 23544152; 23569248; 23575540; 23578665; 23703321; 23721263; 23759331; 23760505; 23798571; 23818965; 23862649; 23922175; 23956138; 24030972; 24080088; 24113185; 24113381; 24155957; 24239288; 24244333; 24457600 heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa) Ensembl:ENSG00000044574 HGNC:5238 HPRD:00682 MIM:138120 Vega:OTTHUMG00000020672 Other designations: 78 kDa glucose-regulated protein|endoplasmic reticulum lumenal Ca(2+)-binding protein grp78|epididymis secretory sperm binding protein Li 89n|immunoglobulin heavy chain-binding protein HSPA5 OGG:3000003337 Bin Zhao, Yue Liu, Oliver He HSPF1 Hdj1 Hsp40 RSPH16B Sis1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1 3337 19p13.2 9606 19 GO_0005515 (EC: IPI, PMID:17024176); GO_0005730 (EC: IEA); GO_0005737 (EC: IEA); GO_0006986 (EC: TAS, PMID:8975727); GO_0051082 (EC: IEA); GO_0051085 (EC: IEA); GO_0070062 (EC: IDA, PMID:19056867); GO_0070389 (EC: IDA, PMID:18620420) PMID:1586970; 1754405; 8250930; 8670798; 8764402; 8975727; 9499401; 9545528; 9727490; 9920933; 10075921; 10330192; 10593983; 10811660; 10816573; 11093761; 11147971; 11457725; 11500375; 11809754; 11821413; 12150907; 12417652; 12477932; 14499622; 14503850; 14702039; 14743183; 14752510; 15075330; 15194794; 15362566; 15489334; 16009940; 16179353; 16196087; 16842747; 16919237; 17012257; 17024176; 17601350; 18032501; 18187620; 18211704; 18457437; 18620420; 18624398; 18977241; 19056867; 19254810; 19615732; 19738201; 19779646; 19901540; 20026329; 20084477; 20360068; 20516149; 20562859; 20735358; 20801936; 20809635; 20811636; 20885985; 21044950; 21124777; 21139048; 21139202; 21145461; 21163940; 21249176; 21480956; 21639839; 21698289; 21763498; 21832049; 21890473; 21906983; 21987572; 22022600; 22075554; 22505724; 22779921; 22863883; 22990118; 23000965; 23395854; 23400395; 23482560; 24091676; 24196953; 24255178; 24318877; 24361594 DnaJ (Hsp40) homolog, subfamily B, member 1 Ensembl:ENSG00000132002 HGNC:5270 HPRD:05198 MIM:604572 Vega:OTTHUMG00000183289 Other designations: DnaJ (Hsp40) homolog, subfmaily B, member 1|dnaJ homolog subfamily B member 1|dnaJ protein homolog 1|hDj-1|heat shock 40 kDa protein 1|heat shock 40kD protein 1|heat shock protein 40|human DnaJ protein 1|radial spoke 16 homolog B DNAJB1 OGG:3000003338 Bin Zhao, Yue Liu, Oliver He DANJC4 HSPF2 MCG18 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC4 DnaJ (Hsp40) homolog, subfamily C, member 4 3338 11q13 9606 11 GO_0005515 (EC: IPI, PMID:17500595); GO_0005739 (EC: IEA); GO_0006457 (EC: NAS, PMID:9473517); GO_0006986 (EC: TAS, PMID:9473517); GO_0016020 (EC: NAS, PMID:9473517); GO_0016021 (EC: IEA); GO_0051082 (EC: NAS, PMID:9473517) PMID:9473517; 11147971; 12477932; 15489334; 17207965; 17500595; 19913121; 20029029; 20237496; 20628086; 20877624; 21832049 DnaJ (Hsp40) homolog, subfamily C, member 4 Ensembl:ENSG00000110011 HGNC:5271 MIM:604189 Vega:OTTHUMG00000167792 Other designations: dnaJ homolog subfamily C member 4|dnaJ-like protein HSPF2|heat shock 40kD protein 2|multiple endocrine neoplasia type 1 candidate protein number 18 DNAJC4 OGG:3000003339 Bin Zhao, Yue Liu, Oliver He HSPG PLC PRCAN SJA SJS SJS1 WEB: http://www.ncbi.nlm.nih.gov/gene HSPG2 heparan sulfate proteoglycan 2 3339 RP11-132G19.2 1p36.1-p34 9606 1 Official from a nomenclature committee GO_0001523 (EC: TAS); GO_0001525 (EC: IEA); GO_0001958 (EC: IEA); GO_0002062 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11956183); GO_0005576 (EC: TAS); GO_0005605 (EC: IEA); GO_0005615 (EC: IDA); GO_0005796 (EC: TAS); GO_0005886 (EC: TAS); GO_0005975 (EC: TAS); GO_0006024 (EC: TAS); GO_0006027 (EC: TAS); GO_0007420 (EC: IEA); GO_0007603 (EC: TAS); GO_0008022 (EC: IPI, PMID: 12604605); GO_0008104 (EC: IEA); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0030203 (EC: TAS); GO_0030204 (EC: TAS); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0031012 (EC: ISS, Qualifier: colocalizes_with); GO_0042157 (EC: TAS); GO_0043202 (EC: TAS); GO_0044281 (EC: TAS); GO_0046872 (EC: IEA); GO_0048704 (EC: IEA); GO_0048738 (EC: IEA); GO_0060351 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 1569102; 1679749; 1685141; 1730768; 2687294; 2745554; 7500359; 8234307; 8541852; 9136074; 9307034; 9313766; 9431988; 9688542; 9692901; 9733643; 10545953; 10579711; 10702276; 11101850; 11148217; 11279527; 11493006; 11574465; 11847210; 11847221; 11941538; 11956183; 11968010; 12036876; 12435733; 12477932; 12604605; 12754519; 12811819; 12900424; 14563633; 14625044; 14630925; 14702039; 14973356; 14974815; 15031130; 15081423; 15211644; 15231748; 15240572; 15567441; 15591058; 15657057; 15905187; 16129435; 16269412; 16283481; 16335952; 16407285; 16570819; 16620836; 16713569; 16914267; 16927315; 16984910; 17356275; 18024432; 18658137; 19056867; 19066875; 19380743; 19506372; 19553700; 19669783; 19738201; 19788922; 19789387; 19839757; 19889475; 19913121; 20053631; 20072119; 20074558; 20452482; 20507176; 20628086; 20673868; 20690028; 21078624; 21126803; 21255062; 21596751; 21808285; 22003087; 22076637; 22268729; 22457785; 22643235; 23060442; 23104139; 23161552; 23235151; 23336978; 23374253; 23436656; 23509972; 23568740; 23599406; 24101524 heparan sulfate proteoglycan 2 Ensembl:ENSG00000142798 HGNC:5273 HPRD:00804 MIM:142461 Vega:OTTHUMG00000002674 Other designations: basement membrane-specific heparan sulfate proteoglycan core protein|endorepellin (domain V region)|perlecan proteoglycan HSPG2 OGG:3000003439 Bin Zhao, Yue Liu, Oliver He IFL IFN IFN-ALPHA IFN-alphaD IFNA13 IFNA@ WEB: http://www.ncbi.nlm.nih.gov/gene IFNA1 interferon, alpha 1 3439 9p22 20140408 9606 9 protein-coding Official from a nomenclature committee PMID: 1381203; 1385305; 1708818; 1849076; 1905933; 2014240; 2552026; 2985969; 3262520; 4057246; 6157095; 6157600; 6159536; 6163083; 6310510; 6479148; 7511078; 7526537; 7532202; 7583919; 7815507; 7904170; 7913356; 7932753; 8345204; 8438572; 8454630; 8661419; 8668211; 8764000; 9108403; 9181467; 9225992; 9271440; 9343822; 9425112; 9520456; 9658081; 9865497; 11032395; 11315919; 11744801; 11986939; 11991671; 12070711; 12089333; 12091360; 12097384; 12162875; 12242445; 12323007; 12393722; 12410802; 12435568; 12477932; 12530117; 12538683; 12543882; 12581491; 12620797; 12682235; 12749388; 12759354; 12761564; 12804771; 12817009; 12967644; 14500632; 14734746; 15056668; 15087447; 15164053; 15188363; 15233997; 15240148; 15481145; 15489334; 15571260; 15585849; 15621727; 15634924; 15674657; 15699120; 15790787; 15795269; 15883164; 15941912; 15989801; 16005433; 16160188; 16175599; 16253303; 16278001; 16375755; 16418394; 16426578; 16785534; 16797201; 16859998; 16948893; 17180012; 17360657; 17517919; 17572490; 17597478; 17703412; 17785816; 17911607; 17933493; 17956986; 17968925; 17968926; 18005734; 18050196; 18071879; 18184042; 18200009; 18200012; 18218993; 18272764; 18283629; 18311820; 18318750; 18405996; 18414664; 18576315; 18606657; 18633131; 18672082; 18708672; 18771758; 18926293; 19000144; 19004943; 19050236; 19095736; 19124763; 19158240; 19203249; 19258923; 19339987; 19401392; 19434718; 19559726; 19651532; 19657094; 19706714; 19754307; 19796531; 19796549; 19817985; 19857525; 19913121; 20018632; 20065083; 20096141; 20112359; 20149251; 20164424; 20174557; 20182777; 20237496; 20299058; 20303780; 20331378; 20465564; 20473322; 20503287; 20506305; 20554782; 20565368; 20574843; 20588103; 20588308; 20592282; 20628086; 20628092; 20810735; 20817881; 20857263; 20860222; 20875078; 20959405; 20964804; 20980519; 21120500; 21177291; 21213104; 21263073; 21268015; 21276246; 21317915; 21320124; 21339641; 21361792; 21376046; 21525212; 21645334; 21705624; 21772053; 21821707; 21918813; 21923413; 22149411; 22156987; 22192711; 22195005; 22222875; 22226324; 22242767; 22249201; 22264514; 22315404; 22396599; 22661095; 22684144; 22685561; 22693567; 22706089; 22739040; 22814248; 22925929; 23026954; 23042723; 23224365; 23237992; 23303061; 23382558; 23434493; 23462180; 23479228; 23649622; 23724117; 23814052; 23890815; 23910645; 24049170; 24269682 interferon, alpha 1 Ensembl:ENSG00000197919 HGNC:5417 HPRD:00974 MIM:147660 Vega:OTTHUMG00000019673 IFNA1 OGG:3000003440 Bin Zhao, Yue Liu, Oliver He IFN-alphaA IFNA IFNA2B INFA2 WEB: http://www.ncbi.nlm.nih.gov/gene IFNA2 interferon, alpha 2 3440 RP11-354P17.2 9p22 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0005125 (EC: IEA); GO_0005132 (EC: TAS, PMID: 6158094); GO_0005515 (EC: IPI, PMID: 7759950); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0006915 (EC: TAS, PMID: 10477584); GO_0006954 (EC: TAS, PMID: 10477584); GO_0007166 (EC: TAS, PMID: 6158094); GO_0007267 (EC: TAS, PMID: 10477584); GO_0007596 (EC: TAS); GO_0010629 (EC: IDA); GO_0019221 (EC: TAS); GO_0042517 (EC: IDA); GO_0045087 (EC: TAS); GO_0045581 (EC: IDA); GO_0045892 (EC: IDA); GO_0046597 (EC: IDA); GO_0051607 (EC: IDA); GO_0060337 (EC: TAS); GO_0060338 (EC: TAS); GO_2000552 (EC: IDA); GO_2000663 (EC: IDA); GO_2000666 (EC: IDA) PMID: 1381203; 1385305; 1708818; 1834641; 1905933; 2014240; 2049076; 2552026; 3906813; 6158094; 6159537; 6159538; 6162107; 6163083; 6164056; 6170983; 6310510; 7511078; 7526537; 7532202; 7583919; 7627809; 7759950; 7815507; 7904170; 7913356; 8234245; 8345204; 8366289; 8438572; 8661419; 8668211; 8764000; 8994971; 9108403; 9181467; 9225992; 9343822; 9417943; 9425112; 9520456; 9658081; 9694076; 9865497; 10339405; 10477584; 11694501; 11888273; 12010658; 12089333; 12477932; 15004750; 15233997; 15481145; 16160188; 16171819; 16278001; 16375755; 16418394; 16697656; 16920161; 17116765; 17180012; 17181634; 17360657; 17477817; 17703412; 17880940; 18005734; 18027911; 18032529; 18200009; 18200012; 18272764; 18414664; 18584346; 18672082; 18729739; 18937499; 19000144; 19004943; 19055755; 19153447; 19258923; 19345260; 19559726; 19564411; 19574459; 19621225; 19706714; 19790049; 20159042; 20237496; 20309637; 20331378; 20503287; 20532927; 20574843; 20588308; 21057730; 21115688; 21223583; 21411783; 21466707; 21757613; 21854986; 22204827; 22315404; 22332739; 22482409; 22570109; 22571879; 22610275; 22610944; 22685550; 22731491; 22739040; 22814248; 22885264; 22951153; 23055569; 23184955; 23213068; 23437155; 23913484; 24089560; 24269682 interferon, alpha 2 Ensembl:ENSG00000188379 HGNC:5423 HPRD:00950 MIM:147562 Vega:OTTHUMG00000019674 Other designations: IFN-alpha-2|alpha-2a interferon|interferon alpha 2a|interferon alpha 2b|interferon alpha A|interferon alpha-2|leIF A IFNA2 OGG:3000003454 Bin Zhao, Yue Liu, Oliver He AVP IFN-alpha-REC IFNAR IFNBR IFRC WEB: http://www.ncbi.nlm.nih.gov/gene IFNAR1 interferon (alpha, beta and omega) receptor 1 3454 21q22.11 20140408 9606 21 protein-coding Official from a nomenclature committee GO_0004905 (EC: TAS, PMID: 7665574); GO_0005515 (EC: IPI, PMID: 12220192); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 8181059); GO_0007166 (EC: TAS, PMID: 7665574); GO_0007259 (EC: TAS, PMID: 7665574); GO_0009615 (EC: TAS, PMID: 2153461); GO_0019221 (EC: TAS); GO_0032729 (EC: IEA); GO_0042110 (EC: IEA); GO_0045351 (EC: IEA); GO_0051607 (EC: IEA); GO_0060337 (EC: TAS); GO_0060338 (EC: TAS) PMID: 1350660; 1370833; 1834641; 2148760; 2153461; 7526154; 7559568; 7665574; 7932753; 8125298; 8181059; 8524272; 8605876; 8626489; 9029147; 9121453; 9174595; 9225992; 9403695; 9677371; 9733772; 10490982; 10542297; 10830953; 11167825; 11301323; 11694501; 11786546; 12220192; 12477932; 12554654; 12618863; 12620806; 12697242; 12761564; 14532120; 14647450; 14727154; 15063762; 15337770; 15356134; 15389589; 15449939; 15489334; 15589821; 15885318; 15946680; 15990456; 16171819; 16338279; 16624932; 17001036; 17027223; 17125879; 17310065; 17517919; 17667505; 17703412; 17823081; 17923090; 18056411; 18166147; 18250407; 18338947; 18362156; 18474601; 18535656; 18761606; 18801736; 18937499; 18953482; 19103527; 19124753; 19220955; 19258923; 19299650; 19434718; 19453261; 19501422; 19559055; 19561067; 19730683; 19773451; 19796549; 19805514; 19817957; 19879773; 19913121; 19948722; 19957332; 20020050; 20065083; 20237496; 20331378; 20378664; 20503287; 20565290; 20588308; 20628086; 20811626; 21139048; 21173164; 21540188; 21690295; 21695243; 21716316; 21756311; 21757742; 21821707; 21830897; 21832278; 21865166; 22036215; 22136495; 22156349; 22162633; 22218495; 22258259; 22786773; 22824466; 23128233; 23129613; 23201923; 23209811; 23663046; 24250222 interferon (alpha, beta and omega) receptor 1 Ensembl:ENSG00000142166 HGNC:5432 HPRD:00126 MIM:107450 Vega:OTTHUMG00000065126 IFNAR1 OGG:3000003455 Bin Zhao, Yue Liu, Oliver He IFN-R IFN-alpha-REC IFNABR IFNARB WEB: http://www.ncbi.nlm.nih.gov/gene IFNAR2 interferon (alpha, beta and omega) receptor 2 3455 21q22.11 20140408 9606 21 protein-coding Official from a nomenclature committee GO_0004905 (EC: IDA, PMID: 7759950); GO_0005515 (EC: IPI, PMID: 11046044); GO_0005576 (EC: TAS, PMID: 7588638); GO_0005615 (EC: IDA, PMID: 7759950); GO_0005615 (EC: IEA); GO_0005886 (EC: TAS); GO_0005887 (EC: IDA, PMID: 7759950); GO_0006357 (EC: IEA); GO_0007166 (EC: TAS, PMID: 8798579); GO_0007259 (EC: TAS, PMID: 7588638); GO_0008283 (EC: IEA); GO_0009615 (EC: TAS, PMID: 7588638); GO_0019221 (EC: TAS); GO_0019901 (EC: IPI, PMID: 7759950); GO_0019962 (EC: IPI, PMID: 7759950); GO_0035455 (EC: IDA, PMID: 7759950); GO_0060337 (EC: TAS); GO_0060338 (EC: TAS) PMID: 7570186; 7588638; 7665574; 7759950; 8181059; 8798579; 8889548; 8969169; 9121453; 10339405; 10395669; 10830953; 11046044; 11301323; 11694501; 11786546; 11888273; 12105218; 12133952; 12218119; 12220192; 12477932; 12618863; 12842042; 12960323; 14647450; 14980076; 15063762; 15286706; 15287740; 15389589; 15449939; 15717316; 15885318; 16000408; 16054712; 16106266; 16518956; 16624932; 16710296; 17095088; 17517919; 17567994; 17572016; 17667505; 17697365; 17703412; 17923090; 18027911; 18338947; 18456457; 18456658; 18676680; 18715339; 18801736; 18971450; 19170196; 19258923; 19299650; 19362011; 19401692; 19434718; 19453261; 19505916; 19625176; 19667218; 19692168; 19714778; 19773279; 19773451; 19796549; 19817957; 19913121; 20065083; 20087947; 20237496; 20331378; 20453000; 20485444; 20503287; 20588308; 20628086; 20811626; 21690295; 21988832; 22236545; 22632162; 23128233; 23663046; 23745570 interferon (alpha, beta and omega) receptor 2 Ensembl:ENSG00000159110 HGNC:5433 HPRD:03850 MIM:602376 Vega:OTTHUMG00000065127 Other designations: IFN-R-2|IFN-alpha/beta receptor 2|human interferon alpha/beta receptor|interferon alpha binding protein|interferon alpha/beta receptor 2|interferon-alpha/beta receptor beta chain|type I interferon receptor 2 IFNAR2 OGG:3000003456 Bin Zhao, Yue Liu, Oliver He IFB IFF IFNB WEB: http://www.ncbi.nlm.nih.gov/gene IFNB1 interferon, beta 1, fibroblast 3456 RP11-113D19.1 9p21 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0002250 (EC: IEA); GO_0002286 (EC: IBA); GO_0002312 (EC: IMP, PMID: 12932356); GO_0002323 (EC: IBA); GO_0005125 (EC: IBA); GO_0005125 (EC: IDA, PMID: 19008854); GO_0005132 (EC: NAS, PMID: 2414376); GO_0005576 (EC: IC, PMID: 2414376); GO_0005576 (EC: TAS); GO_0005615 (EC: IBA); GO_0006959 (EC: IBA); GO_0007166 (EC: TAS, PMID: 10640778); GO_0007596 (EC: TAS); GO_0009615 (EC: NAS, PMID: 12120696); GO_0019221 (EC: IBA); GO_0019221 (EC: TAS); GO_0030101 (EC: NAS, PMID: 11987821); GO_0030183 (EC: IBA); GO_0033141 (EC: IDA, PMID: 18035482); GO_0042100 (EC: NAS, PMID: 3135963); GO_0042742 (EC: IEA); GO_0043330 (EC: IDA); GO_0045071 (EC: IDA, PMID: 19008854); GO_0045087 (EC: TAS); GO_0045089 (EC: NAS, PMID: 11987821); GO_0045343 (EC: NAS, PMID: 8805651); GO_0045581 (EC: IDA); GO_0045944 (EC: IDA, PMID: 18035482); GO_0051607 (EC: TAS, PMID: 19416887); GO_0060337 (EC: TAS); GO_0060338 (EC: TAS); GO_0071360 (EC: TAS); GO_2000552 (EC: IDA); GO_2001235 (EC: IDA, PMID: 10918594) PMID: 1708818; 1834641; 2414376; 3135963; 3667593; 3872918; 6157094; 6157601; 6159580; 6159584; 6159597; 6162107; 6164984; 6171735; 6178110; 6183692; 6500557; 6762376; 7532202; 7913356; 8083608; 8107259; 8605876; 8661419; 8805651; 9225992; 9342320; 9713311; 10229237; 10395669; 10482360; 10640778; 10918594; 10963806; 11337497; 11694501; 11781186; 11972054; 11987821; 12050353; 12068083; 12089333; 12096926; 12097388; 12120696; 12184914; 12405292; 12477932; 12581491; 12761564; 12847277; 12932356; 14519761; 14519765; 14727154; 14747551; 15004750; 15107417; 15163707; 15163721; 15280450; 15340234; 15481145; 15489334; 15557158; 15621727; 15652402; 15737993; 15752772; 15767399; 16002711; 16185826; 16338279; 16375755; 16504056; 16504464; 16505900; 16545883; 16593086; 16631220; 16697656; 16873258; 16951313; 16954376; 16984921; 16989575; 17079289; 17142768; 17167270; 17182689; 17215277; 17328045; 17548221; 17560375; 17574024; 17652396; 17675303; 17968925; 17968926; 17985330; 18035482; 18209079; 18272195; 18322185; 18370868; 18381783; 18382694; 18389079; 18420941; 18437017; 18571728; 18581327; 18611945; 18614013; 18614628; 18641315; 18653385; 18653650; 18708672; 18715339; 18771559; 18781139; 18823997; 18989459; 19008854; 19017631; 19017982; 19017994; 19056675; 19201909; 19240061; 19351494; 19353519; 19380831; 19416887; 19449179; 19453261; 19546225; 19564073; 19564411; 19622906; 19667093; 19728309; 19758707; 19795416; 19804729; 19833099; 19846511; 19898481; 19913121; 19934272; 20007272; 20048166; 20127681; 20154210; 20174559; 20181693; 20187765; 20237496; 20331378; 20375222; 20404187; 20518826; 20519382; 20538852; 20554782; 20561040; 20573816; 20574843; 20588308; 20592282; 20628086; 20631305; 20699220; 20711230; 20844191; 20846052; 20850164; 21040977; 21068253; 21071089; 21113677; 21115688; 21129405; 21160051; 21170271; 21170385; 21213104; 21228327; 21276246; 21288362; 21320124; 21321205; 21325029; 21361792; 21368231; 21389130; 21518144; 21652010; 21690236; 21698224; 21764463; 21778165; 21792910; 21829730; 21855056; 21886773; 21886806; 21889215; 21897875; 21952237; 22072748; 22112394; 22149411; 22192711; 22200507; 22222875; 22226324; 22258259; 22278222; 22293894; 22301134; 22344395; 22383950; 22396773; 22396801; 22442431; 22527232; 22531926; 22629479; 22674996; 22698399; 22730532; 22731491; 22738830; 22745372; 22814248; 22842821; 22843696; 22879913; 22889324; 22938469; 22951153; 22970235; 22992810; 23008447; 23056170; 23166786; 23221969; 23284052; 23333334; 23383510; 23396947; 23449998; 23507702; 23518714; 23552410; 23616277; 23631912; 23649622; 23675467; 23685241; 23686695; 23814052; 23824799; 23986588; 23990053; 24049179; 24067967; 24144296; 24227842 interferon, beta 1, fibroblast Ensembl:ENSG00000171855 HGNC:5434 HPRD:00972 MIM:147640 Vega:OTTHUMG00000019652 IFNB1 OGG:3000003458 Bin Zhao, Yue Liu, Oliver He IFG IFI WEB: http://www.ncbi.nlm.nih.gov/gene IFNG interferon, gamma 3458 12q14 20140408 9606 12 protein-coding Official from a nomenclature committee GO_0000060 (EC: IDA, PMID: 15604419); GO_0000122 (EC: ISS); GO_0001781 (EC: IEA); GO_0002026 (EC: IEA); GO_0002053 (EC: ISS); GO_0002250 (EC: IBA); GO_0002302 (EC: IEA); GO_0003340 (EC: ISS); GO_0005125 (EC: IBA); GO_0005133 (EC: IEA); GO_0005576 (EC: IDA); GO_0005576 (EC: TAS); GO_0005615 (EC: IBA); GO_0006915 (EC: IGI, PMID: 7828849); GO_0006928 (EC: TAS, PMID: 10477596); GO_0006959 (EC: IBA); GO_0007050 (EC: IDA, PMID: 16942485); GO_0007166 (EC: TAS, PMID: 10477596); GO_0009615 (EC: IDA, PMID: 16280321); GO_0009897 (EC: IEA); GO_0019221 (EC: TAS); GO_0019882 (EC: IEA); GO_0030593 (EC: IEA); GO_0030968 (EC: IEA); GO_0031642 (EC: IEA); GO_0032224 (EC: IEA); GO_0032700 (EC: IDA, PMID: 18501882); GO_0032735 (EC: IDA, PMID: 7605994); GO_0032747 (EC: IDA); GO_0032760 (EC: IEA); GO_0033141 (EC: IDA, PMID: 16280321); GO_0033141 (EC: NAS); GO_0034393 (EC: IDA, PMID: 16942485); GO_0042102 (EC: IEA); GO_0042493 (EC: IEA); GO_0042511 (EC: IDA, PMID: 15604419); GO_0042742 (EC: IEA); GO_0042832 (EC: IEA); GO_0044130 (EC: IEA); GO_0045080 (EC: IEA); GO_0045084 (EC: IEA); GO_0045348 (EC: IEA); GO_0045410 (EC: IEA); GO_0045429 (EC: IDA, PMID: 8383325); GO_0045666 (EC: IEA); GO_0045672 (EC: IDA, PMID: 16220542); GO_0045785 (EC: IEA); GO_0045944 (EC: IEA); GO_0048304 (EC: IEA); GO_0048662 (EC: IDA, PMID: 16942485); GO_0050718 (EC: IEA); GO_0050796 (EC: IDA, PMID: 8383325); GO_0051044 (EC: IDA, PMID: 18373975); GO_0051607 (EC: IEA); GO_0051712 (EC: IDA, PMID: 7544003); GO_0060333 (EC: TAS); GO_0060334 (EC: TAS); GO_0060550 (EC: IDA, PMID: 9282826); GO_0060552 (EC: IDA, PMID: 9282826); GO_0060557 (EC: IDA, PMID: 9282826); GO_0060559 (EC: IDA, PMID: 9282826); GO_0071222 (EC: IEA); GO_0071351 (EC: IEA); GO_0072308 (EC: ISS); GO_0097191 (EC: IDA, PMID: 16942485); GO_2000309 (EC: IDA, PMID: 16220542) PMID: 1400376; 1525157; 1662603; 1708818; 1902591; 1905933; 1905983; 2452186; 2504704; 2514776; 2860101; 3109913; 3139842; 6173769; 6176945; 6180322; 6305337; 6329718; 6427223; 7511078; 7523014; 7526537; 7544003; 7583919; 7587386; 7590734; 7605994; 7617032; 7673114; 7815507; 7818827; 7828849; 7904170; 7941321; 8065455; 8102828; 8188658; 8247028; 8345204; 8383325; 8537091; 8557999; 8598486; 8619916; 8631301; 8648753; 8661419; 8679287; 8706326; 8760410; 8764000; 8765022; 8769094; 8809126; 8974399; 9108403; 9225992; 9282826; 9534962; 9651359; 9658081; 9712080; 9743208; 9916748; 10358150; 10388525; 10438928; 10446807; 10477596; 10775602; 10860730; 10933622; 10986460; 11240951; 11250200; 11266927; 11266928; 11292301; 11298489; 11298547; 11315919; 11316066; 11354638; 11391238; 11404167; 11528517; 11544427; 11544434; 11700035; 11751951; 11755617; 11772518; 11774563; 11781187; 11781192; 11786536; 11796707; 11821159; 11830476; 11831440; 11841489; 11854199; 11854210; 11857052; 11857344; 11861290; 11865054; 11876761; 11900986; 11906646; 11920321; 11936954; 11943142; 11947926; 11953317; 11964313; 11966872; 11970958; 11980899; 11981433; 11984595; 11986281; 11986939; 11991675; 12006410; 12011077; 12020266; 12042661; 12047360; 12050152; 12060750; 12070781; 12084660; 12089333; 12089714; 12097398; 12102661; 12105273; 12162871; 12162874; 12165521; 12170266; 12191570; 12192641; 12203138; 12209087; 12219025; 12223098; 12223516; 12232842; 12239181; 12296868; 12358843; 12366695; 12368207; 12370350; 12370385; 12377943; 12389079; 12393446; 12394188; 12401479; 12420205; 12438348; 12438388; 12441140; 12444137; 12451269; 12471139; 12473063; 12477932; 12479817; 12486605; 12507818; 12526950; 12531694; 12531774; 12533683; 12542496; 12548511; 12552499; 12555203; 12558814; 12579348; 12581491; 12588705; 12590978; 12594832; 12595908; 12609526; 12615834; 12633940; 12645529; 12653164; 12700631; 12727482; 12727483; 12738388; 12750172; 12751024; 12754213; 12761564; 12788307; 12788577; 12794718; 12804771; 12813035; 12818128; 12819637; 12850811; 12851716; 12854077; 12890425; 12909463; 12914676; 12917425; 12928400; 12938195; 12944981; 12960156; 12965263; 12968017; 12975380; 14499500; 14511565; 14514772; 14522096; 14558082; 14566095; 14601649; 14602571; 14607827; 14607900; 14607968; 14625191; 14631168; 14661818; 14675394; 14675398; 14681912; 14688135; 14690454; 14692664; 14694183; 14698136; 14704034; 14734640; 14734771; 14753294; 14872501; 14959851; 14962095; 14969768; 14976609; 14978096; 14988089; 14992891; 14993214; 15004750; 15007355; 15018649; 15019280; 15041164; 15051500; 15066699; 15068623; 15078471; 15115662; 15120189; 15135368; 15162834; 15166131; 15170937; 15182335; 15189946; 15194285; 15200452; 15207246; 15214940; 15215891; 15235581; 15247172; 15251440; 15265425; 15271977; 15297269; 15316224; 15320903; 15322002; 15322007; 15324937; 15327519; 15345584; 15347683; 15361128; 15361241; 15367434; 15372109; 15374002; 15381817; 15390286; 15448160; 15458467; 15462469; 15481145; 15489334; 15498860; 15499631; 15501397; 15511228; 15522880; 15550390; 15556691; 15570643; 15580300; 15585559; 15599305; 15603866; 15604419; 15611657; 15621151; 15624893; 15628695; 15634895; 15638726; 15643599; 15644127; 15652446; 15661939; 15674394; 15675129; 15679925; 15681246; 15681825; 15695523; 15708894; 15709194; 15710386; 15718915; 15725351; 15731046; 15733644; 15737643; 15749687; 15763337; 15773449; 15778222; 15780879; 15784411; 15800938; 15811521; 15815688; 15816837; 15818327; 15841043; 15842590; 15853924; 15858598; 15870936; 15880044; 15890243; 15900487; 15901906; 15905622; 15919929; 15925543; 15931634; 15932621; 15932627; 15935691; 15936090; 15941525; 15944226; 15944319; 15950283; 15969687; 15979955; 15985639; 15992611; 16002423; 16014948; 16024776; 16024856; 16034083; 16051062; 16051377; 16051797; 16085646; 16098562; 16108727; 16115485; 16127458; 16129616; 16148108; 16148152; 16160188; 16166103; 16182624; 16183136; 16200827; 16201318; 16204617; 16210653; 16216674; 16220542; 16232344; 16243534; 16257975; 16263796; 16266858; 16280321; 16302211; 16310045; 16318585; 16323127; 16364177; 16367922; 16375755; 16378074; 16386594; 16391178; 16403098; 16409297; 16410273; 16421220; 16425360; 16427044; 16427155; 16430971; 16433832; 16434471; 16474934; 16476013; 16478776; 16484229; 16487026; 16487180; 16493441; 16504056; 16538877; 16540751; 16567828; 16574426; 16616105; 16621981; 16647017; 16672072; 16678358; 16681592; 16689860; 16690980; 16704689; 16718821; 16720107; 16723718; 16724074; 16730575; 16737571; 16754651; 16762155; 16785527; 16820703; 16824159; 16861661; 16861684; 16863661; 16873363; 16889932; 16897354; 16903774; 16914208; 16916659; 16919160; 16930778; 16938461; 16938650; 16942485; 16944293; 16950634; 16961714; 16962335; 16966412; 16970687; 16984280; 17002607; 17006334; 17013806; 17013989; 17015683; 17021766; 17023015; 17026468; 17028199; 17033822; 17035315; 17049266; 17082625; 17097497; 17110450; 17117487; 17121582; 17136124; 17138053; 17138064; 17142750; 17142760; 17145371; 17148586; 17152005; 17154717; 17159260; 17180012; 17182600; 17198275; 17207568; 17209781; 17211638; 17215337; 17215375; 17215524; 17217140; 17227821; 17237409; 17238853; 17257312; 17261759; 17262717; 17266440; 17276141; 17300840; 17301401; 17304101; 17347451; 17348243; 17355643; 17363708; 17363736; 17373677; 17376993; 17388919; 17392024; 17392368; 17405833; 17441979; 17444864; 17454884; 17456233; 17470541; 17477815; 17495004; 17498265; 17509455; 17521325; 17521731; 17532201; 17544674; 17546485; 17552041; 17553352; 17566759; 17572155; 17582674; 17600593; 17612762; 17613714; 17627763; 17640674; 17641021; 17641061; 17654453; 17655693; 17656678; 17674321; 17682837; 17697145; 17697357; 17700165; 17703412; 17709420; 17713715; 17714919; 17719815; 17728221; 17765942; 17786190; 17827383; 17845304; 17846855; 17852079; 17875674; 17878156; 17885647; 17889143; 17900510; 17911610; 17916356; 17922402; 17936906; 17937104; 17940602; 17947510; 17953379; 17960405; 17974504; 17976320; 17981204; 17986123; 17986321; 17988266; 17988330; 17989610; 17994425; 17996064; 18039196; 18041006; 18051824; 18056971; 18062835; 18062910; 18070901; 18077789; 18091521; 18158121; 18174230; 18174256; 18174382; 18192275; 18199488; 18199828; 18199975; 18205804; 18209080; 18209488; 18230112; 18249037; 18263601; 18266836; 18275276; 18275349; 18276105; 18279717; 18286551; 18287876; 18287963; 18300036; 18300344; 18307517; 18312596; 18322182; 18332247; 18337305; 18339625; 18339897; 18361934; 18361939; 18365030; 18366487; 18368485; 18373975; 18375019; 18385742; 18385764; 18388182; 18388249; 18390192; 18394346; 18410260; 18414664; 18414898; 18417583; 18426658; 18476609; 18485114; 18497880; 18501882; 18502564; 18506884; 18512784; 18514317; 18519231; 18521569; 18522869; 18525269; 18533937; 18539368; 18547161; 18548239; 18550653; 18556463; 18560378; 18560870; 18568448; 18569454; 18571695; 18572307; 18576303; 18579762; 18580959; 18582197; 18589089; 18593330; 18593367; 18600325; 18614592; 18620489; 18627514; 18632425; 18633131; 18633332; 18639520; 18641361; 18655181; 18660489; 18663124; 18670216; 18672993; 18676680; 18678243; 18678988; 18680515; 18684979; 18693134; 18708162; 18708672; 18712791; 18773331; 18776133; 18787531; 18789440; 18792803; 18793716; 18793860; 18802076; 18802113; 18805021; 18806746; 18818748; 18820938; 18832710; 18842170; 18843763; 18923705; 18932275; 18937577; 18941172; 18945465; 18945831; 18953482; 18972297; 18976633; 18989229; 19005292; 19010294; 19012493; 19019335; 19031096; 19058987; 19065267; 19066394; 19071156; 19074829; 19074885; 19089914; 19089920; 19091593; 19095736; 19096039; 19101991; 19109132; 19116009; 19117745; 19121222; 19122650; 19122664; 19124156; 19126646; 19129484; 19135418; 19141860; 19149916; 19152246; 19155099; 19160541; 19168733; 19170196; 19172849; 19177264; 19189859; 19190772; 19192232; 19199539; 19200845; 19207121; 19210359; 19225954; 19227440; 19231233; 19232001; 19236347; 19247692; 19250279; 19254267; 19255340; 19258311; 19258593; 19258635; 19258923; 19264674; 19264973; 19269302; 19269948; 19274101; 19279332; 19279357; 19289181; 19297619; 19306922; 19317046; 19332120; 19336263; 19336370; 19336475; 19339796; 19340290; 19358670; 19370405; 19372249; 19372459; 19375805; 19386363; 19386798; 19401385; 19403671; 19408823; 19419945; 19426601; 19427704; 19428330; 19437232; 19450146; 19450149; 19457071; 19458616; 19461480; 19470040; 19472212; 19479051; 19480854; 19481774; 19488421; 19489682; 19495883; 19505916; 19508433; 19527514; 19536281; 19543959; 19547871; 19552791; 19559726; 19586939; 19592490; 19594368; 19596857; 19597472; 19608431; 19622834; 19625176; 19626047; 19634484; 19639725; 19642044; 19652739; 19657406; 19665935; 19681846; 19682920; 19683555; 19692168; 19696431; 19706920; 19707556; 19710464; 19723394; 19727876; 19729799; 19733878; 19735490; 19747638; 19756986; 19757192; 19757302; 19759281; 19765856; 19766898; 19768696; 19773451; 19773677; 19789190; 19796538; 19813110; 19818655; 19822083; 19822293; 19840475; 19858302; 19860911; 19861015; 19861016; 19879772; 19890236; 19893204; 19913121; 19913506; 19917178; 19918044; 19919944; 19929378; 19934306; 19934811; 19938203; 19938975; 19940027; 19941336; 19948975; 19958312; 19959217; 19960790; 20001857; 20004112; 20004979; 20008289; 20027291; 20028654; 20030937; 20038203; 20055726; 20056084; 20059579; 20061995; 20067407; 20082482; 20097948; 20100010; 20105444; 20110463; 20123968; 20130213; 20131287; 20145925; 20154512; 20167631; 20177758; 20178622; 20186935; 20194818; 20196868; 20207982; 20213229; 20217044; 20228669; 20228799; 20230666; 20231691; 20231901; 20237496; 20303284; 20305143; 20331378; 20331838; 20345984; 20348497; 20349753; 20353805; 20359550; 20367137; 20368273; 20368278; 20370995; 20375623; 20379614; 20381453; 20388088; 20394835; 20404426; 20415786; 20418110; 20419805; 20443055; 20453000; 20477883; 20482522; 20484443; 20484656; 20484876; 20485444; 20503287; 20504369; 20510064; 20511558; 20525893; 20530519; 20531015; 20533927; 20535218; 20544370; 20565368; 20574006; 20580745; 20581146; 20586818; 20587546; 20587610; 20588103; 20588308; 20596075; 20603050; 20625487; 20628086; 20636896; 20640364; 20644110; 20653995; 20655098; 20665551; 20666952; 20685939; 20696832; 20711808; 20714752; 20720198; 20720222; 20720564; 20722470; 20726231; 20732366; 20799037; 20808133; 20809185; 20811626; 20814675; 20817868; 20821074; 20825427; 20828526; 20839488; 20848535; 20849534; 20875052; 20883321; 20888416; 20889558; 20889566; 20932510; 20934357; 20939703; 20949125; 20953611; 20958339; 20959405; 20960273; 20974954; 20974955; 20979795; 20980339; 21037509; 21061434; 21067601; 21078084; 21082024; 21084489; 21085635; 21086908; 21090238; 21094940; 21099673; 21112094; 21115099; 21117871; 21127885; 21127993; 21132384; 21149447; 21161299; 21167738; 21168725; 21179438; 21183733; 21189447; 21196650; 21199896; 21204904; 21211989; 21215074; 21215285; 21224476; 21226554; 21229844; 21239188; 21248298; 21271775; 21281983; 21282066; 21288140; 21297633; 21323572; 21323660; 21332391; 21334249; 21368230; 21381020; 21385594; 21403886; 21418620; 21423578; 21427975; 21430066; 21433155; 21440743; 21441456; 21458658; 21470497; 21477169; 21487893; 21491089; 21493784; 21505270; 21510811; 21515918; 21531896; 21533215; 21540006; 21562161; 21562768; 21572044; 21586573; 21591983; 21613464; 21622562; 21641233; 21649525; 21658970; 21659535; 21669226; 21688665; 21703188; 21711552; 21712100; 21719187; 21721104; 21724697; 21725055; 21728784; 21729551; 21752694; 21755390; 21772053; 21774972; 21778700; 21798578; 21798758; 21802664; 21805152; 21819478; 21829141; 21847627; 21857377; 21858117; 21864611; 21872231; 21873264; 21917128; 21926633; 21930700; 21931651; 21937453; 21940994; 21949691; 21962843; 21966356; 21966367; 22037448; 22041017; 22045868; 22057682; 22058328; 22069319; 22075702; 22079980; 22095765; 22117500; 22137120; 22140472; 22143036; 22163006; 22172723; 22189538; 22194871; 22221541; 22226324; 22228808; 22263663; 22268679; 22283891; 22323453; 22325340; 22327783; 22350281; 22358381; 22378844; 22385244; 22392581; 22395607; 22410067; 22410761; 22416258; 22422499; 22426116; 22444955; 22447512; 22465880; 22466287; 22474288; 22484483; 22487478; 22496218; 22526675; 22554587; 22564607; 22587568; 22610275; 22622197; 22623148; 22624006; 22647601; 22672824; 22673732; 22677194; 22683002; 22684265; 22685317; 22691562; 22698804; 22699677; 22704696; 22706089; 22711893; 22718836; 22727646; 22731611; 22738830; 22740319; 22748084; 22749533; 22753928; 22757586; 22759859; 22766105; 22767256; 22778764; 22784413; 22805115; 22809599; 22814515; 22815836; 22824211; 22826629; 22847200; 22851706; 22880090; 22882906; 22885102; 22896630; 22898392; 22924705; 22932225; 22952667; 22983442; 22983646; 22986484; 22992806; 23028695; 23040881; 23045477; 23061992; 23071273; 23077565; 23101722; 23107828; 23125442; 23128233; 23133532; 23133672; 23139419; 23152883; 23159874; 23179933; 23185315; 23213275; 23223131; 23224615; 23240025; 23243276; 23252864; 23253667; 23255246; 23259293; 23265966; 23271704; 23280240; 23289765; 23295883; 23321919; 23343479; 23349093; 23359533; 23362867; 23378427; 23388331; 23401468; 23404187; 23412855; 23416458; 23449998; 23460743; 23461851; 23462597; 23487038; 23507374; 23582260; 23592910; 23632060; 23638863; 23639073; 23685791; 23692034; 23711712; 23720660; 23737189; 23740952; 23785756; 23786562; 23793505; 23803376; 23806637; 23811275; 23857000; 23874969; 23880295; 23891168; 23901078; 23998448; 24012417; 24055710; 24088808; 24140406; 24313836; 24459820 interferon, gamma Ensembl:ENSG00000111537 HGNC:5438 HPRD:00957 MIM:147570 Vega:OTTHUMG00000169113 Other designations: IFN-gamma|immune interferon|interferon gamma IFNG OGG:3000003484 Bin Zhao, Yue Liu, Oliver He AFBP IBP1 IGF-BP25 PP12 hIGFBP-1 WEB: http://www.ncbi.nlm.nih.gov/gene IGFBP1 insulin-like growth factor binding protein 1 3484 tcag7.702 7p13-p12 9606 7 GO_0005520 (EC: IEA); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0006987 (EC: TAS); GO_0007165 (EC: TAS, PMID:2454104); GO_0008286 (EC: IEA); GO_0030307 (EC: IEA); GO_0030968 (EC: TAS); GO_0042246 (EC: IEA); GO_0044267 (EC: TAS) PMID:1373120; 1691735; 1701175; 1718783; 2454104; 2457513; 2458522; 2461294; 2466665; 2474129; 2478445; 2849945; 2971653; 3419931; 7504269; 7678248; 7683522; 7683525; 7694877; 8754754; 9408744; 10329650; 10350456; 10352394; 10364674; 10407151; 10691413; 10810289; 10965886; 10987657; 11050672; 11297622; 11397868; 11752456; 11762714; 11793026; 11834727; 11956162; 11969341; 11972304; 12006706; 12082253; 12119297; 12135130; 12150454; 12153746; 12163461; 12351482; 12466191; 12477932; 12489207; 12493691; 12519841; 12556485; 12571183; 12679458; 12690205; 12746292; 12746836; 12843178; 12843192; 12853948; 12861174; 12870155; 12882925; 12933666; 14568572; 14624764; 14715837; 14718574; 14726451; 14764802; 15070833; 15070959; 15166120; 15489334; 15598684; 15613433; 15736102; 15797461; 15890677; 15959422; 15972819; 15987820; 15987847; 16002526; 16041536; 16118248; 16222695; 16293667; 16306374; 16337840; 16338475; 16404426; 16687408; 16776662; 16809446; 16868142; 16924115; 16973813; 17035411; 17062566; 17113753; 17164371; 17264182; 17300730; 17341623; 17465992; 17485842; 17566087; 17634530; 17640761; 17655506; 17803702; 17890489; 17914103; 17972051; 17972510; 18166823; 18259111; 18305566; 18496669; 18513511; 18596909; 18636124; 18665784; 18676680; 18701096; 18772238; 18793810; 18828733; 18924579; 19064572; 19124510; 19158202; 19170196; 19193607; 19308628; 19434535; 19453261; 19463807; 19539506; 19551864; 19625176; 19692168; 19730683; 19732896; 19765076; 19843326; 19858071; 19913121; 19917654; 19948975; 20039319; 20102313; 20143870; 20144192; 20149700; 20155489; 20413521; 20416304; 20453000; 20484221; 20587581; 20628086; 20634197; 20637724; 20711952; 20731527; 20734064; 20810604; 20884247; 20885978; 21078522; 21104586; 21140206; 21198359; 21212012; 21247237; 21378090; 21457161; 21521316; 21741060; 21852217; 21892205; 21930730; 21933314; 21940708; 22072736; 22104117; 22113073; 22187946; 22239027; 22325929; 22357965; 22442270; 22554827; 22745191; 22843786; 22894543; 23095194; 23190203; 23354097; 23377640; 23408645; 23585335; 23603247; 23815140; 23942851; 24132762; 24248464 insulin-like growth factor binding protein 1 Ensembl:ENSG00000146678 HGNC:5469 HPRD:00897 MIM:146730 Vega:OTTHUMG00000152343 Other designations: IBP-1|IGF-binding protein 1|IGFBP-1|alpha-pregnancy-associated endometrial globulin|amniotic fluid binding protein|binding protein-25|binding protein-26|binding protein-28|growth hormone independent-binding protein|insulin-like growth factor-binding protein 1|placental protein 12 IGFBP1 OGG:3000003485 Bin Zhao, Yue Liu, Oliver He IBP2 IGF-BP53 WEB: http://www.ncbi.nlm.nih.gov/gene IGFBP2 insulin-like growth factor binding protein 2, 36kDa 3485 2q33-q34 9606 2 GO_0001558 (EC: IEA); GO_0005515 (EC: IPI, PMID:19095771); GO_0005576 (EC: ISS); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID:15694994); GO_0007165 (EC: IEA); GO_0007565 (EC: IEA); GO_0007568 (EC: IEA); GO_0007584 (EC: IEA); GO_0009612 (EC: IEA); GO_0010226 (EC: IEA); GO_0016324 (EC: IEA); GO_0031410 (EC: IEA); GO_0031994 (EC: IDA, PMID:19081843); GO_0031995 (EC: ISS); GO_0032355 (EC: IEA); GO_0032526 (EC: IEA); GO_0032870 (EC: IEA); GO_0042104 (EC: IDA, PMID:15694994); GO_0042493 (EC: IEA); GO_0043567 (EC: IC, PMID:19081843); GO_0043567 (EC: ISS); GO_0044267 (EC: TAS); GO_0051384 (EC: IEA) PMID:1376411; 1380437; 1697583; 1710112; 1712312; 1714916; 1716260; 1726837; 2465304; 2479552; 7511544; 7680905; 8675597; 8781553; 9156044; 9408744; 10407151; 10912521; 11063745; 11297622; 11358513; 12006706; 12102164; 12477932; 12519841; 12575534; 12672024; 12727212; 12794762; 12810534; 12839944; 12907597; 12955485; 14691340; 14710363; 14744083; 15147770; 15171717; 15489334; 15643522; 15651061; 15661050; 15686601; 15694994; 15735679; 15932773; 15956340; 15994346; 16183342; 16306230; 16444283; 16543235; 16569642; 16884361; 16893667; 16901920; 17020769; 17071580; 17072950; 17102589; 17113753; 17280861; 17285230; 17289850; 17341887; 17352648; 17369847; 17372210; 17395163; 17475624; 17485236; 17606927; 17655506; 17827400; 17970029; 17985932; 18210030; 18210156; 18217408; 18259111; 18373644; 18437351; 18461161; 18524796; 18556354; 18676680; 18952587; 18953566; 18980989; 19064572; 19081843; 19095771; 19124510; 19127217; 19164435; 19170196; 19276395; 19324937; 19453261; 19625176; 19679880; 19692168; 19764562; 19843326; 19845745; 19846739; 19862325; 19877176; 19948975; 19956906; 19962924; 20150439; 20306690; 20370577; 20468064; 20514406; 20515648; 20541521; 20634197; 20730703; 20731527; 20734064; 20810604; 20819778; 20858761; 21304397; 21339190; 21899885; 21951978; 21972778; 21988832; 22242132; 22253890; 22277732; 22293585; 22345562; 22459634; 22527168; 22554827; 22555360; 22571677; 22623219; 22672618; 22869145; 23071652; 23165420; 23233738; 23291564; 23397525; 23435424; 23515291; 23714241; 23767917; 23959956 insulin-like growth factor binding protein 2, 36kDa Ensembl:ENSG00000115457 HGNC:5471 HPRD:00898 MIM:146731 Vega:OTTHUMG00000155341 Other designations: IBP-2|IGF-binding protein 2|IGFBP-2|insulin-like growth factor-binding protein 2 IGFBP2 OGG:3000003486 Bin Zhao, Yue Liu, Oliver He BP-53 IBP3 WEB: http://www.ncbi.nlm.nih.gov/gene IGFBP3 insulin-like growth factor binding protein 3 3486 tcag7.703 7p13-p12 9606 7 GO_0001558 (EC: IEA); GO_0001933 (EC: IDA, PMID:17591901); GO_0001968 (EC: IEA); GO_0005515 (EC: IPI, PMID:14561895); GO_0005520 (EC: NAS, PMID:12599210); GO_0005576 (EC: NAS, PMID:14718574); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID:17119061); GO_0005634 (EC: IDA, PMID:17434920); GO_0006468 (EC: IDA, PMID:17434920); GO_0006915 (EC: IEA); GO_0008160 (EC: IDA, PMID:11940579); GO_0008285 (EC: IGI, PMID:19258508); GO_0009968 (EC: NAS, PMID:11940579); GO_0010906 (EC: IEA); GO_0014912 (EC: IDA, PMID:10766744); GO_0016942 (EC: IC, PMID:10766744); GO_0031994 (EC: IPI, PMID:10766744); GO_0043065 (EC: IMP, PMID:11971816); GO_0043085 (EC: IDA, PMID:11940579); GO_0043410 (EC: IEA); GO_0043568 (EC: IEA); GO_0044267 (EC: TAS); GO_0044342 (EC: IEA); GO_0045663 (EC: IDA, PMID:12599210); GO_0046872 (EC: NAS, PMID:14576163); GO_0048662 (EC: IDA, PMID:10766744) PMID:1280211; 1293182; 1373120; 1383255; 1695633; 1697583; 2464130; 7508771; 7523391; 7538844; 7566179; 8550744; 8675597; 8708531; 8843739; 8964576; 9252371; 9275067; 9337997; 9388210; 9389554; 9408744; 9446566; 9497324; 9688635; 10076184; 10218588; 10226805; 10352394; 10407151; 10511594; 10512690; 10650937; 10766744; 10770214; 10811646; 10823924; 10849447; 10874028; 11095942; 11238520; 11264294; 11297622; 11319179; 11344214; 11375929; 11600567; 11749962; 11751851; 11762714; 11784719; 11801256; 11804742; 11886859; 11914023; 11914026; 11940579; 11948969; 11953210; 11959812; 11971816; 11997031; 12006706; 12011225; 12051736; 12054563; 12068000; 12111701; 12122101; 12127836; 12135130; 12150454; 12163384; 12200149; 12210764; 12213898; 12219010; 12220677; 12242693; 12473575; 12477932; 12506097; 12508918; 12519841; 12571183; 12571851; 12575534; 12590636; 12599210; 12690205; 12725526; 12730416; 12735930; 12810533; 12810534; 12853948; 12865482; 12870155; 12907612; 12925957; 12926118; 12937269; 12962157; 14561895; 14576163; 14576164; 14597676; 14598881; 14644829; 14674122; 14693733; 14702039; 14710345; 14718574; 14744783; 14751238; 14760718; 15014034; 15047131; 15059907; 15066922; 15067329; 15069073; 15070968; 15086466; 15126567; 15140235; 15178549; 15198293; 15221971; 15247132; 15247904; 15282325; 15298948; 15302288; 15340161; 15379965; 15448002; 15485880; 15489334; 15517912; 15625284; 15641262; 15641264; 15642160; 15642732; 15651061; 15661050; 15668470; 15681824; 15703779; 15734965; 15769996; 15781645; 15800934; 15802501; 15809062; 15817480; 15844718; 15894673; 15894694; 15927849; 15941947; 15959422; 15986122; 15987847; 16015705; 16030120; 16049980; 16169070; 16181731; 16189247; 16189260; 16210470; 16211216; 16215864; 16275148; 16303743; 16306136; 16322329; 16335952; 16394092; 16404426; 16448675; 16455777; 16489075; 16489531; 16540651; 16541420; 16543235; 16552541; 16614079; 16617154; 16645643; 16723126; 16763062; 16775172; 16776662; 16793770; 16825320; 16887362; 16915540; 16935391; 16965600; 16969385; 17018785; 17035411; 17044098; 17047053; 17051426; 17056474; 17063263; 17070193; 17085968; 17096329; 17113753; 17119061; 17172410; 17187018; 17210081; 17237715; 17264182; 17287408; 17289909; 17293864; 17297462; 17300730; 17350302; 17388800; 17396438; 17434446; 17434920; 17446556; 17447118; 17453001; 17457048; 17546465; 17555512; 17560154; 17566087; 17567756; 17577982; 17591901; 17593323; 17597108; 17624927; 17627014; 17635417; 17655506; 17668637; 17689128; 17719815; 17724372; 17761791; 17763192; 17803702; 17823260; 17827406; 17879951; 17912004; 17952116; 17957164; 17959403; 17972510; 17997337; 18006928; 18031946; 18059035; 18084616; 18162523; 18163429; 18171112; 18177247; 18178497; 18259111; 18287864; 18329388; 18335323; 18375957; 18398029; 18410545; 18450319; 18459102; 18471292; 18481170; 18498652; 18534134; 18562769; 18596909; 18602100; 18615538; 18618736; 18624627; 18636124; 18676680; 18812263; 18818748; 18929499; 18984657; 18992148; 18992263; 19004037; 19019335; 19020726; 19036873; 19064126; 19064572; 19077426; 19121847; 19124506; 19124510; 19127217; 19129715; 19138871; 19158946; 19170196; 19190540; 19194113; 19207313; 19217707; 19223521; 19240240; 19257984; 19258508; 19332270; 19414355; 19449212; 19453261; 19455605; 19477944; 19491931; 19492232; 19509068; 19527514; 19540231; 19551141; 19551864; 19556345; 19568604; 19588500; 19591553; 19596932; 19625176; 19633297; 19634593; 19672706; 19692168; 19734278; 19764562; 19784788; 19786462; 19786971; 19789190; 19800385; 19833751; 19845745; 19846909; 19858071; 19863750; 19913121; 19917654; 19919528; 19938081; 19941883; 19944347; 19948975; 19960406; 20003326; 20023704; 20039319; 20051649; 20084546; 20099974; 20102313; 20119675; 20121533; 20144192; 20145156; 20155489; 20204283; 20215856; 20219400; 20228135; 20302654; 20307522; 20350746; 20357812; 20378848; 20403354; 20416304; 20423985; 20427254; 20453000; 20468064; 20484221; 20501753; 20513670; 20540360; 20580999; 20587610; 20599318; 20613589; 20628086; 20628624; 20634197; 20677014; 20731527; 20734064; 20801067; 20810604; 20848532; 20851879; 20860465; 20884247; 20889360; 20920870; 20921904; 20945273; 21068693; 21076409; 21078522; 21140206; 21195059; 21216879; 21254935; 21347663; 21378090; 21383009; 21388950; 21392749; 21435441; 21447628; 21447640; 21455575; 21471542; 21474793; 21478207; 21520041; 21520165; 21521316; 21525788; 21529443; 21536375; 21536469; 21551235; 21562710; 21585623; 21636299; 21648284; 21697095; 21698457; 21701930; 21737444; 21761353; 21788435; 21823995; 21852217; 21892705; 21898383; 21930730; 21944866; 22001433; 22004906; 22026507; 22032863; 22085490; 22113073; 22128038; 22167391; 22246875; 22253890; 22278433; 22318747; 22328165; 22332214; 22347413; 22363400; 22381038; 22389159; 22415309; 22415807; 22441125; 22442270; 22475139; 22494072; 22500655; 22527168; 22543588; 22554827; 22565227; 22643116; 22739332; 22745191; 22751133; 22778398; 22801219; 22847383; 22879989; 22882716; 22884472; 22892437; 22894543; 22936258; 22951368; 23011725; 23041555; 23158139; 23174226; 23178489; 23185474; 23341348; 23348700; 23377640; 23383064; 23498137; 23527244; 23527725; 23592916; 23611528; 23619263; 23720424; 23748063; 23770368; 23789983; 23792502; 23831640; 23864804; 23962053; 24022308; 24250222 insulin-like growth factor binding protein 3 Ensembl:ENSG00000146674 HGNC:5472 HPRD:00899 MIM:146732 Vega:OTTHUMG00000023769 Other designations: IBP-3|IGF-binding protein 3|IGFBP-3|acid stable subunit of the 140 K IGF complex|binding protein 29|binding protein 53|growth hormone-dependent binding protein|insulin-like growth factor-binding protein 3 IGFBP3 OGG:3000003487 Bin Zhao, Yue Liu, Oliver He BP-4 HT29-IGFBP IBP4 IGFBP-4 WEB: http://www.ncbi.nlm.nih.gov/gene IGFBP4 insulin-like growth factor binding protein 4 3487 17q12-q21.1 9606 17 GO_0001501 (EC: TAS, PMID:1377672); GO_0001558 (EC: IEA); GO_0005520 (EC: IEA); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0006259 (EC: TAS, PMID:1377672); GO_0006954 (EC: IEA); GO_0007165 (EC: TAS, PMID:1377672); GO_0008283 (EC: TAS, PMID:1377672); GO_0010906 (EC: IEA); GO_0043410 (EC: IEA); GO_0043568 (EC: IEA); GO_0044267 (EC: TAS); GO_0044342 (EC: IEA) PMID:1370941; 1375185; 1377672; 1380437; 1704481; 1707125; 1709161; 1709585; 7507078; 7511544; 7680905; 7683646; 7689953; 7778269; 8648179; 8889548; 8964576; 9138096; 9275067; 9408744; 9615225; 9722589; 9751498; 10407151; 11052994; 11068878; 11297622; 12163000; 12193384; 12241545; 12477932; 12733722; 12904166; 12970325; 14705967; 14767471; 14996716; 15062981; 15146197; 15146551; 15204833; 15489334; 15661050; 16540175; 16586492; 16685432; 16924115; 16973813; 17070193; 17071580; 17177834; 17312271; 17824980; 19025658; 19038974; 19453261; 19956906; 20628624; 20634197; 20654748; 20734064; 20810604; 21166939; 21207373; 21274331; 22134921; 22246875; 22332214; 22689691; 23079385; 23455924; 23499909; 23563607; 23603559 insulin-like growth factor binding protein 4 Ensembl:ENSG00000141753 HGNC:5473 HPRD:00900 MIM:146733 Vega:OTTHUMG00000133326 Other designations: IBP-4|IGF-binding protein 4|insulin-like growth factor-binding protein 4 IGFBP4 OGG:3000003488 Bin Zhao, Yue Liu, Oliver He IBP5 WEB: http://www.ncbi.nlm.nih.gov/gene IGFBP5 insulin-like growth factor binding protein 5 3488 2q33-q36 9606 2 GO_0001558 (EC: IEA); GO_0001649 (EC: IEA); GO_0001968 (EC: IEA); GO_0005515 (EC: IPI, PMID:15700281); GO_0005576 (EC: NAS, PMID:14718574); GO_0005576 (EC: TAS); GO_0006006 (EC: IEA); GO_0007165 (EC: NAS, PMID:7525452); GO_0010906 (EC: IEA); GO_0014912 (EC: IDA, PMID:10766744); GO_0016942 (EC: IC, PMID:10766744); GO_0017148 (EC: IDA, PMID:15700281); GO_0030336 (EC: IDA, PMID:15700281); GO_0031069 (EC: IEA); GO_0031994 (EC: IPI, PMID:10766744); GO_0035556 (EC: IEA); GO_0042593 (EC: IEA); GO_0043568 (EC: IEA); GO_0043569 (EC: IDA, PMID:10766744); GO_0044267 (EC: TAS); GO_0044342 (EC: IEA); GO_0045668 (EC: IEA); GO_0048630 (EC: IEA); GO_0048662 (EC: IDA, PMID:10766744); GO_0051146 (EC: IEA); GO_0051897 (EC: IEA); GO_0060056 (EC: IEA); GO_0071320 (EC: IDA, PMID:7559606); GO_0071407 (EC: IDA, PMID:7559606) PMID:1147105; 1709938; 1710112; 1850257; 1850258; 7511544; 7511611; 7525452; 7559606; 8619474; 8817691; 9110174; 9202242; 9497324; 9528953; 9786878; 9822601; 9883900; 10336724; 10407151; 10698186; 10766744; 10811646; 11095942; 11264294; 11297622; 11751588; 11821401; 11874691; 11905402; 11923300; 11973331; 12005306; 12466191; 12477932; 12766061; 12777377; 12810534; 14645245; 14718574; 15001525; 15140223; 15155755; 15489334; 15534875; 15618969; 15650232; 15661050; 15681824; 15700281; 15777798; 15780948; 15802501; 15930103; 16007340; 16169070; 16195401; 16311053; 16344560; 16543235; 16716263; 16865675; 17067554; 17071587; 17242174; 17290407; 17312271; 17316888; 17496250; 17595320; 17651454; 17804819; 17823924; 17892529; 18085517; 18161051; 18210156; 18311789; 18373644; 18602100; 18624948; 18665784; 18676680; 18710598; 18762576; 18775916; 18805800; 18809517; 18957933; 19170196; 19250630; 19341485; 19453261; 19476635; 19610136; 19625176; 19628764; 19692168; 19808657; 19843326; 19877176; 19948051; 19950226; 20345844; 20354179; 20379614; 20416304; 20468064; 20508032; 20583135; 20628624; 20634197; 20734064; 20810604; 20819778; 20944648; 20949447; 21029365; 21191810; 21256825; 21460855; 21852217; 22246875; 22252554; 22328518; 22571677; 22589738; 23408906; 23499909; 23539739; 23576565; 23665505 insulin-like growth factor binding protein 5 Ensembl:ENSG00000115461 HGNC:5474 HPRD:00901 MIM:146734 Vega:OTTHUMG00000133058 Other designations: IBP-5|IGF-binding protein 5|IGFBP-5|insulin-like growth factor-binding protein 5 IGFBP5 OGG:3000003489 Bin Zhao, Yue Liu, Oliver He IBP6 WEB: http://www.ncbi.nlm.nih.gov/gene IGFBP6 insulin-like growth factor binding protein 6 3489 12q13 9606 12 GO_0001558 (EC: IEA); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0005794 (EC: IEA); GO_0007165 (EC: NAS, PMID:10087296); GO_0008285 (EC: TAS, PMID:7539002); GO_0031994 (EC: IEA); GO_0044267 (EC: TAS) PMID:1697583; 1709161; 1719383; 1850257; 1850258; 2154495; 2551732; 7511544; 7539002; 7683540; 7683646; 7692907; 9572875; 10087296; 10329650; 10407151; 10414596; 11267670; 11297622; 11914024; 12006706; 12477932; 12558805; 14710364; 15308688; 15366928; 15489334; 15661050; 15797461; 15889232; 16713569; 17519236; 17978469; 18039785; 18395833; 18676680; 18724896; 18957410; 18982452; 18985860; 19170196; 19453261; 19625176; 19692168; 19913121; 19950226; 20432455; 20628086; 20634197; 20734064; 20810604; 21054968; 21458526; 21548981; 21618524; 21820463; 21940310; 21997736; 23126425; 23623986; 24003225 insulin-like growth factor binding protein 6 Ensembl:ENSG00000167779 HGNC:5475 HPRD:00902 MIM:146735 Vega:OTTHUMG00000169773 Other designations: IBP-6|IGF binding protein 6|IGF-binding protein 6|IGFBP-6|insulin-like growth factor-binding protein 6 IGFBP6 OGG:3000003490 Bin Zhao, Yue Liu, Oliver He AGM FSTL2 IBP-7 IGFBP-7 IGFBP-7v IGFBPRP1 MAC25 PSF RAMSVPS TAF WEB: http://www.ncbi.nlm.nih.gov/gene IGFBP7 insulin-like growth factor binding protein 7 3490 4q12 9606 4 GO_0001558 (EC: IEA); GO_0005515 (EC: IPI, PMID:9388210); GO_0005520 (EC: IEA); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA); GO_0007155 (EC: IDA, PMID:8117260); GO_0007566 (EC: IEA); GO_0008285 (EC: TAS, PMID:8939990); GO_0009408 (EC: IEA); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0032526 (EC: IEA); GO_0032870 (EC: IEA); GO_0048839 (EC: IEA); GO_0050810 (EC: IEA); GO_0051414 (EC: IEA) PMID:7538673; 7694637; 7980422; 8117260; 8939990; 9100611; 9313760; 9388210; 10502291; 10595934; 10820148; 10859029; 10985926; 11549700; 12065244; 12407018; 12477932; 12592389; 12679483; 12843194; 12847218; 14521955; 14633696; 15077158; 15340161; 15489334; 15708897; 16302002; 16873698; 17048309; 17136345; 17312390; 17465992; 17972510; 18160415; 18267069; 18711401; 18981723; 19019211; 19374835; 19542015; 19638426; 19710688; 19829302; 19919630; 20029996; 20407444; 20433702; 20440262; 20464481; 20478260; 20535151; 20599521; 20977730; 21040219; 21095038; 21139048; 21328580; 21413833; 21525788; 21562573; 21835307; 21908579; 21909106; 21988832; 22005787; 22173745; 22277373; 22383111; 22392074; 22544761; 22622471; 22750143; 22906661; 22939629; 23250396; 23381221; 23382691; 23543219; 23546957; 23600329; 23713052 insulin-like growth factor binding protein 7 Ensembl:ENSG00000163453 HGNC:5476 HPRD:04183 MIM:602867 Other designations: IGF-binding protein 7|IGFBP-rP1|PGI2-stimulating factor|angiomodulin|insulin-like growth factor-binding protein 7|prostacyclin-stimulating factor|tumor-derived adhesion factor IGFBP7 OGG:3000003491 Bin Zhao, Yue Liu, Oliver He CCN1 GIG1 IGFBP10 WEB: http://www.ncbi.nlm.nih.gov/gene CYR61 cysteine-rich, angiogenic inducer, 61 3491 1p22.3 9606 1 GO_0001558 (EC: IEA); GO_0001649 (EC: IEA); GO_0001934 (EC: IDA); GO_0002041 (EC: IEA); GO_0003181 (EC: IEA); GO_0003278 (EC: IEA); GO_0003281 (EC: IEA); GO_0005178 (EC: IEA); GO_0005520 (EC: IEA); GO_0005576 (EC: IEA); GO_0006935 (EC: IEA); GO_0008201 (EC: IEA); GO_0008283 (EC: TAS, PMID:9135077); GO_0009653 (EC: TAS, PMID:9135077); GO_0010518 (EC: IEA); GO_0010811 (EC: IEA); GO_0030198 (EC: IEA); GO_0030335 (EC: IDA); GO_0030513 (EC: IGI); GO_0033690 (EC: IDA); GO_0043065 (EC: IEA); GO_0043066 (EC: IEA); GO_0043280 (EC: IEA); GO_0044319 (EC: IDA); GO_0045669 (EC: IDA); GO_0045860 (EC: IDA); GO_0045944 (EC: IDA); GO_0050840 (EC: IEA); GO_0060413 (EC: IEA); GO_0060591 (EC: IEA); GO_0060710 (EC: IEA); GO_0060716 (EC: IEA); GO_0061036 (EC: IEA); GO_0070372 (EC: IDA); GO_0072593 (EC: IEA); GO_2000304 (EC: IEA) PMID:8125298; 8635876; 9135077; 9446626; 9488038; 9528960; 9536281; 9600969; 10446209; 10821835; 10852911; 11120741; 11287419; 11584015; 11600415; 11751417; 11810026; 11840342; 12036876; 12217894; 12364323; 12374462; 12444554; 12477932; 12736251; 12826661; 12831056; 12899698; 12939282; 14702039; 14988385; 15041728; 15044484; 15044605; 15053922; 15077166; 15389821; 15471875; 15489334; 15526358; 15564459; 15592521; 15782120; 15878827; 15961723; 16243794; 16344560; 16581771; 16675545; 16804865; 16877350; 17056474; 17234971; 17314511; 17361185; 17429007; 17437852; 17579708; 17601910; 17626014; 17673559; 17699553; 17718860; 17765657; 18004727; 18025257; 18058471; 18089610; 18202125; 18212329; 18381294; 18575751; 18599605; 18687805; 18800188; 18819928; 18936953; 18941464; 18950845; 19007976; 19147534; 19180570; 19244129; 19288017; 19364818; 19542562; 19584265; 19632997; 19950293; 20010302; 20043874; 20056838; 20097175; 20195466; 20233866; 20237132; 20237496; 20360068; 20531301; 20628624; 20641097; 21081514; 21138874; 21139048; 21153366; 21159247; 21212405; 21232118; 21249313; 21312266; 21349946; 21393426; 21397653; 21447598; 21488975; 21505992; 21601497; 21618249; 21628462; 21711965; 21963094; 21976359; 21995436; 22023263; 22025384; 22056874; 22160564; 22253074; 22363611; 22401280; 22527715; 22532143; 22540002; 22547695; 22551568; 22566095; 22692860; 22694338; 22752926; 22797925; 23027863; 23045290; 23141184; 23196056; 23259998; 23316072; 23504324; 23528710; 23618859; 23623839; 23667531; 23744557; 23798676; 24449575 cysteine-rich, angiogenic inducer, 61 Ensembl:ENSG00000142871 HGNC:2654 HPRD:09089 MIM:602369 Vega:OTTHUMG00000010577 Other designations: CCN family member 1|IBP-10|IGF-binding protein 10|IGFBP-10|cysteine-rich heparin-binding protein 61|cysteine-rich, anigogenic inducer, 61|insulin-like growth factor-binding protein 10|protein CYR61 CYR61 OGG:3000003551 Bin Zhao, Yue Liu, Oliver He IKK-beta IKK2 IKKB IMD15 NFKBIKB WEB: http://www.ncbi.nlm.nih.gov/gene IKBKB inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase beta 3551 8p11.2 9606 8 GO_0001782 (EC: IEA); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0004672 (EC: IDA); GO_0004674 (EC: TAS); GO_0005515 (EC: IPI, PMID:10521409); GO_0005524 (EC: IEA); GO_0005634 (EC: IEA); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006468 (EC: IDA); GO_0006468 (EC: NAS, PMID:9346484); GO_0006954 (EC: TAS, PMID:18626576); GO_0007249 (EC: TAS, PMID:18626576); GO_0007252 (EC: TAS, PMID:18626576); GO_0008384 (EC: TAS, PMID:18626576); GO_0008385 (EC: TAS, PMID:18626576); GO_0009615 (EC: TAS, PMID:18626576); GO_0009898 (EC: ISS); GO_0010765 (EC: IEA); GO_0019901 (EC: IPI, PMID:12492477); GO_0032481 (EC: TAS); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035631 (EC: ISS); GO_0035666 (EC: TAS); GO_0035872 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042501 (EC: IDA); GO_0042803 (EC: IDA); GO_0043066 (EC: TAS); GO_0043123 (EC: TAS); GO_0045087 (EC: TAS, PMID:18626576); GO_0045121 (EC: IEA); GO_0045893 (EC: NAS, PMID:9346484); GO_0045944 (EC: IDA); GO_0046982 (EC: IDA); GO_0048011 (EC: TAS); GO_0050852 (EC: TAS); GO_0051092 (EC: IDA, PMID:15790681); GO_0051092 (EC: TAS, PMID:18626576); GO_0070423 (EC: TAS); GO_0071356 (EC: IDA); GO_2001259 (EC: IEA) PMID:8601309; 8657102; 9214631; 9252186; 9346241; 9346484; 9346485; 9520446; 9632806; 9689078; 9721103; 9744859; 9751059; 9751060; 9763654; 9813230; 9819420; 9878263; 9891086; 9914500; 10022904; 10195894; 10356400; 10469655; 10485711; 10497169; 10521409; 10713178; 10722755; 10723127; 10733566; 10755617; 10779355; 10783893; 10807933; 10848580; 10962033; 10968790; 10980203; 11002417; 11057907; 11080499; 11096118; 11113112; 11120819; 11158290; 11278268; 11359906; 11429546; 11460167; 11527961; 11585904; 11594795; 11606564; 11777949; 11815618; 11821416; 11830587; 11839743; 11864612; 11945026; 11954826; 11959143; 11971985; 11976329; 12054687; 12070292; 12133833; 12210728; 12244103; 12351658; 12393548; 12411322; 12459277; 12477932; 12482991; 12486103; 12486112; 12492477; 12547194; 12589056; 12612076; 12637324; 12645577; 12657630; 12707358; 12709429; 12842894; 12890679; 12943667; 14514672; 14560022; 14585846; 14585847; 14585990; 14597638; 14625285; 14654787; 14702039; 14715628; 14743216; 14990741; 15084260; 15125834; 15128824; 15140882; 15184390; 15217951; 15218148; 15226300; 15254232; 15276183; 15319427; 15383283; 15389287; 15456791; 15489227; 15489334; 15492226; 15494311; 15564333; 15601829; 15749833; 15761153; 15790681; 15802604; 15808510; 15837793; 15856005; 15856023; 15880043; 15951441; 16024783; 16046471; 16051665; 16082226; 16123045; 16126728; 16135815; 16177806; 16207722; 16267042; 16280329; 16286467; 16291755; 16319058; 16344560; 16365431; 16393995; 16424386; 16497931; 16547522; 16583354; 16603398; 16611882; 16728640; 16840786; 16906147; 16920630; 16938294; 16966325; 16982623; 16989899; 16997282; 16998237; 17000764; 17016640; 17047224; 17079871; 17114296; 17145747; 17182689; 17213322; 17237423; 17244613; 17287217; 17363905; 17363973; 17419715; 17446166; 17466952; 17568778; 17616684; 17684021; 17693255; 17703412; 17891179; 17939994; 17947699; 17962807; 17977820; 17997719; 18029348; 18037881; 18163512; 18180283; 18207244; 18260825; 18266324; 18266467; 18308615; 18316610; 18362886; 18408758; 18411264; 18434448; 18456659; 18490760; 18571841; 18583959; 18600306; 18626576; 18636537; 18657515; 18692471; 18949366; 18952604; 18957422; 18981174; 18990758; 19050262; 19104039; 19109741; 19141566; 19150425; 19196987; 19202066; 19243472; 19258923; 19270264; 19365808; 19422324; 19453261; 19488402; 19526344; 19573080; 19591457; 19594441; 19656241; 19675099; 19716809; 19728335; 19730683; 19773279; 19786027; 19815509; 19818716; 19820708; 19850743; 20005846; 20007573; 20026656; 20051109; 20056178; 20068038; 20098747; 20145131; 20152798; 20164171; 20167598; 20176108; 20331378; 20347815; 20368414; 20371626; 20410276; 20421348; 20434986; 20448038; 20448286; 20449947; 20465575; 20503287; 20529849; 20568250; 20600852; 20614026; 20627395; 20657549; 20693425; 20797629; 20803413; 20856938; 20925653; 20932476; 20933503; 20977779; 21029719; 21048031; 21139048; 21204785; 21220427; 21248029; 21317297; 21331078; 21344388; 21390216; 21399639; 21474709; 21482671; 21575199; 21606193; 21606198; 21670849; 21703539; 21724995; 21784860; 21798539; 21803029; 21810613; 21811235; 21903422; 21911292; 21985298; 21987722; 21988832; 21993219; 22022389; 22099304; 22262057; 22331067; 22511786; 22605335; 22637744; 22766331; 22824620; 22848663; 22863883; 22891964; 22955948; 22990857; 23007157; 23016877; 23017601; 23032264; 23069812; 23090968; 23108365; 23123196; 23178494; 23349803; 23386606; 23453969; 23589370; 23636414; 23732909; 23743204; 23776175; 23776406; 23792959; 23817200; 23872070; 23974204; 23986494; 24127568; 24240172; 24266532; 24369075 inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase beta Ensembl:ENSG00000104365 HGNC:5960 HPRD:04462 MIM:603258 Vega:OTTHUMG00000164092 Other designations: I-kappa-B kinase 2|I-kappa-B-kinase beta|IKK-B|inhibitor of nuclear factor kappa-B kinase subunit beta|nuclear factor NF-kappa-B inhibitor kinase beta IKBKB OGG:3000003552 Bin Zhao, Yue Liu, Oliver He IL-1A IL1 IL1-ALPHA IL1F1 WEB: http://www.ncbi.nlm.nih.gov/gene IL1A interleukin 1, alpha 3552 2q14 9606 2 Official from a nomenclature committee GO_0001660 (EC: IEA); GO_0005125 (EC: IMP, PMID: 2989698); GO_0005149 (EC: IEA); GO_0005507 (EC: IDA, PMID: 12746488); GO_0005515 (EC: IPI, PMID: 12746488); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 12746488); GO_0005615 (EC: IMP, PMID: 3493774); GO_0005829 (EC: IDA, PMID: 12746488); GO_0006915 (EC: TAS, PMID: 1924307); GO_0006954 (EC: TAS, PMID: 6209582); GO_0006955 (EC: IEA); GO_0008283 (EC: TAS, PMID: 6209582); GO_0008285 (EC: IDA, PMID: 3493774); GO_0010575 (EC: ISS); GO_0019221 (EC: IMP, PMID: 2989698); GO_0034605 (EC: IDA, PMID: 12746488); GO_0035234 (EC: IEA); GO_0045086 (EC: IMP, PMID: 2989698); GO_0045766 (EC: ISS); GO_0045840 (EC: IMP, PMID: 2989698); GO_0045944 (EC: IEA); GO_0046688 (EC: IDA, PMID: 12746488); GO_0050715 (EC: IDA, PMID: 1739124); GO_0051781 (EC: IEA); GO_0097192 (EC: IEA); GO_2001240 (EC: TAS, PMID: 10748004) PMID: 1548758; 1584804; 1675504; 1739124; 1905933; 1924307; 1993354; 2346741; 2536171; 2635664; 2783369; 2946959; 2989698; 2994016; 3281727; 3485152; 3486405; 3493774; 6209582; 7494249; 7499244; 7511078; 7526541; 7561697; 7566121; 7695626; 7706435; 7815507; 7818827; 7857652; 7878046; 8188271; 8346241; 8370968; 8436814; 8458986; 8621446; 8764000; 8892361; 8938574; 9108403; 9169134; 9185130; 9225992; 9658081; 9820540; 10441334; 10512743; 10625660; 10744718; 10748004; 10854325; 10860666; 10861041; 10953177; 10998424; 11065142; 11079552; 11093146; 11138328; 11145356; 11145836; 11233912; 11241561; 11264025; 11278614; 11350500; 11350506; 11423389; 11427627; 11436125; 11448121; 11453239; 11466363; 11554782; 11574262; 11640949; 11669478; 11703512; 11737511; 11774556; 11774564; 11777547; 11784248; 11790645; 11840488; 11858158; 11895290; 11895546; 11911995; 11921766; 11930657; 11940570; 11956022; 11991668; 11991722; 12028539; 12034804; 12037600; 12047332; 12051868; 12052540; 12052541; 12070246; 12082592; 12089333; 12100571; 12101079; 12102486; 12115161; 12115182; 12140751; 12149413; 12161036; 12164325; 12195069; 12209090; 12210881; 12212456; 12218254; 12220547; 12242547; 12362317; 12370389; 12390476; 12404162; 12425801; 12445219; 12445604; 12453471; 12477932; 12519748; 12528118; 12528119; 12530978; 12558814; 12558933; 12562360; 12598547; 12613995; 12622850; 12626603; 12631337; 12641660; 12651617; 12667716; 12673844; 12702109; 12710950; 12714264; 12729191; 12730545; 12737276; 12742380; 12746420; 12746488; 12749050; 12752101; 12752325; 12759172; 12782964; 12794386; 12801479; 12824054; 12869004; 12874528; 12890860; 12899665; 12901853; 12913118; 12928052; 12928381; 12930304; 12930389; 12931024; 12946945; 12947160; 12974682; 13679381; 14514232; 14533660; 14566095; 14584862; 14612453; 14633625; 14634838; 14639688; 14644395; 14656692; 14664464; 14672899; 14673470; 14674121; 14688369; 14693849; 14705223; 14735144; 14974822; 14983027; 14984963; 14986816; 14997019; 15007345; 15009111; 15036245; 15039285; 15050696; 15068111; 15082121; 15117956; 15130917; 15170937; 15190266; 15201366; 15219382; 15220553; 15238767; 15248873; 15270852; 15308963; 15338333; 15341923; 15351436; 15361128; 15377701; 15381245; 15465625; 15468358; 15476179; 15481145; 15489227; 15489334; 15514971; 15551344; 15561982; 15562658; 15562910; 15563458; 15566952; 15581980; 15587751; 15592292; 15633328; 15638425; 15679580; 15679582; 15694997; 15723707; 15726267; 15727567; 15732864; 15733644; 15737206; 15745939; 15777329; 15797878; 15830637; 15836820; 15854776; 15931231; 15951664; 15954918; 15974847; 15986200; 16021081; 16030091; 16046471; 16078996; 16100774; 16101131; 16106254; 16115908; 16155691; 16159520; 16160188; 16206345; 16226351; 16230423; 16246569; 16268484; 16291395; 16304445; 16317381; 16318580; 16361815; 16369899; 16375755; 16378839; 16384981; 16389181; 16403098; 16410064; 16410066; 16411061; 16428739; 16433908; 16464738; 16478776; 16504015; 16508980; 16510430; 16517748; 16546408; 16564702; 16564703; 16567828; 16573560; 16619041; 16636934; 16684536; 16702372; 16708852; 16719905; 16720107; 16733901; 16788102; 16792821; 16814297; 16842617; 16856121; 16879223; 16885196; 16888077; 16900886; 16905534; 16907768; 16911569; 16918024; 16930778; 16931944; 16934308; 16938461; 16945028; 16961803; 16965524; 16965825; 16971486; 16978691; 17002905; 17012236; 17034724; 17083033; 17138334; 17140155; 17141301; 17149369; 17179726; 17197697; 17205326; 17214636; 17244613; 17257312; 17290104; 17293495; 17309781; 17331078; 17335370; 17335371; 17335373; 17348886; 17353161; 17355643; 17360358; 17369174; 17371964; 17378887; 17388919; 17391495; 17436000; 17440718; 17444587; 17444864; 17448042; 17449468; 17458495; 17460270; 17471097; 17473736; 17477815; 17492470; 17500214; 17507369; 17532232; 17541168; 17549071; 17573384; 17575917; 17584583; 17596594; 17610660; 17621543; 17622713; 17627763; 17638785; 17703412; 17711477; 17716546; 17717316; 17823082; 17889143; 17907045; 17919610; 17926179; 17932347; 17941080; 17948066; 17949817; 17954336; 17960403; 17964974; 17978470; 17986158; 17997719; 18024394; 18038187; 18052703; 18063673; 18085494; 18086816; 18157711; 18158110; 18166103; 18199150; 18211631; 18271063; 18278133; 18284424; 18288454; 18292602; 18306451; 18315433; 18321309; 18322311; 18329368; 18336824; 18361934; 18393655; 18395750; 18416755; 18416756; 18441098; 18469698; 18484169; 18484691; 18496214; 18498295; 18510611; 18576312; 18583979; 18587204; 18607773; 18615092; 18615110; 18624935; 18628242; 18628526; 18631256; 18632425; 18633131; 18666137; 18673406; 18676404; 18676680; 18676870; 18702109; 18708672; 18709454; 18714935; 18716798; 18717723; 18723088; 18760325; 18763028; 18773331; 18787502; 18815552; 18818748; 18821666; 18832862; 18834321; 18838388; 18941541; 18952231; 18971305; 18974840; 18974842; 18976975; 19012493; 19013788; 19019335; 19026558; 19028820; 19035492; 19042953; 19046297; 19053923; 19066720; 19074885; 19076825; 19086955; 19088500; 19099590; 19110536; 19117745; 19131662; 19141488; 19141860; 19155622; 19158434; 19170196; 19180518; 19180798; 19184295; 19188531; 19191034; 19194673; 19204921; 19225544; 19240061; 19247692; 19247983; 19258923; 19263529; 19267917; 19279357; 19280228; 19290009; 19294239; 19307598; 19332120; 19336370; 19336475; 19348329; 19408823; 19431193; 19435817; 19453261; 19470040; 19479237; 19497711; 19505916; 19527514; 19546559; 19559392; 19563289; 19573080; 19594368; 19625176; 19648252; 19658300; 19661089; 19671938; 19680808; 19683555; 19684156; 19692168; 19701653; 19702713; 19708438; 19729601; 19733643; 19738620; 19742166; 19764937; 19773279; 19773451; 19775068; 19786079; 19789190; 19792847; 19805069; 19811432; 19820020; 19844779; 19860911; 19884766; 19889475; 19892918; 19913121; 19917630; 19926874; 19934104; 19948975; 20005085; 20011938; 20027454; 20056178; 20059417; 20059631; 20065999; 20070880; 20080142; 20113359; 20113413; 20116409; 20127018; 20131253; 20140262; 20141484; 20157068; 20169140; 20173430; 20178882; 20182449; 20192980; 20196868; 20200332; 20207250; 20213229; 20217044; 20220089; 20227257; 20237496; 20299682; 20335539; 20347268; 20353565; 20371868; 20400062; 20413850; 20418110; 20427258; 20445556; 20452482; 20453000; 20459687; 20472930; 20490394; 20490891; 20495422; 20503287; 20534741; 20536507; 20536609; 20551628; 20561568; 20565898; 20568250; 20574532; 20594066; 20595916; 20602615; 20603037; 20603050; 20619343; 20628086; 20630038; 20673868; 20677014; 20725607; 20800603; 20811626; 20844546; 20847078; 20848459; 20889944; 20934174; 20940514; 20942594; 20959405; 20961668; 21035110; 21037510; 21048327; 21054222; 21070631; 21086908; 21107309; 21133705; 21154765; 21196890; 21205020; 21235388; 21270123; 21279638; 21311438; 21336718; 21385326; 21393239; 21394384; 21449691; 21509504; 21518761; 21620624; 21621860; 21682548; 21712624; 21768915; 21795706; 21816944; 21847358; 21871094; 21968104; 22083707; 22092925; 22124068; 22143786; 22151432; 22153345; 22177239; 22197408; 22211888; 22216303; 22234841; 22282663; 22285242; 22312160; 22344672; 22348697; 22364598; 22417897; 22513697; 22582837; 22633328; 22675954; 22678894; 22732089; 22795294; 22805136; 22868802; 22879895; 22894561; 22949675; 23018032; 23052182; 23076369; 23100272; 23159404; 23203659; 23216199; 23241110; 23271701; 23289806; 23322030; 23349093; 23395675; 23454256; 23509928; 23527710; 23542780; 23554905; 23592003; 23639700; 23645090; 23723976; 23747396; 23846687; 23900673; 23927441; 24060296; 24062309; 24103372; 24146121; 24265545; 24273934; 24275344; 24313836 interleukin 1, alpha HGNC:5991 HPRD:00988 MIM:147760 Other designations: IL-1 alpha|hematopoietin-1|interleukin-1 alpha|preinterleukin 1 alpha|pro-interleukin-1-alpha IL1A OGG:3000003553 Bin Zhao, Yue Liu, Oliver He IL-1 IL1-BETA IL1F2 WEB: http://www.ncbi.nlm.nih.gov/gene IL1B interleukin 1, beta 3553 2q14 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0000165 (EC: IMP); GO_0000187 (EC: IDA, PMID: 10748004); GO_0001660 (EC: IEA); GO_0001934 (EC: IDA, PMID: 10748004); GO_0001934 (EC: NAS, PMID: 16477012); GO_0002711 (EC: IC, PMID: 1919436); GO_0005125 (EC: IDA, PMID: 1919436); GO_0005125 (EC: IMP, PMID: 2989698); GO_0005149 (EC: NAS, PMID: 1919436); GO_0005576 (EC: IDA); GO_0005576 (EC: NAS, PMID: 1919436); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 12483741); GO_0005615 (EC: IMP, PMID: 3493774); GO_0005829 (EC: TAS); GO_0006915 (EC: TAS, PMID: 9218611); GO_0006954 (EC: IDA, PMID: 10748004); GO_0006954 (EC: NAS, PMID: 1919436); GO_0006955 (EC: IEA); GO_0007165 (EC: TAS, PMID: 10786823); GO_0007267 (EC: TAS, PMID: 2989698); GO_0007566 (EC: TAS, PMID: 16720713); GO_0008285 (EC: IDA, PMID: 3493774); GO_0009743 (EC: IEA); GO_0010575 (EC: IDA, PMID: 12958148); GO_0010575 (EC: ISS); GO_0010829 (EC: ISS, PMID: 16865359); GO_0014805 (EC: NAS, PMID: 16477012); GO_0019221 (EC: IDA, PMID: 10748004); GO_0019904 (EC: IPI, PMID: 16575408); GO_0030141 (EC: IEA); GO_0030213 (EC: IDA, PMID: 15100360); GO_0030593 (EC: IEA); GO_0030730 (EC: IDA, PMID: 19032770); GO_0030949 (EC: IC, PMID: 12958148); GO_0031622 (EC: ISS); GO_0031663 (EC: IDA); GO_0032308 (EC: ISS); GO_0032611 (EC: IEA); GO_0032725 (EC: IDA); GO_0032729 (EC: IDA); GO_0032755 (EC: TAS, PMID: 16865359); GO_0032757 (EC: IDA, PMID: 19524870); GO_0033129 (EC: NAS); GO_0033198 (EC: IEA); GO_0034116 (EC: IDA, PMID: 15100360); GO_0034116 (EC: NAS, PMID: 19281832); GO_0035066 (EC: NAS); GO_0035234 (EC: IEA); GO_0035505 (EC: IDA, PMID: 18390750); GO_0035690 (EC: IDA, PMID: 19158679); GO_0042102 (EC: IDA, PMID: 1919436); GO_0042346 (EC: IDA, PMID: 18390750); GO_0043122 (EC: IDA, PMID: 10748004); GO_0043123 (EC: IEA); GO_0043407 (EC: ISS, PMID: 16865359); GO_0043491 (EC: IMP); GO_0045080 (EC: IEA); GO_0045086 (EC: IMP, PMID: 2989698); GO_0045410 (EC: IEA); GO_0045429 (EC: IDA, PMID: 8383325); GO_0045766 (EC: ISS); GO_0045833 (EC: ISS, PMID: 16865359); GO_0045840 (EC: IMP, PMID: 2989698); GO_0045893 (EC: IDA, PMID: 15100360); GO_0045944 (EC: IEA); GO_0046330 (EC: IEA); GO_0046627 (EC: ISS, PMID: 16865359); GO_0046827 (EC: NAS, PMID: 19281832); GO_0050796 (EC: IDA, PMID: 8383325); GO_0050995 (EC: IDA, PMID: 19032770); GO_0050996 (EC: ISS, PMID: 16865359); GO_0051044 (EC: IDA, PMID: 18373975); GO_0051091 (EC: IDA, PMID: 10748004); GO_0051092 (EC: IDA, PMID: 10383454); GO_0051781 (EC: IEA); GO_0060355 (EC: NAS, PMID: 19281832); GO_0060559 (EC: IDA, PMID: 16720713); GO_0070164 (EC: ISS, PMID: 16865359); GO_0070487 (EC: IDA, PMID: 15100360); GO_0071260 (EC: IEP, PMID: 19593445); GO_0071310 (EC: IDA, PMID: 19158679); GO_0071407 (EC: IDA); GO_0071639 (EC: IDA, PMID: 19524870); GO_0097192 (EC: IEA); GO_2001240 (EC: IDA, PMID: 10748004) PMID: 1548758; 1753956; 1835838; 1837236; 1905933; 1907279; 1918997; 1919001; 1919436; 1993354; 2001363; 2137098; 2372550; 2466831; 2536171; 2585509; 2602367; 2635664; 2898301; 2946959; 2954882; 2989698; 3259176; 3264123; 3281727; 3490654; 3493774; 6083565; 6209582; 7494249; 7511078; 7526541; 7561697; 7642516; 7706435; 7797510; 7815507; 7818827; 7878046; 7981229; 8188271; 8383325; 8432529; 8537091; 8663297; 8764000; 8852605; 8869030; 8892361; 8939574; 9062193; 9108403; 9169134; 9185130; 9218611; 9225992; 9230816; 9288832; 9378998; 9658081; 9714181; 9820540; 10339575; 10358063; 10383454; 10438928; 10512743; 10625660; 10744718; 10746728; 10748004; 10756100; 10779559; 10786823; 10854325; 10860666; 10964543; 11023482; 11051551; 11057907; 11076651; 11079552; 11083263; 11093146; 11127488; 11138328; 11145836; 11171832; 11211945; 11226333; 11233912; 11238007; 11241561; 11260714; 11264025; 11278614; 11350500; 11350506; 11380940; 11422336; 11423389; 11427627; 11448121; 11466363; 11476790; 11481169; 11498264; 11500085; 11506478; 11527622; 11531943; 11574262; 11578018; 11579484; 11600466; 11606496; 11640949; 11641511; 11665666; 11669478; 11686217; 11686480; 11703512; 11704656; 11737511; 11751881; 11751921; 11756575; 11762793; 11770040; 11774564; 11777965; 11784248; 11790645; 11801594; 11806247; 11838837; 11840488; 11847219; 11849463; 11851889; 11853544; 11857060; 11858158; 11858187; 11868623; 11876744; 11895290; 11896542; 11898000; 11920321; 11921766; 11930657; 11950481; 11955925; 11958432; 11981835; 11991722; 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12651071; 12651617; 12667023; 12667656; 12668157; 12673844; 12694213; 12699881; 12700687; 12702109; 12705485; 12714264; 12718576; 12718598; 12718604; 12722027; 12725322; 12726991; 12727794; 12729191; 12730545; 12730860; 12743452; 12744771; 12746420; 12746914; 12749050; 12751042; 12752101; 12756345; 12761889; 12775358; 12788304; 12790892; 12795791; 12801479; 12801886; 12802423; 12807444; 12824054; 12828754; 12837173; 12842905; 12854083; 12860389; 12869004; 12874528; 12881225; 12890860; 12891537; 12899665; 12901853; 12913327; 12928052; 12930389; 12945076; 12958148; 12958619; 12965265; 12970400; 12974682; 13129651; 13679820; 14510824; 14512722; 14514232; 14515062; 14521725; 14522096; 14523823; 14527933; 14533660; 14563376; 14566095; 14566840; 14582815; 14584052; 14584862; 14585879; 14617515; 14632761; 14633943; 14634838; 14638340; 14644395; 14656692; 14657427; 14661113; 14662866; 14664464; 14669220; 14672899; 14673470; 14675093; 14675394; 14681913; 14691340; 14723749; 14735144; 14746807; 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22629855; 22649552; 22673037; 22708826; 22710193; 22714811; 22727020; 22738689; 22739237; 22750393; 22759516; 22763042; 22763186; 22764136; 22768033; 22791816; 22795101; 22795647; 22796164; 22796220; 22796605; 22804923; 22805115; 22808497; 22811570; 22815289; 22818022; 22818222; 22822059; 22829602; 22829643; 22869038; 22878044; 22884582; 22884587; 22894561; 22898394; 22902304; 22904187; 22909148; 22911481; 22923190; 22937208; 22946471; 22947907; 22951596; 22955577; 22960943; 22995155; 22997256; 23006543; 23009887; 23013363; 23018032; 23020284; 23029154; 23052182; 23062767; 23065753; 23079713; 23105097; 23110185; 23169178; 23181791; 23184659; 23192617; 23195019; 23195574; 23199001; 23208827; 23209292; 23209411; 23209664; 23209696; 23210983; 23215648; 23215728; 23216199; 23217179; 23220433; 23226210; 23226468; 23229544; 23233369; 23237500; 23239492; 23241110; 23264411; 23269671; 23276701; 23313749; 23315075; 23317890; 23322904; 23323013; 23328087; 23328930; 23331079; 23349093; 23375040; 23383347; 23386602; 23391392; 23406266; 23417678; 23421536; 23425136; 23437386; 23452206; 23457635; 23459183; 23460134; 23460908; 23472661; 23484124; 23500159; 23508571; 23509682; 23531221; 23536554; 23546865; 23554905; 23555186; 23564444; 23571448; 23592003; 23592910; 23592922; 23610862; 23630220; 23633957; 23643268; 23650922; 23651237; 23654353; 23656735; 23657597; 23659674; 23660804; 23666803; 23680697; 23689297; 23702978; 23704929; 23717664; 23723976; 23726808; 23728092; 23737648; 23740952; 23747396; 23762029; 23773024; 23784458; 23793845; 23821953; 23822621; 23839215; 23840644; 23841472; 23884315; 23884363; 23892591; 23911403; 23927441; 23935506; 23936458; 23963575; 24022484; 24025329; 24035972; 24046015; 24078775; 24081990; 24146121; 24186874; 24265545; 24275344; 24313836; 24314919; 24338609; 24552038; 24611340 interleukin 1, beta Ensembl:ENSG00000125538 HGNC:5992 HPRD:00985 MIM:147720 Vega:OTTHUMG00000131344 Other designations: IL-1 beta|catabolin|interleukin-1 beta|preinterleukin 1 beta|pro-interleukin-1-beta IL1B OGG:3000003557 Bin Zhao, Yue Liu, Oliver He DIRA ICIL-1RA IL-1RN IL-1ra IL-1ra3 IL1F3 IL1RA IRAP MVCD4 WEB: http://www.ncbi.nlm.nih.gov/gene IL1RN interleukin 1 receptor antagonist 3557 2q14.2 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0001660 (EC: IEA); GO_0001960 (EC: IDA, PMID: 2137200); GO_0002439 (EC: IEA); GO_0005149 (EC: IDA, PMID: 2137200); GO_0005150 (EC: IPI, PMID: 1828071); GO_0005151 (EC: IPI, PMID: 1830582); GO_0005152 (EC: IDA, PMID: 2137200); GO_0005152 (EC: TAS, PMID: 7629520); GO_0005615 (EC: IDA, PMID: 10443688); GO_0005622 (EC: NAS, PMID: 7629520); GO_0005737 (EC: IEA); GO_0005886 (EC: TAS); GO_0006629 (EC: IEA); GO_0006953 (EC: IDA, PMID: 9185517); GO_0006955 (EC: NAS, PMID: 7629520); GO_0007565 (EC: IEA); GO_0007613 (EC: IEA); GO_0010243 (EC: IEA); GO_0014050 (EC: IEA); GO_0019752 (EC: IEA); GO_0030073 (EC: IEA); GO_0030336 (EC: IEA); GO_0032496 (EC: IEA); GO_0034115 (EC: IDA, PMID: 2139180); GO_0042493 (EC: IEA); GO_0043066 (EC: IEA); GO_0043507 (EC: IEA); GO_0045352 (EC: IDA, PMID: 1828071); GO_0045353 (EC: IDA, PMID: 1830582); GO_0045837 (EC: IEA); GO_0051384 (EC: IDA, PMID: 10443688); GO_0070062 (EC: IDA, PMID: 19056867); GO_0070670 (EC: IEA); GO_2000660 (EC: IDA, PMID: 2137200) PMID: 1385987; 1386337; 1479000; 1534997; 1827201; 1828071; 1828896; 1830582; 1834644; 2137200; 2137201; 2139180; 2143761; 2147937; 7629520; 7867645; 8045306; 8175703; 8188271; 8432529; 8726668; 8852605; 8992991; 9062194; 9169134; 9185517; 9514884; 9597123; 9710237; 9933103; 10443688; 10512743; 10625660; 10673296; 10744718; 10786823; 10860666; 10948677; 10988299; 11023482; 11027520; 11033452; 11045853; 11093146; 11127488; 11138328; 11145836; 11171832; 11233912; 11247888; 11264025; 11278614; 11423389; 11448121; 11466363; 11531943; 11574262; 11600466; 11606494; 11606496; 11640949; 11641511; 11665981; 11686217; 11762793; 11770040; 11784248; 11793861; 11802774; 11803448; 11816697; 11840488; 11841485; 11841553; 11846196; 11858187; 11876744; 11876758; 11991722; 12044341; 12070246; 12082590; 12082592; 12095061; 12102486; 12105837; 12111633; 12114904; 12115161; 12115182; 12133467; 12136897; 12140751; 12160520; 12161036; 12161099; 12164325; 12165808; 12220547; 12239970; 12240899; 12355453; 12441323; 12445219; 12445604; 12452470; 12453918; 12454835; 12468823; 12472674; 12477932; 12483741; 12496176; 12519748; 12530098; 12547728; 12551827; 12568735; 12578333; 12593203; 12595908; 12609525; 12618859; 12624309; 12626603; 12645941; 12667023; 12667286; 12679428; 12686792; 12694213; 12714264; 12718576; 12722027; 12729191; 12730545; 12730860; 12746420; 12746914; 12764021; 12768436; 12775358; 12788304; 12794527; 12801479; 12820354; 12824054; 12828754; 12847695; 12854083; 12891537; 12901853; 12913327; 12919285; 12930389; 12938145; 12958619; 14504049; 14514232; 14521725; 14522096; 14533660; 14566095; 14568678; 14585879; 14586324; 14611908; 14632761; 14633943; 14634579; 14634582; 14644395; 14647192; 14652282; 14656692; 14657427; 14664464; 14669220; 14672899; 14673228; 14734209; 14735144; 14750640; 14753487; 14758530; 14982742; 14984963; 14986816; 14997019; 15020290; 15030461; 15036245; 15036607; 15056081; 15077300; 15082121; 15127646; 15141093; 15144571; 15170937; 15171792; 15181037; 15184943; 15188516; 15190266; 15201366; 15205567; 15223609; 15231136; 15233701; 15235132; 15236174; 15241561; 15247172; 15250242; 15266130; 15270852; 15286433; 15292002; 15305821; 15318032; 15325407; 15338333; 15339690; 15379752; 15457475; 15476179; 15485792; 15489334; 15507960; 15507961; 15512788; 15530901; 15535834; 15539764; 15540224; 15551344; 15562761; 15566952; 15570075; 15574426; 15579481; 15602586; 15610073; 15644653; 15670034; 15672946; 15679582; 15694997; 15704154; 15717635; 15723707; 15727567; 15730917; 15733644; 15766560; 15797878; 15800325; 15803022; 15830637; 15836820; 15851404; 15866604; 15878285; 15884119; 15885804; 15900570; 15923123; 15927855; 15931231; 15943888; 15954918; 15986200; 16019127; 16019233; 16025481; 16026159; 16043936; 16053468; 16078996; 16088107; 16096333; 16098232; 16100774; 16106254; 16109659; 16114018; 16115908; 16126303; 16128937; 16142351; 16159520; 16164697; 16172101; 16174285; 16183821; 16195370; 16200608; 16202742; 16217062; 16226351; 16244470; 16246569; 16263000; 16268484; 16284368; 16284379; 16301842; 16318998; 16319982; 16335952; 16361275; 16361815; 16362796; 16369899; 16389181; 16403098; 16405550; 16409203; 16414081; 16423338; 16436009; 16454826; 16456536; 16510430; 16519819; 16538639; 16540751; 16549749; 16550552; 16553947; 16573560; 16579840; 16595248; 16596202; 16635219; 16635751; 16636119; 16637265; 16638698; 16698387; 16699452; 16741227; 16764597; 16766392; 16769128; 16777324; 16804398; 16815316; 16817913; 16820326; 16820919; 16824064; 16839849; 16842617; 16856121; 16873708; 16879054; 16885604; 16886894; 16900886; 16905295; 16906455; 16907768; 16911569; 16921503; 16937503; 16938461; 16980335; 16984283; 16985030; 17002905; 17005410; 17026469; 17034724; 17035400; 17068065; 17069782; 17074546; 17083033; 17096351; 17107994; 17113632; 17114844; 17115419; 17174563; 17176440; 17177339; 17182583; 17207379; 17222831; 17224277; 17235630; 17256873; 17257312; 17258699; 17286233; 17290743; 17292896; 17295877; 17309751; 17314118; 17324969; 17327408; 17332449; 17335371; 17348243; 17351514; 17359523; 17373677; 17380888; 17388919; 17391700; 17413037; 17443229; 17444587; 17444864; 17446060; 17448214; 17453104; 17454884; 17459217; 17482260; 17483707; 17532232; 17548705; 17572155; 17584583; 17592300; 17593860; 17596285; 17607501; 17607547; 17610660; 17611547; 17611673; 17618436; 17627763; 17640324; 17645476; 17656565; 17703412; 17716546; 17760842; 17846855; 17847930; 17867984; 17899305; 17900737; 17903994; 17907045; 17914732; 17926179; 17948066; 17959519; 17963170; 17964974; 17993728; 18008080; 18029348; 18038187; 18047563; 18052703; 18052726; 18063673; 18069935; 18086767; 18165865; 18180150; 18186699; 18239554; 18243027; 18271063; 18272394; 18278133; 18288276; 18288454; 18299273; 18321309; 18322311; 18329282; 18332090; 18333945; 18336824; 18354254; 18361937; 18364273; 18385937; 18386294; 18389618; 18396210; 18416755; 18423886; 18451331; 18455629; 18464913; 18468936; 18471873; 18484169; 18484691; 18494930; 18496214; 18545091; 18551993; 18565646; 18572364; 18579366; 18581280; 18583979; 18589098; 18597398; 18624935; 18632425; 18633131; 18665932; 18666137; 18676680; 18688110; 18702109; 18703194; 18715339; 18723088; 18728809; 18754838; 18761558; 18763028; 18771989; 18773331; 18779738; 18782283; 18805892; 18807132; 18808736; 18810365; 18814951; 18815552; 18818748; 18821666; 18832862; 18838927; 18853133; 18926055; 18940468; 18942754; 18987561; 19004046; 19009622; 19012493; 19013788; 19019335; 19026124; 19026700; 19030199; 19031173; 19046297; 19053923; 19056867; 19058789; 19066720; 19073760; 19074885; 19076825; 19086955; 19102413; 19111743; 19117745; 19125864; 19127455; 19129082; 19132772; 19134476; 19135625; 19141860; 19142372; 19151976; 19170196; 19191798; 19203086; 19247692; 19258032; 19258923; 19267917; 19269948; 19272615; 19280228; 19290009; 19290417; 19295440; 19322919; 19332120; 19334424; 19336370; 19336475; 19338208; 19347053; 19375283; 19399323; 19408823; 19418669; 19419456; 19427781; 19431193; 19453261; 19470040; 19489682; 19494218; 19495883; 19497711; 19505916; 19505919; 19506726; 19527514; 19544559; 19544973; 19550417; 19573080; 19574724; 19594368; 19603010; 19607807; 19618316; 19625176; 19638314; 19643686; 19644155; 19664671; 19683555; 19684156; 19692168; 19701653; 19702713; 19706048; 19711225; 19729601; 19733643; 19733878; 19764937; 19773279; 19804405; 19811432; 19811433; 19811434; 19818512; 19820020; 19822419; 19822442; 19839644; 19844779; 19850242; 19860911; 19876593; 19889076; 19892918; 19900796; 19904560; 19909950; 19913121; 19925477; 19930406; 19934104; 19948975; 20002810; 20005085; 20012999; 20032313; 20034444; 20056442; 20070880; 20080142; 20087638; 20092400; 20113413; 20131253; 20140262; 20141484; 20169140; 20175886; 20178882; 20185814; 20188863; 20192980; 20193596; 20196868; 20200422; 20207250; 20213229; 20213597; 20237151; 20237496; 20301318; 20305143; 20334849; 20335539; 20347268; 20353565; 20364673; 20378664; 20379614; 20399384; 20400062; 20412719; 20427258; 20450372; 20452482; 20453000; 20463618; 20467172; 20472930; 20482626; 20484876; 20485444; 20486195; 20495422; 20503287; 20536609; 20538031; 20551628; 20564140; 20568250; 20581747; 20592454; 20595916; 20603050; 20621920; 20626741; 20628086; 20630038; 20631624; 20650788; 20654748; 20673868; 20709104; 20734064; 20800651; 20802378; 20837746; 20839488; 20863445; 20880168; 20880945; 20934174; 20940514; 20942594; 20975573; 21035110; 21037510; 21044950; 21048327; 21049406; 21054807; 21086908; 21111725; 21174170; 21182747; 21235388; 21241861; 21243433; 21248262; 21265111; 21278303; 21357189; 21394384; 21455057; 21523343; 21558284; 21575667; 21591983; 21621860; 21655939; 21671260; 21768915; 21848462; 21968104; 21980458; 22027586; 22032624; 22035161; 22059992; 22127713; 22205395; 22267087; 22285242; 22286731; 22312160; 22322675; 22327782; 22370044; 22431772; 22455686; 22498095; 22537067; 22744645; 22753384; 22795294; 22829643; 22882323; 22909148; 22939635; 22948742; 23009887; 23013217; 23014359; 23028694; 23049596; 23049925; 23053980; 23122308; 23168096; 23192617; 23195019; 23212299; 23251650; 23251661; 23308180; 23323013; 23388595; 23406623; 23449693; 23462747; 23472661; 23499887; 23554905; 23562526; 23577098; 23592003; 23602199; 23602982; 23609451; 23633206; 23743874; 23765978; 23800434; 23818854; 23969696; 24611340 interleukin 1 receptor antagonist Ensembl:ENSG00000136689 HGNC:6000 HPRD:00978 MIM:147679 Vega:OTTHUMG00000131341 IL1RN OGG:3000003558 Bin Zhao, Yue Liu, Oliver He IL-2 TCGF lymphokine WEB: http://www.ncbi.nlm.nih.gov/gene IL2 interleukin 2 3558 4q26-q27 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0001933 (EC: IEA); GO_0002903 (EC: IDA, PMID: 9184696); GO_0005125 (EC: IDA, PMID: 10072077); GO_0005134 (EC: IDA, PMID: 8262055); GO_0005134 (EC: TAS, PMID: 3925347); GO_0005576 (EC: TAS); GO_0005615 (EC: TAS, PMID: 6608729); GO_0006955 (EC: TAS, PMID: 2342538); GO_0007155 (EC: TAS, PMID: 10929056); GO_0007204 (EC: IEA); GO_0007205 (EC: IEA); GO_0007267 (EC: TAS, PMID: 8476561); GO_0008083 (EC: TAS, PMID: 8476561); GO_0008284 (EC: TAS, PMID: 8476561); GO_0019209 (EC: TAS, PMID: 8476561); GO_0030101 (EC: TAS, PMID: 8476561); GO_0030217 (EC: TAS, PMID: 8476561); GO_0030246 (EC: IEA); GO_0030307 (EC: TAS, PMID: 8476561); GO_0030890 (EC: IDA, PMID: 9184696); GO_0031851 (EC: IEA); GO_0032729 (EC: IEA); GO_0032740 (EC: IDA, PMID: 16482511); GO_0034105 (EC: IC, PMID: 16482511); GO_0042104 (EC: IDA, PMID: 10072077); GO_0042523 (EC: IDA, PMID: 19088061); GO_0043066 (EC: TAS, PMID: 8476561); GO_0043208 (EC: IEA); GO_0045591 (EC: IEA); GO_0045822 (EC: IEA); GO_0045944 (EC: IEA); GO_0046013 (EC: IEA); GO_0048304 (EC: IEA); GO_0050672 (EC: IEA); GO_0050728 (EC: IEA); GO_0050729 (EC: IC, PMID: 16482511); GO_0051024 (EC: IEA); GO_0060999 (EC: IEA); GO_0097192 (EC: IEA) PMID: 1316918; 1346976; 1394441; 1396583; 1510960; 1527859; 1631562; 1830926; 1832084; 1888898; 1905933; 1993646; 2052609; 2109157; 2303462; 2315327; 2342538; 2552026; 2793860; 2842093; 3260003; 3262520; 3264184; 3265909; 3491296; 3500515; 3877307; 3925347; 6201860; 6306584; 6312994; 6318318; 6321163; 6324170; 6330695; 6333684; 6403867; 6608729; 7523014; 7529123; 7589092; 7591871; 7642615; 7695626; 7697734; 7722480; 7734194; 7957556; 7963560; 7983746; 7999066; 8049354; 8095514; 8102828; 8118889; 8183373; 8207793; 8262055; 8402910; 8476561; 8493579; 8598486; 8626603; 8706326; 8757311; 8765022; 8769094; 8824916; 9007200; 9045614; 9045910; 9065434; 9184696; 9187267; 9209269; 9226175; 9311917; 9334723; 9516115; 9517986; 9534962; 9712080; 9811677; 10072077; 10196292; 10201969; 10207088; 10393966; 10570282; 10618429; 10662798; 10825200; 10929056; 10985305; 11035066; 11093171; 11114167; 11254713; 11261789; 11315919; 11350667; 11354638; 11385624; 11418623; 11525806; 11544437; 11689614; 11714800; 11743717; 11826762; 11841848; 11911478; 11914641; 11940709; 11981437; 12055219; 12072494; 12089714; 12105273; 12121273; 12144536; 12162871; 12171778; 12176041; 12193716; 12200381; 12354082; 12354383; 12358847; 12392859; 12393431; 12409183; 12456594; 12464620; 12477932; 12480696; 12486027; 12504009; 12536241; 12542496; 12557940; 12582206; 12604780; 12605694; 12610796; 12633940; 12646760; 12687247; 12717025; 12727482; 12727483; 12759392; 12808095; 12816983; 12826155; 12826231; 12851716; 12864971; 12884288; 12944981; 12960316; 14499500; 14522096; 14566095; 14607923; 14607929; 14675394; 14680494; 14687725; 14688528; 14707112; 14715519; 14722108; 14975604; 15001467; 15005726; 15057902; 15100259; 15104679; 15120188; 15152368; 15170937; 15175153; 15187164; 15191519; 15238074; 15247007; 15259063; 15271977; 15339934; 15347678; 15353479; 15361128; 15458467; 15489334; 15514847; 15539078; 15562014; 15563472; 15638726; 15654770; 15676209; 15686714; 15710467; 15728489; 15733644; 15749888; 15814282; 15841182; 15841456; 15895884; 15904474; 15910743; 15951664; 15964333; 15976176; 16060678; 16091861; 16100774; 16125242; 16132828; 16148026; 16164695; 16169852; 16293250; 16293754; 16323127; 16333313; 16354571; 16361891; 16389181; 16393999; 16477002; 16478922; 16482511; 16518704; 16567828; 16573560; 16584887; 16606671; 16621991; 16678358; 16690518; 16783532; 16805135; 16824159; 16864905; 16864906; 16885196; 16889932; 16920920; 16938461; 16961803; 16966412; 16984280; 17002904; 17052299; 17077180; 17097050; 17110377; 17115417; 17142786; 17152005; 17175263; 17177332; 17203290; 17207965; 17215524; 17222831; 17237447; 17257312; 17327408; 17332243; 17336597; 17337059; 17355643; 17396252; 17439892; 17444587; 17457216; 17460561; 17537734; 17541281; 17558408; 17571248; 17604883; 17627763; 17651815; 17703412; 17714919; 17715020; 17728221; 17761346; 17889143; 17900510; 17913045; 17949552; 17956522; 17981641; 17981806; 17985312; 17994425; 18021367; 18021981; 18023521; 18073500; 18077789; 18095604; 18097023; 18165865; 18174230; 18192685; 18207244; 18209044; 18239807; 18271063; 18275276; 18299274; 18309287; 18311140; 18324310; 18331736; 18348982; 18418394; 18423386; 18430737; 18481948; 18496418; 18522869; 18539368; 18543227; 18566561; 18570590; 18574615; 18576303; 18593762; 18614637; 18624934; 18628433; 18632425; 18633131; 18650128; 18663124; 18670216; 18676680; 18676770; 18714042; 18755820; 18761558; 18768844; 18769450; 18773331; 18776133; 18780166; 18780949; 18794598; 18805825; 18818748; 18932275; 18942754; 18972297; 18991615; 19013323; 19019335; 19058298; 19058987; 19073967; 19088061; 19099187; 19105930; 19117745; 19126646; 19135418; 19141488; 19170196; 19200845; 19201773; 19234188; 19250279; 19258923; 19275586; 19279357; 19284443; 19302705; 19332120; 19339796; 19351491; 19364969; 19375249; 19404967; 19406689; 19408823; 19414780; 19427348; 19430480; 19450160; 19453859; 19470040; 19471255; 19494280; 19495883; 19497711; 19502081; 19505916; 19522766; 19523143; 19527514; 19543959; 19573080; 19594368; 19625176; 19638314; 19648290; 19675167; 19683555; 19692168; 19693089; 19693092; 19707465; 19710466; 19718824; 19733878; 19773279; 19773451; 19787624; 19832038; 19860911; 19889958; 19892918; 19913121; 19925666; 19938203; 19951419; 19965651; 20012528; 20027321; 20049409; 20060205; 20072139; 20082482; 20100932; 20112382; 20129796; 20145925; 20177758; 20179739; 20182632; 20184734; 20190192; 20190752; 20193755; 20203524; 20213229; 20219786; 20221423; 20222161; 20225066; 20227890; 20233754; 20236616; 20331378; 20378664; 20418110; 20424473; 20438365; 20444755; 20452482; 20453000; 20453842; 20465575; 20484443; 20485444; 20498205; 20503287; 20535218; 20542085; 20544350; 20553587; 20557936; 20561440; 20562654; 20568250; 20594918; 20595916; 20596022; 20599261; 20603050; 20626741; 20628086; 20671116; 20673868; 20679529; 20716621; 20802378; 20811626; 20814620; 20839488; 20870937; 20880293; 20883322; 20926141; 20942272; 20960273; 20962850; 21035858; 21037099; 21061265; 21072155; 21085635; 21086908; 21112091; 21162873; 21167738; 21176845; 21179414; 21198755; 21258967; 21269573; 21282039; 21288140; 21292764; 21297633; 21304239; 21317396; 21372257; 21375519; 21383498; 21394196; 21423578; 21425124; 21425313; 21482826; 21531896; 21532597; 21620040; 21640045; 21642596; 21648020; 21685912; 21688385; 21711552; 21819478; 21829393; 21839273; 21876034; 21889323; 21890374; 21905023; 21905024; 21925225; 21976679; 21978000; 21984699; 22036096; 22040441; 22062588; 22077623; 22111667; 22112982; 22174157; 22242968; 22246628; 22281835; 22313865; 22337875; 22434682; 22461703; 22467658; 22472080; 22474330; 22479496; 22504653; 22524835; 22554193; 22585398; 22609631; 22623329; 22634617; 22645657; 22732586; 22736314; 22791129; 22797138; 22819245; 22891215; 22905203; 22910795; 22932225; 22984628; 23009887; 23019580; 23058031; 23103669; 23104097; 23128233; 23129528; 23172754; 23185455; 23192659; 23217119; 23265966; 23272100; 23278180; 23303246; 23317891; 23319613; 23328843; 23349093; 23380740; 23414538; 23418630; 23451206; 23487197; 23541403; 23586039; 23640893; 23645042; 23665382; 23676143; 23677467; 23724099; 23806696; 23817571; 23857000; 24019486; 24098138 interleukin 2 HGNC:6001 HPRD:00979 MIM:147680 Other designations: T cell growth factor|aldesleukin|interleukin-2|involved in regulation of T-cell clonal expansion IL2 OGG:3000003559 Bin Zhao, Yue Liu, Oliver He CD25 IDDM10 IL2R TCGFR WEB: http://www.ncbi.nlm.nih.gov/gene IL2RA interleukin 2 receptor, alpha 3559 RP11-536K7.1 10p15-p14 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0002437 (EC: IEA); GO_0004911 (EC: IEA); GO_0005886 (EC: TAS); GO_0006915 (EC: TAS, PMID: 9096364); GO_0006924 (EC: IEA); GO_0006955 (EC: TAS, PMID: 9096364); GO_0007166 (EC: TAS, PMID: 2983318); GO_0007219 (EC: IEA); GO_0008144 (EC: IEA); GO_0008283 (EC: TAS, PMID: 2983318); GO_0009897 (EC: IEA); GO_0016021 (EC: IEA); GO_0019976 (EC: IEA); GO_0042104 (EC: IEA); GO_0042130 (EC: IEA); GO_0045582 (EC: IEA); GO_0046013 (EC: IEA); GO_0050687 (EC: IEA); GO_0050728 (EC: IEA); GO_0050777 (EC: IEA) PMID: 1394441; 1511461; 1685671; 1693645; 1832084; 1976256; 1993646; 2016116; 2083254; 2153927; 2303462; 2308942; 2315327; 2467293; 2497520; 2785715; 2843775; 2901720; 2941417; 2983318; 2990220; 2996141; 2999698; 3030566; 3097520; 3134887; 3135323; 3925551; 6090948; 6090949; 6096720; 7529123; 7539755; 7588634; 7734194; 7853525; 7862168; 7903128; 8098618; 8125298; 8364583; 8493579; 8530186; 8752938; 8896456; 8943338; 9096364; 9203962; 9223324; 9268307; 9341758; 9637477; 10602027; 10815800; 10825200; 10848593; 11416131; 11485747; 11856346; 11886175; 11960393; 11986281; 12171778; 12200381; 12230826; 12374985; 12486319; 12525482; 12581498; 12698200; 12970897; 14680494; 15123239; 15197226; 15263076; 15328201; 15353339; 15365604; 15503821; 15617342; 15619904; 15649306; 15713622; 15714205; 15731180; 15776395; 15784911; 15885081; 15964425; 15972448; 15985167; 16003241; 16034095; 16060678; 16087671; 16126178; 16226465; 16293754; 16339919; 16380476; 16385451; 16410445; 16477002; 16491350; 16690518; 16698664; 16750991; 16758122; 16889540; 16911870; 16920911; 16955142; 17062437; 17074352; 17152005; 17175221; 17205058; 17237241; 17275508; 17294624; 17302593; 17304105; 17313446; 17371467; 17372588; 17389235; 17395754; 17420929; 17431094; 17462597; 17523134; 17543960; 17591854; 17604883; 17615291; 17645467; 17660530; 17661330; 17676041; 17703412; 17712998; 17878392; 17944116; 17975141; 17981806; 17985312; 18021968; 18059223; 18089681; 18162781; 18174382; 18204854; 18261176; 18287585; 18354419; 18376303; 18390743; 18451325; 18556337; 18593762; 18641303; 18641304; 18650830; 18715339; 18780166; 18818748; 18978792; 19019335; 19034005; 19073967; 19077408; 19106270; 19116909; 19119414; 19125193; 19139102; 19141347; 19155502; 19155519; 19192224; 19231135; 19240061; 19258923; 19264985; 19265545; 19289595; 19303058; 19327240; 19375175; 19375249; 19377213; 19430480; 19447046; 19471255; 19499289; 19505389; 19506219; 19522766; 19523791; 19525953; 19525955; 19527514; 19565500; 19637754; 19664391; 19667946; 19667950; 19701192; 19715524; 19734224; 19794070; 19798683; 19822714; 19833889; 19834503; 19849846; 19865102; 19879194; 19913121; 19923221; 19951265; 19956099; 19956753; 20032294; 20033399; 20063526; 20140262; 20164820; 20179739; 20203524; 20213609; 20219786; 20224778; 20237496; 20346270; 20362271; 20368992; 20378605; 20388015; 20403730; 20410501; 20424473; 20448211; 20450971; 20452482; 20453842; 20483636; 20484297; 20498205; 20503287; 20518821; 20539016; 20545784; 20562654; 20595929; 20596022; 20599261; 20615141; 20628086; 20673868; 20716621; 20716663; 20729906; 20810507; 20849903; 20930173; 21048031; 21094786; 21102463; 21131424; 21132303; 21157146; 21179414; 21180073; 21211217; 21239413; 21249500; 21278348; 21300823; 21376048; 21437244; 21525574; 21533205; 21557210; 21557772; 21571262; 21651772; 21722762; 21744325; 21757642; 21815908; 21829393; 21833088; 21839272; 21911588; 21941578; 21949691; 21980389; 22012429; 22032685; 22117963; 22158072; 22190364; 22195034; 22211793; 22213266; 22222639; 22228203; 22266274; 22293688; 22294642; 22309031; 22310634; 22313865; 22419479; 22436290; 22446965; 22447883; 22461703; 22466163; 22479496; 22516956; 22537764; 22554193; 22558434; 22564647; 22576476; 22623161; 22672991; 22824721; 22897480; 23103669; 23116454; 23121673; 23128233; 23129754; 23170961; 23217119; 23282736; 23320892; 23340699; 23345407; 23383287; 23416241; 23418630; 23508266; 23510625; 23512675; 23529819; 23665204; 23676143; 23715268; 23758320; 23817569; 23870656; 23874506; 23904478; 24134837; 24159173; 24163352; 24449572 interleukin 2 receptor, alpha Ensembl:ENSG00000134460 HGNC:6008 HPRD:00986 MIM:147730 Vega:OTTHUMG00000017616 IL2RA OGG:3000003560 Bin Zhao, Yue Liu, Oliver He CD122 IL15RB P70-75 WEB: http://www.ncbi.nlm.nih.gov/gene IL2RB interleukin 2 receptor, beta 3560 RP5-1170K4.6 22q13.1 20140408 9606 22 protein-coding Official from a nomenclature committee GO_0004911 (EC: IDA, PMID: 7736574); GO_0004911 (EC: TAS, Qualifier: contributes_to, PMID: 2467293); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 8514792); GO_0006461 (EC: TAS, PMID: 2467293); GO_0007165 (EC: TAS, PMID: 2785715); GO_0009897 (EC: ISS); GO_0016032 (EC: IEA); GO_0019221 (EC: IDA, PMID: 7736574); GO_0019976 (EC: ISS); GO_0038110 (EC: IDA, PMID: 7736574); GO_0038110 (EC: TAS, PMID: 2467293); GO_0043066 (EC: IDA, PMID: 7736574) PMID: 1394441; 1557373; 1639773; 1915291; 1973832; 2047859; 2303462; 2315327; 2333293; 2467293; 2785715; 2843775; 3925551; 7529123; 7600304; 7641685; 7693677; 7734194; 7736574; 7973658; 7973659; 8026467; 8041779; 8049354; 8294403; 8483935; 8493579; 8514792; 8648694; 8700888; 9176231; 9341758; 9520455; 9553136; 9637477; 9774657; 10214954; 10373548; 10514520; 10591208; 10602027; 10825200; 11035066; 11133764; 11238664; 11359922; 11463390; 11750878; 11856346; 11886175; 12133952; 12200137; 12230826; 12477932; 12676936; 12960323; 14680494; 15063762; 15191519; 15350462; 15461802; 15489334; 16084898; 16284400; 16293754; 16380905; 16477002; 17108990; 17115417; 17152005; 17703412; 18299274; 18445679; 18490721; 18589435; 18592269; 18715339; 18774388; 18791162; 18818748; 18829468; 19019335; 19240061; 19258923; 19471255; 19527514; 19602517; 19615332; 19773451; 19817957; 19822714; 19913121; 19923221; 20049410; 20140262; 20179739; 20219786; 20237496; 20379614; 20424473; 20495002; 20498205; 20503287; 20585888; 20628086; 20728947; 20811626; 20860503; 21345943; 21362618; 21653640; 21674833; 21829393; 21834013; 21839273; 21865161; 21984699; 22558434; 22573796; 23341462; 23418630; 23512675; 23628622; 23676143 interleukin 2 receptor, beta Ensembl:ENSG00000100385 HGNC:6009 HPRD:00896 MIM:146710 Vega:OTTHUMG00000150534 Other designations: CD122 antigen|IL-2 receptor subunit beta|IL-2R subunit beta|IL-2RB|high affinity IL-2 receptor beta subunit|high affinity IL-2 receptor subunit beta|interleukin 15 receptor, beta|interleukin-2 receptor subunit beta|p75 IL2RB OGG:3000003562 Bin Zhao, Yue Liu, Oliver He IL-3 MCGF MULTI-CSF WEB: http://www.ncbi.nlm.nih.gov/gene IL3 interleukin 3 3562 5q31.1 20140409 9606 5 protein-coding Official from a nomenclature committee GO_0005125 (EC: IEA); GO_0005135 (EC: TAS, PMID: 2544122); GO_0005576 (EC: TAS); GO_0005615 (EC: ISS); GO_0006955 (EC: IEA); GO_0007267 (EC: TAS, PMID: 3497400); GO_0007399 (EC: TAS, PMID: 9736740); GO_0008083 (EC: IEA); GO_0008284 (EC: ISS); GO_0035162 (EC: IDA); GO_0042523 (EC: IDA, PMID: 9722506); GO_0045740 (EC: IDA, PMID: 9722506); GO_0050731 (EC: ISS) PMID: 1833064; 2268499; 2544122; 3127463; 3489530; 3497400; 3497843; 7642615; 7957082; 8018916; 8516290; 8649415; 8676386; 9030599; 9113989; 9209414; 9278420; 9551928; 9629242; 9659156; 9722506; 9736740; 10477722; 10677502; 11179015; 11399510; 11486081; 11700046; 11714768; 11763346; 11861295; 11994280; 12002675; 12055233; 12089333; 12093816; 12135758; 12165512; 12423306; 12477932; 12612065; 12759409; 12855588; 12884288; 12943658; 14551608; 14564341; 14615378; 14628073; 14675189; 14755254; 15060062; 15372022; 15372320; 15489334; 15576295; 15585837; 15878977; 15988318; 16785501; 17179997; 17207965; 17273755; 17362254; 17507237; 17541278; 17624239; 17703412; 18633131; 18676680; 18692472; 18768389; 18804346; 18826654; 18829683; 19074885; 19131452; 19158269; 19170196; 19201898; 19247692; 19258923; 19262575; 19529981; 19578876; 19625176; 19692168; 19730683; 19829692; 19845895; 19913121; 20147630; 20210668; 20237496; 20332709; 20381581; 20424473; 20452482; 20453000; 20472554; 20503287; 20516062; 20628086; 20673868; 20738848; 20800603; 20964623; 21071541; 21102463; 21168724; 21224257; 21262803; 21506110; 21643009; 22321809; 22412388; 22515947; 23024272; 23128233; 23226269; 23726808 interleukin 3 Ensembl:ENSG00000164399 HGNC:6011 HPRD:00987 MIM:147740 Vega:OTTHUMG00000059640 Other designations: P-cell stimulating factor|P-cell-stimulating factor|colony-stimulating factor, multiple|hematopoietic growth factor|interleukin 3 (colony-stimulating factor, multiple)|interleukin-3|mast cell growth factor|mast-cell growth factor|multilineage-colony-stimulating factor|multipotential colony-stimulating factor IL3 OGG:3000003565 Bin Zhao, Yue Liu, Oliver He BCGF-1 BCGF1 BSF-1 BSF1 IL-4 WEB: http://www.ncbi.nlm.nih.gov/gene IL4 interleukin 4 3565 5q31.1 9606 5 Official from a nomenclature committee GO_0002227 (EC: IEA); GO_0002296 (EC: IEA); GO_0002674 (EC: IEA); GO_0002677 (EC: IEA); GO_0005125 (EC: IEA); GO_0005136 (EC: TAS, PMID: 11418631); GO_0005515 (EC: IPI, PMID: 10219247); GO_0005615 (EC: TAS, PMID: 11418631); GO_0006935 (EC: TAS, PMID: 10725748); GO_0006955 (EC: TAS, PMID: 3016727); GO_0006968 (EC: TAS, PMID: 10725748); GO_0007565 (EC: IEA); GO_0007584 (EC: IEA); GO_0008083 (EC: NAS, PMID: 11418631); GO_0008203 (EC: ISS, PMID: 11971948); GO_0009897 (EC: IEA); GO_0010155 (EC: IEA); GO_0014070 (EC: IEA); GO_0030183 (EC: TAS, PMID: 11418631); GO_0030890 (EC: ISS); GO_0031296 (EC: IEA); GO_0032733 (EC: IEA); GO_0032736 (EC: IDA, PMID: 19346497); GO_0034097 (EC: IEA); GO_0035745 (EC: IDA); GO_0042092 (EC: TAS, PMID: 11676128); GO_0042102 (EC: ISS); GO_0042104 (EC: IEA); GO_0042325 (EC: ISS); GO_0042493 (EC: IEA); GO_0042523 (EC: IEA); GO_0042832 (EC: IEA); GO_0043031 (EC: IEA); GO_0043066 (EC: ISS); GO_0045019 (EC: IEA); GO_0045064 (EC: IEA); GO_0045080 (EC: IEA); GO_0045189 (EC: TAS, PMID: 11967989); GO_0045191 (EC: TAS, PMID: 11418631); GO_0045348 (EC: ISS); GO_0045471 (EC: IEA); GO_0045582 (EC: IDA); GO_0045671 (EC: ISS); GO_0045892 (EC: IDA, PMID: 18579517); GO_0045893 (EC: IDA, PMID: 18579517); GO_0045944 (EC: ISS); GO_0048295 (EC: ISS); GO_0048304 (EC: ISS); GO_0050776 (EC: ISS); GO_0051091 (EC: IEA); GO_0071288 (EC: IEA); GO_0097028 (EC: IDA); GO_0097192 (EC: IEA); GO_2000320 (EC: IEA); GO_2001237 (EC: IEA) PMID: 1197194; 1346976; 1400355; 1511746; 1567880; 1567881; 1569578; 1609277; 1932028; 1946344; 1993171; 2535858; 3016727; 3257560; 7523014; 7589092; 7664036; 7695626; 7806280; 7963560; 8151703; 8266078; 8516290; 8602263; 8603435; 8609418; 8764000; 9113989; 9130521; 9130652; 9334723; 9799097; 9856950; 10219247; 10438901; 10473513; 10623799; 10710213; 10714547; 10725748; 10753117; 10853974; 11023480; 11035134; 11122213; 11149986; 11167377; 11233912; 11258628; 11258696; 11294568; 11298547; 11315919; 11316066; 11316069; 11320251; 11350513; 11396683; 11418631; 11466338; 11496248; 11502824; 11528525; 11587989; 11676128; 11678851; 11704810; 11728464; 11777980; 11786020; 11811777; 11841848; 11842291; 11872954; 11877044; 11881490; 11886168; 11897522; 11897999; 11907068; 11920312; 11922633; 11930331; 11950517; 11953141; 11960309; 11967989; 11968047; 11971948; 11980568; 11994288; 12020266; 12030894; 12039414; 12063527; 12066847; 12072494; 12082592; 12089714; 12102661; 12105273; 12107748; 12115161; 12121273; 12124654; 12133437; 12144536; 12161424; 12162874; 12165514; 12207324; 12220533; 12358844; 12363051; 12366695; 12368275; 12402189; 12420205; 12426308; 12435565; 12441140; 12442007; 12470598; 12477932; 12479817; 12504082; 12508140; 12508786; 12509382; 12513914; 12515722; 12517954; 12525574; 12542496; 12552499; 12574355; 12578333; 12587822; 12595908; 12600829; 12613995; 12626590; 12660931; 12663328; 12667657; 12687213; 12687247; 12689929; 12694433; 12700447; 12715242; 12738651; 12748907; 12753568; 12813360; 12851716; 12877559; 12884288; 12897746; 12900808; 12902508; 12911786; 12940513; 12944981; 12973929; 14499500; 14503851; 14522096; 14523823; 14530362; 14551608; 14561191; 14568946; 14583474; 14610476; 14634065; 14634100; 14652008; 14654080; 14675394; 14681304; 14688371; 14692664; 14693849; 14697238; 14697936; 14725568; 14729510; 14746805; 14764715; 14767810; 14983029; 14986816; 15001290; 15004182; 15007352; 15013759; 15014952; 15021309; 15041089; 15042002; 15051937; 15057902; 15063762; 15084933; 15086621; 15087090; 15100288; 15122773; 15123681; 15128803; 15163899; 15166131; 15170937; 15177147; 15178889; 15187156; 15191519; 15210741; 15213252; 15215692; 15241348; 15274656; 15292002; 15297269; 15298559; 15322832; 15361128; 15367434; 15373917; 15474066; 15489334; 15501397; 15527169; 15528258; 15563083; 15570643; 15591113; 15592292; 15596681; 15627726; 15644127; 15660235; 15660293; 15661875; 15676220; 15678501; 15679809; 15687724; 15695802; 15713213; 15714203; 15723707; 15733644; 15755291; 15778356; 15811521; 15816837; 15825027; 15869882; 15883744; 15885323; 15900570; 15900573; 15904474; 15919378; 15932621; 15941525; 15951665; 15969687; 15970635; 16001979; 16002690; 16004996; 16034134; 16043936; 16044136; 16046318; 16053729; 16083175; 16083600; 16091861; 16100774; 16164695; 16166103; 16184405; 16190985; 16193177; 16195814; 16215326; 16230423; 16232344; 16249002; 16289646; 16301860; 16313303; 16313681; 16315031; 16334248; 16343431; 16375755; 16380445; 16387595; 16388492; 16403098; 16427155; 16429138; 16429733; 16449530; 16461126; 16466711; 16487180; 16492782; 16511411; 16520888; 16522370; 16544245; 16547227; 16547693; 16551465; 16573560; 16574063; 16596275; 16601843; 16640778; 16681592; 16690518; 16702372; 16707627; 16720107; 16722389; 16750991; 16750993; 16759385; 16810739; 16864907; 16867043; 16877367; 16914241; 16916659; 16929824; 16930576; 16931887; 16938461; 16950634; 16973957; 16987060; 17006724; 17014622; 17015714; 17015735; 17063753; 17097641; 17117487; 17121586; 17133536; 17141086; 17143971; 17148075; 17151125; 17151939; 17152005; 17159260; 17177148; 17203290; 17207024; 17208210; 17209513; 17213232; 17222831; 17237413; 17257312; 17284225; 17291854; 17295710; 17299718; 17303794; 17303923; 17309781; 17311314; 17327605; 17355643; 17369174; 17371990; 17379175; 17388919; 17389011; 17389870; 17405833; 17420820; 17428692; 17433443; 17444864; 17451413; 17454884; 17460561; 17523428; 17524861; 17530998; 17536219; 17540990; 17541280; 17548690; 17563406; 17566759; 17576577; 17623648; 17627763; 17631734; 17640324; 17640674; 17644317; 17653830; 17655693; 17656331; 17662651; 17678726; 17703412; 17714919; 17851828; 17855802; 17882904; 17889143; 17908769; 17914408; 17916404; 17916900; 17937745; 17938902; 17961771; 17968425; 18008330; 18031948; 18042256; 18056382; 18058260; 18064451; 18088017; 18156980; 18165865; 18174230; 18179754; 18179773; 18202702; 18204280; 18206261; 18210751; 18211631; 18230112; 18239807; 18243101; 18251702; 18263811; 18273035; 18273643; 18276105; 18286287; 18294957; 18295676; 18310157; 18322173; 18342537; 18351434; 18371377; 18385759; 18389618; 18394346; 18396027; 18403443; 18410779; 18418228; 18422436; 18425216; 18433468; 18439079; 18441098; 18448485; 18454680; 18455629; 18476609; 18485518; 18497474; 18522869; 18533937; 18538381; 18547691; 18558283; 18566561; 18568448; 18568476; 18574615; 18579517; 18593330; 18596736; 18597704; 18599603; 18610831; 18610832; 18614592; 18624944; 18625055; 18626468; 18628242; 18629290; 18632425; 18633131; 18635180; 18636124; 18641314; 18651887; 18662263; 18674658; 18676680; 18676870; 18682601; 18688110; 18694328; 18696265; 18708672; 18716132; 18776133; 18781131; 18818748; 18834248; 18924208; 18927306; 18931892; 18936436; 18941246; 18955794; 18971287; 18971305; 18974110; 18974840; 19008611; 19013323; 19019335; 19028820; 19050632; 19058298; 19058839; 19066394; 19074885; 19116009; 19117745; 19122650; 19126646; 19129082; 19131452; 19131662; 19141349; 19164348; 19168731; 19169254; 19170196; 19185507; 19190772; 19193442; 19200845; 19222422; 19247692; 19249119; 19251840; 19254294; 19258923; 19261373; 19262574; 19263529; 19264973; 19275586; 19279357; 19332120; 19332998; 19336370; 19346497; 19347053; 19351467; 19370405; 19372547; 19375306; 19382262; 19385959; 19408823; 19409508; 19419769; 19421745; 19426601; 19437232; 19470040; 19479237; 19495883; 19497039; 19505916; 19508433; 19515749; 19521787; 19527514; 19536153; 19541591; 19544559; 19544973; 19552791; 19555572; 19559392; 19566553; 19573080; 19575932; 19578876; 19586918; 19586939; 19594368; 19621989; 19625176; 19657367; 19682920; 19683555; 19692168; 19698128; 19699526; 19706316; 19707465; 19718656; 19718824; 19721012; 19726720; 19735490; 19753334; 19762488; 19772762; 19773279; 19773451; 19799628; 19804407; 19811408; 19817957; 19818512; 19835477; 19840389; 19845895; 19857574; 19860911; 19862939; 19878651; 19882211; 19892918; 19910025; 19913121; 19915002; 19933216; 19938203; 19948975; 19959237; 20003246; 20010912; 20012528; 20016407; 20027321; 20030788; 20039421; 20049266; 20053586; 20056178; 20059579; 20082482; 20093796; 20100010; 20112007; 20121760; 20128416; 20139223; 20140262; 20145925; 20147633; 20177758; 20184663; 20192866; 20213229; 20217044; 20219689; 20222161; 20237496; 20299965; 20304823; 20305143; 20332709; 20349326; 20349753; 20364398; 20367137; 20394509; 20395963; 20403914; 20406299; 20413987; 20416077; 20418110; 20424473; 20442634; 20444155; 20452482; 20453000; 20459687; 20485362; 20503287; 20506498; 20517665; 20524005; 20525402; 20530519; 20533927; 20536507; 20565368; 20568250; 20580039; 20603037; 20603050; 20618516; 20620947; 20628086; 20644561; 20673868; 20703737; 20711808; 20713631; 20716621; 20719954; 20723894; 20726231; 20736038; 20808855; 20811626; 20814620; 20839488; 20852371; 20859068; 20880001; 20921925; 20942272; 20970781; 20980261; 21048327; 21054877; 21061265; 21067483; 21071541; 21085635; 21086908; 21106245; 21106524; 21111725; 21127885; 21191414; 21195738; 21198753; 21211660; 21268015; 21270410; 21276216; 21323696; 21354455; 21460743; 21471214; 21478113; 21501388; 21611195; 21636115; 21640045; 21644211; 21645924; 21646796; 21658970; 21690322; 21713407; 21729106; 21749213; 21755390; 21771210; 21788379; 21799768; 21819409; 21846818; 21857939; 21890374; 21900165; 21913997; 21966389; 21989417; 22045834; 22053598; 22087298; 22092872; 22104567; 22142023; 22143036; 22156341; 22157213; 22170601; 22174091; 22214155; 22226971; 22227092; 22249152; 22358381; 22365405; 22366824; 22387551; 22406175; 22441356; 22484241; 22484276; 22512783; 22521249; 22528336; 22538865; 22574929; 22583827; 22594992; 22615205; 22652416; 22675249; 22705603; 22805022; 22805115; 22824342; 22875803; 22884982; 22892939; 22921153; 22942430; 22986179; 22992805; 22997428; 23070918; 23087426; 23107766; 23110190; 23124025; 23128233; 23185315; 23222300; 23234779; 23245479; 23259293; 23276701; 23306429; 23333893; 23334651; 23376457; 23394902; 23398789; 23454622; 23511027; 23527200; 23527710; 23559861; 23572437; 23576103; 23591975; 23644020; 23651591; 23654077; 23668806; 23685257; 23694808; 23756167; 23756192; 23766027; 23768103; 23797532; 23831512; 23844087; 23883285; 23913957; 23923066; 23924473; 23935100; 23936398; 23958647; 23964553; 23983153; 24406619; 24510574 interleukin 4 Ensembl:ENSG00000113520 HGNC:6014 HPRD:00989 MIM:147780 Vega:OTTHUMG00000059724 Other designations: B cell growth factor 1|B_cell stimulatory factor 1|binetrakin|interleukin 4 variant 2|interleukin-4|lymphocyte stimulatory factor 1|pitrakinra IL4 OGG:3000003567 Bin Zhao, Yue Liu, Oliver He EDF IL-5 TRF WEB: http://www.ncbi.nlm.nih.gov/gene IL5 interleukin 5 3567 5q31.1 20140409 9606 5 protein-coding Official from a nomenclature committee GO_0005125 (EC: IEA); GO_0005137 (EC: IEA); GO_0005515 (EC: IPI, PMID: 1495999); GO_0005576 (EC: IDA); GO_0005576 (EC: TAS); GO_0005615 (EC: TAS, PMID: 3024129); GO_0006954 (EC: IEA); GO_0006955 (EC: IEA); GO_0008083 (EC: IEA); GO_0019221 (EC: IEA); GO_0030890 (EC: IEA); GO_0045645 (EC: IEA); GO_0045893 (EC: IEA); GO_0046427 (EC: IEA); GO_0050731 (EC: ISS); GO_0051024 (EC: IEA); GO_0051091 (EC: IEA); GO_0071803 (EC: IDA, PMID: 15220135) PMID: 1495999; 1698795; 1732409; 1833065; 2037074; 2361960; 2563351; 2823259; 2824500; 3024129; 3498940; 7534492; 7721873; 7957082; 8419187; 8438156; 8483502; 8892648; 9136909; 10417272; 10477722; 10753117; 10880230; 10973484; 11101310; 11763346; 11830476; 11842300; 11877300; 11897983; 12097386; 12202242; 12354764; 12366695; 12393708; 12444155; 12477932; 12525574; 12534990; 12575459; 12581193; 12759409; 12771545; 12851716; 12910312; 12915771; 14564341; 14581138; 14630612; 14634065; 15007355; 15155645; 15220135; 15271374; 15367434; 15489334; 15528381; 15534922; 15549733; 15563083; 15713213; 15735688; 15802551; 15805995; 15826943; 15826950; 15835818; 15842590; 15845862; 15935984; 15951665; 15964392; 16001979; 16036415; 16236836; 16243713; 16449530; 16556602; 16596275; 16722389; 16879311; 16922677; 16929824; 17015735; 17362254; 17438848; 17517104; 17567994; 17581195; 17620002; 17620072; 17623648; 17628972; 17690326; 17703412; 17845581; 18028994; 18056382; 18206982; 18273035; 18383036; 18395252; 18519231; 18633131; 18676870; 18686101; 18687755; 18712166; 18772129; 18818748; 18844613; 18849614; 18925696; 18996999; 19019335; 19050632; 19131452; 19141349; 19152965; 19168731; 19180571; 19198610; 19200845; 19222422; 19247692; 19258923; 19299749; 19336370; 19360850; 19379606; 19419945; 19478474; 19486544; 19527514; 19533685; 19573080; 19578876; 19698128; 19773279; 19773451; 19840389; 19845895; 19860791; 19913121; 19914334; 20047188; 20237496; 20332709; 20403914; 20418110; 20452482; 20453000; 20503287; 20523065; 20530519; 20561085; 20568250; 20628086; 20636896; 20650294; 20673868; 20825427; 20943047; 20952689; 21168500; 21235536; 21323726; 21418620; 21609545; 21849680; 21986312; 22092535; 22153509; 22186238; 22230487; 22528658; 22541618; 22710862; 22805115; 22962576; 23128233; 23306429; 23306834; 23328843; 23382558; 23401558; 23555579; 23684072; 23770289 interleukin 5 Ensembl:ENSG00000113525 HGNC:6016 HPRD:00997 MIM:147850 Vega:OTTHUMG00000059496 Other designations: B-cell differentiation factor I|T-cell replacing factor|colony-stimulating factor, eosinophil|eosinophil differentiation factor|interleukin 5 (colony-stimulating factor, eosinophil)|interleukin-5 IL5 OGG:3000003569 Bin Zhao, Yue Liu, Oliver He BSF2 HGF HSF IFNB2 IL-6 WEB: http://www.ncbi.nlm.nih.gov/gene IL6 interleukin 6 3569 7p21 9606 7 Official from a nomenclature committee GO_0001781 (EC: IDA, PMID: 7595060); GO_0002384 (EC: IDA, PMID: 2444978); GO_0002384 (EC: TAS, PMID: 12832423); GO_0002446 (EC: IC, PMID: 16034137); GO_0002548 (EC: IC, PMID: 10510402); GO_0002675 (EC: IDA, PMID: 2444978); GO_0002690 (EC: IC, PMID: 16034137); GO_0005125 (EC: IDA, PMID: 3023045); GO_0005125 (EC: NAS, PMID: 10443688); GO_0005138 (EC: IPI, PMID: 12829785); GO_0005138 (EC: IPI, Qualifier: contributes_to, PMID: 12829785); GO_0005138 (EC: NAS, PMID: 1883960); GO_0005515 (EC: IPI, PMID: 11238858); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 10443688); GO_0005896 (EC: IDA, PMID: 12829785); GO_0006469 (EC: IEA); GO_0006953 (EC: TAS, PMID: 12832423); GO_0006954 (EC: IDA, PMID: 10443688); GO_0006959 (EC: IC, PMID: 3491322); GO_0007568 (EC: IEA); GO_0008083 (EC: IDA, PMID: 12643274); GO_0008284 (EC: IDA, PMID: 2261637); GO_0008284 (EC: IMP, PMID: 18719127); GO_0008285 (EC: IEA); GO_0008360 (EC: IEA); GO_0009408 (EC: IEA); GO_0009409 (EC: IEA); GO_0009612 (EC: IEA); GO_0009897 (EC: IEA); GO_0010574 (EC: IDA, PMID: 8557680); GO_0010888 (EC: NAS, PMID: 16464856); GO_0016049 (EC: IEA); GO_0019221 (EC: IDA, PMID: 12643274); GO_0030168 (EC: TAS, PMID: 7831669); GO_0031000 (EC: IEA); GO_0031018 (EC: ISS, PMID: 18719127); GO_0031175 (EC: IMP, PMID: 3264880); GO_0031667 (EC: IEA); GO_0032494 (EC: IEP, PMID: 16034137); GO_0032496 (EC: IEA); GO_0032722 (EC: IDA, PMID: 10510402); GO_0032722 (EC: IMP, PMID: 16034137); GO_0032755 (EC: IDA, PMID: 10510402); GO_0032868 (EC: IEA); GO_0032966 (EC: IDA, PMID: 12419823); GO_0033138 (EC: IDA, PMID: 7508917); GO_0033160 (EC: IEA); GO_0042102 (EC: IDA, PMID: 3130269); GO_0042493 (EC: IEA); GO_0042517 (EC: IDA, PMID: 12643274); GO_0042832 (EC: IEA); GO_0043065 (EC: IDA, PMID: 9949178); GO_0043066 (EC: IDA, PMID: 7595060); GO_0043154 (EC: IEA); GO_0043200 (EC: IEA); GO_0043410 (EC: IDA, PMID: 12419823); GO_0045079 (EC: ISS); GO_0045188 (EC: IEA); GO_0045429 (EC: IEA); GO_0045454 (EC: IEA); GO_0045599 (EC: NAS, PMID: 16464856); GO_0045630 (EC: IEA); GO_0045666 (EC: IEA); GO_0045669 (EC: TAS, PMID: 12372336); GO_0045721 (EC: IEA); GO_0045727 (EC: IDA, PMID: 16732314); GO_0045740 (EC: IEA); GO_0045765 (EC: IC, PMID: 8557680); GO_0045893 (EC: IDA, PMID: 7749983); GO_0045944 (EC: IDA, PMID: 17324931); GO_0046427 (EC: IDA, PMID: 12419823); GO_0046677 (EC: IEA); GO_0046716 (EC: IEA); GO_0046849 (EC: IEA); GO_0046888 (EC: IEA); GO_0048635 (EC: IEA); GO_0048661 (EC: IDA, PMID: 10510402); GO_0050679 (EC: IEA); GO_0050710 (EC: IEA); GO_0050731 (EC: IDA, PMID: 7508917); GO_0050829 (EC: IEP, PMID: 16034137); GO_0050830 (EC: IEP, PMID: 16034137); GO_0050871 (EC: IDA, PMID: 3491322); GO_0051024 (EC: IDA, PMID: 3491322); GO_0051091 (EC: IDA, PMID: 7749983); GO_0051092 (EC: IDA, Qualifier: NOT, PMID: 12419823); GO_0051384 (EC: IDA, PMID: 10443688); GO_0051592 (EC: IEA); GO_0051602 (EC: IEA); GO_0051607 (EC: IDA, PMID: 3023045); GO_0051897 (EC: IEA); GO_0051971 (EC: IEA); GO_0060445 (EC: IEA); GO_0060664 (EC: IEA); GO_0070091 (EC: ISS, PMID: 18719127); GO_0070102 (EC: IDA, PMID: 12552091); GO_0070301 (EC: IDA, PMID: 19168699); GO_0070374 (EC: IEA); GO_0072540 (EC: ISS); GO_1901215 (EC: IEA); GO_2000366 (EC: IC, PMID: 17324931); GO_2000676 (EC: TAS, PMID: 18719127) PMID: 1113021; 1291290; 1346976; 1610348; 1656094; 1883960; 1918997; 2037043; 2261637; 2444978; 2472117; 2610854; 2680567; 2788034; 2789513; 2829354; 2906047; 3023045; 3130269; 3264880; 3266463; 3279116; 3294161; 3320204; 3491322; 3500852; 3538015; 3758081; 7494249; 7508917; 7511078; 7511596; 7523444; 7526541; 7536422; 7553888; 7595060; 7656270; 7693046; 7704970; 7749983; 7803268; 7815507; 7831669; 7851440; 7986583; 8018916; 8086129; 8113688; 8179923; 8190832; 8206884; 8247028; 8510564; 8555185; 8557680; 8764000; 8806809; 8938574; 9094636; 9108403; 9118960; 9159484; 9169458; 9225992; 9378998; 9658081; 9671211; 9792375; 9927325; 9949178; 10358063; 10388525; 10415019; 10443688; 10510402; 10657672; 10671302; 10775602; 10777583; 10925276; 10964543; 11028446; 11040178; 11054276; 11072134; 11072751; 11116068; 11145851; 11167813; 11196676; 11196678; 11199329; 11204808; 11212160; 11224491; 11233912; 11238858; 11266856; 11266927; 11266928; 11267084; 11282548; 11312376; 11315919; 11316066; 11342474; 11354638; 11355017; 11371414; 11391238; 11397324; 11404167; 11448119; 11485024; 11500818; 11517385; 11520812; 11544427; 11544434; 11544437; 11557672; 11574109; 11640949; 11687509; 11689614; 11692078; 11703956; 11713964; 11716039; 11728144; 11733366; 11751408; 11758653; 11774563; 11777983; 11781191; 11788581; 11792588; 11794009; 11801594; 11818668; 11820460; 11847482; 11849463; 11853279; 11855786; 11858187; 11862386; 11884027; 11884029; 11884401; 11884403; 11889177; 11895465; 11902285; 11906646; 11914754; 11918227; 11919083; 11922913; 11949822; 11950481; 11950697; 11956023; 11959895; 11960393; 11961304; 11966578; 11981433; 11983287; 11984595; 11988246; 11988625; 11990931; 11992567; 12000745; 12012622; 12027404; 12031914; 12032172; 12036196; 12038454; 12047360; 12050565; 12051396; 12067898; 12070032; 12080442; 12082590; 12082592; 12086705; 12089333; 12089714; 12091348; 12095061; 12096924; 12096927; 12107724; 12110411; 12114287; 12117737; 12117921; 12117953; 12121679; 12133353; 12140751; 12149213; 12150965; 12151314; 12164325; 12165085; 12176919; 12183057; 12185451; 12187073; 12198224; 12200114; 12201209; 12202945; 12214260; 12215823; 12217290; 12218157; 12219016; 12220549; 12226829; 12232842; 12235153; 12239630; 12240899; 12297113; 12297725; 12352619; 12359225; 12359431; 12370346; 12370360; 12370503; 12371985; 12372336; 12382118; 12383455; 12391243; 12392859; 12393446; 12393542; 12393699; 12394188; 12396456; 12412787; 12413693; 12419823; 12430875; 12431817; 12445202; 12445803; 12451269; 12453469; 12468916; 12472176; 12477932; 12482836; 12483530; 12491092; 12493411; 12495721; 12507818; 12509497; 12517591; 12517814; 12519862; 12526950; 12540635; 12552091; 12553555; 12554901; 12558814; 12559950; 12560330; 12560873; 12571160; 12574335; 12574550; 12584029; 12585340; 12589429; 12590978; 12591385; 12592380; 12594059; 12595908; 12606524; 12615367; 12618859; 12626585; 12629515; 12633940; 12634650; 12637697; 12643274; 12647840; 12651071; 12653788; 12657090; 12660820; 12660878; 12663465; 12664314; 12668153; 12668157; 12681965; 12690205; 12694213; 12709682; 12713584; 12714254; 12714267; 12716337; 12719374; 12720537; 12727482; 12727794; 12727841; 12727948; 12727959; 12736743; 12737276; 12742994; 12743452; 12745542; 12746914; 12748876; 12754410; 12756345; 12757654; 12760309; 12768442; 12770686; 12771987; 12789531; 12790760; 12792728; 12794182; 12796383; 12799618; 12802423; 12810629; 12811627; 12815949; 12818128; 12819039; 12828754; 12829659; 12829785; 12830005; 12832117; 12832326; 12832423; 12839942; 12840146; 12843190; 12843357; 12846758; 12850808; 12853948; 12857677; 12857678; 12870175; 12871882; 12876073; 12883476; 12888915; 12897342; 12900415; 12901869; 12919773; 12923493; 12926107; 12928051; 12928784; 12932839; 12934185; 12937023; 12938195; 12940515; 12944981; 12945076; 12952969; 12958150; 12960275; 12960348; 12967650; 12969979; 12970232; 13678786; 14508181; 14508221; 14512079; 14514772; 14521945; 14522096; 14523169; 14523823; 14532843; 14557255; 14557477; 14557872; 14563376; 14566095; 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21211286; 21220315; 21226932; 21228692; 21229891; 21233768; 21235536; 21238488; 21239715; 21241793; 21245598; 21245987; 21252539; 21253506; 21253618; 21255427; 21258401; 21277639; 21278254; 21278793; 21279994; 21282066; 21282107; 21282511; 21287288; 21292497; 21293887; 21294915; 21296109; 21298325; 21300046; 21307288; 21312239; 21314275; 21316985; 21320026; 21321193; 21321840; 21321954; 21323660; 21329460; 21333594; 21334078; 21334625; 21343371; 21350025; 21352255; 21353307; 21353594; 21353595; 21355310; 21357189; 21362045; 21376376; 21377916; 21382729; 21385538; 21388350; 21393356; 21407237; 21408055; 21410438; 21414799; 21419646; 21421628; 21421702; 21422077; 21424184; 21436461; 21442077; 21454528; 21455087; 21466366; 21468030; 21468565; 21474330; 21474332; 21474440; 21478032; 21481788; 21490101; 21490132; 21492332; 21493089; 21497830; 21498913; 21511827; 21512395; 21515913; 21518761; 21518763; 21520044; 21520052; 21526159; 21527852; 21530175; 21535154; 21535317; 21536090; 21540553; 21546767; 21547256; 21559372; 21562768; 21565862; 21586579; 21591973; 21592994; 21594636; 21595886; 21600698; 21611774; 21619709; 21619877; 21620438; 21621860; 21623995; 21626471; 21632260; 21639625; 21640816; 21645137; 21656745; 21658317; 21664423; 21668366; 21681687; 21684758; 21689404; 21697747; 21700657; 21702700; 21708999; 21709158; 21712995; 21714933; 21716327; 21729562; 21740541; 21752694; 21757719; 21757746; 21762913; 21767605; 21769475; 21771210; 21773651; 21776298; 21778161; 21795706; 21801267; 21802729; 21811961; 21811986; 21813290; 21833041; 21833517; 21843047; 21845403; 21845872; 21845926; 21851175; 21854184; 21858117; 21863560; 21870243; 21875833; 21876502; 21880216; 21881374; 21881585; 21886773; 21889771; 21898505; 21898706; 21898993; 21900165; 21902578; 21911244; 21912394; 21913828; 21919032; 21921047; 21923250; 21925926; 21929671; 21931651; 21933586; 21935443; 21938724; 21952248; 21953462; 21954831; 21957581; 21959016; 21961943; 21965736; 21966220; 21967801; 21976712; 21977994; 21982018; 21983734; 21984125; 21989726; 21995322; 21995333; 21996739; 22000300; 22004976; 22010855; 22012292; 22015309; 22015454; 22018243; 22019000; 22019436; 22021612; 22023383; 22024650; 22025890; 22027148; 22030312; 22030478; 22035595; 22046434; 22048241; 22052387; 22053612; 22055894; 22068677; 22068875; 22070971; 22072054; 22072539; 22075267; 22078452; 22082020; 22084439; 22105366; 22107760; 22113576; 22113815; 22115178; 22117975; 22119941; 22122521; 22132241; 22133543; 22135153; 22140472; 22150003; 22155094; 22156348; 22158046; 22159219; 22171160; 22171994; 22174866; 22180363; 22187702; 22192353; 22194466; 22196489; 22203929; 22203932; 22205395; 22209080; 22228719; 22229879; 22230324; 22234866; 22242132; 22243796; 22252554; 22261689; 22265273; 22272811; 22289556; 22296202; 22296277; 22301094; 22301607; 22303451; 22304944; 22306454; 22324945; 22330622; 22334615; 22337942; 22349830; 22350281; 22357713; 22362117; 22364742; 22365967; 22366404; 22367386; 22369948; 22382666; 22385075; 22386866; 22386961; 22387051; 22389450; 22403134; 22407921; 22410655; 22417709; 22417897; 22420891; 22421411; 22422499; 22425021; 22426116; 22426177; 22426431; 22427231; 22427564; 22427681; 22428468; 22431998; 22434029; 22436412; 22441019; 22445549; 22452603; 22452847; 22457277; 22457856; 22459738; 22462419; 22466975; 22468900; 22473756; 22475215; 22479352; 22481167; 22486303; 22491065; 22496403; 22496888; 22503230; 22507133; 22508062; 22513191; 22516897; 22521547; 22531363; 22531887; 22532634; 22532637; 22539302; 22552350; 22553973; 22554382; 22562290; 22563871; 22565057; 22569438; 22571276; 22575724; 22577092; 22579111; 22579472; 22580582; 22580886; 22583691; 22586157; 22592039; 22595649; 22615316; 22616715; 22617158; 22617683; 22634718; 22642105; 22644871; 22647735; 22648519; 22667128; 22672862; 22673037; 22677780; 22677919; 22681487; 22686131; 22687336; 22688021; 22692705; 22695063; 22696056; 22698992; 22701584; 22710869; 22711534; 22711691; 22714907; 22726456; 22728071; 22734797; 22739041; 22739042; 22740511; 22743617; 22752116; 22753384; 22761193; 22761857; 22763042; 22763101; 22769440; 22773460; 22782910; 22796263; 22808178; 22810465; 22814248; 22814515; 22818022; 22819248; 22819326; 22819759; 22836752; 22843654; 22843899; 22849850; 22867712; 22869038; 22872134; 22883217; 22883518; 22894740; 22895491; 22904305; 22906998; 22908985; 22921280; 22923190; 22923236; 22924939; 22927445; 22931953; 22948743; 22956742; 22964303; 22968454; 22976070; 22977256; 22977658; 22982189; 22983646; 22984080; 22984233; 22986484; 22990627; 23009764; 23013217; 23013513; 23018032; 23019398; 23022409; 23025692; 23027872; 23027890; 23034889; 23036532; 23038213; 23043537; 23044206; 23052480; 23052692; 23056300; 23058014; 23058031; 23062767; 23065424; 23071313; 23073774; 23078005; 23078984; 23086036; 23087143; 23088295; 23092922; 23097096; 23100065; 23116190; 23117246; 23118848; 23124416; 23124693; 23136553; 23136554; 23136556; 23142265; 23154434; 23158132; 23159256; 23159283; 23161179; 23166328; 23168096; 23168996; 23175672; 23177780; 23178494; 23180271; 23185547; 23190106; 23195133; 23197841; 23198942; 23204162; 23206733; 23207068; 23219526; 23224211; 23225885; 23227240; 23232337; 23233117; 23236659; 23242654; 23246692; 23250823; 23251686; 23255681; 23257175; 23262029; 23265967; 23269580; 23272057; 23276493; 23276701; 23281720; 23289913; 23298711; 23300019; 23303450; 23311694; 23320781; 23322593; 23322904; 23326472; 23332218; 23336844; 23344094; 23347173; 23348396; 23349093; 23349310; 23350010; 23357299; 23357300; 23363979; 23364322; 23369187; 23371411; 23375410; 23377045; 23378274; 23378460; 23380741; 23389820; 23392112; 23399848; 23408619; 23411129; 23415255; 23421536; 23423626; 23425215; 23428306; 23441314; 23444260; 23461479; 23461851; 23470607; 23470916; 23478175; 23480455; 23484124; 23487197; 23489698; 23490068; 23490413; 23498057; 23505291; 23506572; 23509207; 23510010; 23510983; 23517877; 23524623; 23525184; 23536722; 23538947; 23555579; 23555719; 23559389; 23561329; 23564454; 23564789; 23567762; 23569034; 23582441; 23582716; 23591770; 23593036; 23593346; 23601055; 23616277; 23617681; 23619188; 23622344; 23625043; 23630220; 23632023; 23633489; 23633491; 23637318; 23637926; 23638863; 23639700; 23648010; 23651237; 23654074; 23657600; 23658720; 23665320; 23666170; 23674845; 23701120; 23735697; 23737648; 23743311; 23746176; 23748363; 23756867; 23761639; 23762476; 23762858; 23766379; 23770252; 23774701; 23776669; 23777202; 23784949; 23785756; 23791019; 23792529; 23807226; 23815102; 23819403; 23821953; 23828679; 23832741; 23844163; 23884764; 23889749; 23893709; 23910616; 23913484; 23921153; 23928667; 23929842; 23933386; 23936495; 23953057; 23953866; 23954444; 23954871; 23968978; 23969696; 24032723; 24043651; 24044580; 24051035; 24077340; 24078775; 24114793; 24120137; 24136650; 24152848; 24186266; 24200066; 24243972; 24265545; 24294778; 24299316; 24308236; 24314919; 24340926; 24409674; 24434384; 24547612 interleukin 6 Ensembl:ENSG00000136244 HGNC:6018 HPRD:00970 MIM:147620 Vega:OTTHUMG00000023178 Other designations: B-cell differentiation factor|B-cell stimulatory factor 2|BSF-2|CDF|CTL differentiation factor|IFN-beta-2|hybridoma growth factor|interferon beta-2|interferon, beta 2|interleukin 6 (interferon, beta 2)|interleukin BSF-2|interleukin-6 IL6 OGG:3000003570 Bin Zhao, Yue Liu, Oliver He CD126 IL-6R-1 IL-6RA IL6Q IL6RA IL6RQ gp80 WEB: http://www.ncbi.nlm.nih.gov/gene IL6R interleukin 6 receptor 3570 1q21 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0002384 (EC: TAS, PMID: 12832423); GO_0002446 (EC: IC, PMID: 16034137); GO_0002548 (EC: IC, PMID: 10510402); GO_0002690 (EC: IC, PMID: 16034137); GO_0002690 (EC: TAS, PMID: 15100312); GO_0004897 (EC: IMP, Qualifier: contributes_to, PMID: 12643274); GO_0004915 (EC: IDA, Qualifier: contributes_to, PMID: 2261637); GO_0005138 (EC: IPI, Qualifier: contributes_to, PMID: 12829785); GO_0005515 (EC: IPI, PMID: 11238858); GO_0005576 (EC: IDA, PMID: 12748171); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 12419823); GO_0005886 (EC: TAS); GO_0005896 (EC: IDA, PMID: 12829785); GO_0006953 (EC: TAS, PMID: 12832423); GO_0008284 (EC: IDA, PMID: 2261637); GO_0008284 (EC: IMP, PMID: 18719127); GO_0009986 (EC: IEA); GO_0010536 (EC: IDA, PMID: 12419823); GO_0016323 (EC: IEA); GO_0016324 (EC: IDA, PMID: 16034137); GO_0019221 (EC: IDA, PMID: 2261637); GO_0019899 (EC: IPI, PMID: 12748171); GO_0019981 (EC: IPI, PMID: 12829785); GO_0031018 (EC: IC, PMID: 18719127); GO_0031018 (EC: IMP, PMID: 18719127); GO_0032717 (EC: IEP, PMID: 16034137); GO_0032722 (EC: IDA, PMID: 10510402); GO_0032755 (EC: IDA, PMID: 10510402); GO_0032966 (EC: IDA, PMID: 12419823); GO_0034097 (EC: IDA, PMID: 2261637); GO_0042517 (EC: IMP, PMID: 12643274); GO_0042803 (EC: IPI, PMID: 12633863); GO_0043410 (EC: IDA, PMID: 12419823); GO_0045669 (EC: TAS, PMID: 12372336); GO_0048661 (EC: IDA, PMID: 10510402); GO_0050731 (EC: IDA, PMID: 11884403); GO_0050829 (EC: IEP, PMID: 16034137); GO_0050830 (EC: IEP, PMID: 16034137); GO_0051092 (EC: IDA, Qualifier: NOT, PMID: 12419823); GO_0070102 (EC: IMP, PMID: 12643274); GO_0070119 (EC: IPI, PMID: 12643274); GO_0070120 (EC: IMP, PMID: 12643274); GO_0097191 (EC: TAS, PMID: 15100312) PMID: 1281789; 1381187; 1872801; 1889804; 2112585; 2157217; 2261637; 2529343; 2788034; 3136546; 8056053; 8125298; 8265649; 8428753; 8450224; 8467812; 8889549; 9169421; 9927325; 10066782; 10462375; 10510402; 10777583; 10785334; 10982829; 11017875; 11238858; 11884403; 12002769; 12008038; 12079407; 12372336; 12412787; 12414855; 12419823; 12445803; 12461182; 12472176; 12477932; 12553038; 12553555; 12574959; 12633863; 12643274; 12748171; 12748876; 12789531; 12829785; 12832423; 12857602; 12917504; 14557255; 14592826; 14718574; 15041717; 15063602; 15100312; 15166129; 15213442; 15284182; 15297310; 15306846; 15456942; 15489334; 15561970; 15562008; 15579373; 15625895; 15641051; 15816827; 15837717; 15857508; 15895091; 16034137; 16127269; 16270750; 16372246; 16557588; 16710414; 16731080; 16794539; 16817825; 16899024; 16912152; 16973585; 17151125; 17160948; 17310346; 17313958; 17346257; 17357077; 17519976; 17570254; 17619842; 17652155; 17671508; 17703412; 17898129; 17903307; 17908769; 17984249; 18065760; 18276608; 18320358; 18439548; 18464913; 18490707; 18508242; 18538149; 18543249; 18676680; 18719127; 18781131; 18784373; 18818748; 18852330; 18853133; 18971377; 18980999; 19019335; 19026125; 19088723; 19124510; 19170196; 19258923; 19277666; 19280716; 19336475; 19396608; 19406470; 19420002; 19422646; 19453261; 19495883; 19503017; 19505916; 19527514; 19567438; 19573080; 19625176; 19633828; 19665805; 19671870; 19692168; 19713205; 19733878; 19773279; 19773451; 19790045; 19877065; 19913121; 19914334; 19926672; 19966016; 20017315; 20026129; 20031577; 20083667; 20140262; 20145925; 20157327; 20159251; 20186139; 20197062; 20237496; 20379614; 20438838; 20452482; 20453000; 20463041; 20484876; 20503287; 20551110; 20568250; 20599261; 20600579; 20628086; 20661738; 20673868; 20698883; 20727736; 20800603; 20811626; 20823887; 20839491; 20856253; 20951753; 20974296; 21159831; 21173340; 21196890; 21220034; 21229891; 21255427; 21282511; 21295508; 21300955; 21401300; 21490132; 21496483; 21515913; 21700295; 21748280; 21813064; 21835044; 21846873; 21851175; 21879314; 21907864; 21968316; 21981268; 21989726; 22072558; 22079540; 22128229; 22133618; 22209080; 22295972; 22319020; 22421339; 22449275; 22552503; 22554704; 22642608; 22742541; 22761857; 22911828; 22984080; 23073775; 23078005; 23094986; 23242610; 23375120; 23428306; 23564454; 23582566; 23582716; 23593036; 23648090; 23658720; 23677452; 23902164; 23935104; 23969696; 24032723; 24152848 interleukin 6 receptor Ensembl:ENSG00000160712 HGNC:6019 HPRD:01000 MIM:147880 Vega:OTTHUMG00000036073 Other designations: CD126 antigen|IL-6 receptor subunit alpha|IL-6R 1|interleukin-6 receptor subunit alpha|membrane glycoprotein 80 IL6R OGG:3000003574 Bin Zhao, Yue Liu, Oliver He IL-7 WEB: http://www.ncbi.nlm.nih.gov/gene IL7 interleukin 7 3574 8q12-q13 20140408 9606 8 protein-coding Official from a nomenclature committee GO_0002360 (EC: IEA); GO_0005125 (EC: IEA); GO_0005139 (EC: IEA); GO_0005515 (EC: IPI, PMID: 8266077); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0006959 (EC: TAS, PMID: 2643102); GO_0007267 (EC: TAS, PMID: 2643102); GO_0008083 (EC: ISS); GO_0008284 (EC: TAS, PMID: 2643102); GO_0009887 (EC: TAS, PMID: 2643102); GO_0010468 (EC: IEA); GO_0030890 (EC: ISS); GO_0043066 (EC: ISS); GO_0043086 (EC: IEA); GO_0045453 (EC: ISS); GO_0045582 (EC: ISS); GO_0046622 (EC: IEA); GO_0048873 (EC: IEA); GO_2001240 (EC: IEA) PMID: 2320434; 2329282; 2643102; 2786840; 7686307; 7769137; 8125298; 8266077; 8473051; 8840152; 8862549; 9010926; 9158092; 9200446; 9215626; 9407080; 9475337; 9493287; 9561370; 10390077; 10850801; 11447288; 11564764; 11672535; 11858939; 11927620; 11929775; 12010786; 12027403; 12072494; 12149213; 12427286; 12433286; 12441142; 12477932; 12742982; 12792903; 12816983; 12847229; 12882655; 14530372; 14601648; 14607751; 14978141; 15028279; 15048088; 15133032; 15226432; 15247003; 15353558; 15489334; 15598813; 15630452; 15911446; 15964403; 15993713; 16162475; 16284535; 16322477; 16344560; 16626395; 16709829; 16923550; 16967044; 17053062; 17110377; 17205128; 17284597; 17296584; 17328044; 17373935; 17438097; 17524612; 17584976; 17635814; 17656007; 17665400; 17703412; 17894415; 17909291; 17913246; 17956896; 18158957; 18289383; 18322183; 18390701; 18401975; 18431516; 18441236; 18949045; 18976766; 19001329; 19002156; 19008454; 19092841; 19141282; 19147839; 19155487; 19230961; 19240061; 19248116; 19258923; 19279003; 19299724; 19366834; 19432535; 19675167; 19714586; 19770269; 19796902; 19847194; 19864382; 19889552; 19904747; 19913121; 19923894; 20035760; 20067635; 20089933; 20131250; 20167604; 20190192; 20190194; 20200205; 20226540; 20237496; 20382196; 20386468; 20465565; 20503287; 20505146; 20546594; 20628086; 20660706; 20673240; 20815339; 21048031; 21159243; 21209878; 21239710; 21257970; 21418620; 21455214; 21647866; 21680796; 21711552; 21753149; 21795588; 21832049; 21833088; 21876448; 21912394; 21920046; 21988832; 22027639; 22113713; 22194871; 22247488; 22312161; 22314878; 22384197; 22398700; 22506826; 22618230; 22795293; 22859301; 22897934; 22911005; 22921903; 22949940; 22955921; 23018454; 23053510; 23129754; 23157741; 23160470; 23188693; 23244154; 23325887; 23437070; 23454692; 23454917; 23554911; 23628622; 23963040; 23966629 interleukin 7 Ensembl:ENSG00000104432 HGNC:6023 HPRD:00892 MIM:146660 Vega:OTTHUMG00000164620 Other designations: interleukin-7 IL7 OGG:3000003576 Bin Zhao, Yue Liu, Oliver He CXCL8 GCP-1 GCP1 LECT LUCT LYNAP MDNCF MONAP NAF NAP-1 NAP1 WEB: http://www.ncbi.nlm.nih.gov/gene IL8 interleukin 8 3576 4q13-q21 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0001525 (EC: TAS, PMID: 11483765); GO_0002237 (EC: IDA, PMID: 19912257); GO_0005153 (EC: IPI, PMID: 1840701); GO_0005515 (EC: IPI, PMID: 10880251); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0006928 (EC: TAS, PMID: 10820279); GO_0006935 (EC: TAS, PMID: 12782716); GO_0006954 (EC: TAS, PMID: 11483765); GO_0006955 (EC: IEA); GO_0006987 (EC: TAS); GO_0007050 (EC: IDA, PMID: 11564821); GO_0007165 (EC: TAS, PMID: 10820279); GO_0007186 (EC: TAS, PMID: 8381837); GO_0008009 (EC: TAS, PMID: 12782716); GO_0008285 (EC: TAS, PMID: 9551928); GO_0019722 (EC: TAS, PMID: 11877327); GO_0030155 (EC: IDA, PMID: 2007144); GO_0030593 (EC: IGI, PMID: 11564821); GO_0030968 (EC: TAS); GO_0031623 (EC: IDA, PMID: 10734056); GO_0034976 (EC: IDA); GO_0035556 (EC: IDA, PMID: 10734056); GO_0042119 (EC: TAS, PMID: 11483765); GO_0044267 (EC: TAS); GO_0044344 (EC: IEP, PMID: 9407497); GO_0045091 (EC: IDA, PMID: 11483765); GO_0045744 (EC: IDA, PMID: 10734056); GO_0048566 (EC: IEP); GO_0050930 (EC: IGI, PMID: 11564821); GO_0071222 (EC: IDA, PMID: 19912257); GO_0071347 (EC: IEP, PMID: 9407497); GO_0071356 (EC: IEP, PMID: 9407497); GO_0090023 (EC: TAS, PMID: 1699135) PMID: 1281554; 1391327; 1639201; 1673289; 1699135; 1840701; 1895676; 1988949; 2005614; 2007144; 2145175; 2170450; 2182630; 2184886; 2200751; 2212672; 2456256; 2523801; 2555418; 2648135; 2648569; 2655583; 2659722; 2663993; 2664463; 2681204; 2834384; 2953813; 3057503; 3223947; 3260265; 3279957; 3322281; 3480540; 7673721; 7695626; 8077676; 8081002; 8381837; 8626516; 8631339; 8662698; 8663179; 8702798; 8995686; 9141135; 9323208; 9363947; 9378998; 9407497; 9464567; 9510190; 9551928; 9659156; 9828130; 9921412; 10343098; 10361232; 10368283; 10376933; 10491366; 10620615; 10707023; 10734056; 10764593; 10775602; 10820279; 10823949; 10880251; 10881932; 10929056; 10982368; 10985244; 10985253; 11023497; 11069235; 11083887; 11160671; 11226151; 11328384; 11483765; 11509627; 11564821; 11756416; 11784713; 11814358; 11854210; 11855786; 11868823; 11876744; 11877327; 11884401; 11884459; 11888846; 11896938; 11910304; 11911801; 11940655; 11950481; 11956621; 11960393; 11964077; 11966578; 11973337; 11978786; 11989790; 11999552; 12021366; 12027404; 12033786; 12034575; 12039947; 12055238; 12055326; 12056817; 12060853; 12067976; 12081586; 12089333; 12090473; 12091490; 12093676; 12096924; 12096927; 12100025; 12101072; 12115500; 12117737; 12117926; 12117969; 12117995; 12123753; 12126643; 12133438; 12139952; 12149127; 12150710; 12151316; 12151344; 12163591; 12164325; 12165085; 12169092; 12169272; 12186702; 12186913; 12187073; 12195386; 12223528; 12225945; 12239630; 12359770; 12364441; 12366401; 12370346; 12382118; 12384994; 12388718; 12388959; 12391099; 12393171; 12410798; 12415593; 12453441; 12477932; 12480084; 12485855; 12496258; 12502445; 12513912; 12520365; 12524080; 12529421; 12530093; 12533683; 12543081; 12547728; 12548717; 12565901; 12573991; 12576442; 12584113; 12586630; 12594001; 12594058; 12615831; 12626597; 12628493; 12632066; 12633940; 12634636; 12637525; 12646250; 12653788; 12654635; 12654834; 12660426; 12662377; 12702497; 12707271; 12720537; 12727029; 12729795; 12738388; 12744776; 12748056; 12748173; 12777373; 12782302; 12782716; 12792476; 12797546; 12802400; 12818188; 12820969; 12839933; 12839942; 12849706; 12850808; 12855659; 12857601; 12870115; 12871882; 12876073; 12898436; 12898448; 12901801; 12902511; 12909591; 12919697; 12933891; 12952969; 12960242; 13129857; 14500465; 14500470; 14500479; 14530367; 14550286; 14578856; 14604894; 14623984; 14625302; 14630611; 14634582; 14634584; 14641180; 14645117; 14657869; 14669337; 14672330; 14675394; 14676125; 14688120; 14711052; 14714557; 14718619; 14725568; 14729508; 14730209; 14756945; 14767470; 14977935; 15001458; 15021975; 15022458; 15039334; 15047831; 15057743; 15063730; 15069060; 15072962; 15077296; 15079071; 15085176; 15096327; 15102084; 15120188; 15133028; 15143062; 15146413; 15152368; 15158775; 15169673; 15178568; 15178703; 15181190; 15194816; 15196572; 15203561; 15203565; 15208657; 15208668; 15209388; 15214047; 15218164; 15220553; 15222686; 15265021; 15271933; 15273081; 15280021; 15280372; 15292066; 15297389; 15300588; 15302608; 15321994; 15321998; 15331599; 15337758; 15342208; 15356171; 15356575; 15358661; 15364108; 15379213; 15385484; 15453805; 15454487; 15469436; 15481145; 15489227; 15489334; 15494311; 15496610; 15498828; 15514971; 15521010; 15528384; 15529362; 15531763; 15534087; 15541716; 15542429; 15556942; 15564333; 15569594; 15579374; 15579377; 15579481; 15583145; 15585560; 15585673; 15591054; 15598788; 15607204; 15607368; 15609321; 15613411; 15615716; 15627645; 15630185; 15630732; 15641067; 15650393; 15650394; 15652404; 15652492; 15659384; 15661856; 15664665; 15667946; 15679580; 15701651; 15708897; 15710978; 15731050; 15746434; 15760459; 15760676; 15784717; 15803062; 15805227; 15828019; 15831558; 15845475; 15845476; 15845864; 15854776; 15862344; 15866212; 15894298; 15897801; 15902922; 15914533; 15917409; 15945132; 15962221; 15972644; 15976103; 15976326; 15979992; 15987860; 15989802; 16004996; 16007706; 16029496; 16038881; 16038986; 16039610; 16052590; 16085794; 16088182; 16096323; 16098041; 16098254; 16101867; 16107255; 16107886; 16110031; 16125276; 16134994; 16164755; 16166417; 16168518; 16185356; 16195477; 16195815; 16197369; 16202743; 16204411; 16207434; 16220540; 16240219; 16251188; 16251427; 16270354; 16273337; 16280123; 16284368; 16289597; 16293628; 16293707; 16299055; 16313297; 16317381; 16322472; 16365152; 16373669; 16375755; 16387844; 16394009; 16403098; 16406804; 16411061; 16429233; 16487026; 16491014; 16498082; 16499908; 16503988; 16525644; 16541418; 16545602; 16547413; 16547804; 16552338; 16552751; 16554734; 16573784; 16581825; 16618781; 16620395; 16632517; 16635219; 16679868; 16679918; 16687414; 16697675; 16698420; 16702372; 16719905; 16720107; 16757060; 16769764; 16775170; 16777061; 16788380; 16793206; 16794530; 16795034; 16797773; 16806015; 16820307; 16824064; 16825597; 16846747; 16862120; 16864907; 16864908; 16873245; 16890267; 16897191; 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19436689; 19446037; 19448676; 19454705; 19460731; 19460789; 19467703; 19470239; 19474090; 19484147; 19494510; 19496969; 19505916; 19506726; 19506876; 19514335; 19526283; 19527294; 19527514; 19535567; 19556613; 19561378; 19567187; 19570208; 19570915; 19573080; 19578117; 19588509; 19591568; 19596978; 19597126; 19597830; 19608678; 19608729; 19617600; 19622587; 19625176; 19646263; 19661010; 19661014; 19667085; 19668110; 19668231; 19674346; 19681642; 19688109; 19692168; 19692203; 19694638; 19699525; 19714766; 19719901; 19720161; 19726162; 19726280; 19732956; 19733855; 19734226; 19734969; 19747898; 19751561; 19755917; 19760027; 19773182; 19773279; 19773451; 19777350; 19786303; 19787256; 19789190; 19794965; 19799797; 19801670; 19805069; 19816813; 19819266; 19819989; 19834107; 19835476; 19837667; 19838218; 19840968; 19842025; 19852851; 19855073; 19858310; 19874800; 19887538; 19890050; 19898747; 19904283; 19906815; 19912257; 19913121; 19914270; 19929572; 19932683; 19948975; 19950606; 19956874; 19994728; 19995941; 19996617; 19996656; 20004360; 20005738; 20008399; 20012528; 20015396; 20026745; 20037740; 20038977; 20039880; 20044268; 20047188; 20056178; 20061995; 20084405; 20102417; 20103651; 20106902; 20107186; 20118277; 20127012; 20148189; 20150959; 20162422; 20166885; 20172018; 20174873; 20181930; 20185670; 20187772; 20190550; 20194723; 20194818; 20198307; 20206550; 20207250; 20217044; 20218918; 20220108; 20222161; 20227257; 20237496; 20298300; 20300863; 20306660; 20363151; 20363644; 20369436; 20378727; 20379392; 20380014; 20384861; 20384872; 20398511; 20399512; 20400187; 20400292; 20405297; 20406964; 20410302; 20418110; 20431935; 20437058; 20438785; 20441409; 20444155; 20448351; 20452482; 20453000; 20454998; 20463618; 20465445; 20470938; 20473875; 20483454; 20483667; 20485444; 20486195; 20487506; 20488171; 20501448; 20503287; 20506652; 20510674; 20512787; 20518825; 20523065; 20540789; 20540853; 20540976; 20546607; 20556966; 20562101; 20564140; 20568250; 20571236; 20574123; 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22935637; 22939387; 22964303; 22983351; 23000201; 23002445; 23007230; 23029099; 23029125; 23042271; 23043537; 23058014; 23070988; 23072563; 23091318; 23092711; 23110185; 23118425; 23124693; 23125416; 23128233; 23145117; 23149083; 23160385; 23160800; 23165450; 23168996; 23197259; 23198942; 23204162; 23207068; 23221335; 23225384; 23242124; 23244113; 23247723; 23251686; 23259986; 23268406; 23269580; 23269842; 23276701; 23297014; 23321310; 23325853; 23325889; 23327592; 23334651; 23342280; 23347173; 23389820; 23392805; 23403077; 23405070; 23409168; 23418512; 23418647; 23425997; 23434371; 23441821; 23444260; 23456515; 23463699; 23478175; 23490412; 23498057; 23519334; 23526216; 23545310; 23546865; 23546898; 23576566; 23577098; 23584701; 23597430; 23603048; 23610962; 23615914; 23624000; 23632023; 23633491; 23680697; 23688054; 23704827; 23712703; 23714383; 23762476; 23770363; 23773024; 23779254; 23782136; 23785756; 23821953; 23831257; 23831464; 23867456; 23870461; 23887394; 23888551; 23890815; 23894194; 23912333; 23924923; 23972657; 23992011; 24032673; 24076166; 24080022; 24099766; 24121485; 24161763; 24186266; 24260304; 24273918; 24284797; 24313836; 24344010 interleukin 8 Ensembl:ENSG00000169429 HGNC:6025 HPRD:00909 MIM:146930 Vega:OTTHUMG00000151316 Other designations: T-cell chemotactic factor|alveolar macrophage chemotactic factor I|beta endothelial cell-derived neutrophil activating peptide|beta-thromboglobulin-like protein|chemokine (C-X-C motif) ligand 8|emoctakin|granulocyte chemotactic protein 1|interleukin-8|lung giant cell carcinoma-derived chemotactic protein|lymphocyte derived neutrophil activating peptide|monocyte-derived neutrophil chemotactic factor|monocyte-derived neutrophil-activating peptide|neutrophil-activating peptide 1|small inducible cytokine subfamily B, member 8|tumor necrosis factor-induced gene 1 IL8 OGG:3000003586 Bin Zhao, Yue Liu, Oliver He CSIF GVHDS IL-10 IL10A TGIF WEB: http://www.ncbi.nlm.nih.gov/gene IL10 interleukin 10 3586 RP11-262N9.1 1q31-q32 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0002237 (EC: IDA, PMID: 17449476); GO_0002740 (EC: IDA, PMID: 10443688); GO_0002875 (EC: IEA); GO_0002904 (EC: IDA, PMID: 9184696); GO_0005125 (EC: NAS, PMID: 10443688); GO_0005141 (EC: NAS, PMID: 1847510); GO_0005615 (EC: IDA, PMID: 10443688); GO_0006954 (EC: IDA, PMID: 10443688); GO_0007253 (EC: NAS, PMID: 10975994); GO_0007267 (EC: IC, PMID: 1847510); GO_0008083 (EC: NAS, PMID: 1371884); GO_0010468 (EC: IDA, PMID: 9184696); GO_0014823 (EC: IEA); GO_0014854 (EC: IEA); GO_0030097 (EC: TAS, PMID: 11244051); GO_0030183 (EC: NAS, PMID: 8228801); GO_0030595 (EC: TAS, PMID: 9405662); GO_0030886 (EC: IEA); GO_0030889 (EC: IDA, PMID: 9184696); GO_0032689 (EC: IEA); GO_0032695 (EC: IEA); GO_0032715 (EC: IDA, PMID: 10443688); GO_0032720 (EC: IEA); GO_0032800 (EC: IDA, PMID: 10443688); GO_0032868 (EC: IEA); GO_0034465 (EC: IEA); GO_0042092 (EC: TAS, PMID: 11244051); GO_0042100 (EC: NAS, PMID: 8228801); GO_0042130 (EC: NAS, PMID: 14971032); GO_0042493 (EC: IEA); GO_0042536 (EC: IEA); GO_0042742 (EC: IEA); GO_0043066 (EC: NAS, PMID: 8312229); GO_0044130 (EC: IEA); GO_0045019 (EC: IEA); GO_0045191 (EC: NAS, PMID: 8228801); GO_0045347 (EC: TAS, PMID: 11244051); GO_0045348 (EC: IEA); GO_0045355 (EC: NAS, PMID: 9637497); GO_0045893 (EC: IDA, PMID: 7749983); GO_0045944 (EC: IEA); GO_0050715 (EC: IDA, PMID: 10443688); GO_0051045 (EC: IDA, PMID: 18383040); GO_0051091 (EC: IDA, PMID: 7749983); GO_0051384 (EC: IDA, PMID: 10443688); GO_0051930 (EC: IEA); GO_0060670 (EC: IEA); GO_0071222 (EC: NAS, PMID: 14971032); GO_0071392 (EC: IEA) PMID: 1121048; 1350294; 1371884; 1847510; 2173142; 7511078; 7527834; 7547951; 7553888; 7590988; 7591871; 7695626; 7749063; 7749983; 7759550; 7815507; 8037735; 8228801; 8248239; 8312229; 8364028; 8402911; 8499633; 8590020; 8764000; 8881045; 8897595; 8898665; 8910398; 9043871; 9096366; 9108403; 9143942; 9162098; 9184696; 9225992; 9234486; 9312047; 9334723; 9405662; 9463379; 9534962; 9637497; 9658081; 9689103; 9743208; 9788463; 10064624; 10089566; 10231374; 10443688; 10542212; 10714547; 10775602; 10807185; 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19766898; 19771178; 19773279; 19773451; 19778488; 19779724; 19781301; 19782084; 19786281; 19796538; 19798061; 19802007; 19805095; 19811408; 19813110; 19817985; 19819209; 19821803; 19822020; 19823053; 19838195; 19852851; 19856416; 19860911; 19861958; 19882211; 19889024; 19889076; 19889475; 19890236; 19892918; 19895848; 19907653; 19908064; 19908237; 19912737; 19913121; 19915572; 19917162; 19934104; 19936625; 19938203; 19939284; 19948975; 19956635; 19957794; 19958312; 19996617; 19996656; 20001857; 20010527; 20012528; 20014019; 20015215; 20016407; 20016783; 20017308; 20018615; 20030788; 20032313; 20037209; 20042578; 20042580; 20044609; 20047977; 20051670; 20052801; 20059417; 20061995; 20070620; 20070836; 20072143; 20080912; 20082482; 20082647; 20083555; 20087644; 20087693; 20087947; 20089329; 20097948; 20102414; 20107186; 20138641; 20144201; 20145925; 20148913; 20150436; 20150742; 20163933; 20171114; 20176734; 20177758; 20178529; 20181890; 20184663; 20188863; 20189706; 20190550; 20191326; 20191386; 20195402; 20195716; 20196868; 20200511; 20202139; 20204402; 20207250; 20207982; 20213229; 20217044; 20227257; 20227772; 20228669; 20228798; 20228799; 20232770; 20233508; 20236506; 20236616; 20237496; 20299965; 20302034; 20305143; 20306684; 20335604; 20337945; 20339193; 20339966; 20349753; 20356901; 20359252; 20363151; 20367137; 20369436; 20370995; 20371920; 20378550; 20378664; 20381257; 20384861; 20385468; 20388088; 20388104; 20393813; 20395963; 20399512; 20404426; 20410487; 20413987; 20416077; 20418110; 20419805; 20421626; 20424473; 20424554; 20424918; 20430716; 20431935; 20438703; 20445748; 20447254; 20448110; 20452482; 20453000; 20454933; 20457266; 20459687; 20463618; 20470442; 20471133; 20472930; 20473875; 20477882; 20482524; 20484443; 20484876; 20485362; 20485444; 20486195; 20490277; 20490891; 20503287; 20509889; 20518833; 20518842; 20519163; 20523065; 20525402; 20527514; 20529592; 20530519; 20531015; 20536507; 20536548; 20551628; 20553628; 20558465; 20561040; 20564140; 20565774; 20567520; 20568250; 20570082; 20571871; 20576226; 20578820; 20587610; 20588103; 20588308; 20589076; 20591588; 20592893; 20595152; 20602615; 20603037; 20603050; 20617924; 20618176; 20622753; 20622878; 20622879; 20625422; 20628086; 20628373; 20638860; 20640364; 20644561; 20646924; 20650298; 20659236; 20661303; 20661604; 20662694; 20671651; 20673868; 20711808; 20714960; 20716621; 20720222; 20722024; 20723894; 20725607; 20732366; 20735825; 20737205; 20798845; 20804371; 20805562; 20807264; 20809522; 20809684; 20811626; 20825427; 20825636; 20830806; 20835611; 20838432; 20839488; 20860222; 20861424; 20863526; 20879862; 20880001; 20880267; 20880745; 20881642; 20883321; 20884746; 20889146; 20889800; 20922456; 20927126; 20934598; 20934961; 20942272; 20952070; 20953818; 20957732; 20970781; 20976276; 21030268; 21037509; 21040915; 21048327; 21052690; 21054877; 21055074; 21055733; 21057561; 21057730; 21061265; 21067483; 21067752; 21068755; 21076061; 21086908; 21088899; 21090240; 21098222; 21102463; 21107607; 21107665; 21123382; 21131395; 21135123; 21138342; 21160051; 21168854; 21183270; 21191065; 21205466; 21211963; 21215074; 21215285; 21216474; 21223691; 21227406; 21238445; 21239715; 21240493; 21254836; 21255795; 21267581; 21281983; 21297633; 21300911; 21303362; 21309719; 21314735; 21316985; 21317876; 21323660; 21328800; 21332458; 21339768; 21354456; 21357266; 21357402; 21358669; 21359250; 21372199; 21398611; 21398617; 21402594; 21406270; 21413929; 21424183; 21426411; 21439624; 21440743; 21455338; 21463487; 21466366; 21467695; 21468030; 21468579; 21478113; 21481602; 21508509; 21518800; 21519827; 21526166; 21527907; 21532858; 21549291; 21553228; 21558138; 21560494; 21567173; 21595995; 21609779; 21621860; 21624746; 21626471; 21641950; 21642542; 21658228; 21658363; 21669226; 21688665; 21689404; 21699407; 21721376; 21724486; 21725623; 21729106; 21730023; 21744325; 21756510; 21757655; 21764596; 21767236; 21777343; 21779975; 21786452; 21791113; 21792878; 21808111; 21812905; 21816135; 21829393; 21830424; 21839042; 21858117; 21861711; 21862302; 21863566; 21863628; 21869490; 21873118; 21876975; 21878338; 21901441; 21902578; 21909800; 21910858; 21917128; 21918473; 21923667; 21925952; 21926547; 21931651; 21936714; 21940055; 21968303; 21972680; 21986577; 21998459; 22010076; 22019000; 22032897; 22033829; 22038351; 22048455; 22050548; 22057691; 22057973; 22058059; 22070668; 22075762; 22077544; 22079540; 22081333; 22082370; 22092594; 22095765; 22100578; 22105495; 22116520; 22122951; 22123389; 22129927; 22140263; 22140472; 22144535; 22156547; 22157213; 22158873; 22160576; 22168225; 22172723; 22174866; 22176654; 22182686; 22184725; 22187388; 22189417; 22189756; 22205204; 22205395; 22213066; 22219323; 22225835; 22235320; 22239992; 22263663; 22279662; 22287022; 22288916; 22298356; 22307790; 22311038; 22323454; 22325340; 22335769; 22347492; 22350281; 22356904; 22358381; 22366404; 22371646; 22378604; 22387064; 22390924; 22393278; 22410761; 22416256; 22424164; 22425021; 22425265; 22427230; 22436502; 22442690; 22445549; 22466287; 22475179; 22484198; 22484241; 22487811; 22494514; 22503116; 22507621; 22520513; 22529524; 22535664; 22537067; 22537751; 22544931; 22547702; 22547705; 22549091; 22556042; 22565155; 22566507; 22572643; 22575708; 22578382; 22580886; 22582500; 22586040; 22592039; 22592860; 22594912; 22595646; 22628023; 22634719; 22644143; 22653776; 22655468; 22664006; 22673037; 22677268; 22678905; 22681958; 22682876; 22685028; 22687336; 22698805; 22710869; 22711892; 22715992; 22732092; 22740130; 22749664; 22753934; 22753938; 22763734; 22768144; 22784413; 22788775; 22795294; 22796266; 22805022; 22812212; 22812241; 22818022; 22825546; 22835429; 22835835; 22848356; 22850906; 22851691; 22859398; 22859944; 22880107; 22886309; 22897390; 22902304; 22911481; 22924705; 22931953; 22932817; 22940633; 22966128; 22972930; 22981868; 22986179; 22989497; 23013217; 23013641; 23017230; 23020144; 23021880; 23027536; 23028907; 23029361; 23034167; 23046616; 23046617; 23053983; 23062006; 23062580; 23069299; 23071313; 23073467; 23075771; 23079832; 23086275; 23088578; 23094074; 23095823; 23096091; 23118878; 23125413; 23128233; 23143946; 23149083; 23152883; 23159283; 23166328; 23168096; 23185315; 23192326; 23207823; 23209731; 23210681; 23220432; 23225254; 23232337; 23235789; 23237063; 23237776; 23251077; 23265747; 23272193; 23273903; 23273955; 23276701; 23294711; 23299779; 23300021; 23300769; 23325892; 23326478; 23334981; 23335974; 23343479; 23349310; 23355741; 23357299; 23363891; 23376084; 23379624; 23380741; 23415626; 23416458; 23430974; 23432860; 23438682; 23444260; 23449984; 23450495; 23453286; 23460834; 23485354; 23485538; 23485736; 23488731; 23498167; 23525950; 23541976; 23544075; 23556339; 23562725; 23570798; 23574339; 23582441; 23583365; 23591975; 23595519; 23602200; 23602201; 23607333; 23613317; 23623844; 23638863; 23640160; 23640982; 23645090; 23654353; 23663047; 23663500; 23668806; 23679256; 23690289; 23711712; 23712703; 23716201; 23720844; 23723980; 23725154; 23725178; 23733877; 23743567; 23749933; 23752129; 23752604; 23762097; 23768819; 23772925; 23777202; 23797738; 23798430; 23814099; 23818986; 23834952; 23838435; 23846686; 23875023; 23880295; 23880623; 23886125; 23897063; 23898109; 23901045; 23910644; 23936042; 23990628; 24015034; 24042116; 24043893; 24067460; 24077340; 24130510; 24174668; 24216477; 24327156; 24340926; 24379064 interleukin 10 Ensembl:ENSG00000136634 HGNC:5962 HPRD:00495 MIM:124092 Vega:OTTHUMG00000036386 Other designations: T-cell growth inhibitory factor|cytokine synthesis inhibitory factor|interleukin-10 IL10 OGG:3000003592 Bin Zhao, Yue Liu, Oliver He CLMF IL-12A NFSK NKSF1 P35 WEB: http://www.ncbi.nlm.nih.gov/gene IL12A interleukin 12A 3592 3q25.33 9606 3 GO_0001916 (EC: IDA, PMID:1674604); GO_0002860 (EC: IDA, PMID:7903063); GO_0005125 (EC: IDA, Qualifier: contributes_to, PMID:1674604); GO_0005125 (EC: TAS, Qualifier: contributes_to, PMID:1673147); GO_0005143 (EC: NAS, PMID:1674604); GO_0005515 (EC: IPI, PMID:10899108); GO_0005615 (EC: IDA, PMID:16456693); GO_0005737 (EC: IEA); GO_0006955 (EC: TAS, PMID:9789052); GO_0007050 (EC: IDA, PMID:16942485); GO_0008083 (EC: IDA, Qualifier: contributes_to, PMID:1674604); GO_0008083 (EC: NAS, Qualifier: contributes_to, PMID:1673147); GO_0009615 (EC: IEP, PMID:16548883); GO_0010224 (EC: IDA, PMID:8992506); GO_0016477 (EC: IDA, PMID:7903063); GO_0032496 (EC: IDA, PMID:7605994); GO_0032700 (EC: IDA, PMID:16482511); GO_0032729 (EC: IDA, PMID:11114383); GO_0032816 (EC: IDA, PMID:1674604); GO_0034393 (EC: IDA, PMID:16942485); GO_0042102 (EC: IEA); GO_0042163 (EC: IEA); GO_0042520 (EC: IDA, PMID:12372421); GO_0042832 (EC: IEA); GO_0043514 (EC: IDA, PMID:11114383); GO_0043514 (EC: NAS, PMID:14718574); GO_0045513 (EC: IPI, PMID:9342359); GO_0045582 (EC: IEA); GO_0045785 (EC: IDA, PMID:7903063); GO_0045954 (EC: IDA, PMID:2204066); GO_0046982 (EC: IPI, PMID:1674604); GO_0048662 (EC: IDA, PMID:16942485); GO_0050671 (EC: IDA, PMID:1674604); GO_0050830 (EC: IEP, PMID:1357073); GO_0051135 (EC: IDA, PMID:19088061); GO_0097191 (EC: IDA, PMID:16942485) PMID:934235; 1350290; 1357073; 1358798; 1673147; 1674604; 2204066; 7516408; 7527811; 7605994; 7695626; 7867080; 7903063; 8557999; 8648753; 8700208; 8760829; 8992506; 9108403; 9158092; 9225992; 9334723; 9342359; 9516412; 9603732; 9616161; 9671213; 9712080; 9789052; 10089131; 10320373; 10352291; 10899108; 11087201; 11114383; 11751963; 11940489; 12117904; 12213961; 12242445; 12270766; 12358856; 12370346; 12372421; 12444143; 12472178; 12477932; 12542496; 12558814; 12576336; 12633940; 12672403; 12719551; 12911539; 12944981; 14566095; 14597672; 14629328; 14660053; 14675394; 14718574; 14764743; 14962816; 15051764; 15087447; 15142381; 15170937; 15331709; 15356557; 15361128; 15448160; 15489234; 15643599; 15741223; 15780175; 15810889; 15817944; 15863393; 15937086; 15956545; 15963597; 16230423; 16456693; 16482511; 16544245; 16548883; 16573560; 16702372; 16754651; 16803996; 16862120; 16885196; 16938461; 16942485; 16961803; 17002904; 17007011; 17062130; 17077296; 17152005; 17225924; 17236132; 17257312; 17304101; 17361014; 17431094; 17444864; 17461482; 17509455; 17553352; 17564777; 17586317; 17627763; 17640324; 17653830; 17671745; 17703412; 17846855; 17881511; 17922692; 17947455; 18050195; 18092318; 18159163; 18190588; 18260379; 18300344; 18311140; 18385764; 18413324; 18417583; 18419254; 18554158; 18566447; 18588867; 18606709; 18628242; 18632425; 18633131; 18671862; 18672993; 18676680; 18717726; 18773331; 18805825; 18972297; 18976327; 19012493; 19013323; 19031096; 19073967; 19074885; 19088061; 19117745; 19118071; 19126646; 19144161; 19148899; 19170196; 19200845; 19230467; 19234184; 19253530; 19258923; 19275586; 19297619; 19299334; 19332120; 19339796; 19376105; 19408823; 19454678; 19458352; 19470040; 19505916; 19508433; 19516896; 19525953; 19543959; 19566870; 19573080; 19594368; 19625176; 19646340; 19692168; 19693089; 19710469; 19773279; 19789190; 19797506; 19798410; 19879194; 19885559; 19913121; 19950173; 19956842; 20012528; 20027291; 20054003; 20060272; 20061784; 20082482; 20190752; 20213229; 20231901; 20237496; 20331378; 20350312; 20372811; 20418110; 20446002; 20452482; 20453000; 20485444; 20503287; 20521253; 20544370; 20551083; 20555355; 20568250; 20581146; 20603050; 20628086; 20634089; 20639880; 20647273; 20673868; 20714168; 20716621; 20818961; 20881642; 20960273; 21044109; 21086908; 21145044; 21177981; 21285006; 21387004; 21397857; 21399635; 21402701; 21513752; 21518507; 21518761; 21606320; 21689404; 21833088; 21878338; 22005588; 22011063; 22038227; 22040814; 22133036; 22438968; 22581790; 22614250; 22655069; 22656398; 22691562; 22734699; 22819329; 22940148; 23053983; 23065210; 23154182; 23285065; 23291587; 23297419; 23377640; 23388728; 23619469; 23657466; 23717436; 23734222; 23752604; 23755218; 24273881 interleukin 12A Ensembl:ENSG00000168811 HGNC:5969 HPRD:01193 MIM:161560 Vega:OTTHUMG00000158942 Other designations: CLMF p35|IL-12, subunit p35|IL35 subunit|NF cell stimulatory factor chain 1|NK cell stimulatory factor chain 1|cytotoxic lymphocyte maturation factor 1, p35|cytotoxic lymphocyte maturation factor 35 kDa subunit|interleukin 12, p35|interleukin 12A (natural killer cell stimulatory factor 1, cytotoxic lymphocyte maturation factor 1, p35)|interleukin-12 alpha chain|interleukin-12 subunit alpha IL12A OGG:3000003593 Bin Zhao, Yue Liu, Oliver He CLMF CLMF2 IL-12B NKSF NKSF2 WEB: http://www.ncbi.nlm.nih.gov/gene IL12B interleukin 12B 3593 5q31.1-q33.1 20140409 9606 5 protein-coding Official from a nomenclature committee GO_0001916 (EC: ISS); GO_0002230 (EC: IDA, PMID: 12421946); GO_0002230 (EC: ISS); GO_0002323 (EC: IEA); GO_0002827 (EC: IDA, PMID: 15114670); GO_0002827 (EC: ISS); GO_0002860 (EC: IDA, PMID: 7903063); GO_0002862 (EC: IEA); GO_0004896 (EC: IEA); GO_0005125 (EC: IDA, Qualifier: contributes_to, PMID: 1674604); GO_0005143 (EC: TAS, PMID: 1674604); GO_0005143 (EC: TAS, Qualifier: contributes_to, PMID: 9603733); GO_0005515 (EC: IPI, PMID: 10899108); GO_0005615 (EC: TAS, PMID: 1673147); GO_0005737 (EC: IEA); GO_0007050 (EC: IDA, PMID: 16942485); GO_0008083 (EC: IDA, Qualifier: contributes_to, PMID: 1674604); GO_0010224 (EC: IDA, PMID: 8992506); GO_0010535 (EC: IDA, PMID: 12023369); GO_0016020 (EC: IEA); GO_0016477 (EC: IDA, PMID: 7903063); GO_0019233 (EC: IEA); GO_0019953 (EC: TAS, PMID: 16772281); GO_0030101 (EC: IDA, PMID: 1673147); GO_0032693 (EC: IMP, PMID: 16751425); GO_0032700 (EC: IDA, PMID: 16482511); GO_0032725 (EC: IDA); GO_0032729 (EC: IDA, PMID: 11114383); GO_0032733 (EC: IDA, PMID: 15265908); GO_0032733 (EC: TAS, PMID: 18675459); GO_0032735 (EC: IDA); GO_0032740 (EC: IDA, PMID: 16482511); GO_0032760 (EC: IMP, PMID: 16751425); GO_0032816 (EC: IC); GO_0032816 (EC: IDA, PMID: 1674604); GO_0032819 (EC: IDA, PMID: 19088061); GO_0034105 (EC: IC, PMID: 16482511); GO_0034393 (EC: IDA, PMID: 16942485); GO_0042035 (EC: TAS, PMID: 1673147); GO_0042088 (EC: TAS, PMID: 1673147); GO_0042093 (EC: IDA, PMID: 1673147); GO_0042095 (EC: TAS, PMID: 1673147); GO_0042102 (EC: IDA, PMID: 12023369); GO_0042104 (EC: IDA, PMID: 11114383); GO_0042164 (EC: IEA); GO_0042346 (EC: TAS); GO_0042510 (EC: IDA, PMID: 12023369); GO_0042517 (EC: IDA, PMID: 12023369); GO_0042520 (EC: IDA, PMID: 11114383); GO_0042523 (EC: IDA, PMID: 12023369); GO_0042802 (EC: IPI, PMID: 7527811); GO_0042803 (EC: IEA); GO_0042832 (EC: IEA); GO_0043382 (EC: ISS); GO_0043514 (EC: IDA, PMID: 11114383); GO_0044130 (EC: IEA); GO_0045078 (EC: TAS, PMID: 1673147); GO_0045519 (EC: IDA, Qualifier: contributes_to, PMID: 11114383); GO_0045672 (EC: IDA, PMID: 17888176); GO_0045785 (EC: IDA, PMID: 7903063); GO_0046982 (EC: IPI, PMID: 1674604); GO_0048662 (EC: IDA, PMID: 16942485); GO_0050671 (EC: IDA, PMID: 1674604); GO_0050729 (EC: IC, PMID: 16482511); GO_0050829 (EC: IDA, PMID: 15114670); GO_0051135 (EC: IC); GO_0051135 (EC: IDA, PMID: 19088061); GO_0051142 (EC: IDA, PMID: 19088061); GO_0051607 (EC: IEA); GO_0070743 (EC: IDA, PMID: 11114383); GO_0071222 (EC: IEA); GO_0071346 (EC: IEA); GO_2000318 (EC: ISS); GO_2000330 (EC: ISS) PMID: 1358798; 1673147; 1674604; 2070420; 2204066; 7527439; 7527811; 7565674; 7695626; 7698768; 7836910; 7843232; 7867080; 7903063; 8551218; 8648753; 8760829; 8799158; 8992506; 9108403; 9158092; 9225992; 9516412; 9603732; 9603733; 9671213; 9700192; 9712080; 9789052; 9854038; 10207176; 10320373; 10352291; 10419056; 10890924; 10899108; 11087201; 11110796; 11114383; 11196715; 11197695; 11751963; 11753820; 11813133; 11820460; 11940489; 11972887; 11978670; 12023369; 12065887; 12086971; 12100467; 12117904; 12117918; 12202149; 12207325; 12241719; 12270766; 12297341; 12370346; 12413772; 12421946; 12424624; 12424627; 12472178; 12477932; 12542496; 12672403; 12719551; 12857749; 12876411; 12914676; 14551880; 14597672; 14675396; 14679201; 14746806; 14764743; 14962816; 14976188; 15004750; 15007350; 15057902; 15102082; 15114670; 15265908; 15285014; 15295696; 15322986; 15331709; 15356557; 15448160; 15464247; 15482860; 15483662; 15489334; 15523691; 15603869; 15620465; 15644581; 15837792; 15858599; 15869883; 15871664; 15937086; 15941730; 15988104; 15993716; 16005098; 16039994; 16100774; 16210052; 16216674; 16482511; 16514412; 16574246; 16600026; 16637265; 16681592; 16712658; 16750991; 16751425; 16772281; 16789008; 16942485; 16948912; 16966828; 17077296; 17148969; 17152005; 17172248; 17207965; 17236132; 17327408; 17388919; 17392024; 17403771; 17431094; 17445208; 17477815; 17504509; 17509455; 17513774; 17554261; 17564777; 17567674; 17579859; 17587057; 17644387; 17653830; 17703412; 17846855; 17881511; 17888176; 17889143; 17901940; 17932439; 17945537; 17993580; 17994425; 18034172; 18048021; 18075513; 18082575; 18086266; 18092318; 18163209; 18190588; 18192685; 18219280; 18240960; 18300039; 18319400; 18341612; 18367309; 18369459; 18383521; 18389618; 18413324; 18422730; 18438406; 18449199; 18485489; 18497679; 18512797; 18522869; 18557702; 18563338; 18587394; 18588591; 18606709; 18619507; 18628242; 18631256; 18632587; 18633131; 18675459; 18676680; 18680750; 18703108; 18717726; 18800148; 18821674; 18827961; 18834321; 19012493; 19013323; 19035472; 19088061; 19118071; 19134014; 19169254; 19169255; 19170196; 19174780; 19185507; 19210338; 19234184; 19247692; 19249008; 19258635; 19258923; 19262574; 19264456; 19274925; 19279357; 19328947; 19342681; 19419334; 19422935; 19435421; 19487916; 19495883; 19505916; 19516896; 19525409; 19554267; 19573080; 19625176; 19646340; 19683555; 19692168; 19705136; 19733878; 19760754; 19773279; 19773451; 19782084; 19819209; 19832040; 19838195; 19860911; 19861958; 19913121; 19956104; 20003322; 20012528; 20014019; 20016509; 20027321; 20054003; 20060272; 20061784; 20105444; 20145925; 20217072; 20236616; 20237496; 20331378; 20349123; 20350312; 20371868; 20372811; 20387064; 20395963; 20399512; 20416077; 20452482; 20453000; 20483637; 20485444; 20503287; 20521253; 20525402; 20530519; 20544370; 20551083; 20568250; 20570966; 20621951; 20628086; 20653817; 20653995; 20658240; 20673868; 20705102; 20711808; 20714168; 20716621; 20802378; 20811626; 20875078; 20875477; 20953186; 20953188; 20953190; 21055733; 21072187; 21102463; 21145044; 21196650; 21198744; 21208785; 21278068; 21297633; 21310195; 21321105; 21339808; 21351215; 21397857; 21443923; 21470215; 21513752; 21567173; 21623733; 21637332; 21641076; 21689404; 21733366; 21743469; 21747388; 21753150; 21796650; 21819616; 21833088; 21878338; 21972680; 22005588; 22011063; 22045842; 22070668; 22144535; 22190364; 22194214; 22296201; 22327783; 22383962; 22384203; 22479607; 22503230; 22581790; 22614250; 22621617; 22655069; 22656398; 22702905; 22739501; 22740240; 22819329; 22863216; 22897389; 22930279; 22940148; 23006423; 23028907; 23053983; 23065198; 23065210; 23071313; 23093722; 23099807; 23103228; 23128233; 23137633; 23154183; 23240095; 23285955; 23297015; 23297419; 23376980; 23403235; 23429356; 23441821; 23527200; 23575353; 23578145; 23600862; 23621408; 23665963; 23679818; 23717436; 23734222; 23755218; 23817431; 23830516; 23901045; 23955419; 23991654; 24127073 interleukin 12B Ensembl:ENSG00000113302 HGNC:5970 HPRD:01194 MIM:161561 Vega:OTTHUMG00000130307 Other designations: CLMF p40|IL-12 subunit p40|IL12, subunit p40|NK cell stimulatory factor chain 2|cytotoxic lymphocyte maturation factor 40 kDa subunit|interleukin 12, p40|interleukin 12B (natural killer cell stimulatory factor 2, cytotoxic lymphocyte maturation factor 2, p40)|interleukin-12 beta chain|interleukin-12 subunit beta|natural killer cell stimulatory factor, 40 kD subunit IL12B OGG:3000003596 Bin Zhao, Yue Liu, Oliver He IL-13 P600 WEB: http://www.ncbi.nlm.nih.gov/gene IL13 interleukin 13 3596 5q31 20140408 9606 5 protein-coding Official from a nomenclature committee GO_0002639 (EC: IEA); GO_0005125 (EC: IEA); GO_0005144 (EC: IEA); GO_0005515 (EC: IPI, PMID: 18243101); GO_0005576 (EC: IDA); GO_0005615 (EC: ISS, PMID: 16275384); GO_0005737 (EC: IEA); GO_0006928 (EC: TAS, PMID: 10725748); GO_0006954 (EC: TAS, PMID: 8096327); GO_0006955 (EC: IEA); GO_0007165 (EC: NAS, PMID: 10725748); GO_0007267 (EC: IC, PMID: 10725748); GO_0009897 (EC: IEA); GO_0010155 (EC: IEA); GO_0030890 (EC: IEA); GO_0032496 (EC: IEA); GO_0032723 (EC: IEA); GO_0035094 (EC: IEA); GO_0042526 (EC: IEA); GO_0043032 (EC: IEA); GO_0045471 (EC: IEA); GO_0048661 (EC: IEA); GO_0050714 (EC: IEA); GO_0051281 (EC: IEA); GO_0071260 (EC: IEA); GO_0071345 (EC: IEA); GO_0071635 (EC: IEA); GO_1901247 (EC: NAS); GO_1901251 (EC: NAS); GO_2000231 (EC: IEA) PMID: 1408833; 7521694; 7530359; 7721105; 8096327; 8097324; 8099936; 8605348; 8609418; 9139718; 9177784; 9226003; 9856949; 9856950; 10227975; 10623799; 10651852; 10699178; 10725748; 10753117; 11003391; 11149986; 11197307; 11278629; 11396683; 11588017; 11678850; 11709756; 11786536; 11825773; 11830476; 11940068; 11980568; 12063528; 12067309; 12089333; 12089714; 12097410; 12145428; 12152987; 12163193; 12165514; 12189139; 12207328; 12223527; 12370393; 12370400; 12377947; 12396617; 12413765; 12424628; 12441140; 12477932; 12525574; 12548511; 12594065; 12654630; 12682264; 12704784; 12748293; 12748907; 12794003; 12884288; 12897746; 12920029; 12928861; 12935900; 12944981; 14510917; 14512310; 14551608; 14561191; 14564352; 14634100; 14669230; 14734771; 14756548; 14764428; 14983029; 14984938; 15004182; 15005726; 15007352; 15007355; 15014952; 15146247; 15155567; 15155645; 15163701; 15163899; 15187156; 15191916; 15229217; 15308043; 15315330; 15356556; 15356573; 15361241; 15388001; 15474066; 15483090; 15488706; 15528258; 15596681; 15634905; 15642470; 15660293; 15661077; 15687724; 15699166; 15711639; 15713213; 15728267; 15731584; 15820084; 15845862; 15869882; 15870068; 15879126; 15904474; 15919378; 15951665; 15969687; 16001979; 16024651; 16024972; 16034134; 16046318; 16101942; 16133987; 16166103; 16195814; 16200868; 16210662; 16236836; 16272823; 16275384; 16303333; 16315031; 16327802; 16375755; 16387595; 16388492; 16403098; 16428771; 16461126; 16493441; 16522370; 16681592; 16702372; 16750991; 16751012; 16832637; 16849505; 16867043; 16914241; 16918506; 16951338; 16961803; 16987060; 17001290; 17006604; 17016624; 17082655; 17090525; 17091279; 17097743; 17142763; 17182591; 17183946; 17201240; 17209513; 17235327; 17251453; 17264150; 17284225; 17287067; 17291854; 17303794; 17303923; 17313976; 17346294; 17347445; 17355643; 17388919; 17418380; 17451413; 17517104; 17543424; 17548690; 17560640; 17561245; 17563406; 17597813; 17603012; 17615386; 17623648; 17644317; 17703412; 17717322; 17868461; 17883727; 17911623; 18006935; 18028994; 18037162; 18056382; 18073124; 18186920; 18204280; 18243101; 18243827; 18251702; 18263811; 18273035; 18296657; 18296848; 18312531; 18341619; 18348727; 18385759; 18395486; 18403443; 18410415; 18410779; 18417506; 18418228; 18441092; 18441098; 18497474; 18506597; 18545091; 18551035; 18625055; 18633131; 18674658; 18676680; 18676870; 18688040; 18691306; 18699941; 18712166; 18815020; 18818748; 18849614; 18927306; 18931077; 18931892; 18941246; 18949100; 18974840; 18989750; 19005922; 19011907; 19019335; 19074885; 19109239; 19116009; 19122650; 19131452; 19131662; 19141347; 19169254; 19170196; 19178408; 19190772; 19192232; 19220774; 19222422; 19225544; 19231232; 19247692; 19251840; 19254294; 19258923; 19262574; 19263529; 19264973; 19326508; 19332998; 19333920; 19417211; 19420105; 19470259; 19479237; 19487697; 19505916; 19507063; 19515749; 19527514; 19536153; 19554022; 19555572; 19559392; 19573080; 19575932; 19578876; 19586918; 19602238; 19625176; 19635933; 19654941; 19659863; 19674346; 19692168; 19706316; 19706623; 19726720; 19729601; 19739097; 19759281; 19772762; 19773279; 19773451; 19789190; 19796199; 19840389; 19862939; 19910508; 19913121; 19933216; 19948975; 19968504; 19995275; 20051514; 20081054; 20085599; 20093796; 20107485; 20140262; 20159242; 20177070; 20194818; 20198887; 20207250; 20208004; 20219689; 20224668; 20236697; 20237496; 20299965; 20306654; 20332709; 20358028; 20368097; 20394509; 20395963; 20403202; 20403914; 20406594; 20418110; 20418295; 20444155; 20453000; 20484924; 20485362; 20503287; 20530519; 20536507; 20539013; 20543112; 20568250; 20572918; 20589076; 20603037; 20628086; 20644561; 20652946; 20703737; 20714168; 20800603; 20802378; 20811626; 20860503; 20861864; 20942272; 20975284; 21061265; 21067601; 21071541; 21076368; 21097505; 21191414; 21191416; 21198753; 21235536; 21236478; 21239604; 21275604; 21289305; 21325281; 21425907; 21426411; 21430433; 21478113; 21489615; 21576506; 21613309; 21616524; 21677024; 21762457; 21913997; 21920770; 22013915; 22023794; 22039015; 22039304; 22045834; 22053598; 22075330; 22087298; 22092872; 22123380; 22154382; 22166239; 22170601; 22204768; 22222605; 22226971; 22229804; 22236719; 22286212; 22287592; 22317767; 22325047; 22355542; 22370092; 22376040; 22407982; 22432974; 22441356; 22471460; 22506826; 22521249; 22534877; 22573806; 22574126; 22661199; 22686311; 22698804; 22741617; 22749024; 22750299; 22846750; 22952702; 22981205; 23042114; 23045480; 23070918; 23108822; 23128233; 23171465; 23184931; 23222300; 23223131; 23246181; 23249391; 23300643; 23317483; 23333326; 23376457; 23382814; 23395224; 23437086; 23510983; 23521898; 23545317; 23614810; 23663500; 23666277; 23713409; 23754348; 23810766; 23815671; 23817569; 23841068; 23865080; 23874547; 23886662; 24001799; 24053708; 24105413 interleukin 13 Ensembl:ENSG00000169194 HGNC:5973 HPRD:00981 MIM:147683 Vega:OTTHUMG00000059723 Other designations: interleukin-13 IL13 OGG:3000003600 Bin Zhao, Yue Liu, Oliver He IL-15 WEB: http://www.ncbi.nlm.nih.gov/gene IL15 interleukin 15 3600 4q31 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0001779 (EC: IEA); GO_0001866 (EC: IEA); GO_0005125 (EC: IEA); GO_0005126 (EC: IEA); GO_0005515 (EC: IPI, PMID: 16284400); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005615 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005768 (EC: TAS, PMID: 10851076); GO_0005794 (EC: TAS, PMID: 10851076); GO_0005887 (EC: TAS, PMID: 10851076); GO_0006954 (EC: IEA); GO_0006955 (EC: IEA); GO_0007165 (EC: TAS, PMID: 8178155); GO_0007267 (EC: TAS, PMID: 7759105); GO_0007568 (EC: IEA); GO_0008284 (EC: TAS, PMID: 10851076); GO_0009986 (EC: IEA); GO_0014732 (EC: IEA); GO_0016020 (EC: TAS, PMID: 10851076); GO_0030212 (EC: IEA); GO_0032740 (EC: IDA, PMID: 16482511); GO_0032819 (EC: IEA); GO_0032825 (EC: IEA); GO_0034105 (EC: IC, PMID: 16482511); GO_0042102 (EC: IEA); GO_0042517 (EC: IEA); GO_0045062 (EC: IEA); GO_0045580 (EC: IEA); GO_0048469 (EC: IEA); GO_0048535 (EC: IEA); GO_0048662 (EC: IEA); GO_0050691 (EC: IEA); GO_0050729 (EC: IC, PMID: 16482511); GO_0050778 (EC: IEA); GO_0071305 (EC: IEA) PMID: 7568001; 7641685; 7759105; 8026467; 8178155; 8568232; 8668345; 8932977; 8977197; 9176231; 9405632; 10388525; 10784451; 10851076; 10869346; 11122241; 11134140; 11134366; 11168804; 11287118; 11369758; 11581322; 11680634; 11702064; 11746271; 11751999; 11807773; 11814312; 11830476; 11876762; 11919076; 11972069; 12089333; 12089714; 12114302; 12115611; 12147628; 12165497; 12237122; 12297341; 12379638; 12391205; 12393488; 12401478; 12421959; 12453470; 12477932; 12542496; 12571184; 12598649; 12623850; 12734346; 12747456; 12757260; 12759422; 12805064; 12826231; 12847234; 12857602; 12865812; 12960322; 14499665; 14581351; 14607929; 14607946; 14617758; 14648805; 14662842; 14684414; 14702039; 14718574; 14762166; 14967307; 14982947; 14984938; 15034035; 15039446; 15131572; 15225634; 15328153; 15347678; 15353479; 15358647; 15489334; 15531573; 15536127; 15557159; 15563472; 15598425; 15710591; 15713701; 15770395; 15778359; 15943034; 15976176; 15993713; 16024007; 16060678; 16098919; 16109314; 16136475; 16148110; 16273100; 16284400; 16333313; 16427155; 16474399; 16482511; 16507118; 16606671; 16629787; 16670327; 16772281; 16791279; 17001647; 17077296; 17110377; 17142786; 17158609; 17324400; 17363780; 17431094; 17537415; 17554368; 17616399; 17635814; 17655329; 17703412; 17938255; 17947730; 17964972; 17982063; 17986095; 18086532; 18275895; 18280748; 18295891; 18311795; 18348982; 18365236; 18419254; 18424079; 18431516; 18482208; 18493613; 18493981; 18505820; 18509087; 18514540; 18523245; 18524812; 18580966; 18583567; 18633131; 18656487; 18676680; 18697873; 18706446; 18782269; 18818748; 18840707; 18981132; 19013323; 19019335; 19047106; 19088135; 19133918; 19170196; 19176441; 19188921; 19233474; 19237603; 19240061; 19247692; 19258923; 19325034; 19406127; 19414768; 19414770; 19414780; 19449444; 19505916; 19527514; 19546878; 19570824; 19573080; 19592095; 19593212; 19625176; 19657406; 19692168; 19696432; 19703339; 19710458; 19756346; 19773279; 19796965; 19821081; 19835475; 19913121; 19949092; 20007590; 20012528; 20043070; 20083555; 20140262; 20142427; 20153259; 20166880; 20190192; 20237496; 20331472; 20381491; 20414345; 20430958; 20444155; 20453000; 20483740; 20503287; 20538758; 20560915; 20568250; 20622171; 20628086; 20631381; 20670353; 20671116; 20732850; 20736143; 20956026; 21048031; 21049047; 21074481; 21132303; 21169670; 21190865; 21204897; 21242188; 21300928; 21307608; 21334074; 21474552; 21487524; 21539877; 21562158; 21572025; 21715685; 21723324; 21724805; 21765616; 21769475; 21779162; 21788945; 21813181; 21832049; 21852331; 21911607; 21925225; 21943235; 21945396; 21973023; 21984699; 21988722; 21988832; 22055728; 22084435; 22242124; 22261234; 22363690; 22440823; 22447977; 22467658; 22471460; 22496150; 22510877; 22535664; 22537815; 22563505; 22565311; 22785229; 23058476; 23072822; 23074221; 23104097; 23153537; 23157547; 23160470; 23214284; 23214303; 23325887; 23401701; 23417200; 23437070; 23577098; 23637340; 23649624; 23649772; 23873932; 23904478; 23996684; 24184554 interleukin 15 Ensembl:ENSG00000164136 HGNC:5977 HPRD:02776 MIM:600554 Vega:OTTHUMG00000133418 Other designations: interleukin-15 IL15 OGG:3000003604 Bin Zhao, Yue Liu, Oliver He 4-1BB CD137 CDw137 ILA WEB: http://www.ncbi.nlm.nih.gov/gene TNFRSF9 tumor necrosis factor receptor superfamily, member 9 3604 1p36 9606 1 Official from a nomenclature committee GO_0004872 (EC: IEA); GO_0005615 (EC: IEA); GO_0005887 (EC: TAS, PMID: 8262389); GO_0006915 (EC: TAS, PMID: 8639902); GO_0008285 (EC: TAS, PMID: 8639902); GO_0009897 (EC: IEA); GO_0019955 (EC: IEA); GO_0070207 (EC: IEA); GO_2001180 (EC: IEA); GO_2001183 (EC: IEA) PMID: 2784565; 7622190; 8088337; 8262389; 8639902; 9045669; 9207223; 9418902; 9464265; 9541583; 9607925; 10556203; 10604232; 11804328; 11828369; 11970964; 12009595; 12101260; 12356681; 12384425; 12477932; 12516549; 12645943; 13130507; 14716821; 15031666; 15301860; 15308117; 15340161; 15342556; 15353478; 15489334; 15618293; 15638367; 15941918; 16232366; 16596186; 16710414; 17309825; 17878391; 17878400; 18024793; 18276843; 18519814; 18645038; 18668547; 18768897; 18838252; 19211796; 19406689; 19573080; 19759901; 19773279; 19913121; 20008291; 20026323; 20190752; 20237496; 20347151; 20568250; 20616340; 20628086; 20643812; 21297633; 21396356; 21669186; 21670469; 21745658; 21747409; 21890473; 21963611; 22144129; 22204816; 22282196; 22326955; 22343053; 22343199; 22593548; 22797667; 22896640; 22901750; 23000965; 23128233; 23204227; 23437083; 23557259; 23560068; 23640752; 23690480; 23750604 tumor necrosis factor receptor superfamily, member 9 HGNC:11924 HPRD:03767 MIM:602250 Other designations: 4-1BB ligand receptor|CD137 antigen|T cell antigen ILA|T-cell antigen 4-1BB homolog|T-cell antigen ILA|homolog of mouse 4-1BB|induced by lymphocyte activation (ILA)|interleukin-activated receptor, homolog of mouse Ly63|receptor protein 4-1BB|tumor necrosis factor receptor superfamily member 9 TNFRSF9 OGG:3000003605 Bin Zhao, Yue Liu, Oliver He CTLA8 IL-17 IL-17A IL17 WEB: http://www.ncbi.nlm.nih.gov/gene IL17A interleukin 17A 3605 6p12 20140408 9606 6 protein-coding Official from a nomenclature committee GO_0005125 (EC: IEA); GO_0005615 (EC: IEA); GO_0006486 (EC: TAS, PMID: 7499828); GO_0006915 (EC: TAS, PMID: 7499828); GO_0006954 (EC: IEA); GO_0006955 (EC: TAS, PMID: 7499828); GO_0007267 (EC: TAS, PMID: 7499828); GO_0008219 (EC: TAS, PMID: 8390535); GO_0009897 (EC: IEA); GO_0032747 (EC: IDA); GO_0045672 (EC: IDA, PMID: 17888176); GO_0045944 (EC: IDA, PMID: 16982811); GO_0071347 (EC: IEA); GO_0072537 (EC: IDA); GO_1900017 (EC: IEA) PMID: 7499828; 8390535; 8676080; 9367539; 9518462; 9764847; 9765276; 9878122; 9973514; 10225978; 10328864; 11472426; 11936535; 12165487; 12183057; 12297109; 12417590; 12421973; 12477932; 12667656; 12721789; 12772186; 14718574; 15025215; 15218177; 15305382; 15321994; 15340161; 15388258; 15459204; 15489334; 15535837; 15642151; 15811054; 15811056; 15845864; 15916703; 15972674; 16008887; 16207434; 16419159; 16533341; 16859642; 16874957; 16982811; 17083726; 17207965; 17384030; 17486092; 17545490; 17613395; 17635957; 17644317; 17682667; 17703412; 17828618; 17876645; 17888176; 17912466; 17965778; 17982039; 18075825; 18079209; 18092129; 18097022; 18156204; 18157139; 18203309; 18311793; 18311821; 18329249; 18337720; 18362142; 18373953; 18392953; 18400187; 18432274; 18434325; 18440075; 18446062; 18483277; 18501882; 18512780; 18579762; 18585926; 18588867; 18591410; 18591412; 18600325; 18602680; 18615114; 18617638; 18663128; 18669891; 18684971; 18684981; 18769923; 18786233; 18793860; 18802076; 18802458; 18832156; 18926293; 18941172; 18941201; 18941244; 18992745; 19014637; 19050268; 19050297; 19056110; 19075290; 19079215; 19124735; 19127457; 19131064; 19174010; 19177575; 19187277; 19199539; 19201028; 19208686; 19210369; 19226302; 19234216; 19235914; 19239321; 19240794; 19242409; 19244159; 19247658; 19255340; 19258923; 19260856; 19265112; 19265168; 19273860; 19295614; 19322214; 19325128; 19329213; 19333939; 19339380; 19343046; 19347604; 19404732; 19414056; 19424201; 19426392; 19428338; 19431078; 19439651; 19457169; 19476112; 19476435; 19479806; 19479869; 19483719; 19485773; 19487306; 19535626; 19536281; 19543237; 19545679; 19550095; 19566585; 19587005; 19589271; 19620772; 19627579; 19628296; 19672092; 19692128; 19700754; 19724898; 19728295; 19737863; 19741026; 19741298; 19748982; 19797506; 19822653; 19825828; 19830738; 19835883; 19838198; 19843935; 19844129; 19857751; 19861249; 19878510; 19895848; 19904747; 19907660; 19912248; 19912249; 19912251; 19912252; 19917178; 19929695; 19931506; 19936899; 19940509; 19968632; 19969371; 20016509; 20022135; 20026736; 20026744; 20032993; 20042592; 20061410; 20070409; 20099977; 20106535; 20107878; 20112373; 20127054; 20159251; 20167120; 20173024; 20173782; 20185422; 20200272; 20207161; 20228195; 20228199; 20228201; 20237496; 20299682; 20305686; 20306850; 20334681; 20339909; 20350814; 20352428; 20357253; 20357258; 20379614; 20395418; 20418110; 20437253; 20445554; 20493423; 20503287; 20506642; 20511548; 20511558; 20515574; 20533542; 20563617; 20581151; 20592279; 20596075; 20596087; 20618180; 20620187; 20624941; 20646637; 20664052; 20665551; 20667562; 20682672; 20685755; 20718783; 20720207; 20810982; 20812962; 20814021; 20825419; 20840794; 20848848; 20856230; 20874252; 20889558; 20952660; 20974984; 20976193; 21029245; 21044126; 21048031; 21060663; 21062492; 21062626; 21091665; 21103795; 21109552; 21116820; 21116822; 21124836; 21129248; 21143945; 21161669; 21178008; 21181220; 21182094; 21189442; 21196925; 21204897; 21217016; 21217785; 21225222; 21231819; 21236478; 21245272; 21248258; 21282514; 21292197; 21294864; 21294892; 21346774; 21357259; 21369705; 21396350; 21426710; 21440743; 21447959; 21455110; 21474820; 21477350; 21478400; 21498517; 21505189; 21518507; 21521755; 21524680; 21526159; 21528751; 21530487; 21530504; 21546069; 21573786; 21602493; 21606249; 21625016; 21637854; 21641076; 21651870; 21654633; 21654831; 21659501; 21672939; 21674477; 21685328; 21689402; 21691744; 21710691; 21721104; 21732985; 21737283; 21741035; 21746882; 21749686; 21752104; 21755509; 21760911; 21761512; 21762495; 21781514; 21785272; 21795048; 21796151; 21798287; 21828034; 21865860; 21872532; 21887369; 21894475; 21896776; 21897004; 21904631; 21911461; 21926059; 21929599; 21943235; 21949023; 21949691; 21949768; 21959034; 21960179; 21964025; 21966367; 21968742; 21972211; 21977994; 21980832; 21982596; 21984702; 21994045; 21996014; 21996293; 21998454; 22020264; 22025620; 22026963; 22028838; 22031591; 22035960; 22042699; 22048239; 22051182; 22079540; 22082565; 22123224; 22123380; 22138182; 22171994; 22186234; 22191467; 22207110; 22219048; 22219320; 22229441; 22235998; 22237416; 22258491; 22261033; 22262980; 22302060; 22312940; 22362575; 22395503; 22417709; 22419580; 22442208; 22444300; 22461912; 22462422; 22464815; 22466961; 22483685; 22496194; 22507625; 22527432; 22532631; 22534817; 22537748; 22541406; 22559912; 22563781; 22585726; 22627363; 22629719; 22641009; 22647601; 22655909; 22660635; 22677045; 22683003; 22692973; 22696687; 22744708; 22748016; 22759859; 22789685; 22795370; 22800829; 22808218; 22812212; 22814515; 22816799; 22818182; 22819243; 22825627; 22827846; 22840497; 22851868; 22876724; 22880090; 22902060; 22902077; 22928014; 22955875; 22960198; 22965992; 22974591; 22984500; 22989213; 22989874; 22993227; 23009764; 23012664; 23018031; 23019580; 23033269; 23034167; 23049595; 23071273; 23091305; 23098499; 23101722; 23131423; 23137879; 23147652; 23158993; 23181791; 23192273; 23204182; 23207971; 23215950; 23223131; 23226545; 23226926; 23227158; 23232337; 23237940; 23238559; 23262228; 23269607; 23271701; 23273903; 23274784; 23274801; 23298391; 23304063; 23322904; 23323524; 23327801; 23334598; 23335253; 23352235; 23388330; 23400328; 23401702; 23409930; 23411595; 23414478; 23416458; 23444260; 23448394; 23448791; 23472658; 23485736; 23490420; 23501056; 23505558; 23555269; 23555579; 23596310; 23613503; 23614810; 23616636; 23652560; 23656167; 23661335; 23664273; 23683514; 23690194; 23692034; 23695682; 23711712; 23732752; 23764374; 23800059; 23815507; 23825942; 23826419; 23842754; 23849453; 23876429; 23888551; 23923066; 23924903; 23965869; 23970818; 23995070; 24021410; 24042116; 24080022; 24086143; 24096234; 24120361; 24141678; 24185279; 24323355; 24409666; 24409674; 24579469 interleukin 17A Ensembl:ENSG00000112115 HGNC:5981 HPRD:04396 MIM:603149 Vega:OTTHUMG00000014840 Other designations: CTLA-8|cytotoxic T-lymphocyte-associated antigen 8|cytotoxic T-lymphocyte-associated protein 8|interleukin 17 (cytotoxic T-lymphocyte-associated serine esterase 8)|interleukin-17A IL17A OGG:3000003606 Bin Zhao, Yue Liu, Oliver He IGIF IL-18 IL-1g IL1F4 WEB: http://www.ncbi.nlm.nih.gov/gene IL18 interleukin 18 3606 11q22.2-q22.3 20140409 9606 11 protein-coding Official from a nomenclature committee GO_0000165 (EC: IMP); GO_0001525 (EC: IDA, PMID: 11466388); GO_0005125 (EC: TAS, PMID: 11598150); GO_0005576 (EC: TAS, PMID: 11598150); GO_0005615 (EC: IEA); GO_0005829 (EC: TAS); GO_0006954 (EC: IDA); GO_0006955 (EC: TAS, PMID: 8999896); GO_0007267 (EC: TAS, PMID: 9792649); GO_0010628 (EC: IEA); GO_0030101 (EC: IEA); GO_0030155 (EC: IDA, PMID: 11477102); GO_0030431 (EC: ISS, PMID: 11506998); GO_0031663 (EC: IDA); GO_0032725 (EC: IDA); GO_0032729 (EC: IDA, PMID: 19088061); GO_0032740 (EC: IDA, PMID: 16482511); GO_0032819 (EC: IDA, PMID: 19088061); GO_0034105 (EC: IC, PMID: 16482511); GO_0042033 (EC: TAS, PMID: 11598150); GO_0042088 (EC: IDA, PMID: 8766574); GO_0042092 (EC: TAS, PMID: 11905033); GO_0042094 (EC: TAS, PMID: 10653850); GO_0042095 (EC: TAS, PMID: 10227975); GO_0042104 (EC: IDA, PMID: 10000000); GO_0042231 (EC: TAS, PMID: 10227975); GO_0042253 (EC: TAS, PMID: 10653850); GO_0042346 (EC: IEA); GO_0050729 (EC: IC, PMID: 16482511); GO_0051142 (EC: IDA, PMID: 19088061); GO_0071407 (EC: IDA) PMID: 7477296; 8666798; 8766574; 8999548; 8999896; 9108085; 9325300; 9334240; 9693051; 9792649; 10000000; 10227975; 10460493; 10639148; 10653850; 10681439; 11466388; 11477102; 11506998; 11598150; 11714750; 11714826; 11770036; 11781190; 11790772; 11798931; 11805151; 11855785; 11888846; 11894141; 11895335; 11905033; 11907126; 11920321; 11936774; 11958300; 11960649; 12096920; 12105209; 12149432; 12172382; 12207348; 12366781; 12377944; 12381835; 12387830; 12390326; 12401730; 12424620; 12438388; 12456593; 12472176; 12472673; 12477932; 12482935; 12517977; 12527894; 12571842; 12572878; 12594843; 12616343; 12654091; 12679613; 12738632; 12748489; 12759422; 12788305; 12794718; 12796418; 12819633; 12847274; 12857602; 12858406; 12874316; 12911784; 12938205; 12941729; 12947340; 14504095; 14556808; 14561165; 14581397; 14584052; 14605444; 14617033; 14630085; 14640907; 14660053; 14662834; 14679107; 14697936; 14709415; 14718574; 14725568; 14734463; 14738910; 14764217; 14960579; 14991611; 14998974; 15005726; 15104599; 15140035; 15212675; 15225625; 15230817; 15277983; 15302292; 15308504; 15326478; 15327523; 15358638; 15371332; 15463896; 15471361; 15489334; 15555533; 15581980; 15585330; 15643599; 15644127; 15645140; 15646011; 15663745; 15674367; 15710458; 15728489; 15731584; 15753257; 15760905; 15786533; 15789055; 15802534; 15806006; 15816833; 15826815; 15842270; 15860738; 15860756; 15863395; 15894108; 15896202; 15927856; 15932380; 15955098; 15963597; 16024007; 16043644; 16049975; 16051062; 16052331; 16053025; 16059673; 16061751; 16078996; 16084898; 16186395; 16215941; 16243298; 16260350; 16266857; 16273766; 16306550; 16306764; 16306765; 16315783; 16316892; 16325763; 16339124; 16358956; 16373926; 16405895; 16406079; 16406656; 16420594; 16424284; 16428475; 16433722; 16433859; 16443795; 16482511; 16492204; 16493047; 16514436; 16516851; 16556702; 16563174; 16571086; 16584830; 16621994; 16635219; 16647017; 16650813; 16671950; 16738942; 16759385; 16767839; 16772281; 16780720; 16806233; 16820919; 16827865; 16839849; 16842597; 16883062; 16903774; 16909454; 16943580; 16948912; 16971411; 16979683; 17001321; 17016692; 17027359; 17055358; 17072982; 17075246; 17077020; 17117487; 17142727; 17192354; 17222831; 17225121; 17225924; 17235324; 17237446; 17252172; 17262717; 17299019; 17301041; 17336309; 17343316; 17355643; 17361200; 17364073; 17373930; 17396252; 17399992; 17445542; 17461482; 17487222; 17517100; 17517876; 17530707; 17586702; 17597334; 17597823; 17605864; 17610422; 17611614; 17611643; 17611971; 17625598; 17626902; 17658666; 17666338; 17671745; 17674327; 17683383; 17687255; 17688413; 17691022; 17703412; 17708609; 17765248; 17767553; 17845300; 17851127; 17851835; 17854431; 17893261; 17907957; 17919265; 17922692; 17948066; 17951325; 17959666; 17962365; 17964972; 17965486; 17981284; 17984243; 17988833; 18024284; 18043444; 18050195; 18050226; 18064631; 18092318; 18093181; 18160214; 18160936; 18163476; 18165223; 18178861; 18200581; 18225542; 18225563; 18235016; 18237555; 18250135; 18279187; 18286551; 18287807; 18295214; 18295340; 18297714; 18307517; 18336908; 18359638; 18386818; 18391570; 18399311; 18433937; 18442334; 18464913; 18484687; 18504197; 18514203; 18514661; 18520705; 18523012; 18538088; 18555694; 18562922; 18566306; 18594952; 18599493; 18628791; 18632660; 18662786; 18678419; 18683145; 18684981; 18685607; 18706445; 18773860; 18777510; 18780764; 18781864; 18803662; 18818748; 18818761; 18819819; 18821674; 18835036; 18853133; 18922682; 18930181; 18937548; 18940019; 18949051; 18983635; 19016763; 19019335; 19031096; 19036565; 19064572; 19073159; 19074166; 19074885; 19077897; 19088061; 19091595; 19092166; 19097518; 19102398; 19110334; 19126646; 19131059; 19138654; 19152241; 19176284; 19178691; 19200605; 19208460; 19229765; 19230467; 19236760; 19247692; 19258923; 19263242; 19265133; 19265174; 19285156; 19288449; 19309308; 19339355; 19342689; 19347053; 19387647; 19390575; 19394601; 19403407; 19420105; 19443970; 19453784; 19455410; 19466545; 19469892; 19470251; 19473509; 19508433; 19509137; 19527514; 19538326; 19550095; 19553661; 19573080; 19581111; 19584085; 19593889; 19605669; 19622039; 19633236; 19637196; 19638090; 19638429; 19639049; 19642044; 19657406; 19669125; 19669363; 19684151; 19687159; 19692203; 19699611; 19712260; 19740312; 19745201; 19757044; 19758166; 19773279; 19789190; 19796548; 19811440; 19816189; 19817957; 19865096; 19879772; 19900154; 19907017; 19913121; 19954659; 19961286; 19961892; 20003764; 20017708; 20056178; 20060272; 20061784; 20083555; 20096599; 20097272; 20137369; 20140262; 20140691; 20150558; 20169140; 20186552; 20216908; 20227257; 20227263; 20233133; 20237496; 20304021; 20306652; 20306665; 20331838; 20331879; 20339966; 20340055; 20349123; 20350254; 20374388; 20399512; 20412718; 20414054; 20416077; 20418295; 20423837; 20424918; 20441695; 20452482; 20478055; 20482998; 20485444; 20490717; 20490891; 20522205; 20525402; 20530519; 20538124; 20545903; 20558561; 20565717; 20568250; 20586818; 20617584; 20627039; 20628086; 20673868; 20689079; 20725807; 20735470; 20797704; 20818961; 20824296; 20885390; 20960175; 20964873; 20971720; 21035858; 21061265; 21118329; 21120501; 21126942; 21139048; 21145535; 21149337; 21149398; 21224476; 21225442; 21239711; 21241672; 21249128; 21264805; 21273776; 21288140; 21321938; 21323571; 21323573; 21334074; 21336086; 21356600; 21382268; 21393015; 21394384; 21395662; 21398142; 21418456; 21418867; 21421008; 21437204; 21440322; 21448661; 21464751; 21470492; 21481392; 21484426; 21487696; 21510800; 21526496; 21532063; 21538928; 21571262; 21611751; 21636628; 21656327; 21661419; 21672342; 21681500; 21710494; 21723753; 21733366; 21742406; 21742843; 21802664; 21832842; 21836143; 21836147; 21840518; 21842238; 21864160; 21867627; 21876975; 21906983; 21922295; 21943853; 21963094; 21965503; 21969001; 21988832; 22008665; 22015107; 22058412; 22125454; 22135309; 22136483; 22141572; 22149501; 22226490; 22228436; 22289535; 22307326; 22325058; 22347372; 22364914; 22373801; 22386125; 22462419; 22468101; 22484385; 22489883; 22493490; 22515481; 22518072; 22531046; 22537138; 22537218; 22587568; 22595646; 22596175; 22613414; 22639237; 22664470; 22678894; 22686311; 22723447; 22749533; 22811364; 22825306; 22837141; 22840759; 22863216; 22883217; 22900713; 22913567; 22945280; 22980562; 22996386; 23000965; 23018032; 23023653; 23027874; 23028054; 23056251; 23073298; 23075512; 23085113; 23121308; 23132931; 23137633; 23153245; 23171362; 23178856; 23207179; 23214284; 23232703; 23238919; 23242610; 23257837; 23269628; 23276493; 23298491; 23302036; 23327592; 23403235; 23419721; 23433789; 23459183; 23499732; 23522322; 23526823; 23546966; 23557801; 23587914; 23603311; 23632060; 23656272; 23675517; 23702484; 23702978; 23707237; 23723976; 23741523; 23746337; 23793845; 23794112; 23883285; 23885403; 23888552; 23901078; 23904224; 23938462; 24331389 interleukin 18 Ensembl:ENSG00000150782 HGNC:5986 HPRD:02976 MIM:600953 Vega:OTTHUMG00000167006 IL18 OGG:3000003627 Bin Zhao, Yue Liu, Oliver He C7 IFI10 INP10 IP-10 SCYB10 crg-2 gIP-10 mob-1 WEB: http://www.ncbi.nlm.nih.gov/gene CXCL10 chemokine (C-X-C motif) ligand 10 3627 4q21 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0002690 (EC: IEA); GO_0005102 (EC: TAS, PMID: 10201891); GO_0005515 (EC: IPI, PMID: 18275857); GO_0005576 (EC: IDA); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0006935 (EC: IDA, PMID: 12782716); GO_0006954 (EC: IEA); GO_0006955 (EC: IEA); GO_0007165 (EC: TAS, PMID: 10201891); GO_0007166 (EC: TAS, PMID: 10903763); GO_0007186 (EC: IMP, PMID: 12782716); GO_0007267 (EC: TAS, PMID: 3925348); GO_0007517 (EC: TAS, PMID: 8798675); GO_0008009 (EC: IDA, PMID: 12782716); GO_0008015 (EC: TAS, PMID: 8798675); GO_0008201 (EC: IMP, PMID: 18645041); GO_0008284 (EC: IEA); GO_0008603 (EC: TAS, PMID: 10903763); GO_0009306 (EC: IEA); GO_0009409 (EC: IEA); GO_0009897 (EC: IEA); GO_0010332 (EC: IEA); GO_0010818 (EC: IMP, PMID: 18645041); GO_0010996 (EC: IEA); GO_0016525 (EC: IEA); GO_0030816 (EC: IDA, PMID: 12782716); GO_0032496 (EC: IEA); GO_0033280 (EC: IEA); GO_0034605 (EC: IEA); GO_0042127 (EC: IDA, PMID: 12782716); GO_0043950 (EC: IDA, PMID: 12782716); GO_0045859 (EC: TAS, PMID: 10903763); GO_0045944 (EC: TAS, PMID: 12782716); GO_0048248 (EC: IDA, PMID: 12782716); GO_0051281 (EC: IDA, PMID: 12782716); GO_0051607 (EC: IEA); GO_0070098 (EC: IMP, PMID: 18645041) PMID: 2437586; 3925348; 7566098; 8145049; 8423327; 8798675; 9022006; 9060447; 9462486; 9705166; 10201891; 10201901; 10233762; 10903763; 10982368; 11083865; 11110785; 11390394; 11401991; 11418676; 11467655; 11559369; 11818520; 11867072; 11878903; 11897701; 12016104; 12089333; 12117914; 12117926; 12126650; 12162873; 12173928; 12189440; 12270371; 12356205; 12384933; 12393716; 12441140; 12445801; 12477932; 12539042; 12571234; 12584353; 12603854; 12663757; 12667820; 12668159; 12698106; 12718750; 12737818; 12782716; 12794718; 12819030; 12819903; 12847218; 12847282; 12856973; 12884299; 12930373; 12946268; 14507644; 14550288; 14578618; 14600836; 14630801; 14739277; 15063730; 15081247; 15081261; 15150261; 15307834; 15315758; 15489334; 15518810; 15644410; 15725351; 15745922; 15814716; 15843529; 15879427; 15880073; 15885315; 15919935; 15944327; 15988033; 16181055; 16195357; 16200621; 16210647; 16243485; 16490936; 16507178; 16581825; 16645011; 16697675; 16709871; 16733654; 16825597; 16864907; 16867276; 16920957; 16931519; 16934957; 16969644; 17018607; 17052298; 17052299; 17085967; 17211148; 17244787; 17250724; 17255201; 17360657; 17364892; 17467667; 17505511; 17541284; 17628646; 17652371; 17668902; 17763275; 17763328; 17766680; 17875534; 17912012; 17943641; 17957030; 17963704; 17996064; 18037659; 18046562; 18085351; 18234638; 18240029; 18259970; 18275857; 18281042; 18282714; 18325387; 18379127; 18415893; 18424889; 18538864; 18569454; 18645041; 18647352; 18682747; 18684849; 18702954; 18729739; 18798334; 18855195; 18973545; 18985732; 18986693; 19031697; 19065267; 19070948; 19088500; 19105984; 19134328; 19155980; 19175890; 19181310; 19187771; 19195322; 19203362; 19223260; 19258635; 19274094; 19281798; 19327225; 19342252; 19342664; 19410617; 19441886; 19447045; 19459809; 19472212; 19479051; 19506876; 19508602; 19523460; 19558503; 19565490; 19590927; 19639049; 19641142; 19694638; 19756997; 19800124; 19817957; 19821051; 19827943; 19880820; 19887486; 19901067; 19918044; 19939453; 19941336; 19969087; 20041963; 20056178; 20059481; 20137269; 20137825; 20144041; 20153790; 20164184; 20186422; 20186843; 20187787; 20299237; 20302596; 20404089; 20473322; 20485145; 20485444; 20523065; 20525556; 20592450; 20626297; 20648615; 20680966; 20833730; 20856926; 20929277; 20942936; 20943047; 20948191; 20980518; 21045270; 21054674; 21062959; 21099280; 21106778; 21167783; 21183794; 21191639; 21219680; 21254158; 21270681; 21274647; 21303425; 21303517; 21390311; 21454254; 21457060; 21475065; 21489350; 21497908; 21508508; 21531038; 21601475; 21613464; 21645215; 21649525; 21708014; 21725974; 21802343; 21811993; 21812928; 21849907; 21897004; 21906079; 21912394; 21962843; 21966356; 22004287; 22008312; 22022583; 22037980; 22038159; 22053613; 22058116; 22117591; 22136974; 22160826; 22168752; 22178859; 22192885; 22367045; 22390571; 22393386; 22401175; 22471703; 22472061; 22491449; 22496888; 22562465; 22564606; 22621182; 22634718; 22652417; 22675025; 22685032; 22697070; 22738089; 22746298; 22800603; 22809599; 22814248; 22892369; 22896023; 22905138; 22975476; 22989785; 22996399; 23011799; 23012327; 23024806; 23034049; 23056251; 23065240; 23092582; 23118425; 23118858; 23144331; 23150742; 23213058; 23265968; 23272100; 23288171; 23291247; 23291435; 23306067; 23312578; 23322900; 23333920; 23352833; 23437705; 23458521; 23505918; 23542734; 23559389; 23589576; 23600831; 23614810; 23629827; 23630573; 23684765; 23740952; 23743311; 23762283; 23873303; 23905710; 23998932; 24023775; 24025324; 24063316; 24273934; 24600982 chemokine (C-X-C motif) ligand 10 Ensembl:ENSG00000169245 HGNC:10637 HPRD:00930 MIM:147310 Vega:OTTHUMG00000160887 Other designations: 10 kDa interferon gamma-induced protein|C-X-C motif chemokine 10|gamma IP10|gamma-IP10|interferon-inducible cytokine IP-10|protein 10 from interferon (gamma)-induced cell line|small inducible cytokine subfamily B (Cys-X-Cys), member 10|small-inducible cytokine B10 CXCL10 gene OGG:3000003638 Bin Zhao, Yue Liu, Oliver He CL-6 CL6 WEB: http://www.ncbi.nlm.nih.gov/gene INSIG1 insulin induced gene 1 3638 7q36 9606 7 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 12202038); GO_0005783 (EC: IDA, PMID: 12202038); GO_0005789 (EC: TAS); GO_0006641 (EC: IEA); GO_0006695 (EC: IEA); GO_0008152 (EC: TAS, PMID: 9268630); GO_0008283 (EC: TAS, PMID: 9268630); GO_0010894 (EC: IEA); GO_0032933 (EC: IDA, PMID: 12242332); GO_0032937 (EC: IDA, PMID: 15899885); GO_0042472 (EC: IEA); GO_0042474 (EC: IEA); GO_0044281 (EC: TAS); GO_0045599 (EC: IEA); GO_0045717 (EC: IEA); GO_0060021 (EC: IEA); GO_0060363 (EC: IEA); GO_1901303 (EC: IMP, PMID: 15899885) PMID: 9268630; 12115587; 12202038; 12242332; 12242342; 12477932; 12482938; 12535518; 12690205; 12842885; 12869692; 12963821; 14660594; 14702039; 15085196; 15247248; 15304479; 15489334; 15782218; 15899885; 16168377; 16344560; 16399501; 16549805; 16606821; 17043353; 17106696; 18187584; 18195716; 18660489; 18835813; 18989534; 19322201; 19458199; 19617589; 19638338; 19740467; 19815544; 19913121; 19965593; 20068067; 20444954; 20458442; 20628086; 20877301; 21081644; 21343306; 21906983; 21963094; 22143767; 22505724; 22648509; 23223569; 24371122 insulin induced gene 1 Ensembl:ENSG00000186480 HGNC:6083 HPRD:03633 MIM:602055 Vega:OTTHUMG00000151330 Other designations: INSIG-1 membrane protein|insulin-induced gene 1 protein INSIG1 OGG:3000003646 Bin Zhao, Yue Liu, Oliver He EIF3-P48 EIF3S6 INT6 eIF3-p46 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3E eukaryotic translation initiation factor 3, subunit E 3646 8q22-q23 9606 8 GO_0000184 (EC: IMP, PMID:17468741); GO_0000785 (EC: NAS, Qualifier: colocalizes_with, PMID:17468741); GO_0001731 (EC: IEA); GO_0003743 (EC: IC, PMID:9295280); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005515 (EC: IPI, PMID:10504338); GO_0005634 (EC: IDA); GO_0005654 (EC: NAS, PMID:17468741); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0005852 (EC: NAS, PMID:10504338); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: NAS, PMID:17468741); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0016605 (EC: IDA, Qualifier: colocalizes_with, PMID:10504338); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0045947 (EC: NAS, PMID:10504338); GO_0047485 (EC: IPI, PMID:10504338); GO_0070062 (EC: IDA) PMID:8688078; 8995409; 8995410; 9295280; 9403073; 9733766; 9822659; 10504338; 10644362; 11118224; 11121040; 11590142; 12220626; 12386384; 12435599; 12477932; 12553909; 12588972; 14519125; 14667819; 14702039; 15030549; 15231748; 15489334; 15558017; 15592455; 15862967; 15867213; 16045761; 16169070; 16189514; 16343815; 16766523; 17220478; 17310990; 17314511; 17322308; 17324924; 17353931; 17403899; 17468741; 17516841; 17581632; 17623298; 18029348; 18562274; 18599441; 18628297; 18781797; 19454010; 19471022; 19615732; 19738201; 20360068; 20434207; 20453879; 20462248; 20890303; 21139048; 21319273; 21693764; 21732829; 21890473; 21906983; 21963094; 21987572; 21988832; 22053931; 22190034; 22268729; 22505724; 22508697; 22532700; 22553336; 22586326; 22623428; 22797925; 22863883; 22907435; 22939629; 23000965; 23184937; 23402259; 23455922; 23463506; 23478175; 24092755; 24250222 eukaryotic translation initiation factor 3, subunit E Ensembl:ENSG00000104408 HGNC:3277 HPRD:03734 MIM:602210 Vega:OTTHUMG00000164858 Other designations: eIF-3 p48|eukaryotic translation initiation factor 3 subunit 6|eukaryotic translation initiation factor 3 subunit E|eukaryotic translation initiation factor 3, subunit 6 (48kD)|eukaryotic translation initiation factor 3, subunit 6 48kDa|mammary tumor-associated protein INT6|murine mammary tumor integration site 6 (oncogene homolog)|viral integration site protein INT-6 homolog EIF3E OGG:3000003659 Bin Zhao, Yue Liu, Oliver He IRF-1 MAR WEB: http://www.ncbi.nlm.nih.gov/gene IRF1 interferon regulatory factor 1 3659 5q31.1 20140408 9606 5 protein-coding Official from a nomenclature committee GO_0000790 (EC: IDA, PMID: 18035482); GO_0000978 (EC: IDA, PMID: 18035482); GO_0002819 (EC: TAS, PMID: 11846971); GO_0003677 (EC: TAS, PMID: 11846971); GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10702232); GO_0005634 (EC: TAS, PMID: 11846971); GO_0005654 (EC: TAS); GO_0005737 (EC: ISS); GO_0005829 (EC: TAS); GO_0006366 (EC: TAS, PMID: 2475256); GO_0006915 (EC: IDA, PMID: 19851330); GO_0007050 (EC: IDA); GO_0007596 (EC: TAS); GO_0008285 (EC: TAS, PMID: 11846974); GO_0019221 (EC: TAS); GO_0032481 (EC: ISS); GO_0032728 (EC: IMP); GO_0034124 (EC: ISS); GO_0035458 (EC: IDA, PMID: 18035482); GO_0043374 (EC: IEA); GO_0045084 (EC: IEA); GO_0045088 (EC: TAS, PMID: 11846971); GO_0045590 (EC: ISS); GO_0045892 (EC: IMP, PMID: 18084608); GO_0045893 (EC: IDA); GO_0045893 (EC: IMP, PMID: 15509808); GO_0045944 (EC: IEA); GO_0051607 (EC: IDA); GO_0051726 (EC: TAS, PMID: 11846974); GO_0060333 (EC: ISS); GO_0060333 (EC: TAS); GO_0060337 (EC: TAS); GO_0071260 (EC: IEP, PMID: 19593445); GO_2000564 (EC: ISS) PMID: 1382447; 1680796; 2475256; 2726461; 3409321; 7507207; 7768900; 8438156; 8746784; 9593745; 9649509; 9659924; 9679752; 9742224; 9865486; 9865487; 10022868; 10094406; 10357819; 10438822; 10702232; 10764778; 11069564; 11240951; 11304541; 11315919; 11483597; 11559933; 11675348; 11716756; 11721695; 11804954; 11846971; 11846972; 11846974; 11909852; 11948194; 11970993; 12021315; 12067985; 12105194; 12115600; 12162881; 12191570; 12420205; 12420214; 12433281; 12477932; 12479817; 12482935; 12545159; 12677441; 12711307; 12732645; 12759449; 12788988; 12799427; 14599866; 14662860; 14675396; 14764039; 14993214; 15078941; 15173018; 15226432; 15241475; 15265939; 15331704; 15489234; 15489334; 15509808; 15511228; 15548708; 15560761; 15576464; 15710386; 15778351; 15863386; 15878912; 15893730; 15907481; 16085646; 16195385; 16195814; 16223733; 16483648; 16512786; 16636311; 16679314; 16703666; 16857162; 16894313; 16914093; 16944293; 16961714; 17016442; 17121613; 17177148; 17213842; 17255955; 17328074; 17498560; 17516545; 17617740; 17703412; 17852336; 17869652; 17918184; 17924060; 17942705; 17947510; 17970693; 17985330; 18035482; 18079498; 18084608; 18200030; 18216101; 18316378; 18338947; 18381204; 18401423; 18454680; 18641303; 18655181; 18676680; 18678606; 18688264; 18694960; 18986693; 19012493; 19028144; 19056926; 19129219; 19131452; 19145247; 19170196; 19247692; 19258923; 19295429; 19345417; 19404407; 19426920; 19428110; 19433065; 19450680; 19463200; 19482358; 19502235; 19536153; 19548631; 19574175; 19593445; 19625176; 19642896; 19692168; 19697121; 19805480; 19845895; 19851330; 19858727; 19880820; 20031576; 20031577; 20177805; 20177960; 20211142; 20435892; 20457620; 20459687; 20485362; 20503287; 20525893; 20533260; 20588308; 20817723; 20846942; 20861350; 20947504; 20980339; 21102463; 21200019; 21245151; 21257209; 21288140; 21300955; 21389130; 21411754; 21586271; 21683060; 21725055; 21740303; 21790247; 21803131; 21834067; 21903422; 21988832; 22096509; 22139419; 22213332; 22345458; 22367195; 22401175; 22874466; 22879909; 23040881; 23046934; 23071666; 23128233; 23134341; 23226549; 23255602; 23378427; 23487038; 23554911; 23729439; 23746807; 23799084; 23807161; 23811275; 23934855; 23969696 interferon regulatory factor 1 Ensembl:ENSG00000125347 HGNC:6116 HPRD:00961 MIM:147575 Vega:OTTHUMG00000059497 Other designations: interferon regulatory factor 1 isoform d78 IRF1 OGG:3000003661 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene IRF3 interferon regulatory factor 3 3661 19q13.3-q13.4 20140408 9606 19 protein-coding Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0002224 (EC: TAS); GO_0002756 (EC: TAS); GO_0003677 (EC: NAS, PMID: 12062447); GO_0003700 (EC: IEA); GO_0003712 (EC: TAS, PMID: 8524823); GO_0005515 (EC: IPI, PMID: 15841462); GO_0005634 (EC: IDA, PMID: 17079289); GO_0005654 (EC: TAS); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006366 (EC: TAS, PMID: 8524823); GO_0006915 (EC: TAS); GO_0006974 (EC: TAS, PMID: 16979567); GO_0016032 (EC: IEA); GO_0019221 (EC: TAS); GO_0031663 (EC: IEA); GO_0032480 (EC: TAS); GO_0032481 (EC: TAS); GO_0032727 (EC: ISS); GO_0032728 (EC: ISS); GO_0032728 (EC: TAS, PMID: 16979567); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0035666 (EC: TAS); GO_0039530 (EC: TAS, PMID: 16979567); GO_0042802 (EC: IPI, PMID: 15841462); GO_0042803 (EC: IPI, PMID: 12062447); GO_0043123 (EC: IEA); GO_0043330 (EC: IEA); GO_0044212 (EC: IEA); GO_0045087 (EC: TAS); GO_0045351 (EC: IEA); GO_0045358 (EC: IEA); GO_0050689 (EC: IEA); GO_0050715 (EC: IEA); GO_0051607 (EC: ISS); GO_0060333 (EC: TAS); GO_0060337 (EC: TAS); GO_0060340 (EC: IEA); GO_0071359 (EC: IEA); GO_0071888 (EC: TAS, PMID: 16846591) PMID: 8524823; 9463386; 9488451; 9566918; 9649509; 9660935; 9803267; 9865487; 10082512; 10492399; 10521456; 10805757; 10920266; 11035028; 11124948; 11162841; 11303025; 11314014; 11724783; 11846977; 11884139; 11907205; 11940575; 11972054; 12062447; 12138184; 12354379; 12473110; 12477932; 12524442; 12582166; 12604599; 12692549; 12702806; 12829834; 12829839; 12883638; 14517278; 14555995; 14555996; 14557267; 14668346; 14702039; 14703513; 14729983; 14739303; 14747533; 14747536; 14982987; 15107417; 15220448; 15251447; 15276183; 15303122; 15315758; 15342556; 15452220; 15489334; 15502848; 15510218; 15582653; 15695821; 15761153; 15764595; 15767394; 15841462; 15919920; 15955070; 16143103; 16153868; 16154084; 16182584; 16189514; 16199137; 16301520; 16344560; 16362036; 16394098; 16501100; 16513254; 16537515; 16585524; 16699525; 16846591; 16940530; 16979567; 16984921; 16988763; 17015689; 17079289; 17079482; 17121613; 17126870; 17138826; 17142768; 17182689; 17215277; 17251580; 17296604; 17328045; 17393359; 17449641; 17526488; 17540767; 17560375; 17599067; 17608743; 17626075; 17641046; 17652396; 17703412; 17761676; 17823124; 18029348; 18082865; 18203148; 18216110; 18252870; 18272195; 18272581; 18362887; 18440553; 18450748; 18539711; 18579584; 18635538; 18636086; 18641315; 18676680; 18711448; 18713996; 18781139; 18818105; 18927075; 19012493; 19017982; 19028691; 19038458; 19124752; 19152337; 19153595; 19170196; 19201840; 19211751; 19213861; 19239434; 19258923; 19265157; 19349300; 19380831; 19426920; 19434718; 19445677; 19454348; 19515829; 19553679; 19625176; 19646728; 19656901; 19692168; 19701189; 19706707; 19710021; 19826915; 19854139; 19858727; 19890046; 19893624; 19913121; 19955181; 19956647; 20048147; 20048166; 20154210; 20211142; 20308324; 20331378; 20351107; 20360684; 20380698; 20380700; 20381110; 20418377; 20454685; 20483755; 20485298; 20501320; 20503287; 20511230; 20581830; 20604809; 20628086; 20628368; 20631144; 20711230; 20826620; 20886096; 20933442; 20980500; 21079688; 21084468; 21084487; 21120614; 21182093; 21200386; 21225257; 21228327; 21245146; 21248248; 21281747; 21347389; 21411754; 21419663; 21468605; 21497908; 21632562; 21698224; 21768204; 21782231; 21816816; 21835786; 21859832; 21886773; 21890473; 21903422; 21906983; 21931555; 21935451; 21940674; 21988832; 22027828; 22028379; 22072751; 22079989; 22114345; 22127978; 22158869; 22170100; 22208359; 22294846; 22307793; 22388039; 22394560; 22394562; 22479513; 22588174; 22593165; 22647704; 22705311; 22709905; 22745372; 22843696; 22906770; 22908223; 23027953; 23028469; 23077293; 23122814; 23154183; 23281696; 23303668; 23478265; 23512614; 23532851; 23552418; 23596302; 23649622; 23650567; 23824799; 23846693; 23951545; 23994473; 24049179; 24250222; 24275658 interferon regulatory factor 3 IRF3 OGG:3000003665 Bin Zhao, Yue Liu, Oliver He IRF-7H IRF7A IRF7B IRF7C IRF7H WEB: http://www.ncbi.nlm.nih.gov/gene IRF7 interferon regulatory factor 7 3665 11p15.5 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0000122 (EC: TAS, PMID: 9315633); GO_0000979 (EC: IDA, PMID: 17404045); GO_0000982 (EC: IDA, PMID: 17404045); GO_0002224 (EC: TAS); GO_0002756 (EC: TAS); GO_0002819 (EC: IDA, PMID: 17404045); GO_0003677 (EC: IMP, PMID: 12374802); GO_0005515 (EC: IPI, PMID: 11943871); GO_0005634 (EC: TAS, PMID: 9786932); GO_0005654 (EC: TAS); GO_0005737 (EC: TAS, PMID: 9786932); GO_0005829 (EC: TAS); GO_0006366 (EC: TAS, PMID: 9315633); GO_0006974 (EC: TAS, PMID: 16979567); GO_0009615 (EC: TAS); GO_0010008 (EC: TAS); GO_0016064 (EC: IEA); GO_0019043 (EC: TAS); GO_0019221 (EC: TAS); GO_0032479 (EC: TAS); GO_0032481 (EC: TAS); GO_0032607 (EC: ISS); GO_0032608 (EC: ISS); GO_0032727 (EC: IDA, PMID: 16127453); GO_0032727 (EC: TAS, PMID: 16979567); GO_0032728 (EC: TAS, PMID: 16979567); GO_0034124 (EC: ISS); GO_0034127 (EC: ISS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034162 (EC: TAS); GO_0035666 (EC: TAS); GO_0039530 (EC: TAS, PMID: 16979567); GO_0045087 (EC: TAS, PMID: 17404045); GO_0045351 (EC: IEA); GO_0045655 (EC: TAS); GO_0045893 (EC: IMP, PMID: 12374802); GO_0045944 (EC: IDA, PMID: 16127453); GO_0050776 (EC: TAS); GO_0060333 (EC: TAS); GO_0060337 (EC: TAS); GO_0060340 (EC: IEA); GO_2000110 (EC: TAS) PMID: 9315633; 9660935; 9786932; 9865487; 10924517; 11031102; 11073981; 11124948; 11162841; 11314014; 11846980; 11877397; 11884139; 11943871; 12374802; 12477932; 12539042; 12604599; 12692549; 12915551; 14517278; 14729983; 14739303; 14747533; 14759258; 14968112; 15251447; 15265881; 15276183; 15308637; 15361868; 15664159; 15664995; 15695821; 15767370; 16127453; 16153868; 16237059; 16341674; 16344560; 16484229; 16778376; 16979567; 17079482; 17121613; 17374731; 17393359; 17404045; 17522209; 17599067; 17823124; 18227218; 18397234; 18505922; 18539711; 18635538; 18641315; 18710948; 18922877; 18987133; 19017798; 19152337; 19285439; 19349300; 19404407; 19426920; 19515829; 19858727; 19880818; 20112359; 20154210; 20209099; 20331378; 20381110; 20392859; 20467438; 20483755; 20581830; 20588308; 20628624; 20668674; 20689596; 20810735; 20844090; 20943654; 20962850; 20980251; 20980500; 21084487; 21167895; 21183682; 21360504; 21435390; 21632682; 21890473; 21903422; 21906983; 21926187; 21931555; 21940674; 21988832; 22095711; 22112518; 22140520; 22194884; 22301143; 22433914; 22455868; 22505724; 22588174; 22709905; 22787218; 22820642; 23175366; 23490285; 23535064; 23740937; 23846693; 23956435; 24275658 interferon regulatory factor 7 Ensembl:ENSG00000185507 HGNC:6122 HPRD:05441 MIM:605047 Vega:OTTHUMG00000132019 Other designations: IRF-7|interferon regulatory factor-7H IRF7 OGG:3000003669 Bin Zhao, Yue Liu, Oliver He CD25 HEM45 WEB: http://www.ncbi.nlm.nih.gov/gene ISG20 interferon stimulated exonuclease gene 20kDa 3669 15q26 20140408 9606 15 protein-coding Official from a nomenclature committee GO_0000175 (EC: IDA, PMID: 11401564); GO_0000738 (EC: IDA, PMID: 11401564); GO_0004527 (EC: IMP); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, PMID: 16514659); GO_0005737 (EC: IDA, PMID: 16514659); GO_0006364 (EC: IEA); GO_0006401 (EC: IDA, PMID: 11401564); GO_0008283 (EC: TAS, PMID: 9569007); GO_0008310 (EC: IDA, PMID: 11401564); GO_0008859 (EC: IEA); GO_0009615 (EC: IDA, PMID: 12594219); GO_0015030 (EC: IDA, PMID: 16514659); GO_0016605 (EC: IDA, PMID: 9235947); GO_0019221 (EC: TAS); GO_0030619 (EC: IDA, PMID: 16514659); GO_0030620 (EC: IDA, PMID: 16514659); GO_0034511 (EC: IDA, PMID: 16514659); GO_0045071 (EC: IMP); GO_0046872 (EC: IEA); GO_0051607 (EC: IMP); GO_0060337 (EC: TAS); GO_0090503 (EC: IDA, PMID: 11401564) PMID: 9235947; 9569007; 9605874; 11401564; 12477932; 12539042; 12594219; 14702039; 15489334; 15527770; 16514659; 18278447; 21036379; 21732829; 21963094; 22647704; 23251661; 23830076 interferon stimulated exonuclease gene 20kDa HGNC:6130 HPRD:05169 MIM:604533 ISG20 OGG:3000003688 Bin Zhao, Yue Liu, Oliver He CD29 FNRB GPIIA MDF2 MSK12 VLA-BETA VLAB WEB: http://www.ncbi.nlm.nih.gov/gene ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12) 3688 RP11-479G22.2 10p11.2 9606 10 Official from a nomenclature committee GO_0000082 (EC: IEA); GO_0001618 (EC: IEA); GO_0001669 (EC: IEA); GO_0001701 (EC: IEA); GO_0001708 (EC: IEA); GO_0001726 (EC: TAS, PMID: 11919189); GO_0001894 (EC: IEA); GO_0001948 (EC: IEA); GO_0001968 (EC: IEA); GO_0002020 (EC: IEA); GO_0002042 (EC: IEA); GO_0003779 (EC: IDA, PMID: 16803572); GO_0005178 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10604475); GO_0005518 (EC: IEA); GO_0005604 (EC: IEA); GO_0005737 (EC: IDA, PMID: 16803572); GO_0005886 (EC: IDA, PMID: 12869515); GO_0005886 (EC: TAS); GO_0005925 (EC: IDA, PMID: 12417594); GO_0005925 (EC: IDA, Qualifier: colocalizes_with, PMID: 14970227); GO_0006874 (EC: IEA); GO_0006968 (EC: TAS, PMID: 10201960); GO_0007156 (EC: TAS, PMID: 10201960); GO_0007159 (EC: IDA, PMID: 1715889); GO_0007160 (EC: IMP, PMID: 18156211); GO_0007161 (EC: IGI, PMID: 19651211); GO_0007229 (EC: IEA); GO_0007411 (EC: TAS); GO_0007596 (EC: TAS); GO_0008277 (EC: IEA); GO_0008284 (EC: IEA); GO_0008285 (EC: IEA); GO_0008305 (EC: NAS, PMID: 9552005); GO_0008354 (EC: IEA); GO_0009897 (EC: IEA); GO_0009986 (EC: IDA, PMID: 1715889); GO_0010811 (EC: IEA); GO_0010976 (EC: IEA); GO_0014704 (EC: IEA); GO_0014823 (EC: IEA); GO_0016032 (EC: IEA); GO_0016477 (EC: TAS, PMID: 11919189); GO_0019901 (EC: IEA); GO_0019904 (EC: IEA); GO_0021943 (EC: IEA); GO_0030027 (EC: IEA); GO_0030056 (EC: IEA); GO_0030175 (EC: IDA, PMID: 16803572); GO_0030183 (EC: IC, PMID: 1715889); GO_0030198 (EC: TAS); GO_0030335 (EC: IEA); GO_0031345 (EC: IEA); GO_0031594 (EC: IDA, PMID: 9415431); GO_0032154 (EC: IEA); GO_0032587 (EC: IDA, Qualifier: colocalizes_with, PMID: 14970227); GO_0032594 (EC: IEA); GO_0033631 (EC: IEP, PMID: 17704059); GO_0034329 (EC: TAS); GO_0034667 (EC: IEA); GO_0034677 (EC: IEA); GO_0034678 (EC: TAS); GO_0034679 (EC: IEA); GO_0034698 (EC: IEA); GO_0035748 (EC: IEA); GO_0042277 (EC: IEA); GO_0042383 (EC: IDA, PMID: 9415431); GO_0042470 (EC: IEA); GO_0042493 (EC: IEA); GO_0043065 (EC: IGI, PMID: 19364818); GO_0043235 (EC: IDA); GO_0043236 (EC: IEA); GO_0043410 (EC: IEA); GO_0045121 (EC: IDA, PMID: 14559243); GO_0045214 (EC: IEA); GO_0045665 (EC: IEA); GO_0045666 (EC: IEA); GO_0045807 (EC: IEA); GO_0046872 (EC: IEA); GO_0046982 (EC: NAS, PMID: 9552005); GO_0050731 (EC: IEA); GO_0050776 (EC: TAS); GO_0050839 (EC: IPI, PMID: 12869515); GO_0050900 (EC: TAS); GO_0051393 (EC: IEA); GO_0051726 (EC: IEA); GO_0055007 (EC: IEA); GO_0055037 (EC: IEA); GO_0060135 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0070830 (EC: IEA); GO_0071260 (EC: IEA); GO_0071305 (EC: IEA); GO_0071479 (EC: IEA); GO_0071559 (EC: IEA); GO_2000811 (EC: IMP, PMID: 15006356) PMID: 1551917; 1690718; 1693624; 1715889; 2116421; 2138612; 2156854; 2202737; 2249781; 2524991; 2527614; 2572537; 2649503; 2958481; 2967289; 3546305; 7504269; 7523423; 7539135; 7541634; 7544298; 7545396; 7559467; 7657702; 7681433; 7690138; 7768999; 8120056; 8163531; 8245132; 8387021; 8428973; 8444890; 8537347; 8538749; 8567725; 8630057; 8649427; 8757325; 8757349; 8757599; 8798654; 8831898; 8838570; 8889548; 9117345; 9281591; 9281592; 9295027; 9360995; 9360996; 9415431; 9425259; 9431988; 9442085; 9494094; 9501082; 9517988; 9547293; 9552005; 9565552; 9614184; 9645947; 9660880; 9685391; 9686320; 9688542; 9722563; 9736715; 9812906; 9813091; 9889149; 9914169; 9916748; 10065872; 10201960; 10209034; 10229664; 10388537; 10397731; 10397733; 10459022; 10464311; 10486209; 10506186; 10593924; 10604475; 10613898; 10623819; 10673366; 10676904; 10684262; 10694273; 10734060; 10741407; 10778855; 10804218; 10811835; 10852818; 10906324; 10944199; 10944520; 10982388; 11010812; 11054877; 11076863; 11149921; 11208159; 11230166; 11238109; 11256614; 11278628; 11278916; 11279249; 11309411; 11313964; 11358957; 11387256; 11435317; 11462216; 11507094; 11553610; 11668187; 11716783; 11728829; 11741908; 11751905; 11775028; 11776052; 11779688; 11805102; 11807098; 11861761; 11882657; 11884516; 11884618; 11888933; 11893752; 11907260; 11909975; 11914080; 11918217; 11919189; 11931654; 11932920; 11934885; 11941451; 11964076; 11967148; 11980922; 11981820; 11989791; 11996105; 11997396; 12020426; 12054567; 12070135; 12091396; 12097820; 12118253; 12138200; 12138201; 12140560; 12163503; 12171996; 12174366; 12175627; 12181350; 12181354; 12200131; 12209735; 12218055; 12221126; 12364323; 12372334; 12372459; 12376466; 12392763; 12393420; 12397374; 12397575; 12411441; 12417594; 12427871; 12435334; 12445830; 12456677; 12477932; 12480921; 12486108; 12496264; 12500944; 12509413; 12514714; 12517798; 12574205; 12578911; 12595495; 12606711; 12637511; 12639940; 12639965; 12662928; 12681287; 12682293; 12694355; 12695522; 12699087; 12788934; 12791669; 12799374; 12803239; 12807887; 12826661; 12844491; 12865438; 12869515; 12871973; 12883474; 12893184; 12893831; 12904899; 12907437; 12909644; 12915563; 12918102; 12919677; 12931024; 12941630; 12947314; 12954625; 12969374; 12970173; 14502569; 14512423; 14522909; 14525968; 14532964; 14550305; 14559243; 14559906; 14562042; 14563646; 14602071; 14607975; 14610084; 14612440; 14612932; 14623330; 14633626; 14645603; 14662754; 14666169; 14671618; 14675422; 14676841; 14679206; 14681217; 14699013; 14699139; 14722085; 14766759; 14963009; 14970227; 14983010; 14998999; 15006356; 15024036; 15070678; 15090462; 15100006; 15117962; 15156152; 15158122; 15166232; 15171717; 15181153; 15226304; 15231747; 15240572; 15247268; 15254262; 15256055; 15265786; 15276495; 15276642; 15280429; 15292185; 15292257; 15302884; 15304053; 15389531; 15466867; 15485856; 15489336; 15500293; 15507484; 15509657; 15514009; 15522237; 15539082; 15567743; 15572366; 15583842; 15590642; 15611085; 15633218; 15645131; 15647274; 15647827; 15677332; 15677455; 15684035; 15699160; 15713743; 15713750; 15723043; 15731179; 15737747; 15757908; 15777792; 15795318; 15805105; 15872091; 15878864; 15881415; 15905178; 15919367; 15947241; 15949469; 15961545; 15978109; 15978110; 15983209; 15987639; 16002725; 16005200; 16043429; 16055535; 16055706; 16076904; 16099422; 16103120; 16105875; 16113793; 16148152; 16157583; 16195423; 16213489; 16228294; 16247454; 16258728; 16275327; 16301336; 16326706; 16335952; 16341674; 16344560; 16357324; 16363250; 16365170; 16373174; 16381901; 16385340; 16385451; 16390868; 16415171; 16421008; 16430945; 16448724; 16457822; 16459165; 16501085; 16504015; 16510444; 16537545; 16547007; 16547500; 16569430; 16705158; 16707493; 16731529; 16732726; 16754661; 16754960; 16762342; 16773720; 16803572; 16807379; 16820945; 16878156; 16882656; 16908668; 16908762; 16916750; 16920931; 16940508; 16972245; 16984420; 17012251; 17015707; 17060328; 17081065; 17110618; 17116465; 17141917; 17170699; 17186162; 17286276; 17300927; 17311314; 17312461; 17318179; 17331499; 17352405; 17371832; 17380111; 17407140; 17408410; 17469136; 17481915; 17490870; 17498594; 17514628; 17515951; 17521731; 17530710; 17538005; 17560548; 17573778; 17597073; 17603494; 17609118; 17630833; 17634906; 17638891; 17664272; 17671519; 17704059; 17706641; 17726369; 17760843; 17868650; 17888902; 17899316; 17901052; 17960115; 17968567; 17991734; 17997226; 18026855; 18032709; 18037995; 18048360; 18048918; 18054915; 18057877; 18155697; 18156211; 18186923; 18230652; 18243286; 18250451; 18310319; 18322799; 18326820; 18341635; 18356158; 18375753; 18378436; 18383324; 18413316; 18425328; 18425341; 18445685; 18448666; 18462748; 18477477; 18491034; 18492066; 18499669; 18501656; 18512729; 18519809; 18549800; 18554474; 18567578; 18577581; 18583538; 18587047; 18611961; 18613064; 18614994; 18615555; 18632734; 18635536; 18644869; 18648521; 18676377; 18676743; 18687805; 18695939; 18707587; 18727519; 18755811; 18760454; 18787945; 18794852; 18820259; 18826391; 18844239; 18845630; 18846341; 18850009; 18940913; 18945876; 18947333; 18957620; 18973153; 18983487; 18984674; 18990704; 18992284; 19005162; 19020712; 19026687; 19056867; 19057841; 19064571; 19064666; 19073896; 19074826; 19087624; 19115199; 19123990; 19130304; 19164533; 19168626; 19169646; 19170051; 19176753; 19179533; 19190332; 19228923; 19240021; 19250636; 19261610; 19297531; 19297850; 19307303; 19322201; 19323811; 19342381; 19346516; 19350017; 19359599; 19364818; 19395705; 19397781; 19404550; 19411307; 19416892; 19434537; 19435806; 19448673; 19454674; 19458194; 19467326; 19469865; 19478484; 19502598; 19516006; 19527220; 19527712; 19564406; 19574430; 19579970; 19608669; 19617714; 19622836; 19641149; 19646550; 19651211; 19670701; 19679609; 19700757; 19710103; 19714342; 19717562; 19724904; 19725119; 19738201; 19747169; 19752234; 19755493; 19768654; 19775453; 19776755; 19780039; 19796635; 19811096; 19815047; 19822142; 19847290; 19850917; 19885568; 19887442; 19887601; 19889638; 19913121; 19927126; 19930715; 19940135; 19960514; 19995941; 20007695; 20051050; 20063417; 20063990; 20075392; 20127017; 20133364; 20145038; 20171211; 20178602; 20183869; 20213106; 20231384; 20232313; 20236590; 20237496; 20237901; 20333644; 20336352; 20337027; 20351310; 20352103; 20352300; 20362630; 20388801; 20407016; 20427540; 20432448; 20435742; 20472470; 20485444; 20510000; 20522645; 20531279; 20565758; 20598296; 20607601; 20613771; 20616308; 20624912; 20628086; 20628624; 20634879; 20639577; 20643357; 20650890; 20650901; 20660204; 20661303; 20678483; 20686611; 20693403; 20713715; 20714794; 20723423; 20725651; 20800221; 20802515; 20811680; 20826546; 20869114; 20877569; 20889506; 20947017; 21045155; 21048156; 21053345; 21067603; 21071450; 21112327; 21114537; 21119363; 21119598; 21134100; 21134644; 21135504; 21139048; 21149578; 21170718; 21178109; 21195710; 21217148; 21255062; 21298552; 21302295; 21320503; 21321939; 21325030; 21341269; 21344385; 21357540; 21359179; 21359644; 21363926; 21374738; 21400218; 21406228; 21426305; 21429937; 21441381; 21471204; 21474814; 21478906; 21501586; 21521694; 21524887; 21558392; 21567400; 21606500; 21613543; 21618249; 21630092; 21639857; 21642953; 21647271; 21652699; 21658756; 21691075; 21701559; 21705617; 21732280; 21747167; 21762625; 21772312; 21784851; 21787362; 21799154; 21850018; 21876768; 21890473; 21906983; 21947080; 21951552; 21961047; 21963094; 21967109; 21987572; 21988832; 22002573; 22015659; 22027826; 22045736; 22100988; 22114305; 22130661; 22136719; 22151306; 22160595; 22232555; 22241990; 22247553; 22266309; 22268729; 22287577; 22298882; 22304920; 22345562; 22349830; 22353524; 22361176; 22370635; 22374686; 22378044; 22378065; 22382453; 22384145; 22386417; 22388103; 22389402; 22396498; 22402981; 22422622; 22423313; 22449099; 22451694; 22454518; 22461623; 22472442; 22496232; 22505724; 22562249; 22590584; 22613833; 22614033; 22627583; 22648170; 22648415; 22711564; 22721769; 22723286; 22734003; 22735632; 22740085; 22829201; 22843693; 22863953; 22865233; 22869523; 22894137; 22898815; 22917688; 22936677; 22939629; 22940691; 22949126; 22986527; 22999999; 23000965; 23007402; 23023061; 23069938; 23074279; 23118221; 23125415; 23132859; 23139422; 23148235; 23160057; 23204528; 23208492; 23238518; 23242739; 23248240; 23284715; 23284937; 23289672; 23317506; 23359252; 23416109; 23436775; 23441154; 23444218; 23455756; 23482612; 23522389; 23532895; 23536555; 23541832; 23552693; 23558678; 23576567; 23590307; 23595626; 23613949; 23642664; 23664187; 23665237; 23677397; 23687274; 23704882; 23709605; 23762436; 23857544; 23884246; 23889963; 23936390; 23938462; 24056178; 24091324; 24135056; 24239175; 24244022; 24311785; 24455846; 24510996 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12) Ensembl:ENSG00000150093 HGNC:6153 HPRD:00628 MIM:135630 Vega:OTTHUMG00000017928 Other designations: glycoprotein IIa|integrin VLA-4 beta subunit|integrin beta-1|very late activation protein, beta polypeptide ITGB1 OGG:3000003690 Bin Zhao, Yue Liu, Oliver He BDPLT16 BDPLT2 CD61 GP3A GPIIIa GT WEB: http://www.ncbi.nlm.nih.gov/gene ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61) 3690 17q21.32 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0001934 (EC: TAS, PMID: 19267251); GO_0001938 (EC: IMP, PMID: 10022831); GO_0002576 (EC: TAS); GO_0003756 (EC: IDA, PMID: 12204115); GO_0004872 (EC: IEA); GO_0005161 (EC: TAS, PMID: 19267251); GO_0005515 (EC: IPI, PMID: 10822899); GO_0005634 (EC: IDA); GO_0005886 (EC: IDA, PMID: 15466936); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 2452834); GO_0005925 (EC: IEA); GO_0006457 (EC: IDA, PMID: 12204115); GO_0007044 (EC: IEA); GO_0007155 (EC: TAS, PMID: 10429193); GO_0007160 (EC: IEA); GO_0007229 (EC: TAS); GO_0007411 (EC: TAS); GO_0007596 (EC: TAS); GO_0008305 (EC: IDA, PMID: 15215180); GO_0010595 (EC: IMP, PMID: 10022831); GO_0010745 (EC: IMP, PMID: 15215180); GO_0010888 (EC: IMP, PMID: 15215180); GO_0014909 (EC: IMP, PMID: 8837777); GO_0016032 (EC: IEA); GO_0030168 (EC: IMP, PMID: 15466936); GO_0030168 (EC: TAS); GO_0030198 (EC: TAS); GO_0030949 (EC: TAS, PMID: 19267251); GO_0031092 (EC: TAS); GO_0031258 (EC: IEA); GO_0032147 (EC: IMP, PMID: 10022831); GO_0032369 (EC: IMP, PMID: 15215180); GO_0035295 (EC: TAS, PMID: 19267251); GO_0042060 (EC: IC, PMID: 8837777); GO_0042470 (EC: IDA, PMID: 15466936); GO_0042802 (EC: IPI, PMID: 11606749); GO_0043184 (EC: IPI, PMID: 10022831); GO_0043184 (EC: TAS, PMID: 19267251); GO_0043235 (EC: IDA); GO_0045124 (EC: TAS, PMID: 19267251); GO_0045715 (EC: IMP, PMID: 15215180); GO_0050731 (EC: IMP, PMID: 10022831); GO_0050748 (EC: IMP, PMID: 15215180); GO_0050839 (EC: IPI, PMID: 8837777); GO_0050900 (EC: TAS); GO_0060055 (EC: TAS, PMID: 19267251); GO_0070062 (EC: IDA); GO_0070527 (EC: IMP, PMID: 15466936); GO_0071062 (EC: TAS, PMID: 19267251) PMID: 1371279; 1382574; 1429573; 1430225; 1438206; 1549507; 1602006; 1693624; 1693626; 1694173; 1953640; 1967954; 2001252; 2010551; 2138612; 2145280; 2202737; 2341395; 2345548; 2392682; 2452834; 2454952; 2478219; 2565345; 2787511; 3165296; 3494014; 3607284; 3801670; 3828395; 7505120; 7532190; 7539135; 7592818; 7593198; 7682219; 7690138; 7694683; 7878622; 8093349; 8132570; 8132607; 8198553; 8244378; 8298129; 8387021; 8400294; 8467233; 8631894; 8649427; 8663236; 8757599; 8781422; 8798654; 8831898; 8837777; 9030514; 9169439; 9195946; 9215749; 9256940; 9376589; 9517988; 9684783; 9686320; 9790984; 9916748; 10022831; 10037797; 10233432; 10391209; 10397733; 10429193; 10438928; 10497223; 10605720; 10640428; 10684262; 10747940; 10749942; 10822899; 10835423; 10837460; 10848816; 10896934; 10964917; 10964931; 10982404; 11028489; 11042121; 11053714; 11151063; 11235724; 11238109; 11257275; 11279932; 11331301; 11341749; 11397354; 11447076; 11454259; 11460491; 11470407; 11533523; 11545752; 11546839; 11568114; 11577104; 11583324; 11588040; 11606749; 11683411; 11686325; 11704375; 11714857; 11723131; 11739968; 11776310; 11807098; 11812069; 11812775; 11858476; 11858493; 11864709; 11867691; 11875117; 11877390; 11884718; 11891802; 11897046; 11927607; 11932255; 11934894; 11940607; 11953315; 11959660; 11962738; 11994301; 12008962; 12031826; 12036875; 12038797; 12049640; 12071877; 12073410; 12082590; 12082592; 12083483; 12140290; 12152649; 12152651; 12161360; 12168086; 12198771; 12200372; 12204115; 12209993; 12210725; 12218055; 12237112; 12237321; 12297512; 12353082; 12358597; 12362250; 12364323; 12370491; 12372433; 12372469; 12372811; 12393510; 12399420; 12426312; 12427871; 12460991; 12477932; 12486108; 12499711; 12511588; 12514663; 12518110; 12535520; 12553378; 12578602; 12586134; 12606711; 12609844; 12637342; 12639965; 12645863; 12660257; 12665801; 12668663; 12682293; 12690117; 12690916; 12691260; 12694355; 12714203; 12716314; 12719784; 12720308; 12730600; 12736272; 12738509; 12750158; 12765524; 12771130; 12791034; 12799374; 12807887; 12818249; 12818251; 12826159; 12827240; 12855229; 12871468; 12871600; 12874388; 12899665; 12902444; 12902636; 12911597; 12932598; 12941045; 12952967; 12957761; 13678940; 14499914; 14517343; 14521607; 14524530; 14525764; 14557872; 14593208; 14614355; 14629479; 14634961; 14669168; 14675395; 14681217; 14681220; 14690453; 14691438; 14691579; 14746139; 14963009; 14963283; 14966135; 14987913; 14992889; 15044441; 15045135; 15056669; 15067009; 15076187; 15131115; 15134555; 15147527; 15156152; 15166241; 15166939; 15166947; 15166949; 15178823; 15187087; 15215180; 15219201; 15226180; 15227729; 15299032; 15331787; 15344881; 15355503; 15355504; 15456946; 15466936; 15468167; 15489334; 15509546; 15546585; 15564935; 15565371; 15575508; 15583747; 15590407; 15609125; 15627799; 15634267; 15638730; 15663601; 15676177; 15695828; 15699036; 15701653; 15701721; 15705408; 15730528; 15748237; 15795319; 15817799; 15826939; 15834425; 15834589; 15840736; 15842360; 15847651; 15863506; 15886806; 15890274; 15897908; 15917997; 15921657; 15968394; 15970922; 15976180; 15978110; 15990752; 15998788; 16005200; 16005629; 16035619; 16051597; 16051604; 16091654; 16100725; 16102042; 16105876; 16113799; 16115959; 16133898; 16150802; 16153930; 16157382; 16158739; 16166568; 16195248; 16213489; 16228296; 16248996; 16263699; 16275649; 16307159; 16317099; 16317580; 16322334; 16322781; 16335952; 16339753; 16340127; 16353042; 16357324; 16359515; 16380674; 16385340; 16400188; 16407244; 16412752; 16444441; 16469512; 16504741; 16513293; 16567932; 16573563; 16581250; 16582881; 16634766; 16635210; 16636497; 16675000; 16676352; 16702043; 16716076; 16721604; 16723352; 16724005; 16731529; 16756721; 16790523; 16818691; 16822941; 16831169; 16859511; 16875034; 16877710; 16879215; 16895913; 16905953; 16933105; 16935858; 16969099; 17032655; 17034033; 17074516; 17092301; 17111197; 17127487; 17138951; 17146626; 17158881; 17160992; 17175151; 17192395; 17196570; 17203213; 17203304; 17206538; 17218263; 17220212; 17230042; 17258347; 17264806; 17272505; 17278970; 17290027; 17320454; 17332246; 17334320; 17337041; 17346829; 17357883; 17369840; 17376438; 17406648; 17414216; 17432927; 17439948; 17446174; 17468108; 17482311; 17483236; 17515951; 17538005; 17550972; 17556058; 17559347; 17561290; 17607710; 17615290; 17621633; 17630485; 17635696; 17641225; 17642204; 17644514; 17665449; 17679464; 17681328; 17714854; 17728329; 17763154; 17827388; 17854909; 17855352; 17907177; 17912026; 17928472; 17954176; 17957566; 17959856; 18021403; 18031296; 18035074; 18041653; 18045240; 18045606; 18045938; 18051367; 18056258; 18057877; 18062611; 18064323; 18065693; 18067652; 18084301; 18088350; 18156175; 18160561; 18160589; 18162078; 18174155; 18175315; 18191725; 18200665; 18201749; 18208809; 18211801; 18214290; 18230083; 18237139; 18247041; 18260892; 18310319; 18310446; 18312855; 18316775; 18317590; 18321071; 18331351; 18331836; 18334487; 18343248; 18345483; 18353318; 18353785; 18364349; 18375753; 18383324; 18396070; 18399841; 18405917; 18419255; 18433460; 18441324; 18458155; 18484951; 18503143; 18512729; 18513389; 18516040; 18549690; 18550570; 18573917; 18577523; 18635536; 18638089; 18641368; 18648521; 18657307; 18665040; 18673340; 18674955; 18685811; 18709641; 18712091; 18728123; 18791937; 18796633; 18803625; 18814143; 18821851; 18824633; 18826388; 18832906; 18836720; 18836731; 18841997; 18854176; 18927433; 18927546; 18930220; 18936436; 18974842; 18978678; 18979363; 18989530; 19001202; 19008959; 19017937; 19018779; 19019827; 19037107; 19038456; 19061491; 19071013; 19072566; 19074851; 19104837; 19106083; 19110485; 19117493; 19118033; 19118218; 19123042; 19131662; 19132198; 19141530; 19184277; 19197137; 19205270; 19207108; 19212436; 19212638; 19230252; 19232685; 19235843; 19238444; 19245802; 19255147; 19262211; 19263529; 19264973; 19267251; 19279667; 19286442; 19329429; 19334037; 19336355; 19336370; 19336737; 19345676; 19350519; 19350618; 19361361; 19366731; 19368146; 19371633; 19374152; 19388931; 19390575; 19395327; 19461049; 19463111; 19463119; 19469865; 19475568; 19487690; 19515580; 19526385; 19527712; 19527732; 19530321; 19541645; 19546854; 19559392; 19562259; 19570064; 19573311; 19588468; 19604247; 19617625; 19630800; 19633306; 19635510; 19637098; 19654300; 19656390; 19670701; 19691478; 19695571; 19702628; 19704023; 19729601; 19730003; 19740098; 19751734; 19765213; 19778317; 19789190; 19804783; 19805198; 19808093; 19808644; 19815712; 19816083; 19821948; 19824427; 19837659; 19860767; 19863457; 19876733; 19882657; 19888429; 19889638; 19903699; 19906129; 19913121; 19923980; 19934566; 19948007; 19956635; 19959486; 19996122; 20002543; 20020534; 20033473; 20048261; 20075254; 20076847; 20078877; 20106508; 20138334; 20149160; 20161734; 20162297; 20181715; 20192979; 20204402; 20230421; 20237496; 20306691; 20308600; 20339539; 20363746; 20369606; 20379614; 20406466; 20425806; 20438394; 20452482; 20458832; 20472470; 20477989; 20485444; 20492470; 20519501; 20532885; 20538554; 20546203; 20554778; 20565758; 20584077; 20592457; 20595101; 20600001; 20615878; 20628086; 20634891; 20638909; 20661303; 20667040; 20673868; 20679525; 20691446; 20702409; 20717043; 20739287; 20739877; 20802378; 20819594; 20826760; 20828133; 20837477; 20846430; 20857483; 20873239; 20929856; 20945385; 20978323; 21034162; 21039385; 21044892; 21054877; 21071690; 21080081; 21091771; 21102624; 21109038; 21122545; 21135163; 21143381; 21156831; 21182210; 21190668; 21241403; 21283814; 21325030; 21344378; 21353223; 21508388; 21529934; 21570717; 21590707; 21622897; 21626402; 21645227; 21645497; 21678053; 21764795; 21813062; 21832081; 21917754; 21935711; 21951552; 21966982; 21978494; 22002573; 22015616; 22015659; 22028352; 22078565; 22094875; 22095620; 22102273; 22116617; 22132110; 22136613; 22171266; 22174124; 22174684; 22190468; 22207115; 22268819; 22308022; 22328516; 22362758; 22407444; 22422622; 22448399; 22452684; 22456341; 22457811; 22461623; 22466811; 22484027; 22528484; 22531012; 22538781; 22581054; 22613710; 22641344; 22669259; 22698642; 22730538; 22879933; 22948415; 23003125; 23022044; 23022222; 23119061; 23125415; 23150579; 23161541; 23181508; 23184042; 23197154; 23204516; 23216754; 23234019; 23238957; 23243278; 23243309; 23253071; 23289212; 23300803; 23382103; 23382691; 23384292; 23386126; 23389628; 23451109; 23469002; 23494007; 23519467; 23527123; 23545624; 23571313; 23580774; 23628433; 23640055; 23725446; 23726972; 23744557; 23770013; 23840404; 23845726; 23857544; 23867618; 23929305; 23981581; 24023288; 24030382; 24037888; 24096143; 24109241; 24136164; 24176823; 24437179; 24437181 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61) Ensembl:ENSG00000259207 HGNC:6156 HPRD:01428 MIM:173470 Vega:OTTHUMG00000171956 Other designations: integrin beta-3|platelet membrane glycoprotein IIIa ITGB3 OGG:3000003692 Bin Zhao, Yue Liu, Oliver He CAB EIF3A ITGB4BP b(2)gcn eIF-6 p27(BBP) p27BBP WEB: http://www.ncbi.nlm.nih.gov/gene EIF6 eukaryotic translation initiation factor 6 3692 RP4-614O4.1 20q12 9606 20 GO_0003743 (EC: IEA); GO_0005515 (EC: IPI); GO_0005634 (EC: IDA); GO_0005638 (EC: IEA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IEA); GO_0042256 (EC: IMP); GO_0043022 (EC: IDA); GO_0070062 (EC: IDA, PMID:19056867) PMID:9374518; 9405604; 9653160; 9740680; 10085284; 10348637; 10906324; 11042152; 11290417; 11780052; 11790298; 12477932; 12917340; 14654845; 15122657; 15146197; 15231747; 15489334; 15592455; 15635413; 15946946; 16169070; 16341674; 16530192; 17353931; 17507929; 17569113; 18029348; 18327211; 18391951; 18624398; 18781797; 19056867; 19738201; 20546612; 20585627; 21029697; 21084295; 21139048; 21145461; 21536732; 21832049; 21900206; 21903422; 21963094; 21988832; 22178446; 22295858; 22348144; 22365962; 22415777; 22586326; 22863883; 22939629; 22990118; 23115272; 23752268; 24457600 eukaryotic translation initiation factor 6 Ensembl:ENSG00000242372 HGNC:6159 HPRD:04221 MIM:602912 Vega:OTTHUMG00000032328 Other designations: B4 integrin interactor|eukaryotic translation initiation factor 3A|p27 beta-4 integrin-binding protein EIF6 OGG:3000003716 Bin Zhao, Yue Liu, Oliver He JAK1A JAK1B JTK3 WEB: http://www.ncbi.nlm.nih.gov/gene JAK1 Janus kinase 1 3716 1p32.3-p31.3 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0004713 (EC: EXP); GO_0004713 (EC: TAS); GO_0004715 (EC: IEA); GO_0005131 (EC: ISS, PMID: 10502458); GO_0005515 (EC: IPI, PMID: 16273093); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA, PMID: 10502458); GO_0005737 (EC: IDA, PMID: 10502458); GO_0005829 (EC: TAS); GO_0005856 (EC: IEA); GO_0006468 (EC: TAS, PMID: 1848670); GO_0007167 (EC: IEA); GO_0012505 (EC: IEA); GO_0016020 (EC: IEA); GO_0019221 (EC: TAS); GO_0019903 (EC: IPI, PMID: 11909529); GO_0031730 (EC: IEA); GO_0035556 (EC: IEA); GO_0038110 (EC: IDA, PMID: 11909529); GO_0046677 (EC: IDA, PMID: 16280321); GO_0046777 (EC: IEA); GO_0060333 (EC: TAS); GO_0060334 (EC: TAS); GO_0060337 (EC: TAS); GO_0060338 (EC: TAS) PMID: 1213395; 1373877; 1581631; 1848670; 7499365; 7510216; 7512720; 7543024; 7589562; 7629131; 7657660; 7690989; 7698020; 7759950; 7973658; 7973659; 8041779; 8232552; 8247543; 8272872; 8493579; 8536716; 8609418; 8612580; 8626374; 8647212; 8657151; 8700888; 8702790; 8756628; 8995399; 9020188; 9047382; 9133424; 9178903; 9388212; 9417082; 9446616; 9452495; 9484840; 9492017; 9510175; 9516124; 9520455; 9553136; 9566874; 9597132; 9651359; 9774657; 9774693; 10037796; 10373548; 10433356; 10502458; 10531356; 10586060; 10702271; 10707961; 10777583; 10809230; 10825200; 10856136; 10875931; 10899310; 10918587; 10954736; 10982844; 10993906; 11016959; 11036942; 11133764; 11160325; 11162588; 11163768; 11201744; 11294897; 11350938; 11418623; 11468294; 11527382; 11557047; 11694501; 11722592; 11742534; 11751854; 11751884; 11786531; 11801527; 11839738; 11909529; 11940572; 12089333; 12130510; 12133952; 12163560; 12200137; 12207328; 12223098; 12242343; 12244095; 12374810; 12403768; 12447867; 12456798; 12477932; 12549820; 12551917; 12559972; 12576423; 12620806; 12626508; 12637327; 12734330; 12738762; 12775419; 12777975; 12817007; 12960323; 14551213; 14674010; 14978237; 15063116; 15194700; 15277531; 15284024; 15322115; 15526032; 15588985; 15883164; 15894543; 15923602; 15988755; 15996891; 16102578; 16239216; 16273093; 16280321; 16474838; 16710296; 16767694; 17158029; 17290288; 17353931; 17433443; 17641294; 17686504; 17703412; 17951261; 17982039; 18160671; 18178840; 18187620; 18266209; 18270328; 18271526; 18320073; 18362173; 18390202; 18413761; 18430728; 18559588; 18566411; 18787400; 18787531; 18789440; 18948751; 18976975; 19017763; 19139102; 19167051; 19176360; 19180571; 19239328; 19255588; 19258923; 19434718; 19457567; 19464057; 19470474; 19559055; 19604093; 19730683; 19764985; 19802007; 19887489; 19900094; 19913121; 20052595; 20065083; 20072651; 20103601; 20128689; 20139093; 20167706; 20237496; 20368117; 20379614; 20467438; 20503287; 20588308; 20628086; 20697856; 20868368; 20974963; 20980339; 21048031; 21051030; 21139048; 21151131; 21160051; 21216930; 21220115; 21277633; 21325207; 21420464; 21439476; 21537335; 21551237; 21679692; 21689637; 21827323; 21840487; 21861134; 21880637; 21880948; 21890473; 21903422; 21906983; 21949722; 21963094; 21965659; 21987572; 22084247; 22226123; 22301404; 22368272; 22406175; 22427350; 22505724; 22542455; 22558273; 22661199; 22684105; 22748021; 22844427; 22859983; 22901011; 22939624; 23000965; 23084401; 23184937; 23185365; 23246001; 23402259; 23406773; 23611997; 23674219; 23703473; 23768868; 23818941; 23860541; 23920124; 23941832; 24413661 Janus kinase 1 Ensembl:ENSG00000162434 HGNC:6190 HPRD:00992 MIM:147795 Vega:OTTHUMG00000009310 Other designations: tyrosine-protein kinase JAK1 JAK1 OGG:3000003725 Bin Zhao, Yue Liu, Oliver He AP-1 AP1 c-Jun WEB: http://www.ncbi.nlm.nih.gov/gene JUN jun proto-oncogene 3725 1p32-p31 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0000228 (EC: TAS, PMID: 10918580); GO_0000980 (EC: IDA, PMID: 19861239); GO_0001077 (EC: IEA); GO_0001102 (EC: IPI, PMID: 19861239); GO_0001190 (EC: IC, PMID: 19861239); GO_0001525 (EC: IEA); GO_0001774 (EC: IEA); GO_0001836 (EC: IEA); GO_0001889 (EC: IEA); GO_0001938 (EC: IEA); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0003151 (EC: IEA); GO_0003677 (EC: TAS, PMID: 2825349); GO_0003690 (EC: IEA); GO_0003700 (EC: IDA, PMID: 9732876); GO_0003705 (EC: IC, PMID: 19861239); GO_0003705 (EC: IDA, PMID: 2833704); GO_0003713 (EC: IDA, PMID: 2833704); GO_0005100 (EC: IDA, PMID: 11804590); GO_0005515 (EC: IPI, PMID: 10327051); GO_0005654 (EC: TAS); GO_0005667 (EC: IEA); GO_0005719 (EC: IDA, PMID: 19861239); GO_0005829 (EC: IEA); GO_0007179 (EC: IDA, PMID: 9732876); GO_0007184 (EC: IDA, PMID: 9732876); GO_0007568 (EC: IEA); GO_0007612 (EC: IEA); GO_0007623 (EC: IEA); GO_0008134 (EC: IPI, PMID: 16007074); GO_0008285 (EC: IEA); GO_0009314 (EC: IEA); GO_0009612 (EC: IEA); GO_0017053 (EC: IEA); GO_0030224 (EC: IEA); GO_0031103 (EC: IEA); GO_0031953 (EC: IEA); GO_0032321 (EC: IDA, PMID: 11804590); GO_0032496 (EC: IEA); GO_0034097 (EC: IEA); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035026 (EC: IEA); GO_0035497 (EC: IDA, PMID: 19861239); GO_0035666 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042493 (EC: IEA); GO_0042542 (EC: IEA); GO_0043392 (EC: IDA, PMID: 14645924); GO_0043524 (EC: IEA); GO_0043525 (EC: IEA); GO_0043922 (EC: IDA, PMID: 2833704); GO_0043923 (EC: IDA, PMID: 2833704); GO_0044212 (EC: IDA, PMID: 14645924); GO_0044822 (EC: IDA); GO_0045087 (EC: TAS); GO_0045657 (EC: IEA); GO_0045740 (EC: IEA); GO_0045892 (EC: IDA, PMID: 2833704); GO_0045893 (EC: IDA, PMID: 2833704); GO_0045944 (EC: IC, PMID: 19861239); GO_0045944 (EC: IDA, PMID: 2833704); GO_0048146 (EC: IEA); GO_0048661 (EC: IEA); GO_0051090 (EC: TAS); GO_0051365 (EC: IEA); GO_0051403 (EC: TAS); GO_0051591 (EC: IEA); GO_0051726 (EC: IEA); GO_0051899 (EC: IEA); GO_0060395 (EC: IDA, PMID: 9732876); GO_0070412 (EC: IPI, PMID: 9732876); GO_0071277 (EC: IEA); GO_0071837 (EC: IEA) GO_0000228 (EC: TAS, PMID:10918580); GO_0000980 (EC: IDA, PMID:19861239); GO_0001077 (EC: IEA); GO_0001102 (EC: IPI, PMID:19861239); GO_0001190 (EC: IC, PMID:19861239); GO_0001525 (EC: IEA); GO_0001774 (EC: IEA); GO_0001836 (EC: IEA); GO_0001889 (EC: IEA); GO_0001938 (EC: IEA); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0003151 (EC: IEA); GO_0003677 (EC: TAS, PMID:2825349); GO_0003690 (EC: IEA); GO_0003700 (EC: IDA, PMID:9732876); GO_0003705 (EC: IC, PMID:19861239); GO_0003705 (EC: IDA, PMID:2833704); GO_0003713 (EC: IDA, PMID:2833704); GO_0005100 (EC: IDA, PMID:11804590); GO_0005515 (EC: IPI, PMID:10327051); GO_0005654 (EC: TAS); GO_0005667 (EC: IEA); GO_0005719 (EC: IDA, PMID:19861239); GO_0005829 (EC: IEA); GO_0007179 (EC: IDA, PMID:9732876); GO_0007184 (EC: IDA, PMID:9732876); GO_0007568 (EC: IEA); GO_0007612 (EC: IEA); GO_0007623 (EC: IEA); GO_0008134 (EC: IPI, PMID:16007074); GO_0008285 (EC: IEA); GO_0009314 (EC: IEA); GO_0009612 (EC: IEA); GO_0017053 (EC: IEA); GO_0030224 (EC: IEA); GO_0031103 (EC: IEA); GO_0031953 (EC: IEA); GO_0032321 (EC: IDA, PMID:11804590); GO_0032496 (EC: IEA); GO_0034097 (EC: IEA); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035026 (EC: IEA); GO_0035497 (EC: IDA, PMID:19861239); GO_0035666 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042493 (EC: IEA); GO_0042542 (EC: IEA); GO_0043392 (EC: IDA, PMID:14645924); GO_0043524 (EC: IEA); GO_0043525 (EC: IEA); GO_0043922 (EC: IDA, PMID:2833704); GO_0043923 (EC: IDA, PMID:2833704); GO_0044212 (EC: IDA, PMID:14645924); GO_0044822 (EC: IDA); GO_0045087 (EC: TAS); GO_0045657 (EC: IEA); GO_0045740 (EC: IEA); GO_0045892 (EC: IDA, PMID:2833704); GO_0045893 (EC: IDA, PMID:2833704); GO_0045944 (EC: IC, PMID:19861239); GO_0045944 (EC: IDA, PMID:2833704); GO_0048146 (EC: IEA); GO_0048661 (EC: IEA); GO_0051090 (EC: TAS); GO_0051365 (EC: IEA); GO_0051403 (EC: TAS); GO_0051591 (EC: IEA); GO_0051726 (EC: IEA); GO_0051899 (EC: IEA); GO_0060395 (EC: IDA, PMID:9732876); GO_0070412 (EC: IPI, PMID:9732876); GO_0071277 (EC: IEA); GO_0071837 (EC: IEA) PMID: 1310896; 1448082; 1516134; 1631061; 1651323; 1827203; 1922387; 2138276; 2320002; 2825349; 2833704; 3194415; 7623830; 7642615; 7662174; 7666555; 7690421; 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18985028; 18992165; 19015316; 19018257; 19020743; 19022561; 19028685; 19035162; 19064921; 19080373; 19105933; 19123467; 19131506; 19156129; 19164581; 19165171; 19166930; 19176525; 19193763; 19206162; 19215067; 19219074; 19231233; 19238531; 19249008; 19258923; 19270716; 19281909; 19306295; 19334540; 19343052; 19357699; 19358752; 19384981; 19433309; 19435822; 19471022; 19495976; 19499154; 19513521; 19527717; 19528235; 19531482; 19578717; 19591174; 19595408; 19616043; 19653276; 19654329; 19656241; 19701800; 19714312; 19723051; 19734233; 19734545; 19738058; 19758340; 19758438; 19782465; 19787273; 19794957; 19795388; 19806201; 19811296; 19818398; 19837979; 19841138; 19859790; 19860880; 19861239; 19874574; 19878434; 19885545; 19898747; 19910471; 19910486; 19913121; 19919900; 19921846; 19937141; 19937979; 19939924; 19944700; 19959471; 19965873; 20012528; 20042607; 20044606; 20051654; 20053993; 20074357; 20093361; 20093369; 20102411; 20133937; 20137127; 20170659; 20185758; 20193273; 20195357; 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23382074; 23437118; 23454483; 23467542; 23523566; 23546882; 23562910; 23580428; 23583295; 23602568; 23608488; 23614275; 23615400; 23624934; 23625009; 23625206; 23661758; 23665382; 23669365; 23671702; 23678002; 23682787; 23686163; 23690655; 23720779; 23747343; 23749999; 23762330; 23770289; 23814048; 23818969; 23832539; 23844083; 23906792; 23929433; 23942796; 24027432; 24113186 PMID:1310896; 1448082; 1516134; 1631061; 1651323; 1827203; 1922387; 2138276; 2320002; 2825349; 2833704; 3194415; 7623830; 7642615; 7662174; 7666555; 7690421; 7738014; 7816143; 7823959; 7848298; 7957556; 8001819; 8027667; 8087846; 8108109; 8137421; 8224842; 8302594; 8380166; 8387155; 8397339; 8440710; 8464713; 8480425; 8557686; 8570175; 8586671; 8617242; 8621542; 8621941; 8622660; 8628277; 8649793; 8654373; 8662824; 8663380; 8663478; 8733011; 8763994; 8798722; 8816797; 8816798; 8837781; 8846788; 8945519; 8974016; 8985011; 9020136; 9030721; 9129988; 9154808; 9155018; 9160889; 9207092; 9211894; 9223324; 9235954; 9334186; 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18347071; 18351441; 18352974; 18384814; 18410487; 18414033; 18429822; 18435914; 18443042; 18443043; 18445313; 18448277; 18467434; 18485515; 18487146; 18494816; 18497564; 18515365; 18543249; 18570890; 18572021; 18597608; 18600430; 18617512; 18619508; 18621151; 18644981; 18646516; 18650425; 18653452; 18653705; 18664273; 18671972; 18692129; 18708361; 18716056; 18725194; 18757369; 18775869; 18805449; 18823944; 18838675; 18844221; 18845538; 18922473; 18923650; 18931081; 18936204; 18940179; 18950845; 18952102; 18957410; 18957422; 18985028; 18992165; 19015316; 19018257; 19020743; 19022561; 19028685; 19035162; 19064921; 19080373; 19105933; 19123467; 19131506; 19156129; 19164581; 19165171; 19166930; 19176525; 19193763; 19206162; 19215067; 19219074; 19231233; 19238531; 19249008; 19258923; 19270716; 19281909; 19306295; 19334540; 19343052; 19357699; 19358752; 19384981; 19433309; 19435822; 19471022; 19495976; 19499154; 19513521; 19527717; 19528235; 19531482; 19578717; 19591174; 19595408; 19616043; 19653276; 19654329; 19656241; 19701800; 19714312; 19723051; 19734233; 19734545; 19738058; 19758340; 19758438; 19782465; 19787273; 19794957; 19795388; 19806201; 19811296; 19818398; 19837979; 19841138; 19859790; 19860880; 19861239; 19874574; 19878434; 19885545; 19898747; 19910471; 19910486; 19913121; 19919900; 19921846; 19937141; 19937979; 19939924; 19944700; 19959471; 19965873; 20012528; 20042607; 20044606; 20051654; 20053993; 20074357; 20093361; 20093369; 20102411; 20133937; 20137127; 20170659; 20185758; 20193273; 20195357; 20198339; 20203690; 20222112; 20225236; 20227498; 20232342; 20304822; 20306472; 20331627; 20331972; 20331980; 20333648; 20353950; 20353996; 20371606; 20376080; 20395206; 20410304; 20430872; 20432452; 20448330; 20459032; 20479273; 20479762; 20482821; 20483790; 20503287; 20505831; 20507572; 20508969; 20510020; 20511396; 20519498; 20531301; 20543003; 20554528; 20557936; 20590529; 20607803; 20619956; 20628086; 20628624; 20665665; 20680410; 20683948; 20688351; 20697347; 20698984; 20732415; 20837772; 20852630; 20936779; 20939893; 20942798; 20943203; 20952681; 20955203; 20976196; 20977688; 21030269; 21034562; 21081043; 21081472; 21106530; 21106746; 21134350; 21139048; 21145111; 21148792; 21196933; 21212516; 21268080; 21289643; 21338584; 21349840; 21350237; 21357535; 21360282; 21364631; 21381700; 21393476; 21397653; 21410405; 21417953; 21439937; 21451046; 21454713; 21496208; 21511059; 21518489; 21526160; 21530485; 21555589; 21559334; 21565167; 21570970; 21607373; 21617575; 21617851; 21640141; 21647439; 21675959; 21685329; 21693764; 21697091; 21699750; 21703547; 21732343; 21739277; 21743958; 21745629; 21799768; 21801875; 21814482; 21822357; 21829441; 21835421; 21835891; 21860413; 21862593; 21872498; 21890473; 21895606; 21937452; 21972703; 21988832; 21989944; 22001392; 22002117; 22051934; 22077140; 22083952; 22092038; 22110360; 22119392; 22132731; 22139817; 22176144; 22189957; 22235337; 22239235; 22265050; 22266871; 22271085; 22271878; 22307329; 22327296; 22328508; 22331067; 22354960; 22384197; 22384232; 22394497; 22399296; 22417306; 22429882; 22438909; 22450687; 22484283; 22508041; 22512945; 22570239; 22597534; 22675553; 22685373; 22688014; 22719067; 22749179; 22771387; 22791811; 22797068; 22801218; 22843696; 22853846; 22860098; 22869147; 22879913; 22911824; 22926518; 22933572; 22966201; 22974165; 22981541; 22988241; 23027969; 23028371; 23041974; 23047699; 23135283; 23153494; 23163821; 23182717; 23223231; 23226410; 23236059; 23269699; 23300800; 23331079; 23339184; 23362975; 23382074; 23437118; 23454483; 23467542; 23523566; 23546882; 23562910; 23580428; 23583295; 23602568; 23608488; 23614275; 23615400; 23624934; 23625009; 23625206; 23661758; 23665382; 23669365; 23671702; 23678002; 23682787; 23686163; 23690655; 23720779; 23747343; 23749999; 23762330; 23770289; 23814048; 23818969; 23832539; 23844083; 23906792; 23929433; 23942796; 24027432; 24113186 jun proto-oncogene Ensembl:ENSG00000177606 HGNC:6204 HPRD:01302 MIM:165160 Vega:OTTHUMG00000008376 Other designations: Jun activation domain binding protein|activator protein 1|enhancer-binding protein AP1|jun oncogene|p39|proto-oncogene c-Jun|transcription factor AP-1|v-jun avian sarcoma virus 17 oncogene homolog|v-jun sarcoma virus 17 oncogene homolog JUN OGG:3000003726 Bin Zhao, Yue Liu, Oliver He AP-1 WEB: http://www.ncbi.nlm.nih.gov/gene JUNB jun B proto-oncogene 3726 19p13.2 9606 19 GO_0000785 (EC: TAS, PMID:2513129); GO_0000977 (EC: IEA); GO_0001570 (EC: IEA); GO_0001649 (EC: IEA); GO_0001829 (EC: IEA); GO_0003677 (EC: TAS, PMID:10764760); GO_0003690 (EC: IEA); GO_0003700 (EC: IEA); GO_0003713 (EC: TAS, PMID:2513129); GO_0003714 (EC: TAS, PMID:2513129); GO_0005515 (EC: IPI, PMID:16511568); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0006351 (EC: TAS); GO_0006357 (EC: TAS, PMID:2513129); GO_0006367 (EC: TAS); GO_0007179 (EC: TAS); GO_0009416 (EC: IEA); GO_0009612 (EC: IEA); GO_0010467 (EC: TAS); GO_0030316 (EC: IEA); GO_0032570 (EC: IEA); GO_0032870 (EC: IEA); GO_0033687 (EC: IEA); GO_0034097 (EC: IEA); GO_0042493 (EC: IEA); GO_0043434 (EC: IEA); GO_0045597 (EC: IEA); GO_0045944 (EC: TAS); GO_0046697 (EC: IEA); GO_0051412 (EC: IEA); GO_0051591 (EC: IEA); GO_0051726 (EC: IEA); GO_0060136 (EC: IEA); GO_0060716 (EC: IEA); GO_0071277 (EC: IEA) PMID:1406655; 1633872; 1899335; 2112242; 2513129; 8125298; 8432525; 8530030; 8570175; 8649827; 8654373; 8917518; 8945519; 8954125; 9128241; 9154808; 9405416; 9872330; 9889198; 10220381; 10764760; 10777209; 10903323; 11036094; 11053448; 11477071; 11726656; 12080089; 12145210; 12165517; 12371906; 12393503; 12477932; 12506033; 12522006; 12592382; 12907453; 12907627; 14499865; 14673171; 15025563; 15231748; 15240010; 15302935; 15308641; 15489334; 15507668; 15867431; 16189514; 16511568; 16552541; 16880520; 17081983; 17204476; 17306025; 17495958; 17510411; 17601350; 17681951; 17690253; 17965727; 18029348; 18042260; 18259752; 18391017; 18424718; 18628455; 18843287; 18977241; 19064921; 19151755; 19321746; 19409613; 19471022; 19666408; 19923172; 20006998; 20030915; 20056077; 20132737; 20195357; 20200942; 21225234; 21289643; 21326808; 21393445; 21423810; 21693764; 21822216; 21906983; 21937452; 21963094; 21988832; 22020339; 22082156; 22242598; 22252121; 22328780; 22710716; 23000965; 23297064; 23308222; 23661758; 23749999; 24136993; 24200694 jun B proto-oncogene Ensembl:ENSG00000171223 HGNC:6205 HPRD:01303 MIM:165161 Vega:OTTHUMG00000180373 Other designations: activator protein 1|transcription factor jun-B JUNB OGG:3000003727 Bin Zhao, Yue Liu, Oliver He AP-1 WEB: http://www.ncbi.nlm.nih.gov/gene JUND jun D proto-oncogene 3727 19p13.2 9606 19 GO_0000785 (EC: TAS, PMID:1903194); GO_0002076 (EC: IEA); GO_0003690 (EC: IEA); GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID:17577209); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0006357 (EC: TAS, PMID:1903194); GO_0006366 (EC: IEA); GO_0007568 (EC: IEA); GO_0007623 (EC: IEA); GO_0009416 (EC: IEA); GO_0009612 (EC: IEA); GO_0014070 (EC: IEA); GO_0016922 (EC: IEA); GO_0032496 (EC: IEA); GO_0043234 (EC: IEA); GO_0043434 (EC: IEA); GO_0043565 (EC: IEA); GO_0044212 (EC: IDA, PMID:1903194); GO_0045669 (EC: IEA); GO_0045944 (EC: IEA); GO_0071277 (EC: IEA) PMID:1899335; 1903194; 2112242; 7848298; 8125298; 8152431; 8432525; 8570175; 8654373; 8837781; 8889548; 8945519; 9154808; 9739985; 9872330; 9989505; 10220381; 10500243; 10523647; 10713367; 10934195; 10942775; 11221882; 11431474; 11477071; 11903046; 12032852; 12052834; 12052862; 12054733; 12080089; 12082101; 12105216; 12165517; 12193410; 12226747; 12477932; 12615916; 12727841; 14559791; 14676207; 15044019; 15302935; 15507668; 15563473; 15688015; 15706351; 15867431; 16007120; 16129800; 16264271; 16423552; 16651450; 17081983; 17204476; 17205062; 17495958; 17510411; 17577209; 17651017; 17681951; 18071306; 18078517; 18095154; 18321953; 18386285; 18443593; 18454173; 18562690; 18671972; 18952102; 19166930; 19211927; 19322201; 19470832; 19471022; 20195357; 21145461; 21315773; 21393445; 21473742; 21559334; 21693764; 21734453; 21906983; 21937452; 22327296; 22493372; 22696638; 23000965; 23289756; 23376981; 23382074; 23667531; 23942796; 24140207 jun D proto-oncogene Ensembl:ENSG00000130522 HGNC:6206 HPRD:01304 MIM:165162 Vega:OTTHUMG00000183355 Other designations: JunD-FL isoform|activator protein 1|transcription factor jun-D JUND OGG:3000003778 Bin Zhao, Yue Liu, Oliver He BKTM KCa1.1 MaxiK SAKCA SLO SLO-ALPHA SLO1 bA205K10.1 mSLO1 WEB: http://www.ncbi.nlm.nih.gov/gene KCNMA1 potassium large conductance calcium-activated channel, subfamily M, alpha member 1 3778 RP11-443A13.1 10q22.3 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0001666 (EC: IDA, PMID: 15528406); GO_0003779 (EC: IDA, PMID: 15703204); GO_0005249 (EC: IDA, PMID: 11880513); GO_0005515 (EC: IPI, PMID: 10692449); GO_0005783 (EC: IEA); GO_0005886 (EC: TAS); GO_0005901 (EC: IDA, PMID: 15703204); GO_0006813 (EC: IDA, PMID: 11245614); GO_0006970 (EC: IDA, PMID: 10840032); GO_0007268 (EC: TAS); GO_0007596 (EC: TAS); GO_0007605 (EC: IEA); GO_0007628 (EC: IEA); GO_0008076 (EC: IDA, PMID: 7573516); GO_0009897 (EC: IEA); GO_0015269 (EC: IDA, PMID: 11245614); GO_0016021 (EC: IDA, PMID: 11880513); GO_0016324 (EC: IDA, PMID: 10840032); GO_0019228 (EC: IEA); GO_0030007 (EC: IDA, PMID: 11245614); GO_0032344 (EC: IEA); GO_0034465 (EC: IDA, PMID: 15528406); GO_0034465 (EC: IMP, PMID: 18180950); GO_0042391 (EC: IDA, PMID: 7877450); GO_0042491 (EC: IEA); GO_0043065 (EC: IMP, PMID: 11245614); GO_0043195 (EC: IEA); GO_0045211 (EC: IEA); GO_0045475 (EC: IEA); GO_0045794 (EC: IDA, PMID: 12388065); GO_0046541 (EC: IEA); GO_0046872 (EC: IEA); GO_0048469 (EC: IEA); GO_0050885 (EC: IEA); GO_0051260 (EC: IEA); GO_0051592 (EC: IDA, PMID: 12388065); GO_0060072 (EC: IDA, PMID: 7993625); GO_0060072 (EC: IMP, PMID: 15703204); GO_0060073 (EC: IDA, PMID: 11641143); GO_0060082 (EC: IEA); GO_0060083 (EC: IDA, PMID: 11641143); GO_0060087 (EC: IEA); GO_0071805 (EC: IBA); GO_0071805 (EC: IDA, PMID: 11880513) PMID: 7573516; 7687074; 7877450; 7987297; 7993625; 8006036; 8612769; 8821792; 8962157; 9391153; 9829973; 10097176; 10489376; 10692449; 10758170; 10840032; 11245614; 11401860; 11604135; 11641143; 11832330; 11880485; 11880513; 11986367; 12009018; 12016222; 12161564; 12223479; 12388065; 12391293; 12434576; 12438308; 12477932; 12566537; 14522958; 14523450; 14584897; 14631046; 14702039; 14715246; 15164054; 15174051; 15194822; 15251455; 15280542; 15489334; 15528406; 15703204; 15849354; 15937479; 16042390; 16081418; 16100257; 16382103; 16385451; 16396928; 16790810; 16895996; 16951373; 17146446; 17150299; 17166942; 17468961; 17483867; 17521822; 17586600; 17591987; 17591990; 17706472; 17901123; 17989352; 18084004; 18162557; 18180950; 18227273; 18316727; 18345016; 18367663; 18385281; 18404672; 18414909; 18458941; 18480178; 18559348; 18719396; 18854754; 19052171; 19096717; 19118164; 19168436; 19204046; 19344525; 19430934; 19456106; 19482008; 19552602; 19617704; 19640305; 19718020; 19738431; 20012488; 20037152; 20051533; 20379614; 20400778; 20424473; 20427280; 20457834; 20479001; 20508092; 20574420; 20624858; 20630939; 20677014; 20808839; 20959415; 21072171; 21078868; 21301863; 21413024; 21613417; 21670298; 21708048; 21724437; 21757754; 22074915; 22140451; 22194818; 22331907; 22446331; 22474334; 22504420; 22538239; 22710124; 22896041; 22899999; 23232643; 23237801; 23255603; 23267835; 23626738; 23831469; 23992640; 24067659; 24457600 potassium large conductance calcium-activated channel, subfamily M, alpha member 1 Ensembl:ENSG00000156113 HGNC:6284 HPRD:15967 MIM:600150 Vega:OTTHUMG00000018543 Other designations: BK channel alpha subunit|BKCA alpha subunit|calcium-activated potassium channel subunit alpha-1|calcium-activated potassium channel, subfamily M subunit alpha-1|hSlo|k(VCA)alpha|maxi-K channel HSLO|slo homolog|slowpoke homolog|stretch-activated Kca channel KCNMA1 OGG:3000003818 Bin Zhao, Yue Liu, Oliver He KLK3 PPK WEB: http://www.ncbi.nlm.nih.gov/gene KLKB1 kallikrein B, plasma (Fletcher factor) 1 3818 4q35 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0002542 (EC: TAS, PMID: 2510163); GO_0004252 (EC: IEA); GO_0005515 (EC: IPI, PMID: 2844223); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 89876); GO_0005886 (EC: TAS); GO_0006508 (EC: TAS, PMID: 1993180); GO_0007596 (EC: TAS); GO_0007597 (EC: TAS); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0031638 (EC: TAS, PMID: 2510163); GO_0031639 (EC: IDA, PMID: 89876); GO_0042730 (EC: IEA); GO_0051919 (EC: IDA, PMID: 89876) PMID: 89876; 291905; 500690; 694428; 1466300; 1993180; 1998666; 2510163; 2551064; 2844223; 3521732; 3636155; 7686159; 7944388; 8025275; 8226803; 8280154; 8555184; 8761966; 9535413; 10068459; 10226805; 10464316; 10543447; 10604527; 10962009; 11031105; 11383556; 11434682; 11864713; 12372819; 12477932; 12754519; 12887060; 12944405; 14718574; 15146197; 15489334; 16199530; 16335952; 17318641; 17696780; 17922805; 18029348; 18160576; 18413232; 18713009; 19342086; 19372141; 19423540; 19583818; 19620246; 20135073; 20339536; 20406964; 20438785; 20725119; 21886157; 22286219; 22916037; 23251661; 23381795; 23672780 kallikrein B, plasma (Fletcher factor) 1 Ensembl:ENSG00000164344 HGNC:6371 HPRD:01971 MIM:229000 Vega:OTTHUMG00000150347 Other designations: Fletcher factor|kininogenin|plasma kallikrein|plasma kallikrein heavy chain|plasma kallikrein light chain|plasma prekallikrein KLKB1 OGG:3000003821 Bin Zhao, Yue Liu, Oliver He CD159A NKG2 NKG2A WEB: http://www.ncbi.nlm.nih.gov/gene KLRC1 killer cell lectin-like receptor subfamily C, member 1 3821 12p13 20140408 9606 12 protein-coding Official from a nomenclature committee GO_0004888 (EC: TAS, PMID: 2007850); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 2007850); GO_0007166 (EC: TAS, PMID: 2007850); GO_0030246 (EC: IEA); GO_0050776 (EC: TAS) PMID: 2007850; 8436421; 8753859; 8943374; 9034158; 9218532; 9485206; 9486650; 9598306; 9842883; 10320637; 10488737; 11238637; 11513152; 12165520; 12387742; 12444112; 12461076; 12477932; 12618865; 15489334; 15528343; 15550116; 15561299; 15687235; 16434388; 16690409; 16951318; 17545086; 17706207; 17767552; 17927829; 17976318; 18056444; 18083576; 18172398; 18332182; 18448674; 18500933; 18700876; 18941190; 18981088; 19002424; 19124726; 19395088; 19615756; 19694640; 19782712; 20012119; 20139023; 20237496; 20379614; 20550548; 20587610; 20648603; 20654155; 20696944; 20700504; 20952657; 21212510; 21518478; 21538351; 22486170 killer cell lectin-like receptor subfamily C, member 1 Ensembl:ENSG00000134545 HGNC:6374 HPRD:01192 MIM:161555 Vega:OTTHUMG00000168584 Other designations: C-lectin type II protein|CD159 antigen-like family member A|NK cell receptor A|NKG2-1/B activating NK receptor|NKG2-A/B type II integral membrane protein|NKG2-A/B-activating NK receptor|NKG2-A/NKG2-B type II integral membrane protein|natural killer cell lectin|natural killer group protein 2 KLRC1 OGG:3000003833 Bin Zhao, Yue Liu, Oliver He HSET KNSL2 WEB: http://www.ncbi.nlm.nih.gov/gene KIFC1 kinesin family member C1 3833 DAQB-126H3.5 6p21.3 9606 6 Official from a nomenclature committee GO_0000070 (EC: NAS, PMID: 8276466); GO_0003777 (EC: NAS, PMID: 8276466); GO_0005524 (EC: NAS, PMID: 8276466); GO_0005634 (EC: IEA); GO_0005769 (EC: IEA); GO_0005815 (EC: IEA); GO_0005819 (EC: IEA); GO_0005871 (EC: IEA); GO_0005874 (EC: IEA); GO_0007018 (EC: TAS); GO_0007596 (EC: TAS); GO_0008017 (EC: IEA); GO_0008152 (EC: NAS, PMID: 8276466) PMID: 8276466; 10369922; 11416179; 12477932; 14574404; 15489334; 17081983; 17326138; 18082152; 19116309; 19190132; 19525938; 19679349; 19851445; 21139048; 21252943; 21832049; 21890473; 21963094; 22201025; 22946058; 23000965; 23318213; 24250222 kinesin family member C1 Ensembl:ENSG00000237649 HGNC:6389 MIM:603763 Vega:OTTHUMG00000031209 Other designations: kinesin-like 2|kinesin-like protein 2|kinesin-like protein KIFC1|kinesin-related protein HSET KIFC1 OGG:3000003939 Bin Zhao, Yue Liu, Oliver He GSD11 HEL-S-133P LDH1 LDHM WEB: http://www.ncbi.nlm.nih.gov/gene LDHA lactate dehydrogenase A 3939 PIG19 11p15.4 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0004459 (EC: NAS, PMID: 1953713); GO_0005515 (EC: IPI); GO_0005739 (EC: IEA); GO_0005829 (EC: TAS); GO_0005929 (EC: IEA); GO_0006090 (EC: TAS); GO_0006096 (EC: NAS, PMID: 1953713); GO_0021762 (EC: IEP); GO_0031668 (EC: IEA); GO_0044237 (EC: TAS); GO_0044262 (EC: IEA); GO_0044281 (EC: TAS); GO_0070062 (EC: IDA, PMID: 11487543) PMID: 1297552; 1445373; 1953713; 1959923; 2315312; 2334430; 2434947; 3000353; 3838278; 5014440; 7273846; 7908613; 8125298; 8327147; 10508479; 10897012; 11125887; 11276087; 11487543; 11582518; 12107167; 12145195; 12160330; 12477932; 12555229; 12629811; 12712614; 14702039; 14760703; 15161933; 15231747; 15240094; 15489334; 15592455; 15635413; 15710247; 16009940; 16027165; 16132575; 16196087; 16263121; 16344560; 16766262; 17178662; 17220478; 17483170; 18039033; 18160415; 18521687; 18534967; 18781797; 18814027; 18821170; 19021062; 19135240; 19276158; 19668225; 19738201; 19838163; 19847924; 19923867; 20385008; 20639865; 20677014; 20828817; 20849852; 20877624; 20946988; 20951115; 21044950; 21081666; 21124955; 21139048; 21145461; 21249322; 21252943; 21319273; 21452021; 21632858; 21726808; 21853274; 21858537; 21890473; 21906983; 21963094; 21969607; 21987572; 21988832; 22053931; 22079093; 22127970; 22268729; 22304920; 22360420; 22429998; 22505724; 22536838; 22593701; 22623428; 22863883; 22897481; 22923663; 22939629; 22948140; 22961700; 22990118; 23000965; 23166385; 23184277; 23266049; 23318563; 23349634; 23404405; 23467744; 23516535; 23722553; 23797802; 23859015; 24250222; 24457600 lactate dehydrogenase A Ensembl:ENSG00000134333 HGNC:6535 HPRD:01025 MIM:150000 Vega:OTTHUMG00000167721 Other designations: L-lactate dehydrogenase A chain|LDH muscle subunit|LDH-A|LDH-M|cell proliferation-inducing gene 19 protein|epididymis secretory sperm binding protein Li 133P|lactate dehydrogenase M|proliferation-inducing gene 19|renal carcinoma antigen NY-REN-59 LDHA OGG:3000003956 Bin Zhao, Yue Liu, Oliver He GAL1 GBP WEB: http://www.ncbi.nlm.nih.gov/gene LGALS1 lectin, galactoside-binding, soluble, 1 3956 22q13.1 9606 22 Official from a nomenclature committee GO_0001948 (EC: IEA); GO_0002317 (EC: IEA); GO_0004871 (EC: IMP, PMID: 12761501); GO_0005515 (EC: IPI, PMID: 10369126); GO_0005578 (EC: IEA); GO_0005615 (EC: IDA); GO_0005622 (EC: IDA); GO_0005634 (EC: IEA); GO_0005737 (EC: TAS, PMID: 16130169); GO_0006915 (EC: IEA); GO_0007165 (EC: IMP, PMID: 12761501); GO_0009986 (EC: IEA); GO_0010812 (EC: IEA); GO_0010977 (EC: IEA); GO_0016936 (EC: IEA); GO_0030395 (EC: IEA); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0031012 (EC: ISS, Qualifier: colocalizes_with); GO_0031295 (EC: IEA); GO_0033555 (EC: IEA); GO_0034120 (EC: IEA); GO_0042493 (EC: IEA); GO_0042803 (EC: IEA); GO_0042981 (EC: TAS, PMID: 16130169); GO_0043123 (EC: IMP, PMID: 12761501); GO_0043236 (EC: IEA); GO_0044822 (EC: IDA); GO_0045445 (EC: IEA); GO_0048678 (EC: IEA); GO_0071333 (EC: IEA); GO_0071407 (EC: IEA) PMID: 1602151; 1713454; 1988031; 1996404; 2383549; 2719646; 2719964; 2910856; 3020551; 3065332; 3611046; 7501023; 7750127; 7795414; 7821789; 7869048; 8063692; 8432540; 8449510; 8872948; 9264263; 9572443; 9683529; 10369126; 10425546; 10490978; 10591208; 10642604; 10764829; 10950114; 11076863; 11146440; 11256614; 11522829; 11709720; 11846886; 11850528; 11937561; 12008046; 12125737; 12271131; 12477932; 12527107; 12615972; 12665801; 12761501; 12810474; 12823983; 12853445; 14507657; 14550305; 14612929; 14617626; 14693917; 14769876; 15050916; 15297883; 15461802; 15489334; 15489336; 15556936; 15556941; 15663199; 15690107; 15778371; 15862866; 15910247; 15929990; 15972675; 16033063; 16051185; 16130169; 16247730; 16381901; 16388708; 16530434; 16636291; 16751364; 16785517; 16818733; 16940423; 17043243; 17110462; 17177840; 17182582; 17269744; 17304502; 17353931; 17390012; 17438085; 17523619; 17535296; 17537433; 17603562; 17616672; 17649808; 17880528; 17884770; 17984174; 18007053; 18028978; 18223683; 18258591; 18292532; 18315601; 18431251; 18519761; 18570123; 18581052; 18624398; 18630998; 18633135; 18662664; 18671640; 18691335; 18791848; 18796645; 18802059; 18824694; 18838383; 18947333; 18991278; 19011096; 19032754; 19064001; 19103599; 19116313; 19125585; 19128029; 19148478; 19155496; 19171142; 19225046; 19287070; 19287997; 19363525; 19412433; 19454697; 19471022; 19492862; 19506091; 19520156; 19550395; 19561030; 19635795; 19688976; 19730683; 19738201; 19860718; 19886821; 19898636; 19900702; 19913121; 20006954; 20053628; 20157731; 20177845; 20200618; 20332322; 20360068; 20363255; 20399482; 20525878; 20549082; 20570633; 20592339; 20596638; 20628086; 20644118; 20657665; 20728947; 20816214; 20828557; 20873803; 21113146; 21122983; 21139048; 21147166; 21150319; 21191065; 21292557; 21372130; 21378323; 21385934; 21391228; 21397408; 21505194; 21514365; 21614093; 21632118; 21689853; 21724180; 21747316; 21779348; 21780106; 21807362; 21880716; 21880749; 21890473; 21897333; 21906983; 21963094; 21986812; 21998324; 22022970; 22028908; 22081313; 22155450; 22156919; 22167721; 22174828; 22267483; 22271227; 22285770; 22291012; 22353504; 22373585; 22383798; 22386573; 22432916; 22447203; 22456341; 22524424; 22546645; 22561438; 22583806; 22609846; 22623428; 22689223; 22692729; 22696230; 22716213; 22777171; 22785208; 22844466; 22863883; 22884463; 22936677; 22939629; 22939954; 22942212; 23000965; 23002109; 23022198; 23027923; 23113677; 23121677; 23124203; 23142379; 23223580; 23359172; 23389289; 23402259; 23431236; 23444403; 23510298; 23599627; 23681112; 23862649; 23929302; 23956138; 24211210 lectin, galactoside-binding, soluble, 1 Ensembl:ENSG00000100097 HGNC:6561 HPRD:01040 MIM:150570 Vega:OTTHUMG00000150661 Other designations: 14 kDa laminin-binding protein|14 kDa lectin|HBL|HLBP14|HPL|S-Lac lectin 1|beta-galactoside-binding lectin L-14-I|beta-galactoside-binding protein 14kDa|gal-1|galaptin|galectin 1|galectin-1|lactose-binding lectin 1|putative MAPK-activating protein PM12 LGALS1 OGG:3000004001 Bin Zhao, Yue Liu, Oliver He ADLD LMN LMN2 LMNB WEB: http://www.ncbi.nlm.nih.gov/gene LMNB1 lamin B1 4001 5q23.2 9606 5 Official from a nomenclature committee GO_0005198 (EC: IEA); GO_0005635 (EC: TAS); GO_0005637 (EC: IEA); GO_0005638 (EC: IEA); GO_0005654 (EC: TAS); GO_0006915 (EC: TAS); GO_0006921 (EC: TAS); GO_0031965 (EC: IDA); GO_0043274 (EC: IEA) PMID: 1986862; 2023931; 2325650; 2406262; 2544227; 7557986; 7628545; 8034666; 8324822; 8838815; 8978814; 9128241; 9243284; 9305626; 9367621; 9436978; 9490046; 10679189; 10806082; 10960149; 11095689; 11331782; 11441066; 11691994; 11790298; 11792809; 11901153; 12135703; 12477932; 12490158; 12670476; 12898336; 14504265; 15161933; 15265697; 15284226; 15635413; 16083285; 16196087; 16216881; 16236267; 16283426; 16344560; 16365157; 16410549; 16543417; 17550303; 17620012; 18334554; 18524819; 19001169; 19141474; 19151023; 19198602; 19322201; 19348623; 19383719; 19454010; 19471022; 19522540; 19727227; 19738201; 19765186; 19961535; 20004208; 20085707; 20230530; 20360068; 20816241; 21139048; 21225301; 21346760; 21549307; 21890473; 21897860; 21906983; 21909802; 21963094; 21988832; 22053931; 22155925; 22178446; 22246186; 22265972; 22268729; 22412018; 22446626; 22496421; 22505724; 22623428; 22658654; 22751105; 22863883; 22939629; 23000965; 23261988; 23439683; 23475125; 23649844; 23681646; 23733478; 23798571; 23934658; 23964094; 24157836; 24163370; 24244333; 24457600 lamin B1 Ensembl:ENSG00000113368 HGNC:6637 HPRD:01036 MIM:150340 Vega:OTTHUMG00000128969 Other designations: lamin-B1 LMNB1 gene OGG:3000004018 Bin Zhao, Yue Liu, Oliver He AK38 APOA LP WEB: http://www.ncbi.nlm.nih.gov/gene LPA lipoprotein, Lp(a) 4018 6q26 9606 6 Official from a nomenclature committee GO_0001968 (EC: IPI, PMID: 2531657); GO_0004252 (EC: IDA, PMID: 2531657); GO_0004866 (EC: TAS, PMID: 8047165); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005576 (EC: TAS); GO_0006629 (EC: NAS, PMID: 8047165); GO_0006869 (EC: IEA); GO_0006898 (EC: TAS); GO_0008015 (EC: TAS, PMID: 8047165); GO_0008201 (EC: NAS, PMID: 2531657); GO_0010951 (EC: TAS, PMID: 8047165); GO_0034185 (EC: IPI, PMID: 9269765); GO_0034358 (EC: IDA, PMID: 2531657); GO_0042157 (EC: TAS); GO_0044281 (EC: TAS) PMID: 2530631; 2531657; 3410459; 3670400; 7918682; 8047165; 8642595; 8864963; 9111002; 9269765; 9548923; 9717723; 9925657; 10073957; 10187779; 10484779; 10672142; 10980194; 11126727; 11285247; 11294842; 11332648; 11440434; 11485023; 11816712; 11822583; 11833851; 11865151; 11947970; 11999088; 12082592; 12111551; 12127051; 12220441; 12359323; 12482643; 12562843; 12578871; 12738397; 12940514; 14718574; 14746139; 15041277; 15258620; 15479125; 15515480; 15523644; 15543335; 15654123; 15708348; 15905467; 15983325; 16053196; 16113787; 16122830; 16150826; 16197951; 16202171; 16403785; 16497311; 16625232; 16840570; 16893192; 17145597; 17460176; 17462619; 17478739; 17537433; 17569884; 17603063; 17683612; 17845920; 17908332; 17923276; 17942087; 17975119; 18086931; 18163888; 18198982; 18280807; 18304554; 18386550; 18464913; 18479303; 18513389; 18560444; 18582452; 18594118; 18599799; 18622136; 18660489; 18682748; 18682798; 18775538; 18776185; 18806883; 18848929; 18983515; 19014618; 19023099; 19124843; 19131662; 19198611; 19208510; 19222374; 19233690; 19263529; 19335423; 19348789; 19349573; 19479237; 19496273; 19509380; 19545557; 19564206; 19572086; 19636317; 19642912; 19646429; 19672030; 19808717; 19880117; 19913121; 19948975; 20014954; 20026018; 20032323; 20036902; 20106478; 20129380; 20129381; 20129382; 20129383; 20143106; 20160194; 20197188; 20303190; 20379614; 20444451; 20452482; 20580413; 20593350; 20601648; 20605575; 20628086; 20673868; 20679960; 20686565; 20691971; 20705065; 20971364; 21078622; 21086792; 21127300; 21149283; 21153771; 21179199; 21231777; 21252144; 21283670; 21300353; 21378990; 21404224; 21473861; 21484527; 21493818; 21519277; 21592478; 21749171; 21802535; 21900290; 21907882; 21914687; 21914962; 21970553; 21986921; 22010162; 22134617; 22192511; 22207727; 22283971; 22327610; 22331829; 22368281; 22387060; 22407494; 22422337; 22485129; 22516069; 22633661; 22710560; 22748161; 22753196; 22762941; 23010950; 23036009; 23040268; 23099120; 23118302; 23137279; 23165148; 23183511; 23202367; 23243000; 23357149; 23375930; 23388002; 23484137; 23652366; 23701995; 23726366; 23735648; 23903772; 23914433; 23973688; 24089516; 24092750 lipoprotein, Lp(a) Ensembl:ENSG00000198670 HGNC:6667 HPRD:01063 MIM:152200 Vega:OTTHUMG00000015956 Other designations: antiangiogenic AK38 protein|apo(a)|apolipoprotein(a)|lp(a) LPA OGG:3000004023 LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Severe mutations that cause LPL deficiency result in type I hyperlipoproteinemia, while less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. [provided by RefSeq, Jul 2008] lipoprotein lipase Ensembl:ENSG00000175445 HGNC:6677 MIM:609708 NCBI-Human-GeneID:4023 NCBI-Mouse-GeneID:16956 NCBI-Rat-GeneID:24539 LPL NCBI-Human-GeneID:4023 http://www.ncbi.nlm.nih.gov/gene/4023 NCBI-Mouse-GeneID:16956 http://www.ncbi.nlm.nih.gov/gene/16956 NCBI-Rat-GeneID:24539 http://www.ncbi.nlm.nih.gov/gene/24539 OGG:3000004047 Bin Zhao, Yue Liu, Oliver He OSC WEB: http://www.ncbi.nlm.nih.gov/gene LSS lanosterol synthase (2,3-oxidosqualene-lanosterol cyclase) 4047 21q22.3 9606 21 Official from a nomenclature committee GO_0000250 (EC: IEA); GO_0005789 (EC: TAS); GO_0005811 (EC: IDA, PMID: 14741744); GO_0006695 (EC: IMP, PMID: 17186944); GO_0006695 (EC: TAS); GO_0008202 (EC: TAS, PMID: 7639730); GO_0044281 (EC: TAS) PMID: 3515096; 7639730; 8593458; 8655142; 8820110; 8889548; 9763219; 10598817; 10830953; 11421484; 12477932; 14702039; 14741744; 14766201; 15489334; 15525992; 15790807; 16344560; 16806233; 17186944; 17255364; 18660489; 19119143; 19913121; 20379614; 20628086; 21139048; 21890473; 21906983; 21963094; 21987572; 21988832; 22053931; 22505724; 23000965; 24250222 lanosterol synthase (2,3-oxidosqualene-lanosterol cyclase) Ensembl:ENSG00000160285 HGNC:6708 HPRD:02945 MIM:600909 Vega:OTTHUMG00000090633 Other designations: 2,3-epoxysqualene--lanosterol cyclase|2,3-epoxysqualene-lanosterol cyclase|hOSC|lanosterol synthase|oxidosqualene--lanosterol cyclase LSS OGG:3000004051 Bin Zhao, Yue Liu, Oliver He CPF3 CYP4F LTB4H WEB: http://www.ncbi.nlm.nih.gov/gene CYP4F3 cytochrome P450, family 4, subfamily F, polypeptide 3 4051 19p13.2 9606 19 GO_0004497 (EC: TAS, PMID:8486631); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006690 (EC: TAS); GO_0006691 (EC: TAS); GO_0006805 (EC: TAS); GO_0016021 (EC: IEA); GO_0019369 (EC: TAS); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS); GO_0050051 (EC: IEA); GO_0052871 (EC: IEA) PMID:8026587; 8486631; 9068972; 9539102; 10409674; 11461919; 12477932; 12709424; 14715252; 15128046; 16344560; 16380383; 17980168; 18065749; 18566475; 18577768; 19138970; 19343046; 20047521; 20237496; 21666788; 21906983; 22706230 cytochrome P450, family 4, subfamily F, polypeptide 3 Ensembl:ENSG00000186529 HGNC:2646 HPRD:03169 MIM:601270 Vega:OTTHUMG00000182374 Other designations: CYPIVF3|cytochrome P-450|cytochrome P450 4F3|cytochrome P450, subfamily IVF, polypeptide 3 (leukotriene B4 omega hydroxylase)|cytochrome P450-LTB-omega|leukotriene B4 omega hydroxylase|leukotriene-B(4) 20-monooxygenase 2|leukotriene-B(4) omega-hydroxylase 2|leukotriene-B4 20-monooxygenase CYP4F3 OGG:3000004061 Bin Zhao, Yue Liu, Oliver He RIG-E RIGE SCA-2 SCA2 TSA-1 WEB: http://www.ncbi.nlm.nih.gov/gene LY6E lymphocyte antigen 6 complex, locus E 4061 8q24.3 20140408 9606 8 protein-coding Official from a nomenclature committee GO_0001701 (EC: IEA); GO_0005887 (EC: TAS, PMID: 8650192); GO_0007166 (EC: TAS, PMID: 8650192); GO_0030325 (EC: IEA); GO_0031225 (EC: IEA); GO_0035265 (EC: IEA); GO_0042415 (EC: IEA); GO_0048242 (EC: IEA); GO_0055010 (EC: IEA) PMID: 8125298; 8650192; 8757598; 9366413; 9551972; 9575182; 11576217; 11784869; 12477932; 12516096; 15489334; 16712791; 18755862; 18990604; 19672991; 20237496; 21963094 lymphocyte antigen 6 complex, locus E Ensembl:ENSG00000160932 HGNC:6727 HPRD:03227 MIM:601384 Vega:OTTHUMG00000164754 LY6E OGG:3000004153 Bin Zhao, Yue Liu, Oliver He COLEC1 HSMBPC MBL MBL2D MBP MBP-C MBP1 MBPD WEB: http://www.ncbi.nlm.nih.gov/gene MBL2 mannose-binding lectin (protein C) 2, soluble 4153 RP11-94H3.1 10q11.2 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0001867 (EC: IDA, PMID: 15148336); GO_0001867 (EC: IPI, PMID: 11549596); GO_0001867 (EC: TAS); GO_0005102 (EC: IPI, PMID: 11549596); GO_0005515 (EC: IPI, PMID: 11485744); GO_0005537 (EC: NAS, PMID: 11549596); GO_0005537 (EC: TAS, PMID: 2477488); GO_0005576 (EC: TAS); GO_0005581 (EC: IEA); GO_0005615 (EC: IEA); GO_0006953 (EC: TAS, PMID: 2477488); GO_0006956 (EC: TAS); GO_0006958 (EC: IEA); GO_0006979 (EC: NAS, PMID: 11549596); GO_0008228 (EC: TAS, PMID: 2477488); GO_0009986 (EC: TAS, PMID: 2477488); GO_0042742 (EC: TAS, PMID: 2477488); GO_0044130 (EC: IDA, PMID: 15148336); GO_0045087 (EC: TAS); GO_0048306 (EC: IPI, PMID: 12421953); GO_0050766 (EC: IEA); GO_0050830 (EC: IDA, PMID: 15148336); GO_0051873 (EC: IEA) PMID: 1303250; 1304173; 1458688; 1672848; 1675710; 2450948; 2477486; 2477488; 2590164; 7634089; 7707811; 7982896; 8062452; 8206524; 8267903; 8666845; 9087411; 9476117; 9570553; 9743385; 9799711; 10368295; 10447262; 10578050; 10639434; 10725420; 10878362; 10888598; 10925294; 11023480; 11145046; 11196679; 11196698; 11255386; 11274270; 11302870; 11361219; 11393663; 11485744; 11487077; 11532276; 11549596; 11560994; 11564800; 11712863; 11737072; 11781711; 11804586; 11891230; 11906616; 11986203; 12047967; 12175909; 12370377; 12375325; 12393699; 12421953; 12439623; 12472676; 12477932; 12485445; 12487819; 12492252; 12517417; 12560567; 12595908; 12640191; 12641410; 12648279; 12651071; 12672193; 12699957; 12715245; 12761563; 12770793; 12847552; 12918709; 12921293; 12934195; 12941144; 12957407; 14564351; 14582818; 14669753; 14739370; 14764589; 14994386; 15061663; 15101708; 15117456; 15127191; 15144709; 15148336; 15148337; 15161763; 15249448; 15254284; 15292002; 15295097; 15306844; 15381182; 15381817; 15467537; 15472209; 15480986; 15488604; 15489334; 15516675; 15535834; 15572157; 15592292; 15627619; 15645196; 15647440; 15653690; 15674393; 15697204; 15723707; 15728497; 15730518; 15742161; 15753758; 15790942; 15829288; 15829302; 15838797; 15853952; 15855341; 15857180; 15888042; 15989776; 15994813; 16006058; 16029433; 16034120; 16046196; 16083697; 16094691; 16099048; 16099912; 16102832; 16105157; 16110781; 16112196; 16115848; 16152689; 16170752; 16178865; 16185324; 16200716; 16208516; 16214215; 16216673; 16220211; 16231358; 16256117; 16320344; 16369192; 16385451; 16385529; 16429424; 16439442; 16476012; 16487239; 16500704; 16517152; 16522396; 16553818; 16677572; 16681863; 16721783; 16729310; 16738667; 16750996; 16751976; 16792667; 16801331; 16827883; 16856624; 16911830; 16912583; 16916656; 16951387; 16953214; 16955210; 16960176; 17014624; 17044201; 17045187; 17071626; 17072973; 17083310; 17083312; 17092257; 17096357; 17133182; 17157384; 17174748; 17178888; 17195187; 17202308; 17222001; 17259116; 17266113; 17275645; 17289451; 17303612; 17311505; 17314117; 17337399; 17357060; 17380431; 17419286; 17439930; 17442667; 17442954; 17470593; 17478467; 17480019; 17482281; 17484222; 17496053; 17513174; 17552055; 17554527; 17559949; 17565323; 17567900; 17610319; 17610322; 17626901; 17634432; 17651383; 17652092; 17653692; 17659761; 17665457; 17678865; 17703412; 17763324; 17845414; 17846289; 17848669; 17855170; 17869647; 17872904; 17875183; 17896801; 17898783; 17921115; 17922403; 17942155; 17942372; 17990579; 18029348; 18031556; 18052966; 18082567; 18091754; 18166320; 18174230; 18177377; 18192915; 18194386; 18209939; 18211540; 18214570; 18221301; 18231631; 18288881; 18292811; 18317236; 18322223; 18334024; 18336595; 18347304; 18348874; 18361935; 18361938; 18368489; 18374983; 18396436; 18400978; 18415846; 18452612; 18455525; 18478332; 18486762; 18494378; 18495592; 18496832; 18498240; 18543229; 18552214; 18562462; 18582923; 18592362; 18596036; 18602571; 18602696; 18611155; 18612667; 18633131; 18637104; 18637753; 18641104; 18676680; 18700861; 18715406; 18727690; 18729778; 18754287; 18782274; 18818748; 18823346; 18831943; 18847375; 18927129; 18936436; 18950864; 18952132; 18957309; 18988385; 19019335; 19021583; 19035512; 19050632; 19056797; 19057812; 19064572; 19073229; 19083122; 19086549; 19094203; 19104434; 19139195; 19143554; 19161617; 19169708; 19170196; 19185543; 19199550; 19238444; 19252378; 19258923; 19273450; 19275921; 19276308; 19286845; 19307021; 19328949; 19336370; 19344414; 19352197; 19366862; 19371855; 19380618; 19408100; 19416237; 19423540; 19425063; 19430499; 19432958; 19465640; 19466271; 19467940; 19468207; 19477015; 19480845; 19481774; 19501100; 19517215; 19527514; 19540295; 19557622; 19580835; 19590686; 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21091907; 21106539; 21142772; 21171930; 21182784; 21192229; 21194488; 21203938; 21211797; 21281477; 21327568; 21334396; 21394075; 21488869; 21496252; 21510992; 21536088; 21544638; 21554230; 21557458; 21592999; 21640628; 21655939; 21681178; 21695215; 21702710; 21707593; 21722964; 21729275; 21733090; 21893516; 21895981; 21911261; 21920399; 21974696; 22002015; 22019001; 22022564; 22050689; 22050925; 22082351; 22131319; 22134613; 22172537; 22173059; 22183303; 22206649; 22215653; 22221294; 22225939; 22247351; 22258234; 22282660; 22296677; 22301353; 22302853; 22331020; 22335808; 22360648; 22363494; 22377282; 22380611; 22441636; 22444663; 22504420; 22512728; 22523362; 22578937; 22607836; 22633170; 22650645; 22673492; 22674410; 22762710; 22774989; 22813781; 22820623; 22848725; 22882323; 22938690; 22974720; 22994203; 23000376; 23000377; 23062612; 23065234; 23073041; 23094532; 23172101; 23225056; 23246423; 23289185; 23326517; 23348713; 23417614; 23423485; 23439277; 23448728; 23563916; 23602874; 23637788; 23662819; 23711995; 23741476; 23750697; 23806468; 23861212; 23911397; 24045948; 24047736; 24126531; 24227370; 24391218; 24429128 mannose-binding lectin (protein C) 2, soluble Ensembl:ENSG00000165471 HGNC:6922 HPRD:01107 MIM:154545 Vega:OTTHUMG00000150270 Other designations: collectin-1|mannan-binding lectin|mannose-binding lectin (protein C) 2, soluble (opsonic defect)|mannose-binding lectin 2, soluble (opsonic defect)|mannose-binding protein C MBL2 OGG:3000004189 Bin Zhao, Yue Liu, Oliver He ERdj4 MDG-1 MDG1 MST049 MSTP049 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB9 DnaJ (Hsp40) homolog, subfamily B, member 9 4189 UNQ743/PRO1471 7q31|14q24.2-q24.3 9606 7 GO_0005515 (EC: IPI, PMID:19815549); GO_0005730 (EC: ISS); GO_0005737 (EC: ISS); GO_0005783 (EC: IDA); GO_0005788 (EC: IEA); GO_0005789 (EC: TAS); GO_0006987 (EC: TAS); GO_0030433 (EC: IMP, PMID:18400946); GO_0030968 (EC: TAS); GO_0044267 (EC: TAS); GO_0051787 (EC: IDA, PMID:18400946); GO_0070062 (EC: IDA, PMID:19199708) PMID:9533036; 11042152; 11147971; 11230166; 11256614; 11525638; 11836248; 12356756; 12477932; 12581160; 12690205; 12975309; 14516790; 14559994; 14702039; 15456888; 15489334; 15882996; 16169070; 16205636; 16344560; 17132139; 17936241; 18400946; 18431251; 19123479; 19199708; 19322201; 19815549; 20054003; 20335527; 20554776; 20682791; 21906983; 21988832; 22006218; 24250222 DnaJ (Hsp40) homolog, subfamily B, member 9 Ensembl:ENSG00000128590 HGNC:6968 HPRD:07047 MIM:602634 Vega:OTTHUMG00000154866 Other designations: ER-resident protein ERdj4|dnaJ homolog subfamily B member 9|endoplasmic reticulum DNA J domain-containing protein 4|endoplasmic reticulum DnaJ homolog 4|microvascular endothelial differentiation gene 1 protein DNAJB9 OGG:3000004193 Bin Zhao, Yue Liu, Oliver He ACTFS HDMX hdm2 WEB: http://www.ncbi.nlm.nih.gov/gene MDM2 MDM2 oncogene, E3 ubiquitin protein ligase 4193 12q14.3-q15 9606 12 Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 9271120); GO_0002039 (EC: IPI, PMID: 15053879); GO_0004842 (EC: IDA, PMID: 9450543); GO_0004842 (EC: IMP, PMID: 19372219); GO_0005515 (EC: IPI, PMID: 10196247); GO_0005634 (EC: IDA, PMID: 10360174); GO_0005634 (EC: IMP); GO_0005654 (EC: IDA, PMID: 10707090); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, PMID: 10707090); GO_0005737 (EC: IMP); GO_0005829 (EC: TAS); GO_0005886 (EC: TAS); GO_0006461 (EC: IDA, PMID: 10608892); GO_0006977 (EC: IMP); GO_0006977 (EC: TAS); GO_0007089 (EC: IEA); GO_0007173 (EC: TAS); GO_0007268 (EC: TAS); GO_0008270 (EC: IDA, PMID: 10722742); GO_0008284 (EC: TAS, PMID: 7791904); GO_0008543 (EC: TAS); GO_0009743 (EC: IEA); GO_0010039 (EC: IEA); GO_0010628 (EC: IEA); GO_0010955 (EC: IEA); GO_0016032 (EC: IEA); GO_0016567 (EC: IDA, PMID: 15878855); GO_0016604 (EC: IDA, Qualifier: colocalizes_with, PMID: 10360174); GO_0018205 (EC: IMP, PMID: 19372219); GO_0019899 (EC: IPI, PMID: 15577914); GO_0030666 (EC: TAS); GO_0031625 (EC: IPI, PMID: 18382127); GO_0031648 (EC: IDA, PMID: 10360174); GO_0032026 (EC: IEA); GO_0032436 (EC: IDA, PMID: 11278372); GO_0034504 (EC: IDA, PMID: 10360174); GO_0038095 (EC: TAS); GO_0042176 (EC: IDA, PMID: 9153395); GO_0042220 (EC: IEA); GO_0042493 (EC: IEA); GO_0042787 (EC: IDA, PMID: 11278372); GO_0042802 (EC: IPI, PMID: 17159902); GO_0042975 (EC: IEA); GO_0043066 (EC: IEA); GO_0043154 (EC: IEA); GO_0043234 (EC: IDA, PMID: 9529249); GO_0043278 (EC: IEA); GO_0043518 (EC: IDA, PMID: 10360174); GO_0045087 (EC: TAS); GO_0045184 (EC: IDA, PMID: 10360174); GO_0045202 (EC: IEA); GO_0045472 (EC: IEA); GO_0045892 (EC: IDA, PMID: 9271120); GO_0045931 (EC: IMP, PMID: 17290220); GO_0046677 (EC: IEP); GO_0046827 (EC: IEA); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0070301 (EC: IEA); GO_0071157 (EC: IDA, PMID: 9529249); GO_0071229 (EC: IEA); GO_0071236 (EC: IEA); GO_0071301 (EC: IEA); GO_0071312 (EC: IEA); GO_0071375 (EC: IEA); GO_0071391 (EC: IEA); GO_0071456 (EC: IEP); GO_0071494 (EC: IEA); GO_0097110 (EC: IEA) PMID: 1535557; 1614537; 7590734; 7606365; 7651818; 7686617; 7689721; 7791904; 7935455; 8058315; 8064888; 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20871633; 20874444; 20875869; 20881839; 20922573; 20930521; 20935493; 20948295; 20951946; 20972445; 20972456; 20979563; 21034743; 21047201; 21048031; 21051533; 21051655; 21057548; 21060154; 21071676; 21080085; 21081495; 21081496; 21084285; 21084564; 21088494; 21092204; 21093410; 21097889; 21098709; 21113617; 21132010; 21133853; 21149449; 21157430; 21170087; 21183956; 21191186; 21204735; 21209460; 21211512; 21229604; 21261729; 21268124; 21285945; 21290342; 21295542; 21305319; 21316347; 21316605; 21317463; 21317535; 21317707; 21317885; 21333377; 21336260; 21338495; 21339197; 21386656; 21389118; 21399665; 21402876; 21404460; 21444629; 21451571; 21454483; 21455220; 21460101; 21466165; 21477265; 21478269; 21479369; 21503588; 21504894; 21525355; 21530075; 21539745; 21547352; 21561866; 21565629; 21572037; 21602883; 21624367; 21647873; 21656578; 21665242; 21667122; 21685937; 21706156; 21725357; 21725850; 21726810; 21743494; 21750659; 21756282; 21761395; 21768776; 21770737; 21785463; 21804542; 21814224; 21822304; 21833626; 21844567; 21852383; 21862876; 21867960; 21877955; 21887275; 21890473; 21896991; 21900752; 21903592; 21906983; 21925390; 21925707; 21930127; 21933600; 21957016; 21963094; 21965653; 21982800; 21986495; 21986500; 21988832; 21990374; 22004076; 22004425; 22032989; 22038760; 22047081; 22056306; 22081073; 22083959; 22085928; 22095636; 22103682; 22104152; 22108807; 22120712; 22124327; 22128911; 22134502; 22137485; 22157679; 22173032; 22180099; 22180176; 22187011; 22195963; 22197810; 22205265; 22244827; 22245141; 22264786; 22266832; 22266850; 22266868; 22285926; 22290440; 22292622; 22301280; 22301498; 22301501; 22310835; 22318725; 22330136; 22331460; 22333590; 22336889; 22336942; 22337874; 22343716; 22349818; 22350919; 22379189; 22383580; 22391559; 22397410; 22410433; 22411991; 22413855; 22444248; 22467100; 22472959; 22487680; 22487911; 22493164; 22505724; 22510592; 22525275; 22558411; 22563815; 22566641; 22575647; 22586610; 22591662; 22593196; 22609775; 22634534; 22659184; 22668018; 22672907; 22685613; 22699518; 22701761; 22705356; 22710720; 22716509; 22729912; 22733537; 22737255; 22744426; 22773013; 22777350; 22787160; 22797925; 22807444; 22819825; 22825724; 22825850; 22842367; 22843172; 22844496; 22869143; 22892142; 22902369; 22902907; 22907703; 22912717; 22914606; 22914926; 22916154; 22916255; 22938470; 22939400; 22940738; 22976441; 22989009; 23028042; 23039052; 23039163; 23044487; 23045280; 23060298; 23089923; 23092970; 23096687; 23113306; 23132866; 23134341; 23139272; 23145162; 23147543; 23150668; 23159155; 23167335; 23167337; 23169665; 23201157; 23210739; 23218882; 23238568; 23244604; 23246961; 23252402; 23259295; 23260144; 23261415; 23292895; 23303139; 23318437; 23324352; 23347235; 23352573; 23356517; 23359199; 23383041; 23383273; 23391506; 23393136; 23405218; 23416275; 23423487; 23425231; 23437037; 23438693; 23451111; 23483203; 23506010; 23506213; 23529275; 23563151; 23564787; 23572512; 23609977; 23624782; 23652204; 23661019; 23671280; 23677067; 23679294; 23728348; 23745682; 23747528; 23749209; 23776060; 23776465; 23777425; 23786219; 23802716; 23826318; 23826411; 23837945; 23845465; 23870475; 23871895; 23874713; 23912932; 23933584; 23934659; 23946421; 23979978; 23982177; 23994832; 24003224; 24018792; 24027430; 24061453; 24143256; 24163099; 24167073; 24174547; 24240108; 24314634; 24325471; 24361594; 24413081; 24413661 MDM2 oncogene, E3 ubiquitin protein ligase Ensembl:ENSG00000135679 HGNC:6973 HPRD:01272 MIM:164785 Vega:OTTHUMG00000142827 Other designations: E3 ubiquitin-protein ligase Mdm2|Mdm2, p53 E3 ubiquitin protein ligase homolog|Mdm2, transformed 3T3 cell double minute 2, p53 binding protein|double minute 2, human homolog of; p53-binding protein|oncoprotein Mdm2 MDM2 gene OGG:3000004199 Bin Zhao, Yue Liu, Oliver He HUMNDME MES WEB: http://www.ncbi.nlm.nih.gov/gene ME1 malic enzyme 1, NADP(+)-dependent, cytosolic 4199 6q12 9606 6 Official from a nomenclature committee GO_0004470 (EC: IDA, PMID: 7622060); GO_0004471 (EC: IEA); GO_0004473 (EC: IDA, PMID: 8187880); GO_0004473 (EC: ISS); GO_0005739 (EC: IEA); GO_0005829 (EC: ISS); GO_0005829 (EC: TAS); GO_0005975 (EC: NAS, PMID: 8187880); GO_0006108 (EC: IDA, PMID: 7622060); GO_0006741 (EC: TAS, PMID: 8187880); GO_0008948 (EC: IEA); GO_0009055 (EC: TAS, PMID: 7622060); GO_0009725 (EC: ISS); GO_0009743 (EC: TAS, PMID: 8187880); GO_0030145 (EC: IDA, PMID: 7622060); GO_0043531 (EC: TAS, PMID: 7622060); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0050661 (EC: TAS, PMID: 7622060); GO_0051262 (EC: IEA); GO_0051287 (EC: TAS, PMID: 7622060) PMID: 1088824; 2015102; 3169368; 4689040; 7496989; 7622060; 7757881; 8125298; 8187880; 8804575; 9174159; 11085912; 11352855; 11358520; 12121650; 12477932; 14574404; 15489334; 16344560; 16757477; 18029348; 18660489; 19293334; 19416979; 19464998; 20877624; 21139048; 21555518; 21890473; 21906983; 21963094; 22456781; 22863883; 23114090; 23284632; 23334421 malic enzyme 1, NADP(+)-dependent, cytosolic Ensembl:ENSG00000065833 HGNC:6983 HPRD:01102 MIM:154250 Vega:OTTHUMG00000015111 Other designations: Malic enzyme, cytoplasmic|NADP-ME|NADP-dependent malic enzyme|malate dehydrogenase|malic enzyme 1, soluble|pyruvic-malic carboxylase ME1 OGG:3000004257 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene microsomal glutathione S-transferase 1 4257 9606 Official from a nomenclature committee GO_0004364 (EC: IDA); GO_0004602 (EC: IDA); GO_0005515 (EC: IPI); GO_0005634 (EC: IEA); GO_0005739 (EC: IDA); GO_0005741 (EC: IEA); GO_0005743 (EC: IEA); GO_0005778 (EC: ISS); GO_0005783 (EC: ISS); GO_0005789 (EC: TAS); GO_0006749 (EC: IEA); GO_0006805 (EC: TAS); GO_0010243 (EC: IEA); GO_0016021 (EC: ISS); GO_0032496 (EC: IEA); GO_0033327 (EC: IEA); GO_0042493 (EC: IEA); GO_0042803 (EC: IEA); GO_0043295 (EC: IEA); GO_0044281 (EC: TAS); ... (Note: Only 20 GO IDs shown. See more from web page source or RDF output.)" PMID: 1544849; 2307478; 3372534; 7566098; 7663172; 8812420; 10095775; 10524215; 10673221; 10777602; 11034337; 11587073; 11752456; 12359356; 12477932; 12818425; 14726533; 15338373; 15489334; 16384981; 17483957; 17714764; 18781797; 19343046; 20195357; 20727966; 21139048; 21963094; 22589738; 23314968; 23805041 microsomal glutathione S-transferase 1 Ensembl:ENSG00000008394 HGNC:7061 HPRD:00705 MIM:138330 Vega:OTTHUMG00000168816 MGST1 OGG:3000004258 Bin Zhao, Yue Liu, Oliver He GST2 MGST-II WEB: http://www.ncbi.nlm.nih.gov/gene microsomal glutathione S-transferase 2 4258 9606 Official from a nomenclature committee GO_0004364 (EC: IDA, PMID: 8703034); GO_0004464 (EC: IDA, PMID: 8703034); GO_0004602 (EC: IBA); GO_0005635 (EC: IBA); GO_0005789 (EC: TAS); GO_0005886 (EC: IDA, PMID: 9092565); GO_0006750 (EC: IDA, PMID: 8703034); GO_0006805 (EC: TAS); GO_0008047 (EC: IEA); GO_0010243 (EC: IEA); GO_0016021 (EC: IEA); GO_0019370 (EC: IDA, PMID: 8703034); GO_0032496 (EC: IEA); GO_0043231 (EC: IDA, PMID: 8703034); GO_0044281 (EC: TAS); GO_0055114 (EC: IBA); GO_1901687 (EC: TAS) PMID: 8703034; 8889549; 9092565; 9278457; 9302651; 10673221; 11322876; 12477932; 15489334; 16169070; 16344560; 16498398; 16773312; 19343046; 20379614; 23409838 microsomal glutathione S-transferase 2 Ensembl:ENSG00000085871 HGNC:7063 HPRD:03436 MIM:601733 MGST2 OGG:3000004259 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene microsomal glutathione S-transferase 3 4259 9606 Official from a nomenclature committee GO_0004364 (EC: IBA); GO_0004601 (EC: TAS, PMID: 9278457); GO_0004602 (EC: IBA); GO_0005635 (EC: IBA); GO_0005789 (EC: TAS); GO_0006629 (EC: TAS, PMID: 9278457); GO_0006805 (EC: TAS); GO_0007165 (EC: TAS, PMID: 9278457); GO_0016020 (EC: TAS, PMID: 9278457); GO_0016021 (EC: IEA); GO_0043231 (EC: TAS, PMID: 9278457); GO_0044281 (EC: TAS); GO_0055114 (EC: IBA); GO_0055114 (EC: TAS, PMID: 9278457); GO_1901687 (EC: TAS) PMID: 8125298; 9278457; 10673221; 12477932; 12898215; 15489334; 16169070; 16710414; 17207965; 17719568; 18781797; 19064610; 19322201; 19343046; 19471022; 19536175; 20360068; 20379614; 21116278; 21139048; 21853274; 21890473; 21906983; 21963094; 22939629; 24250222 microsomal glutathione S-transferase 3 Ensembl:ENSG00000143198 HGNC:7064 HPRD:05192 MIM:604564 Vega:OTTHUMG00000034627 MGST3 OGG:3000004313 Bin Zhao, Yue Liu, Oliver He CLG4 CLG4A MMP-II MONA TBE-1 WEB: http://www.ncbi.nlm.nih.gov/gene MMP2 matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase) 4313 16q13-q21 9606 16 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0001666 (EC: IEA); GO_0001955 (EC: IEA); GO_0001957 (EC: IEA); GO_0004222 (EC: IEA); GO_0004252 (EC: TAS); GO_0005515 (EC: IPI); GO_0005576 (EC: TAS); GO_0005578 (EC: IEA); GO_0005615 (EC: IDA, PMID: 18492766); GO_0005634 (EC: IEA); GO_0005739 (EC: IEA); GO_0005886 (EC: IEA); GO_0006508 (EC: TAS, PMID: 2834383); GO_0007566 (EC: IEA); GO_0008270 (EC: IEA); GO_0022617 (EC: TAS); GO_0030017 (EC: IEA); GO_0030198 (EC: TAS); GO_0030574 (EC: TAS); GO_0044267 (EC: TAS); GO_0060325 (EC: IEA); GO_0060346 (EC: IEA); GO_0071230 (EC: IEA) PMID: 1460022; 1846313; 1851724; 2071140; 2158484; 2162831; 2834383; 7523391; 7583664; 7683678; 7694569; 7782289; 7935812; 7947821; 7998967; 8549817; 8663297; 8663332; 8692946; 8862926; 9119036; 9148753; 9182583; 9343394; 9344465; 9438380; 9640131; 9699154; 9737711; 9853262; 9933646; 10196161; 10356396; 10419448; 10551873; 10652000; 10652271; 10900205; 10947989; 10986281; 10991943; 11114309; 11134507; 11168762; 11179305; 11220743; 11368514; 11382769; 11420387; 11431697; 11485914; 11571304; 11598182; 11728453; 11748988; 11756567; 11762702; 11782389; 11790786; 11792711; 11824472; 11833938; 11839588; 11844598; 11854622; 11889208; 11895494; 11918086; 11920503; 11928808; 11928813; 11929863; 11935310; 11948127; 11956628; 11961384; 12007723; 12023034; 12029498; 12032297; 12034345; 12039803; 12077518; 12085233; 12087091; 12103254; 12115722; 12122099; 12147229; 12147339; 12149192; 12193399; 12194986; 12198653; 12225805; 12235151; 12371906; 12372458; 12374789; 12376362; 12393408; 12393872; 12431239; 12438229; 12439941; 12451991; 12470034; 12471459; 12473650; 12475252; 12477932; 12479097; 12486137; 12522578; 12559990; 12569569; 12586836; 12587534; 12589095; 12601782; 12602913; 12614934; 12615834; 12632066; 12632084; 12642591; 12651627; 12657623; 12676736; 12684625; 12753080; 12764090; 12810672; 12832446; 12845641; 12861074; 12873995; 12878157; 12879005; 12880418; 12914776; 12939660; 12952836; 12967855; 12970394; 12970724; 14500349; 14519487; 14520690; 14580155; 14583471; 14604886; 14614057; 14644155; 14644777; 14661256; 14666611; 14679018; 14694003; 14697951; 14710472; 14713104; 14732714; 14744781; 14766248; 14871985; 14973177; 14981939; 14982725; 14983226; 14990702; 14990972; 14996438; 15004438; 15009703; 15015767; 15051038; 15056834; 15067014; 15102849; 15146192; 15165255; 15201662; 15241180; 15248212; 15248826; 15250832; 15254682; 15255544; 15265790; 15271946; 15277330; 15280384; 15280448; 15317806; 15317818; 15351863; 15375490; 15381707; 15449075; 15475447; 15485653; 15489233; 15489334; 15492291; 15522165; 15541021; 15557756; 15567754; 15569994; 15604254; 15609121; 15609318; 15609323; 15616792; 15621117; 15632190; 15637056; 15651999; 15665288; 15665394; 15672417; 15691365; 15731163; 15743799; 15754118; 15756447; 15820246; 15831360; 15841469; 15866216; 15878967; 15885317; 15904490; 15911696; 15929171; 15944607; 15949313; 15955221; 15955448; 15955449; 15983226; 15998676; 15998788; 16005367; 16018746; 16023005; 16023011; 16042227; 16082623; 16083752; 16097959; 16134528; 16142392; 16142692; 16146757; 16158251; 16168111; 16188099; 16188574; 16213873; 16260653; 16275157; 16306050; 16308106; 16313894; 16338908; 16339461; 16341461; 16344560; 16356191; 16359987; 16361361; 16364202; 16379022; 16407830; 16413616; 16414983; 16424893; 16425263; 16438723; 16453304; 16456793; 16458924; 16476613; 16510149; 16551362; 16575904; 16585124; 16615109; 16647062; 16718267; 16718824; 16722933; 16728425; 16739355; 16755991; 16772717; 16776850; 16778129; 16803520; 16829143; 16840178; 16884384; 16888681; 16891619; 16894529; 16897078; 16919028; 16940985; 16961137; 16967187; 16987162; 17000679; 17008230; 17012225; 17029196; 17033924; 17065436; 17067460; 17070879; 17071711; 17081126; 17088079; 17088321; 17089188; 17099140; 17109104; 17151781; 17175151; 17177839; 17178858; 17181997; 17182940; 17188706; 17189319; 17203213; 17203468; 17205957; 17208328; 17217338; 17226791; 17236757; 17237723; 17243139; 17258390; 17265493; 17289174; 17299802; 17299841; 17314270; 17320450; 17326127; 17335808; 17350093; 17357514; 17363400; 17364896; 17367869; 17374529; 17377415; 17383306; 17384031; 17409012; 17429393; 17435175; 17437609; 17448043; 17473191; 17486447; 17487426; 17488654; 17493172; 17493602; 17516913; 17540340; 17541305; 17545513; 17546628; 17559909; 17563705; 17564313; 17570740; 17589947; 17593815; 17607721; 17611666; 17613170; 17616173; 17623663; 17624083; 17624726; 17638886; 17640671; 17650671; 17653824; 17660250; 17661346; 17666398; 17671679; 17678975; 17680282; 17699594; 17706116; 17706812; 17718386; 17725804; 17786346; 17845054; 17851253; 17876296; 17879021; 17886098; 17893005; 17893430; 17901377; 17908800; 17923814; 17943549; 17949555; 17950725; 17958893; 17962725; 17972522; 17981679; 17986062; 18000234; 18025061; 18029348; 18031543; 18035073; 18035727; 18038907; 18042068; 18045645; 18049448; 18052707; 18062285; 18063683; 18069632; 18070420; 18081721; 18088350; 18091353; 18093986; 18155181; 18160708; 18166633; 18172354; 18177474; 18177649; 18182154; 18185989; 18187184; 18194849; 18205826; 18208802; 18210196; 18214299; 18217401; 18220784; 18236174; 18251742; 18253117; 18256065; 18265895; 18283635; 18288638; 18288718; 18291374; 18292822; 18292932; 18295959; 18298353; 18308831; 18314110; 18329693; 18330957; 18332090; 18332634; 18337444; 18340378; 18359774; 18366007; 18378414; 18398039; 18400453; 18424416; 18425389; 18426670; 18431027; 18438431; 18444803; 18455130; 18462748; 18468407; 18469019; 18472160; 18473733; 18477480; 18483282; 18492766; 18496568; 18498066; 18506186; 18543216; 18552985; 18560213; 18575776; 18579756; 18580857; 18593949; 18597705; 18611410; 18618693; 18627313; 18636124; 18641922; 18644390; 18644862; 18651826; 18652765; 18653973; 18663625; 18664479; 18665467; 18670324; 18683733; 18692810; 18701818; 18707587; 18711060; 18712166; 18713744; 18714566; 18757369; 18773430; 18782525; 18784838; 18802398; 18802702; 18805052; 18814268; 18818748; 18829111; 18829229; 18835646; 18852494; 18937938; 18940384; 18946196; 18950008; 18971037; 18971427; 18974156; 19007982; 19019335; 19020757; 19022775; 19088110; 19088827; 19094228; 19100442; 19101987; 19105397; 19109975; 19116140; 19117773; 19121849; 19122458; 19124506; 19132754; 19134348; 19141395; 19159011; 19165813; 19176371; 19188819; 19189315; 19191857; 19196101; 19199380; 19212830; 19221481; 19223381; 19236750; 19241124; 19243899; 19248107; 19249761; 19266599; 19274436; 19281093; 19286653; 19287959; 19288452; 19295411; 19303106; 19324884; 19330734; 19331801; 19332048; 19337556; 19338750; 19345347; 19358835; 19360430; 19386107; 19391484; 19395678; 19426551; 19438747; 19445018; 19448672; 19449375; 19454611; 19455469; 19459623; 19460733; 19464975; 19465902; 19466389; 19469865; 19477063; 19484988; 19507256; 19515587; 19523650; 19523958; 19525975; 19527514; 19528914; 19529860; 19546837; 19551542; 19551856; 19560452; 19562509; 19574670; 19575173; 19577357; 19578796; 19580633; 19581306; 19594729; 19610062; 19615732; 19617223; 19617714; 19625121; 19637058; 19643940; 19653001; 19671357; 19682073; 19687355; 19698156; 19700865; 19709349; 19716817; 19723042; 19723139; 19724860; 19724922; 19731823; 19760465; 19780834; 19786072; 19787626; 19789190; 19814619; 19816602; 19820359; 19821096; 19853299; 19861308; 19874467; 19875168; 19875755; 19885578; 19887570; 19889076; 19901964; 19903768; 19903858; 19913121; 19921476; 19930715; 19939245; 19954064; 19956847; 19995403; 19995435; 19997654; 20003765; 20021962; 20021964; 20031158; 20044778; 20064641; 20071690; 20082877; 20091096; 20100617; 20110530; 20113256; 20129576; 20133364; 20138860; 20140262; 20145123; 20160036; 20175118; 20195229; 20207476; 20211062; 20211065; 20216978; 20219012; 20222942; 20230421; 20233617; 20305284; 20333791; 20346360; 20353950; 20360147; 20364697; 20372784; 20375027; 20381119; 20382120; 20394501; 20404912; 20416077; 20432471; 20435584; 20450704; 20452482; 20453000; 20453486; 20455995; 20473759; 20482566; 20484597; 20485444; 20501419; 20501425; 20510080; 20514432; 20514437; 20514447; 20529817; 20541540; 20563853; 20565774; 20576603; 20586027; 20587546; 20590473; 20600798; 20616161; 20616708; 20625418; 20625691; 20628086; 20628624; 20634891; 20646497; 20646600; 20652762; 20654108; 20654122; 20672350; 20673868; 20685029; 20717917; 20724289; 20725135; 20730428; 20730561; 20808730; 20811691; 20843706; 20845079; 20855151; 20864363; 20887714; 20889295; 20921293; 20932173; 20936527; 20936699; 20937816; 20948207; 20963502; 20970160; 20977637; 21041295; 21041693; 21045016; 21048031; 21053100; 21086628; 21103065; 21104439; 21104440; 21116502; 21142815; 21145461; 21147512; 21148629; 21151391; 21165404; 21174062; 21174909; 21193558; 21205070; 21206012; 21212676; 21228795; 21229878; 21248144; 21261731; 21264536; 21265099; 21276823; 21277149; 21307882; 21316839; 21331614; 21334717; 21336947; 21343160; 21344498; 21349701; 21359202; 21378341; 21393869; 21397857; 21401309; 21418186; 21421877; 21427648; 21432777; 21437624; 21453685; 21454822; 21461859; 21463121; 21471148; 21478099; 21483125; 21489023; 21503582; 21515251; 21516345; 21524920; 21526499; 21531813; 21541352; 21541674; 21565179; 21569377; 21574189; 21575462; 21576412; 21590355; 21611838; 21612407; 21620625; 21620672; 21624249; 21624510; 21627988; 21630198; 21637818; 21641389; 21656154; 21661398; 21667117; 21681346; 21687932; 21694463; 21705840; 21707819; 21712445; 21721010; 21722821; 21723775; 21734530; 21735328; 21745270; 21750404; 21756063; 21760911; 21764444; 21777461; 21782323; 21784671; 21794897; 21813640; 21820153; 21839835; 21842128; 21857898; 21858102; 21858104; 21880183; 21889192; 21901248; 21908153; 21909361; 21924036; 21928345; 21938405; 21956669; 21957576; 21958210; 21965295; 21968416; 21969874; 21989104; 21993452; 22006368; 22010139; 22020421; 22024074; 22030137; 22072145; 22082680; 22094096; 22110735; 22117411; 22169692; 22199296; 22200256; 22200661; 22200690; 22200710; 22204652; 22212960; 22227305; 22237453; 22252755; 22286800; 22288519; 22289521; 22291969; 22302011; 22303700; 22309692; 22323339; 22327101; 22327326; 22336124; 22342364; 22349830; 22374248; 22391064; 22396544; 22402435; 22406112; 22428754; 22448134; 22451655; 22455335; 22460086; 22472880; 22490679; 22490851; 22493443; 22509276; 22513045; 22513785; 22515887; 22519916; 22522455; 22527932; 22527933; 22531681; 22532131; 22534113; 22534634; 22546345; 22550139; 22551568; 22577146; 22580443; 22590832; 22591362; 22618590; 22634718; 22642972; 22646815; 22651889; 22652796; 22659470; 22669775; 22672240; 22684547; 22694915; 22707264; 22727191; 22783577; 22785600; 22820140; 22835601; 22836342; 22846578; 22848537; 22863019; 22865631; 22876575; 22883193; 22883459; 22898815; 22901190; 22931588; 22936257; 22938472; 22951829; 22959677; 22960198; 22964525; 22968857; 22985025; 23005037; 23006733; 23013132; 23038275; 23043936; 23057632; 23059760; 23064462; 23093058; 23096596; 23098370; 23100088; 23107277; 23107342; 23114726; 23134156; 23136827; 23146278; 23158991; 23164104; 23166329; 23171686; 23184003; 23201304; 23205572; 23220260; 23232575; 23242659; 23254288; 23257253; 23261429; 23264224; 23271497; 23271813; 23273944; 23280016; 23292837; 23306155; 23313298; 23320481; 23333895; 23343958; 23349885; 23357697; 23364396; 23375518; 23378725; 23381805; 23384723; 23387827; 23388341; 23388475; 23390835; 23395821; 23412981; 23424616; 23428182; 23440286; 23465389; 23494562; 23498792; 23510467; 23510472; 23516489; 23544610; 23557756; 23559867; 23566884; 23577575; 23588386; 23613407; 23623988; 23637955; 23650722; 23651923; 23660954; 23661021; 23661254; 23663265; 23673111; 23676485; 23685894; 23696025; 23696797; 23705892; 23716178; 23725476; 23736018; 23737137; 23763335; 23766685; 23768069; 23773714; 23791966; 23793312; 23796708; 23807209; 23814095; 23814098; 23817219; 23819399; 23832737; 23847438; 23852912; 23855590; 23870474; 23886165; 23897811; 23915070; 23915071; 23922934; 23936390; 24037915; 24047437; 24062440; 24067484; 24122234; 24164447; 24297171; 24335416; 24344010; 24374173; 24479343; 24479348 matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase) Ensembl:ENSG00000087245 HGNC:7166 HPRD:00386 MIM:120360 Vega:OTTHUMG00000133202 Other designations: 72 kDa gelatinase|72 kDa type IV collagenase|MMP-2|collagenase type IV-A|gelatinase A|matrix metalloproteinase-2|matrix metalloproteinase-II|neutrophil gelatinase MMP2 gene OGG:3000004318 Bin Zhao, Yue Liu, Oliver He CLG4B GELB MANDP2 MMP-9 WEB: http://www.ncbi.nlm.nih.gov/gene MMP9 matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase) 4318 20q11.2-q13.1 9606 20 Official from a nomenclature committee GO_0001501 (EC: IEA); GO_0001503 (EC: IEA); GO_0004222 (EC: IDA, PMID: 16192646); GO_0005515 (EC: IPI, PMID: 16512877); GO_0005518 (EC: TAS, PMID: 2251898); GO_0005576 (EC: TAS); GO_0005578 (EC: IEA); GO_0005615 (EC: IDA, PMID: 2251898); GO_0006508 (EC: IDA, PMID: 2551898); GO_0007566 (EC: IEA); GO_0008270 (EC: TAS, PMID: 2251898); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0030225 (EC: TAS, PMID: 2251898); GO_0030574 (EC: TAS); GO_0042802 (EC: IPI); GO_0043065 (EC: IEA); GO_0050900 (EC: IEA); GO_0051549 (EC: IMP, PMID: 17704059) PMID: 1281792; 1371271; 1400481; 1645657; 1653055; 1653238; 1851724; 1932376; 2158484; 2251898; 2551898; 7669817; 7694569; 7762981; 7896811; 8012988; 8216228; 8426746; 8568270; 8691515; 8978762; 9261109; 9268487; 9344465; 9360944; 9378998; 9578462; 9590175; 9789069; 9878537; 10095777; 10339412; 10389762; 10419448; 10580107; 10598806; 10636480; 10642956; 10644727; 10652271; 10706134; 10796887; 10859319; 10900205; 10988146; 11023497; 11081634; 11134254; 11168762; 11179305; 11279011; 11410119; 11468147; 11486009; 11546917; 11557670; 11576356; 11606713; 11675412; 11688724; 11708786; 11742492; 11756567; 11780052; 11781819; 11813159; 11827795; 11827968; 11830485; 11833938; 11839588; 11839746; 11854622; 11875051; 11876767; 11890521; 11916008; 11920503; 11920505; 11935310; 11940298; 11956628; 11958288; 11971760; 11978564; 11986939; 11994547; 11999552; 12004062; 12029498; 12034345; 12050187; 12051944; 12054499; 12062817; 12063180; 12077439; 12081477; 12082590; 12082592; 12084167; 12103254; 12105194; 12126625; 12127674; 12183836; 12193399; 12205736; 12208863; 12219015; 12231534; 12235127; 12235151; 12356580; 12372334; 12376362; 12398893; 12414663; 12431239; 12431981; 12437116; 12443715; 12444074; 12452001; 12464265; 12471459; 12477932; 12479097; 12479099; 12559990; 12569569; 12586837; 12587534; 12589095; 12606037; 12612199; 12615834; 12626459; 12642591; 12651627; 12663332; 12668489; 12671895; 12704537; 12712078; 12717622; 12717827; 12724312; 12727228; 12728308; 12745093; 12750540; 12753719; 12769333; 12789238; 12791318; 12810681; 12811828; 12824186; 12830465; 12847101; 12850503; 12861851; 12865405; 12866035; 12874388; 12879005; 12880418; 12914776; 12921631; 12947332; 12949792; 12950257; 12952836; 12958623; 12960156; 12960961; 12967855; 12970724; 14500349; 14520690; 14550288; 14550924; 14551878; 14561155; 14581136; 14605329; 14607966; 14624478; 14633819; 14644158; 14661062; 14661256; 14675172; 14676438; 14681642; 14687896; 14697951; 14705229; 14719079; 14744773; 14766231; 14767860; 14963289; 14973177; 14981939; 14982353; 14983226; 14990702; 15009705; 15015767; 15022328; 15033492; 15034761; 15064242; 15067014; 15070833; 15075244; 15084374; 15085249; 15094060; 15105396; 15118287; 15122332; 15123665; 15131051; 15132991; 15146197; 15165255; 15169910; 15191941; 15201662; 15204835; 15212936; 15214991; 15223247; 15239215; 15241180; 15247301; 15248826; 15254682; 15256791; 15265790; 15271946; 15277439; 15288392; 15311942; 15313474; 15316122; 15327032; 15328199; 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20673868; 20674181; 20699364; 20704821; 20707923; 20707992; 20725135; 20725776; 20725790; 20732728; 20800577; 20800911; 20802378; 20808730; 20812964; 20813982; 20818082; 20824409; 20825973; 20827608; 20837483; 20838751; 20842516; 20843706; 20853162; 20857147; 20864363; 20872564; 20878580; 20889295; 20923324; 20936527; 20936699; 20937775; 20942234; 20948207; 20957628; 20960272; 20964870; 20970160; 20971661; 20971732; 20977848; 21034616; 21039753; 21041986; 21044610; 21047774; 21048031; 21081040; 21086628; 21089052; 21089054; 21094936; 21103065; 21106094; 21108787; 21116502; 21120482; 21128246; 21135557; 21136273; 21143201; 21146069; 21147512; 21148633; 21150136; 21151179; 21159039; 21159820; 21162890; 21165404; 21170498; 21170718; 21174909; 21187089; 21190541; 21194909; 21195432; 21205837; 21208653; 21212676; 21222132; 21227015; 21229878; 21231907; 21232745; 21238444; 21244504; 21249198; 21254649; 21261731; 21265099; 21274725; 21277149; 21277671; 21279695; 21283828; 21288887; 21305678; 21321391; 21336947; 21349701; 21354279; 21355964; 21367627; 21371122; 21376533; 21389674; 21391238; 21391788; 21393869; 21401309; 21424088; 21425178; 21425912; 21427648; 21428178; 21429222; 21430243; 21437624; 21437990; 21439274; 21442180; 21454378; 21454822; 21455563; 21455583; 21455597; 21461577; 21461859; 21462131; 21463121; 21473134; 21481333; 21485219; 21491088; 21496113; 21503582; 21503589; 21505993; 21506705; 21515251; 21516345; 21519142; 21525012; 21535601; 21541352; 21541674; 21550738; 21553521; 21557297; 21559401; 21559835; 21565179; 21567393; 21574189; 21577212; 21600177; 21601305; 21612954; 21616098; 21620482; 21620625; 21620672; 21621856; 21624249; 21641584; 21652634; 21655354; 21663729; 21664966; 21667159; 21672616; 21676452; 21678108; 21681346; 21687932; 21707819; 21707906; 21710351; 21710717; 21717058; 21718298; 21721010; 21723775; 21726963; 21733941; 21735328; 21737808; 21740772; 21742938; 21750188; 21752154; 21760532; 21760911; 21762266; 21763143; 21764478; 21764480; 21777517; 21781516; 21791204; 21802713; 21813510; 21814723; 21819758; 21824169; 21833719; 21839130; 21840940; 21842128; 21844877; 21855630; 21857898; 21857935; 21860087; 21861843; 21867689; 21872914; 21873432; 21881840; 21882477; 21889192; 21900582; 21913037; 21915713; 21922298; 21923032; 21928345; 21933581; 21933988; 21936677; 21940962; 21946941; 21956669; 21957576; 21958210; 21959615; 21963461; 21963570; 21963718; 21965756; 21969093; 21975935; 21983728; 21989104; 21993004; 21993452; 22005258; 22009750; 22020222; 22027013; 22030137; 22041445; 22052126; 22053594; 22086927; 22092736; 22094096; 22094285; 22107133; 22112973; 22113040; 22116092; 22117411; 22118839; 22121096; 22126484; 22132194; 22138288; 22139647; 22142952; 22151540; 22167195; 22178867; 22194464; 22197032; 22197408; 22200256; 22200563; 22200661; 22200690; 22204652; 22206665; 22210296; 22213073; 22215147; 22220395; 22220905; 22227305; 22228328; 22229442; 22232962; 22234512; 22237453; 22237587; 22241750; 22244537; 22252121; 22253805; 22259987; 22270366; 22272343; 22275073; 22278305; 22280559; 22288519; 22289521; 22289522; 22289852; 22291969; 22303700; 22304569; 22305865; 22309286; 22309692; 22321809; 22327326; 22336124; 22343748; 22391064; 22392094; 22394598; 22395516; 22395947; 22402435; 22402936; 22406112; 22406264; 22407864; 22410369; 22428754; 22433859; 22433968; 22439866; 22446321; 22448134; 22455335; 22459050; 22461694; 22465218; 22465234; 22472880; 22490156; 22490851; 22496335; 22513045; 22514348; 22516898; 22527933; 22528837; 22531699; 22532131; 22534634; 22541398; 22542663; 22547904; 22550024; 22573202; 22581515; 22582506; 22582975; 22591361; 22591362; 22608171; 22613329; 22619232; 22640376; 22640735; 22645431; 22646815; 22658256; 22664146; 22667130; 22674412; 22675930; 22677171; 22684547; 22684781; 22692967; 22694915; 22695075; 22697069; 22706255; 22710862; 22727497; 22729913; 22730324; 22738689; 22740037; 22740332; 22752570; 22773464; 22782080; 22796276; 22806308; 22808470; 22809399; 22810092; 22819245; 22821546; 22829602; 22832979; 22847199; 22848630; 22860023; 22863720; 22865631; 22866313; 22868188; 22878890; 22879913; 22880464; 22883193; 22883281; 22883459; 22884843; 22887854; 22888638; 22890115; 22906271; 22907074; 22914468; 22922035; 22923171; 22931588; 22936257; 22938481; 22942228; 22950839; 22954486; 22955446; 22957785; 22960198; 22964525; 22967049; 22969161; 22974233; 22977287; 22984561; 22985578; 22990627; 22994087; 23010359; 23011799; 23016931; 23018543; 23019342; 23031673; 23054355; 23064462; 23071279; 23076139; 23085464; 23091417; 23100088; 23104504; 23107277; 23107342; 23110201; 23114726; 23122824; 23123160; 23128233; 23134156; 23136157; 23146278; 23150684; 23151854; 23170789; 23175213; 23176145; 23179648; 23182966; 23183822; 23190621; 23201304; 23213753; 23221126; 23229548; 23232575; 23238437; 23240894; 23249715; 23252412; 23257253; 23257658; 23258534; 23263825; 23264211; 23269605; 23271730; 23273944; 23288142; 23292863; 23295196; 23303633; 23306155; 23307113; 23313298; 23317273; 23320481; 23326131; 23328249; 23341882; 23343958; 23349885; 23350235; 23353996; 23356642; 23372434; 23373240; 23375032; 23377317; 23387490; 23387827; 23388475; 23390835; 23401127; 23401274; 23409137; 23441116; 23454149; 23456480; 23476138; 23490413; 23504993; 23509357; 23510467; 23510472; 23516489; 23525277; 23525523; 23526143; 23536722; 23544610; 23547785; 23550278; 23554968; 23555986; 23557756; 23559867; 23566884; 23570558; 23575435; 23580092; 23601700; 23606791; 23615401; 23617547; 23637955; 23639553; 23650722; 23657566; 23660954; 23661254; 23663265; 23673111; 23679245; 23681803; 23696797; 23696833; 23697266; 23708302; 23715826; 23725476; 23742776; 23762835; 23768069; 23770289; 23770367; 23792205; 23793312; 23794948; 23801886; 23805466; 23807209; 23807291; 23814095; 23819814; 23824974; 23825535; 23829879; 23847438; 23870474; 23886165; 23897811; 23901237; 23908067; 23922934; 23936495; 23987197; 23991961; 23993112; 24025248; 24039251; 24065232; 24067484; 24072693; 24075964; 24099107; 24099425; 24122234; 24136650; 24141084; 24174628; 24210229; 24291031; 24297171; 24326842; 24330623; 24335416; 24344010; 24344026; 24374173; 24479343; 24479348 matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase) Ensembl:ENSG00000100985 HGNC:7176 HPRD:00387 MIM:120361 Vega:OTTHUMG00000033044 Other designations: 92 kDa gelatinase|92 kDa type IV collagenase|macrophage gelatinase|matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)|matrix metalloproteinase-9|type V collagenase MMP9 gene OGG:3000004345 Bin Zhao, Yue Liu, Oliver He MOX1 MOX2 MRC OX-2 WEB: http://www.ncbi.nlm.nih.gov/gene CD200 CD200 molecule 4345 My033 3q13.2 9606 3 Official from a nomenclature committee GO_0005515 (EC: IPI); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 3032785); GO_0050776 (EC: TAS) PMID: 2902568; 3032785; 10981966; 11099416; 11260322; 11726033; 12477932; 12960329; 15489334; 15699757; 15955564; 16177086; 16303743; 16344560; 16354172; 17964286; 18008004; 18040859; 18060403; 18060862; 18164423; 18838168; 18946351; 19086995; 19151626; 19230971; 19386363; 20050020; 20375636; 20379614; 20442224; 20959655; 21164290; 21206086; 21982860; 21988832; 22064604; 22319630; 22334534; 22363701; 22430636; 22462561; 22496920; 22575528; 22621248; 22875025; 22899296; 23179394; 23206327; 23489112; 23541619; 23560298; 23643150; 23690219; 23841472; 24045551; 24183830; 24344047 CD200 molecule Ensembl:ENSG00000091972 HGNC:7203 MIM:155970 Vega:OTTHUMG00000159248 Other designations: CD200 antigen|MRC OX-2 antigen|OX-2 membrane glycoprotein|antigen identified by monoclonal antibody MRC OX-2 CD200 OGG:3000004599 Bin Zhao, Yue Liu, Oliver He IFI-78K IFI78 MX MxA WEB: http://www.ncbi.nlm.nih.gov/gene MX1 myxovirus (influenza virus) resistance 1, interferon-inducible protein p78 (mouse) 4599 21q22.3 20140408 9606 21 protein-coding Official from a nomenclature committee GO_0003924 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15047845); GO_0005525 (EC: IEA); GO_0005634 (EC: IEA); GO_0005737 (EC: IDA); GO_0005789 (EC: IEA); GO_0005829 (EC: IDA, PMID: 16780588); GO_0005829 (EC: TAS); GO_0006915 (EC: TAS, PMID: 9389754); GO_0006952 (EC: TAS, PMID: 2154602); GO_0007165 (EC: TAS, PMID: 9389754); GO_0009615 (EC: IMP, PMID: 15047845); GO_0019221 (EC: TAS); GO_0034340 (EC: TAS); GO_0045071 (EC: IDA, PMID: 14687945); GO_0045087 (EC: TAS, PMID: 16202617); GO_0048471 (EC: IDA, PMID: 15047845); GO_0051607 (EC: IEA); GO_0060337 (EC: TAS) PMID: 1548781; 1629950; 1674496; 2154602; 2161946; 2481229; 2607176; 3162334; 8125298; 8411374; 8798556; 9060610; 9093949; 9389754; 9735310; 9933640; 10590150; 10830953; 10942113; 10971132; 11716541; 11805446; 11847228; 11880649; 11911186; 11916975; 12447867; 12477932; 12539042; 12595530; 12867637; 12944978; 14499622; 14687945; 14702039; 14752052; 14872030; 15047845; 15063762; 15117331; 15135736; 15163707; 15221897; 15355513; 15489334; 15602733; 15757897; 15766558; 15850793; 16009940; 16168514; 16202617; 16344560; 16390004; 16413306; 16459719; 16595158; 16704297; 16712791; 16769349; 16780588; 16792864; 16824203; 16843495; 16894313; 16978069; 17075576; 17126411; 17177148; 17307214; 17374778; 17407708; 17570575; 17845304; 17947524; 18549400; 18668195; 18676680; 18782441; 18843779; 19109387; 19170196; 19177264; 19236454; 19297326; 19434718; 19462904; 19625176; 19625466; 19635103; 19692168; 19744071; 19817957; 20019841; 20237496; 20309637; 20331378; 20428112; 20462354; 20494980; 20538602; 20588308; 20603636; 20628624; 20921509; 20959021; 21166595; 21645334; 21832049; 21859714; 21900240; 21906983; 21918813; 21935451; 21962493; 21992152; 22340769; 22507598; 22531919; 22647704; 22714910; 22950423; 22985419; 22998463; 23015724; 23084925; 23115279; 23152507; 23160781; 23232524; 23274784; 23382691; 23438650; 24049170; 24314641 myxovirus (influenza virus) resistance 1, interferon-inducible protein p78 (mouse) Ensembl:ENSG00000157601 HGNC:7532 HPRD:00919 MIM:147150 Vega:OTTHUMG00000086755 Other designations: interferon-induced GTP-binding protein Mx1|interferon-induced protein p78|interferon-regulated resistance GTP-binding protein MxA|myxoma resistance protein 1 MX1 OGG:3000004605 Bin Zhao, Yue Liu, Oliver He B-MYB BMYB WEB: http://www.ncbi.nlm.nih.gov/gene MYBL2 v-myb avian myeloblastosis viral oncogene homolog-like 2 4605 20q13.1 9606 20 Official from a nomenclature committee GO_0000086 (EC: TAS); GO_0000278 (EC: TAS); GO_0003677 (EC: IEA); GO_0003682 (EC: IEA); GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID: 17159899); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0006351 (EC: IEA); GO_0031523 (EC: IEA); GO_0051726 (EC: TAS); GO_0090307 (EC: IEA) PMID: 1376749; 1717494; 1984793; 3060855; 7642110; 8062924; 8123011; 8125298; 8142646; 8314782; 8812502; 9012818; 9840932; 10095772; 10544265; 10593981; 10645009; 10656684; 10744766; 10766737; 10770937; 10871850; 11259168; 11264176; 11423988; 11522824; 11733503; 11780052; 11973331; 11997503; 12439743; 12475768; 12477932; 12645566; 12673206; 12748276; 12927788; 12947099; 14506250; 14769798; 15256398; 15302935; 15489334; 15618219; 16055500; 16476973; 16551698; 17081983; 17098733; 17159899; 17531812; 17563750; 17588787; 17671431; 18026132; 18548008; 18676680; 19016757; 19043454; 19170196; 19383908; 19471022; 19625176; 19692168; 19725879; 19821490; 20211142; 20360068; 20734103; 20857481; 20864510; 21148321; 21187425; 21304178; 21367750; 21419759; 21480327; 21693764; 21900206; 21988832; 22910183; 23032261; 23555285; 24199710 v-myb avian myeloblastosis viral oncogene homolog-like 2 Ensembl:ENSG00000101057 HGNC:7548 HPRD:03247 MIM:601415 Vega:OTTHUMG00000033062 Other designations: myb-like protein 2|myb-related protein B|v-myb myeloblastosis viral oncogene homolog-like 2 MYBL2 OGG:3000004609 Bin Zhao, Yue Liu, Oliver He MRTL MYCC bHLHe39 c-Myc WEB: http://www.ncbi.nlm.nih.gov/gene MYC v-myc avian myelocytomatosis viral oncogene homolog 4609 8q24.21 9606 8 Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 9924025); GO_0000165 (EC: IMP, PMID: 17873522); GO_0001658 (EC: ISS); GO_0002053 (EC: ISS); GO_0003677 (EC: ISS); GO_0003677 (EC: TAS, PMID: 10597290); GO_0003700 (EC: IDA, PMID: 9924025); GO_0005515 (EC: IPI, PMID: 10597290); GO_0005634 (EC: IDA, PMID: 11793365); GO_0005654 (EC: IDA, PMID: 17558397); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, PMID: 17558397); GO_0005819 (EC: IEA); GO_0006112 (EC: NAS, PMID: 9924025); GO_0006338 (EC: IDA); GO_0006351 (EC: TAS); GO_0006367 (EC: TAS); GO_0006879 (EC: IDA, PMID: 9924025); GO_0006974 (EC: IDA, PMID: 17873522); GO_0007050 (EC: IDA, PMID: 10962037); GO_0007179 (EC: TAS); GO_0007219 (EC: TAS); GO_0008134 (EC: IPI, PMID: 15674325); GO_0008284 (EC: IDA, PMID: 15994933); GO_0010332 (EC: IDA, PMID: 19179467); GO_0010467 (EC: TAS); GO_0010468 (EC: IDA); GO_0015671 (EC: NAS, PMID: 9924025); GO_0032204 (EC: IMP, PMID: 17765874); GO_0032403 (EC: IDA, PMID: 18987311); GO_0032873 (EC: ISS); GO_0034644 (EC: IEP, PMID: 17873522); GO_0035690 (EC: IDA, PMID: 17873522); GO_0042493 (EC: IEP, PMID: 18291362); GO_0043066 (EC: ISS); GO_0043234 (EC: IDA, PMID: 17873522); GO_0043280 (EC: IDA, PMID: 19179467); GO_0044346 (EC: TAS, PMID: 10962037); GO_0045656 (EC: IMP, PMID: 9924025); GO_0045893 (EC: IDA, PMID: 10962037); GO_0045944 (EC: IMP, PMID: 9924025); GO_0045944 (EC: TAS); GO_0046983 (EC: IEA); GO_0048146 (EC: IDA, PMID: 18987311); GO_0048146 (EC: IMP, PMID: 15674325); GO_0048147 (EC: IDA, PMID: 10962037); GO_0050679 (EC: IDA, PMID: 18987311); GO_0051276 (EC: IDA, PMID: 10962037); GO_0051782 (EC: IDA, PMID: 10962037); GO_0060070 (EC: IDA); GO_0070491 (EC: IPI, PMID: 15674325); GO_0070848 (EC: TAS, PMID: 18987311); GO_0070888 (EC: IDA, PMID: 18818310); GO_0090096 (EC: ISS); GO_2000573 (EC: IMP, PMID: 9924025); GO_2001022 (EC: IDA, PMID: 19179467) PMID: 1318011; 1559612; 1597196; 1651323; 1748630; 1914517; 2006410; 2430795; 2663470; 2834731; 3033665; 3243428; 3277717; 3540591; 3778453; 6298632; 6304538; 6304729; 6321164; 6324175; 6414718; 6419122; 6431612; 6547209; 6578511; 6714223; 7565735; 7642555; 7651436; 7729426; 7838535; 7892279; 7957875; 8076603; 8220424; 8224841; 8247524; 8266081; 8377829; 8386367; 8668343; 8755740; 9129988; 9155018; 9184233; 9187264; 9207092; 9308237; 9312026; 9315742; 9461566; 9528857; 9680483; 9689053; 9708738; 9788437; 9792694; 9797456; 9924025; 9927431; 10229200; 10319872; 10380878; 10421840; 10446203; 10465786; 10551811; 10593926; 10597290; 10611234; 10899308; 10918583; 10962037; 11046155; 11182042; 11208609; 11274368; 11282029; 11283613; 11306501; 11311202; 11431533; 11441001; 11443860; 11509179; 11511539; 11567024; 11585818; 11602341; 11673469; 11777933; 11793365; 11795828; 11804592; 11817538; 11839798; 11840336; 11844794; 11848444; 11848471; 11850082; 11861398; 11877042; 11877298; 11877389; 11891322; 11909963; 11916966; 11956070; 11960382; 11968011; 12027803; 12031912; 12032779; 12036888; 12049739; 12072203; 12077335; 12080043; 12082260; 12091391; 12130502; 12149248; 12149649; 12177005; 12196529; 12209953; 12213716; 12226097; 12237776; 12356725; 12360279; 12362975; 12379776; 12391307; 12394763; 12420224; 12435808; 12446731; 12452058; 12477932; 12490316; 12509468; 12529648; 12538578; 12545156; 12553908; 12562237; 12575534; 12584560; 12637327; 12637527; 12644583; 12646176; 12660246; 12673205; 12688321; 12706874; 12721301; 12729735; 12748187; 12769844; 12776177; 12776737; 12783888; 12808131; 12818373; 12821782; 12824159; 12824180; 12829833; 12842909; 12855588; 12857727; 12873812; 12909717; 12944920; 12963825; 12970749; 14532990; 14559996; 14563837; 14576301; 14612409; 14625288; 14645543; 14645547; 14663479; 14663583; 14672406; 14697225; 14724288; 14744757; 14749374; 14760071; 14769798; 14991929; 15048125; 15067010; 15071503; 15077166; 15083194; 15084259; 15098029; 15103331; 15108364; 15126105; 15150404; 15160911; 15190416; 15191563; 15192039; 15198123; 15199070; 15199147; 15210690; 15243561; 15282543; 15286700; 15287031; 15355849; 15358760; 15361884; 15457447; 15459488; 15468060; 15474507; 15489334; 15498494; 15502847; 15516975; 15522869; 15528212; 15542830; 15572685; 15580293; 15595642; 15601838; 15616584; 15616592; 15629428; 15645079; 15663936; 15674325; 15688026; 15697230; 15716988; 15723053; 15723054; 15735755; 15739117; 15743499; 15756435; 15763593; 15769738; 15780936; 15800668; 15808510; 15839202; 15856024; 15878876; 15910003; 15929079; 15937962; 15944709; 15965094; 15972952; 15986448; 15988031; 15991278; 15992821; 15994933; 16007143; 16023596; 16081735; 16085756; 16094360; 16107691; 16107734; 16116477; 16126174; 16139224; 16140957; 16167342; 16169462; 16172399; 16173081; 16174239; 16201965; 16205115; 16210249; 16247449; 16260605; 16269333; 16287840; 16293596; 16295419; 16308474; 16316993; 16328057; 16352593; 16367922; 16376880; 16378632; 16410719; 16410805; 16423995; 16423996; 16432227; 16455494; 16466700; 16478988; 16490593; 16494045; 16508012; 16537449; 16537801; 16541139; 16543245; 16552729; 16554306; 16572399; 16582589; 16596619; 16628215; 16631470; 16675879; 16682952; 16690525; 16705173; 16706751; 16724113; 16785237; 16788099; 16797278; 16809765; 16857742; 16874304; 16878156; 16940161; 16964280; 16984727; 16996503; 17001014; 17028906; 17046748; 17050536; 17070983; 17072308; 17081983; 17082179; 17082780; 17093053; 17114293; 17141659; 17145812; 17146437; 17146439; 17151361; 17157259; 17158641; 17159920; 17170079; 17219990; 17264126; 17268552; 17289033; 17297307; 17308053; 17310999; 17314511; 17353931; 17363738; 17401363; 17401366; 17404030; 17404512; 17418410; 17419941; 17419945; 17431415; 17444495; 17445886; 17452451; 17466258; 17466981; 17471507; 17482131; 17485441; 17486099; 17503467; 17525531; 17541401; 17558397; 17560940; 17567920; 17568564; 17573914; 17587243; 17597761; 17599065; 17606868; 17613764; 17616526; 17622571; 17632056; 17634226; 17643117; 17646408; 17656250; 17670825; 17698969; 17699159; 17700029; 17700062; 17704800; 17706770; 17726380; 17728244; 17765874; 17766436; 17784791; 17785433; 17785457; 17822678; 17873522; 17877160; 17881732; 17881904; 17885207; 17908964; 17913706; 17917571; 17927853; 17959148; 17967894; 17989722; 17993259; 18003922; 18024371; 18026954; 18059336; 18059365; 18060517; 18066065; 18084761; 18085637; 18089500; 18157115; 18190704; 18204787; 18206534; 18206725; 18216297; 18235046; 18240345; 18242516; 18247372; 18256156; 18256542; 18262050; 18271930; 18291362; 18292777; 18297523; 18308950; 18314492; 18320361; 18321953; 18323656; 18345030; 18348166; 18348176; 18349290; 18365874; 18369647; 18375382; 18381641; 18382371; 18393360; 18398700; 18408012; 18413597; 18422165; 18426604; 18426731; 18433872; 18451027; 18460403; 18483244; 18483343; 18490439; 18498136; 18535662; 18542060; 18544539; 18556416; 18559552; 18562319; 18566574; 18567993; 18586674; 18593994; 18597608; 18621930; 18623111; 18628098; 18628958; 18632605; 18642056; 18647998; 18676680; 18677108; 18679422; 18713946; 18714337; 18722373; 18752058; 18752503; 18754028; 18776924; 18780787; 18782427; 18794855; 18808065; 18809243; 18813796; 18813857; 18816594; 18818310; 18818322; 18838534; 18851746; 18852287; 18923429; 18932273; 18937283; 18950845; 18953412; 18985155; 18987311; 18987359; 19008924; 19017648; 19020659; 19020761; 19022255; 19022256; 19022773; 19033664; 19038003; 19061835; 19061838; 19084934; 19086036; 19087307; 19111069; 19118200; 19119907; 19126644; 19131971; 19134217; 19143767; 19147754; 19164469; 19170058; 19170196; 19174556; 19176757; 19179467; 19180571; 19202062; 19204574; 19211792; 19219026; 19259613; 19269368; 19270750; 19276364; 19287990; 19322201; 19330026; 19330811; 19331129; 19332536; 19336552; 19351506; 19358757; 19364925; 19379561; 19387923; 19395026; 19398483; 19407242; 19453846; 19454499; 19461583; 19470954; 19481339; 19497851; 19524285; 19535347; 19549807; 19549847; 19554081; 19560862; 19561607; 19562729; 19564413; 19568426; 19573080; 19574298; 19575869; 19578763; 19581307; 19586553; 19594747; 19596917; 19596922; 19597184; 19602047; 19623651; 19625176; 19633646; 19672269; 19673870; 19684017; 19690609; 19692168; 19696787; 19700410; 19704118; 19729955; 19730683; 19740707; 19748357; 19755676; 19766114; 19773279; 19786833; 19787269; 19815507; 19818711; 19821490; 19840458; 19843847; 19855079; 19857615; 19881537; 19895682; 19900447; 19908297; 19923826; 19934275; 19956635; 19966299; 19966300; 19996270; 20008140; 20008325; 20010808; 20010876; 20063409; 20065031; 20071475; 20086171; 20087644; 20113841; 20118770; 20133585; 20133671; 20143187; 20144848; 20170530; 20173740; 20190818; 20194507; 20195357; 20208519; 20212154; 20215511; 20221419; 20232342; 20233711; 20300622; 20308430; 20348956; 20359089; 20378577; 20379146; 20382893; 20383333; 20402410; 20416159; 20423888; 20426839; 20434984; 20440510; 20442643; 20453196; 20473309; 20487546; 20493879; 20498406; 20509972; 20515470; 20520840; 20551172; 20561405; 20562918; 20564213; 20573831; 20579853; 20596624; 20598117; 20607354; 20634801; 20643075; 20647308; 20659471; 20661666; 20662834; 20691906; 20697356; 20714214; 20716114; 20716118; 20737197; 20737421; 20820186; 20848231; 20852628; 20852632; 20873543; 20878079; 20890087; 20936779; 20946988; 20949568; 20950152; 20956327; 20962620; 20970423; 20972266; 20972438; 20974848; 20974860; 20981461; 21036740; 21039844; 21048031; 21054888; 21059853; 21059911; 21060841; 21073496; 21092188; 21098095; 21098324; 21113618; 21120662; 21129250; 21131959; 21135252; 21138684; 21148746; 21150319; 21173787; 21187426; 21217079; 21219856; 21242960; 21245140; 21262914; 21264535; 21284881; 21298377; 21302450; 21317922; 21324178; 21336720; 21346144; 21378543; 21383696; 21390222; 21394210; 21400515; 21405945; 21406394; 21406400; 21412688; 21419292; 21435462; 21441954; 21447796; 21460180; 21468039; 21478095; 21478429; 21497295; 21527520; 21533051; 21556123; 21557726; 21575199; 21610111; 21618595; 21620836; 21627565; 21628855; 21638011; 21640157; 21643008; 21646687; 21667531; 21668996; 21692100; 21693596; 21693764; 21708481; 21724525; 21741827; 21769863; 21774525; 21781227; 21783402; 21793975; 21795698; 21807902; 21808024; 21833088; 21835891; 21851818; 21856782; 21862873; 21876152; 21878679; 21882178; 21885567; 21890444; 21890473; 21903590; 21906983; 21908617; 21909081; 21913186; 21915097; 21941025; 21941367; 21949397; 21963094; 21969377; 21975934; 21986497; 21987572; 21988832; 21998677; 22002311; 22002575; 22005580; 22010341; 22011035; 22015605; 22016811; 22020439; 22022427; 22025562; 22037351; 22068108; 22081066; 22090452; 22094256; 22108803; 22120970; 22121953; 22128178; 22145969; 22155254; 22157079; 22158906; 22159222; 22168746; 22169291; 22172699; 22178210; 22184109; 22186139; 22205151; 22235332; 22245592; 22249265; 22253833; 22281794; 22285861; 22286234; 22307329; 22310977; 22314191; 22317895; 22326218; 22327960; 22328504; 22330139; 22333584; 22333947; 22364879; 22371483; 22383169; 22384171; 22393362; 22417306; 22429595; 22430491; 22448750; 22453922; 22456335; 22484426; 22484818; 22496461; 22505724; 22510570; 22535747; 22543587; 22545246; 22547830; 22573578; 22573825; 22578181; 22581054; 22614067; 22615405; 22623531; 22623730; 22661084; 22665062; 22665537; 22670178; 22706665; 22707729; 22710719; 22713676; 22733550; 22736142; 22739149; 22754359; 22768805; 22791812; 22801218; 22804688; 22814375; 22826122; 22826319; 22833560; 22842522; 22844532; 22851565; 22863009; 22880082; 22884659; 22887866; 22889122; 22897848; 22912356; 22941468; 22942279; 22945648; 22949148; 22957790; 22967991; 22976378; 22986535; 22992334; 22999547; 23000965; 23012230; 23012233; 23018644; 23024800; 23029531; 23042398; 23045412; 23053136; 23062488; 23071356; 23079660; 23079661; 23088399; 23089465; 23106691; 23108410; 23112173; 23113893; 23135913; 23143306; 23143645; 23145106; 23155275; 23175515; 23177619; 23178486; 23178487; 23237560; 23237807; 23239811; 23243310; 23249808; 23250739; 23266555; 23266556; 23269272; 23277542; 23291854; 23308051; 23318434; 23330001; 23335369; 23341364; 23355209; 23364919; 23380875; 23389829; 23424671; 23438603; 23449635; 23455924; 23466707; 23468463; 23504319; 23507140; 23509080; 23521519; 23530127; 23532756; 23535729; 23535730; 23538750; 23552692; 23555992; 23560086; 23560736; 23574779; 23576579; 23578955; 23583198; 23588620; 23588859; 23589839; 23601184; 23603171; 23603392; 23613397; 23649631; 23704919; 23714368; 23716601; 23720054; 23770341; 23775087; 23776131; 23791182; 23792459; 23797802; 23816886; 23817571; 23821202; 23860446; 23860775; 23861098; 23894778; 23901000; 23907459; 23908595; 23930820; 23939148; 23982173; 23994632; 24009228; 24036151; 24053468; 24063893; 24095110; 24140063; 24157866; 24169826; 24216476; 24249258; 24259667; 24272483; 24316975; 24333422 v-myc avian myelocytomatosis viral oncogene homolog Ensembl:ENSG00000136997 HGNC:7553 HPRD:01818 MIM:190080 Vega:OTTHUMG00000128475 Other designations: avian myelocytomatosis viral oncogene homolog|class E basic helix-loop-helix protein 39|myc proto-oncogene protein|myc-related translation/localization regulatory factor|proto-oncogene c-Myc|transcription factor p64|v-myc myelocytomatosis viral oncogene homolog MYC OGG:3000004613 Bin Zhao, Yue Liu, Oliver He MODED MYCNOT N-myc NMYC ODED bHLHe37 WEB: http://www.ncbi.nlm.nih.gov/gene MYCN v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog 4613 2p24.3 9606 2 Official from a nomenclature committee GO_0000785 (EC: TAS, PMID: 3796607); GO_0001502 (EC: IEA); GO_0002053 (EC: IEA); GO_0003677 (EC: TAS, PMID: 10597290); GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10597290); GO_0005634 (EC: IDA, PMID: 10597290); GO_0006357 (EC: TAS, PMID: 3796607); GO_0010942 (EC: IEA); GO_0030324 (EC: IEA); GO_0042733 (EC: IEA); GO_0045944 (EC: IEA); GO_0046983 (EC: IEA); GO_0048704 (EC: IEA); GO_0048712 (EC: IEA); GO_0048754 (EC: IEA); GO_2000378 (EC: IEA) PMID: 1419902; 1425701; 1549498; 1695323; 2006410; 2582423; 2834684; 2869488; 2987858; 3008339; 3299258; 3437890; 3510398; 3552210; 3796607; 3940169; 6575396; 6700732; 6719137; 6728001; 8668343; 9856457; 10229200; 10407192; 10597290; 10677303; 11593398; 11602341; 11826111; 11850545; 11861392; 11881792; 12153570; 12192602; 12219017; 12232763; 12438307; 12477932; 12545167; 12569580; 12660036; 12670915; 12808116; 12819037; 12907629; 14645238; 14647433; 14719101; 14737110; 15117961; 15198123; 15218241; 15258910; 15302935; 15314226; 15316056; 15331636; 15489334; 15547663; 15632181; 15644444; 15660126; 15833843; 16166307; 16278682; 16516635; 16596176; 16906565; 16912187; 16912192; 17020972; 17023822; 17055458; 17172827; 17213019; 17289033; 17327229; 17464317; 17495526; 17506115; 17525631; 17535087; 17554788; 17611020; 17643814; 17704800; 17710228; 18004567; 18059033; 18097563; 18165268; 18198336; 18278068; 18281664; 18335505; 18348317; 18391076; 18470948; 18488021; 18504438; 18591937; 18610847; 18671284; 18769732; 18785023; 18851746; 18949372; 18955045; 19006223; 19047142; 19047152; 19061778; 19111882; 19208763; 19301388; 19401549; 19495417; 19608868; 19615087; 19649205; 19656550; 19724862; 19766596; 19852433; 19885598; 19924232; 19946337; 19956635; 19997598; 20007697; 20017904; 20080637; 20103633; 20144241; 20145147; 20173740; 20179233; 20180881; 20190806; 20236072; 20301770; 20332316; 20395439; 20409325; 20424123; 20425471; 20478998; 20575024; 20607354; 20697349; 20719933; 20811720; 20946988; 20961996; 20980091; 21046119; 21073496; 21112821; 21123453; 21173028; 21214410; 21224895; 21258086; 21288077; 21297076; 21304178; 21370425; 21378543; 21384249; 21498633; 21501490; 21508638; 21533284; 21572098; 21646478; 21698133; 21725357; 21731748; 21750863; 21796614; 21796619; 21822304; 21856782; 21862876; 21882282; 21908575; 21929510; 21963094; 22035742; 22052359; 22065083; 22068108; 22090452; 22120721; 22123490; 22146831; 22202125; 22218692; 22286764; 22337647; 22383024; 22439933; 22484425; 22544364; 22623531; 22624711; 22751132; 22907398; 22907436; 22921766; 22952844; 22975311; 23042116; 23091029; 23152863; 23186832; 23284291; 23284678; 23308108; 23317189; 23320395; 23341988; 23358695; 23362253; 23430699; 23498719; 23563570; 23578955; 23639551; 23812427; 23901000; 23962557; 24011394; 24130166; 24260886 v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog Ensembl:ENSG00000134323 HGNC:7559 HPRD:01278 MIM:164840 Vega:OTTHUMG00000039579 Other designations: N-myc proto-oncogene protein|class E basic helix-loop-helix protein 37|neuroblastoma MYC oncogene|neuroblastoma-derived v-myc avian myelocytomatosis viral related oncogene|oncogene NMYC|pp65/67 MYCN OGG:3000004616 Bin Zhao, Yue Liu, Oliver He GADD45BETA MYD118 WEB: http://www.ncbi.nlm.nih.gov/gene GADD45B growth arrest and DNA-damage-inducible, beta 4616 19p13.3 9606 19 Official from a nomenclature committee GO_0000185 (EC: IDA, PMID: 9827804); GO_0000186 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12052864); GO_0005634 (EC: IDA, PMID: 9827804); GO_0005737 (EC: IDA, PMID: 9827804); GO_0006469 (EC: IEA); GO_0006915 (EC: IEA); GO_0006950 (EC: IEA); GO_0007275 (EC: IEA); GO_0030154 (EC: IEA); GO_0043065 (EC: IDA, PMID: 9827804); GO_0046330 (EC: IDA, PMID: 9827804); GO_0051726 (EC: IEA); GO_1900745 (EC: IDA, PMID: 9827804) PMID: 1899477; 8700517; 8889548; 9151207; 9827804; 10101024; 10773677; 10828065; 10872826; 10973963; 11078829; 11498536; 12052864; 12124778; 12162804; 12477932; 12716909; 12759252; 12855571; 14630914; 14743220; 15057824; 15342556; 15489334; 15509538; 15546867; 15616591; 15642734; 16144844; 16256071; 17437852; 17485467; 17591973; 18343408; 18515079; 18576389; 19064572; 19834918; 19877043; 20530689; 20558744; 20942912; 21062976; 21127053; 21139048; 21810943; 22048458; 22096849; 22797925; 23110778; 24104471; 24104474 growth arrest and DNA-damage-inducible, beta Ensembl:ENSG00000099860 HGNC:4096 HPRD:05382 MIM:604948 Vega:OTTHUMG00000180434 Other designations: growth arrest and DNA damage-inducible protein GADD45 beta|myeloid differentiation primary response protein MyD118|negative growth regulatory protein MyD118 GADD45B OGG:3000004673 Bin Zhao, Yue Liu, Oliver He NAP1 NAP1L NRP WEB: http://www.ncbi.nlm.nih.gov/gene NAP1L1 nucleosome assembly protein 1-like 1 4673 12q21.2 9606 12 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 11940655); GO_0005634 (EC: IEA); GO_0006260 (EC: TAS, PMID: 8297347); GO_0006334 (EC: IEA); GO_0008284 (EC: TAS, PMID: 8297347); GO_0042470 (EC: IEA); GO_0044822 (EC: IDA) PMID: 7821789; 8297347; 11073993; 11940655; 12477932; 12777385; 14702039; 14966293; 15308774; 15345747; 15489334; 16169070; 16196087; 16287874; 16565220; 16964243; 17081065; 17081983; 17339334; 17620599; 17725712; 18226242; 18781797; 18985028; 19322201; 19339032; 19471022; 19884766; 19888548; 20002496; 20195357; 20473970; 20639865; 20697350; 20972266; 21044950; 21110914; 21139048; 21145461; 21319273; 21333655; 21565611; 21890473; 21900206; 21906983; 21963094; 21988832; 22053931; 22134777; 22145905; 22174317; 22242598; 22505724; 22586326; 22810585; 22863883; 22939629; 23000965; 23251661; 23438482; 23455922; 23691099; 23824909 nucleosome assembly protein 1-like 1 Ensembl:ENSG00000187109 HGNC:7637 HPRD:01248 MIM:164060 Vega:OTTHUMG00000169786 Other designations: HSP22-like protein interacting protein|NAP-1 related protein|NAP-1-related protein|hNRP NAP1L1 OGG:3000004747 Bin Zhao, Yue Liu, Oliver He CMT1F CMT2E NF-L NF68 NFL WEB: http://www.ncbi.nlm.nih.gov/gene NEFL neurofilament, light polypeptide 4747 8p21 9606 8 Official from a nomenclature committee GO_0005200 (EC: IDA, PMID: 12432080); GO_0005515 (EC: IPI, PMID: 12837694); GO_0005737 (EC: ISS); GO_0005829 (EC: TAS); GO_0005883 (EC: IDA, PMID: 15857389); GO_0007268 (EC: TAS); GO_0008022 (EC: IPI, PMID: 12226091); GO_0008089 (EC: IMP, PMID: 15857389); GO_0008090 (EC: IMP, PMID: 15857389); GO_0019896 (EC: IMP, PMID: 15857389); GO_0030424 (EC: IDA, PMID: 14662745); GO_0030674 (EC: ISS); GO_0033596 (EC: IDA, Qualifier: colocalizes_with, PMID: 12226091); GO_0033693 (EC: IDA, PMID: 12432080); GO_0033693 (EC: IMP, PMID: 15857389); GO_0042802 (EC: IPI, PMID: 12432080); GO_0045109 (EC: IMP, PMID: 12432080) PMID: 1497855; 1902666; 2516804; 3034332; 3036423; 3121319; 3145240; 6135695; 8125298; 8180132; 8344946; 8530496; 8615909; 8621664; 8665664; 8863508; 9388258; 9425014; 9481670; 9763415; 10373510; 10841809; 11220745; 12133495; 12226091; 12231460; 12403814; 12432080; 12477167; 12477932; 12481988; 12566280; 12730211; 12815021; 12837694; 12911634; 14622581; 14662745; 14733962; 15111691; 15122254; 15241803; 15324660; 15383276; 15489334; 15654615; 15686490; 15857389; 16084104; 16169070; 16344560; 16452125; 16678934; 16930284; 17052987; 17290105; 17475803; 17620486; 17683050; 17903209; 17923616; 18023247; 18758688; 19034380; 19110265; 19123978; 19158810; 19286384; 19488899; 19678766; 19950375; 20039262; 20086018; 20201926; 20213320; 20301366; 20301384; 20301462; 20381070; 21039366; 21044950; 21139048; 21197541; 21860087; 21890473; 21983493; 22246235; 22288874; 22302611; 22319610; 22586326; 22680408; 22765307; 22797925; 23455924; 23705811; 23827424; 23870535; 24244333 neurofilament, light polypeptide HGNC:7739 HPRD:01206 MIM:162280 Other designations: light molecular weight neurofilament protein|neurofilament light polypeptide|neurofilament protein, light chain|neurofilament subunit NF-L|neurofilament triplet L protein|neurofilament, light polypeptide 68kDa NEFL OGG:3000004763 Bin Zhao, Yue Liu, Oliver He NFNS VRNF WSS WEB: http://www.ncbi.nlm.nih.gov/gene NF1 neurofibromin 1 4763 17q11.2 9606 17 Official from a nomenclature committee GO_0000165 (EC: ISS); GO_0001649 (EC: ISS); GO_0001656 (EC: ISS); GO_0001666 (EC: ISS); GO_0001889 (EC: ISS); GO_0001937 (EC: IMP, PMID: 16648142); GO_0001938 (EC: IEA); GO_0001952 (EC: ISS); GO_0001953 (EC: IEA); GO_0005099 (EC: IDA, PMID: 1568247); GO_0005515 (EC: IPI, PMID: 11356864); GO_0005634 (EC: ISS, PMID: 1550670); GO_0005737 (EC: IBA); GO_0005737 (EC: ISS, PMID: 1550670); GO_0006469 (EC: ISS); GO_0007154 (EC: ISS); GO_0007265 (EC: ISS); GO_0007406 (EC: ISS); GO_0007420 (EC: ISS); GO_0007422 (EC: ISS); GO_0007507 (EC: ISS); GO_0007519 (EC: IEA); GO_0008429 (EC: IDA, PMID: 17187824); GO_0008542 (EC: ISS); GO_0008625 (EC: IEA); GO_0014044 (EC: ISS); GO_0014065 (EC: ISS); GO_0016525 (EC: IEA); GO_0021510 (EC: ISS); GO_0021897 (EC: ISS); GO_0021915 (EC: IEA); GO_0021987 (EC: ISS); GO_0022011 (EC: ISS); GO_0030036 (EC: ISS); GO_0030198 (EC: ISS); GO_0030199 (EC: ISS); GO_0030325 (EC: ISS); GO_0030336 (EC: IMP, PMID: 16648142); GO_0030424 (EC: IDA, PMID: 1550670); GO_0030425 (EC: IDA, PMID: 1550670); GO_0031210 (EC: IDA, PMID: 17187824); GO_0031235 (EC: IBA); GO_0032228 (EC: IEA); GO_0032318 (EC: IMP, PMID: 1570015); GO_0032320 (EC: IDA, PMID: 2121371); GO_0032320 (EC: IMP, PMID: 16648142); GO_0032320 (EC: ISS); GO_0035021 (EC: IEA); GO_0042060 (EC: ISS); GO_0042992 (EC: ISS); GO_0043065 (EC: ISS); GO_0043407 (EC: ISS); GO_0043409 (EC: IMP, PMID: 16648142); GO_0043409 (EC: ISS); GO_0043473 (EC: ISS); GO_0043525 (EC: ISS); GO_0043535 (EC: IMP, PMID: 17404841); GO_0045124 (EC: ISS); GO_0045671 (EC: IEA); GO_0045685 (EC: ISS); GO_0045762 (EC: ISS); GO_0045765 (EC: IMP, PMID: 17404841); GO_0046580 (EC: IBA); GO_0046929 (EC: IEA); GO_0048147 (EC: ISS); GO_0048169 (EC: IEA); GO_0048485 (EC: ISS); GO_0048593 (EC: ISS); GO_0048712 (EC: IEA); GO_0048715 (EC: ISS); GO_0048745 (EC: ISS); GO_0048844 (EC: ISS); GO_0048853 (EC: ISS); GO_0050890 (EC: IMP, PMID: 17299016); GO_1902043 (EC: IEA); GO_2001241 (EC: IEA) PMID: 1302608; 1329097; 1339276; 1457041; 1550670; 1568247; 1570015; 1662505; 1715669; 1719426; 1745350; 1757093; 1783401; 1923522; 1937470; 2114220; 2116237; 2121370; 2121371; 2125369; 2134734; 2491776; 7519874; 7570581; 7633431; 7633452; 7649559; 7686513; 7774960; 7874161; 7903661; 7904209; 7959746; 7981679; 7981724; 8069310; 8081387; 8176268; 8317503; 8417346; 8544190; 8602361; 8619474; 8628317; 8664912; 8807336; 8825042; 8825634; 8834249; 8836031; 8931693; 9002664; 9003501; 9101300; 9110174; 9150739; 9298829; 9300663; 9529361; 9639526; 9668168; 9706718; 10220149; 10336779; 10553997; 10607834; 10625171; 10712197; 10721668; 10862698; 11140831; 11258625; 11356864; 11704931; 11727199; 11727265; 11735023; 11748857; 11751683; 11754043; 11857752; 11896214; 11896613; 11934389; 12073021; 12077339; 12095621; 12152785; 12191989; 12199909; 12368469; 12387455; 12438263; 12477932; 12483293; 12522551; 12552569; 12566521; 12660952; 12707950; 12730209; 12746402; 12807981; 12872266; 12963615; 13679444; 13680360; 14647436; 14722914; 14988005; 15096131; 15146197; 15146469; 15233998; 15302935; 15342556; 15371411; 15389774; 15520408; 15523626; 15523642; 15583390; 15627836; 15735964; 15767669; 15944227; 15988004; 15999204; 16005615; 16081245; 16083285; 16116616; 16138909; 16169856; 16199547; 16344560; 16374483; 16380919; 16405917; 16467218; 16470740; 16479075; 16565220; 16644864; 16648142; 16741618; 16773574; 16813595; 16830335; 16835260; 16835897; 16908010; 16914719; 16944271; 16944272; 17036045; 17053831; 17096025; 17102080; 17160901; 17187824; 17200120; 17216419; 17295913; 17299016; 17353900; 17404841; 17426081; 17514731; 17563086; 17581973; 17668375; 17726231; 17876295; 17880527; 17914445; 17960768; 17999360; 18021924; 18055911; 18086893; 18172006; 18183042; 18212816; 18214791; 18215124; 18218617; 18316778; 18331998; 18407053; 18484666; 18485440; 18503770; 18511569; 18546366; 18592002; 18802710; 18948576; 19041782; 19048115; 19061981; 19120036; 19142971; 19144660; 19215943; 19220708; 19221814; 19238080; 19291764; 19292874; 19351817; 19417008; 19449407; 19601812; 19650418; 19718661; 19773259; 19845691; 19913121; 19940123; 20002172; 20006588; 20015894; 20052761; 20082856; 20124472; 20129251; 20160012; 20160346; 20164853; 20301288; 20358387; 20379614; 20422842; 20428205; 20435627; 20442305; 20503322; 20505189; 20513137; 20543202; 20571392; 20587590; 20602485; 20624961; 20628086; 20655465; 20680410; 20687928; 20725927; 20927530; 21048031; 21089070; 21139048; 21142935; 21157378; 21199919; 21236316; 21244408; 21278392; 21280148; 21283084; 21337692; 21365283; 21478499; 21551249; 21674567; 21728811; 21732117; 21782795; 21890473; 21903422; 21931722; 21963094; 22015770; 22096509; 22105171; 22108604; 22125493; 22190464; 22207399; 22240541; 22241097; 22250039; 22293200; 22294457; 22354384; 22399775; 22412049; 22488919; 22573716; 22581253; 22585738; 22586326; 22700876; 22751498; 22807134; 22837079; 22925204; 22945628; 22962301; 22965642; 22965773; 23000965; 23010473; 23047742; 23077663; 23082153; 23135915; 23145129; 23165953; 23171796; 23222849; 23244495; 23288408; 23292448; 23312374; 23335975; 23437333; 23455922; 23460398; 23481210; 23528211; 23583712; 23624750; 23668869; 23906300; 23947441; 24249802; 24250222; 24255178 neurofibromin 1 Ensembl:ENSG00000196712 HGNC:7765 HPRD:01203 MIM:613113 Vega:OTTHUMG00000132871 Other designations: neurofibromatosis-related protein NF-1|neurofibromin NF1 OGG:3000004780 NRF2 WEB: http://www.ncbi.nlm.nih.gov/gene nuclear factor, erythroid 2-like 2 4780 2q31 9606 2 Official from a nomenclature committee GO_0000785 (EC: IEA); GO_0001102 (EC: IPI); GO_0003677 (EC: IDA, PMID: 18554677); GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID: 16888629); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA); GO_0005813 (EC: IDA); GO_0005829 (EC: IDA); GO_0005886 (EC: IDA); GO_0006366 (EC: TAS, PMID: 7937919); GO_0010499 (EC: IDA, PMID: 19424503); GO_0016567 (EC: IDA, PMID: 15983046); GO_0019904 (EC: IPI, PMID: 11256947); GO_0030194 (EC: IEA); GO_0030968 (EC: IEA); GO_0036003 (EC: IMP); GO_0043161 (EC: IDA, PMID: 15983046); GO_0043565 (EC: IEA); GO_0045944 (EC: IMP, PMID: 18202225) PMID: 7868116; 7937919; 9150357; 9872330; 9887101; 10419538; 10510468; 10747902; 10930400; 11013233; 11035812; 11256947; 11274184; 11439354; 11683914; 11909699; 12020345; 12084617; 12084707; 12145307; 12198130; 12360409; 12370194; 12435735; 12441344; 12446695; 12477932; 12490281; 12506115; 12556532; 12805554; 12947090; 14517290; 14517554; 14529549; 14565864; 14585973; 14612418; 14985350; 15020583; 15282312; 15358217; 15367669; 15379550; 15475350; 15489334; 15525690; 15572695; 15601839; 15734732 abhydrolase domain containing 1 Ensembl:ENSG00000116044 HGNC:7782 HPRD:02732 MIM:600492 Vega:OTTHUMG00000133620 NFE2L2 OGG:3000004790 Bin Zhao, Yue Liu, Oliver He EBP-1 KBF1 NF-kB1 NF-kappa-B NF-kappaB NFKB-p105 NFKB-p50 NFkappaB p105 p50 WEB: http://www.ncbi.nlm.nih.gov/gene NFKB1 nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 4790 4q24 9606 4 GO_0000122 (EC: IC, PMID:16938301); GO_0000122 (EC: IMP, PMID:19881551); GO_0000975 (EC: IDA, PMID:17426251); GO_0000976 (EC: IDA, PMID:18718911); GO_0001071 (EC: IDA, PMID:17426251); GO_0001818 (EC: IEA); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0003690 (EC: IEA); GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID:10023675); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005739 (EC: IDA); GO_0005829 (EC: TAS); GO_0006366 (EC: TAS, PMID:1992489); GO_0006915 (EC: IEA); GO_0006954 (EC: TAS, PMID:1992489); GO_0006979 (EC: IEA); GO_0008134 (EC: IDA, PMID:18270204); GO_0009617 (EC: IEA); GO_0010744 (EC: IC, PMID:16938301); GO_0010884 (EC: IC, PMID:16938301); GO_0010956 (EC: IDA, PMID:15243130); GO_0010957 (EC: IC, PMID:15243130); GO_0031072 (EC: IEA); GO_0031293 (EC: TAS); GO_0032269 (EC: IC, PMID:16938301); GO_0032375 (EC: IC, PMID:16938301); GO_0032481 (EC: TAS); GO_0033256 (EC: TAS, PMID:16938301); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035666 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042803 (EC: IEA); GO_0043066 (EC: TAS, PMID:10811897); GO_0044212 (EC: IDA, PMID:16938301); GO_0045083 (EC: IEA); GO_0045087 (EC: TAS); GO_0045893 (EC: IDA, PMID:17426251); GO_0045893 (EC: IMP); GO_0045893 (EC: NAS, PMID:8096091); GO_0045944 (EC: IEA); GO_0046688 (EC: IEA); GO_0048011 (EC: TAS); GO_0050728 (EC: IEA); GO_0050852 (EC: TAS); GO_0051092 (EC: TAS); GO_0071260 (EC: IEP, PMID:19593445); GO_0071347 (EC: IEP, PMID:12958148); GO_0090263 (EC: IMP); GO_1900127 (EC: IDA, PMID:17324121) PMID:1505523; 1508666; 1518839; 1527859; 1583734; 1612589; 1992489; 2017258; 2050119; 2108863; 2203531; 2234062; 2497520; 7494249; 7651415; 7690421; 7692236; 7694229; 7729429; 7739549; 7742037; 7788295; 7800480; 7823959; 7830764; 7838536; 7859743; 7862168; 7891711; 7933095; 7957556; 8087845; 8096091; 8113688; 8139561; 8151786; 8178481; 8196632; 8207793; 8246997; 8255759; 8290595; 8319912; 8423996; 8428580; 8441377; 8550813; 8615004; 8621941; 8627654; 8628291; 8631829; 8642313; 8649779; 8676466; 8692272; 8709193; 8717528; 8724035; 8746784; 8790371; 8798655; 8814265; 8825636; 8834464; 8870842; 8887676; 8997639; 9094628; 9110146; 9135156; 9218802; 9223487; 9235945; 9250404; 9252186; 9278385; 9315679; 9334723; 9368006; 9468519; 9510190; 9525916; 9529257; 9535861; 9556555; 9560267; 9566873; 9566883; 9572494; 9584180; 9621091; 9722548; 9730685; 9738011; 9792375; 9809067; 9837938; 9865693; 9865694; 9895331; 9950430; 9990852; 10023675; 10075655; 10207088; 10225209; 10235509; 10357819; 10362352; 10384093; 10393859; 10400814; 10426996; 10446807; 10469655; 10480634; 10498867; 10562553; 10580107; 10625680; 10635328; 10644332; 10644726; 10646849; 10671224; 10704334; 10723127; 10775602; 10777532; 10799874; 10811897; 10835356; 10847592; 10856288; 10928981; 10931834; 10969074; 10970863; 11020244; 11036073; 11044099; 11094166; 11158290; 11160671; 11241736; 11278695; 11297557; 11299302; 11313474; 11356851; 11385624; 11418662; 11425860; 11468175; 11511100; 11522182; 11526476; 11579140; 11590148; 11607785; 11696595; 11704662; 11739381; 11756416; 11779220; 11819787; 11827962; 11830587; 11830590; 11833470; 11859566; 11880271; 11931769; 11942414; 11943214; 11953428; 11959143; 11970949; 11971907; 11972054; 11976329; 11980335; 11983170; 12019209; 12021045; 12032828; 12032830; 12040437; 12052823; 12057007; 12058256; 12067898; 12077118; 12077347; 12086956; 12089148; 12091382; 12115625; 12122011; 12133438; 12135603; 12145210; 12150710; 12150997; 12166787; 12167619; 12173051; 12181421; 12195699; 12198114; 12203044; 12230568; 12237108; 12244126; 12296854; 12297126; 12297724; 12297725; 12365017; 12388747; 12393603; 12396456; 12406554; 12419805; 12427593; 12428105; 12431991; 12433922; 12444143; 12444202; 12470471; 12471041; 12473373; 12477932; 12482504; 12482669; 12482991; 12485413; 12488445; 12495677; 12496256; 12496485; 12496486; 12538487; 12574335; 12592338; 12594215; 12594338; 12604365; 12606501; 12606947; 12618429; 12620896; 12623850; 12637324; 12644014; 12646168; 12646204; 12667451; 12673201; 12676577; 12693954; 12699902; 12700228; 12709429; 12711606; 12715098; 12727023; 12738634; 12743697; 12743709; 12748173; 12767057; 12771144; 12771929; 12783888; 12820969; 12821113; 12829026; 12832450; 12839942; 12843241; 12855659; 12857898; 12859994; 12860389; 12867284; 12871932; 12872153; 12878172; 12883671; 12884915; 12914931; 12917325; 12919943; 12921778; 12944982; 12947093; 12952968; 12958148; 12958623; 12958678; 12960163; 12963997; 12966099; 12972430; 12972607; 12972622; 12973300; 13679070; 13680285; 14530285; 14534291; 14550290; 14558943; 14561767; 14570916; 14572449; 14573617; 14576361; 14578856; 14581467; 14585847; 14593105; 14597672; 14613970; 14624448; 14625285; 14625298; 14645533; 14647412; 14657027; 14662860; 14663476; 14676829; 14678988; 14679201; 14679213; 14684616; 14685242; 14689584; 14690596; 14691449; 14697238; 14715628; 14729568; 14737065; 14739303; 14743216; 14743471; 14744759; 14747545; 14760757; 14769797; 14963043; 14966375; 15013753; 15016307; 15020601; 15039334; 15043934; 15044484; 15047705; 15053878; 15056731; 15063762; 15068390; 15073126; 15073170; 15078930; 15084608; 15087454; 15090542; 15093615; 15102862; 15103018; 15130920; 15137059; 15142381; 15143182; 15147743; 15169888; 15173174; 15175625; 15178248; 15179048; 15184376; 15184390; 15187159; 15188354; 15190178; 15203187; 15208298; 15217951; 15218148; 15226292; 15226448; 15238257; 15241416; 15242768; 15243130; 15251447; 15252018; 15254772; 15257133; 15258149; 15276183; 15280372; 15280531; 15297971; 15310755; 15314185; 15315758; 15319438; 15327770; 15337758; 15345718; 15351720; 15358208; 15364309; 15373762; 15383283; 15383523; 15389633; 15457532; 15459191; 15466412; 15467918; 15469820; 15471861; 15477018; 15485865; 15486815; 15489334; 15494311; 15496460; 15498932; 15501771; 15514680; 15521376; 15522218; 15528271; 15532722; 15535802; 15543947; 15545823; 15550679; 15561713; 15563086; 15564333; 15569630; 15569997; 15578154; 15591054; 15591119; 15597152; 15601829; 15610077; 15618021; 15618216; 15623625; 15627743; 15638726; 15640523; 15642694; 15642734; 15647756; 15650392; 15650393; 15650394; 15653692; 15657065; 15661045; 15670752; 15677444; 15678501; 15687488; 15688415; 15694363; 15701651; 15713218; 15713234; 15718492; 15722350; 15722553; 15725353; 15725474; 15727562; 15735699; 15735750; 15743789; 15746262; 15746428; 15757899; 15767394; 15780175; 15799966; 15802604; 15809302; 15811852; 15817944; 15827086; 15829968; 15830705; 15869598; 15870177; 15876358; 15894171; 15905616; 15905705; 15920558; 15922296; 15940251; 15941782; 15944151; 15951441; 15955209; 15964798; 15964800; 15972330; 15972853; 15979574; 15979856; 15982633; 15991283; 16001969; 16004996; 16005433; 16029077; 16039990; 16039994; 16044154; 16046401; 16046415; 16079148; 16081580; 16082226; 16087150; 16088959; 16105840; 16108830; 16116232; 16123212; 16142329; 16142871; 16155293; 16167336; 16199137; 16203728; 16204234; 16206345; 16207722; 16210649; 16212965; 16219794; 16223733; 16234240; 16236134; 16237100; 16243842; 16258173; 16260783; 16266460; 16270046; 16280329; 16285952; 16288847; 16289658; 16291755; 16299251; 16299518; 16303162; 16305395; 16306043; 16306601; 16308565; 16313306; 16318585; 16319921; 16319923; 16325763; 16341093; 16364464; 16380507; 16387424; 16397577; 16397579; 16407234; 16408727; 16410801; 16410802; 16410803; 16418290; 16424045; 16429131; 16429138; 16436380; 16439988; 16441485; 16452479; 16455661; 16465659; 16476711; 16485028; 16490783; 16491128; 16497967; 16498458; 16504042; 16513645; 16514159; 16519794; 16519819; 16528384; 16543241; 16554660; 16569657; 16571778; 16601113; 16616657; 16624823; 16630341; 16631615; 16635909; 16644866; 16651450; 16651613; 16678126; 16680372; 16684768; 16690938; 16697675; 16709572; 16722389; 16728660; 16740634; 16740744; 16751281; 16756716; 16757480; 16769768; 16771709; 16774937; 16778171; 16799643; 16804398; 16804400; 16816390; 16820889; 16822500; 16835229; 16840782; 16840786; 16857678; 16879221; 16891304; 16893890; 16906147; 16907704; 16912315; 16914552; 16919057; 16919536; 16926151; 16927804; 16928771; 16938301; 16951147; 16973832; 16979873; 16979925; 16980310; 16984419; 16984731; 16997282; 17000776; 17002577; 17003112; 17005562; 17011110; 17013094; 17039240; 17046972; 17047155; 17047486; 17049230; 17052690; 17053167; 17054067; 17062574; 17079333; 17085785; 17088249; 17103034; 17111814; 17114179; 17117949; 17129456; 17132229; 17133356; 17159900; 17174275; 17192276; 17194723; 17197380; 17200110; 17222798; 17242904; 17244613; 17255362; 17255956; 17256751; 17266559; 17276726; 17292586; 17296734; 17303384; 17303559; 17312171; 17314097; 17316355; 17318773; 17324121; 17334226; 17340152; 17354234; 17376917; 17387583; 17401435; 17405920; 17405935; 17409218; 17418100; 17419715; 17420005; 17426251; 17447895; 17452475; 17452529; 17462862; 17466952; 17468103; 17468848; 17471012; 17471239; 17475880; 17485237; 17490702; 17492467; 17495961; 17496784; 17498291; 17499812; 17502349; 17502353; 17507309; 17507655; 17521736; 17522703; 17530443; 17532054; 17538633; 17540609; 17543500; 17545521; 17545551; 17548685; 17549794; 17555878; 17565687; 17577783; 17583675; 17590380; 17590503; 17597077; 17600378; 17602748; 17603079; 17604336; 17607147; 17607549; 17611682; 17620428; 17622249; 17626072; 17627037; 17638883; 17638900; 17644514; 17644577; 17644777; 17652082; 17671417; 17684021; 17690684; 17692805; 17693123; 17700572; 17701919; 17702576; 17702846; 17704737; 17709376; 17712623; 17719653; 17725175; 17728102; 17761976; 17766391; 17785586; 17827154; 17828582; 17852842; 17873517; 17876541; 17878161; 17878165; 17882263; 17895971; 17896809; 17904523; 17908953; 17908957; 17910475; 17918160; 17925880; 17927847; 17928629; 17929131; 17932106; 17936701; 17938575; 17942533; 17947462; 17947496; 17950943; 17953212; 17959673; 17962196; 17962807; 17963943; 17967787; 17975552; 17978477; 17982228; 17986144; 17991734; 17997719; 17999917; 18006812; 18006844; 18008176; 18025803; 18029348; 18031796; 18032824; 18035048; 18039660; 18045535; 18050214; 18054783; 18064631; 18070982; 18070983; 18073330; 18074095; 18079108; 18082293; 18083845; 18090157; 18092345; 18158619; 18160848; 18163488; 18171526; 18172861; 18174252; 18178551; 18184402; 18199400; 18201555; 18202112; 18203956; 18212740; 18215660; 18216101; 18219313; 18224252; 18224424; 18226221; 18230685; 18234964; 18242184; 18248671; 18252714; 18252806; 18253935; 18260825; 18270204; 18275043; 18279996; 18292749; 18304423; 18305042; 18307978; 18308615; 18316375; 18316378; 18316606; 18316610; 18316612; 18322992; 18325349; 18329615; 18330586; 18331465; 18331590; 18336259; 18336908; 18341653; 18344086; 18347181; 18352974; 18356846; 18367547; 18375836; 18398749; 18422166; 18424438; 18425349; 18425350; 18426800; 18429822; 18433717; 18434448; 18436431; 18443042; 18443271; 18444250; 18450748; 18461473; 18466468; 18474259; 18476609; 18502748; 18504431; 18505918; 18508109; 18515093; 18523147; 18533190; 18538010; 18549623; 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19820695; 19821157; 19826638; 19829671; 19837667; 19838207; 19838218; 19844776; 19845758; 19862523; 19878981; 19879919; 19881551; 19884766; 19885551; 19885592; 19885862; 19887846; 19892748; 19897484; 19898747; 19901262; 19903813; 19903815; 19909783; 19911254; 19913121; 19915152; 19917706; 19928652; 19932734; 19940361; 19941056; 19943112; 19947250; 19948975; 19954665; 19955102; 19956647; 19956670; 19956890; 19958645; 19959479; 19966852; 19995347; 20004763; 20004764; 20006706; 20008294; 20009901; 20012522; 20027638; 20030038; 20038977; 20042710; 20043910; 20051109; 20051532; 20052674; 20061391; 20064526; 20065107; 20065354; 20066092; 20066093; 20066094; 20066113; 20068069; 20069553; 20073580; 20074357; 20086239; 20097762; 20100571; 20102618; 20103633; 20106524; 20107185; 20110362; 20110513; 20124446; 20126979; 20127012; 20127709; 20129940; 20130217; 20133937; 20138641; 20139130; 20139322; 20139419; 20140262; 20145198; 20148897; 20149620; 20154269; 20160043; 20164171; 20171262; 20172018; 20172044; 20194722; 20195357; 20198307; 20204281; 20211142; 20213318; 20218898; 20224721; 20226764; 20226854; 20228198; 20230666; 20230686; 20231411; 20237496; 20237821; 20298930; 20299603; 20301198; 20304615; 20307555; 20331378; 20332099; 20333648; 20336759; 20337891; 20346059; 20346360; 20350779; 20351780; 20353025; 20353939; 20354190; 20356387; 20356841; 20360864; 20367887; 20368414; 20372806; 20372820; 20375583; 20376775; 20379146; 20379614; 20380698; 20380700; 20385556; 20388715; 20389059; 20391111; 20392247; 20392262; 20398057; 20406326; 20406964; 20414006; 20414373; 20416077; 20416168; 20418905; 20419804; 20424119; 20424169; 20432452; 20433755; 20436512; 20438785; 20439115; 20448038; 20448286; 20449947; 20450542; 20451919; 20452482; 20453000; 20454998; 20458747; 20460684; 20470938; 20479762; 20482842; 20483790; 20484576; 20485444; 20492683; 20498636; 20501937; 20506652; 20507572; 20509140; 20511226; 20512787; 20514026; 20516073; 20519510; 20519647; 20521099; 20522558; 20523058; 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21113131; 21132531; 21138333; 21139048; 21145111; 21145461; 21148792; 21149600; 21150337; 21155242; 21155719; 21159881; 21166501; 21172429; 21190575; 21203561; 21220295; 21222514; 21228323; 21242888; 21242976; 21245992; 21264233; 21266470; 21273489; 21293511; 21293853; 21300060; 21308734; 21324206; 21331078; 21333439; 21334713; 21338484; 21343618; 21344487; 21352816; 21364020; 21383007; 21387831; 21389131; 21389697; 21390241; 21399635; 21399639; 21402921; 21406399; 21408173; 21411116; 21411444; 21411734; 21414799; 21417823; 21423202; 21424730; 21434324; 21448225; 21451109; 21463955; 21464588; 21468605; 21471377; 21472776; 21479189; 21483817; 21486470; 21490402; 21490927; 21491088; 21501152; 21503877; 21507981; 21511059; 21518763; 21525354; 21526963; 21527635; 21527913; 21528358; 21529841; 21531730; 21535601; 21540330; 21547539; 21549062; 21569377; 21570865; 21571356; 21573030; 21573053; 21574100; 21575498; 21576089; 21592054; 21602448; 21604024; 21606198; 21613824; 21617575; 21617851; 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22046434; 22063737; 22066734; 22067113; 22068612; 22072831; 22077140; 22083956; 22090103; 22090112; 22092568; 22093097; 22095071; 22096476; 22102915; 22118627; 22123322; 22131135; 22132199; 22132240; 22138609; 22138672; 22139845; 22145100; 22147524; 22152775; 22153345; 22156489; 22157716; 22170554; 22171160; 22172699; 22174879; 22184967; 22185489; 22187158; 22199285; 22207455; 22211660; 22212641; 22217202; 22226472; 22226621; 22226679; 22227305; 22229121; 22229442; 22248180; 22252121; 22258247; 22261743; 22264835; 22267549; 22284893; 22286758; 22287454; 22293503; 22306268; 22307688; 22320942; 22320981; 22321707; 22327383; 22328149; 22331067; 22334708; 22341466; 22343628; 22346248; 22347372; 22348310; 22354461; 22359280; 22362744; 22380486; 22384099; 22384168; 22386866; 22388891; 22394598; 22396537; 22406367; 22406815; 22417709; 22427141; 22429999; 22430136; 22450687; 22461522; 22464415; 22465880; 22479419; 22484638; 22490020; 22490899; 22496225; 22505595; 22507528; 22509384; 22513115; 22521419; 22526587; 22527100; 22528837; 22530801; 22534017; 22537555; 22538516; 22547075; 22552288; 22558282; 22562129; 22566686; 22581854; 22593154; 22593207; 22597534; 22605335; 22613333; 22614238; 22618514; 22641218; 22645312; 22674419; 22685329; 22685373; 22698986; 22699931; 22707304; 22735811; 22740410; 22742857; 22742859; 22749179; 22749770; 22749879; 22760211; 22762947; 22763043; 22764136; 22767505; 22768179; 22776619; 22798425; 22801426; 22806547; 22815893; 22825241; 22828805; 22833150; 22836752; 22843550; 22846605; 22849850; 22851693; 22851696; 22855173; 22855490; 22859938; 22863753; 22869145; 22874821; 22874878; 22880008; 22884975; 22887854; 22891614; 22898922; 22902396; 22917497; 22924768; 22927965; 22933289; 22936809; 22941344; 22945510; 22949302; 22952582; 22954486; 22955189; 22967049; 22967106; 22975586; 22984526; 22988296; 22995914; 23000144; 23001849; 23006728; 23009565; 23017833; 23027537; 23027628; 23028875; 23039130; 23041324; 23044494; 23053371; 23061681; 23066037; 23091063; 23092922; 23096115; 23110043; 23117246; 23123205; 23125120; 23128233; 23132271; 23132857; 23135727; 23152563; 23152895; 23153769; 23155052; 23160072; 23170789; 23174100; 23176038; 23178493; 23185316; 23193970; 23205493; 23219896; 23221546; 23224146; 23226410; 23230212; 23237063; 23249930; 23259994; 23261678; 23266528; 23269488; 23269842; 23271730; 23275439; 23280137; 23296075; 23299027; 23299493; 23310954; 23317209; 23319823; 23322360; 23322721; 23322906; 23322997; 23327061; 23328932; 23331079; 23332158; 23334076; 23339870; 23357300; 23364895; 23369793; 23378274; 23386606; 23392668; 23399035; 23402362; 23405894; 23416929; 23426622; 23428345; 23437386; 23439561; 23444213; 23451236; 23452206; 23457512; 23496811; 23503472; 23503975; 23504987; 23510475; 23530144; 23552418; 23563313; 23576799; 23577181; 23583295; 23585913; 23603894; 23615072; 23615397; 23616277; 23616566; 23618653; 23634218; 23634661; 23636254; 23656347; 23659359; 23664977; 23669642; 23671649; 23675986; 23684722; 23687337; 23690573; 23708311; 23715268; 23724129; 23728913; 23732112; 23732909; 23744075; 23751348; 23752607; 23754270; 23756813; 23757261; 23774208; 23791017; 23791833; 23806437; 23821202; 23831825; 23843455; 23861985; 23869088; 23880092; 23887394; 23900863; 23908590; 23911423; 23921373; 23935876; 23942618; 23954632; 23969028; 23982206; 24008839; 24027435; 24035972; 24041570; 24045046; 24048682; 24054986; 24065232; 24067962; 24077340; 24097561; 24098051; 24099783; 24109220; 24109241; 24113181; 24145029; 24145431; 24152244; 24175631; 24258200; 24270572; 24282904; 24297735; 24316229; 24321067; 24352326; 24367071; 24368180; 24436266; 24510559 nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 Ensembl:ENSG00000109320 HGNC:7794 HPRD:01238 MIM:164011 Vega:OTTHUMG00000161080 Other designations: DNA binding factor KBF1|DNA-binding factor KBF1|NF-kappabeta|nuclear factor NF-kappa-B p105 subunit|nuclear factor NF-kappa-B p50 subunit|nuclear factor kappa-B DNA binding subunit NFKB1 OGG:3000004791 Bin Zhao, Yue Liu, Oliver He CVID10 H2TF1 LYT-10 LYT10 NF-kB2 p105 p52 WEB: http://www.ncbi.nlm.nih.gov/gene NFKB2 nuclear factor of kappa light polypeptide gene enhancer in B-cells 2 (p49/p100) 4791 10q24 9606 10 GO_0002224 (EC: TAS); GO_0002268 (EC: IEA); GO_0002467 (EC: IEA); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0003677 (EC: IEA); GO_0003700 (EC: IEA); GO_0003713 (EC: TAS, PMID:1876189); GO_0005515 (EC: IPI, PMID:11239468); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006351 (EC: IEA); GO_0006355 (EC: IDA, PMID:8360178); GO_0030198 (EC: IEA); GO_0032481 (EC: TAS); GO_0033257 (EC: IDA, PMID:9407099); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035666 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0045087 (EC: TAS); GO_0048536 (EC: IEA); GO_0051092 (EC: TAS) PMID:1473734; 1505523; 1531086; 1583734; 1612589; 1760839; 1876189; 7478612; 7494249; 7541912; 7597296; 7690421; 7729429; 7800480; 7823959; 7838536; 7859743; 7925301; 7933095; 7949142; 7969113; 8036016; 8108127; 8108136; 8113688; 8152812; 8207793; 8208540; 8336950; 8360178; 8378093; 8413211; 8423996; 8441377; 8453667; 8615004; 8627654; 8676466; 8709193; 8717528; 8724035; 8834464; 8887665; 9021684; 9110146; 9135156; 9264393; 9278385; 9315679; 9359707; 9384586; 9407099; 9510190; 9523851; 9525916; 9529131; 9566873; 9730685; 9792375; 9895331; 10207088; 10225209; 10384093; 10393859; 10400814; 10446807; 10480634; 10562553; 10580107; 10597218; 10644332; 10644726; 10671224; 10713675; 10723127; 10799874; 10823818; 10830747; 11044099; 11160671; 11239468; 11241736; 11299302; 11385624; 11468175; 11511100; 11522182; 11526476; 11579140; 11704662; 11707390; 11827962; 11833470; 11980335; 11994270; 12040437; 12167619; 12185077; 12351572; 12352969; 12374738; 12389034; 12427593; 12473373; 12477932; 12482669; 12485413; 12505990; 12524526; 12697057; 12808109; 12835724; 12874295; 12894228; 12917325; 12927781; 14532284; 14576817; 14676825; 14678988; 14743216; 15103018; 15140882; 15164054; 15258149; 15310758; 15469820; 15485830; 15489334; 15629778; 15677444; 15677466; 15782119; 15799966; 16009713; 16108830; 16223731; 16260623; 16303288; 16344560; 16368877; 16385451; 16477006; 16613850; 16651533; 16751281; 16940298; 16990795; 17003035; 17028057; 17039258; 17183367; 17197385; 17237370; 17254973; 17292587; 17363471; 17476277; 17548614; 17563756; 17703412; 17715223; 17962807; 18025196; 18025803; 18029348; 18160848; 18321863; 18377428; 18383001; 18434448; 18466468; 18538010; 18550535; 18617892; 18660489; 18781579; 18818748; 18971284; 19098713; 19219072; 19258923; 19302050; 19471022; 19479051; 19524538; 19527514; 19542561; 19573080; 19591173; 19773279; 19860880; 19913121; 19948975; 20037209; 20038584; 20211142; 20301476; 20346360; 20353939; 20388792; 20448286; 20460684; 20503287; 20558726; 20568250; 20598117; 20628086; 20628624; 20708837; 20734064; 20800578; 21048223; 21131783; 21139048; 21228035; 21325409; 21846842; 21871426; 21906983; 21963094; 21987572; 21988832; 22017875; 22083306; 22096027; 22198284; 22341466; 22388891; 22435556; 22642622; 22708077; 22734038; 22797925; 22864569; 22879398; 23211527; 23219896; 23301098; 23383273; 23389097; 23524849; 23699654; 23873932; 24008839; 24140114 nuclear factor of kappa light polypeptide gene enhancer in B-cells 2 (p49/p100) Ensembl:ENSG00000077150 HGNC:7795 HPRD:01239 MIM:164012 Vega:OTTHUMG00000018962 Other designations: DNA-binding factor KBF2|NFKB, p52/p100 subunit|lymphocyte translocation chromosome 10 protein|nuclear factor Kappa-B, subunit 2|nuclear factor NF-kappa-B p100 subunit|nuclear factor of Kappa light chain gene enhancer in B cells 2|oncogene Lyt-10|transcription factor NFKB2 NFKB2 OGG:3000004792 Bin Zhao, Yue Liu, Oliver He IKBA MAD-3 NFKBI WEB: http://www.ncbi.nlm.nih.gov/gene NFKBIA nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha 4792 14q13 20140408 9606 14 protein-coding Official from a nomenclature committee GO_0000060 (EC: IEA); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0005515 (EC: IPI, PMID: 10498867); GO_0005634 (EC: IDA, PMID: 16648481); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA); GO_0006915 (EC: TAS, PMID: 10747850); GO_0007253 (EC: IMP, PMID: 16938301); GO_0008134 (EC: TAS, PMID: 10928981); GO_0008139 (EC: IPI, PMID: 1493333); GO_0010745 (EC: IMP, PMID: 16938301); GO_0010875 (EC: IMP, PMID: 16938301); GO_0010888 (EC: IMP, PMID: 16938301); GO_0016032 (EC: IEA); GO_0019899 (EC: IPI, PMID: 16648481); GO_0031072 (EC: IEA); GO_0031625 (EC: IPI, PMID: 9859996); GO_0031663 (EC: IEA); GO_0032088 (EC: IDA, PMID: 11931770); GO_0032270 (EC: IMP, PMID: 16938301); GO_0032403 (EC: IEA); GO_0032481 (EC: TAS); GO_0032495 (EC: IEA); GO_0033256 (EC: TAS, PMID: 16938301); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035666 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042127 (EC: IEA); GO_0042345 (EC: NAS, PMID: 3140380); GO_0042802 (EC: IPI, PMID: 16951195); GO_0042994 (EC: IDA, PMID: 1493333); GO_0043066 (EC: TAS); GO_0043330 (EC: IEA); GO_0043392 (EC: NAS, PMID: 3140380); GO_0045087 (EC: TAS); GO_0045638 (EC: IEA); GO_0045746 (EC: IEA); GO_0045944 (EC: IDA, PMID: 19245366); GO_0045944 (EC: IMP, PMID: 16938301); GO_0048011 (EC: TAS); GO_0050852 (EC: TAS); GO_0051059 (EC: IDA, PMID: 11931770); GO_0051059 (EC: IPI, PMID: 7739562); GO_0051092 (EC: TAS); GO_0070417 (EC: NAS, PMID: 16750872); GO_0070427 (EC: IEA); GO_0070431 (EC: IEA) PMID: 1427874; 1493333; 1829648; 3140380; 7479976; 7565415; 7628694; 7679069; 7700645; 7739525; 7739549; 7739562; 7878004; 7891711; 8139561; 8246997; 8601309; 8615004; 8622692; 8631829; 8657102; 8709193; 8797825; 8887627; 8887633; 8887676; 8889548; 8940099; 8978697; 9057089; 9060679; 9135156; 9214631; 9244310; 9252186; 9261139; 9334723; 9346485; 9362451; 9372968; 9409737; 9452483; 9566883; 9572494; 9689078; 9721103; 9734360; 9738011; 9751059; 9792645; 9859996; 9865693; 9865694; 9873017; 9875328; 9882613; 9891086; 9892650; 9914500; 9990852; 9990853; 10023675; 10026139; 10066434; 10066435; 10075690; 10085062; 10085161; 10094049; 10102628; 10230406; 10329681; 10362352; 10393859; 10398585; 10421793; 10480634; 10498867; 10514433; 10521480; 10570937; 10580107; 10582246; 10635328; 10637284; 10644755; 10655476; 10657303; 10706725; 10713156; 10723127; 10733566; 10747850; 10783893; 10848576; 10869418; 10882136; 10928981; 10930447; 10968793; 10969074; 11020244; 11027288; 11042193; 11064457; 11080499; 11095741; 11106428; 11113112; 11231305; 11278695; 11287411; 11313474; 11415944; 11483504; 11493922; 11511100; 11533489; 11572859; 11696595; 11799106; 11809792; 11830587; 11913973; 11931770; 11950839; 11959143; 11983170; 12028809; 12054687; 12084717; 12086926; 12138192; 12151397; 12165731; 12167702; 12190313; 12193729; 12244195; 12297126; 12324474; 12377412; 12388747; 12406554; 12411322; 12419805; 12419806; 12429743; 12433922; 12477728; 12477932; 12486103; 12518988; 12589049; 12620896; 12651903; 12704657; 12709429; 12711606; 12748192; 12897149; 12921778; 12943667; 12944982; 12972430; 12973300; 13680285; 14500727; 14523047; 14534291; 14561767; 14576361; 14623898; 14685242; 14690596; 14743216; 14961554; 15068390; 15073126; 15084260; 15103018; 15125834; 15142381; 15161102; 15173174; 15173580; 15184376; 15202778; 15218148; 15247916; 15276183; 15330761; 15337789; 15389589; 15389633; 15489334; 15536134; 15590691; 15601829; 15613239; 15657065; 15670770; 15671028; 15725353; 15746428; 15749833; 15782119; 15799966; 15808510; 15811852; 15817944; 15856023; 15858823; 15917220; 15979856; 16001969; 16046415; 16098527; 16105840; 16169070; 16189514; 16195219; 16210649; 16236267; 16258173; 16286467; 16291755; 16319058; 16354686; 16371367; 16378096; 16407234; 16426569; 16429138; 16481475; 16540234; 16547522; 16573520; 16611882; 16648481; 16737960; 16750872; 16756995; 16919536; 16931600; 16938301; 16951195; 16955245; 16997282; 17003112; 17053167; 17060341; 17062574; 17079871; 17115186; 17148610; 17284228; 17307728; 17316064; 17318178; 17318773; 17333217; 17351338; 17354114; 17363905; 17363973; 17379600; 17384642; 17463416; 17492467; 17593226; 17607549; 17612295; 17681786; 17701919; 17703412; 17910475; 17942396; 17956732; 17991436; 18003900; 18029348; 18045535; 18071880; 18074035; 18199400; 18215193; 18255255; 18260825; 18356846; 18429822; 18434448; 18474597; 18501560; 18503636; 18511071; 18515365; 18555796; 18600435; 18606063; 18636124; 18636537; 18660489; 18672082; 18716880; 18818748; 18949366; 18950845; 18957422; 18981174; 18981184; 19019440; 19046417; 19053519; 19187648; 19206148; 19213954; 19219072; 19222990; 19223558; 19245366; 19258923; 19296948; 19297320; 19363678; 19453261; 19456861; 19494296; 19500386; 19507254; 19522780; 19527514; 19543524; 19554506; 19573080; 19591507; 19622906; 19625650; 19648161; 19673747; 19733238; 19758175; 19773279; 19773451; 19797428; 19798070; 19816602; 19879840; 19886988; 19891769; 19913121; 19933270; 19941056; 19948975; 20012522; 20056178; 20065107; 20068069; 20080849; 20132559; 20133937; 20164548; 20193848; 20237821; 20304615; 20335171; 20347421; 20353940; 20379146; 20379614; 20385620; 20388715; 20434986; 20448286; 20449947; 20453000; 20495844; 20503287; 20546338; 20551178; 20558726; 20563630; 20568250; 20628086; 20628624; 20638939; 20652762; 20659425; 20674643; 20696864; 20716621; 20797629; 20811626; 20836841; 20890592; 20932476; 20953189; 20953190; 20980497; 21048031; 21175304; 21175585; 21217772; 21220295; 21228035; 21263074; 21376060; 21451109; 21454528; 21606193; 21664225; 21712995; 21778941; 21811235; 21862596; 21896478; 21906983; 21951552; 21963094; 21988832; 22022389; 22078572; 22081069; 22156201; 22184009; 22187158; 22302838; 22388891; 22393418; 22509384; 22590978; 22605335; 22685297; 22935973; 22990857; 23046941; 23054188; 23069812; 23250755; 23274114; 23284737; 23285182; 23322360; 23383273; 23393163; 23422506; 23439505; 23453579; 23457512; 23487427; 23555990; 23563313; 23604351; 23732909; 23746843; 23818606; 24085292; 24248593; 24295474; 24367071 nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha Ensembl:ENSG00000100906 HGNC:7797 HPRD:01235 MIM:164008 Vega:OTTHUMG00000140220 Other designations: I-kappa-B-alpha|IkappaBalpha|NF-kappa-B inhibitor alpha|ikB-alpha|major histocompatibility complex enhancer-binding protein MAD3|nuclear factor of kappa light chain gene enhancer in B-cells NFKBIA OGG:3000004830 Bin Zhao, Yue Liu, Oliver He AWD GAAD NB NBS NDKA NDPK-A NDPKA NM23 NM23-H1 WEB: http://www.ncbi.nlm.nih.gov/gene NME1 NME/NM23 nucleoside diphosphate kinase 1 4830 17q21.3 9606 17 Official from a nomenclature committee GO_0000287 (EC: IDA, PMID: 11555662); GO_0000977 (EC: IEA); GO_0002762 (EC: IEA); GO_0003697 (EC: IEA); GO_0004536 (EC: IDA, PMID: 11555662); GO_0004550 (EC: IDA, PMID: 12972261); GO_0005515 (EC: IPI, PMID: 10602478); GO_0005524 (EC: IDA, PMID: 12972261); GO_0005525 (EC: IDA, PMID: 12972261); GO_0005634 (EC: IDA, PMID: 16814409); GO_0005634 (EC: TAS, PMID: 16130169); GO_0005737 (EC: TAS, PMID: 16130169); GO_0005739 (EC: IEA); GO_0005813 (EC: IEA); GO_0005829 (EC: IDA, PMID: 16814409); GO_0005829 (EC: TAS); GO_0006183 (EC: IEA); GO_0006228 (EC: IEA); GO_0006241 (EC: IEA); GO_0006308 (EC: IDA, PMID: 11555662); GO_0006897 (EC: IEA); GO_0007595 (EC: IEA); GO_0008285 (EC: TAS, PMID: 1851158); GO_0010629 (EC: IEA); GO_0010976 (EC: IEA); GO_0014075 (EC: IEA); GO_0015949 (EC: TAS); GO_0019215 (EC: IEA); GO_0019901 (EC: IEA); GO_0021766 (EC: IEA); GO_0032587 (EC: IDA, PMID: 16814409); GO_0033574 (EC: IEA); GO_0035690 (EC: IEA); GO_0042802 (EC: IPI, PMID: 10602478); GO_0042981 (EC: TAS, PMID: 16130169); GO_0043015 (EC: IEA); GO_0043024 (EC: IPI, PMID: 16814409); GO_0043388 (EC: IDA, PMID: 17975005); GO_0044281 (EC: TAS); GO_0044822 (EC: IDA); GO_0048471 (EC: IEA); GO_0050679 (EC: IMP, PMID: 16862176); GO_0051591 (EC: IEA); GO_0055086 (EC: TAS); GO_0071333 (EC: IEA); GO_0071398 (EC: IEA) PMID: 1851158; 2015608; 2056128; 2509941; 2566996; 7916650; 8047138; 8245015; 8270257; 8392752; 8395939; 8810265; 8858107; 9480811; 9488696; 9513729; 9593706; 10512675; 10602478; 10611312; 10618642; 11042679; 11231635; 11274357; 11280768; 11319942; 11555662; 11687967; 11726210; 11776896; 11835509; 11918081; 11919189; 11935309; 11960382; 11963831; 11998956; 12007505; 12105213; 12135660; 12137595; 12163590; 12174914; 12200143; 12405283; 12452062; 12474051; 12477932; 12490715; 12524539; 12601555; 12624546; 12628186; 12669312; 12684753; 12859952; 12883690; 12910292; 12972261; 14499630; 14558955; 14664140; 14960567; 15040016; 15073128; 15129904; 15280446; 15334673; 15489334; 15512982; 15568401; 15592684; 15645378; 15650182; 15684389; 15757202; 15777972; 15833843; 15870434; 15882758; 16011248; 16044917; 16130169; 16189514; 16196087; 16232196; 16277028; 16313181; 16317582; 16415009; 16466905; 16531762; 16631833; 16739125; 16739379; 16759016; 16814409; 16848180; 16862176; 16891807; 16944571; 16957985; 17008916; 17103045; 17155928; 17197349; 17283532; 17314099; 17348207; 17359290; 17578003; 17591363; 17655525; 17688968; 17695492; 17885583; 17918157; 17975005; 18029348; 18058029; 18089805; 18154714; 18219290; 18239814; 18301251; 18307927; 18330957; 18408655; 18440302; 18457437; 18470881; 18476632; 18635542; 18668641; 18676749; 18700747; 18728402; 18781797; 18810774; 18815136; 18996649; 19024519; 19026164; 19060904; 19170058; 19183483; 19186179; 19263457; 19332021; 19513384; 19615732; 19619546; 19624895; 19655221; 19664043; 19664078; 19724852; 19852809; 19951590; 19956735; 20099494; 20101217; 20113651; 20145075; 20209495; 20301782; 20304626; 20403806; 20448457; 20508983; 20559153; 20560137; 20570897; 20599259; 20639865; 20671611; 20713695; 20841469; 20872186; 20877624; 20955383; 20959063; 21045303; 21080107; 21081666; 21085602; 21121676; 21139048; 21169412; 21176535; 21221850; 21265090; 21270158; 21273640; 21350102; 21442621; 21448569; 21469425; 21478336; 21484438; 21553004; 21575865; 21769563; 21846466; 21890473; 21906983; 21913743; 21963094; 21987572; 21988832; 22035418; 22053931; 22268729; 22290468; 22328561; 22349375; 22364921; 22421058; 22429576; 22451184; 22505724; 22531683; 22683585; 22718351; 22863883; 22869372; 22903495; 22920000; 22939629; 23000965; 23137649; 23158994; 23448979; 23464856; 23479363; 23519676; 23583378; 23679306; 23694823; 23725501; 23734265; 23768014; 23818346; 24457600 NME/NM23 nucleoside diphosphate kinase 1 Ensembl:ENSG00000239672 HGNC:7849 HPRD:01131 MIM:156490 Vega:OTTHUMG00000137474 Other designations: NDP kinase A|granzyme A-activated DNase|metastasis inhibition factor nm23|non-metastatic cells 1, protein (NM23A) expressed in|nucleoside diphosphate kinase A|tumor metastatic process-associated protein NME1 OGG:3000004925 Bin Zhao, Yue Liu, Oliver He HEL-S-109 NEFA WEB: http://www.ncbi.nlm.nih.gov/gene NUCB2 nucleobindin 2 4925 11p15.1 9606 11 Official from a nomenclature committee GO_0003677 (EC: IEA); GO_0005509 (EC: IEA); GO_0005515 (EC: IPI); GO_0005615 (EC: TAS, PMID: 7811391); GO_0005640 (EC: IEA); GO_0005783 (EC: IEA); GO_0005793 (EC: IDA, PMID: 15308636); GO_0005794 (EC: IDA); GO_0005829 (EC: TAS, PMID: 7811391); GO_0005886 (EC: TAS, PMID: 7811391); GO_0070062 (EC: IDA, PMID: 19199708) PMID: 7811391; 9639681; 10381334; 10915798; 11749975; 12087473; 12477932; 12909641; 14702039; 15308636; 15604093; 16344560; 16407280; 18029348; 18154733; 19199708; 19262995; 19351608; 19913121; 20030931; 20032201; 20427481; 20427483; 20625762; 20628086; 20813143; 20881960; 20937336; 21139048; 21145461; 21252251; 21459029; 21554911; 21653697; 21803054; 21890473; 21988594; 21988832; 22020667; 22036920; 22108805; 22203468; 22225987; 22270345; 22334726; 22367584; 22863883; 22950627; 23141462; 23155701; 23178145; 23266808; 23269222; 23346951; 23515787; 23613885; 23739643; 23764403; 23768444 nucleobindin 2 Ensembl:ENSG00000070081 HGNC:8044 HPRD:09726 MIM:608020 Vega:OTTHUMG00000166050 Other designations: DNA-binding protein NEFA|epididymis secretory protein Li 109|gastric cancer antigen Zg4|nesfatin-1|nucleobindin-2|nucleobinding 2|prepronefastin|prepronesfatin NUCB2 OGG:3000004938 Bin Zhao, Yue Liu, Oliver He IFI-4 OIAS OIASI WEB: http://www.ncbi.nlm.nih.gov/gene OAS1 2'-5'-oligoadenylate synthetase 1, 40/46kDa 4938 12q24.2 20140408 9606 12 protein-coding Official from a nomenclature committee GO_0001730 (EC: IDA, PMID: 11682059); GO_0003725 (EC: IDA, PMID: 12799444); GO_0005515 (EC: IPI); GO_0005524 (EC: TAS); GO_0005576 (EC: IEA); GO_0005634 (EC: IDA, PMID: 3753689); GO_0005634 (EC: IEA); GO_0005737 (EC: IDA, PMID: 19923450); GO_0005739 (EC: IEA); GO_0005783 (EC: IEA); GO_0005829 (EC: TAS); GO_0006006 (EC: IMP); GO_0006164 (EC: IDA, PMID: 11682059); GO_0008270 (EC: IDA, PMID: 11682059); GO_0009615 (EC: IDA, PMID: 18931074); GO_0019221 (EC: TAS); GO_0035457 (EC: IDA, PMID: 3753689); GO_0042593 (EC: IMP); GO_0045071 (EC: IDA, PMID: 18931074); GO_0046872 (EC: IEA); GO_0051259 (EC: IDA, PMID: 11682059); GO_0051607 (EC: IDA, PMID: 19923450); GO_0051607 (EC: IEA); GO_0060333 (EC: TAS); GO_0060337 (EC: TAS); GO_0060700 (EC: IDA, PMID: 19923450) PMID: 1651324; 1708818; 2411547; 2416561; 2426799; 2440675; 2456211; 2830497; 3121313; 3175763; 3753689; 3754863; 6348777; 8125298; 9407111; 9790745; 10464285; 11092454; 11682059; 11980899; 11986302; 12082089; 12447867; 12477932; 12799444; 12944978; 14702039; 15489334; 15732009; 15766558; 15850793; 15855350; 15865429; 15893726; 16014697; 16235172; 16541075; 16644715; 16712791; 16824203; 17092260; 17360168; 17963609; 18029348; 18931074; 19203244; 19247438; 19434718; 19462904; 19515215; 19559055; 19575500; 19665006; 19799013; 19923450; 19956105; 20079393; 20309637; 20588308; 20628624; 20679634; 21050126; 21182542; 21450824; 21638280; 21735172; 21935451; 21988832; 22709583; 22710942; 23011799; 23149075; 23196181; 23220500; 23319625; 23337612; 23455924; 23575436 2'-5'-oligoadenylate synthetase 1, 40/46kDa Ensembl:ENSG00000089127 HGNC:8086 HPRD:08879 MIM:164350 Vega:OTTHUMG00000169792 Other designations: (2-5')oligo(A) synthase 1|(2-5')oligo(A) synthetase 1|2',5'-oligo A synthetase 1|2',5'-oligoadenylate synthetase 1, 40/46kDa|2'-5' oligoadenylate synthetase 1 p48 isoform|2'-5' oligoadenylate synthetase 1 p52 isoform|2'-5'-oligoadenylate synthase 1|2'-5'-oligoisoadenylate synthetase 1|2-5A synthase 1|2-5A synthetase 1|E18/E16|p46/p42 OAS OAS1 OGG:3000005021 Bin Zhao, Yue Liu, Oliver He OT-R WEB: http://www.ncbi.nlm.nih.gov/gene OXTR oxytocin receptor 5021 3p25 20140408 9606 3 protein-coding Official from a nomenclature committee GO_0001967 (EC: IEA); GO_0001975 (EC: IEA); GO_0004990 (EC: IEA); GO_0005000 (EC: IEA); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 10858434); GO_0005902 (EC: IEA); GO_0005913 (EC: IEA); GO_0006936 (EC: TAS, PMID: 1313946); GO_0007166 (EC: TAS, PMID: 1313946); GO_0007204 (EC: IEA); GO_0007507 (EC: IEA); GO_0007565 (EC: IEA); GO_0007595 (EC: TAS, PMID: 1313946); GO_0007613 (EC: IEA); GO_0010701 (EC: IEA); GO_0016324 (EC: IEA); GO_0017046 (EC: IEA); GO_0021537 (EC: IEA); GO_0030431 (EC: IEA); GO_0032230 (EC: IEA); GO_0032355 (EC: IEA); GO_0032570 (EC: IEA); GO_0034059 (EC: IEA); GO_0034097 (EC: IEA); GO_0035176 (EC: IEA); GO_0042220 (EC: IEA); GO_0042493 (EC: IEA); GO_0042711 (EC: IEA); GO_0042713 (EC: IEA); GO_0042755 (EC: IEA); GO_0043434 (EC: IEA); GO_0045777 (EC: IEA); GO_0048565 (EC: IEA); GO_0051965 (EC: IEA); GO_0051968 (EC: IEA); GO_0060137 (EC: IEA); GO_0060206 (EC: IEA); GO_0060406 (EC: IEA); GO_0060455 (EC: IEA); GO_0070371 (EC: IEA); GO_0070474 (EC: IEA) PMID: 1313946; 7607693; 7798245; 7921229; 8077313; 8593829; 8593830; 9283088; 9433921; 10027615; 10453463; 10698266; 10858434; 10910058; 11140838; 11279203; 11955056; 12126740; 12161007; 12166628; 12270111; 12477932; 12810550; 12843193; 12955084; 14664707; 14691010; 14749664; 15035619; 15044599; 15089975; 15089977; 15093695; 15452121; 15591449; 15705593; 15831296; 15992526; 16042376; 16333859; 16754659; 16888077; 16966388; 17148753; 17383819; 17492653; 17726073; 17728669; 17893705; 17939166; 17952758; 18082926; 18207134; 18312604; 19001515; 19015103; 19086053; 19126785; 19336370; 19347709; 19376182; 19423652; 19461999; 19515497; 19598235; 19777562; 19845972; 19934046; 19943975; 20094064; 20096818; 20097922; 20196918; 20303388; 20347913; 20400491; 20413116; 20436377; 20452482; 20488544; 20547007; 20547038; 20585395; 20647384; 20670427; 20673868; 20708845; 20711752; 20724662; 20832055; 20926803; 21090345; 21208749; 21561435; 21734268; 21876222; 21896752; 21906983; 21934640; 21963428; 21964067; 21984889; 22015110; 22064162; 22084107; 22123970; 22146101; 22212599; 22296985; 22336563; 22357335; 22372486; 22421562; 22457427; 22487732; 22510359; 22563705; 22763666; 22809402; 22882465; 22892716; 22986294; 22999795; 23040540; 23089921; 23219106; 23252931; 23284802; 23354128; 23355275; 23470776; 23637833; 23678036; 23684879; 23889750; 23915847; 24367110 oxytocin receptor Ensembl:ENSG00000180914 HGNC:8529 HPRD:01328 MIM:167055 Vega:OTTHUMG00000090537 OXTR OGG:3000005034 Bin Zhao, Yue Liu, Oliver He DSI ERBA2L GIT P4Hbeta PDI PDIA1 PHDB PO4DB PO4HB PROHB WEB: http://www.ncbi.nlm.nih.gov/gene P4HB prolyl 4-hydroxylase, beta polypeptide 5034 17q25 9606 17 Official from a nomenclature committee GO_0003756 (EC: IBA); GO_0004656 (EC: IDA, Qualifier: contributes_to, PMID: 7753822); GO_0005515 (EC: IPI, PMID: 12095988); GO_0005576 (EC: NAS, PMID: 14718574); GO_0005783 (EC: IDA, PMID: 12095988); GO_0005788 (EC: TAS); GO_0005793 (EC: IDA, PMID: 15308636); GO_0005886 (EC: IEA); GO_0006457 (EC: IBA); GO_0006662 (EC: IEA); GO_0015035 (EC: IEA); GO_0016222 (EC: IDA, PMID: 7753822); GO_0018401 (EC: IDA, PMID: 7753822); GO_0030198 (EC: TAS); GO_0034976 (EC: IMP, PMID: 12095988); GO_0042157 (EC: TAS); GO_0042470 (EC: IEA); GO_0044281 (EC: TAS); GO_0044822 (EC: IDA); GO_0045454 (EC: IEA); GO_0046982 (EC: IEA); GO_0055114 (EC: IDA, PMID: 7753822); GO_0055114 (EC: TAS, PMID: 2846539); GO_0070062 (EC: IDA, PMID: 19199708); GO_0071456 (EC: IMP, PMID: 12095988); GO_1902175 (EC: IMP, PMID: 12095988) PMID: 1286669; 1339453; 1559965; 1597478; 1667665; 1677563; 1699755; 2079031; 2846539; 3032969; 3034602; 3342239; 3467900; 3611107; 7753822; 8111381; 8580850; 8672469; 9150948; 9399589; 10329688; 10383197; 10436013; 10636893; 11181151; 11257307; 11707400; 11790298; 11847130; 12095988; 12218051; 12218052; 12475965; 12477932; 12485997; 12493773; 12643545; 12665801; 12874193; 14500733; 14592831; 14702039; 14718574; 14871477; 15146195; 15158710; 15231747; 15308636; 15324660; 15358778; 15489334; 15590633; 15611098; 15644496; 15695804; 15952740; 16169070; 16303743; 16344560; 16847061; 17055437; 17081065; 17301129; 17353931; 17620599; 18029348; 18781797; 19199708; 19471022; 19890397; 19913121; 20000738; 20360068; 20628086; 20668226; 21081666; 21139048; 21145461; 21299467; 21319273; 21373848; 21693764; 21890473; 21906983; 21963094; 21988832; 22079093; 22174317; 22190034; 22268729; 22304920; 22337587; 22536838; 22586326; 22863883; 22936677; 22939629; 23000965; 23141538; 23246001; 23337974; 23444257; 23455922; 23824909; 23862649; 23956138; 24244333; 24250222; 24457600 prolyl 4-hydroxylase, beta polypeptide Ensembl:ENSG00000185624 HGNC:8548 HPRD:07181 MIM:176790 Vega:OTTHUMG00000150269 Other designations: cellular thyroid hormone-binding protein|collagen prolyl 4-hydroxylase beta|glutathione-insulin transhydrogenase|p55|procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide|prolyl 4-hydroxylase subunit beta|protein disulfide isomerase family A, member 1|protein disulfide isomerase-associated 1|protein disulfide isomerase/oxidoreductase|protein disulfide-isomerase|protocollagen hydroxylase|thyroid hormone-binding protein p55 P4HB OGG:3000005045 Bin Zhao, Yue Liu, Oliver He FUR PACE PCSK3 SPC1 WEB: http://www.ncbi.nlm.nih.gov/gene FURIN furin (paired basic amino acid cleaving enzyme) 5045 15q26.1 20140408 9606 15 protein-coding Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0002020 (EC: IPI, PMID: 14744861); GO_0004175 (EC: IDA, PMID: 17010968); GO_0004252 (EC: IDA, PMID: 10567353); GO_0004867 (EC: IDA, PMID: 10567353); GO_0005615 (EC: IDA, Qualifier: NOT, PMID: 10567353); GO_0005796 (EC: TAS); GO_0005802 (EC: IDA, PMID: 14744861); GO_0005886 (EC: TAS); GO_0006465 (EC: IDA, PMID: 16912035); GO_0006508 (EC: TAS); GO_0007179 (EC: TAS); GO_0007219 (EC: TAS); GO_0008233 (EC: IDA, PMID: 10526337); GO_0008283 (EC: IMP, PMID: 15899807); GO_0009966 (EC: IEA); GO_0009986 (EC: IDA, PMID: 16537537); GO_0010951 (EC: IDA, PMID: 10567353); GO_0016021 (EC: IEA); GO_0016032 (EC: TAS); GO_0016485 (EC: IDA, PMID: 10526337); GO_0016485 (EC: IMP, PMID: 15899807); GO_0016486 (EC: IDA, PMID: 9242664); GO_0017187 (EC: TAS); GO_0019058 (EC: IEP, PMID: 8940009); GO_0019068 (EC: TAS); GO_0019082 (EC: TAS); GO_0022617 (EC: TAS); GO_0030140 (EC: IDA, PMID: 15078902); GO_0030198 (EC: TAS); GO_0030574 (EC: TAS); GO_0032455 (EC: TAS); GO_0032804 (EC: IDA, PMID: 16912035); GO_0032902 (EC: IDA, PMID: 8615794); GO_0032904 (EC: IDA, Qualifier: NOT, PMID: 10567353); GO_0032911 (EC: IMP, PMID: 15899807); GO_0032940 (EC: IDA, PMID: 8615794); GO_0042176 (EC: IMP, PMID: 15899807); GO_0042277 (EC: IDA, PMID: 8940009); GO_0043043 (EC: IDA, PMID: 8262946); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS); GO_0045121 (EC: IDA, PMID: 17010968); GO_0046872 (EC: IEA); GO_0048011 (EC: TAS); GO_0048406 (EC: IDA, PMID: 8615794); GO_0051044 (EC: IC, PMID: 17010968); GO_0052548 (EC: IDA, PMID: 14744861); GO_0070062 (EC: IDA, PMID: 19199708) PMID: 1360148; 1571548; 1629222; 1713771; 1741956; 2112085; 2251280; 2408021; 2674906; 3023061; 7508380; 7639757; 7690548; 7721880; 7737999; 7774724; 7781597; 7782070; 8020465; 8163529; 8174106; 8189547; 8262946; 8546712; 8615794; 8670066; 8846780; 8940009; 8995623; 9094426; 9166946; 9242664; 9412467; 9442015; 9521771; 9599222; 9642263; 9653148; 9695949; 9827567; 9927419; 10037747; 10050053; 10225274; 10373500; 10409610; 10452538; 10526337; 10567353; 10593987; 10887202; 10888676; 10900462; 11071887; 11237874; 11294867; 11323410; 11331585; 11380615; 11416205; 11422372; 11571266; 11723118; 11804956; 11861638; 11861826; 11921231; 12006600; 12058031; 12058067; 12071862; 12220680; 12354117; 12411321; 12460941; 12477932; 12482870; 12547702; 12584323; 12586364; 12644459; 12670890; 12736257; 12787574; 14596804; 14644155; 14739277; 14741044; 14744861; 15078902; 15082773; 15135058; 15240540; 15247425; 15371436; 15489334; 15564468; 15584904; 15606899; 15611046; 15637056; 15659365; 15899807; 15911696; 16407210; 16537537; 16600625; 16627761; 16648485; 16912035; 16942750; 17010968; 17283058; 17301129; 17360815; 17477394; 17525470; 17641413; 17905608; 17905609; 17909005; 17938254; 17948127; 18037384; 18064302; 18174282; 18245819; 18323532; 18343183; 18353966; 18467449; 18544638; 18546152; 18665212; 18826955; 19056739; 19152512; 19193799; 19199708; 19322201; 19477160; 19492430; 19541935; 19913121; 19998449; 20055586; 20062797; 20101215; 20605791; 20608975; 20628086; 20634490; 20635860; 20707915; 20811902; 20945401; 21147780; 21296375; 21406565; 21503879; 21550985; 21805236; 21805237; 21880759; 21889147; 21890473; 21909115; 21988832; 22038627; 22247010; 22479394; 22505724; 22577343; 22679642; 22808247; 22995191; 23000965; 23135270; 23302673; 23390091; 23558288; 23568742; 23598405; 23653353; 23661674; 23686857; 23744066; 23775089; 23936445 furin (paired basic amino acid cleaving enzyme) Ensembl:ENSG00000140564 HGNC:8568 HPRD:00653 MIM:136950 Vega:OTTHUMG00000149831 FURIN OGG:3000005095 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene PCCA propionyl CoA carboxylase, alpha polypeptide 5095 RP11-151A6.1 13q32 9606 13 Official from a nomenclature committee GO_0004075 (EC: IEA); GO_0004658 (EC: IEA); GO_0005524 (EC: IEA); GO_0005759 (EC: TAS); GO_0005829 (EC: TAS); GO_0006635 (EC: TAS); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0006768 (EC: TAS); GO_0009374 (EC: TAS, PMID: 3460076); GO_0019626 (EC: TAS); GO_0019899 (EC: IPI, PMID: 19157941); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0046872 (EC: IEA) PMID: 1427880; 2740237; 3460076; 3555348; 3687944; 7656816; 8125298; 8188292; 8434582; 8889548; 8895530; 10101253; 10329019; 10502773; 11136555; 11592820; 11749052; 12226704; 12385775; 12477932; 12559849; 14702039; 15059621; 15489334; 15890657; 16344560; 16751776; 17051315; 17966092; 18457437; 18678647; 19157941; 19157943; 19296078; 19913121; 20301313; 20379614; 20628086; 20725044; 20877624; 21139048; 21642987; 22156789; 22593918; 23396134; 23455922; 24244333 propionyl CoA carboxylase, alpha polypeptide Other designations: PCCase alpha subunit|pccA complementation group|propanoyl-CoA:carbon dioxide ligase alpha subunit|propionyl Coenzyme A carboxylase, alpha polypeptide|propionyl-CoA carboxylase alpha chain, mitochondrial PCCA OGG:3000005101 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene PCDH9 protocadherin 9 5101 RP11-335P18.3 13q21.32 9606 13 Official from a nomenclature committee GO_0005509 (EC: IEA); GO_0005886 (EC: IEA); GO_0007156 (EC: IEA); GO_0016021 (EC: IEA); GO_0030900 (EC: IEA) PMID: 9787079; 10716726; 10817752; 10835267; 12477932; 14702039; 15057823; 16147992; 16344560; 19322201; 19913121; 20379614; 20628086; 21552555; 21875946; 22300792; 22424883; 23064961; 24250222 protocadherin 9 Other designations: cadherin superfamily protein VR4-11|protocadherin-9 PCDH9 OGG:3000005105 Bin Zhao, Yue Liu, Oliver He PEPCK-C PEPCK1 PEPCKC WEB: http://www.ncbi.nlm.nih.gov/gene PCK1 phosphoenolpyruvate carboxykinase 1 (soluble) 5105 20q13.31 20140408 9606 20 protein-coding Official from a nomenclature committee GO_0000287 (EC: IDA, PMID: 11851336); GO_0004613 (EC: ISS); GO_0005525 (EC: IDA, PMID: 11851336); GO_0005737 (EC: ISS); GO_0005829 (EC: TAS); GO_0005975 (EC: TAS); GO_0006006 (EC: IMP, PMID: 14764811); GO_0006006 (EC: TAS); GO_0006094 (EC: IEA); GO_0006094 (EC: ISS); GO_0006094 (EC: TAS); GO_0006107 (EC: IEA); GO_0006475 (EC: IDA); GO_0014823 (EC: IEA); GO_0017144 (EC: TAS); GO_0019003 (EC: IEA); GO_0030145 (EC: IDA, PMID: 11851336); GO_0031406 (EC: IDA, PMID: 11851336); GO_0032868 (EC: IDA, PMID: 14764811); GO_0042593 (EC: ISS); GO_0044281 (EC: TAS); GO_0046327 (EC: ISS); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 1492743; 1657985; 2993287; 8325643; 8432541; 8490617; 8547315; 11689615; 11780052; 11851336; 11997389; 12237288; 12324453; 12477932; 14744869; 14764811; 15046742; 15489334; 15951444; 16132948; 16144962; 16282543; 16341674; 16344560; 16620271; 16978381; 17192490; 17440948; 17495004; 18029348; 18460190; 18492826; 18660489; 18801732; 18830724; 18976975; 18996102; 19021757; 19056482; 19056867; 19070910; 19329064; 19578796; 19725958; 19913121; 20098747; 20134411; 20574532; 20602615; 20628086; 20682687; 20691246; 20800603; 21145461; 21152065; 21726808; 21832049; 21906983; 21988832; 22489460; 23092637; 23149075; 23300278; 23465595; 23940030 phosphoenolpyruvate carboxykinase 1 (soluble) Ensembl:ENSG00000124253 HGNC:8724 HPRD:02028 MIM:614168 Vega:OTTHUMG00000032825 Other designations: PEP carboxykinase|phosphoenolpyruvate carboxykinase, cytosolic|phosphoenolpyruvate carboxykinase, cytosolic [GTP]|phosphoenolpyruvate carboxylase|phosphopyruvate carboxylase PCK1 OGG:3000005106 Bin Zhao, Yue Liu, Oliver He PEPCK PEPCK-M PEPCK2 WEB: http://www.ncbi.nlm.nih.gov/gene PCK2 phosphoenolpyruvate carboxykinase 2 (mitochondrial) 5106 14q11.2 9606 14 Official from a nomenclature committee GO_0004611 (EC: TAS, PMID: 8645161); GO_0004613 (EC: IEA); GO_0005515 (EC: IPI); GO_0005525 (EC: IEA); GO_0005739 (EC: IDA); GO_0005759 (EC: TAS); GO_0005975 (EC: TAS); GO_0006006 (EC: TAS); GO_0006090 (EC: IEA); GO_0006094 (EC: IEA); GO_0006094 (EC: TAS); GO_0006107 (EC: IEA); GO_0006116 (EC: IEA); GO_0032024 (EC: IEA); GO_0044281 (EC: TAS); GO_0046872 (EC: IEA); GO_0051384 (EC: IEA); GO_0071333 (EC: IEA) PMID: 8645161; 9657976; 12477932; 12916001; 15315819; 15489334; 16132948; 17097062; 18660489; 19521512; 19587243; 20682687; 20797423; 20877624; 21139048; 21733854; 21832049; 21906983; 21988832; 22955269 phosphoenolpyruvate carboxykinase 2 (mitochondrial) Ensembl:ENSG00000100889 HGNC:8725 HPRD:02026 MIM:614095 Vega:OTTHUMG00000028791 Other designations: PEP carboxykinase|phosphoenolpyruvate carboxykinase [GTP], mitochondrial|phosphoenolpyruvate carboxylase|phosphopyruvate carboxylase PCK2 OGG:3000005133 Bin Zhao, Yue Liu, Oliver He CD279 PD-1 PD1 SLEB2 hPD-1 hPD-l hSLE1 WEB: http://www.ncbi.nlm.nih.gov/gene PDCD1 programmed cell death 1 5133 2q37.3 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0004871 (EC: TAS, PMID: 1396582); GO_0005515 (EC: IPI); GO_0005886 (EC: TAS); GO_0006915 (EC: IEA); GO_0006959 (EC: TAS, PMID: 9332365); GO_0007165 (EC: TAS, PMID: 1396582); GO_0007275 (EC: TAS, PMID: 9332365); GO_0009897 (EC: IEA); GO_0016021 (EC: IEA); GO_0031295 (EC: TAS) PMID: 1396582; 7851902; 9141617; 9332365; 9843982; 9843983; 10677248; 10677315; 11224527; 12095712; 12402038; 12477932; 12517932; 12719480; 12893276; 14617032; 14730631; 15022318; 15188352; 15322919; 15334473; 15352422; 15818672; 15883854; 15912506; 15934088; 15959535; 16171790; 16227604; 16265694; 16278812; 16471222; 16493037; 16917489; 16921384; 16954372; 16956940; 16988698; 17002900; 17024563; 17064404; 17130567; 17136123; 17203303; 17228327; 17272504; 17311651; 17344889; 17468813; 17490403; 17535987; 17567698; 17570250; 17603844; 17610472; 17641065; 17721918; 17868872; 17885290; 17942371; 17963598; 17968013; 17999073; 18037500; 18041714; 18042085; 18056444; 18067228; 18069935; 18096476; 18160439; 18171281; 18173375; 18174230; 18203952; 18250483; 18294387; 18322304; 18337305; 18401354; 18440040; 18448390; 18455515; 18490780; 18494554; 18510628; 18549878; 18550794; 18566376; 18578969; 18594468; 18676751; 18680238; 18707923; 18756934; 18768824; 18771758; 18799583; 18822202; 18830259; 18925909; 18981091; 19035512; 19050238; 19056397; 19058313; 19074163; 19095563; 19116915; 19141860; 19147248; 19160029; 19197939; 19202444; 19220647; 19224853; 19234630; 19263877; 19332785; 19380770; 19395117; 19420358; 19423728; 19439344; 19449188; 19468750; 19500502; 19505258; 19539220; 19564339; 19581275; 19651643; 19695683; 19739236; 19759858; 19794071; 19800335; 19811417; 19811426; 19828602; 19900372; 19949078; 19959217; 19998245; 20012629; 20066438; 20070620; 20087161; 20113370; 20128032; 20185964; 20381020; 20388336; 20445553; 20447384; 20473887; 20506224; 20514052; 20518841; 20587542; 20617899; 20636820; 20657553; 20661763; 20668808; 20677149; 20693422; 20700634; 20709947; 20738778; 20819923; 20825974; 20826917; 20837075; 20848568; 20881011; 20883163; 20886079; 20890291; 20943073; 20959405; 20975732; 21064032; 21084749; 21091911; 21110433; 21113674; 21148500; 21161353; 21237493; 21263070; 21268005; 21269571; 21276005; 21291295; 21328438; 21346771; 21376795; 21383382; 21408177; 21442435; 21481848; 21487727; 21514692; 21547439; 21562156; 21645441; 21651862; 21652684; 21659460; 21712100; 21717461; 21791547; 21795591; 21851845; 21856939; 21868077; 21876620; 21907333; 21908482; 21912640; 21914188; 21927903; 21943489; 21961966; 21982860; 21989349; 22039410; 22042085; 22105417; 22133721; 22152383; 22153879; 22205715; 22246361; 22274654; 22322668; 22342451; 22397719; 22430646; 22441249; 22466343; 22503210; 22532845; 22549384; 22635166; 22722467; 22740686; 22742708; 22797302; 22892379; 22894700; 22895698; 22900886; 22916009; 22956035; 23041554; 23101188; 23189845; 23209326; 23220495; 23267208; 23288508; 23291409; 23297127; 23300177; 23331211; 23383287; 23398844; 23403273; 23417675; 23458521; 23504559; 23521696; 23610399; 23620109; 23628397; 23661793; 23732914; 23772031; 23773130; 23792703; 23907003; 23918986; 24035365; 24127452; 24138884; 24240160 programmed cell death 1 Ensembl:ENSG00000188389 HGNC:8760 HPRD:02590 MIM:600244 Vega:OTTHUMG00000151342 Other designations: programmed cell death protein 1|protein PD-1|systemic lupus erythematosus susceptibility 2 PDCD1 OGG:3000005138 Bin Zhao, Yue Liu, Oliver He CGS-PDE PDE2A1 PED2A4 cGSPDE WEB: http://www.ncbi.nlm.nih.gov/gene PDE2A phosphodiesterase 2A, cGMP-stimulated 5138 11q13.4 9606 11 Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 17329248); GO_0004112 (EC: IDA, PMID: 15938621); GO_0004118 (EC: IDA, PMID: 17329248); GO_0005262 (EC: TAS, PMID: 10375378); GO_0005515 (EC: IPI, PMID: 17329248); GO_0005634 (EC: IDA, PMID: 10375378); GO_0005737 (EC: IDA, PMID: 10375378); GO_0005759 (EC: ISS); GO_0005783 (EC: ISS); GO_0005794 (EC: ISS); GO_0005829 (EC: IDA, PMID: 17329248); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA, PMID: 19252089); GO_0005886 (EC: IDA, Qualifier: colocalizes_with, PMID: 17329248); GO_0006198 (EC: IDA, PMID: 14687666); GO_0006198 (EC: IMP, PMID: 19252089); GO_0006626 (EC: ISS); GO_0007596 (EC: TAS); GO_0008144 (EC: IDA, PMID: 15938621); GO_0008144 (EC: IPI, PMID: 15938621); GO_0008152 (EC: IDA, PMID: 17329248); GO_0019933 (EC: IMP, PMID: 17704206); GO_0019934 (EC: IMP, PMID: 17704206); GO_0030224 (EC: IEP, PMID: 14687666); GO_0030424 (EC: IEA); GO_0030425 (EC: IEA); GO_0030552 (EC: IMP, PMID: 15938621); GO_0030553 (EC: IDA, PMID: 17329248); GO_0030553 (EC: IMP, PMID: 15938621); GO_0030818 (EC: ISS); GO_0030911 (EC: IPI, PMID: 17329248); GO_0033159 (EC: IDA, PMID: 17329248); GO_0035690 (EC: IEP, PMID: 14687666); GO_0035690 (EC: IMP, PMID: 15938621); GO_0036006 (EC: IDA, PMID: 14687666); GO_0042734 (EC: ISS); GO_0042803 (EC: IPI, PMID: 19828435); GO_0043116 (EC: IMP, PMID: 17704206); GO_0043117 (EC: IMP, PMID: 17704206); GO_0046069 (EC: IDA, PMID: 14687666); GO_0046872 (EC: IEA); GO_0048471 (EC: IDA, PMID: 10375378); GO_0050729 (EC: ISS); GO_0061028 (EC: ISS); GO_0070588 (EC: TAS, PMID: 10375378); GO_0071260 (EC: ISS); GO_0071321 (EC: IDA, PMID: 17704206); GO_0071560 (EC: IEP, PMID: 17704206); GO_0097011 (EC: IDA, PMID: 14687666) PMID: 8557689; 9210593; 10375378; 11156964; 12038792; 12271124; 12477932; 14687666; 14702039; 15650061; 15938621; 16344560; 17329248; 17704206; 19252089; 19390057; 19506089; 19689430; 19828435; 19913121; 20351714; 20395239; 20628086; 21697861; 21724846; 21766240; 21987572; 22446963; 23381931; 23810893; 23899287 phosphodiesterase 2A, cGMP-stimulated Ensembl:ENSG00000186642 HGNC:8777 HPRD:04041 MIM:602658 Vega:OTTHUMG00000102045 Other designations: cGMP-dependent 3',5'-cyclic phosphodiesterase|cGMP-stimulated phosphodiesterase 1|cGMP-stimulated phosphodiesterase 4|cyclic GMP-stimulated phosphodiesterase PDE2A OGG:3000005166 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene PDK4 pyruvate dehydrogenase kinase, isozyme 4 5166 7q21.3 9606 7 Official from a nomenclature committee GO_0004672 (EC: IDA, PMID: 18658136); GO_0004674 (EC: IEA); GO_0004740 (EC: ISS); GO_0005524 (EC: IDA, PMID: 18658136); GO_0005739 (EC: TAS, PMID: 8798399); GO_0005743 (EC: IEA); GO_0005759 (EC: TAS); GO_0006006 (EC: IEA); GO_0006090 (EC: TAS); GO_0006468 (EC: IDA, PMID: 18658136); GO_0006468 (EC: ISS); GO_0006468 (EC: TAS, PMID: 8798399); GO_0006885 (EC: ISS); GO_0008286 (EC: IMP); GO_0009267 (EC: IDA, PMID: 14966024); GO_0010510 (EC: IMP); GO_0010510 (EC: TAS); GO_0010565 (EC: ISS); GO_0010906 (EC: IMP); GO_0042304 (EC: IMP); GO_0042593 (EC: ISS); GO_0042594 (EC: ISS); GO_0044237 (EC: TAS); GO_0044281 (EC: TAS); GO_0045124 (EC: IEA); GO_0046320 (EC: ISS); GO_0071398 (EC: IMP); GO_0072593 (EC: IMP); GO_2000811 (EC: IMP) PMID: 7499431; 8125298; 8798399; 9787110; 11001762; 11485553; 11486000; 11701428; 11978179; 12145475; 12477932; 12573248; 12582211; 12606505; 12676647; 12690205; 12853948; 14702039; 14966024; 15047604; 15489334; 15516373; 15581486; 15618316; 15721319; 15776585; 15955060; 16344560; 16757381; 17623298; 17652214; 17669420; 18468620; 18519799; 18658136; 18660489; 20715114; 20877624; 21852536; 21883960; 21904029; 21906983; 21963094; 22019269; 23050013 pyruvate dehydrogenase kinase, isozyme 4 Other designations: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial|[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4, mitochondrial|pyruvate dehydrogenase kinase, isoenzyme 4|pyruvate dehydrogenase, lipoamide, kinase isozyme 4, mitochondrial PDK4 OGG:3000005209 Bin Zhao, Yue Liu, Oliver He IPFK2 PFK2 WEB: http://www.ncbi.nlm.nih.gov/gene PFKFB3 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 5209 RP11-298K24.3 10p15.1 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0003873 (EC: NAS, PMID: 8830046); GO_0004331 (EC: IEA); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005829 (EC: TAS); GO_0005975 (EC: TAS); GO_0006000 (EC: IEA); GO_0006003 (EC: IEA); GO_0006006 (EC: TAS); GO_0006096 (EC: TAS); GO_0044281 (EC: TAS); GO_0046835 (EC: NAS, PMID: 8830046) PMID: 7574501; 8830046; 9092801; 9146922; 9276680; 9828130; 10072580; 10077634; 10508479; 10673355; 11245921; 11245987; 12384552; 12477932; 12935880; 12963966; 14702039; 15466858; 15489334; 15896703; 16115917; 16306349; 16311927; 16316985; 16344560; 16385451; 16698023; 17143338; 17353931; 17499765; 17620599; 18039179; 19322201; 19473963; 19490427; 20080744; 20453422; 20639865; 20921411; 21139048; 21402913; 21860432; 21890473; 21906983; 21963094; 21987444; 22053931; 22106309; 22275052; 22505724; 23000965; 23084401; 23548149; 23911327; 24043759 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 Ensembl:ENSG00000170525 HGNC:8874 HPRD:05612 MIM:605319 Vega:OTTHUMG00000017621 Other designations: 6-phosphofructo-2-kinase/ fructose-2,6-bisphosphatase|6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase|6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3|6PF-2-K/Fru-2,6-P2ase 3|6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme|PFK/FBPase 3|fructose-6-phosphate,2-kinase/fructose-2, 6-bisphosphatase|iPFK-2|inducible 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase|renal carcinoma antigen NY-REN-56 PFKFB3 OGG:3000005241 Bin Zhao, Yue Liu, Oliver He NR3C3 PR WEB: http://www.ncbi.nlm.nih.gov/gene PGR progesterone receptor 5241 11q22-q23 9606 11 Official from a nomenclature committee GO_0001542 (EC: IEA); GO_0002070 (EC: IEA); GO_0003677 (EC: TAS, PMID: 3551956); GO_0003707 (EC: IEA); GO_0004879 (EC: IEA); GO_0005102 (EC: IPI, PMID: 12771131); GO_0005496 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12011095); GO_0005654 (EC: TAS); GO_0005741 (EC: IEA); GO_0006367 (EC: TAS); GO_0007165 (EC: TAS, PMID: 1557371); GO_0007267 (EC: TAS, PMID: 1557371); GO_0008270 (EC: IEA); GO_0010467 (EC: TAS); GO_0010629 (EC: IEP); GO_0019899 (EC: IPI, PMID: 12039952); GO_0043565 (EC: IEA); GO_0050678 (EC: IEA); GO_0050847 (EC: IEA); GO_0060748 (EC: IEA) PMID: 1557371; 2328727; 2736623; 3551956; 6849751; 7481822; 7983041; 7989520; 8626413; 8671234; 9115274; 9223281; 9305541; 9598870; 9620806; 9671457; 9710597; 9891052; 10338464; 10480874; 10655479; 10684807; 10722692; 10750018; 10757795; 10819762; 10840043; 10903152; 11110801; 11117526; 11117529; 11323389; 11326686; 11545730; 11668223; 11668524; 11677150; 11689696; 11717311; 11821088; 11918216; 11948021; 12009358; 12010857; 12011095; 12021276; 12021930; 12038703; 12039952; 12048256; 12088866; 12090595; 12101239; 12113882; 12114521; 12149147; 12174912; 12218173; 12297552; 12402980; 12414909; 12446585; 12466272; 12511607; 12517594; 12529333; 12538866; 12554765; 12554776; 12556966; 12574227; 12579263; 12594000; 12612073; 12644308; 12650698; 12650714; 12672823; 12673676; 12699057; 12748280; 12759236; 12771131; 12861133; 12874288; 12899921; 12917342; 12943706; 14500352; 14519645; 14551264; 14557830; 14586360; 14617569; 14634838; 14667966; 14667967; 14684847; 14764828; 14769635; 14978266; 15001645; 15019994; 15036714; 15084343; 15084345; 15102680; 15171716; 15184270; 15219637; 15272913; 15272917; 15282304; 15282324; 15308690; 15330195; 15381922; 15509639; 15535845; 15555905; 15562029; 15563544; 15572421; 15579801; 15598772; 15601848; 15607534; 15613410; 15632380; 15654614; 15694343; 15694360; 15698546; 15718480; 15728178; 15743833; 15797250; 15798179; 15807882; 15863956; 15866121; 15937332; 15996107; 16109739; 16126772; 16168103; 16244490; 16323958; 16331541; 16339279; 16339776; 16352595; 16360811; 16384861; 16439457; 16477637; 16478993; 16481409; 16484338; 16524927; 16537702; 16614108; 16646051; 16647340; 16728408; 16740656; 16759928; 16762974; 16772530; 16799708; 16901007; 16920727; 16973758; 16985250; 16999816; 17006756; 17018785; 17021053; 17081988; 17224149; 17259978; 17277083; 17291258; 17293450; 17316413; 17347654; 17413977; 17484509; 17512111; 17522428; 17592773; 17599361; 17609436; 17609999; 17646097; 17717077; 17727850; 17785366; 17805208; 17845055; 17847935; 17885486; 17896177; 17914494; 17919323; 17950525; 17951080; 17958742; 17965625; 17992477; 18029348; 18042733; 18048499; 18096667; 18184269; 18189290; 18197009; 18202149; 18215457; 18219286; 18249378; 18276950; 18281038; 18313072; 18316616; 18321550; 18375150; 18378698; 18384825; 18386458; 18391223; 18392676; 18394649; 18421469; 18481002; 18483177; 18483761; 18508999; 18510611; 18511503; 18557990; 18617611; 18628428; 18629635; 18631401; 18636124; 18645713; 18665217; 18668363; 18676680; 18681990; 18683043; 18686353; 18691687; 18722616; 18776045; 18798271; 18801410; 18818748; 18819936; 18835831; 18850387; 18980792; 19019335; 19031960; 19056530; 19061285; 19064572; 19093516; 19094228; 19095059; 19106225; 19124506; 19147544; 19147702; 19152063; 19154258; 19170196; 19175383; 19196877; 19205874; 19205877; 19208263; 19208313; 19211567; 19217090; 19220894; 19258476; 19267271; 19284643; 19296948; 19299443; 19309393; 19330259; 19336370; 19339282; 19357364; 19367380; 19372234; 19382201; 19383545; 19389812; 19415745; 19419938; 19423537; 19423654; 19436038; 19458022; 19462450; 19476621; 19497994; 19499404; 19527514; 19551860; 19555469; 19574343; 19574486; 19604497; 19609353; 19625176; 19636371; 19657752; 19673915; 19676041; 19692168; 19696694; 19701771; 19706513; 19715581; 19720911; 19739075; 19762712; 19782484; 19809499; 19820388; 19835506; 19838027; 19846565; 19852793; 19887485; 19913121; 19940123; 19940364; 19952285; 19952937; 19961842; 19996313; 20000807; 20019164; 20026682; 20063045; 20076999; 20082859; 20082875; 20087430; 20087433; 20090851; 20096719; 20097334; 20123965; 20124487; 20140262; 20148360; 20167054; 20228224; 20299092; 20305341; 20308044; 20308837; 20335148; 20337826; 20374701; 20379614; 20381444; 20392877; 20400074; 20404095; 20436503; 20453000; 20467438; 20484415; 20547493; 20550710; 20557310; 20586553; 20592363; 20628086; 20634197; 20646629; 20661446; 20690804; 20713855; 20716560; 20719308; 20734064; 20814185; 20829392; 20844986; 20861224; 20872186; 20873988; 20890067; 20920367; 20946440; 20956022; 20959426; 20960162; 20962507; 21029696; 21062926; 21085752; 21086036; 21093858; 21095220; 21119048; 21141441; 21145845; 21148628; 21152100; 21152841; 21184272; 21184768; 21243274; 21269613; 21271213; 21273440; 21340479; 21397694; 21422407; 21432776; 21437249; 21444077; 21447625; 21459801; 21464042; 21491087; 21518957; 21531767; 21544804; 21600232; 21619605; 21655654; 21700456; 21730049; 21736840; 21749714; 21751163; 21762477; 21764500; 21815951; 21816898; 21840784; 21840910; 21877015; 21901395; 21980607; 22004841; 22022496; 22047608; 22057681; 22092403; 22093824; 22102068; 22105149; 22107784; 22119825; 22199306; 22201220; 22203942; 22217299; 22281037; 22329840; 22369759; 22394363; 22396492; 22414972; 22419721; 22466340; 22492871; 22496908; 22509838; 22529366; 22535964; 22545144; 22564243; 22580007; 22590818; 22613790; 22633539; 22697792; 22722322; 22727345; 22808109; 22891251; 22972951; 23018797; 23022996; 23029355; 23060300; 23177737; 23199240; 23209664; 23222299; 23307470; 23349706; 23397283; 23474171; 23485561; 23490124; 23506845; 23558572; 23570281; 23574718; 23603247; 23666965; 23668054; 23687977; 23699411; 23723333; 23764995; 23810009; 23812730; 23818346; 23818347; 23818363; 23859042; 23873108; 23880761; 23881388; 23907837; 23995840; 24036907; 24269135; 24302725 progesterone receptor Ensembl:ENSG00000082175 HGNC:8910 HPRD:07077 MIM:607311 Vega:OTTHUMG00000167531 Other designations: nuclear receptor subfamily 3 group C member 3 PGR OGG:3000005288 Bin Zhao, Yue Liu, Oliver He PI3K-C2-gamma PI3K-C2GAMMA WEB: http://www.ncbi.nlm.nih.gov/gene PIK3C2G phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 gamma 5288 12p12 9606 12 Official from a nomenclature committee GO_0005524 (EC: IEA); GO_0005829 (EC: TAS); GO_0005886 (EC: IBA); GO_0005942 (EC: IBA); GO_0006644 (EC: TAS); GO_0006661 (EC: TAS); GO_0006935 (EC: IEA); GO_0008150 (EC: ND); GO_0016303 (EC: NAS, PMID: 9878262); GO_0016307 (EC: NAS, PMID: 9878262); GO_0035005 (EC: IBA); GO_0035091 (EC: IEA); GO_0036092 (EC: NAS, PMID: 9878262); GO_0044281 (EC: TAS); GO_0048015 (EC: IEA) PMID: 8636073; 8798481; 9247029; 9341793; 9394803; 9446795; 9514948; 9516481; 9708406; 9808187; 9878262; 10208934; 10985305; 11154208; 11156964; 11289809; 11994280; 12077252; 12477932; 12526811; 12551992; 12584329; 12960231; 14602571; 15689238; 16081599; 16524887; 17157319; 17632570; 17893707; 17991425; 18453587; 18854243; 18996102; 20019835; 20602615; 20818790; 21029719; 21114830; 22369086; 24086445 phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 gamma Ensembl:ENSG00000139144 HGNC:8973 HPRD:16416 MIM:609001 Vega:OTTHUMG00000168841 Other designations: PTDINS-3-kinase C2 gamma|phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit gamma|phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing gamma polypeptide|phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma|phosphoinositide-3-kinase, class 2, gamma polypeptide|ptdIns-3-kinase C2 subunit gamma PIK3C2G OGG:3000005290 Bin Zhao, Yue Liu, Oliver He CLOVE CWS5 MCAP MCM MCMTC PI3K p110-alpha WEB: http://www.ncbi.nlm.nih.gov/gene PIK3CA phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit alpha 5290 3q26.3 9606 3 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0001944 (EC: TAS, PMID: 19200708); GO_0004674 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10490823); GO_0005524 (EC: IEA); GO_0005829 (EC: TAS); GO_0005886 (EC: IBA); GO_0005942 (EC: ISS); GO_0005943 (EC: IDA); GO_0006006 (EC: IEA); GO_0006644 (EC: TAS); GO_0006661 (EC: TAS); GO_0007173 (EC: TAS); GO_0007596 (EC: TAS); GO_0008286 (EC: TAS); GO_0008543 (EC: TAS); GO_0016301 (EC: TAS); GO_0016303 (EC: IDA, PMID: 2174051); GO_0030027 (EC: IEA); GO_0030168 (EC: TAS); GO_0030295 (EC: IEA); GO_0031295 (EC: TAS); GO_0033138 (EC: IEA); GO_0035004 (EC: ISS); GO_0035004 (EC: TAS, PMID: 19200708); GO_0035005 (EC: IBA); GO_0036092 (EC: IDA, PMID: 2174051); GO_0038028 (EC: TAS, PMID: 19200708); GO_0038095 (EC: TAS); GO_0038096 (EC: TAS); GO_0040014 (EC: IEA); GO_0043491 (EC: IEA); GO_0043524 (EC: IEA); GO_0043542 (EC: TAS, PMID: 19200708); GO_0043560 (EC: IEA); GO_0044029 (EC: IEA); GO_0044281 (EC: TAS); GO_0045087 (EC: TAS); GO_0046854 (EC: ISS); GO_0046934 (EC: TAS); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0050852 (EC: TAS); GO_0050900 (EC: TAS); GO_0060048 (EC: TAS, PMID: 19147653); GO_2000270 (EC: IEA); GO_2000653 (EC: IEA); GO_2000811 (EC: IMP) PMID: 1322797; 2174051; 7713498; 7820549; 7929193; 8020561; 8246987; 8636073; 8665852; 8702949; 8798481; 9043658; 9113989; 9119889; 9150145; 9247029; 9341793; 9394803; 9415396; 9446795; 9708406; 9808187; 9915850; 9916799; 10208934; 10213474; 10357815; 10358930; 10490823; 10571082; 10608806; 10620012; 10648629; 10783161; 10803462; 10921882; 10949031; 10985305; 11029009; 11154208; 11156964; 11157475; 11278864; 11279232; 11289809; 11334418; 11353842; 11438544; 11577104; 11606067; 11676480; 11912194; 11959846; 11969417; 11994280; 12077252; 12167717; 12477932; 12526811; 12538664; 12551992; 12584329; 12637493; 12660731; 12704201; 12754211; 12890670; 12893243; 12933652; 12954600; 12960231; 14511371; 14583609; 14602571; 14724584; 14729945; 15016963; 15213298; 15254419; 15289301; 15377662; 15467468; 15489334; 15520168; 15605984; 15632060; 15647370; 15664519; 15689238; 15707590; 15712344; 15784156; 15805248; 15834429; 15837735; 15924253; 15928251; 15930273; 15940673; 15950905; 15994075; 16034135; 16043515; 16081599; 16114017; 16135792; 16150119; 16150444; 16168105; 16203798; 16287065; 16288007; 16317585; 16322209; 16339173; 16339315; 16341083; 16344560; 16353168; 16354680; 16376301; 16380997; 16397024; 16406609; 16432179; 16522324; 16524887; 16533766; 16569657; 16582596; 16618717; 16627990; 16682946; 16728507; 16764926; 16775835; 16778113; 16788758; 16790501; 16806069; 16815198; 16820791; 16822308; 16837650; 16839745; 16840732; 16885334; 16930767; 16949921; 16968743; 17006756; 17050665; 17052259; 17060456; 17062663; 17141917; 17157319; 17202311; 17219054; 17222361; 17235514; 17237249; 17307335; 17314276; 17317825; 17332342; 17341442; 17363507; 17369495; 17376864; 17377809; 17426084; 17449641; 17468516; 17471559; 17487277; 17507466; 17546593; 17549376; 17575221; 17586693; 17590872; 17632570; 17635910; 17657213; 17669465; 17673550; 17681398; 17803655; 17827385; 17855350; 17875942; 17877460; 17923698; 17924977; 17936563; 17942548; 17947469; 17971428; 17982280; 17986027; 17990317; 18000091; 18022911; 18029348; 18064631; 18070887; 18074223; 18079394; 18084252; 18097548; 18180098; 18181165; 18183466; 18193083; 18216097; 18221484; 18224685; 18262558; 18270270; 18285463; 18317450; 18335034; 18343945; 18355852; 18371219; 18382359; 18418043; 18449193; 18453587; 18503601; 18516290; 18621636; 18624398; 18641990; 18660489; 18669866; 18676830; 18679714; 18691552; 18757405; 18769113; 18782444; 18794094; 18794883; 18798071; 18829572; 18835245; 18852163; 18854243; 18951408; 18980969; 18990689; 18996102; 19003996; 19012001; 19027487; 19029838; 19029981; 19064572; 19069650; 19076977; 19143676; 19147653; 19148475; 19164214; 19172191; 19196980; 19200708; 19223544; 19233141; 19234438; 19237633; 19240718; 19261849; 19272638; 19276248; 19305151; 19330652; 19349352; 19351817; 19366826; 19380724; 19380743; 19383818; 19394761; 19411071; 19418217; 19420344; 19440000; 19440799; 19443396; 19487299; 19549383; 19573809; 19584164; 19603024; 19608668; 19622295; 19633047; 19638206; 19654299; 19671852; 19679877; 19685490; 19686742; 19701705; 19704056; 19706770; 19735264; 19789314; 19789368; 19805105; 19807924; 19815551; 19818761; 19822807; 19826477; 19839777; 19844234; 19844788; 19845664; 19853286; 19861897; 19874421; 19891769; 19898424; 19903786; 19903845; 19913121; 20008098; 20018188; 20019835; 20022634; 20028853; 20030946; 20034918; 20041213; 20056178; 20098682; 20101210; 20103642; 20107891; 20130133; 20167866; 20177704; 20186503; 20237496; 20301425; 20308328; 20308428; 20331378; 20368287; 20379197; 20398348; 20407443; 20413299; 20416077; 20416519; 20447721; 20453000; 20479250; 20491626; 20493625; 20495538; 20508983; 20514448; 20526288; 20535651; 20551053; 20557351; 20569675; 20571907; 20593314; 20602615; 20616362; 20619739; 20622004; 20628086; 20629536; 20629539; 20652941; 20691427; 20699365; 20702582; 20703095; 20713702; 20718712; 20736745; 20813562; 20813970; 20818790; 20824703; 20826237; 20827662; 20838624; 20857497; 20860430; 20881644; 20937558; 20940279; 20953381; 20954287; 20959404; 21029719; 21035469; 21042767; 21048031; 21051183; 21062993; 21071597; 21072204; 21092549; 21093899; 21103049; 21113138; 21113787; 21123564; 21127054; 21139048; 21168197; 21169263; 21179398; 21185392; 21191416; 21209852; 21209903; 21225506; 21228233; 21252315; 21255011; 21258250; 21266528; 21290341; 21300060; 21303542; 21310649; 21332555; 21345071; 21355052; 21357506; 21358673; 21367892; 21372221; 21377268; 21406404; 21407159; 21408138; 21412012; 21419810; 21424126; 21440011; 21442372; 21454528; 21468554; 21469098; 21474066; 21480388; 21482133; 21482677; 21490305; 21499215; 21501368; 21507233; 21531001; 21531708; 21538027; 21557211; 21558396; 21594665; 21595858; 21617917; 21620836; 21620963; 21622527; 21646525; 21660567; 21663621; 21667306; 21673026; 21676217; 21682666; 21706016; 21708979; 21711108; 21713404; 21725367; 21735444; 21765914; 21768115; 21769475; 21788516; 21789382; 21822287; 21824802; 21829508; 21830111; 21861134; 21872252; 21887250; 21893189; 21899695; 21906875; 21932420; 21937609; 21945955; 21949775; 21970855; 21990951; 21991326; 21994334; 21997360; 22006429; 22020193; 22026810; 22033276; 22037177; 22039088; 22045127; 22064833; 22072736; 22095222; 22105580; 22107784; 22120431; 22135231; 22146375; 22146979; 22157930; 22172323; 22185283; 22188534; 22188813; 22190283; 22208359; 22209294; 22212451; 22214007; 22227580; 22258409; 22271473; 22285706; 22285928; 22287190; 22301279; 22302350; 22315990; 22325221; 22330809; 22336203; 22336586; 22340730; 22351695; 22355357; 22357840; 22363436; 22363598; 22383975; 22417847; 22430133; 22430209; 22460814; 22463491; 22471665; 22488590; 22495819; 22498935; 22522453; 22522847; 22552288; 22556157; 22556379; 22575839; 22579930; 22586484; 22619175; 22623730; 22635024; 22640628; 22648906; 22649008; 22658544; 22662165; 22675430; 22675553; 22683270; 22689060; 22704443; 22705003; 22705004; 22723903; 22729222; 22729223; 22729224; 22736407; 22737248; 22744290; 22768164; 22768179; 22779686; 22782554; 22798500; 22807617; 22840496; 22842715; 22851869; 22863784; 22870241; 22875023; 22880054; 22897848; 22897902; 22905202; 22912864; 22923510; 22928013; 22931052; 22936809; 22938585; 22940133; 22949056; 22949682; 22955107; 22964641; 22982396; 22988297; 22994622; 22994717; 22997091; 22998445; 23013731; 23021375; 23028762; 23051731; 23066026; 23066039; 23071680; 23082158; 23085752; 23092874; 23094721; 23100325; 23107319; 23110163; 23115297; 23125007; 23136191; 23136247; 23172887; 23182717; 23184205; 23185308; 23192871; 23219661; 23224067; 23233531; 23237847; 23243017; 23246288; 23248156; 23261389; 23266353; 23275335; 23292187; 23300780; 23301057; 23318440; 23335533; 23341541; 23345407; 23352210; 23374602; 23383294; 23386617; 23392229; 23401445; 23409016; 23417417; 23418602; 23429328; 23435830; 23453624; 23475955; 23523798; 23532889; 23538402; 23546602; 23548132; 23549875; 23563091; 23564819; 23568272; 23580570; 23583669; 23588386; 23592373; 23604317; 23612454; 23615713; 23624506; 23625205; 23626817; 23633456; 23640046; 23643389; 23660947; 23680019; 23684925; 23695676; 23708425; 23709421; 23725225; 23728071; 23734265; 23739063; 23743572; 23785428; 23787421; 23813545; 23832540; 23851329; 23867512; 23867821; 23884447; 23886157; 23891627; 23936502; 23946963; 23981382; 24001613; 24011934; 24062397; 24077110; 24099783; 24231454; 24233241; 24299208; 24314632; 24323026; 24323028; 24360885; 24364210; 24374682 phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit alpha HGNC:8975 HPRD:01382 MIM:171834 Other designations: PI3-kinase p110 subunit alpha|PI3K-alpha|phosphatidylinositol 3-kinase, catalytic, 110-KD, alpha|phosphatidylinositol 3-kinase, catalytic, alpha polypeptide|phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform|phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha|phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit, alpha isoform|phosphoinositide-3-kinase, catalytic, alpha polypeptide|ptdIns-3-kinase subunit p110-alpha|serine/threonine protein kinase PIK3CA PIK3CA OGG:3000005308 Bin Zhao, Yue Liu, Oliver He ARP1 Brx1 IDG2 IGDS IGDS2 IHG2 IRID2 Otlx2 PTX2 RGS RIEG RIEG1 RS WEB: http://www.ncbi.nlm.nih.gov/gene PITX2 paired-like homeodomain 2 5308 4q25 9606 4 Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 16449236); GO_0000976 (EC: IDA, PMID: 12612071); GO_0000978 (EC: IEA); GO_0001077 (EC: IEA); GO_0001078 (EC: IDA, PMID: 16449236); GO_0001085 (EC: IPI, PMID: 15466416); GO_0001102 (EC: IPI, PMID: 12612071); GO_0001105 (EC: IDA, PMID: 9685346); GO_0001191 (EC: IDA, PMID: 16449236); GO_0001569 (EC: IEA); GO_0001570 (EC: IEA); GO_0001701 (EC: IEA); GO_0001764 (EC: IEA); GO_0002074 (EC: IEA); GO_0003171 (EC: IEA); GO_0003253 (EC: ISS); GO_0003350 (EC: IEA); GO_0003700 (EC: IDA, PMID: 15385555); GO_0005515 (EC: IPI, PMID: 16449236); GO_0005634 (EC: IDA); GO_0005667 (EC: IDA, PMID: 15385555); GO_0005737 (EC: IEA); GO_0006355 (EC: IDA, PMID: 15385555); GO_0007368 (EC: ISS); GO_0007520 (EC: IEA); GO_0008134 (EC: IPI, PMID: 15385555); GO_0008584 (EC: IEA); GO_0008585 (EC: IEA); GO_0009725 (EC: IEA); GO_0016055 (EC: IEA); GO_0021763 (EC: IEA); GO_0021855 (EC: IEA); GO_0030334 (EC: IEA); GO_0031076 (EC: IEA); GO_0031490 (EC: IEA); GO_0033189 (EC: IEA); GO_0035116 (EC: IEA); GO_0035315 (EC: IC, PMID: 19251162); GO_0035886 (EC: IEA); GO_0035993 (EC: IMP, PMID: 18312615); GO_0042475 (EC: IEA); GO_0042476 (EC: IMP, PMID: 14630904); GO_0042803 (EC: IPI, PMID: 12612071); GO_0043010 (EC: IMP, PMID: 9618168); GO_0043021 (EC: IC, PMID: 19174163); GO_0043388 (EC: IEA); GO_0045944 (EC: IDA, PMID: 15466416); GO_0048536 (EC: ISS); GO_0048557 (EC: IEA); GO_0051219 (EC: IPI, PMID: 19174163); GO_0055009 (EC: IEA); GO_0055015 (EC: IEA); GO_0060126 (EC: TAS, PMID: 10372733); GO_0060127 (EC: TAS, PMID: 10372733); GO_0060412 (EC: IEA); GO_0060460 (EC: IEA); GO_0060577 (EC: IEA); GO_0060578 (EC: IEA); GO_0061031 (EC: IEA); GO_0061072 (EC: IMP, PMID: 9437321); GO_0061325 (EC: ISS); GO_0070986 (EC: ISS); GO_2000288 (EC: IEA) PMID: 1303248; 7581385; 8942889; 8944018; 9437321; 9539779; 9618168; 9685346; 9708732; 10051017; 10372733; 11157981; 11487566; 11763998; 11774072; 11821690; 11948188; 12130547; 12223489; 12381896; 12464179; 12477932; 12612071; 12732450; 14630904; 14975719; 14985297; 15255117; 15342556; 15385555; 15466416; 15489334; 15591271; 15728254; 15895993; 16274491; 16449236; 16498627; 16638984; 16834779; 16876867; 16884686; 16936096; 17065505; 17167399; 17197537; 17486624; 17558846; 17603472; 17850355; 17965955; 18312615; 18331556; 18339718; 18616618; 18711169; 18775326; 18946986; 19052653; 19174163; 19218601; 19233404; 19251162; 19513095; 19597492; 19801652; 19913121; 19954729; 20022124; 20170812; 20173747; 20211142; 20301552; 20332099; 20372070; 20478579; 20628086; 20634891; 20875405; 20881290; 20881294; 20978111; 21221769; 21278591; 21282332; 21414601; 21427120; 21479692; 21498098; 21511879; 21531708; 21574119; 21617755; 21803613; 21810944; 21837767; 22224469; 22495974; 22544366; 22555092; 22569110; 22615897; 22735262; 23041239; 23042660; 23088713; 23132660; 23229549; 23354914; 23505501; 23913021; 24083357; 24162257; 24250222 paired-like homeodomain 2 Ensembl:ENSG00000164093 HGNC:9005 HPRD:03328 MIM:601542 Vega:OTTHUMG00000132837 Other designations: ALL1-responsive protein ARP1|all1-responsive gene 1|homeobox protein PITX2|paired-like homeodomain transcription factor 2|pituitary homeobox 2|rieg bicoid-related homeobox transcription factor 1|solurshin PITX2 OGG:3000005315 Bin Zhao, Yue Liu, Oliver He CTHBP HEL-S-30 OIP3 PK3 PKM2 TCB THBP1 WEB: http://www.ncbi.nlm.nih.gov/gene PKM pyruvate kinase, muscle 5315 15q22 20140408 9606 15 protein-coding Official from a nomenclature committee GO_0000287 (EC: IEA); GO_0004743 (EC: TAS, PMID: 2040271); GO_0005515 (EC: IPI, PMID: 12620389); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA, PMID: 17308100); GO_0005737 (EC: IDA); GO_0005739 (EC: IDA); GO_0005829 (EC: NAS, PMID: 2813362); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA); GO_0005929 (EC: IEA); GO_0005975 (EC: TAS); GO_0006006 (EC: TAS); GO_0006096 (EC: IEA); GO_0006096 (EC: TAS); GO_0012501 (EC: IDA, PMID: 17308100); GO_0023026 (EC: IDA); GO_0030955 (EC: IEA); GO_0044281 (EC: TAS); GO_0044822 (EC: IDA); GO_0070062 (EC: IDA, PMID: 11487543) PMID: 2040271; 2169315; 2174328; 2813362; 2838416; 2854097; 2931560; 3102533; 6930359; 8125298; 8895530; 9329624; 9466265; 9657767; 11162730; 11256614; 11487543; 11895152; 11960989; 12477932; 12565818; 12620389; 12650930; 12665801; 12820312; 12820320; 12820337; 14702039; 15128873; 15161933; 15231747; 15294093; 15489334; 15592455; 15862967; 15952740; 15967462; 15996096; 16009940; 16055720; 16132722; 16169070; 16196087; 16226712; 16263121; 16289162; 16335966; 16344560; 16964243; 17011640; 17081983; 17220478; 17308100; 17406361; 17414054; 17558393; 17620599; 17623298; 18029348; 18191611; 18298799; 18303054; 18337815; 18394773; 18464261; 18468620; 18519040; 18789002; 18996102; 19097497; 19135240; 19265196; 19401544; 19596686; 19734428; 19738201; 19754967; 19759913; 19820423; 19920249; 19920251; 20000738; 20010808; 20082317; 20133837; 20195357; 20304929; 20332442; 20360068; 20391533; 20458337; 20592362; 20602615; 20639865; 20667897; 20721957; 20847263; 20857498; 20962042; 20972266; 20977946; 21044950; 21081666; 21139048; 21145461; 21252943; 21319273; 21325052; 21565611; 21620138; 21725354; 21800051; 21832049; 21853274; 21890473; 21900206; 21906983; 21963094; 21987572; 21988832; 22044881; 22052977; 22053931; 22056988; 22079093; 22118674; 22140559; 22190034; 22231432; 22236875; 22268729; 22271574; 22304920; 22306293; 22334075; 22465421; 22505724; 22509023; 22536838; 22623428; 22627140; 22736014; 22807066; 22824010; 22863883; 22864959; 22889453; 22901803; 22939629; 22944692; 23000965; 23064226; 23071357; 23086999; 23123196; 23130662; 23155487; 23178880; 23212076; 23267074; 23383273; 23398456; 23402259; 23423437; 23428871; 23451252; 23455922; 23463506; 23530218; 23537643; 23576436; 23602568; 23640882; 23703321; 23794342; 23814019; 23846818; 23880164; 24100037; 24120138; 24120661; 24142698; 24316223; 24344305; 24457600 pyruvate kinase, muscle Ensembl:ENSG00000067225 HGNC:9021 HPRD:01529 MIM:179050 Vega:OTTHUMG00000172709 Other designations: OIP-3|OPA-interacting protein 3|PK, muscle type|cytosolic thyroid hormone-binding protein|epididymis secretory protein Li 30|p58|pyruvate kinase 2/3|pyruvate kinase PKM|pyruvate kinase isozymes M1/M2|pyruvate kinase muscle isozyme|thyroid hormone-binding protein 1|thyroid hormone-binding protein, cytosolic|tumor M2-PK PKM OGG:3000005319 Bin Zhao, Yue Liu, Oliver He PLA2 PLA2A PPLA2 WEB: http://www.ncbi.nlm.nih.gov/gene PLA2G1B phospholipase A2, group IB (pancreas) 5319 12q24.31 9606 12 Official from a nomenclature committee GO_0000187 (EC: ISS, PMID: 15528384); GO_0002446 (EC: ISS, PMID: 16005851); GO_0004623 (EC: IDA, PMID: 1918029); GO_0005102 (EC: IDA, PMID: 1918029); GO_0005102 (EC: IPI, PMID: 7721806); GO_0005509 (EC: IDA, PMID: 7060561); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 7060561); GO_0006633 (EC: IDA, PMID: 1918029); GO_0006644 (EC: TAS); GO_0006654 (EC: TAS); GO_0007015 (EC: TAS, PMID: 9886417); GO_0007165 (EC: TAS, PMID: 9886417); GO_0009986 (EC: IDA, PMID: 1918029); GO_0010524 (EC: ISS, PMID: 15528384); GO_0015758 (EC: ISS, PMID: 1918029); GO_0019370 (EC: ISS, PMID: 16005851); GO_0030141 (EC: IEA); GO_0030593 (EC: ISS, PMID: 16005851); GO_0032052 (EC: ISS, PMID: 7060561); GO_0032431 (EC: TAS, PMID: 17981679); GO_0032637 (EC: ISS, PMID: 15528384); GO_0032869 (EC: ISS, PMID: 1918029); GO_0035556 (EC: ISS, PMID: 15528384); GO_0036148 (EC: TAS); GO_0036149 (EC: TAS); GO_0036150 (EC: TAS); GO_0036151 (EC: TAS); GO_0036152 (EC: TAS); GO_0044240 (EC: IDA, PMID: 7060561); GO_0044281 (EC: TAS); GO_0045740 (EC: IDA, PMID: 1918029); GO_0045944 (EC: ISS, PMID: 15528384); GO_0046470 (EC: IDA, PMID: 7060561); GO_0046474 (EC: TAS); GO_0047498 (EC: IDA, PMID: 7060561); GO_0048146 (EC: IC, PMID: 1918029); GO_0050482 (EC: TAS, PMID: 12423354); GO_0050714 (EC: TAS, PMID: 17981679); GO_0050778 (EC: ISS, PMID: 16005851); GO_0051092 (EC: ISS, PMID: 15528384) PMID: 1918029; 2052621; 3028739; 6349696; 6477929; 7060561; 7584826; 7590434; 7721806; 8175726; 8300559; 8358438; 9188469; 9377118; 9745929; 9847074; 9848887; 9886417; 10509674; 10551547; 10735945; 10873103; 10905638; 10964913; 11025364; 11353443; 11510783; 11807183; 11851982; 12423354; 12477932; 12759552; 14557262; 14998370; 15220446; 15489334; 15528384; 15736947; 16005851; 16391564; 16392040; 16495221; 16541075; 16567514; 17065600; 17223797; 17434532; 17470210; 17488462; 17981679; 18212756; 18492292; 18636547; 19297324; 19913121; 20536387; 20628086; 21988832; 22528125; 22680611 phospholipase A2, group IB (pancreas) Ensembl:ENSG00000170890 HGNC:9030 HPRD:01396 MIM:172410 Vega:OTTHUMG00000169343 Other designations: phosphatidylcholine 2-acylhydrolase 1B|phospholipase A2 PLA2G1B OGG:3000005322 Bin Zhao, Yue Liu, Oliver He FRFB GV-PLA2 PLA2-10 hVPLA(2) WEB: http://www.ncbi.nlm.nih.gov/gene PLA2G5 phospholipase A2, group V 5322 1p36-p34 9606 1 Official from a nomenclature committee GO_0005509 (EC: IEA); GO_0005576 (EC: TAS); GO_0005794 (EC: IEA); GO_0005886 (EC: IEA); GO_0006644 (EC: TAS); GO_0006654 (EC: TAS); GO_0006663 (EC: IEA); GO_0008201 (EC: IEA); GO_0009986 (EC: IEA); GO_0016042 (EC: IEA); GO_0019370 (EC: IEA); GO_0034097 (EC: IEA); GO_0036148 (EC: TAS); GO_0036149 (EC: TAS); GO_0036150 (EC: TAS); GO_0036151 (EC: TAS); GO_0036152 (EC: TAS); GO_0044281 (EC: TAS); GO_0046474 (EC: TAS); GO_0047498 (EC: IEA); GO_0048471 (EC: IEA); GO_0050482 (EC: IEA); GO_0051591 (EC: IEA) PMID: 8300559; 8838795; 8889548; 9377118; 9745929; 9767110; 10531350; 10751642; 10839997; 10873151; 11080676; 11522612; 11741884; 12124392; 12423354; 12477932; 12796497; 12963740; 14702039; 15259375; 15377291; 15489334; 16040605; 16115226; 16146426; 16476735; 16601231; 16710414; 16785555; 16794232; 17545304; 19913121; 20083228; 20448053; 20628086; 22041135; 22137173; 23650617 phospholipase A2, group V HGNC:9038 HPRD:03117 MIM:601192 Other designations: Ca2+-dependent phospholipase A2|calcium-dependent phospholipase A2|phosphatidylcholine 2-acylhydrolase 5 PLA2G5 OGG:3000005340 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene PLG plasminogen 5340 RP1-81D8.1 6q26 20140408 9606 6 protein-coding Official from a nomenclature committee GO_0002576 (EC: TAS); GO_0004252 (EC: IDA, PMID: 14699093); GO_0005515 (EC: IPI, PMID: 10077593); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 6216475); GO_0005886 (EC: TAS); GO_0007596 (EC: IMP, PMID: 1986355); GO_0007596 (EC: TAS); GO_0008285 (EC: TAS, PMID: 8910613); GO_0009986 (EC: IDA, PMID: 14699093); GO_0010812 (EC: IDA, PMID: 14699093); GO_0019904 (EC: IPI, PMID: 9786936); GO_0022617 (EC: IDA, PMID: 14699093); GO_0022617 (EC: TAS); GO_0030168 (EC: TAS); GO_0030198 (EC: TAS); GO_0031093 (EC: TAS); GO_0031232 (EC: IDA, PMID: 14699093); GO_0034185 (EC: IPI, PMID: 16480936); GO_0042246 (EC: IEA); GO_0042730 (EC: TAS); GO_0044267 (EC: TAS); GO_0045445 (EC: IEA); GO_0046716 (EC: IEA); GO_0048771 (EC: IEA); GO_0051603 (EC: IEA); GO_0051918 (EC: IDA, PMID: 14726399); GO_0051919 (EC: IDA, PMID: 6438154); GO_0060707 (EC: IEA); GO_0060716 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19199708); GO_0071674 (EC: IEA); GO_0072562 (EC: IDA); GO_2000048 (EC: TAS, PMID: 17203182) PMID: 122932; 126863; 134998; 142009; 146197; 158022; 479158; 659588; 1427790; 1657148; 1657149; 1909331; 1939207; 1986355; 2065054; 2157850; 2318848; 2437112; 2522013; 2745554; 2829380; 2962191; 2962641; 3030813; 3334852; 3356193; 3920216; 4226004; 4240117; 4694729; 5475635; 6094526; 6148961; 6216475; 6238949; 6438154; 6582496; 6838832; 6919539; 6980881; 7525077; 7538844; 7548163; 7586586; 7814888; 7982919; 8054447; 8162705; 8181475; 8181476; 8360181; 8392398; 8460120; 8478593; 8555184; 8611560; 8612605; 8652577; 8843739; 8910613; 9020112; 9054441; 9102221; 9102401; 9201958; 9234243; 9242524; 9305949; 9337997; 9360944; 9375744; 9428707; 9490681; 9521645; 9548733; 9596664; 9688635; 9737862; 9783753; 9786936; 9834305; 9858247; 10069369; 10077593; 10215610; 10218588; 10233898; 10512713; 10604721; 10625689; 10656799; 10700393; 10889192; 10928473; 10956663; 10964919; 10974350; 10978167; 11027681; 11100730; 11113116; 11169399; 11257124; 11263499; 11342539; 11350170; 11371191; 11438139; 11729324; 11888684; 11928826; 11939791; 12016220; 12036889; 12054798; 12080056; 12093796; 12189145; 12192005; 12228252; 12406896; 12456874; 12477932; 12604689; 12646571; 12692411; 12697748; 12700073; 12736244; 12871329; 12876630; 14574404; 14678821; 14699093; 14719094; 14726399; 14739127; 14739293; 14764098; 14769799; 15090462; 15099286; 15207811; 15211511; 15215240; 15220341; 15299951; 15321992; 15333838; 15489334; 15501816; 15529749; 15609351; 15613921; 15642732; 15677446; 15746964; 15911629; 16043488; 16087677; 16097950; 16229836; 16319056; 16478887; 16480936; 16601838; 16790522; 16828203; 17115186; 17200769; 17203182; 17206383; 17272502; 17379720; 17545513; 17606760; 17616171; 17653767; 17656680; 17890952; 17927806; 17976375; 17978577; 18039838; 18070889; 18160581; 18163891; 18223261; 18279394; 18289715; 18310038; 18329389; 18331597; 18366077; 18392331; 18566672; 18568768; 18624398; 18658146; 18667578; 18685433; 18714035; 18981180; 18983515; 19074676; 19158842; 19199708; 19308255; 19363026; 19465692; 19574304; 19712047; 19800007; 19801674; 19821587; 19850343; 19913121; 20056908; 20095998; 20112045; 20140262; 20143645; 20152941; 20346360; 20346413; 20553606; 20565259; 20617841; 20628086; 20655859; 20702651; 20709033; 20726765; 21072208; 21174000; 21236472; 21300353; 21316746; 21464960; 21467042; 21510941; 21543325; 21680799; 21755014; 21787393; 21802507; 21832858; 21900290; 21988832; 21998162; 22027013; 22079981; 22124123; 22147698; 22187433; 22197896; 22287006; 22507544; 22518846; 22619171; 22641690; 22677171; 22685231; 22732096; 22773346; 22832192; 22987920; 22996753; 23071278; 23071827; 23103380; 23118497; 23140098; 23150713; 23341464; 23449787; 23481605; 23576799; 23583624; 23645683; 23699598; 23702659; 23721211; 23853591; 24029428; 24457600; 24605649 plasminogen PLG OGG:3000005350 Bin Zhao, Yue Liu, Oliver He CMD1P CMH18 PLB WEB: http://www.ncbi.nlm.nih.gov/gene PLN phospholamban 5350 RP3-509L4.2 6q22.1 9606 6 Official from a nomenclature committee GO_0002026 (EC: IC, PMID: 19708671); GO_0004857 (EC: ISS, PMID: 12032137); GO_0005246 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15598648); GO_0005739 (EC: IDA); GO_0005783 (EC: ISS); GO_0006816 (EC: IEA); GO_0008015 (EC: NAS, PMID: 8406504); GO_0008016 (EC: IMP, PMID: 16432188); GO_0010043 (EC: IEA); GO_0010459 (EC: IMP, PMID: 16432188); GO_0010881 (EC: IEA); GO_0016020 (EC: IDA, PMID: 19708671); GO_0031966 (EC: IEA); GO_0031982 (EC: IEA); GO_0032780 (EC: IDA, PMID: 19708671); GO_0032780 (EC: ISS); GO_0033017 (EC: IEA); GO_0033574 (EC: IEA); GO_0042030 (EC: IDA, PMID: 19708671); GO_0042030 (EC: ISS); GO_0042802 (EC: ISS); GO_0043086 (EC: ISS, PMID: 12032137); GO_0048471 (EC: ISS); GO_0048738 (EC: IEA); GO_0051117 (EC: ISS, PMID: 12032137); GO_0051260 (EC: IEA); GO_0051480 (EC: IC, PMID: 19708671); GO_0051924 (EC: IDA); GO_0051924 (EC: ISS); GO_0051926 (EC: IDA, PMID: 19708671); GO_0055119 (EC: TAS); GO_0060314 (EC: IEA); GO_0086004 (EC: IC, PMID: 19708671); GO_0086023 (EC: IEA); GO_0086036 (EC: IC, PMID: 19708671); GO_0086092 (EC: IEA); GO_0090281 (EC: ISS, PMID: 12032137); GO_0090534 (EC: IDA, PMID: 19708671); GO_1901020 (EC: IDA, PMID: 19708671); GO_1901020 (EC: ISS); GO_1901877 (EC: IDA, PMID: 19708671); GO_1901877 (EC: ISS); GO_1901894 (EC: IDA); GO_1901895 (EC: IDA, PMID: 19708671); GO_1901897 (EC: IC, PMID: 19708671); GO_1902081 (EC: ISS) PMID: 1828805; 3759968; 7586307; 7749920; 7779806; 8406504; 8862513; 9345259; 9468536; 9512019; 9845327; 10096878; 10198197; 10551848; 10809745; 11526231; 11854448; 12032137; 12080135; 12477932; 12480535; 12525698; 12610310; 12639993; 12692302; 12705874; 12804600; 14530977; 15342556; 15489334; 15598648; 15640069; 15736939; 16043693; 16235537; 16382369; 16432188; 16476846; 16829191; 17009399; 17010801; 17515962; 17655857; 17766390; 17905829; 18192322; 18241046; 18708665; 19139388; 19305408; 19305409; 19324307; 19584346; 19587794; 19638213; 19671701; 19708671; 19875404; 20301486; 20301725; 20474083; 20634894; 20639392; 21076409; 21108950; 21167350; 21282613; 21332051; 21576492; 21687864; 21988832; 22137083; 22155237; 22172806; 22247554; 22427649; 22820313; 23166209; 23308118; 23349452; 23871674 phospholamban Ensembl:ENSG00000198523 HGNC:9080 HPRD:01395 MIM:172405 Vega:OTTHUMG00000015462 Other designations: cardiac phospholamban PLN OGG:3000005366 Bin Zhao, Yue Liu, Oliver He APR NOXA WEB: http://www.ncbi.nlm.nih.gov/gene PMAIP1 phorbol-12-myristate-13-acetate-induced protein 1 5366 18q21.32 20140408 9606 18 protein-coding Official from a nomenclature committee GO_0001836 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15705586); GO_0005634 (EC: IDA, PMID: 12879012); GO_0005739 (EC: IDA, PMID: 14500711); GO_0005741 (EC: TAS); GO_0005829 (EC: IDA, PMID: 15705586); GO_0005829 (EC: TAS); GO_0006915 (EC: IMP, PMID: 17599062); GO_0006915 (EC: TAS); GO_0006919 (EC: IEA); GO_0009411 (EC: IEA); GO_0010165 (EC: IEA); GO_0010498 (EC: IDA, PMID: 15901672); GO_0010907 (EC: IDA); GO_0010917 (EC: ISS, PMID: 14699081); GO_0032461 (EC: IDA, PMID: 17024184); GO_0042149 (EC: IMP); GO_0042771 (EC: IEA); GO_0043029 (EC: ISS); GO_0043065 (EC: IDA); GO_0043065 (EC: IMP, PMID: 17289999); GO_0043280 (EC: IDA, PMID: 14699081); GO_0043331 (EC: IDA, PMID: 15705586); GO_0043517 (EC: IMP, PMID: 15102863); GO_0043525 (EC: IEA); GO_0046902 (EC: IDA, PMID: 14500711); GO_0048147 (EC: IEA); GO_0051607 (EC: IDA, PMID: 15705586); GO_0071456 (EC: IEP, PMID: 14699081); GO_0072332 (EC: IMP, PMID: 15102863); GO_0072593 (EC: IDA, PMID: 14699081); GO_0090200 (EC: IDA, PMID: 14500711); GO_0090200 (EC: IMP, PMID: 15705586); GO_0097193 (EC: IDA, PMID: 14500711); GO_0097193 (EC: TAS); GO_1900740 (EC: TAS); GO_1902043 (EC: IDA, PMID: 15705586); GO_2001244 (EC: IDA); GO_2001244 (EC: TAS) PMID: 2398525; 10807576; 11181995; 12477932; 12879012; 14500711; 14699081; 15102863; 15299072; 15489334; 15572378; 15694340; 15705586; 15856024; 15901672; 16169070; 16697956; 16782027; 16888645; 16928686; 17024184; 17038534; 17216584; 17227835; 17289999; 17599062; 18192275; 18231856; 18354037; 18398749; 18408751; 18630524; 18708163; 18784742; 19050264; 19148187; 19164757; 19269851; 19298224; 19322201; 19372561; 19452318; 19515722; 19540835; 19815839; 20051518; 20085765; 20156337; 20223826; 20393480; 20639865; 20694148; 20802529; 20935673; 21048031; 21113147; 21139048; 21139584; 21145489; 21153863; 21353614; 21454712; 21516346; 21518486; 21613222; 21628457; 21698224; 21890473; 21900206; 21906983; 21907705; 21911456; 22053931; 22216287; 22219388; 22245094; 22361683; 22430213; 22446329; 22548841; 22590594; 22615771; 22718761; 23000965; 23014529; 23300762; 23302226; 23341456; 23429261; 23499448; 23669352; 23684722; 23770605; 23798675 phorbol-12-myristate-13-acetate-induced protein 1 Ensembl:ENSG00000141682 HGNC:9108 HPRD:12002 MIM:604959 Vega:OTTHUMG00000132765 Other designations: PMA-induced protein 1|adult T cell leukemia-derived PMA-responsive|immediate-early-response protein APR|protein Noxa PMAIP1 OGG:3000005372 Bin Zhao, Yue Liu, Oliver He Sec53 WEB: http://www.ncbi.nlm.nih.gov/gene PMM1 phosphomannomutase 1 5372 22q13.2 9606 22 Official from a nomenclature committee GO_0004615 (EC: IDA, PMID: 16540464); GO_0005829 (EC: TAS); GO_0006013 (EC: IDA, PMID: 16540464); GO_0006488 (EC: TAS); GO_0009298 (EC: IEA); GO_0009298 (EC: TAS); GO_0018279 (EC: TAS); GO_0019307 (EC: IEA); GO_0043025 (EC: IEA); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS); GO_0046872 (EC: IEA) PMID: 9070917; 9119384; 9271215; 9376685; 9603909; 10085245; 10591208; 12477932; 12789572; 14702039; 15461802; 15489334; 16189514; 16540464; 17054774; 17186415; 18591914; 18854154; 18927083; 21078624; 21139048; 21890473; 21906983; 21988832; 23000965 phosphomannomutase 1 Ensembl:ENSG00000100417 HGNC:9114 HPRD:03473 MIM:601786 Vega:OTTHUMG00000150972 Other designations: PMM 1|PMMH-22|brain glucose-1,6-bisphosphatase PMM1 OGG:3000005447 Bin Zhao, Yue Liu, Oliver He CPR CYPOR P450R WEB: http://www.ncbi.nlm.nih.gov/gene POR P450 (cytochrome) oxidoreductase 5447 7q11.2 9606 7 Official from a nomenclature committee GO_0003420 (EC: IEA); GO_0003958 (EC: IDA, PMID: 19448135); GO_0003958 (EC: TAS, PMID: 10048323); GO_0004128 (EC: IEA); GO_0005506 (EC: IEA); GO_0005515 (EC: IPI); GO_0005739 (EC: IEA); GO_0005789 (EC: IEA); GO_0007584 (EC: IEA); GO_0008941 (EC: IEA); GO_0009055 (EC: IEA); GO_0009437 (EC: IEA); GO_0009812 (EC: IEA); GO_0010181 (EC: IEA); GO_0016787 (EC: IEA); GO_0018393 (EC: IEA); GO_0019395 (EC: IEA); GO_0019899 (EC: IEA); GO_0032332 (EC: IEA); GO_0032770 (EC: IDA, PMID: 19448135); GO_0042493 (EC: IEA); GO_0043066 (EC: IEA); GO_0043154 (EC: IEA); GO_0043231 (EC: IDA, PMID: 9618440); GO_0043602 (EC: IEA); GO_0045542 (EC: IEA); GO_0045880 (EC: IEA); GO_0046210 (EC: IEA); GO_0047726 (EC: IEA); GO_0050660 (EC: IEA); GO_0050661 (EC: IEA); GO_0055114 (EC: IDA, PMID: 19448135); GO_0055114 (EC: TAS, PMID: 10048323); GO_0060192 (EC: IEA); GO_0070988 (EC: IEA); GO_0071372 (EC: IEA); GO_0071375 (EC: IEA); GO_0090031 (EC: IEA); GO_0090346 (EC: IDA, PMID: 19448135) PMID: 1550342; 2513880; 2516426; 7703255; 8460938; 8615895; 8812989; 9335117; 9398194; 9618440; 9642268; 9787138; 9847074; 9888582; 10048323; 10448278; 10990198; 11035953; 11118675; 11123926; 11181502; 11329262; 11329263; 11350900; 11716457; 11926825; 11971899; 12477932; 12626517; 12688675; 12725870; 12782579; 12787027; 12901793; 14758361; 14999778; 15220035; 15264278; 15342556; 15483095; 15489334; 15666840; 15680923; 15793702; 16169070; 16344560; 16434211; 16445284; 16467261; 16520232; 16574318; 16998238; 17018578; 17440066; 17505056; 17580970; 17595315; 17635179; 17827787; 17881660; 18216718; 18230729; 18259105; 18397975; 18551037; 18559916; 18630181; 18681889; 18781797; 19161969; 19258400; 19374516; 19448135; 19598235; 19744540; 19805543; 19837910; 19858215; 19884324; 19913121; 20096935; 20301592; 20628086; 20697309; 20722625; 20732302; 20844025; 20849814; 20879989; 20940534; 21070833; 21081644; 21084761; 21139048; 21164260; 21252943; 21265736; 21393444; 21655236; 21726529; 21741353; 21762695; 21770725; 21843508; 21890473; 21900206; 21900384; 21963094; 21973081; 21988832; 22162478; 22177374; 22462747; 22545110; 22547083; 22797925; 23000965; 23353702; 23911089; 24196959 P450 (cytochrome) oxidoreductase Ensembl:ENSG00000127948 HGNC:9208 HPRD:00485 MIM:124015 Vega:OTTHUMG00000130413 Other designations: NADPH--cytochrome P450 reductase|NADPH-dependent cytochrome P450 reductase POR OGG:3000005463 Bin Zhao, Yue Liu, Oliver He BRN5 MPOU TCFB1 WEB: http://www.ncbi.nlm.nih.gov/gene POU6F1 POU class 6 homeobox 1 5463 12q13.13 9606 12 Official from a nomenclature committee GO_0003700 (EC: IEA); GO_0005634 (EC: IEA); GO_0006351 (EC: IEA); GO_0007420 (EC: TAS, PMID: 7908264); GO_0007507 (EC: TAS, PMID: 7908264); GO_0007517 (EC: TAS, PMID: 7908264); GO_0043565 (EC: IEA) PMID: 1408763; 7908264; 8102789; 8567814; 8889548; 12477932; 14702039; 15489334; 16344560; 18029348; 18323601; 18976975; 19450691; 19874398; 20134265 POU class 6 homeobox 1 HGNC:9224 HPRD:17883 Other designations: POU domain, class 6, transcription factor 1|brain-5|brain-specific homeobox/POU domain protein 5|brn-5|mPOU homeobox protein POU6F1 OGG:3000005465 Bin Zhao, Yue Liu, Oliver He NR1C1 PPAR PPARalpha hPPAR WEB: http://www.ncbi.nlm.nih.gov/gene PPARA peroxisome proliferator-activated receptor alpha 5465 SC22CB-5E3.5 22q13.31 9606 22 Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 12700342); GO_0001103 (EC: IPI, PMID: 19955185); GO_0001666 (EC: IEA); GO_0003677 (EC: TAS, PMID: 10860941); GO_0003700 (EC: IDA, PMID: 19955185); GO_0003700 (EC: ISS); GO_0003707 (EC: IDA, PMID: 19955185); GO_0004879 (EC: IDA, PMID: 12955147); GO_0005515 (EC: IPI, PMID: 11915042); GO_0005634 (EC: TAS, PMID: 16271724); GO_0005654 (EC: TAS); GO_0006367 (EC: TAS); GO_0006629 (EC: TAS, PMID: 7684926); GO_0006631 (EC: IEA); GO_0007507 (EC: IEA); GO_0008144 (EC: IDA, PMID: 12955147); GO_0008270 (EC: IEA); GO_0008289 (EC: IDA, PMID: 12955147); GO_0008544 (EC: IEA); GO_0010467 (EC: TAS); GO_0010745 (EC: IC, PMID: 12700342); GO_0010745 (EC: IDA, PMID: 19114110); GO_0010871 (EC: IDA, PMID: 12700342); GO_0010887 (EC: IDA, PMID: 19114110); GO_0010891 (EC: IDA, PMID: 12700342); GO_0015908 (EC: TAS, PMID: 16271724); GO_0019902 (EC: IEA); GO_0019904 (EC: IEA); GO_0030522 (EC: IDA, PMID: 12955147); GO_0031624 (EC: IPI, PMID: 19955185); GO_0032000 (EC: TAS, PMID: 16271724); GO_0032091 (EC: IEA); GO_0032099 (EC: ISS); GO_0032403 (EC: IEA); GO_0032868 (EC: IEA); GO_0035095 (EC: IEA); GO_0042060 (EC: IEA); GO_0042157 (EC: IEA); GO_0043565 (EC: ISS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0045776 (EC: IEA); GO_0045820 (EC: IC, PMID: 19955185); GO_0045893 (EC: IDA, PMID: 12955147); GO_0045944 (EC: IDA, PMID: 19955185); GO_0046321 (EC: ISS); GO_0051525 (EC: IEA); GO_0070166 (EC: IEA); GO_0072363 (EC: IDA, PMID: 19955185); GO_0072366 (EC: IDA, PMID: 19955185); GO_0072369 (EC: IDA, PMID: 19955185); GO_0097371 (EC: IEA); GO_1901215 (EC: IEA); GO_2000678 (EC: IEA) PMID: 7684926; 7981125; 8621574; 8910358; 8993548; 9113987; 9238002; 9407140; 9610365; 9626662; 9627117; 9653119; 9748221; 9792666; 9795230; 9915808; 10022764; 10187842; 10195690; 10336495; 10377439; 10403814; 10542237; 10591208; 10669761; 10681503; 10731636; 10786636; 10860941; 10862523; 10872826; 10903152; 11119019; 11226238; 11337467; 11375929; 11409711; 11466580; 11587644; 11668221; 11698662; 11733490; 11818483; 11840500; 11845213; 11852057; 11864924; 11891224; 11897617; 11897821; 11914252; 11915042; 11923467; 11934839; 11940516; 11980898; 11981036; 12006394; 12023905; 12039952; 12042669; 12048138; 12055195; 12118000; 12118038; 12161442; 12163133; 12189208; 12203367; 12208475; 12395215; 12408750; 12468272; 12477932; 12482853; 12544508; 12554753; 12562861; 12594295; 12594814; 12615366; 12655356; 12700342; 12709436; 12745064; 12810707; 12835617; 12847522; 12855749; 12897377; 12914524; 12932225; 12938026; 12955147; 12962497; 14515181; 14519597; 14523052; 14633846; 14641801; 14671555; 14677049; 14702039; 14730379; 14764586; 14999402; 15001458; 15001550; 15051727; 15067378; 15083308; 15111510; 15128052; 15131257; 15196699; 15199365; 15221005; 15231516; 15258199; 15309680; 15318936; 15456881; 15461802; 15497675; 15500444; 15521013; 15539630; 15549499; 15608561; 15615782; 15642120; 15677519; 15685545; 15699244; 15699916; 15735069; 15759454; 15797250; 15811118; 15870285; 15888456; 15935279; 15940190; 16042408; 16043164; 16162941; 16169070; 16189514; 16221474; 16226051; 16239970; 16271724; 16275545; 16285997; 16288935; 16288986; 16297361; 16309557; 16377806; 16416313; 16492688; 16506057; 16511589; 16554032; 16630553; 16637234; 16652134; 16763159; 16806233; 16822823; 16847426; 16875506; 16956579; 17001213; 17008383; 17084382; 17129741; 17150915; 17181634; 17184146; 17195188; 17200111; 17244467; 17272748; 17300045; 17317762; 17331954; 17342071; 17355223; 17356846; 17363697; 17363837; 17431031; 17436029; 17492134; 17608096; 17616429; 17646210; 17655842; 17700210; 17705849; 17850927; 17926914; 17951966; 17962186; 17963696; 17991667; 17998026; 18003597; 18004978; 18061194; 18172578; 18182682; 18184928; 18219093; 18245819; 18255343; 18268046; 18292238; 18313368; 18336366; 18388689; 18394939; 18398047; 18440986; 18518955; 18541586; 18549840; 18586686; 18652775; 18660489; 18680716; 18710415; 18713766; 18725353; 18726867; 18727927; 18786524; 18787507; 18797151; 18848838; 18853997; 18855529; 18955051; 18977277; 18981151; 18996102; 19070893; 19114110; 19115207; 19118026; 19119483; 19141539; 19157507; 19208777; 19217440; 19223982; 19254215; 19255064; 19263263; 19279199; 19357976; 19362162; 19367093; 19386311; 19420105; 19422369; 19422653; 19433068; 19451226; 19453261; 19458633; 19527689; 19560472; 19628794; 19653005; 19660836; 19681917; 19706994; 19710929; 19733654; 19748481; 19776627; 19780876; 19782026; 19789836; 19822141; 19823578; 19828088; 19878569; 19887568; 19913121; 19937854; 19948841; 19948975; 19955185; 20016041; 20044476; 20045185; 20070029; 20178979; 20214982; 20238044; 20346360; 20379614; 20384434; 20385772; 20399568; 20400503; 20414453; 20421589; 20426853; 20450745; 20452482; 20466884; 20485444; 20496064; 20602615; 20620111; 20628086; 20638986; 20647061; 20653996; 20656057; 20673868; 20679960; 20682687; 20800603; 20810571; 20811626; 20825652; 20838448; 20855565; 20862655; 21030426; 21125992; 21159535; 21245137; 21282101; 21291392; 21304969; 21326871; 21430558; 21443859; 21487230; 21540177; 21562928; 21785974; 21967852; 21988832; 21990353; 22040870; 22065208; 22068265; 22089192; 22092351; 22168458; 22205725; 22215653; 22266374; 22315317; 22336959; 22349506; 22378291; 22435679; 22479552; 22510778; 22547144; 22647601; 22649490; 22654113; 22685582; 22920733; 22932900; 22940187; 22944052; 22983821; 22989886; 23141142; 23144166; 23158661; 23160450; 23208589; 23262340; 23295386; 23329136; 23372804; 23455924; 23476056; 23502212; 23522297; 23567058; 23583468; 23645771; 23657974; 23666678; 23707408; 23711995; 23736812; 23811234; 23814018; 23821302; 23891824; 23919842; 23930676; 24140347; 24169559; 24309288 peroxisome proliferator-activated receptor alpha Ensembl:ENSG00000186951 HGNC:9232 HPRD:01369 MIM:170998 Vega:OTTHUMG00000150443 Other designations: PPAR-alpha|nuclear receptor subfamily 1 group C member 1|peroxisome proliferative activated receptor, alpha|peroxisome proliferator-activated nuclear receptor alpha variant 3 PPARA OGG:3000005562 Bin Zhao, Yue Liu, Oliver He AMPK AMPKa1 WEB: http://www.ncbi.nlm.nih.gov/gene PRKAA1 protein kinase, AMP-activated, alpha 1 catalytic subunit 5562 5p12 9606 5 Official from a nomenclature committee GO_0000187 (EC: NAS, PMID: 11546797); GO_0001666 (EC: NAS, PMID: 8557660); GO_0003682 (EC: ISS); GO_0004672 (EC: IDA, PMID: 17028174); GO_0004679 (EC: IDA, PMID: 18439900); GO_0004691 (EC: NAS, PMID: 8557660); GO_0005515 (EC: IPI, PMID: 16306228); GO_0005524 (EC: IEA); GO_0005622 (EC: IC, PMID: 8557660); GO_0005634 (EC: IDA); GO_0005634 (EC: ISS); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006006 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0006468 (EC: IDA, PMID: 17028174); GO_0006633 (EC: IEA); GO_0006695 (EC: IEA); GO_0006914 (EC: IEA); GO_0007050 (EC: TAS); GO_0007165 (EC: TAS, PMID: 8557660); GO_0008022 (EC: IEA); GO_0008284 (EC: IEA); GO_0008286 (EC: TAS); GO_0008610 (EC: ISS); GO_0009631 (EC: IEA); GO_0010332 (EC: ISS); GO_0010508 (EC: ISS); GO_0010628 (EC: IDA, PMID: 17028174); GO_0014823 (EC: IEA); GO_0016055 (EC: IEA); GO_0016324 (EC: IEA); GO_0019395 (EC: IEA); GO_0019900 (EC: IEA); GO_0031000 (EC: IEA); GO_0031588 (EC: ISS); GO_0031669 (EC: ISS); GO_0032007 (EC: ISS); GO_0035174 (EC: ISS); GO_0042149 (EC: ISS); GO_0042593 (EC: ISS); GO_0042752 (EC: ISS); GO_0043066 (EC: ISS); GO_0045542 (EC: NAS, PMID: 8557660); GO_0045821 (EC: ISS); GO_0046318 (EC: NAS, PMID: 11165240); GO_0046872 (EC: IEA); GO_0047322 (EC: IEA); GO_0048511 (EC: IEA); GO_0050321 (EC: IEA); GO_0050405 (EC: IEA); GO_0050995 (EC: ISS); GO_0051291 (EC: IEA); GO_0055089 (EC: ISS); GO_0060627 (EC: IEA); GO_0070301 (EC: IEA); GO_0071361 (EC: IEA); GO_0071456 (EC: IEA); GO_2000505 (EC: ISS); GO_2001274 (EC: IEA) PMID: 1322130; 2900138; 7907095; 8094892; 8163463; 8557660; 8626596; 8663446; 8910387; 9091312; 9224708; 9710607; 9845345; 9857077; 10698692; 10760274; 10862786; 11042152; 11052978; 11165240; 11171059; 11500364; 11546797; 11903059; 11913976; 11971957; 11997383; 12091379; 12194824; 12368907; 12391032; 12477932; 12788940; 12791703; 12847291; 12853467; 12869384; 12890675; 14557259; 14651849; 14702039; 14709557; 14970221; 14976552; 14985344; 14985505; 15024086; 15261145; 15485651; 15489334; 16054041; 16054095; 16306228; 16344560; 16405649; 16466905; 16806233; 17028174; 17088252; 17584647; 18195011; 18276112; 18303014; 18347656; 18359290; 18403135; 18439900; 18614941; 18663353; 18674809; 18781797; 18801964; 18836454; 18950855; 18976975; 18996102; 19020741; 19049348; 19050283; 19138981; 19197243; 19211918; 19322201; 19442239; 19491292; 19502591; 19556893; 19616115; 19720090; 19723093; 19723094; 19723101; 19723105; 19728147; 19887561; 19913121; 19923924; 19948975; 19966861; 20080969; 20103647; 20167678; 20170185; 20217115; 20368287; 20368732; 20392842; 20421294; 20462511; 20538596; 20562859; 20564492; 20602615; 20622004; 20628086; 20660302; 20682687; 20821366; 20861072; 20876741; 21048031; 21072212; 21079763; 21088205; 21139048; 21209024; 21232561; 21344388; 21416543; 21432774; 21474997; 21651489; 21670147; 21678424; 21728993; 21768291; 21775054; 21807092; 21892142; 21906983; 21909354; 21963094; 21987572; 21988832; 21994947; 22007913; 22021095; 22037551; 22065577; 22212710; 22363791; 22378745; 22406815; 22419736; 22434430; 22462548; 22480519; 22553202; 22564965; 22607554; 22674476; 22688514; 22815988; 22833096; 22869372; 22897928; 22935535; 22939624; 22939629; 22988252; 23000302; 23022380; 23171948; 23221389; 23228943; 23291726; 23306156; 23324179; 23367447; 23376776; 23417417; 23418352; 23455922; 23463002; 23475945; 23506848; 23589839; 23592276; 23602568; 23625915; 23648710; 23671028; 23677989; 23712032; 23716691; 23723070; 23800577; 23819460; 23861218; 23878245; 23904275; 24047437; 24072697; 24095280; 24371122 protein kinase, AMP-activated, alpha 1 catalytic subunit Ensembl:ENSG00000132356 HGNC:9376 HPRD:04115 MIM:602739 Vega:OTTHUMG00000162269 Other designations: 5'-AMP-activated protein kinase catalytic subunit alpha-1|5'-AMP-activated protein kinase, catalytic alpha-1 chain|ACACA kinase|AMP -activate kinase alpha 1 subunit|AMP-activated protein kinase, catalytic, alpha-1|AMPK alpha 1|AMPK subunit alpha-1|HMGCR kinase|acetyl-CoA carboxylase kinase|hydroxymethylglutaryl-CoA reductase kinase|tau-protein kinase PRKAA1 PRKAA1 OGG:3000005570 Bin Zhao, Yue Liu, Oliver He PRKACN2 WEB: http://www.ncbi.nlm.nih.gov/gene PKIB protein kinase (cAMP-dependent, catalytic) inhibitor beta 5570 RP11-95G17.1 6q22.31 20140408 9606 6 protein-coding Official from a nomenclature committee GO_0004862 (EC: IEA) PMID: 2052616; 7684369; 8889548; 10880337; 11978406; 12061725; 12477932; 12748276; 14574404; 15342556; 15489334; 19035091; 19460752; 19483721; 21906983; 21988832; 23224602; 24250222 protein kinase (cAMP-dependent, catalytic) inhibitor beta Ensembl:ENSG00000135549 HGNC:9018 HPRD:06075 MIM:606914 Vega:OTTHUMG00000015488 Other designations: PKI-beta|cAMP-dependent protein kinase inhibitor 2|cAMP-dependent protein kinase inhibitor beta PKIB OGG:3000005579 Bin Zhao, Yue Liu, Oliver He PKC-beta PKCB PRKCB1 PRKCB2 WEB: http://www.ncbi.nlm.nih.gov/gene PRKCB protein kinase C, beta 5579 16p11.2 9606 16 Official from a nomenclature committee GO_0003682 (EC: IDA); GO_0004674 (EC: TAS); GO_0004697 (EC: IEA); GO_0005080 (EC: IPI); GO_0005246 (EC: IEA); GO_0005515 (EC: IPI, PMID: 18162466); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA, PMID: 15632189); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA, PMID: 15632189); GO_0005886 (EC: TAS); GO_0006351 (EC: IEA); GO_0006357 (EC: IMP); GO_0006468 (EC: TAS, PMID: 3755548); GO_0006816 (EC: IEA); GO_0006874 (EC: IEA); GO_0006915 (EC: IEA); GO_0007165 (EC: NAS, PMID: 3755548); GO_0007268 (EC: TAS); GO_0007596 (EC: TAS); GO_0008270 (EC: IEA); GO_0010829 (EC: ISS); GO_0030168 (EC: TAS); GO_0030374 (EC: IMP); GO_0030949 (EC: ISS); GO_0035403 (EC: IDA); GO_0035408 (EC: IDA); GO_0035556 (EC: IEA); GO_0042113 (EC: ISS); GO_0042393 (EC: IDA); GO_0042953 (EC: TAS, PMID: 18981301); GO_0043123 (EC: ISS); GO_0045766 (EC: ISS); GO_0046627 (EC: ISS); GO_0050681 (EC: IDA); GO_0050853 (EC: ISS); GO_0050861 (EC: ISS); GO_0051092 (EC: ISS); GO_0070062 (EC: IDA); GO_0071322 (EC: IEA) PMID: 1321150; 1324914; 1400396; 1556124; 1611098; 1714454; 1832084; 1970444; 2139676; 2140056; 2182321; 2757032; 3259291; 3658678; 3666134; 3677994; 3755548; 7499337; 7588787; 7642615; 7693453; 7716516; 7850771; 7876252; 7876254; 7880442; 7961692; 8034666; 8034726; 8080473; 8089108; 8163551; 8206685; 8327493; 8473314; 8557118; 8599832; 8626698; 8627654; 8631738; 8662663; 8663071; 8694767; 8749392; 8824244; 8898866; 8899875; 8914829; 8940095; 8940188; 8964400; 9021343; 9030777; 9052983; 9151826; 9244383; 9296367; 9446795; 9475183; 9671211; 9677319; 9694886; 9765207; 9814702; 9815893; 9856494; 10194441; 10212259; 10417813; 10433554; 10446219; 10480917; 10490850; 10491200; 10493829; 10502411; 10531036; 10542228; 10641798; 10828076; 10843712; 10856305; 10862698; 10871288; 11003709; 11035810; 11044099; 11063746; 11078718; 11120522; 11120743; 11123317; 11141237; 11145703; 11154208; 11179083; 11278382; 11278415; 11283022; 11306676; 11325528; 11376011; 11502742; 11504923; 11598012; 11700305; 11744714; 11749387; 11765038; 11781100; 11805327; 11833470; 11884598; 11901153; 11919157; 11930178; 12023512; 12033257; 12054501; 12056906; 12070292; 12080070; 12093536; 12118249; 12134071; 12147342; 12149258; 12167592; 12356761; 12435880; 12456365; 12477932; 12482669; 12509514; 12519779; 12551925; 12569090; 12618484; 12665801; 12679936; 12682249; 12724308; 12730099; 12743109; 12765965; 12766174; 12874455; 12917261; 12950453; 12958364; 14527960; 14561740; 14594954; 14602581; 14623273; 14654844; 14654845; 14699138; 14702039; 15037605; 15067001; 15090600; 15188402; 15213298; 15252133; 15322124; 15327405; 15381704; 15384959; 15488737; 15489334; 15499829; 15546881; 15591231; 15611095; 15632189; 15647851; 15689238; 15716278; 15741241; 15880462; 15894802; 15917249; 16000408; 16027742; 16055064; 16080189; 16102725; 16111671; 16224561; 16236825; 16331690; 16356855; 16430878; 16472601; 16517978; 16567829; 16574992; 16574993; 16626305; 16673150; 16775601; 16831865; 16854530; 16930534; 16954220; 17003377; 17069764; 17115053; 17121852; 17133356; 17167344; 17192257; 17203073; 17227757; 17455194; 17545677; 17625596; 17632570; 17719638; 17846295; 17893151; 17926183; 17936705; 17950644; 17991733; 18067888; 18162466; 18162471; 18167130; 18172602; 18278479; 18292183; 18303026; 18317465; 18440851; 18472156; 18497307; 18541226; 18557705; 18577246; 18596232; 18632858; 18637128; 18692180; 18701509; 18714023; 18768137; 18937679; 18981301; 19091746; 19112601; 19168795; 19277684; 19295663; 19363595; 19573263; 19681907; 19693767; 19738201; 19887445; 19895572; 19907441; 19913121; 19920073; 19949911; 19966859; 20015121; 20098747; 20099025; 20141354; 20164467; 20179100; 20228790; 20336759; 20346360; 20379614; 20439192; 20442744; 20511681; 20522523; 20534587; 20618341; 20628086; 20736472; 20842205; 20846475; 21044950; 21134959; 21323641; 21467074; 21482705; 21525390; 21651489; 21817106; 21997316; 22016563; 22114277; 22114345; 22162761; 22197823; 22322241; 22446963; 22479367; 22547057; 22633971; 22670899; 22833470; 22930730; 22939624; 23042805; 23128233; 23204109; 23280626; 23328482; 23337848; 23439007; 23455922; 23458603; 23503679; 23562913; 23960082; 23963366 protein kinase C, beta Ensembl:ENSG00000166501 HGNC:9395 HPRD:01499 MIM:176970 Vega:OTTHUMG00000131615 Other designations: PKC-B|protein kinase C beta type|protein kinase C, beta 1 polypeptide PRKCB OGG:3000005591 Bin Zhao, Yue Liu, Oliver He DNA-PKcs DNAPK DNPK1 HYRC HYRC1 XRCC7 p350 WEB: http://www.ncbi.nlm.nih.gov/gene PRKDC protein kinase, DNA-activated, catalytic polypeptide 5591 8q11 20140408 9606 8 protein-coding Official from a nomenclature committee GO_0000723 (EC: IEA); GO_0001756 (EC: IEA); GO_0002326 (EC: IEA); GO_0002328 (EC: IEA); GO_0002360 (EC: IEA); GO_0003677 (EC: IEA); GO_0004672 (EC: TAS, PMID: 7671312); GO_0004674 (EC: IDA, PMID: 19303849); GO_0004677 (EC: IDA, PMID: 15194694); GO_0005515 (EC: IPI, PMID: 17308091); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005667 (EC: IDA, PMID: 19303849); GO_0005730 (EC: IEA); GO_0005829 (EC: TAS); GO_0005958 (EC: IDA, PMID: 15194694); GO_0006281 (EC: TAS); GO_0006302 (EC: TAS); GO_0006303 (EC: TAS); GO_0006464 (EC: TAS, PMID: 7671312); GO_0007420 (EC: IEA); GO_0007507 (EC: IEA); GO_0008134 (EC: IPI, PMID: 19303849); GO_0008630 (EC: IEA); GO_0010332 (EC: IEA); GO_0018105 (EC: IDA, PMID: 15194694); GO_0019899 (EC: IEA); GO_0031648 (EC: IEA); GO_0032481 (EC: TAS); GO_0032869 (EC: IMP, PMID: 19303849); GO_0033077 (EC: IEA); GO_0033152 (EC: IEA); GO_0033153 (EC: IEA); GO_0035234 (EC: IEA); GO_0043065 (EC: IEA); GO_0044822 (EC: IDA); GO_0045087 (EC: TAS); GO_0045944 (EC: IMP, PMID: 19303849); GO_0070419 (EC: IDA) PMID: 1597196; 2247066; 2507541; 7594449; 7638222; 7671312; 8364539; 8407951; 8422676; 8464713; 8760815; 8804412; 8917110; 9035691; 9038175; 9139719; 9284934; 9295339; 9312071; 9325337; 9362500; 9363941; 9372844; 9398855; 9430729; 9435225; 9442054; 9488450; 9525578; 9586635; 9632806; 9679063; 9722660; 9748231; 9765199; 9766667; 9774685; 9914162; 10026262; 10064605; 10207052; 10213687; 10441130; 10446239; 10464290; 10467406; 10470151; 10547363; 10567342; 10608806; 10673501; 10713094; 10747897; 10750018; 10823961; 10951572; 11000264; 11030616; 11070027; 11101529; 11158303; 11160753; 11279128; 11406603; 11418067; 11551930; 11709713; 11731442; 11739746; 11749722; 11790298; 11801738; 11867762; 11883897; 11889123; 11904432; 11955432; 12023295; 12065055; 12065431; 12171929; 12186630; 12231622; 12379113; 12393188; 12477932; 12509254; 12519782; 12547193; 12672807; 12750264; 12756247; 12897153; 14556663; 14612514; 14627815; 14654699; 14704337; 14734805; 14744996; 14766968; 14966265; 15071507; 15123719; 15140983; 15147269; 15161933; 15163725; 15190070; 15194694; 15258142; 15262962; 15279776; 15286704; 15302935; 15313891; 15324660; 15353130; 15377652; 15381073; 15385968; 15389585; 15456891; 15493013; 15520013; 15574326; 15592499; 15613478; 15634916; 15635413; 15640154; 15664519; 15668230; 15668400; 15671175; 15677476; 15678105; 15698568; 15723802; 15758953; 15811628; 15875659; 15936993; 16000298; 16000400; 16001975; 16046194; 16075307; 16166097; 16196087; 16221682; 16226712; 16263121; 16314509; 16335966; 16397295; 16449650; 16510122; 16520097; 16540648; 16541024; 16565220; 16566590; 16600297; 16603769; 16713581; 16751065; 16759233; 16785234; 16794079; 16857680; 16874298; 17081983; 17110338; 17148452; 17189255; 17196815; 17213819; 17241822; 17242407; 17287830; 17308091; 17314511; 17389609; 17389650; 17400507; 17441731; 17526517; 17593081; 17626748; 17764108; 17786318; 17786349; 17932067; 17963495; 17991316; 18026119; 18158334; 18160036; 18172300; 18246802; 18247557; 18258596; 18270197; 18303054; 18406329; 18415044; 18422577; 18426604; 18449888; 18451257; 18505846; 18508926; 18550272; 18644470; 18644989; 18710952; 18728186; 18781797; 18789131; 18799040; 18922151; 18950845; 18952587; 18957425; 19021771; 19071136; 19074885; 19075392; 19092295; 19144640; 19181665; 19198648; 19224683; 19237606; 19270065; 19303849; 19322201; 19341095; 19351595; 19380743; 19394292; 19444312; 19451221; 19467273; 19573080; 19589246; 19596686; 19624897; 19661379; 19666485; 19672258; 19697154; 19738201; 19773279; 19781633; 19805454; 19815090; 19826009; 19833092; 19851285; 19918261; 20003485; 20023628; 20065038; 20080577; 20085707; 20111054; 20157594; 20204287; 20205745; 20219974; 20356835; 20360068; 20371770; 20379614; 20394854; 20427287; 20479123; 20496165; 20504901; 20522537; 20562859; 20590474; 20610542; 20618440; 20668194; 20711232; 20801936; 20813000; 20878914; 20936779; 20966071; 20972425; 21037379; 21042724; 21075794; 21081666; 21108935; 21139048; 21145461; 21151955; 21175350; 21182205; 21188139; 21209461; 21214942; 21300785; 21319273; 21330363; 21346760; 21415862; 21450944; 21487018; 21504906; 21549307; 21559021; 21565611; 21575865; 21576354; 21671477; 21679440; 21693764; 21723633; 21731742; 21750982; 21773671; 21775006; 21875946; 21890473; 21905307; 21906983; 21907836; 21941773; 21963094; 21969602; 21979916; 21987572; 22009179; 22027841; 22040967; 22053931; 22131882; 22139836; 22145905; 22174317; 22184063; 22190034; 22190353; 22198295; 22242598; 22268729; 22298787; 22310661; 22332739; 22337587; 22343725; 22366412; 22404984; 22499342; 22505724; 22586326; 22623428; 22634101; 22751105; 22753480; 22815474; 22825692; 22863883; 22923485; 22939629; 22952844; 23000965; 23001845; 23022380; 23098447; 23098854; 23108991; 23183621; 23204796; 23322783; 23325550; 23325849; 23398456; 23438482; 23449453; 23455922; 23464991; 23505488; 23603433; 23678292; 23722905; 23752268; 23775790; 23798571; 23824909; 23862649; 23897887; 23956138; 24013362; 24085291; 24136149; 24220101; 24250222; 24255178; 24457600 protein kinase, DNA-activated, catalytic polypeptide Ensembl:ENSG00000253729 HGNC:9413 HPRD:02941 MIM:600899 Other designations: DNA-PK catalytic subunit|DNA-dependent protein kinase catalytic subunit|hyper-radiosensitivity of murine scid mutation, complementing 1|p460 PRKDC OGG:3000005599 Bin Zhao, Yue Liu, Oliver He JNK JNK-46 JNK1 JNK1A2 JNK21B1/2 PRKM8 SAPK1 SAPK1c WEB: http://www.ncbi.nlm.nih.gov/gene MAPK8 mitogen-activated protein kinase 8 5599 10q11.22 9606 10 Official from a nomenclature committee GO_0001503 (EC: IEA); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0004674 (EC: IDA, PMID: 14967141); GO_0004705 (EC: IDA); GO_0005515 (EC: IPI, PMID: 10393177); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005739 (EC: IEA); GO_0005829 (EC: TAS); GO_0006915 (EC: TAS); GO_0006950 (EC: TAS, PMID: 8137421); GO_0007254 (EC: IDA, PMID: 8654373); GO_0007254 (EC: TAS); GO_0007258 (EC: IDA, PMID: 14967141); GO_0009411 (EC: IDA, PMID: 14967141); GO_0010628 (EC: IMP); GO_0018105 (EC: IDA, PMID: 15850461); GO_0018107 (EC: IDA); GO_0018107 (EC: IMP); GO_0031063 (EC: IMP); GO_0032091 (EC: IDA); GO_0032880 (EC: IDA); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035033 (EC: IMP); GO_0035666 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042826 (EC: IPI); GO_0043065 (EC: TAS); GO_0043066 (EC: IDA, PMID: 14967141); GO_0045087 (EC: TAS); GO_0046686 (EC: IEA); GO_0048011 (EC: TAS); GO_0051090 (EC: TAS); GO_0051403 (EC: TAS); GO_0071260 (EC: IEP, PMID: 19593445); GO_0090045 (EC: IMP); GO_0097190 (EC: TAS); GO_0097193 (EC: TAS); GO_1900740 (EC: TAS); GO_2000017 (EC: IEA); GO_2001235 (EC: IEA) PMID: 1748630; 7535770; 7642542; 7737129; 7737130; 7839144; 8001819; 8137421; 8177321; 8224842; 8586671; 8621542; 8632909; 8654373; 8846788; 8917518; 9020136; 9030579; 9045910; 9129988; 9162092; 9195981; 9199329; 9199504; 9207092; 9211903; 9223324; 9235954; 9343414; 9374537; 9393873; 9396779; 9399639; 9403476; 9405400; 9405416; 9520479; 9575168; 9621077; 9661668; 9670954; 9692890; 9724739; 9732264; 9733513; 9774977; 9788880; 9808624; 9851932; 9872331; 9889198; 10187783; 10346818; 10357815; 10383391; 10391943; 10393177; 10394361; 10419510; 10446219; 10471813; 10490659; 10509564; 10521505; 10523642; 10551811; 10567572; 10585392; 10597297; 10601313; 10629060; 10713157; 10722755; 10747973; 10756100; 10797012; 10799874; 10856240; 10878576; 10912793; 10913135; 10962563; 11042694; 11057897; 11062067; 11108663; 11153078; 11238452; 11260070; 11278395; 11278789; 11278799; 11279118; 11279197; 11279232; 11283254; 11323415; 11350938; 11387337; 11408587; 11432831; 11448159; 11468147; 11479302; 11489891; 11504923; 11517249; 11525649; 11551945; 11566021; 11602244; 11606564; 11698270; 11700324; 11707464; 11749722; 11781324; 11788583; 11865055; 11912216; 11931768; 11944898; 11948398; 11971973; 11983683; 11988087; 12023963; 12039864; 12052834; 12058026; 12058028; 12079429; 12089333; 12095152; 12097334; 12121974; 12135322; 12138158; 12140754; 12143039; 12148599; 12167088; 12171600; 12185592; 12189133; 12206715; 12223491; 12225289; 12228228; 12239168; 12242293; 12296995; 12351658; 12351702; 12354774; 12359245; 12376548; 12391307; 12413764; 12417588; 12421945; 12477932; 12478662; 12514174; 12538493; 12576423; 12591950; 12592382; 12646240; 12646564; 12659851; 12689591; 12697749; 12707267; 12714584; 12734330; 12756254; 12763138; 12775419; 12787561; 12788955; 12804775; 12810082; 12818176; 12821118; 12847227; 12853963; 12857973; 12859962; 12874243; 12878610; 12902351; 12917434; 12958075; 12960231; 12963725; 13130464; 14500675; 14500727; 14504284; 14514687; 14517282; 14532003; 14551213; 14557276; 14561739; 14572659; 14597672; 14612408; 14633987; 14637155; 14688370; 14699155; 14701702; 14701799; 14702039; 14724588; 14729602; 14764673; 14766760; 14967141; 14981905; 15013949; 15169762; 15184502; 15225643; 15238629; 15246824; 15276183; 15299005; 15302935; 15326485; 15334056; 15345747; 15383283; 15456887; 15474087; 15483136; 15516492; 15527495; 15528994; 15538975; 15542843; 15569856; 15590691; 15603708; 15629131; 15637062; 15655348; 15657352; 15659383; 15665513; 15677475; 15688026; 15693750; 15696159; 15721744; 15722200; 15733859; 15749833; 15755722; 15769735; 15778365; 15778501; 15827086; 15850461; 15857981; 15860507; 15890690; 15958389; 15979846; 15981086; 15998799; 16007099; 16038800; 16086581; 16105650; 16153436; 16157600; 16166642; 16176806; 16243842; 16260419; 16260609; 16264271; 16282329; 16283431; 16291755; 16307741; 16321971; 16328781; 16339571; 16344560; 16381010; 16395283; 16407310; 16412424; 16434970; 16446428; 16465391; 16481105; 16533805; 16539678; 16549498; 16569638; 16581800; 16611996; 16636664; 16648634; 16687404; 16699726; 16740711; 16760468; 16794185; 16802349; 16810318; 16814421; 16815888; 16824735; 16895791; 16912864; 16927023; 16972261; 16983342; 17008315; 17023523; 17054907; 17074809; 17079291; 17145805; 17158878; 17178870; 17189706; 17192257; 17255354; 17296730; 17303384; 17317777; 17363973; 17453826; 17478078; 17481915; 17496921; 17541429; 17545598; 17568996; 17584736; 17603935; 17620321; 17626013; 17640761; 17652454; 17690186; 17693927; 17699782; 17702750; 17703233; 17704768; 17719653; 17785464; 17875713; 17883418; 17904874; 17908987; 17913539; 17933493; 17942603; 17967471; 17982228; 18003900; 18025271; 18036196; 18055217; 18082745; 18086557; 18087676; 18094581; 18160848; 18164704; 18181766; 18199680; 18212053; 18218857; 18219313; 18249102; 18253836; 18256527; 18276794; 18286207; 18288129; 18292600; 18293403; 18297686; 18316600; 18316603; 18325654; 18337589; 18344085; 18348163; 18356158; 18373696; 18387958; 18401423; 18405916; 18429822; 18439101; 18457359; 18495129; 18506470; 18524773; 18540881; 18541008; 18547751; 18570871; 18573678; 18594007; 18603327; 18620777; 18636174; 18651223; 18663379; 18667537; 18681908; 18682391; 18703151; 18713649; 18713996; 18718914; 18723442; 18757369; 18769111; 18782768; 18813780; 18815275; 18818208; 18845538; 18922473; 18936517; 18950845; 18957422; 18978303; 18979912; 18982452; 18989785; 18996088; 19033664; 19036714; 19037093; 19041150; 19052872; 19056926; 19060920; 19069644; 19071215; 19074436; 19097143; 19153595; 19154785; 19159663; 19166930; 19168796; 19194824; 19204086; 19206162; 19234442; 19245816; 19248119; 19270716; 19275580; 19286999; 19287189; 19319745; 19339050; 19351724; 19352384; 19418584; 19424800; 19454725; 19468799; 19478459; 19479051; 19523467; 19527717; 19567513; 19570911; 19574423; 19589256; 19593445; 19596001; 19604147; 19616043; 19620725; 19638579; 19651615; 19664626; 19667122; 19676104; 19686584; 19690982; 19693773; 19695707; 19723092; 19723627; 19748889; 19778898; 19782079; 19801633; 19802005; 19803394; 19806201; 19815509; 19822148; 19822666; 19859790; 19862774; 19864026; 19877043; 19893453; 19900593; 19901160; 19910486; 19913121; 19923798; 19937141; 19940138; 19940360; 19966288; 19995557; 19996270; 20018857; 20027304; 20051532; 20056178; 20056910; 20060003; 20069553; 20070836; 20070945; 20074375; 20086174; 20088952; 20102411; 20103647; 20116378; 20130137; 20133937; 20138424; 20139358; 20142324; 20145041; 20150185; 20156194; 20173753; 20194509; 20225236; 20336759; 20371626; 20380698; 20432452; 20450729; 20452983; 20457808; 20483637; 20483734; 20490718; 20495362; 20510162; 20511226; 20512919; 20512932; 20525557; 20551953; 20566643; 20573157; 20581839; 20622336; 20628086; 20632440; 20647313; 20648623; 20680486; 20717968; 20732415; 20735357; 20829350; 20870032; 20878914; 20919940; 20944115; 20960177; 21106355; 21122381; 21123173; 21134350; 21139048; 21145111; 21148294; 21148313; 21152872; 21156789; 21172010; 21172429; 21187925; 21191018; 21212517; 21223552; 21237154; 21362231; 21364631; 21364637; 21368226; 21378396; 21384452; 21439937; 21444723; 21454558; 21465527; 21483469; 21483669; 21504622; 21511059; 21524306; 21526344; 21629969; 21651489; 21660049; 21697181; 21719561; 21729547; 21752354; 21757743; 21764057; 21768777; 21775054; 21806545; 21817106; 21822690; 21832049; 21856198; 21863240; 21900206; 21906983; 21930785; 21931671; 21943220; 21948112; 21959987; 21964465; 21984578; 21988832; 22005259; 22014979; 22021110; 22087220; 22100391; 22110360; 22114267; 22154358; 22164242; 22171160; 22184250; 22283740; 22327296; 22351776; 22357202; 22363806; 22394200; 22433870; 22435755; 22446103; 22447977; 22450687; 22456510; 22493283; 22493490; 22505724; 22506718; 22509080; 22689214; 22729748; 22749438; 22763043; 22766602; 22844345; 22850273; 22870247; 22902540; 22920299; 23020677; 23051914; 23056263; 23077074; 23237571; 23258237; 23273084; 23290789; 23326144; 23359252; 23393199; 23416355; 23440494; 23580093; 23602568; 23603344; 23608488; 23608534; 23615449; 23662689; 23712703; 23715767; 23770673; 23861391; 23906792; 23916702; 24023291; 24055030; 24091673; 24184208; 24225136 mitogen-activated protein kinase 8 Ensembl:ENSG00000107643 HGNC:6881 HPRD:03100 MIM:601158 Vega:OTTHUMG00000018172 Other designations: JUN N-terminal kinase|MAP kinase 8|c-Jun N-terminal kinase 1|mitogen-activated protein kinase 8 isoform JNK1 alpha1|mitogen-activated protein kinase 8 isoform JNK1 beta2|stress-activated protein kinase 1|stress-activated protein kinase 1c MAPK8 OGG:3000005608 Bin Zhao, Yue Liu, Oliver He MAPKK6 MEK6 MKK6 PRKMK6 SAPKK-3 SAPKK3 WEB: http://www.ncbi.nlm.nih.gov/gene MAP2K6 mitogen-activated protein kinase kinase 6 5608 17q24.3 9606 17 Official from a nomenclature committee GO_0000187 (EC: TAS); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0002931 (EC: IEA); GO_0004702 (EC: IBA); GO_0004708 (EC: IBA); GO_0004713 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15229216); GO_0005524 (EC: IEA); GO_0005654 (EC: TAS); GO_0005737 (EC: IBA); GO_0005829 (EC: TAS); GO_0005856 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0006915 (EC: IEA); GO_0006975 (EC: TAS, PMID: 10848581); GO_0007050 (EC: TAS, PMID: 10848581); GO_0007165 (EC: TAS, PMID: 8621675); GO_0019901 (EC: IPI, PMID: 11279118); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035666 (EC: TAS); GO_0035872 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042493 (EC: IEA); GO_0042692 (EC: TAS); GO_0043065 (EC: IEA); GO_0045087 (EC: TAS); GO_0051149 (EC: TAS); GO_0051403 (EC: TAS); GO_0060048 (EC: IEA); GO_0070423 (EC: TAS); GO_0072709 (EC: IEA) PMID: 7750576; 8125298; 8621675; 8622669; 8626699; 8663074; 8861944; 9218798; 9430721; 9768359; 9808624; 9841871; 10094049; 10497253; 10570156; 10702308; 10838074; 10848581; 10961885; 11062067; 11062068; 11104681; 11279118; 11460167; 11562357; 11689443; 11727828; 11836244; 11971971; 12054652; 12242293; 12477932; 12509443; 12556533; 12589052; 12609980; 12697810; 12761180; 12820963; 14633987; 15229216; 15276183; 15375157; 15489334; 15492008; 15516490; 15550393; 15590691; 15677464; 15717329; 15722372; 15764709; 15778394; 15790570; 15866172; 15923648; 16157600; 16313339; 16342939; 16344560; 16498455; 16728640; 16893890; 16960152; 17079228; 17255097; 17255949; 17363905; 17363973; 17384642; 18327563; 19047046; 19141286; 19234473; 19302196; 19672773; 19675569; 19737936; 19846005; 19913121; 20067578; 20162623; 20213747; 20364819; 20628086; 20706999; 20805296; 20869211; 20932476; 21078955; 21139048; 21308746; 21368234; 21890473; 21926646; 22154358; 22164285; 22383536; 22569225; 23606331; 23744074 mitogen-activated protein kinase kinase 6 HGNC:6846 HPRD:03155 MIM:601254 Other designations: MAPK/ERK kinase 6|MAPKK 6|MEK 6|SAPK kinase 3|dual specificity mitogen-activated protein kinase kinase 6|protein kinase, mitogen-activated, kinase 6 (MAP kinase kinase 6)|stress-activated protein kinase kinase 3 MAP2K6 OGG:3000005610 Bin Zhao, Yue Liu, Oliver He EIF2AK1 PKR PRKR WEB: http://www.ncbi.nlm.nih.gov/gene EIF2AK2 eukaryotic translation initiation factor 2-alpha kinase 2 5610 2p22-p21 9606 2 GO_0000186 (EC: IMP, PMID:15229216); GO_0001819 (EC: ISS); GO_0003725 (EC: IDA); GO_0004672 (EC: IDA, PMID:12882984); GO_0004672 (EC: IMP); GO_0004674 (EC: TAS, PMID:1695551); GO_0004694 (EC: TAS, PMID:10866685); GO_0004715 (EC: IEA); GO_0005515 (EC: IPI, PMID:10390359); GO_0005524 (EC: IEA); GO_0005634 (EC: IEA); GO_0005737 (EC: IDA, PMID:15121867); GO_0005829 (EC: TAS); GO_0006351 (EC: IEA); GO_0006412 (EC: IEA); GO_0006468 (EC: IDA, PMID:19189853); GO_0008285 (EC: TAS, PMID:1351683); GO_0008601 (EC: TAS, PMID:10866685); GO_0009615 (EC: IMP, PMID:19189853); GO_0017148 (EC: IDA, PMID:12882984); GO_0017148 (EC: IMP, PMID:19189853); GO_0019048 (EC: TAS); GO_0019054 (EC: TAS); GO_0019058 (EC: TAS); GO_0030683 (EC: TAS); GO_0030968 (EC: IEA); GO_0032722 (EC: ISS); GO_0032874 (EC: ISS); GO_0033689 (EC: IMP, PMID:16216244); GO_0035455 (EC: IDA, PMID:19840259); GO_0044822 (EC: IDA); GO_0045071 (EC: IMP, PMID:19189853); GO_0045087 (EC: IEA); GO_0046777 (EC: IDA); GO_0046777 (EC: IMP, PMID:16216244); GO_0048471 (EC: IDA, PMID:15121867); GO_0051092 (EC: IDA, PMID:15121867); GO_0051607 (EC: IEA); GO_1900225 (EC: ISS); GO_1901224 (EC: ISS); GO_1901532 (EC: ISS); GO_1902033 (EC: ISS); GO_1902036 (EC: ISS) PMID:1351683; 1373553; 1373554; 1677563; 1695551; 1708818; 2180064; 7491766; 7568151; 7686883; 7686884; 7738010; 7757816; 8099444; 8576172; 8601309; 8812437; 8887659; 8889548; 8921913; 9079663; 9135145; 9143277; 9214631; 9447982; 9528799; 9687506; 9721103; 9726442; 9735304; 9736623; 9781815; 9819435; 10320367; 10330179; 10348343; 10390359; 10400669; 10400814; 10542257; 10557102; 10620360; 10648614; 10684936; 10723127; 10747897; 10848580; 10866685; 10884347; 11123929; 11152499; 11238927; 11278865; 11337501; 11350938; 11438532; 11438536; 11438540; 11447118; 11468270; 11526399; 11555640; 11773402; 11836380; 11921349; 11985496; 11991642; 12051728; 12055262; 12060652; 12138106; 12231563; 12349906; 12368306; 12368348; 12396729; 12397061; 12447867; 12473108; 12477932; 12483527; 12539042; 12609980; 12665801; 12679338; 12882984; 12944978; 13678666; 14638359; 14698665; 14765129; 14961569; 15121867; 15122791; 15207627; 15229216; 15299030; 15489334; 15535414; 15596837; 15607693; 15625311; 15635413; 15737233; 15815621; 15880455; 15907845; 16009940; 16156900; 16216244; 16271080; 16288713; 16339759; 16373505; 16446363; 16466763; 16580685; 16785445; 16861340; 16861808; 16924232; 16954686; 16957780; 16989899; 17202131; 17284445; 17290288; 17307214; 17318221; 17353931; 17420072; 17451862; 17522227; 17541283; 17596833; 17597457; 17612505; 17686861; 17716668; 17785458; 17851256; 17928244; 17928446; 17959656; 17975119; 17977969; 18023289; 18048689; 18063576; 18087277; 18362360; 18426922; 18496558; 18599499; 18684815; 18684960; 18728014; 18835251; 18927075; 18936160; 18957415; 18976633; 18991615; 19004947; 19023099; 19028691; 19106640; 19109397; 19151623; 19189853; 19210572; 19229320; 19259124; 19322201; 19349624; 19353519; 19364808; 19416861; 19434718; 19445956; 19507191; 19515768; 19605474; 19605483; 19642004; 19651874; 19710021; 19733181; 19744687; 19776135; 19812373; 19840259; 19846517; 19846675; 20006836; 20006840; 20171114; 20181660; 20309637; 20331378; 20353946; 20395957; 20447405; 20485506; 20587610; 20588308; 20628624; 20685959; 20930042; 21029237; 21048031; 21072047; 21123378; 21123651; 21139048; 21145461; 21294215; 21338484; 21377708; 21385567; 21464971; 21468538; 21504114; 21526770; 21698289; 21710204; 21715487; 21790829; 21846836; 21882225; 21890473; 21903422; 21906983; 21907836; 22022264; 22102852; 22174754; 22190034; 22278235; 22281122; 22306812; 22381929; 22473766; 22647704; 22787234; 22801494; 22894766; 22896602; 22912486; 22939624; 22939629; 22948139; 22986343; 23064357; 23084476; 23115276; 23115300; 23148689; 23151878; 23221979; 23229543; 23302873; 23314571; 23320095; 23370317; 23372823; 23399035; 23455922; 23527187; 23682076; 23706307; 23853588; 24089560; 24163370; 24334130 eukaryotic translation initiation factor 2-alpha kinase 2 Ensembl:ENSG00000055332 HGNC:9437 HPRD:01468 MIM:176871 Other designations: P1/eIF-2A protein kinase|double stranded RNA activated protein kinase|eIF-2A protein kinase 2|interferon-induced, double-stranded RNA-activated protein kinase|interferon-inducible elF2alpha kinase|p68 kinase|protein kinase, interferon-inducible double stranded RNA dependent|tyrosine-protein kinase EIF2AK2 EIF2AK2 OGG:3000005611 Bin Zhao, Yue Liu, Oliver He ERdj6 HP58 P58 P58IPK PRKRI WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC3 DnaJ (Hsp40) homolog, subfamily C, member 3 5611 13q32.1 9606 13 GO_0004860 (EC: TAS, PMID:7511204); GO_0005737 (EC: TAS, PMID:8666242); GO_0005788 (EC: TAS); GO_0006469 (EC: TAS, PMID:7511204); GO_0006987 (EC: TAS); GO_0030968 (EC: TAS); GO_0031205 (EC: IEA); GO_0044267 (EC: TAS); GO_0051087 (EC: IEA); GO_0051603 (EC: IEA); GO_0051607 (EC: IEA); GO_0051787 (EC: IEA); GO_0070062 (EC: IDA, PMID:19199708) PMID:7511204; 8576172; 8666242; 8824806; 8824808; 9447982; 9920933; 11116152; 11147971; 11526399; 11939789; 11991713; 12034040; 12446838; 12477932; 12601012; 15057823; 15489334; 18568130; 19199708; 20237496; 20554776; 21139048; 21799829; 21906983; 21963094; 22064321; 22190034; 24250222 DnaJ (Hsp40) homolog, subfamily C, member 3 Ensembl:ENSG00000102580 HGNC:9439 HPRD:03114 MIM:601184 Vega:OTTHUMG00000017227 Other designations: ER-resident protein ERdj6|dnaJ homolog subfamily C member 3|endoplasmic reticulum DNA J domain-containing protein 6|endoplasmic reticulum DnaJ protein 6|interferon-induced, double-stranded RNA-activated protein kinase inhibitor|protein kinase inhibitor of 58 kDa|protein kinase inhibitor p58|protein-kinase, interferon-inducible double stranded RNA dependent inhibitor DNAJC3 OGG:3000005734 Bin Zhao, Yue Liu, Oliver He EP4 EP4R WEB: http://www.ncbi.nlm.nih.gov/gene PTGER4 prostaglandin E receptor 4 (subtype EP4) 5734 5p13.1 9606 5 Official from a nomenclature committee GO_0004957 (EC: IDA, PMID: 8163486); GO_0005515 (EC: IPI, PMID: 16424369); GO_0005886 (EC: TAS); GO_0006955 (EC: IEP, PMID: 8862514); GO_0007188 (EC: IDA, PMID: 8163486); GO_0007254 (EC: ISS); GO_0009612 (EC: IEP); GO_0016021 (EC: NAS, PMID: 8163486); GO_0030278 (EC: IEA); GO_0032496 (EC: IEA); GO_0033624 (EC: IDA); GO_0042093 (EC: ISS); GO_0050710 (EC: ISS); GO_0050715 (EC: ISS); GO_0050728 (EC: IDA, PMID: 16424369); GO_0050729 (EC: ISS); GO_0051492 (EC: ISS); GO_0060348 (EC: ISS); GO_0070371 (EC: ISS); GO_0071260 (EC: ISS); GO_2000420 (EC: IDA) PMID: 7759114; 8078484; 8163486; 8250933; 8661119; 8855294; 8862514; 9214685; 10880739; 11093764; 11344234; 11423555; 11470276; 11597569; 11706038; 11782353; 11876748; 11948128; 11951086; 12036966; 12149218; 12215436; 12228765; 12477932; 12566441; 14517215; 14709160; 15100359; 15290741; 15347673; 15489334; 15528329; 15970595; 16020747; 16424369; 16428339; 16432186; 16574793; 16857763; 17046175; 17130837; 17290397; 17447842; 17496729; 17525067; 17611676; 17631291; 17684544; 17877755; 18005048; 18083712; 18086382; 18254372; 18270204; 18319253; 18516068; 18587394; 18797183; 18802112; 18829529; 19227010; 19273625; 19336370; 19407222; 19407341; 19444759; 19445930; 19453261; 19525953; 19558693; 19760754; 19879194; 19913121; 20014019; 20018632; 20086108; 20145136; 20222910; 20237496; 20353998; 20452482; 20484658; 20503412; 20549515; 20551148; 20561984; 20587336; 20628086; 20673868; 20846217; 20962850; 20970516; 21052031; 21071691; 21072187; 21081469; 21102463; 21111772; 21297633; 21365278; 21424266; 21589857; 21600299; 21681739; 21683675; 21723865; 21743469; 21832044; 21833088; 21890473; 22037551; 22080750; 22199300; 22276108; 22353936; 22362924; 22412388; 22570697; 22580611; 22695889; 22704539; 22706114; 22732652; 22924768; 22936669; 23090667; 23128233; 23242524; 23300802; 23337716; 23613969; 23619266; 23759445; 23817569 prostaglandin E receptor 4 (subtype EP4) Ensembl:ENSG00000171522 HGNC:9596 HPRD:03350 MIM:601586 Vega:OTTHUMG00000094769 Other designations: PGE receptor EP4 subtype|PGE receptor, EP4 subtype|PGE2 receptor EP4 subtype|prostaglandin E2 receptor EP4 subtype|prostanoid EP4 receptor PTGER4 OGG:3000005775 Bin Zhao, Yue Liu, Oliver He MEG PTPMEG PTPMEG1 WEB: http://www.ncbi.nlm.nih.gov/gene PTPN4 protein tyrosine phosphatase, non-receptor type 4 (megakaryocyte) 5775 2q14.2 9606 2 Official from a nomenclature committee GO_0004726 (EC: IEA); GO_0005515 (EC: IPI, PMID: 16169070); GO_0005737 (EC: IDA, PMID: 10940933); GO_0005856 (EC: IEA); GO_0006470 (EC: TAS, PMID: 1648233); GO_0008092 (EC: IEA); GO_0009898 (EC: IDA, PMID: 10940933); GO_0035335 (EC: TAS, PMID: 1648233) PMID: 1648233; 8910369; 8917530; 10748123; 10940933; 11054567; 12477932; 15489334; 16169070; 16226712; 17474147; 18614237; 21900206; 21988832; 23666597; 24250222 protein tyrosine phosphatase, non-receptor type 4 (megakaryocyte) Ensembl:ENSG00000088179 HGNC:9656 HPRD:01471 MIM:176878 Vega:OTTHUMG00000131436 Other designations: PTPase-MEG1|megakaryocyte phosphatase|megakaryocyte protein-tyrosine phosphatase|protein tyrosine phosphatase MEG1|protein-tyrosine phosphatase MEG1|tyrosine-protein phosphatase non-receptor type 4 PTPN4 OGG:3000005777 Bin Zhao, Yue Liu, Oliver He HCP HCPH HPTP1C PTP-1C SH-PTP1 SHP-1 SHP-1L SHP1 WEB: http://www.ncbi.nlm.nih.gov/gene PTPN6 protein tyrosine phosphatase, non-receptor type 6 5777 12p13 9606 12 Official from a nomenclature committee GO_0001784 (EC: IEA); GO_0002924 (EC: IEA); GO_0004725 (EC: TAS); GO_0005001 (EC: IDA, PMID: 11266449); GO_0005515 (EC: IPI, PMID: 10206955); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005737 (EC: IDA, PMID: 10940933); GO_0005829 (EC: TAS); GO_0006470 (EC: IDA, PMID: 11266449); GO_0006915 (EC: TAS, PMID: 10506221); GO_0007186 (EC: TAS, PMID: 7781604); GO_0007596 (EC: TAS); GO_0008283 (EC: IDA, PMID: 11266449); GO_0008284 (EC: IMP, PMID: 19749791); GO_0008285 (EC: NAS, PMID: 10497187); GO_0014068 (EC: IMP, PMID: 19838216); GO_0016020 (EC: TAS, PMID: 10506221); GO_0017124 (EC: IEA); GO_0018108 (EC: IDA, PMID: 18802077); GO_0019221 (EC: TAS); GO_0019901 (EC: IPI, PMID: 11266449); GO_0030154 (EC: IDA, PMID: 11266449); GO_0031295 (EC: TAS); GO_0042105 (EC: IEA); GO_0042130 (EC: IEA); GO_0042169 (EC: IEA); GO_0042267 (EC: IEA); GO_0043407 (EC: IEA); GO_0045577 (EC: IEA); GO_0050732 (EC: IMP, PMID: 19749791); GO_0050853 (EC: IEA); GO_0050860 (EC: IEA); GO_0050900 (EC: TAS); GO_0060333 (EC: TAS); GO_0060334 (EC: TAS); GO_0060337 (EC: TAS); GO_0060338 (EC: TAS); GO_0060397 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867); GO_0070372 (EC: IDA, PMID: 11266449); GO_2000045 (EC: IMP, PMID: 19838216) PMID: 1639416; 1652101; 1732748; 1736296; 7512963; 7518460; 7528577; 7539038; 7539106; 7618087; 7629131; 7665165; 7673163; 7684496; 7716523; 7781604; 7889566; 8114715; 8125298; 8246974; 8524272; 8541543; 8574854; 8627166; 8632004; 8638162; 8647855; 8692915; 8760799; 8780698; 8790380; 8943344; 8943354; 9029147; 9045636; 9064344; 9074930; 9148918; 9151699; 9162089; 9211920; 9244303; 9254654; 9261115; 9285411; 9285412; 9305905; 9368621; 9379041; 9405464; 9482905; 9485206; 9507021; 9520455; 9528781; 9531263; 9590210; 9632636; 9632768; 9712903; 9733788; 9740800; 9765283; 9774441; 9774457; 9788431; 9813145; 9842885; 9867848; 9890995; 9973385; 10072516; 10082557; 10206955; 10228003; 10229828; 10350061; 10457220; 10458769; 10488096; 10497187; 10506221; 10506573; 10521452; 10574931; 10585470; 10617656; 10640770; 10660565; 10660620; 10747947; 10764762; 10772872; 10790433; 10800945; 10835420; 10903717; 10903736; 10940933; 11001933; 11027300; 11042209; 11114375; 11160222; 11162587; 11171044; 11178971; 11266449; 11278955; 11294838; 11328818; 11337495; 11356834; 11414741; 11489943; 11511520; 11544253; 11551923; 11714803; 11723252; 11786908; 11812650; 11826756; 11858824; 11895767; 11907066; 11920268; 11964172; 11986327; 11987243; 12051764; 12130517; 12145285; 12145687; 12163025; 12176037; 12176909; 12196526; 12198247; 12361947; 12393607; 12438221; 12459556; 12468540; 12468645; 12477932; 12482860; 12571228; 12591278; 12646642; 12705885; 12734331; 12774026; 12791978; 12796776; 12832410; 12882840; 12917349; 14500659; 14551136; 14630083; 14662855; 14672952; 14691303; 14976049; 15070900; 15184070; 15187115; 15197735; 15269224; 15339845; 15456853; 15489334; 15549731; 15557341; 15574429; 15579525; 15588985; 15701718; 15746253; 15831474; 15870198; 16169070; 16326706; 16341674; 16344560; 16453023; 16482509; 16501054; 17046078; 17079228; 17142110; 17143285; 17218319; 17227821; 17239936; 17272397; 17404032; 17561098; 17579069; 18029348; 18086677; 18174230; 18209728; 18377662; 18441283; 18502033; 18543080; 18604210; 18729074; 18802077; 18948549; 18952289; 19056867; 19096001; 19104650; 19147543; 19166311; 19167335; 19204726; 19234487; 19379557; 19398961; 19542910; 19543515; 19551406; 19561639; 19591923; 19619438; 19749791; 19789387; 19838216; 19874234; 19950550; 20068065; 20117097; 20130595; 20196786; 20351292; 20398180; 20424160; 20687222; 20696858; 20840866; 21291405; 21357539; 21406173; 21465528; 21505184; 21505186; 21536801; 21604205; 21719561; 21799016; 21806449; 21818116; 21821701; 21890473; 21900501; 21906983; 21964525; 22043923; 22180308; 22210881; 22258937; 22371396; 22458809; 22458980; 22488585; 22505724; 22539788; 22589543; 22730659; 22738830; 22939629; 22960265; 23074279; 23391724; 23406209; 23766558; 23842094; 23979523 protein tyrosine phosphatase, non-receptor type 6 Ensembl:ENSG00000111679 HGNC:9658 HPRD:01475 MIM:176883 Vega:OTTHUMG00000168518 Other designations: hematopoietic cell phosphatase|hematopoietic cell protein-tyrosine phosphatase|protein-tyrosine phosphatase 1C|protein-tyrosine phosphatase SHP-1|tyrosine-protein phosphatase non-receptor type 6 PTPN6 OGG:3000005820 olfactory receptor family 3 subfamily A member 4 pseudogene NCBI-Human-GeneID:5820 PVT1 NCBI-Human-GeneID:5820 https://www.ncbi.nlm.nih.gov/gene/5820 OGG:3000005824 Bin Zhao, Yue Liu, Oliver He D1S2223E HK33 PBD12A PMP1 PMPI PXF PXMP1 WEB: http://www.ncbi.nlm.nih.gov/gene PEX19 peroxisomal biogenesis factor 19 5824 OK/SW-cl.22 1q23.2 9606 1 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 10704444); GO_0005634 (EC: IDA); GO_0005634 (EC: IMP, PMID: 12924628); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005737 (EC: IMP, PMID: 12924628); GO_0005737 (EC: ISS); GO_0005777 (EC: IDA, PMID: 19114594); GO_0005777 (EC: ISS); GO_0005778 (EC: IDA, PMID: 15713480); GO_0005829 (EC: IDA, PMID: 19114594); GO_0005829 (EC: TAS); GO_0006625 (EC: IDA, PMID: 16344115); GO_0006625 (EC: IMP, PMID: 10704444); GO_0007031 (EC: IMP, PMID: 11883941); GO_0007031 (EC: NAS, PMID: 9339377); GO_0016021 (EC: IDA, PMID: 10051604); GO_0016557 (EC: IDA, PMID: 10051604); GO_0016559 (EC: IMP, PMID: 18782765); GO_0031526 (EC: ISS); GO_0036105 (EC: IDA, PMID: 14709540); GO_0043231 (EC: IDA); GO_0043234 (EC: IDA, PMID: 18174172); GO_0045046 (EC: IDA, PMID: 11402059); GO_0047485 (EC: IPI, PMID: 19197237); GO_0050821 (EC: IDA, PMID: 14709540); GO_0051117 (EC: IPI, PMID: 11453642); GO_0055085 (EC: TAS); GO_0061077 (EC: IDA, PMID: 14709540); GO_0072321 (EC: IDA, PMID: 11402059); GO_0072663 (EC: IMP, PMID: 18782765); GO_1900131 (EC: IDA, PMID: 19715730) PMID: 8076834; 9339377; 9418908; 10051604; 10704444; 10777694; 11259404; 11390669; 11402059; 11453642; 11590176; 11883941; 12096124; 12154087; 12477932; 12581788; 12924628; 14558883; 14709540; 14713233; 14715663; 15007061; 15231748; 15252024; 15489334; 15713480; 15781447; 16280322; 16344115; 16459329; 16582619; 16763195; 16791427; 16895967; 16980692; 17069900; 18174172; 18782765; 19114594; 19195843; 19197237; 19322201; 19715730; 20301621; 20531392; 20554521; 20615514; 20683989; 21102411; 21139048; 21525035; 21890473; 21906983; 21963094; 21987572; 21988832; 22053931; 22505724; 22624858; 22939629; 23000965; 23460677; 23956138 peroxisomal biogenesis factor 19 Ensembl:ENSG00000162735 HGNC:9713 HPRD:02610 MIM:600279 Vega:OTTHUMG00000033112 Other designations: 33 kDa housekeeping protein|housekeeping gene, 33kD|peroxin-19|peroxisomal farnesylated protein PEX19 OGG:3000005872 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene RAB13 RAB13, member RAS oncogene family 5872 GIG4 1q21.2 9606 1 Official from a nomenclature committee GO_0003924 (EC: EXP); GO_0005515 (EC: IPI, PMID: 16525024); GO_0005525 (EC: IDA); GO_0005737 (EC: IDA); GO_0005794 (EC: IDA, Qualifier: NOT, PMID: 18779367); GO_0005802 (EC: IDA, PMID: 18779367); GO_0005886 (EC: IDA); GO_0005923 (EC: IDA, PMID: 12058051); GO_0006184 (EC: EXP); GO_0007264 (EC: IEA); GO_0010737 (EC: IMP, PMID: 15096524); GO_0015031 (EC: IEA); GO_0016197 (EC: IMP, PMID: 18779367); GO_0016328 (EC: IDA, PMID: 12058051); GO_0030027 (EC: ISS); GO_0030139 (EC: IDA, PMID: 15528189); GO_0030658 (EC: IEA); GO_0030659 (EC: TAS); GO_0030866 (EC: ISS); GO_0031175 (EC: IMP); GO_0031410 (EC: IDA, PMID: 8294494); GO_0032456 (EC: IMP, PMID: 15528189); GO_0032593 (EC: ISS); GO_0032869 (EC: ISS); GO_0034236 (EC: IEA); GO_0035767 (EC: ISS); GO_0043005 (EC: IDA); GO_0044795 (EC: ISS); GO_0055037 (EC: IDA, PMID: 18779367); GO_0055038 (EC: IEA); GO_0061024 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867); GO_0070830 (EC: IMP, PMID: 12058051); GO_0090002 (EC: IMP, PMID: 15096524); GO_0097368 (EC: ISS) PMID: 8294494; 8375503; 9605854; 9712853; 9918381; 11076863; 12058051; 12477932; 14702039; 15096524; 15146197; 15489334; 15489336; 15528189; 15761153; 16381901; 16525024; 16710414; 16923123; 17891173; 18029348; 18779367; 19056867; 19273188; 19885626; 20360680; 21139048; 21890473; 21906983; 22178446; 22562557; 23000965; 23246001 RAB13, member RAS oncogene family Other designations: RAS-associated protein RAB13|cell growth-inhibiting gene 4 protein|growth-inhibiting gene 4 protein|ras-related protein Rab-13 RAB13 OGG:3000005890 Bin Zhao, Yue Liu, Oliver He R51H2 RAD51L1 REC2 WEB: http://www.ncbi.nlm.nih.gov/gene RAD51B RAD51 paralog B 5890 14q23-q24.2 9606 14 Official from a nomenclature committee GO_0000400 (EC: IDA, Qualifier: contributes_to); GO_0000724 (EC: IMP); GO_0003677 (EC: TAS, PMID: 9512535); GO_0003690 (EC: IDA, PMID: 12441335); GO_0003697 (EC: IDA, PMID: 12441335); GO_0005515 (EC: IPI); GO_0005524 (EC: IEA); GO_0005634 (EC: TAS, PMID: 9512535); GO_0005654 (EC: TAS); GO_0005657 (EC: IDA); GO_0006200 (EC: IDA, PMID: 12441335); GO_0006281 (EC: TAS, PMID: 9512535); GO_0006310 (EC: TAS, PMID: 9512535); GO_0007131 (EC: TAS, PMID: 9441753); GO_0007596 (EC: TAS); GO_0008094 (EC: IDA, PMID: 12441335); GO_0010971 (EC: IMP); GO_0033063 (EC: IDA, PMID: 11751635) PMID: 4595808; 6261043; 8889548; 9207106; 9441753; 9512535; 9788630; 9878257; 9892177; 10565301; 10938124; 11744692; 11751635; 11751636; 11842112; 11842113; 11978964; 12118380; 12427746; 12441335; 12477932; 12508121; 12649198; 12975363; 14595808; 14704354; 15065660; 15115758; 15489334; 15701685; 18270339; 19329439; 19330030; 19657362; 19714462; 19850743; 20095854; 20195514; 20237344; 20379614; 20496165; 20522537; 20610542; 20881960; 21368091; 21399635; 21533530; 21852249; 21965664; 22017238; 22139419; 22232737; 22454379; 23001122; 23108668; 23251661; 23455636; 23535729; 23535732; 23810717; 24022229 RAD51 paralog B Ensembl:ENSG00000182185 HGNC:9822 HPRD:04255 MIM:602948 Vega:OTTHUMG00000157530 Other designations: DNA repair protein RAD51 homolog 2|RAD51 homolog B|RecA-like protein|recombination repair protein RAD51B OGG:3000005933 Bin Zhao, Yue Liu, Oliver He CP107 PRB1 p107 WEB: http://www.ncbi.nlm.nih.gov/gene RBL1 retinoblastoma-like 1 5933 RP11-382A12.1 20q11.2 9606 20 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0000278 (EC: TAS); GO_0005515 (EC: IPI, PMID: 1331501); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005667 (EC: IEA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0006351 (EC: TAS); GO_0006367 (EC: TAS); GO_0007179 (EC: TAS); GO_0008134 (EC: IPI, PMID: 16360038); GO_0010467 (EC: TAS); GO_0016032 (EC: IEA); GO_0016568 (EC: IEA); GO_0043550 (EC: IDA, PMID: 16286473); GO_0045944 (EC: TAS); GO_0051726 (EC: IEA) PMID: 1331501; 1532458; 1833063; 7565695; 7739537; 7760804; 7791762; 7892279; 7935440; 7958924; 7958925; 8076603; 8230483; 8319904; 8622916; 8643455; 8657117; 8798463; 8816797; 8832394; 9242374; 9372959; 9464541; 9472014; 9501179; 9566894; 9697699; 9710587; 9721205; 9724724; 9724731; 9747874; 9858615; 9891079; 9927208; 10022926; 10082561; 10330166; 10376528; 10490602; 10540350; 10766737; 10863094; 11034201; 11313936; 11521194; 11571651; 11573202; 11642725; 11780052; 11799066; 11884610; 12006580; 12096339; 12150994; 12434308; 12439743; 12450794; 12466551; 12477932; 12549820; 12588981; 12621062; 12947099; 14555653; 14666683; 14671316; 15467457; 15479636; 15489334; 15631990; 15716956; 15735762; 15750587; 15827088; 15939381; 16135806; 16189514; 16286473; 16360038; 16537896; 16600870; 16620772; 16712791; 16943418; 17255935; 17531812; 17563750; 17620012; 17671431; 18086563; 18418057; 18799622; 19279001; 19453261; 19738611; 20379614; 20453000; 20663872; 21139048; 21900206; 21903422; 21988832; 22094256; 22157815; 22303805; 22673945; 23455922; 23602568; 23853093 retinoblastoma-like 1 Ensembl:ENSG00000080839 HGNC:9893 HPRD:00312 MIM:116957 Vega:OTTHUMG00000032406 Other designations: 107 kDa retinoblastoma-associated protein|cellular protein 107|retinoblastoma-like 1 (p107)|retinoblastoma-like protein 1 RBL1 OGG:3000005970 Bin Zhao, Yue Liu, Oliver He NFKB3 p65 WEB: http://www.ncbi.nlm.nih.gov/gene RELA v-rel avian reticuloendotheliosis viral oncogene homolog A 5970 11q13 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0001889 (EC: IEA); GO_0001942 (EC: IEA); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0003677 (EC: IDA, PMID: 15790681); GO_0003682 (EC: IDA, PMID: 19058135); GO_0003700 (EC: IDA, PMID: 12048232); GO_0003705 (EC: IDA, PMID: 3091258); GO_0005515 (EC: IPI, PMID: 10498867); GO_0005634 (EC: IDA, PMID: 15790681); GO_0005654 (EC: TAS); GO_0005667 (EC: IDA, PMID: 12048232); GO_0005737 (EC: IDA, PMID: 15790681); GO_0005829 (EC: IDA); GO_0005829 (EC: TAS); GO_0006117 (EC: IEA); GO_0006366 (EC: IDA, PMID: 3091258); GO_0006954 (EC: IDA, PMID: 12924514); GO_0006968 (EC: NAS, PMID: 8717528); GO_0007568 (EC: IEA); GO_0008134 (EC: IPI, PMID: 10849440); GO_0008284 (EC: IDA); GO_0009612 (EC: IEA); GO_0009887 (EC: IEA); GO_0010033 (EC: IDA, PMID: 10747850); GO_0010224 (EC: IDA, PMID: 15616591); GO_0014040 (EC: IEA); GO_0016032 (EC: IEA); GO_0019221 (EC: IDA, PMID: 15876188); GO_0019901 (EC: IPI, PMID: 10521409); GO_0031293 (EC: TAS); GO_0031625 (EC: IPI, PMID: 12748188); GO_0032332 (EC: IEA); GO_0032403 (EC: IEA); GO_0032481 (EC: TAS); GO_0032495 (EC: IEA); GO_0032570 (EC: IEA); GO_0032868 (EC: IEA); GO_0033590 (EC: IEA); GO_0033613 (EC: IPI, PMID: 15489227); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035666 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042177 (EC: IEA); GO_0042301 (EC: IDA, PMID: 10521409); GO_0042493 (EC: IEA); GO_0042802 (EC: IDA, PMID: 9437432); GO_0042802 (EC: IPI, PMID: 10498867); GO_0043066 (EC: IDA, PMID: 10747850); GO_0043066 (EC: TAS); GO_0043123 (EC: IEP, PMID: 12761501); GO_0043200 (EC: IEA); GO_0043278 (EC: IEA); GO_0043565 (EC: IEA); GO_0044212 (EC: IDA, PMID: 17350185); GO_0045084 (EC: IEA); GO_0045087 (EC: TAS); GO_0045892 (EC: IDA, PMID: 17350185); GO_0045893 (EC: IDA, PMID: 17350185); GO_0045944 (EC: IDA, PMID: 17350185); GO_0045944 (EC: IMP, PMID: 10660609); GO_0046627 (EC: IEA); GO_0047485 (EC: IPI, PMID: 7739562); GO_0048011 (EC: TAS); GO_0050727 (EC: ISS); GO_0050852 (EC: TAS); GO_0051059 (EC: IPI, PMID: 8441377); GO_0051092 (EC: IDA, PMID: 15790681); GO_0051092 (EC: TAS); GO_0051591 (EC: IEA); GO_0051607 (EC: NAS, PMID: 8717528); GO_0070301 (EC: IDA); GO_0070431 (EC: IDA, PMID: 12527755); GO_0070491 (EC: IPI, PMID: 10660609); GO_0070555 (EC: IGI, PMID: 15489227); GO_0071222 (EC: IEA); GO_0071347 (EC: IDA, PMID: 18073330); GO_0071356 (EC: IDA, PMID: 18073330); GO_0071532 (EC: IEA); GO_2001237 (EC: IMP) PMID: 1493333; 1505523; 1583734; 1732726; 1740106; 2001591; 2006423; 2050119; 3091258; 3140380; 7494249; 7628694; 7651415; 7659084; 7690421; 7706261; 7729429; 7739549; 7739562; 7800480; 7838536; 7859743; 7878004; 7886940; 7907305; 7933095; 8113688; 8139561; 8152812; 8188306; 8207793; 8246997; 8255759; 8281153; 8290595; 8413211; 8423996; 8428580; 8441377; 8543190; 8550813; 8615004; 8626413; 8627654; 8642313; 8649779; 8657102; 8670842; 8676466; 8709193; 8717528; 8724035; 8746784; 8798655; 8816457; 8834464; 8887627; 8887633; 8918464; 8978697; 9057089; 9096323; 9110146; 9150141; 9250404; 9252186; 9278385; 9315679; 9437432; 9468519; 9482849; 9510190; 9525916; 9548485; 9560267; 9566873; 9566883; 9570146; 9572494; 9584164; 9584180; 9659924; 9660950; 9722548; 9724652; 9730685; 9738011; 9751059; 9792375; 9806899; 9837938; 9865693; 9950430; 9990853; 10066434; 10075655; 10207088; 10225209; 10235267; 10336463; 10357819; 10384093; 10393859; 10400814; 10446807; 10480634; 10488148; 10490645; 10498867; 10521409; 10542237; 10542243; 10562553; 10580107; 10644332; 10644726; 10646849; 10660609; 10671224; 10671503; 10723127; 10747850; 10777532; 10777610; 10799874; 10839990; 10847592; 10849440; 10903762; 10928981; 10935546; 10938077; 10958685; 10995388; 11020244; 11044099; 11114727; 11160671; 11231305; 11241736; 11274168; 11278855; 11287411; 11299302; 11313474; 11385624; 11387332; 11395507; 11511100; 11522182; 11526476; 11533489; 11564889; 11567019; 11579140; 11585920; 11590148; 11591705; 11684013; 11704662; 11739381; 11813986; 11827962; 11833470; 11880271; 11922866; 11931769; 11953203; 11964305; 11967310; 11970949; 11971907; 11976329; 11980335; 11983170; 12019209; 12027803; 12040027; 12040437; 12048232; 12052823; 12055073; 12057007; 12067985; 12077347; 12080470; 12134007; 12138131; 12167619; 12173051; 12181450; 12213807; 12244126; 12350227; 12377934; 12393603; 12398897; 12403783; 12419806; 12419817; 12427593; 12429528; 12444202; 12456660; 12473373; 12477932; 12482669; 12485413; 12493764; 12504098; 12509469; 12517770; 12527755; 12540841; 12553906; 12556500; 12559944; 12581153; 12589049; 12606945; 12606947; 12618429; 12618762; 12628924; 12651903; 12665595; 12672800; 12673201; 12690099; 12693954; 12700228; 12707271; 12736262; 12748188; 12761501; 12767057; 12820969; 12829026; 12842894; 12843241; 12881425; 12917431; 12924514; 12972607; 14508515; 14557267; 14560022; 14576841; 14587029; 14593105; 14597638; 14600157; 14600158; 14623898; 14624448; 14645533; 14657027; 14685242; 14688382; 14690596; 14711835; 14716817; 14743216; 14769797; 14966904; 14970236; 15013781; 15016307; 15029197; 15073167; 15073170; 15079071; 15093710; 15125834; 15128824; 15130920; 15140884; 15152190; 15155458; 15167972; 15171256; 15184881; 15192014; 15200413; 15205244; 15226358; 15231833; 15246972; 15256061; 15276183; 15315758; 15355351; 15383283; 15465828; 15484295; 15485901; 15489227; 15494311; 15496460; 15498932; 15499023; 15543947; 15556937; 15599399; 15601829; 15616591; 15616592; 15652748; 15657065; 15657351; 15657437; 15660126; 15671037; 15682491; 15718492; 15735750; 15746428; 15775976; 15790681; 15799966; 15806143; 15845455; 15845545; 15849198; 15876188; 15885892; 15905616; 15913553; 15917220; 15935276; 15975999; 15988014; 16007092; 16009713; 16034126; 16046471; 16052512; 16081638; 16105840; 16135789; 16186799; 16204234; 16214042; 16243805; 16285952; 16291753; 16319923; 16322332; 16329838; 16331275; 16344560; 16382138; 16407283; 16408727; 16410078; 16452207; 16456540; 16477006; 16481475; 16483679; 16497702; 16497732; 16497877; 16498455; 16524505; 16573520; 16584809; 16608838; 16723503; 16728495; 16735506; 16740634; 16785565; 16829531; 16931600; 16940169; 16951195; 16966488; 16982623; 16997282; 16998237; 16998474; 17000776; 17003035; 17003112; 17012367; 17023015; 17031851; 17041012; 17054067; 17070014; 17079333; 17085785; 17136479; 17138826; 17157788; 17158457; 17167080; 17183367; 17196614; 17207971; 17242904; 17255956; 17258784; 17296604; 17301240; 17317104; 17350185; 17353187; 17362989; 17374495; 17403902; 17439942; 17452529; 17468103; 17468759; 17478731; 17493236; 17521736; 17525529; 17530443; 17537731; 17540171; 17586618; 17590503; 17611696; 17612295; 17620405; 17622249; 17626072; 17631635; 17660862; 17661632; 17675239; 17707233; 17708800; 17715045; 17720813; 17785205; 17827154; 17882263; 17889033; 17889859; 17904523; 17911169; 17932106; 17947640; 17956668; 17959673; 17962362; 17962807; 17969521; 17982102; 17986144; 18021261; 18024283; 18025803; 18034190; 18035048; 18036607; 18037904; 18040287; 18045535; 18059344; 18061975; 18073330; 18095109; 18163488; 18163503; 18172215; 18174252; 18178962; 18187620; 18188593; 18201972; 18212740; 18215193; 18215660; 18227347; 18241676; 18249093; 18280497; 18294642; 18314621; 18316612; 18362147; 18362169; 18422166; 18424071; 18424438; 18434448; 18439422; 18461473; 18466468; 18541671; 18550535; 18598236; 18600306; 18607537; 18650421; 18652316; 18660489; 18692180; 18701591; 18703796; 18714023; 18720533; 18779315; 18798274; 18800364; 18823280; 18854154; 18947494; 18952281; 18976975; 18981184; 18983609; 18990707; 18991026; 19019440; 19038492; 19043589; 19046417; 19058135; 19060926; 19064727; 19064995; 19067848; 19087517; 19103749; 19124506; 19124804; 19132086; 19135889; 19140318; 19157506; 19185596; 19197368; 19204000; 19219072; 19262565; 19270718; 19275580; 19275583; 19289499; 19296848; 19300393; 19309400; 19330832; 19339690; 19350539; 19407977; 19422389; 19428110; 19433587; 19448676; 19453840; 19458474; 19483084; 19502777; 19507243; 19520742; 19573080; 19591173; 19591457; 19619938; 19622906; 19654331; 19662361; 19664333; 19683540; 19706600; 19706715; 19706766; 19734210; 19734226; 19746155; 19751727; 19758175; 19764566; 19773279; 19779021; 19789307; 19800042; 19819989; 19860880; 19864627; 19911008; 19912635; 19913121; 19940030; 19955102; 19957349; 20001970; 20020487; 20026048; 20030038; 20032510; 20035271; 20038977; 20048074; 20049872; 20065107; 20080798; 20100341; 20118004; 20124457; 20127516; 20133937; 20139419; 20145242; 20154269; 20160011; 20164172; 20190799; 20194077; 20211864; 20233629; 20237821; 20299548; 20333651; 20346213; 20346360; 20379146; 20380454; 20385564; 20388487; 20388791; 20406971; 20410276; 20421348; 20428758; 20448286; 20457620; 20457835; 20460684; 20462637; 20482821; 20501702; 20514026; 20514451; 20519647; 20538607; 20547752; 20551178; 20562110; 20564628; 20568106; 20568250; 20571344; 20581863; 20585448; 20596086; 20596645; 20617556; 20619728; 20628086; 20639196; 20651843; 20664977; 20672329; 20674992; 20706634; 20729202; 20740673; 20797629; 20861353; 20862798; 20872175; 20936779; 20942234; 20955203; 20957413; 20980497; 21029719; 21030982; 21041296; 21042750; 21042766; 21048031; 21048223; 21056029; 21084693; 21088498; 21131967; 21139048; 21161056; 21165563; 21167650; 21169414; 21187904; 21189284; 21199955; 21211341; 21217772; 21253969; 21262351; 21268019; 21270162; 21278793; 21294676; 21300980; 21310030; 21339307; 21344388; 21364020; 21364927; 21383699; 21395185; 21430048; 21442076; 21451109; 21454528; 21515635; 21518757; 21549062; 21552325; 21576089; 21576359; 21593732; 21598303; 21610149; 21628458; 21660047; 21674474; 21688043; 21697472; 21697760; 21734268; 21742773; 21750107; 21765619; 21771706; 21771876; 21796632; 21803611; 21816815; 21881048; 21884980; 21887328; 21889270; 21900165; 21900206; 21901538; 21903422; 21903858; 21908405; 21918864; 21929290; 21968997; 21976665; 21983014; 21983900; 21988832; 21996578; 21996739; 22008847; 22020940; 22021035; 22022389; 22027781; 22028792; 22038347; 22047608; 22069318; 22081069; 22102084; 22103356; 22105366; 22108531; 22139845; 22141576; 22186294; 22187158; 22196717; 22220474; 22249179; 22261743; 22282354; 22292036; 22302993; 22312446; 22330808; 22334708; 22337883; 22341466; 22390170; 22397926; 22422610; 22480519; 22485186; 22493284; 22496479; 22525504; 22528837; 22535373; 22545750; 22552851; 22558476; 22590978; 22591684; 22592405; 22593190; 22619232; 22634383; 22649547; 22666436; 22670315; 22688014; 22708120; 22709495; 22740410; 22748181; 22763042; 22781898; 22797919; 22804476; 22809882; 22836752; 22842493; 22859938; 22863883; 22892758; 22927901; 22931618; 22948157; 22955280; 22964303; 23027940; 23038213; 23046941; 23053371; 23054188; 23056468; 23069812; 23071666; 23077289; 23083102; 23088768; 23100252; 23115242; 23123196; 23128233; 23134958; 23150684; 23164673; 23195252; 23209664; 23219896; 23238643; 23250430; 23267096; 23269273; 23281696; 23296075; 23318455; 23349803; 23354694; 23454417; 23456480; 23467542; 23482348; 23504993; 23507189; 23510472; 23528368; 23541563; 23543150; 23563313; 23576453; 23576567; 23583404; 23592772; 23603903; 23604637; 23618358; 23624912; 23636254; 23664323; 23708311; 23712703; 23715780; 23716661; 23734002; 23776612; 23797602; 23824799; 23860225; 23874387; 23904475; 23904479; 23940701; 23963448; 23994473; 24012639; 24039253; 24042437; 24067962; 24096876; 24152492; 24175631; 24248593; 24250222; 24260304; 24302727; 24321067; 24457600 v-rel avian reticuloendotheliosis viral oncogene homolog A Ensembl:ENSG00000173039 HGNC:9955 HPRD:01241 MIM:164014 Vega:OTTHUMG00000166566 Other designations: NF-kappa-B p65delta3|nuclear factor NF-kappa-B p65 subunit|nuclear factor of kappa light polypeptide gene enhancer in B-cells 3|transcription factor p65|v-rel reticuloendotheliosis viral oncogene homolog A RELA gene OGG:3000005991 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene RFX3 regulatory factor X, 3 (influences HLA class II expression) 5991 RP11-32F11.1 9p24.2 9606 9 Official from a nomenclature committee GO_0000790 (EC: IDA); GO_0003677 (EC: TAS, PMID: 8600444); GO_0003700 (EC: NAS, PMID: 8600444); GO_0003705 (EC: TAS, PMID: 8289803); GO_0005515 (EC: IPI); GO_0005634 (EC: IC, PMID: 12411430); GO_0005667 (EC: IC); GO_0006355 (EC: ISS); GO_0006366 (EC: TAS, PMID: 8289803); GO_0031018 (EC: ISS); GO_0042384 (EC: ISS); GO_0044212 (EC: IDA); GO_0045892 (EC: IDA, PMID: 12411430); GO_0045893 (EC: IDA); GO_0045944 (EC: ISS); GO_0048469 (EC: ISS); GO_0050796 (EC: ISS); GO_0060285 (EC: ISS); GO_0060287 (EC: ISS); GO_0072560 (EC: IEA); GO_2000078 (EC: ISS) PMID: 8289803; 8600444; 8889548; 10330134; 11682486; 12411430; 12477932; 14702039; 15024578; 15164053; 15489334; 16189514; 16344560; 19671664; 20211142; 21532573; 22415835; 23822649; 24058526 regulatory factor X, 3 (influences HLA class II expression) Other designations: DNA binding protein RFX3|transcription factor RFX3 RFX3 OGG:3000006045 Bin Zhao, Yue Liu, Oliver He BAP-1 BAP1 DING HIPI3 RING1B RING2 WEB: http://www.ncbi.nlm.nih.gov/gene RNF2 ring finger protein 2 6045 GS1-120K12.1 1q25.3 9606 1 Official from a nomenclature committee GO_0000122 (EC: ISS); GO_0000151 (EC: IDA, PMID: 16714294); GO_0000278 (EC: IEA); GO_0001702 (EC: IEA); GO_0001739 (EC: IEA); GO_0003682 (EC: IEA); GO_0004842 (EC: IDA, Qualifier: contributes_to, PMID: 16714294); GO_0005515 (EC: IPI, PMID: 10369680); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0006351 (EC: IEA); GO_0008270 (EC: IDA, PMID: 16714294); GO_0009948 (EC: IEA); GO_0016604 (EC: IEA); GO_0031519 (EC: IDA, PMID: 16943429); GO_0035102 (EC: IDA, PMID: 12167701); GO_0035518 (EC: IDA, PMID: 16943429); GO_0036353 (EC: ISS); GO_0071339 (EC: IDA, PMID: 15960975); GO_0071535 (EC: IPI, PMID: 16714294) PMID: 10369680; 11439343; 11513855; 11865070; 12167161; 12167701; 12183370; 12477932; 12589020; 14702039; 15009096; 15386022; 15489334; 15563468; 15761153; 15773819; 15931389; 15960975; 16169070; 16359901; 16624538; 16710298; 16710414; 16714294; 16751658; 16943429; 17070805; 17081983; 17088979; 17157253; 17379327; 17428788; 17468742; 17873902; 17936708; 18029348; 18051367; 18339675; 18616292; 18629613; 19337376; 19412891; 19549727; 19584075; 19636380; 19690564; 20237291; 20351251; 20601937; 20696397; 20800574; 20811636; 20854876; 21139048; 21179169; 21282530; 21347701; 21530438; 21596310; 21676867; 21772249; 21890473; 22031506; 22042911; 22099309; 22325352; 22427948; 22493164; 22797925; 22844243; 22902369; 22907436; 22910419; 23000965; 23022380; 23105109; 23207902; 23251661; 23318437; 23319651; 23383273; 23395003; 23455922; 23500468; 23671107; 23712474; 24163370; 24457600; 24614341 ring finger protein 2 Ensembl:ENSG00000121481 HGNC:10061 HPRD:07028 MIM:608985 Vega:OTTHUMG00000035391 Other designations: E3 ubiquitin-protein ligase RING2|HIP2-interacting protein 3|RING finger protein 1B|RING finger protein BAP-1|huntingtin-interacting protein 2-interacting protein 3|protein DinG RNF2 OGG:3000006046 Bin Zhao, Yue Liu, Oliver He D6S113E FSH FSRG1 NAT RING3 RNF3 WEB: http://www.ncbi.nlm.nih.gov/gene BRD2 bromodomain containing 2 6046 DADB-17J1.3 6p21.3 9606 6 Official from a nomenclature committee GO_0003682 (EC: IDA, PMID: 18406326); GO_0005515 (EC: IPI); GO_0005634 (EC: IEA); GO_0005737 (EC: IEA); GO_0006334 (EC: IMP, PMID: 18406326); GO_0006351 (EC: IEA); GO_0006357 (EC: IDA, PMID: 18406326); GO_0007283 (EC: TAS, PMID: 9693039); GO_0016568 (EC: IEA); GO_0070577 (EC: IDA, PMID: 18406326) PMID: 1350857; 1352711; 1663500; 8595877; 8781126; 9373153; 9693039; 10934046; 10965846; 11502199; 11983150; 12145330; 12366783; 12477932; 12600283; 12830434; 14563639; 14574404; 14702039; 14731392; 15146197; 15302935; 15342556; 15489334; 15548137; 15949438; 16344560; 16512664; 16516380; 16786191; 16940503; 17081983; 17111193; 17148447; 17166848; 17848202; 17999746; 18406326; 19204726; 19322201; 19454010; 19766566; 19851445; 19953286; 20036832; 20048151; 20587610; 20709061; 20811636; 21139048; 21608014; 22035730; 22766109; 23115324; 23255218; 23455922; 23756480; 24049186; 24250222 bromodomain containing 2 Ensembl:ENSG00000204256 HGNC:1103 HPRD:03326 MIM:601540 Vega:OTTHUMG00000031241 Other designations: O27.1.1|bromodomain-containing 2|bromodomain-containing protein 2|female sterile homeotic-related gene 1|really interesting new gene 3 protein BRD2 OGG:3000006093 Bin Zhao, Yue Liu, Oliver He P160ROCK ROCK-I WEB: http://www.ncbi.nlm.nih.gov/gene ROCK1 Rho-associated, coiled-coil containing protein kinase 1 6093 18q11.1 9606 18 Official from a nomenclature committee GO_0000139 (EC: IEA); GO_0001726 (EC: ISS); GO_0003383 (EC: IEA); GO_0004672 (EC: TAS, PMID: 10436159); GO_0004674 (EC: IDA, PMID: 10652353); GO_0005515 (EC: IPI, PMID: 10652353); GO_0005524 (EC: IEA); GO_0005814 (EC: IEA); GO_0005829 (EC: TAS); GO_0005856 (EC: ISS); GO_0005886 (EC: ISS); GO_0006468 (EC: TAS, PMID: 10436159); GO_0006915 (EC: TAS); GO_0006921 (EC: TAS); GO_0006939 (EC: TAS, PMID: 12778124); GO_0007159 (EC: IDA, PMID: 12082081); GO_0007165 (EC: TAS, PMID: 10436159); GO_0007266 (EC: TAS, PMID: 8798490); GO_0007411 (EC: TAS); GO_0016525 (EC: IMP, PMID: 19181962); GO_0017048 (EC: IEA); GO_0022614 (EC: IDA, PMID: 12082081); GO_0030027 (EC: ISS); GO_0030036 (EC: IEA); GO_0030155 (EC: TAS, PMID: 12778124); GO_0032059 (EC: IEA); GO_0032060 (EC: IEA); GO_0032956 (EC: TAS, PMID: 12778124); GO_0043524 (EC: IEA); GO_0045616 (EC: IMP, PMID: 19997641); GO_0046872 (EC: IEA); GO_0050900 (EC: IDA, PMID: 12082081); GO_0050901 (EC: IDA, PMID: 12082081); GO_0051451 (EC: ISS); GO_0051492 (EC: TAS, PMID: 12778124); GO_0051893 (EC: TAS, PMID: 12778124); GO_0051894 (EC: ISS); GO_2000114 (EC: TAS); GO_2000145 (EC: TAS, PMID: 12778124) PMID: 2114109; 2155236; 7822264; 8617235; 8798490; 8816443; 9099667; 9354661; 9456324; 9516463; 9565595; 9722579; 9856983; 10209029; 10436159; 10508479; 10559936; 10574968; 10579722; 10601309; 10652353; 10818093; 10970850; 11018042; 11283607; 11340065; 11387207; 11739394; 11751986; 11818523; 11893932; 11931630; 11992112; 12034773; 12082081; 12177195; 12193698; 12220642; 12477932; 12482610; 12563012; 12600888; 12729902; 12748184; 12749591; 12773565; 12778124; 12850840; 14517206; 14610060; 14657354; 14660612; 14702039; 14716844; 14718574; 14962675; 15044207; 15096506; 15208091; 15231748; 15247219; 15252450; 15494373; 15611088; 15647781; 15665056; 15713824; 15723050; 15793569; 15797222; 15843433; 15855233; 15910744; 15956119; 16123592; 16141422; 16249185; 16344560; 16371346; 16407310; 16413470; 16543245; 16687572; 16712513; 16760434; 16772336; 16784244; 16825579; 16862148; 16891369; 16978606; 16983089; 17012370; 17028776; 17044646; 17138966; 17167780; 17172270; 17174923; 17244674; 17344417; 17346310; 17572668; 17620599; 17643375; 17651694; 17673200; 17728102; 17853893; 17855350; 18079197; 18187541; 18204440; 18239683; 18331468; 18353901; 18396681; 18477564; 18495812; 18499753; 18615591; 18648664; 18668558; 18684864; 18694941; 18695890; 18713748; 18723680; 18780293; 18852895; 18922892; 18941185; 18946488; 18948190; 18952846; 19001122; 19036714; 19131646; 19160018; 19167712; 19181962; 19403695; 19404162; 19406912; 19420982; 19549780; 19573309; 19590140; 19667069; 19913121; 19997641; 20039424; 20053635; 20056178; 20056645; 20064505; 20068229; 20070312; 20126978; 20130732; 20140017; 20223287; 20364104; 20379197; 20558775; 20682776; 20734064; 20801872; 20801873; 21035804; 21048031; 21051874; 21085597; 21119662; 21139048; 21206971; 21265091; 21305317; 21387396; 21417762; 21423810; 21445309; 21575520; 21739156; 21747168; 21840487; 21847509; 21906983; 21907926; 21908715; 21986457; 21994419; 22010828; 22031287; 22041269; 22085929; 22155728; 22197032; 22206673; 22232555; 22262769; 22328514; 22348083; 22363817; 22462535; 22493320; 22558309; 22563075; 22584506; 22798677; 22813839; 22846914; 22863883; 22913419; 22942252; 22975682; 22986902; 23022380; 23066013; 23094262; 23097497; 23168335; 23184937; 23188716; 23233531; 23328676; 23350987; 23355470; 23479079; 23602568; 23615712; 23665024; 23670799; 23720748; 23726972; 23775364; 23782575; 23789633; 23828571; 23872151; 23877263; 23936026; 24019071; 24149105; 24240172; 24250222; 24297045; 24324133 Rho-associated, coiled-coil containing protein kinase 1 HGNC:10251 HPRD:03414 MIM:601702 Other designations: Rho kinase|p160 ROCK-1|p160-ROCK|renal carcinoma antigen NY-REN-35|rho-associated protein kinase 1|rho-associated, coiled-coil-containing protein kinase 1|rho-associated, coiled-coil-containing protein kinase I ROCK1 OGG:3000006235 Bin Zhao, Yue Liu, Oliver He S29 WEB: http://www.ncbi.nlm.nih.gov/gene RPS29 ribosomal protein S29 6235 14q 20140408 9606 14 protein-coding Official from a nomenclature committee GO_0000184 (EC: TAS); GO_0003735 (EC: IDA, PMID: 15883184); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006412 (EC: IC, PMID: 15883184); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0006414 (EC: TAS); GO_0006415 (EC: TAS); GO_0006614 (EC: TAS); GO_0008270 (EC: IDA, PMID: 8781548); GO_0010467 (EC: TAS); GO_0015935 (EC: IDA, PMID: 15883184); GO_0016032 (EC: TAS); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0019058 (EC: TAS); GO_0019083 (EC: TAS); GO_0022627 (EC: IDA, PMID: 15883184); GO_0044267 (EC: TAS); GO_0070062 (EC: IDA) PMID: 7772601; 8706699; 8722009; 8781548; 9582194; 10708601; 11751223; 11875025; 12477932; 12588972; 12625830; 15189156; 15489334; 15883184; 16196087; 17353931; 18029348; 21890473; 21906983; 21988832; 22589738; 22863883; 22939629; 23000965; 23455922; 23726511; 24250222 ribosomal protein S29 Ensembl:ENSG00000213741 HGNC:10419 HPRD:04698 MIM:603633 Vega:OTTHUMG00000140272 Other designations: 40S ribosomal protein S29 RPS29 OGG:3000006319 Bin Zhao, Yue Liu, Oliver He FADS5 MSTP008 SCD1 SCDOS WEB: http://www.ncbi.nlm.nih.gov/gene SCD stearoyl-CoA desaturase (delta-9-desaturase) 6319 PRO1933 10q24.31 9606 10 Official from a nomenclature committee GO_0004768 (EC: IEA); GO_0005506 (EC: IEA); GO_0005783 (EC: IDA); GO_0005789 (EC: IEA); GO_0006633 (EC: IEA); GO_0016021 (EC: IEA) PMID: 21148; 6102994; 7909540; 8125298; 9362069; 10229681; 10922050; 11181995; 11397803; 11415448; 11677241; 12061775; 12401889; 12477932; 14683458; 14967817; 14967823; 15164054; 15489334; 15609334; 15610069; 15662557; 15708362; 15851470; 15855323; 15907797; 16213227; 16385451; 16723740; 17614770; 17636091; 17852835; 18029348; 18030445; 18286258; 18340007; 18499418; 18660489; 18697866; 18781797; 18813799; 18832746; 18952834; 19130493; 19154947; 19322201; 19478146; 19710915; 19913121; 19953087; 20032470; 20395685; 20565855; 20579763; 20599700; 20628086; 20639865; 20713121; 21045174; 21060977; 21139048; 21179554; 21331774; 21544602; 21658928; 21674150; 21775116; 21831035; 21832049; 21886157; 21890473; 21898701; 21906983; 21963094; 21987572; 22026420; 22046234; 22049297; 22082156; 22209225; 22457791; 22505724; 22819528; 22946088; 23000965; 23013158; 23015656; 23019225; 23139775; 23208590; 23221600; 23331615; 23362303; 23455922; 23613812; 23633458; 24135379; 24357007 stearoyl-CoA desaturase (delta-9-desaturase) Ensembl:ENSG00000099194 HGNC:10571 HPRD:04941 MIM:604031 Vega:OTTHUMG00000018906 Other designations: acyl-CoA desaturase|delta(9)-desaturase|delta-9 desaturase|delta-9-desaturase|fatty acid desaturase|predicted protein of HQ0998|stearoyl-CoA desaturase opposite strand SCD OGG:3000006341 Bin Zhao, Yue Liu, Oliver He SCOD1 WEB: http://www.ncbi.nlm.nih.gov/gene SCO1 SCO1 cytochrome c oxidase assembly protein 6341 17p13.1 9606 17 Official from a nomenclature committee GO_0005507 (EC: IEA); GO_0005739 (EC: TAS, PMID: 9878253); GO_0005743 (EC: IEA); GO_0006091 (EC: TAS, PMID: 9878253); GO_0006825 (EC: IEA); GO_0006878 (EC: IEA); GO_0008535 (EC: IEA); GO_0030016 (EC: IDA) PMID: 2543907; 2835635; 8619474; 8889548; 9110174; 9878253; 10218584; 10545952; 11013136; 11027508; 11579424; 12477932; 15229189; 15489334; 15659396; 16091356; 16344560; 16520371; 16735468; 17189203; 18458339; 19295170; 19336478; 19465909; 19913121; 20628086; 20864674; 20877624; 21139048; 21890473; 23345593; 24068947 SCO1 cytochrome c oxidase assembly protein Ensembl:ENSG00000133028 HGNC:10603 HPRD:04705 MIM:603644 Vega:OTTHUMG00000130364 Other designations: SCO cytochrome oxidase deficient homolog 1|protein SCO1 homolog, mitochondrial SCO1 OGG:3000006347 Bin Zhao, Yue Liu, Oliver He GDCF-2 HC11 HSMCR30 MCAF MCP-1 MCP1 SCYA2 SMC-CF WEB: http://www.ncbi.nlm.nih.gov/gene CCL2 chemokine (C-C motif) ligand 2 6347 17q11.2-q12 9606 17 Official from a nomenclature committee GO_0000165 (EC: IMP); GO_0001525 (EC: TAS, PMID: 18334747); GO_0001666 (EC: IEA); GO_0001938 (EC: IEA); GO_0002548 (EC: IDA, PMID: 12207323); GO_0004672 (EC: TAS, PMID: 9973507); GO_0005102 (EC: TAS, PMID: 10542238); GO_0005576 (EC: IDA); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0005737 (EC: IEA); GO_0006468 (EC: TAS, PMID: 9670957); GO_0006874 (EC: IEA); GO_0006935 (EC: TAS, PMID: 10623817); GO_0006954 (EC: IDA); GO_0006959 (EC: TAS, PMID: 9548499); GO_0006987 (EC: TAS); GO_0007010 (EC: IDA, PMID: 10072545); GO_0007155 (EC: TAS, PMID: 10198043); GO_0007165 (EC: NAS, PMID: 10770925); GO_0007166 (EC: TAS, PMID: 9548499); GO_0007179 (EC: IEA); GO_0007186 (EC: TAS, PMID: 10542238); GO_0007187 (EC: TAS, PMID: 10770925); GO_0007259 (EC: TAS, PMID: 9670957); GO_0007568 (EC: IEA); GO_0008009 (EC: IEA); GO_0008201 (EC: IEA); GO_0008360 (EC: IDA, PMID: 10072545); GO_0009408 (EC: IEA); GO_0009612 (EC: IEA); GO_0009617 (EC: IEP, PMID: 16034137); GO_0009887 (EC: TAS, PMID: 9364936); GO_0010332 (EC: IEA); GO_0010574 (EC: IEA); GO_0010759 (EC: IEA); GO_0014823 (EC: IEA); GO_0016525 (EC: IEA); GO_0019079 (EC: TAS, PMID: 10985244); GO_0019221 (EC: IDA, PMID: 12207323); GO_0019725 (EC: TAS, PMID: 18334747); GO_0030593 (EC: IEA); GO_0030968 (EC: TAS); GO_0031100 (EC: IEA); GO_0031663 (EC: IDA); GO_0031727 (EC: ISS); GO_0031727 (EC: TAS, PMID: 18021937); GO_0032570 (EC: IEA); GO_0033552 (EC: IEA); GO_0034351 (EC: IDA, PMID: 12753088); GO_0035684 (EC: ISS); GO_0042493 (EC: IEA); GO_0043025 (EC: IEA); GO_0043200 (EC: IEA); GO_0043491 (EC: IMP); GO_0043524 (EC: IDA, PMID: 12753088); GO_0043615 (EC: IDA, PMID: 12271471); GO_0044267 (EC: TAS); GO_0044344 (EC: IEP, PMID: 9407497); GO_0045471 (EC: IEA); GO_0046677 (EC: IEA); GO_0048010 (EC: IEA); GO_0048246 (EC: IDA, PMID: 12207323); GO_0048247 (EC: IEA); GO_0050806 (EC: IEA); GO_0050870 (EC: ISS); GO_0051384 (EC: IEA); GO_0051770 (EC: ISS); GO_0060137 (EC: IEA); GO_0070098 (EC: IEA); GO_0071222 (EC: ISS); GO_0071346 (EC: IEP, PMID: 9407497); GO_0071346 (EC: ISS); GO_0071347 (EC: IEP, PMID: 9407497); GO_0071347 (EC: ISS); GO_0071356 (EC: IEP, PMID: 9407497); GO_0071356 (EC: ISS); GO_0071407 (EC: IDA); GO_0090265 (EC: IEA); GO_2000427 (EC: ISS); GO_2000502 (EC: IDA, PMID: 7545673) PMID: 1661560; 1857712; 2004761; 2071154; 2322286; 2357211; 2465924; 2501656; 2513477; 2518726; 2648385; 2923622; 7545673; 7651403; 8051410; 8107690; 8195247; 8627182; 8631787; 8639605; 8642344; 8898111; 8989326; 9287323; 9364936; 9405404; 9407497; 9501225; 9548499; 9558113; 9670957; 9789057; 9792375; 9792674; 9837883; 9973507; 10068657; 10072545; 10198043; 10453044; 10477718; 10529171; 10542238; 10587439; 10623817; 10644332; 10706668; 10734104; 10751368; 10770925; 10918580; 10982368; 10985244; 11083865; 11145723; 11154208; 11313374; 11350939; 11500196; 11544456; 11750041; 11751881; 11776402; 11844145; 11878903; 11912219; 11929421; 11989790; 11999660; 12009356; 12022754; 12067898; 12078856; 12082252; 12089333; 12093796; 12117737; 12127997; 12149192; 12183528; 12186702; 12195705; 12204371; 12207323; 12234797; 12239249; 12271471; 12351486; 12358851; 12372466; 12374865; 12391099; 12391196; 12393171; 12397639; 12399623; 12408680; 12410798; 12413001; 12419245; 12443832; 12460032; 12462338; 12470469; 12473373; 12477932; 12485413; 12488502; 12505750; 12520153; 12520365; 12540965; 12632067; 12651071; 12665582; 12724308; 12753088; 12758167; 12787135; 12805068; 12826189; 12826377; 12846738; 12904997; 12944979; 12946945; 12957789; 12960255; 13679391; 14517168; 14517792; 14550782; 14571188; 14576080; 14597108; 14602575; 14620921; 14647058; 14651522; 14660607; 14687706; 14733721; 14767014; 15005768; 15016614; 15022320; 15033992; 15034225; 15041705; 15067078; 15077296; 15081318; 15082170; 15110609; 15115316; 15123743; 15135805; 15167690; 15188361; 15191525; 15191888; 15191916; 15194470; 15203564; 15226634; 15257681; 15280531; 15288699; 15296827; 15302103; 15308783; 15312962; 15349727; 15389752; 15466648; 15468376; 15481145; 15488313; 15489334; 15492853; 15529362; 15545821; 15579297; 15599324; 15602730; 15607028; 15611878; 15627719; 15630704; 15654958; 15677312; 15722361; 15740484; 15745922; 15780578; 15832427; 15848524; 15866653; 15880317; 15883814; 15900302; 15919935; 15976326; 15979992; 16003740; 16004967; 16009177; 16009638; 16020745; 16034137; 16050950; 16078996; 16095529; 16105652; 16116069; 16129702; 16160188; 16164699; 16195477; 16204411; 16206161; 16206198; 16213182; 16214031; 16230097; 16249002; 16278381; 16280328; 16280979; 16307829; 16309586; 16318581; 16351713; 16352737; 16356504; 16358960; 16359995; 16362156; 16397773; 16415174; 16427785; 16436595; 16439461; 16439481; 16439891; 16445900; 16474202; 16479072; 16504689; 16516290; 16518346; 16524739; 16597919; 16609683; 16631114; 16636247; 16636603; 16672419; 16697212; 16697654; 16697675; 16705739; 16712788; 16719905; 16730843; 16733654; 16741188; 16750572; 16751386; 16781696; 16795034; 16802342; 16804844; 16814297; 16825597; 16828028; 16835702; 16867220; 16872505; 16873204; 16903979; 16934270; 16939660; 16980310; 16988194; 16997300; 17008880; 17032917; 17046994; 17052731; 17062130; 17065190; 17082648; 17091019; 17098977; 17138827; 17169533; 17187019; 17202846; 17207568; 17218539; 17262819; 17280738; 17283105; 17284607; 17307163; 17322498; 17364892; 17376903; 17379849; 17384985; 17390372; 17395051; 17404035; 17407231; 17416748; 17417600; 17424890; 17426779; 17431224; 17458901; 17465499; 17485071; 17486299; 17490777; 17495598; 17522215; 17525255; 17530707; 17582674; 17596666; 17625600; 17694504; 17700210; 17703277; 17703412; 17704101; 17706208; 17707134; 17728497; 17763208; 17767550; 17804911; 17822317; 17884268; 17886678; 17917677; 17920586; 17922439; 17928143; 17934860; 17940904; 17943082; 17949278; 17968528; 17968796; 17975143; 17977907; 17982227; 18021937; 18022660; 18032547; 18040846; 18042260; 18055544; 18060801; 18061474; 18069114; 18069417; 18070228; 18074388; 18089573; 18093183; 18093816; 18158188; 18164957; 18172114; 18186797; 18190912; 18191726; 18203956; 18205260; 18208975; 18230355; 18242157; 18266131; 18266972; 18270300; 18271757; 18272603; 18274642; 18276775; 18284633; 18310503; 18314120; 18334747; 18347511; 18371304; 18373164; 18381789; 18395486; 18395775; 18402383; 18436581; 18439751; 18443042; 18458846; 18469140; 18495743; 18506929; 18508485; 18515987; 18521742; 18522702; 18525219; 18528529; 18570214; 18611860; 18615095; 18619701; 18623207; 18636124; 18637012; 18646053; 18651322; 18656701; 18660381; 18660489; 18665050; 18678243; 18684531; 18690522; 18702087; 18702954; 18710415; 18718072; 18758234; 18762729; 18784079; 18790652; 18804983; 18808740; 18818748; 18824549; 18829011; 18837094; 18855195; 18937353; 18940815; 18953909; 18954908; 18962899; 18976655; 18976766; 18977211; 18996102; 18996288; 19001328; 19002595; 19009499; 19014891; 19017462; 19019335; 19020833; 19032843; 19032844; 19032966; 19034671; 19048368; 19055601; 19072670; 19074885; 19092169; 19099590; 19099689; 19100389; 19115220; 19132243; 19136823; 19147409; 19148342; 19152916; 19154405; 19155472; 19156168; 19166999; 19167353; 19168721; 19170716; 19176388; 19185603; 19187096; 19211266; 19215923; 19218821; 19228389; 19233564; 19234509; 19242604; 19247692; 19247801; 19258635; 19258923; 19267279; 19277984; 19281798; 19287949; 19288202; 19298002; 19317061; 19327225; 19328242; 19332042; 19347053; 19357773; 19360344; 19361458; 19364494; 19371341; 19373627; 19376162; 19379593; 19392835; 19409809; 19411748; 19420105; 19423540; 19426980; 19439012; 19441883; 19441886; 19443842; 19446037; 19450143; 19458908; 19465691; 19479998; 19494437; 19496969; 19506371; 19524871; 19525388; 19525846; 19526283; 19527514; 19555664; 19558503; 19565503; 19573434; 19576791; 19587356; 19587833; 19625220; 19628738; 19632522; 19639050; 19641159; 19642141; 19642908; 19644155; 19646633; 19658300; 19664934; 19668598; 19706805; 19711822; 19720836; 19726280; 19729601; 19736361; 19755790; 19755933; 19760754; 19773451; 19777601; 19781192; 19781803; 19782713; 19819989; 19822078; 19828696; 19833726; 19844201; 19851831; 19864434; 19865101; 19866475; 19881959; 19885629; 19893256; 19902472; 19904283; 19906815; 19913121; 19923858; 19926874; 19929093; 19938194; 19941075; 19942750; 19948975; 19957783; 19995900; 20000039; 20004457; 20016208; 20029197; 20029451; 20031554; 20038977; 20040767; 20041183; 20056091; 20056178; 20087947; 20097750; 20100200; 20102417; 20111728; 20121167; 20125127; 20137666; 20138641; 20140679; 20177146; 20179890; 20187772; 20193755; 20196868; 20221866; 20228199; 20231199; 20237358; 20237496; 20299238; 20299783; 20339010; 20339966; 20349326; 20351714; 20364004; 20368224; 20370601; 20374368; 20389059; 20406462; 20406964; 20414371; 20416077; 20423879; 20430117; 20431065; 20432237; 20437404; 20438785; 20442634; 20446021; 20449800; 20449809; 20451256; 20452482; 20484496; 20485444; 20488574; 20497022; 20503287; 20504881; 20523065; 20526368; 20531015; 20540976; 20546673; 20563852; 20570966; 20573518; 20576301; 20602615; 20605053; 20607592; 20610178; 20617559; 20625355; 20628086; 20634732; 20637631; 20650649; 20673868; 20677014; 20681057; 20692455; 20725607; 20726788; 20737475; 20811626; 20818133; 20825374; 20859200; 20861640; 20880493; 20934684; 20947712; 20950459; 20960176; 20962626; 20965747; 21033620; 21037509; 21072187; 21073393; 21087336; 21097527; 21102463; 21107756; 21114970; 21134984; 21135144; 21148795; 21181544; 21183736; 21187454; 21190865; 21199725; 21220697; 21224075; 21247529; 21251883; 21264298; 21264360; 21327296; 21328336; 21354997; 21361908; 21368227; 21376205; 21383955; 21384169; 21385934; 21397653; 21401388; 21413027; 21423810; 21447688; 21450101; 21486440; 21486949; 21504590; 21527853; 21529268; 21529952; 21532752; 21551367; 21556333; 21569455; 21574823; 21610567; 21615418; 21620438; 21627744; 21654748; 21691937; 21701898; 21726903; 21734368; 21744268; 21760952; 21774078; 21787749; 21799302; 21851000; 21855541; 21858104; 21859809; 21868018; 21868706; 21883707; 21890375; 21898402; 21900689; 21906274; 21910857; 21920519; 21924076; 21930770; 21951843; 21951854; 21961038; 21975431; 21991356; 21992868; 22026334; 22037282; 22037980; 22059352; 22081934; 22117412; 22117820; 22125641; 22131127; 22132892; 22138288; 22142522; 22147846; 22152380; 22159219; 22183310; 22197827; 22203484; 22210436; 22226505; 22240432; 22265030; 22276574; 22288595; 22300682; 22301094; 22303443; 22319587; 22319627; 22321225; 22362506; 22377751; 22378888; 22381103; 22384203; 22396538; 22412388; 22420243; 22422499; 22425139; 22427564; 22448134; 22466290; 22472119; 22476561; 22484917; 22487967; 22490648; 22493691; 22541401; 22543850; 22554651; 22558273; 22612293; 22617682; 22619484; 22641100; 22664781; 22669976; 22691208; 22694757; 22697070; 22707193; 22711527; 22721162; 22729037; 22733495; 22739041; 22750227; 22752804; 22759858; 22762377; 22763298; 22766373; 22815949; 22823210; 22848642; 22857869; 22859936; 22861370; 22868806; 22927430; 22942263; 22961048; 22980664; 22981148; 22985557; 22989614; 22992722; 23007133; 23017229; 23037589; 23039889; 23069648; 23090289; 23128233; 23135705; 23143679; 23151275; 23154550; 23160182; 23161207; 23166687; 23180368; 23185481; 23185512; 23192155; 23206327; 23211090; 23224211; 23255244; 23274856; 23300810; 23303452; 23349788; 23350010; 23352833; 23375122; 23383162; 23402987; 23408426; 23416968; 23418647; 23429817; 23434371; 23454776; 23474119; 23490412; 23529020; 23542734; 23548612; 23549806; 23555755; 23557387; 23559389; 23583295; 23629827; 23657965; 23686489; 23704830; 23712703; 23762283; 23770363; 23782302; 23816715; 23831464; 23845726; 23886148; 23887394; 23890452; 23939977; 23954399; 23982944; 23999007; 24058270; 24077340; 24078580; 24260304; 24273921 chemokine (C-C motif) ligand 2 Ensembl:ENSG00000108691 HGNC:10618 HPRD:01149 MIM:158105 Vega:OTTHUMG00000132887 Other designations: C-C motif chemokine 2|monocyte chemoattractant protein 1|monocyte chemoattractant protein-1|monocyte chemotactic and activating factor|monocyte chemotactic protein 1|monocyte secretory protein JE|small inducible cytokine A2 (monocyte chemotactic protein 1, homologous to mouse Sig-je)|small inducible cytokine subfamily A (Cys-Cys), member 2|small-inducible cytokine A2 CCL2 OGG:3000006348 Bin Zhao, Yue Liu, Oliver He G0S19-1 LD78ALPHA MIP-1-alpha MIP1A SCYA3 WEB: http://www.ncbi.nlm.nih.gov/gene CCL3 chemokine (C-C motif) ligand 3 6348 17q12 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0000165 (EC: IEP, PMID: 12032188); GO_0000165 (EC: IMP); GO_0001649 (EC: IEP); GO_0001775 (EC: IDA, PMID: 10706735); GO_0002548 (EC: IC, PMID: 10660125); GO_0002548 (EC: IDA, PMID: 10706735); GO_0004672 (EC: IDA, PMID: 10734056); GO_0004698 (EC: IDA, PMID: 15764707); GO_0005515 (EC: IPI); GO_0005576 (EC: IDA); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA); GO_0005622 (EC: IDA, PMID: 10072545); GO_0005737 (EC: IDA); GO_0005829 (EC: IDA, PMID: 19523456); GO_0006468 (EC: IDA, PMID: 10734056); GO_0006816 (EC: IDA, PMID: 10734056); GO_0006874 (EC: IDA, PMID: 10072545); GO_0006887 (EC: IDA, PMID: 10734056); GO_0006935 (EC: IDA, PMID: 10679098); GO_0006954 (EC: IDA, PMID: 10679098); GO_0007010 (EC: IDA, PMID: 10072545); GO_0007267 (EC: IDA, PMID: 10679098); GO_0007610 (EC: IDA); GO_0008009 (EC: IDA, PMID: 10072545); GO_0008360 (EC: IDA, PMID: 10072545); GO_0009636 (EC: IDA, PMID: 10841574); GO_0010628 (EC: IDA, PMID: 10706735); GO_0010629 (EC: IDA); GO_0010818 (EC: IDA, PMID: 10706735); GO_0014808 (EC: IDA, PMID: 19523456); GO_0016004 (EC: IDA, PMID: 10734056); GO_0016301 (EC: IDA); GO_0019722 (EC: IDA, PMID: 10072545); GO_0023052 (EC: IEP, PMID: 12032188); GO_0030335 (EC: IDA, PMID: 10706735); GO_0030502 (EC: IDA); GO_0030593 (EC: IDA, PMID: 10706735); GO_0031663 (EC: IDA); GO_0031726 (EC: IPI, PMID: 10660125); GO_0031730 (EC: IPI, PMID: 10679098); GO_0032760 (EC: ISS); GO_0042056 (EC: IDA, PMID: 10072545); GO_0042802 (EC: IPI); GO_0043085 (EC: IDA, PMID: 10734056); GO_0043308 (EC: IDA, PMID: 10706735); GO_0043491 (EC: IMP); GO_0043525 (EC: ISS); GO_0043615 (EC: ISS); GO_0043922 (EC: IDA, PMID: 10841574); GO_0045671 (EC: IDA); GO_0048245 (EC: IDA, PMID: 10072545); GO_0048246 (EC: ISS); GO_0048247 (EC: IDA, PMID: 10706735); GO_0050718 (EC: ISS); GO_0050729 (EC: ISS); GO_0050850 (EC: IMP, PMID: 10679098); GO_0050918 (EC: IDA, PMID: 10072545); GO_0051897 (EC: IEP); GO_0051928 (EC: IDA, PMID: 15764707); GO_0051930 (EC: IDA, PMID: 15764707); GO_0070374 (EC: IDA); GO_0070723 (EC: IDA, PMID: 19523456); GO_0071346 (EC: IEP, PMID: 9407497); GO_0071347 (EC: IEP, PMID: 9407497); GO_0071356 (EC: IEP, PMID: 9407497); GO_0071407 (EC: IDA); GO_0071621 (EC: IDA, PMID: 10706735); GO_2000503 (EC: IDA, PMID: 7545673) PMID: 1004873; 1296815; 1694014; 1972563; 2271120; 2521882; 3058856; 3086300; 3279154; 7537510; 7545673; 7594543; 7695626; 8077676; 8460127; 8525373; 8541527; 8568261; 8573157; 8613703; 8687429; 8699119; 8898753; 8906795; 9092555; 9175116; 9207199; 9359702; 9366434; 9405404; 9407497; 9420238; 9520456; 9576751; 9653130; 9658081; 9885903; 9973507; 10072545; 10089882; 10198043; 10201982; 10202040; 10347159; 10446313; 10470075; 10477718; 10490959; 10602409; 10644351; 10660125; 10679098; 10706735; 10734056; 10751368; 10820198; 10841574; 10843431; 10857861; 10964543; 10985253; 11023526; 11086082; 11278300; 11461120; 11602715; 11700073; 11751963; 11861262; 12032188; 12070155; 12089333; 12186702; 12200385; 12218153; 12370346; 12370381; 12377943; 12393595; 12393716; 12401480; 12408680; 12413001; 12445801; 12447751; 12477932; 12506012; 12543931; 12560229; 12574335; 12603824; 12651610; 12651617; 12771199; 12960275; 14680814; 14733721; 15001559; 15067078; 15077296; 15142381; 15481145; 15489334; 15531890; 15585099; 15588341; 15602730; 15638726; 15728180; 15764707; 15780175; 15817944; 16160188; 16234357; 16354571; 16379602; 16393999; 16427155; 16439481; 16507178; 16697675; 16712957; 16849642; 17005260; 17270460; 17330138; 17357337; 17572013; 17625600; 17656823; 17765942; 17914560; 18070228; 18076643; 18164590; 18196935; 18242850; 18346864; 18559339; 18619972; 18678243; 18689282; 18762952; 18802359; 18818748; 18945465; 18991615; 19019335; 19055602; 19074730; 19234184; 19436054; 19463769; 19494336; 19523456; 19527514; 19587705; 19841187; 19917679; 20015995; 20041127; 20042585; 20056178; 20124101; 20368576; 20380698; 20403075; 20420712; 20482449; 20518837; 20650649; 20702408; 20725607; 20817073; 20959807; 21030011; 21082024; 21115978; 21118814; 21368236; 21403648; 21756796; 21784977; 21890375; 22042700; 22085486; 22118025; 22146622; 22156348; 22187158; 22295852; 22307528; 22407921; 22691208; 22727097; 22987449; 23029252; 23151487; 23152559; 23223135; 23233369; 23295355; 23334651; 23711864; 23760235; 23818986; 24047437; 24116893; 24370436 chemokine (C-C motif) ligand 3 Ensembl:ENSG00000006075 HGNC:10627 HPRD:01656 MIM:182283 Vega:OTTHUMG00000133000 Other designations: C-C motif chemokine 3|G0/G1 switch regulatory protein 19-1|PAT 464.1|SIS-beta|macrophage inflammatory protein 1-alpha|small inducible cytokine A3 (homologous to mouse Mip-1a)|tonsillar lymphocyte LD78 alpha protein CCL3 OGG:3000006352 Bin Zhao, Yue Liu, Oliver He D17S136E RANTES SCYA5 SIS-delta SISd TCP228 eoCP WEB: http://www.ncbi.nlm.nih.gov/gene CCL5 chemokine (C-C motif) ligand 5 6352 17q12 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0000165 (EC: IMP); GO_0002407 (EC: TAS, PMID: 18337562); GO_0002548 (EC: IC, PMID: 10660125); GO_0002676 (EC: TAS, PMID: 10488085); GO_0004435 (EC: IDA, PMID: 10734056); GO_0004672 (EC: IDA, PMID: 10734056); GO_0005515 (EC: IPI); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0005737 (EC: IEA); GO_0006468 (EC: IDA, PMID: 10734056); GO_0006816 (EC: IDA, PMID: 10734056); GO_0006874 (EC: IDA, PMID: 10734056); GO_0006887 (EC: IDA, PMID: 10734056); GO_0006935 (EC: NAS, PMID: 1380064); GO_0006954 (EC: IDA); GO_0007159 (EC: IDA, PMID: 8558019); GO_0007267 (EC: IDA, PMID: 8558019); GO_0008009 (EC: IDA, PMID: 1699135); GO_0008009 (EC: NAS, PMID: 7524281); GO_0009615 (EC: TAS, PMID: 10488085); GO_0009636 (EC: IDA, PMID: 10841574); GO_0010535 (EC: TAS, PMID: 11278738); GO_0010759 (EC: IDA, PMID: 16778803); GO_0010820 (EC: IDA, PMID: 16778803); GO_0014068 (EC: IDA, PMID: 7544376); GO_0014911 (EC: IDA); GO_0016004 (EC: IDA, PMID: 10734056); GO_0030298 (EC: IDA, PMID: 10488085); GO_0030335 (EC: IDA, PMID: 7545673); GO_0031328 (EC: IDA, PMID: 18337562); GO_0031584 (EC: IDA, PMID: 9469451); GO_0031663 (EC: IDA); GO_0031726 (EC: IDA, PMID: 10910894); GO_0031726 (EC: IPI, PMID: 10660125); GO_0031726 (EC: TAS, PMID: 9417081); GO_0031729 (EC: TAS, PMID: 9417081); GO_0031730 (EC: IPI, PMID: 9139699); GO_0033634 (EC: IDA, PMID: 8558019); GO_0034112 (EC: IDA, PMID: 10488085); GO_0042056 (EC: IDA, PMID: 15001559); GO_0042102 (EC: IDA, PMID: 18832695); GO_0042119 (EC: IDA, PMID: 10488085); GO_0042327 (EC: IDA, PMID: 18337562); GO_0042379 (EC: IPI, PMID: 7517217); GO_0042531 (EC: IDA, PMID: 9417081); GO_0042803 (EC: IDA, PMID: 10488085); GO_0043491 (EC: IMP); GO_0043621 (EC: IDA, PMID: 10488085); GO_0043623 (EC: IDA, PMID: 18337562); GO_0043922 (EC: IDA, PMID: 10841574); GO_0044344 (EC: IEP, PMID: 9407497); GO_0045070 (EC: TAS, PMID: 10488085); GO_0045071 (EC: IDA, PMID: 10490959); GO_0045089 (EC: TAS); GO_0045744 (EC: IDA, PMID: 10734056); GO_0045785 (EC: IDA, PMID: 10910894); GO_0045948 (EC: NAS, PMID: 18337562); GO_0046427 (EC: TAS, PMID: 11278738); GO_0046817 (EC: IDA, PMID: 8631850); GO_0048245 (EC: IDA, PMID: 16778803); GO_0048246 (EC: TAS, PMID: 18337562); GO_0048661 (EC: IDA); GO_0050679 (EC: IEA); GO_0050863 (EC: IDA, PMID: 10488085); GO_0050918 (EC: IDA, PMID: 15001559); GO_0051262 (EC: IDA, PMID: 10488085); GO_0051928 (EC: IDA, PMID: 8699119); GO_0061098 (EC: IDA, PMID: 10488085); GO_0070098 (EC: TAS, PMID: 18337562); GO_0070100 (EC: IDA, PMID: 8631850); GO_0070233 (EC: IDA, PMID: 10488085); GO_0070234 (EC: IDA, PMID: 10488085); GO_0071346 (EC: IEP, PMID: 9407497); GO_0071347 (EC: IEP, PMID: 9407497); GO_0071356 (EC: IEP, PMID: 9407497); GO_0071407 (EC: IDA); GO_0090026 (EC: IDA, PMID: 1699135); GO_2000110 (EC: IEA); GO_2000503 (EC: IDA, PMID: 7545673) PMID: 1380064; 1691736; 1699135; 2456327; 2834384; 7517217; 7524281; 7537088; 7542919; 7544376; 7545673; 7689610; 8525373; 8558019; 8573157; 8576227; 8631850; 8642344; 8663314; 8699119; 8898753; 8976200; 9009162; 9120310; 9139699; 9256481; 9289016; 9359702; 9405404; 9407497; 9417081; 9420238; 9469451; 9516414; 9517988; 9558100; 9576751; 9826729; 9889151; 10200305; 10213461; 10221653; 10415069; 10477718; 10488085; 10490959; 10583963; 10640778; 10644351; 10660125; 10713092; 10734056; 10770925; 10774549; 10775626; 10820198; 10841574; 10872839; 10882583; 10910894; 10964543; 10985253; 11083865; 11116158; 11125885; 11197694; 11278738; 11313374; 11350939; 11390394; 11449371; 11500196; 11509627; 11544456; 11602715; 11750041; 11751963; 11816717; 11844139; 11878903; 11897701; 11907119; 11920567; 11929421; 11959378; 11976403; 12081195; 12089333; 12093895; 12114533; 12139952; 12154092; 12164740; 12165487; 12173306; 12200463; 12204866; 12218153; 12270118; 12359436; 12377943; 12445801; 12462338; 12475226; 12477932; 12509457; 12557141; 12610055; 12660426; 12663241; 12668159; 12753088; 12763925; 12789231; 12803993; 12819030; 12837926; 12842758; 12847218; 12858455; 12953261; 12960233; 14637022; 14647058; 14651522; 14687494; 14687706; 15001559; 15001640; 15021309; 15064621; 15067078; 15122808; 15140220; 15142381; 15192276; 15228586; 15239133; 15256089; 15265023; 15280531; 15302103; 15319853; 15368437; 15459010; 15468376; 15471370; 15481145; 15482330; 15488313; 15489334; 15500552; 15537425; 15588341; 15592421; 15602730; 15611878; 15630704; 15645140; 15715189; 15740484; 15742444; 15780175; 15781227; 15793370; 15794069; 15817944; 15848524; 15850807; 15851378; 15857508; 15863470; 15890969; 15899487; 15923218; 15971427; 15978191; 16024972; 16029496; 16032408; 16046258; 16078996; 16161154; 16206161; 16239564; 16246299; 16254204; 16314800; 16323127; 16340468; 16343773; 16354571; 16379602; 16393999; 16437690; 16441357; 16442182; 16468043; 16489254; 16507178; 16511411; 16517749; 16564576; 16614115; 16635746; 16697675; 16712791; 16719905; 16778803; 16791620; 16799229; 16807236; 16841089; 16855620; 16864713; 16864989; 16865553; 16897666; 16911685; 16988194; 16995340; 16997300; 17005260; 17015691; 17016617; 17018392; 17027916; 17038526; 17063508; 17074812; 17075265; 17076674; 17101151; 17112859; 17117952; 17192395; 17202846; 17207890; 17305874; 17328045; 17413295; 17416433; 17416748; 17417600; 17426779; 17431094; 17488389; 17494888; 17504241; 17519498; 17530998; 17540042; 17541284; 17560067; 17565659; 17585540; 17586317; 17596666; 17599774; 17620002; 17625600; 17653092; 17674321; 17678722; 17678915; 17700210; 17703412; 17711627; 17728497; 17765942; 17884183; 17909104; 17922439; 17984846; 17986095; 17989610; 17990036; 18060801; 18162936; 18186796; 18191726; 18195571; 18217191; 18218038; 18240029; 18306985; 18336625; 18337562; 18361934; 18385174; 18415893; 18426815; 18439751; 18447907; 18461620; 18559339; 18636124; 18663025; 18676680; 18678243; 18696265; 18706447; 18716401; 18790652; 18800033; 18824472; 18832695; 18936436; 18953865; 18956302; 18958622; 18986692; 19017985; 19064579; 19073147; 19080516; 19099590; 19099677; 19105348; 19122644; 19124744; 19140875; 19156204; 19157676; 19170196; 19172384; 19201454; 19201759; 19226274; 19240255; 19242540; 19247692; 19258635; 19258923; 19264973; 19333930; 19334035; 19335954; 19342158; 19347053; 19349390; 19360811; 19382425; 19416867; 19420105; 19423540; 19425063; 19427114; 19455469; 19458908; 19493460; 19524301; 19533303; 19578796; 19607806; 19625176; 19628738; 19646363; 19658300; 19661268; 19692168; 19699525; 19703339; 19730683; 19779041; 19830727; 19841187; 19846984; 19847187; 19874825; 19893003; 19913121; 19917679; 19953896; 19996575; 20038229; 20067109; 20121167; 20186291; 20203694; 20237496; 20299965; 20331378; 20378664; 20395963; 20403075; 20406964; 20430255; 20432237; 20438785; 20453000; 20484300; 20503287; 20518834; 20523058; 20531015; 20540976; 20626297; 20628086; 20685145; 20725607; 20729133; 20731692; 20732991; 20734064; 20799037; 20805685; 20861350; 20869067; 20884746; 20978355; 21054877; 21063127; 21189258; 21196302; 21252118; 21258798; 21335555; 21336628; 21356384; 21368236; 21376715; 21418786; 21454528; 21486440; 21510799; 21547257; 21575514; 21586622; 21610221; 21616095; 21617311; 21638128; 21658938; 21671175; 21701779; 21707929; 21734400; 21738469; 21827949; 21839152; 21890375; 21918813; 21921047; 21945445; 21963154; 21988832; 22085486; 22095608; 22162987; 22189589; 22205974; 22265023; 22271279; 22282655; 22300682; 22321225; 22355269; 22374185; 22380870; 22401175; 22412377; 22444510; 22447977; 22473756; 22490648; 22494696; 22506069; 22534629; 22541401; 22554651; 22576913; 22637726; 22664104; 22664781; 22691208; 22732186; 22738652; 22750227; 22797700; 22857950; 22987449; 23029252; 23039889; 23065234; 23071760; 23074171; 23152559; 23165450; 23179318; 23180368; 23190507; 23207898; 23210681; 23219091; 23267209; 23276697; 23312573; 23480650; 23490419; 23577146; 23660804; 23790189; 23818986; 23900864; 23935096; 23998932; 24053708; 24067464; 24078580; 24116893; 24133061; 24157824; 24273921 chemokine (C-C motif) ligand 5 Ensembl:ENSG00000161570 HGNC:10632 HPRD:01751 MIM:187011 Vega:OTTHUMG00000132949 CCL5 OGG:3000006355 Bin Zhao, Yue Liu, Oliver He HC14 MCP-2 MCP2 SCYA10 SCYA8 WEB: http://www.ncbi.nlm.nih.gov/gene CCL8 chemokine (C-C motif) ligand 8 6355 17q11.2 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0004672 (EC: IDA, PMID: 10734056); GO_0005615 (EC: IEA); GO_0006468 (EC: IDA, PMID: 10734056); GO_0006816 (EC: IDA, PMID: 10734056); GO_0006874 (EC: IDA, PMID: 10734056); GO_0006887 (EC: IDA, PMID: 10734056); GO_0006935 (EC: TAS, PMID: 9468473); GO_0006954 (EC: IEA); GO_0006955 (EC: IEA); GO_0007165 (EC: TAS, PMID: 9119400); GO_0007267 (EC: IDA, PMID: 10734056); GO_0008009 (EC: IEA); GO_0008201 (EC: IEA); GO_0009615 (EC: TAS, PMID: 9468473); GO_0016004 (EC: IDA, PMID: 10734056); GO_0043085 (EC: IDA, PMID: 10734056); GO_0060326 (EC: TAS, PMID: 9468473) PMID: 1613466; 2518726; 8189067; 8661057; 8898111; 9005985; 9070881; 9115216; 9119400; 9405404; 9468473; 9558113; 9730840; 10477718; 10734056; 10734104; 11083865; 11087354; 12149192; 12477932; 12539042; 13679391; 14647058; 15489334; 15607028; 15644410; 17487826; 17703412; 18256320; 18602166; 18636124; 18660381; 18684849; 18818748; 18835932; 19019335; 19224633; 19258923; 19415413; 19423540; 19527514; 19865101; 20056178; 20181935; 20406964; 20438785; 20503287; 21220697; 21514686; 21945122; 22412388; 22987449; 23418602 chemokine (C-C motif) ligand 8 Ensembl:ENSG00000108700 HGNC:10635 HPRD:03791 MIM:602283 Vega:OTTHUMG00000132883 CCL8 OGG:3000006357 Bin Zhao, Yue Liu, Oliver He CKb10 MCP-4 NCC-1 NCC1 SCYA13 SCYL1 WEB: http://www.ncbi.nlm.nih.gov/gene CCL13 chemokine (C-C motif) ligand 13 6357 17q11.2 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0005102 (EC: TAS, PMID: 9195948); GO_0005615 (EC: IEA); GO_0006874 (EC: TAS, PMID: 9195948); GO_0006935 (EC: TAS, PMID: 9195948); GO_0006954 (EC: IEA); GO_0006955 (EC: IEA); GO_0007010 (EC: IDA, PMID: 10072545); GO_0007165 (EC: TAS, PMID: 9195948); GO_0007267 (EC: TAS, PMID: 9195948); GO_0008009 (EC: IDA, PMID: 10072545); GO_0008360 (EC: IDA, PMID: 10072545); GO_0048245 (EC: IDA, PMID: 10072545) PMID: 8642349; 8661057; 8955214; 9060459; 9195948; 9405404; 9558100; 10049733; 10072545; 10477718; 10734104; 11342433; 11400154; 11597922; 12149192; 12477932; 12731055; 12805085; 12915769; 14560935; 15489334; 16169070; 16625196; 16855189; 17181634; 17541284; 17703412; 17824960; 17851891; 18219197; 18660381; 19258923; 19423540; 19565514; 19865101; 20056178; 20139115; 20237496; 20406964; 20438785; 20503287; 20628624; 21327296; 21832049; 22393877; 22412388; 23128233; 23375121 chemokine (C-C motif) ligand 13 Ensembl:ENSG00000181374 HGNC:10611 HPRD:03230 MIM:601391 Vega:OTTHUMG00000132890 CCL13 OGG:3000006372 Bin Zhao, Yue Liu, Oliver He CKA-3 GCP-2 GCP2 SCYB6 WEB: http://www.ncbi.nlm.nih.gov/gene CXCL6 chemokine (C-X-C motif) ligand 6 6372 4q13.3 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0006935 (EC: TAS, PMID: 9164944); GO_0006954 (EC: TAS, PMID: 8399143); GO_0006955 (EC: IEA); GO_0007165 (EC: TAS, PMID: 9164944); GO_0007267 (EC: TAS, PMID: 9164944); GO_0008009 (EC: IEA); GO_0008201 (EC: IEA); GO_0060326 (EC: TAS, PMID: 8399143) PMID: 8399143; 8423327; 9057843; 9164944; 9465307; 9692902; 10343098; 10593335; 12477932; 12524079; 12533683; 12591113; 12628493; 12882792; 12950257; 15214047; 15342556; 15489334; 15652347; 15815621; 17022986; 17703412; 17827342; 18240029; 18443119; 18563170; 18577758; 18782286; 18842116; 19240061; 19258923; 19369450; 20503287; 20507572; 20628624; 21236563; 22886775; 23128233; 23814098 chemokine (C-X-C motif) ligand 6 Ensembl:ENSG00000124875 HGNC:10643 HPRD:00735 MIM:138965 Vega:OTTHUMG00000130010 Other designations: C-X-C motif chemokine 6|Small inducible cytokine subfamily B (Cys-X-Cys), member b|chemokine (C-X-C motif) ligand 6 (granulocyte chemotactic protein 2)|chemokine alpha 3|granulocyte chemotactic protein 2|small inducible cytokine subfamily B (Cys-X-Cys), member 6 (granulocyte chemotactic protein 2)|small-inducible cytokine B6 CXCL6 OGG:3000006400 Bin Zhao, Yue Liu, Oliver He PRO1063 SEL1-LIKE SEL1L1 WEB: http://www.ncbi.nlm.nih.gov/gene SEL1L sel-1 suppressor of lin-12-like (C. elegans) 6400 UNQ128/PRO1063 14q31 20140408 9606 14 protein-coding Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 18264092); GO_0005789 (EC: IEA); GO_0007219 (EC: IEA); GO_0016021 (EC: IEA); GO_0034976 (EC: IEA) PMID: 9417916; 9858735; 10051412; 10496078; 10746565; 11349831; 11544613; 11809711; 12030374; 12477932; 12553058; 12754519; 12975309; 14729273; 15307954; 15342556; 16186509; 16303743; 16331677; 16331889; 16344560; 16412574; 17822620; 17967421; 18264092; 18314878; 18502753; 18711132; 18811591; 19135427; 19204006; 19346256; 19524542; 19706418; 20416077; 21139048; 21359144; 21454652; 21632540; 21656579; 21857022; 21903092; 21903422; 21988832; 22119785; 22190034; 22268729; 22350780; 22905195; 22939629; 23097496; 23356641; 23363602; 23464991; 23867461; 23956138; 24043630 sel-1 suppressor of lin-12-like (C. elegans) Ensembl:ENSG00000071537 HGNC:10717 HPRD:07532 MIM:602329 Vega:OTTHUMG00000171419 Other designations: Suppressor of lin 12 (sel-1), C. elegans, homolog of|protein sel-1 homolog 1|sel-1 suppressor of lin-12-like 1|suppressor of lin-12-like protein 1 SEL1L OGG:3000006401 Bin Zhao, Yue Liu, Oliver He CD62E ELAM ELAM1 ESEL LECAM2 WEB: http://www.ncbi.nlm.nih.gov/gene SELE selectin E 6401 RP1-117P20.2 1q22-q25 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0002092 (EC: IDA, PMID: 9312078); GO_0002523 (EC: TAS, PMID: 18029551); GO_0002687 (EC: IEA); GO_0004888 (EC: IMP, PMID: 12960351); GO_0005515 (EC: IPI, PMID: 18606703); GO_0005615 (EC: IDA, PMID: 9290466); GO_0005886 (EC: TAS); GO_0005901 (EC: IDA, PMID: 12960351); GO_0005905 (EC: IDA, PMID: 18029551); GO_0006954 (EC: TAS, PMID: 2466335); GO_0007157 (EC: IMP, PMID: 18029551); GO_0007159 (EC: IDA, PMID: 7680663); GO_0007202 (EC: IMP, PMID: 12960351); GO_0007596 (EC: TAS); GO_0016021 (EC: IEA); GO_0019722 (EC: TAS, PMID: 12960351); GO_0030029 (EC: IDA, PMID: 8609175); GO_0030863 (EC: IDA, PMID: 8609175); GO_0032496 (EC: TAS, PMID: 18029551); GO_0033691 (EC: IDA, PMID: 7680663); GO_0034612 (EC: TAS, PMID: 18029551); GO_0043274 (EC: IDA, PMID: 12960351); GO_0045121 (EC: IDA, PMID: 18029551); GO_0048471 (EC: IDA, PMID: 12960351); GO_0050727 (EC: TAS, PMID: 18029551); GO_0050900 (EC: TAS); GO_0050901 (EC: IMP, PMID: 18029551); GO_0070492 (EC: IDA, PMID: 7680663); GO_0070555 (EC: IDA, PMID: 8609175) PMID: 1375831; 1689848; 1694218; 1701274; 1703529; 2466335; 7509040; 7523444; 7533025; 7536194; 7538217; 7541576; 7680663; 7681016; 7693046; 7694691; 8557254; 8609175; 8621728; 9024699; 9128259; 9269771; 9290466; 9312078; 9597096; 9920928; 9933738; 10391210; 10419878; 10477700; 10982036; 11097335; 11168027; 11341749; 11359462; 11402070; 11404363; 11466561; 11575217; 11575218; 11602579; 11697721; 11714857; 11764211; 11776680; 11827962; 11828340; 11847011; 11859093; 11882337; 11882338; 11929779; 11935152; 11936588; 11948013; 11981814; 11983205; 12011765; 12020443; 12027924; 12036529; 12082590; 12082592; 12086338; 12165498; 12172318; 12172576; 12175121; 12186696; 12200076; 12200386; 12388172; 12421968; 12477932; 12499405; 12522014; 12595908; 12626663; 12649084; 12673844; 12698264; 12738381; 12768436; 12788528; 12792758; 12820726; 12871600; 12898464; 12940514; 12960351; 14534081; 14557872; 14568956; 14587643; 14592723; 14592840; 14607629; 14691583; 14714557; 14734737; 14763917; 14984317; 14988223; 15009098; 15013273; 15076187; 15076188; 15080580; 15083893; 15086468; 15148373; 15167972; 15179350; 15187162; 15194470; 15254658; 15299021; 15304054; 15308783; 15331359; 15387376; 15488708; 15515123; 15560890; 15584003; 15593054; 15666579; 15735663; 15736116; 15784173; 15833936; 15871853; 15917220; 15979159; 16002039; 16061120; 16080806; 16269612; 16344560; 16426244; 16433632; 16501492; 16544732; 16554320; 16565092; 16710414; 16722397; 16756647; 16773720; 16820586; 16843446; 16892455; 16908800; 16916660; 16963035; 16974056; 16980970; 16982492; 17014013; 17020471; 17036337; 17057786; 17142773; 17143564; 17167725; 17372905; 17389327; 17392035; 17452460; 17515951; 17563404; 17578587; 17684030; 17706337; 17706953; 17875185; 17939599; 17954174; 17956423; 17963163; 17991470; 17996280; 18020971; 18029551; 18094708; 18182036; 18191640; 18197885; 18212564; 18217430; 18276775; 18375392; 18401566; 18484695; 18513389; 18580442; 18590706; 18593916; 18597403; 18597952; 18606703; 18611928; 18613029; 18633131; 18649056; 18676680; 18677293; 18692491; 18704886; 18707907; 18710415; 18726101; 18761727; 18791689; 18794336; 18828734; 18930765; 18973547; 18974840; 18974842; 18991188; 19021457; 19028820; 19056482; 19064610; 19118161; 19131662; 19136145; 19139603; 19170196; 19191721; 19212205; 19225544; 19237221; 19238444; 19240957; 19249917; 19263529; 19361981; 19414551; 19417018; 19420105; 19420919; 19422386; 19423540; 19479237; 19536175; 19538882; 19548631; 19559392; 19564823; 19578796; 19670701; 19692168; 19701669; 19729601; 19729612; 19885579; 19913121; 19942746; 19948975; 19949084; 19996987; 20004427; 20010946; 20044088; 20056442; 20191078; 20193033; 20227257; 20406964; 20416077; 20430730; 20438785; 20445017; 20452482; 20485444; 20495539; 20508517; 20536507; 20580062; 20587315; 20602615; 20603037; 20607758; 20622166; 20628086; 20656374; 20673868; 20680929; 20691427; 20713000; 20796317; 20833389; 20855565; 20937831; 20941749; 21099224; 21138731; 21159528; 21162967; 21286681; 21381877; 21471547; 21486700; 21521525; 21526496; 21544708; 21629188; 21659524; 21756793; 21780194; 21827804; 21881522; 22009003; 22010135; 22021370; 22025563; 22030423; 22068558; 22104155; 22158116; 22159147; 22264805; 22269951; 22271244; 22322211; 22336504; 22366582; 22384091; 22414298; 22497223; 22508864; 22533155; 22589243; 22593709; 22648254; 22718118; 22763042; 22814396; 22815813; 22820001; 22836626; 22922984; 22970241; 23015400; 23041613; 23129313; 23187956; 23190470; 23235150; 23242661; 23353989; 23442851; 23457623; 23565284; 23623010; 23855486; 23906304 selectin E Ensembl:ENSG00000007908 HGNC:10718 HPRD:00566 MIM:131210 Vega:OTTHUMG00000034851 Other designations: CD62 antigen-like family member E|E-selectin|ELAM-1|endothelial adhesion molecule 1|endothelial leukocyte adhesion molecule 1|leukocyte endothelial cell adhesion molecule 2|leukocyte-endothelial cell adhesion molecule 2 SELE OGG:3000006403 Bin Zhao, Yue Liu, Oliver He CD62 CD62P GMP140 GRMP LECAM3 PADGEM PSEL WEB: http://www.ncbi.nlm.nih.gov/gene SELP selectin P (granule membrane protein 140kDa, antigen CD62) 6403 RP1-86F14.2 1q22-q25 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0001530 (EC: IMP, PMID: 16514062); GO_0001948 (EC: IEA); GO_0002576 (EC: TAS); GO_0002687 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11237770); GO_0005615 (EC: IDA, PMID: 9290466); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 1701178); GO_0006954 (EC: IEA); GO_0007155 (EC: TAS, PMID: 2466574); GO_0007157 (EC: IEA); GO_0007159 (EC: IDA, PMID: 7680663); GO_0007596 (EC: TAS); GO_0008201 (EC: IDA, PMID: 7680663); GO_0009897 (EC: IDA, PMID: 16514062); GO_0010572 (EC: ISS, PMID: 16514062); GO_0014068 (EC: IDA, PMID: 17632516); GO_0030168 (EC: TAS); GO_0031088 (EC: TAS); GO_0031092 (EC: IDA, PMID: 15297306); GO_0031092 (EC: TAS); GO_0032496 (EC: IC, PMID: 16514062); GO_0033623 (EC: IMP, PMID: 17632516); GO_0033691 (EC: IDA, PMID: 7680663); GO_0042806 (EC: IDA, PMID: 7680663); GO_0043208 (EC: TAS, PMID: 7680663); GO_0048306 (EC: IEA); GO_0050829 (EC: IC, PMID: 16514062); GO_0050900 (EC: TAS); GO_0050901 (EC: IEA); GO_0070492 (EC: IDA, PMID: 7680663) PMID: 1375831; 1377048; 1435334; 1694218; 1701178; 1705568; 1717161; 2466574; 2472431; 7505680; 7508745; 7680663; 7684381; 7693674; 8467233; 8901515; 9128259; 9129046; 9290466; 9668170; 10391209; 10499919; 10713099; 10733515; 10950950; 11040019; 11081633; 11237770; 11247301; 11597943; 11861803; 11885026; 11936588; 11981814; 12036879; 12036880; 12082590; 12165563; 12200386; 12384485; 12468916; 12477932; 12736150; 12757775; 12783114; 12847232; 12858167; 12860908; 12871503; 12871600; 12888879; 12911583; 12945872; 14557872; 14568956; 14592723; 14615387; 14630802; 14676308; 14680834; 14681304; 14764537; 15026421; 15059608; 15059609; 15080580; 15133030; 15217824; 15221968; 15231569; 15297306; 15297307; 15299021; 15316595; 15351857; 15353601; 15497463; 15543334; 15583743; 15633604; 15705928; 15769472; 15885758; 15916851; 15972662; 16014051; 16100264; 16125711; 16139336; 16184405; 16257118; 16263699; 16332977; 16344560; 16352650; 16390014; 16514062; 16633357; 16636497; 16648968; 16683915; 16764881; 16860607; 16877367; 16928730; 16935700; 16973503; 16982492; 17027652; 17064811; 17074110; 17126824; 17143564; 17192395; 17204688; 17275499; 17279322; 17393020; 17420019; 17437524; 17473568; 17488661; 17497038; 17498578; 17509958; 17510305; 17554801; 17597069; 17598012; 17632516; 17634906; 17698171; 17700216; 17702963; 17706337; 17710630; 17849054; 17890399; 17939599; 17944986; 17945332; 17982310; 18029348; 18034324; 18050247; 18054198; 18080800; 18182036; 18191640; 18217430; 18333373; 18363812; 18363816; 18383329; 18390200; 18449419; 18497306; 18535285; 18539899; 18550060; 18576930; 18580442; 18597952; 18600034; 18606703; 18649055; 18713749; 18818407; 18828734; 18974840; 18974842; 19028820; 19036374; 19047793; 19064610; 19074885; 19082691; 19105599; 19106004; 19131662; 19132251; 19136145; 19138666; 19212907; 19221099; 19228864; 19240957; 19241310; 19247692; 19262138; 19263529; 19264679; 19280705; 19332769; 19361981; 19395438; 19404301; 19423540; 19452728; 19479237; 19493436; 19525192; 19536175; 19559392; 19578796; 19590054; 19638712; 19656773; 19689998; 19729601; 19812370; 19874461; 19913121; 19913879; 19948214; 19948975; 20010946; 20034466; 20051472; 20056442; 20079524; 20097880; 20153702; 20167578; 20205626; 20227257; 20376705; 20406964; 20431845; 20431848; 20435690; 20438785; 20445017; 20452482; 20485444; 20536507; 20580062; 20586826; 20602615; 20603037; 20628086; 20669347; 20673868; 20723301; 20855565; 21071696; 21085001; 21106229; 21116278; 21143192; 21149548; 21159528; 21162967; 21170343; 21245745; 21319374; 21385561; 21441381; 21497813; 21507293; 21521525; 21534853; 21544708; 21545688; 21594636; 21618132; 21638248; 21642543; 21658254; 21714704; 21763287; 21803846; 21816455; 21866298; 22010135; 22021370; 22039451; 22053609; 22068558; 22088599; 22100896; 22142906; 22156911; 22159147; 22192915; 22425972; 22473907; 22593709; 22627390; 22688557; 22703881; 22717029; 22745009; 22836626; 22842622; 23014585; 23018521; 23416763; 23421771; 23442851; 23468382; 23525448; 23593361; 23740526 selectin P (granule membrane protein 140kDa, antigen CD62) Ensembl:ENSG00000174175 HGNC:10721 HPRD:01433 MIM:173610 Vega:OTTHUMG00000034685 Other designations: CD62 antigen-like family member P|GMP-140|P-selectin|granule membrane protein 140|granulocyte membrane protein|leukocyte-endothelial cell adhesion molecule 3|platelet activation dependent granule-external membrane protein|platelet alpha-granule membrane protein SELP OGG:3000006426 Bin Zhao, Yue Liu, Oliver He ASF SF2 SF2p33 SFRS1 SRp30a WEB: http://www.ncbi.nlm.nih.gov/gene SRSF1 serine/arginine-rich splicing factor 1 6426 OK/SW-cl.3 17q22 9606 17 Official from a nomenclature committee GO_0000166 (EC: IEA); GO_0000395 (EC: IDA, PMID: 9885563); GO_0000398 (EC: IC, PMID: 11991638); GO_0000398 (EC: TAS); GO_0001701 (EC: IEA); GO_0003723 (EC: IDA, PMID: 19561594); GO_0003723 (EC: IPI); GO_0003729 (EC: IDA); GO_0005515 (EC: IPI, PMID: 10196197); GO_0005634 (EC: IDA); GO_0005654 (EC: IDA, PMID: 9885563); GO_0005654 (EC: TAS); GO_0005737 (EC: IEA); GO_0006366 (EC: TAS); GO_0006369 (EC: TAS); GO_0006376 (EC: TAS, PMID: 1830244); GO_0006397 (EC: TAS, PMID: 1830244); GO_0006406 (EC: TAS); GO_0008380 (EC: TAS); GO_0010467 (EC: TAS); GO_0016607 (EC: IDA); GO_0031124 (EC: TAS); GO_0035145 (EC: IDA, Qualifier: colocalizes_with, PMID: 16314458); GO_0044822 (EC: IDA); GO_0050733 (EC: IEA); GO_0060048 (EC: IEA); GO_0071013 (EC: IDA, PMID: 11991638) PMID: 1577277; 1741384; 1830244; 1855257; 7512732; 7543047; 8125298; 8139654; 8189522; 8208298; 8223481; 8261509; 8530103; 8617202; 8626563; 8639538; 8798720; 8816452; 9023367; 9237760; 9420331; 9447963; 9472028; 9473574; 9611241; 9671816; 9685421; 9799243; 9885563; 10022843; 10196197; 10225947; 10366588; 10390541; 10713112; 10757789; 10843177; 11101529; 11285240; 11418604; 11683387; 11779509; 11790298; 11801589; 11825891; 11967326; 11991638; 12135490; 12215544; 12221105; 12226669; 12234937; 12270705; 12477932; 12525645; 12565863; 12612063; 14555757; 14559993; 14623875; 15123677; 15163745; 15184380; 15208309; 15210956; 15243141; 15367627; 15452250; 15456888; 15489334; 15546619; 15592455; 15635413; 15652350; 15782174; 15798186; 15848144; 15907217; 15998806; 16000324; 16051665; 16096057; 16189514; 16196087; 16210245; 16223727; 16260492; 16314458; 16344560; 16376875; 16505493; 16611940; 16721827; 16982639; 17081983; 17310252; 17332742; 17353931; 17361185; 17517895; 17609381; 17670832; 17786225; 17959926; 18155240; 18243119; 18315555; 18391021; 18439897; 18457437; 18495665; 18586677; 18687337; 18832178; 18841201; 18945764; 19004959; 19073146; 19111562; 19116412; 19250906; 19322201; 19441081; 19464723; 19477182; 19523114; 19561594; 19602482; 19608861; 19633418; 19657567; 19710015; 19716452; 19738201; 19857271; 19966273; 20085707; 20118245; 20120036; 20139984; 20211142; 20308322; 20360068; 20385090; 20508642; 20516191; 20519389; 20637698; 20639865; 20657585; 20668893; 20682707; 20805487; 20923760; 21045158; 21078624; 21081666; 21139048; 21145461; 21182205; 21297941; 21536904; 21549307; 21622622; 21668763; 21832049; 21853274; 21890473; 21906983; 21907836; 21963094; 21988832; 22053931; 22094256; 22245967; 22268729; 22365833; 22446626; 22454513; 22505724; 22545246; 22839530; 22855529; 22939629; 22952844; 22990118; 23000965; 23084401; 23184937; 23228155; 23319613; 23349975; 23398456; 23462647; 23478443; 23537643; 23592547; 23602568; 23658645; 23707382; 23748175; 24244333; 24250222; 24368769; 24457600 serine/arginine-rich splicing factor 1 HGNC:10780 HPRD:02887 MIM:600812 Other designations: ASF-1|SR splicing factor 1|alternative-splicing factor 1|pre-mRNA-splicing factor SF2, P33 subunit|splicing factor 2|splicing factor, arginine/serine-rich 1 SRSF1 OGG:3000006506 Bin Zhao, Yue Liu, Oliver He EAAT2 GLT-1 WEB: http://www.ncbi.nlm.nih.gov/gene SLC1A2 solute carrier family 1 (glial high affinity glutamate transporter), member 2 6506 11p13-p12 9606 11 Official from a nomenclature committee GO_0005313 (EC: IDA, PMID: 7521911); GO_0005515 (EC: IPI, PMID: 19527721); GO_0005886 (EC: TAS); GO_0006811 (EC: TAS); GO_0007268 (EC: TAS, PMID: 7521911); GO_0007632 (EC: IEA); GO_0009611 (EC: IEA); GO_0010259 (EC: IEA); GO_0015501 (EC: IEA); GO_0016020 (EC: TAS, PMID: 7521911); GO_0016021 (EC: IEA); GO_0017153 (EC: IEA); GO_0021537 (EC: IEA); GO_0030534 (EC: IEA); GO_0030673 (EC: IEA); GO_0031668 (EC: IEA); GO_0035264 (EC: IEA); GO_0042493 (EC: IEA); GO_0043200 (EC: IEA); GO_0046326 (EC: IEA); GO_0051938 (EC: IDA, PMID: 7521911); GO_0055085 (EC: TAS); GO_0070779 (EC: IDA, PMID: 7521911) PMID: 7521911; 7522567; 7587378; 8172925; 8619474; 9110174; 9450673; 9463476; 9539131; 9585360; 11031254; 11038258; 11071482; 11204345; 11357955; 11698255; 11744157; 11792462; 11860269; 11891650; 11994293; 12408226; 12477932; 12578975; 12890621; 12898275; 12950454; 14506254; 14662797; 14702039; 14982736; 15048885; 15135231; 15246112; 15265858; 15296513; 15337309; 15483603; 15494981; 15660126; 15822905; 15927426; 16061389; 16344560; 16567804; 16766085; 17311293; 17311320; 17535102; 17684493; 17823119; 17920768; 18314905; 18326497; 18378006; 18519826; 18658151; 18838545; 19023027; 19086053; 19151621; 19156168; 19268276; 19283393; 19338517; 19527721; 19660525; 19910676; 19998491; 20193040; 20379614; 20398908; 20399272; 20410850; 20416976; 20688910; 20936779; 21098017; 21110225; 21335552; 21471434; 21569822; 21707071; 21711518; 21792905; 21852380; 22069320; 22505712; 22513140; 22522966; 22561518; 22728822; 22750157; 22764253; 22903028; 23023733; 23356950; 23390085; 23415275; 23596072; 23706640; 24068947; 24334928 solute carrier family 1 (glial high affinity glutamate transporter), member 2 Ensembl:ENSG00000110436 HGNC:10940 HPRD:02625 MIM:600300 Vega:OTTHUMG00000044391 Other designations: excitatory amino acid transporter 2|excitotoxic amino acid transporter 2|glutamate/aspartate transporter II|sodium-dependent glutamate/aspartate transporter 2 SLC1A2 OGG:3000006513 Bin Zhao, Yue Liu, Oliver He DYT17 DYT18 DYT9 EIG12 GLUT GLUT1 GLUT1DS HTLVR PED WEB: http://www.ncbi.nlm.nih.gov/gene SLC2A1 solute carrier family 2 (facilitated glucose transporter), member 1 6513 1p34.2 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0001939 (EC: IEA); GO_0005355 (EC: TAS, PMID: 9462754); GO_0005515 (EC: IPI, PMID: 18347014); GO_0005886 (EC: TAS); GO_0005901 (EC: IEA); GO_0005911 (EC: IEA); GO_0005975 (EC: TAS); GO_0006112 (EC: TAS); GO_0006461 (EC: IDA, PMID: 18347014); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0006970 (EC: IEA); GO_0008645 (EC: TAS); GO_0015758 (EC: TAS); GO_0016020 (EC: TAS, PMID: 3028891); GO_0016021 (EC: IEA); GO_0016323 (EC: IEA); GO_0019852 (EC: TAS); GO_0019900 (EC: IEA); GO_0030496 (EC: IDA, PMID: 15166316); GO_0030864 (EC: IDA, PMID: 18347014); GO_0033300 (EC: IEA); GO_0042149 (EC: IEA); GO_0042470 (EC: IEA); GO_0042802 (EC: IPI, PMID: 1429721); GO_0042910 (EC: IEA); GO_0043621 (EC: IDA, PMID: 18347014); GO_0044281 (EC: TAS); GO_0050796 (EC: TAS); GO_0055056 (EC: IEA); GO_0055085 (EC: TAS); GO_0070062 (EC: IDA); GO_0072562 (EC: IDA) PMID: 1429721; 2394733; 2834252; 3028891; 3170580; 3839598; 7798206; 7829101; 8619474; 8662691; 8839927; 9110174; 9153243; 9462754; 10086067; 10198040; 10227690; 10562431; 10655495; 10759149; 10980529; 11007796; 11136715; 11168944; 11231353; 11296192; 11425315; 11477169; 11603379; 11681785; 11747430; 11774318; 11836704; 11842083; 11920478; 11953883; 11991658; 12064911; 12086959; 12112827; 12122099; 12133004; 12145475; 12379105; 12379106; 12477932; 12554125; 12583599; 12673735; 12752470; 12849991; 12942120; 12969152; 14622599; 14674124; 14679154; 14688257; 14702039; 14757434; 14991538; 15073187; 15086844; 15147968; 15166316; 15331928; 15342556; 15454279; 15489334; 15502921; 15682272; 15709778; 15745834; 15767416; 15778389; 15823019; 15847702; 15924676; 15955807; 15967114; 16125330; 16126902; 16136514; 16142350; 16147855; 16169070; 16172126; 16195374; 16220828; 16273245; 16310037; 16344560; 16407180; 16443776; 16519917; 16681687; 16681688; 16800634; 16842248; 17020877; 17064664; 17071132; 17080242; 17081065; 17167225; 17192790; 17294670; 17387384; 17404017; 17442736; 17451637; 17452775; 17504522; 17554865; 17591274; 17611657; 17635959; 17727838; 17854396; 17991316; 18097583; 18172662; 18177733; 18191496; 18212354; 18227718; 18245775; 18246802; 18271924; 18290322; 18311082; 18324916; 18343752; 18347014; 18351386; 18387950; 18401196; 18410529; 18422279; 18451999; 18565734; 18577546; 18613291; 18614966; 18676680; 18695903; 18726700; 18764953; 18821326; 18948400; 18953257; 18973239; 18981181; 18987250; 18990414; 19016655; 19020718; 19020742; 19085834; 19142800; 19152396; 19166280; 19170196; 19173807; 19234439; 19286567; 19289587; 19292042; 19303158; 19304421; 19347605; 19366592; 19386788; 19420105; 19434538; 19449892; 19465749; 19471022; 19490621; 19533082; 19533890; 19536037; 19554504; 19569052; 19587357; 19619276; 19625176; 19630075; 19648108; 19648882; 19655166; 19681047; 19692168; 19709351; 19738201; 19798636; 19819644; 19822956; 19883765; 19948975; 19955252; 20030103; 20063428; 20079187; 20113375; 20221955; 20301603; 20375117; 20382060; 20395120; 20424473; 20428049; 20512538; 20526721; 20527231; 20540786; 20569445; 20574033; 20607826; 20630673; 20679470; 20687207; 20703861; 20730618; 20803547; 20846124; 20854211; 20937822; 20947823; 20965718; 21029693; 21033220; 21075472; 21109935; 21135204; 21139048; 21194153; 21206329; 21252943; 21270293; 21273616; 21281236; 21294792; 21295279; 21306648; 21317389; 21321933; 21332301; 21343253; 21348951; 21384913; 21395180; 21411785; 21438910; 21442770; 21445818; 21475039; 21521642; 21528061; 21546213; 21555602; 21697701; 21707071; 21791420; 21808860; 21832227; 21838819; 21870331; 21899256; 21906983; 21920790; 21938742; 21962875; 21963094; 21986508; 21987572; 21987722; 22011817; 22029179; 22069254; 22072148; 22153830; 22199327; 22200795; 22221271; 22228332; 22234250; 22234467; 22253523; 22263435; 22270867; 22282454; 22282645; 22304920; 22308487; 22363641; 22376167; 22398711; 22437877; 22470192; 22475893; 22483234; 22509097; 22623428; 22663547; 22673619; 22704013; 22707195; 22795339; 22800355; 22812641; 22813791; 22814174; 22835601; 22843905; 22847606; 22888973; 22899793; 22901702; 22939629; 22961556; 22971162; 23000965; 23002041; 23030583; 23076555; 23098453; 23106342; 23108021; 23187830; 23219802; 23227892; 23280796; 23306390; 23359198; 23453806; 23480298; 23483445; 23615963; 23661345; 23720776; 23740044; 23744486; 23861325; 23935399; 24164300; 24343741 solute carrier family 2 (facilitated glucose transporter), member 1 Ensembl:ENSG00000117394 HGNC:11005 HPRD:00683 MIM:138140 Vega:OTTHUMG00000007657 Other designations: GLUT-1|glucose transporter type 1, erythrocyte/brain|hepG2 glucose transporter|human T-cell leukemia virus (I and II) receptor|solute carrier family 2, facilitated glucose transporter member 1 SLC2A1 OGG:3000006515 Bin Zhao, Yue Liu, Oliver He GLUT3 WEB: http://www.ncbi.nlm.nih.gov/gene SLC2A3 solute carrier family 2 (facilitated glucose transporter), member 3 6515 12p13.3 9606 12 Official from a nomenclature committee GO_0005355 (EC: IEA); GO_0005886 (EC: TAS); GO_0005975 (EC: TAS); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0008645 (EC: TAS); GO_0015758 (EC: TAS); GO_0016021 (EC: IEA); GO_0019852 (EC: TAS); GO_0044281 (EC: TAS); GO_0055085 (EC: TAS); GO_0070062 (EC: IDA) PMID: 1417839; 1695905; 3170580; 7502272; 8457197; 9253355; 9477959; 10086067; 11991658; 12064911; 12112827; 12397394; 12477932; 12554125; 12583599; 14757434; 15123239; 15489334; 16049004; 16125330; 16136514; 16169070; 16303743; 17442736; 17559076; 17611657; 17920708; 18029348; 18172662; 18299470; 18401196; 18764953; 18802725; 18976975; 19261894; 19322201; 19536037; 19554504; 19659459; 19681047; 19782666; 19786962; 20308990; 20424473; 20428049; 20468064; 20599725; 20870738; 21890473; 21920790; 21963094; 21987572; 22000473; 22069254; 22113212; 22234467; 22265971; 22270867; 22645302; 22663547; 22706202; 22876317; 22901689; 22901702; 23341039; 23343953; 23720776; 23995067 solute carrier family 2 (facilitated glucose transporter), member 3 Ensembl:ENSG00000059804 HGNC:11007 HPRD:00686 MIM:138170 Vega:OTTHUMG00000133685 Other designations: GLUT-3|glucose transporter type 3, brain|solute carrier family 2, facilitated glucose transporter member 3 SLC2A3 OGG:3000006519 Bin Zhao, Yue Liu, Oliver He ATR1 CSNU1 D2H NBAT RBAT WEB: http://www.ncbi.nlm.nih.gov/gene SLC3A1 solute carrier family 3 (amino acid transporter heavy chain), member 1 6519 2p16.3 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0003333 (EC: TAS, PMID: 10799513); GO_0003824 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12167606); GO_0005743 (EC: IEA); GO_0005774 (EC: IEA); GO_0005886 (EC: TAS); GO_0005887 (EC: IEA); GO_0005975 (EC: IEA); GO_0006520 (EC: TAS, PMID: 8054986); GO_0006811 (EC: TAS); GO_0006865 (EC: TAS); GO_0015171 (EC: TAS, PMID: 10799513); GO_0015174 (EC: TAS, PMID: 8054986); GO_0015184 (EC: TAS, PMID: 8054986); GO_0015802 (EC: TAS, PMID: 8054986); GO_0015811 (EC: TAS, PMID: 8054986); GO_0016020 (EC: TAS, PMID: 8054986); GO_0031526 (EC: IDA, PMID: 12167606); GO_0043169 (EC: IEA); GO_0046982 (EC: IEA); GO_0055085 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 7539209; 7568194; 7573036; 7575432; 7686906; 7789946; 8054986; 8125298; 8486766; 8663184; 9186880; 10574970; 10588648; 10799513; 11318953; 11458794; 11748844; 12060600; 12167606; 12234283; 12239244; 12372889; 12477932; 12820697; 14531788; 14561219; 14702039; 14991253; 15489334; 15635077; 15691362; 15815621; 15818800; 15818801; 15818802; 15913950; 16138908; 16358225; 17010017; 18195088; 18234729; 18332091; 18752446; 18778962; 19056867; 19782624; 20146678; 20800603; 21255007; 22796000; 23794250 solute carrier family 3 (amino acid transporter heavy chain), member 1 HGNC:11025 HPRD:00090 MIM:104614 Other designations: B(0,+)-type amino acid transport protein|SLC3A1 variant B|SLC3A1 variant C|SLC3A1 variant D|SLC3A1 variant E|SLC3A1 variant F|SLC3A1 variant G|amino acid transporter 1|neutral and basic amino acid transport protein rBAT|solute carrier family 3 (cystine, dibasic and neutral amino acid transporters), member 1|solute carrier family 3 (cystine, dibasic and neutral amino acid transporters, activator of cystine, dibasic and neutral amino acid transport), member 1|solute carrier family 3 member 1 SLC3A1 OGG:3000006554 Bin Zhao, Yue Liu, Oliver He NTCP WEB: http://www.ncbi.nlm.nih.gov/gene SLC10A1 solute carrier family 10 (sodium/bile acid cotransporter), member 1 6554 GIG29 14q24.1 9606 14 Official from a nomenclature committee GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 8132774); GO_0006810 (EC: TAS, PMID: 8132774); GO_0008206 (EC: TAS); GO_0008508 (EC: IEA); GO_0015721 (EC: TAS); GO_0016323 (EC: IEA); GO_0044281 (EC: TAS) PMID: 8132774; 11031103; 12044156; 12477932; 12663868; 14660639; 14701722; 15489334; 15604201; 15922475; 16027164; 16123152; 16541252; 17207965; 17635184; 18976975; 19343046; 19815625; 20031551; 20346360; 20424473; 20679960; 20857261; 21109590; 21341987; 21988832; 22029531; 22098322; 22744337; 23150796; 23815591; 23886862; 23930675; 24342612 solute carrier family 10 (sodium/bile acid cotransporter), member 1 HGNC:10905 HPRD:01672 MIM:182396 Other designations: Na(+)/bile acid cotransporter|Na(+)/taurocholate transport protein|Na/taurocholate cotransporting polypeptide|cell growth-inhibiting gene 29 protein|growth-inhibiting protein 29|sodium/bile acid cotransporter|sodium/taurocholate cotransporter|sodium/taurocholate cotransporting polypeptide|solute carrier family 10 (sodium/bile acid cotransporter family), member 1|solute carrier family 10 member 1 SLC10A1 OGG:3000006606 Bin Zhao, Yue Liu, Oliver He BCD541 GEMIN1 SMA SMA1 SMA2 SMA3 SMA4 SMA@ SMN SMNT T-BCD541 TDRD16A WEB: http://www.ncbi.nlm.nih.gov/gene SMN1 survival of motor neuron 1, telomeric 6606 5q13.2 9606 5 Official from a nomenclature committee PMID: 7552146; 7581461; 7639755; 7813012; 8670859; 8808598; 8838816; 8922999; 9147655; 9158159; 9259265; 9302277; 9323129; 9389483; 9503025; 9600994; 9818944; 9837824; 9845364; 10205267; 10339583; 10369862; 10601333; 10725331; 10732802; 10732817; 10734235; 10767334; 10851237; 10942426; 11092763; 11135666; 11149922; 11313744; 11438536; 11448987; 11509230; 11522829; 11551898; 11574476; 11641277; 11704667; 11713266; 11714716; 11720283; 11748230; 11773003; 11791208; 11792806; 11835381; 11875052; 11907229; 11914277; 11935338; 11992267; 11996521; 12021369; 12065586; 12067652; 12095920; 12192051; 12221125; 12361597; 12374765; 12459587; 12477932; 12657835; 12663808; 12668731; 12679382; 12878704; 12975319; 14520560; 14697339; 14715275; 14742439; 14749338; 14972554; 15119481; 15222879; 15249625; 15304326; 15337310; 15345747; 15372022; 15459957; 15489334; 15494309; 15526170; 15580564; 15608400; 15726222; 15832310; 16087681; 16093455; 16118268; 16169070; 16189514; 16331551; 16439605; 16449646; 16481599; 16565220; 16617248; 16651888; 16786553; 16845275; 16931506; 16936383; 17023415; 17049859; 17081983; 17218272; 17250497; 17250498; 17392705; 17415510; 17475491; 17585203; 17592254; 17625510; 17635841; 17682539; 17850955; 17916631; 18071605; 18093976; 18172693; 18269687; 18332255; 18337729; 18533950; 18546169; 18624398; 18633133; 18651653; 18703124; 18752447; 18974562; 19050931; 19103745; 19134255; 19154529; 19179398; 19198020; 19215052; 19244360; 19271042; 19351384; 19447967; 19480685; 19538222; 19596235; 19625283; 19628962; 19648294; 19735367; 19922137; 19928837; 19997741; 20090376; 20188701; 20197730; 20301526; 20373854; 20442745; 20515750; 20563565; 20620147; 20637152; 20659551; 20696395; 20713032; 20947812; 21055263; 21082361; 21145461; 21172665; 21209906; 21233719; 21300694; 21333717; 21335981; 21338334; 21364876; 21462119; 21482919; 21496457; 21565611; 21610747; 21631299; 21672919; 21693563; 21705024; 21732698; 21785216; 21826391; 21890473; 21900206; 21906983; 21920940; 21924051; 21956898; 21963094; 22085534; 22101937; 22118674; 22124016; 22161088; 22190034; 22197680; 22323753; 22324632; 22363433; 22365833; 22454514; 22607171; 22669976; 22824686; 22884440; 22939629; 22990118; 22994313; 23000965; 23112048; 23136128; 23185376; 23221635; 23246001; 23315303; 23398456; 23438482; 23455922; 23455924; 23477310; 23496866; 23615451; 23752268; 24457600 survival of motor neuron 1, telomeric Ensembl:ENSG00000172062 HGNC:11117 HPRD:02646 MIM:600354 Vega:OTTHUMG00000099361 Other designations: component of gems 1|gemin-1|survival motor neuron 1 protein|survival motor neuron protein|tudor domain containing 16A SMN1 OGG:3000006608 Bin Zhao, Yue Liu, Oliver He FZD11 Gx SMOH WEB: http://www.ncbi.nlm.nih.gov/gene SMO smoothened, frizzled class receptor 6608 7q32.3 9606 7 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0001570 (EC: IBA); GO_0001649 (EC: IBA); GO_0001701 (EC: IEA); GO_0001708 (EC: IEA); GO_0001755 (EC: IBA); GO_0001947 (EC: ISS); GO_0002052 (EC: IBA); GO_0002053 (EC: IBA); GO_0003007 (EC: IBA); GO_0003140 (EC: ISS); GO_0003323 (EC: IEA); GO_0004930 (EC: IEA); GO_0005113 (EC: IPI, PMID: 9811851); GO_0005515 (EC: IPI, PMID: 19592253); GO_0005737 (EC: IBA); GO_0005794 (EC: IDA, Qualifier: colocalizes_with, PMID: 11278759); GO_0005886 (EC: IBA); GO_0005886 (EC: IDA, PMID: 19304771); GO_0005901 (EC: IDA, Qualifier: colocalizes_with, PMID: 11278759); GO_0005929 (EC: IBA); GO_0007224 (EC: IEP, PMID: 17850284); GO_0007224 (EC: IMP, PMID: 19304771); GO_0007228 (EC: ISS); GO_0007283 (EC: IBA); GO_0007368 (EC: IBA); GO_0007371 (EC: ISS); GO_0007494 (EC: ISS); GO_0008144 (EC: IDA, PMID: 19304771); GO_0008406 (EC: IBA); GO_0010002 (EC: IBA); GO_0010628 (EC: ISS); GO_0010629 (EC: ISS); GO_0016021 (EC: IEA); GO_0017147 (EC: IBA); GO_0021508 (EC: IBA); GO_0021561 (EC: IBA); GO_0021696 (EC: IBA); GO_0021794 (EC: IEA); GO_0021904 (EC: IBA); GO_0021910 (EC: IBA); GO_0021938 (EC: IBA); GO_0021953 (EC: IBA); GO_0021984 (EC: IBA); GO_0030165 (EC: IBA); GO_0030857 (EC: IEA); GO_0031017 (EC: IBA); GO_0031069 (EC: IEA); GO_0031076 (EC: IBA); GO_0031102 (EC: IBA); GO_0032474 (EC: IBA); GO_0034504 (EC: IEA); GO_0035264 (EC: IEA); GO_0042307 (EC: IEA); GO_0042475 (EC: IBA); GO_0042693 (EC: IBA); GO_0042813 (EC: IBA); GO_0043025 (EC: IBA); GO_0043066 (EC: IBA); GO_0043231 (EC: IDA, PMID: 11278759); GO_0043392 (EC: ISS); GO_0045880 (EC: IBA); GO_0045944 (EC: IEA); GO_0048557 (EC: IBA); GO_0048663 (EC: IBA); GO_0048702 (EC: IBA); GO_0048703 (EC: IBA); GO_0048752 (EC: IBA); GO_0048846 (EC: IBA); GO_0048853 (EC: ISS); GO_0050679 (EC: IBA); GO_0050821 (EC: IEA); GO_0051799 (EC: IEA); GO_0060070 (EC: IBA); GO_0060170 (EC: IEA); GO_0060248 (EC: IMP, PMID: 9422511); GO_0060413 (EC: IEA); GO_0060644 (EC: IEA); GO_0060684 (EC: IEA); GO_0060830 (EC: IBA); GO_0061053 (EC: ISS); GO_0061113 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0071397 (EC: ISS); GO_0072001 (EC: IEP, PMID: 17850284); GO_0072285 (EC: ISS); GO_0072372 (EC: TAS); GO_0090190 (EC: ISS); GO_2000036 (EC: IEA); GO_2000826 (EC: ISS) PMID: 8898207; 8906787; 9422511; 9581815; 9628830; 9764827; 9799615; 9811851; 11042037; 11278759; 11748145; 12123571; 12165511; 12192414; 12241103; 12477932; 12499255; 12690205; 12773389; 15489334; 15618519; 16147992; 16339184; 16344560; 16804411; 16867986; 16945339; 17850284; 17884791; 18359851; 18502968; 18543049; 19056867; 19237606; 19304771; 19351817; 19401682; 19432668; 19453261; 19473442; 19564910; 19592253; 19726788; 19730683; 20050020; 20067614; 20215540; 20561215; 20603613; 20819778; 20937227; 21210262; 21338440; 21757753; 22114142; 22231273; 22253573; 22486854; 22535603; 22864913; 22901214; 23063129; 23098507; 23334667; 23341351; 23348505; 23349881; 23379358; 23448715; 23508962; 23599646; 23636324; 23915072; 24148123; 24277750 smoothened, frizzled class receptor Ensembl:ENSG00000128602 HGNC:11119 HPRD:03294 MIM:601500 Vega:OTTHUMG00000158421 Other designations: frizzled family member 11|protein Gx|seven transmembrane helix receptor|smoothened homolog|smoothened, frizzled family receptor|smoothened, seven transmembrane spanning receptor SMO OGG:3000006609 Bin Zhao, Yue Liu, Oliver He ASM ASMASE NPD WEB: http://www.ncbi.nlm.nih.gov/gene SMPD1 sphingomyelin phosphodiesterase 1, acid lysosomal 6609 11p15.4-p15.1 9606 11 Official from a nomenclature committee GO_0004767 (EC: IEA); GO_0005515 (EC: IPI); GO_0005615 (EC: IEA); GO_0006665 (EC: TAS); GO_0006684 (EC: TAS, PMID: 7670466); GO_0006685 (EC: IEA); GO_0006687 (EC: TAS); GO_0007165 (EC: TAS, PMID: 7670466); GO_0007399 (EC: TAS, PMID: 7670466); GO_0008219 (EC: IEA); GO_0016798 (EC: IEA); GO_0023021 (EC: IMP, PMID: 19279008); GO_0035307 (EC: IMP, PMID: 19279008); GO_0042220 (EC: IEA); GO_0042493 (EC: IEA); GO_0042599 (EC: IEA); GO_0043065 (EC: IEA); GO_0043202 (EC: TAS); GO_0043407 (EC: IMP, PMID: 19279008); GO_0044281 (EC: TAS); GO_0046513 (EC: IMP, PMID: 19279011) PMID: 1292508; 1301192; 1391960; 1618760; 1711683; 1718266; 1740330; 1840600; 1885770; 2004772; 2023926; 2555181; 7670466; 8051942; 8407868; 8664904; 8680412; 8693491; 8889548; 9030779; 9110068; 11001565; 11238738; 11788605; 12208520; 12369017; 12477932; 12556236; 12631268; 12801930; 12815059; 12953170; 15175033; 15221801; 15241805; 15383576; 15509740; 15743760; 15769735; 15849201; 15877209; 15888438; 15997205; 16010684; 16051685; 16245071; 16472269; 16642440; 16787399; 17344303; 17381401; 17698617; 18052040; 18088425; 18264947; 18426979; 18628757; 18815062; 19050888; 19054571; 19059331; 19279008; 19279011; 19300439; 19322201; 19405096; 19817993; 19860808; 19878569; 19913121; 20137294; 20301544; 20386867; 20628086; 20807762; 20956541; 21098024; 21153367; 21294641; 21335555; 21900206; 22367733; 22558155; 22573858; 22613662; 22771321; 22824271; 22879933; 22890197; 22906436; 23356216; 23535491; 23618813; 23770692; 23871123 sphingomyelin phosphodiesterase 1, acid lysosomal Ensembl:ENSG00000166311 HGNC:11120 HPRD:06353 MIM:607608 Vega:OTTHUMG00000165453 Other designations: acid sphingomyelinase|sphingomyelin phosphodiesterase SMPD1 OGG:3000006696 Bin Zhao, Yue Liu, Oliver He BNSP BSPI ETA-1 OPN WEB: http://www.ncbi.nlm.nih.gov/gene SPP1 secreted phosphoprotein 1 6696 PSEC0156 4q22.1 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0001649 (EC: IEA); GO_0005125 (EC: IEA); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 15516325); GO_0006954 (EC: IEA); GO_0007155 (EC: IEA); GO_0007566 (EC: TAS, PMID: 16720713); GO_0010811 (EC: IEA); GO_0022617 (EC: TAS); GO_0030198 (EC: TAS); GO_0030593 (EC: IEA); GO_0031214 (EC: IEA); GO_0031988 (EC: IEA); GO_0033280 (EC: IDA, PMID: 16720713); GO_0042995 (EC: IEA); GO_0045177 (EC: IEA); GO_0045780 (EC: IEA); GO_0046697 (EC: TAS, PMID: 16720713); GO_0048471 (EC: IEA); GO_0048545 (EC: IEA); GO_0048685 (EC: IEA); GO_0050840 (EC: IEA) PMID: 1575754; 1729712; 1974876; 2404984; 2726470; 2736258; 2808373; 7522656; 7532190; 7592829; 7665163; 7837791; 7945249; 8195113; 8325891; 8535605; 8619474; 8663267; 8835534; 8910476; 9110174; 9547293; 9614184; 10593924; 10657301; 10673366; 10698186; 10748043; 10751402; 10766759; 10835423; 11076863; 11162551; 11375993; 11696986; 11721059; 11787071; 11801541; 11807984; 11825898; 11854181; 11861425; 11926891; 11928818; 11933203; 11940202; 11968014; 11979972; 12142743; 12377945; 12456016; 12477932; 12506143; 12527107; 12569382; 12606946; 12620651; 12640447; 12650610; 12650611; 12706004; 12761568; 12771144; 12842452; 12847283; 12879219; 12927044; 12928913; 12939547; 12949055; 12952171; 14517343; 14524533; 14534308; 14563350; 14592838; 14704150; 14706653; 14716823; 14988426; 14990565; 14996707; 15003892; 15004750; 15014008; 15019804; 15101999; 15167446; 15389974; 15479859; 15489334; 15489336; 15494684; 15501463; 15516325; 15579312; 15692970; 15696579; 15712659; 15731245; 15742429; 15742430; 15744522; 15761492; 15776015; 15845635; 15855273; 15857938; 15863395; 15868370; 15869464; 15885319; 15949549; 15954903; 15956076; 15970685; 15993098; 15998376; 15998773; 16000556; 16005200; 16009426; 16047475; 16100012; 16136472; 16145474; 16166420; 16169070; 16189514; 16199891; 16204248; 16208410; 16299231; 16303743; 16331611; 16344560; 16373617; 16381901; 16424021; 16428483; 16433860; 16489073; 16512757; 16533775; 16571650; 16614705; 16632752; 16633066; 16712791; 16713569; 16720713; 16741188; 16765311; 16786357; 16797773; 16807238; 16807684; 16817793; 16830223; 16880782; 16962083; 17005603; 17022822; 17044113; 17110905; 17130676; 17170369; 17188882; 17189522; 17227585; 17244457; 17245215; 17253181; 17289872; 17316167; 17332338; 17343740; 17360982; 17369493; 17384004; 17418101; 17439891; 17441427; 17444956; 17452979; 17464350; 17482182; 17482311; 17493236; 17496055; 17519954; 17545592; 17548669; 17565744; 17595250; 17620367; 17689681; 17696803; 17706953; 17721886; 17848618; 17852826; 17884775; 17896150; 17898038; 17938278; 17960616; 17987038; 18004082; 18037740; 18048491; 18053633; 18072945; 18079410; 18085382; 18155656; 18158320; 18160829; 18162078; 18167187; 18174176; 18178454; 18181047; 18197854; 18210151; 18210878; 18317949; 18335026; 18353318; 18388057; 18393978; 18396783; 18406574; 18410276; 18413297; 18442196; 18443355; 18459127; 18470911; 18474739; 18480255; 18493866; 18508510; 18524812; 18537194; 18549690; 18549897; 18550471; 18563556; 18593988; 18616394; 18627421; 18629582; 18651220; 18660489; 18670302; 18676742; 18682895; 18694621; 18694758; 18701136; 18722093; 18787423; 18807011; 18949741; 18952835; 18972404; 18996613; 18997126; 19010227; 19010864; 19014781; 19016748; 19017937; 19023151; 19028408; 19048398; 19076536; 19138884; 19184356; 19208558; 19212618; 19217889; 19246678; 19260859; 19281985; 19285028; 19285424; 19285954; 19287188; 19301019; 19337795; 19339987; 19340392; 19346516; 19359522; 19365701; 19366056; 19369471; 19376608; 19399415; 19400906; 19453261; 19475568; 19476604; 19528482; 19538464; 19549529; 19556240; 19562270; 19565503; 19573311; 19581305; 19593583; 19597469; 19601999; 19602039; 19603104; 19609729; 19609945; 19634115; 19638732; 19694703; 19706414; 19720619; 19740309; 19763701; 19767100; 19780053; 19781269; 19783881; 19784742; 19790060; 19798549; 19804447; 19805619; 19806573; 19813107; 19834535; 19850036; 19854170; 19885563; 19887478; 19901966; 19913121; 19948844; 19952401; 20004120; 20007708; 20008129; 20019131; 20019453; 20022267; 20037822; 20038306; 20056178; 20071328; 20074733; 20075512; 20085934; 20086024; 20101228; 20109337; 20131968; 20138033; 20144595; 20150368; 20155457; 20207476; 20219412; 20224789; 20349162; 20377868; 20378012; 20384635; 20416077; 20428925; 20453000; 20459645; 20486203; 20495387; 20501415; 20505679; 20511184; 20533542; 20545695; 20549562; 20553297; 20562127; 20576283; 20592361; 20597997; 20598232; 20625700; 20628086; 20628624; 20634891; 20638909; 20659235; 20689445; 20796249; 20819778; 20823889; 20849637; 20851233; 20863582; 20868520; 20874252; 20890897; 20921238; 20935448; 20961744; 20967421; 20967551; 20978319; 21028999; 21034455; 21044748; 21067798; 21071960; 21104439; 21152079; 21165579; 21167394; 21167650; 21174062; 21178099; 21188534; 21190594; 21207061; 21217752; 21247495; 21252118; 21263033; 21272459; 21273567; 21273622; 21290088; 21315424; 21321126; 21343932; 21365018; 21366712; 21374592; 21375772; 21397972; 21440761; 21443102; 21467192; 21469198; 21486700; 21487066; 21487672; 21501293; 21508397; 21512310; 21513757; 21520066; 21521652; 21539822; 21547579; 21556958; 21585607; 21609000; 21616556; 21630219; 21632990; 21645921; 21669963; 21673011; 21703197; 21706367; 21743018; 21763380; 21768699; 21772333; 21785824; 21796134; 21810982; 21822558; 21838826; 21842122; 21853313; 21867616; 21900386; 21909361; 21935388; 21953299; 21962803; 21963599; 21968021; 21983451; 21986140; 21988832; 21992455; 22031818; 22037483; 22037626; 22038347; 22039306; 22080623; 22093695; 22096023; 22115341; 22131818; 22158061; 22175901; 22179617; 22186244; 22207105; 22218639; 22219064; 22242114; 22261033; 22329905; 22402440; 22410369; 22421411; 22431140; 22456539; 22458913; 22461132; 22490528; 22492090; 22495819; 22499302; 22510874; 22516995; 22525502; 22530059; 22558919; 22580396; 22584029; 22591637; 22611763; 22629140; 22658130; 22675553; 22684781; 22699784; 22710694; 22711477; 22730056; 22744661; 22779921; 22784028; 22807608; 22818182; 22835614; 22844418; 22847114; 22855173; 22882568; 22895562; 22918393; 22927944; 22935225; 22960022; 22964303; 22978720; 23008732; 23033660; 23055574; 23064961; 23071279; 23072570; 23074199; 23079960; 23089492; 23097037; 23098767; 23112867; 23119061; 23122494; 23132541; 23165334; 23166604; 23203407; 23204518; 23232694; 23235966; 23244138; 23251004; 23263636; 23269624; 23274598; 23284864; 23352191; 23354516; 23361573; 23373240; 23382482; 23388534; 23407481; 23416968; 23426449; 23427088; 23437160; 23441154; 23515922; 23545719; 23589674; 23619316; 23619422; 23636305; 23652051; 23675517; 23680656; 23692545; 23717583; 23726130; 23729174; 23764959; 23774402; 23775819; 23784265; 23867349; 23880208; 23883434; 23910387; 23952692; 24084099; 24126938; 24140708; 24157812; 24188933; 24240095 secreted phosphoprotein 1 Ensembl:ENSG00000118785 HGNC:11255 HPRD:01325 MIM:166490 Vega:OTTHUMG00000130599 SPP1 OGG:3000006720 Bin Zhao, Yue Liu, Oliver He SREBP-1c SREBP1 bHLHd1 WEB: http://www.ncbi.nlm.nih.gov/gene SREBF1 sterol regulatory element binding transcription factor 1 6720 17p11.2 9606 17 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0000139 (EC: TAS); GO_0003062 (EC: IEA); GO_0003677 (EC: ISS); GO_0003682 (EC: IEA); GO_0003700 (EC: IDA, PMID: 16407292); GO_0005515 (EC: IPI, PMID: 14701856); GO_0005634 (EC: IDA, PMID: 12202038); GO_0005635 (EC: TAS, PMID: 8156598); GO_0005654 (EC: TAS); GO_0005737 (EC: ISS); GO_0005783 (EC: IDA, PMID: 12202038); GO_0005789 (EC: TAS); GO_0005829 (EC: TAS); GO_0006351 (EC: IEA); GO_0006357 (EC: TAS, PMID: 8156598); GO_0006629 (EC: TAS, PMID: 8156598); GO_0007568 (EC: IEA); GO_0008203 (EC: IEA); GO_0008286 (EC: IEA); GO_0008610 (EC: ISS); GO_0009267 (EC: ISS, PMID: 16407292); GO_0009749 (EC: IEA); GO_0010867 (EC: ISS); GO_0012507 (EC: IEA); GO_0016021 (EC: IEA); GO_0019217 (EC: IEA); GO_0019901 (EC: IEA); GO_0030324 (EC: IEA); GO_0031065 (EC: IEA); GO_0032094 (EC: IEA); GO_0032403 (EC: IEA); GO_0032526 (EC: IEA); GO_0032570 (EC: IEA); GO_0032810 (EC: IDA, PMID: 16407292); GO_0033762 (EC: IEA); GO_0042493 (EC: IEA); GO_0043234 (EC: IEA); GO_0043565 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0045542 (EC: IEA); GO_0045944 (EC: IDA, PMID: 12242332); GO_0045944 (EC: IEA); GO_0046676 (EC: IEA); GO_0046983 (EC: IEA); GO_0051591 (EC: IEA); GO_0071398 (EC: IEA) PMID: 7759101; 7903453; 8006035; 8156598; 8314806; 8402897; 8626610; 8918891; 9062340; 9070916; 9242699; 9634703; 9651391; 9765204; 10224053; 10235267; 10585876; 10619424; 10627507; 10915800; 10949029; 11257259; 11334418; 11485982; 11713202; 11834832; 11916923; 11929849; 11997338; 12021179; 12145339; 12177166; 12202038; 12213084; 12242332; 12436350; 12477932; 12531699; 12615929; 12640139; 12657626; 12730330; 12752570; 14615581; 14633850; 14654692; 14701856; 14702039; 14722127; 14742839; 14744869; 14747281; 14748724; 14988272; 15026365; 15085196; 15102555; 15123650; 15161980; 15277400; 15286454; 15317819; 15340088; 15358760; 15388640; 15550381; 15677507; 15769984; 15794649; 15798184; 15809359; 15833942; 16005884; 16007182; 16054087; 16055439; 16141315; 16153721; 16158080; 16162944; 16198472; 16249184; 16303770; 16306078; 16387548; 16407292; 16429400; 16480961; 16713569; 16799563; 16804073; 16806233; 16817902; 16825193; 16880739; 16885156; 17019602; 17081983; 17141191; 17160088; 17198935; 17296605; 17331464; 17344645; 17452746; 17636037; 17655842; 17681345; 17989724; 18065496; 18068676; 18072016; 18192539; 18195716; 18245227; 18267114; 18272927; 18281474; 18304434; 18334917; 18360697; 18385733; 18403372; 18420801; 18435918; 18559965; 18635549; 18654640; 18660489; 18682402; 18692268; 18727921; 18752865; 18774944; 18835813; 18854425; 18936756; 18996102; 19008011; 19032865; 19040658; 19048273; 19056350; 19056482; 19062325; 19126544; 19242521; 19252981; 19292868; 19303849; 19323650; 19336475; 19360318; 19470430; 19533843; 19578796; 19621387; 19720801; 19727213; 19727227; 19733654; 19811452; 19876004; 19878569; 19913121; 19913854; 19948975; 19966780; 20005944; 20026048; 20028734; 20031551; 20067991; 20071336; 20130133; 20145241; 20167577; 20171215; 20173757; 20235787; 20376806; 20466882; 20513236; 20534441; 20554776; 20595232; 20615871; 20628086; 20648548; 20655124; 20817729; 20863500; 20868688; 20965718; 20971080; 20980003; 21093473; 21139048; 21145868; 21146170; 21310851; 21325464; 21540177; 21609284; 21619898; 21645898; 21652712; 21664250; 21693764; 21738487; 21757781; 21775116; 21826653; 21836065; 21871872; 21906983; 21963094; 21987572; 21993218; 22035958; 22059152; 22064655; 22152380; 22153697; 22258239; 22311022; 22331133; 22363740; 22384276; 22425645; 22429355; 22474125; 22505724; 22672904; 22678801; 22690709; 22786746; 22939624; 22966071; 22969152; 22984430; 23000965; 23106379; 23147115; 23208501; 23226416; 23422505; 23465592; 23515281; 23610160; 23680128; 23703028; 23825667; 23913732; 23985808; 24298052 sterol regulatory element binding transcription factor 1 Ensembl:ENSG00000072310 HGNC:11289 HPRD:01701 MIM:184756 Vega:OTTHUMG00000059313 Other designations: SREBP-1|class D basic helix-loop-helix protein 1|sterol regulatory element-binding protein 1 SREBF1 OGG:3000006733 Bin Zhao, Yue Liu, Oliver He SFRSK2 WEB: http://www.ncbi.nlm.nih.gov/gene SRPK2 SRSF protein kinase 2 6733 7q22-q31.1 9606 7 Official from a nomenclature committee GO_0000245 (EC: IDA, PMID: 9472028); GO_0000287 (EC: IDA, PMID: 9472028); GO_0001525 (EC: ISS); GO_0004674 (EC: IDA, PMID: 9472028); GO_0005515 (EC: IPI, PMID: 16189514); GO_0005524 (EC: IDA, PMID: 9472028); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0006468 (EC: IDA, PMID: 9472028); GO_0008284 (EC: IDA, PMID: 18559500); GO_0008380 (EC: IDA, PMID: 9472028); GO_0010628 (EC: ISS); GO_0030154 (EC: IEA); GO_0035063 (EC: ISS); GO_0035556 (EC: IDA, PMID: 9472028); GO_0043525 (EC: ISS); GO_0044822 (EC: IDA); GO_0045070 (EC: IDA); GO_0045071 (EC: IDA, PMID: 12417631); GO_0045087 (EC: IC, PMID: 12417631); GO_0045787 (EC: ISS); GO_0048024 (EC: TAS); GO_0071889 (EC: ISS) PMID: 8208298; 9171351; 9446799; 9472028; 10196197; 12134018; 12417631; 12477932; 12565863; 12853948; 14702039; 15144186; 15489334; 15592455; 16122776; 16189514; 16344560; 17353931; 17620599; 18029348; 18425142; 18559500; 18654987; 19592491; 19902070; 20379614; 20498328; 21145461; 21157427; 21182205; 21832049; 21890473; 22365833; 22990118; 23000965; 23049088; 23326445; 23602568; 24457600 SRSF protein kinase 2 Ensembl:ENSG00000135250 HGNC:11306 HPRD:04280 MIM:602980 Vega:OTTHUMG00000157405 Other designations: SFRS protein kinase 2|SR protein kinase 2|SR-protein-specific kinase 2|serine kinase SRPK2|serine/arginine-rich protein-specific kinase 2|serine/arginine-rich splicing factor kinase 2|serine/threonine-protein kinase SRPK2 SRPK2 OGG:3000006742 Bin Zhao, Yue Liu, Oliver He Mt-SSB SOSS-B1 SSBP mtSSB WEB: http://www.ncbi.nlm.nih.gov/gene SSBP1 single-stranded DNA binding protein 1, mitochondrial 6742 7q34 9606 7 Official from a nomenclature committee GO_0003682 (EC: IDA, PMID: 18063578); GO_0003697 (EC: IEA); GO_0005515 (EC: IPI); GO_0005739 (EC: IDA); GO_0006260 (EC: IEA); GO_0042645 (EC: IDA, PMID: 18063578); GO_0044822 (EC: IDA); GO_0051096 (EC: IDA, PMID: 12975372); GO_0070062 (EC: IDA); GO_0070584 (EC: IEA) PMID: 7789991; 8482537; 9033597; 9452467; 10827171; 11556757; 11964388; 12381786; 12464025; 12477932; 12479417; 12690205; 12853948; 12975372; 15161933; 15342556; 15489334; 15710247; 16407974; 16428295; 18029348; 18063578; 18305033; 18457437; 19066201; 19167051; 19605351; 19683501; 19738201; 19759019; 19786724; 20000738; 20028516; 20100872; 20186120; 20360068; 20434493; 20639865; 20843780; 20877624; 20972266; 21139048; 21145461; 21150319; 21242961; 21319273; 21360678; 21890473; 21906983; 21953457; 22153281; 22190034; 22242598; 22354994; 22505724; 22939629; 23000965; 23042605; 23184057; 23246001; 23290262; 23398456; 23438482; 23568457; 24244333 single-stranded DNA binding protein 1, mitochondrial Ensembl:ENSG00000106028 HGNC:11317 HPRD:02703 MIM:600439 Vega:OTTHUMG00000157572 Other designations: PWP1-interacting protein 17|single-stranded DNA-binding protein, mitochondrial SSBP1 OGG:3000006747 Bin Zhao, Yue Liu, Oliver He TRAPG WEB: http://www.ncbi.nlm.nih.gov/gene SSR3 signal sequence receptor, gamma (translocon-associated protein gamma) 6747 3q25.31 9606 3 Official from a nomenclature committee GO_0005784 (EC: IEA); GO_0006412 (EC: TAS); GO_0006614 (EC: TAS); GO_0010467 (EC: TAS); GO_0030176 (EC: IEA); GO_0044267 (EC: TAS) PMID: 7916687; 9631292; 10471800; 12477932; 14667819; 15489334; 16344560; 17081983; 17353931; 18781797; 18976975; 19615732; 21139048; 21906983; 21963094; 22632162; 22939629; 23000965; 23660295 signal sequence receptor, gamma (translocon-associated protein gamma) Ensembl:ENSG00000114850 HGNC:11325 HPRD:16206 MIM:606213 Vega:OTTHUMG00000158632 Other designations: SSR gamma|SSR-gamma|TRAP-complex gamma subunit|TRAP-gamma|signal sequence receptor subunit gamma|translocon-associated protein gamma subunit|translocon-associated protein subunit gamma SSR3 OGG:3000006772 Bin Zhao, Yue Liu, Oliver He CANDF7 ISGF-3 STAT91 WEB: http://www.ncbi.nlm.nih.gov/gene STAT1 signal transducer and activator of transcription 1, 91kDa 6772 2q32.2 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0000122 (EC: ISS); GO_0000790 (EC: IDA, PMID: 18035482); GO_0000978 (EC: IDA, PMID: 18035482); GO_0000979 (EC: IDA); GO_0000983 (EC: IDA); GO_0001937 (EC: IMP, PMID: 16585190); GO_0002053 (EC: ISS); GO_0003340 (EC: ISS); GO_0003690 (EC: IDA, PMID: 9630226); GO_0003700 (EC: IDA, PMID: 10820245); GO_0003700 (EC: IDA, Qualifier: NOT, PMID: 10820245); GO_0004871 (EC: IEA); GO_0005164 (EC: IPI, PMID: 10848577); GO_0005509 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10848577); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006357 (EC: IDA, Qualifier: NOT, PMID: 10820245); GO_0006366 (EC: IDA); GO_0006915 (EC: ISS); GO_0007259 (EC: IDA); GO_0007584 (EC: IEA); GO_0008015 (EC: ISS); GO_0009612 (EC: IEA); GO_0016032 (EC: IEA); GO_0016525 (EC: IMP, PMID: 16585190); GO_0019221 (EC: TAS); GO_0019899 (EC: IPI); GO_0030424 (EC: ISS); GO_0030425 (EC: ISS); GO_0031663 (EC: IEA); GO_0031730 (EC: IEA); GO_0032869 (EC: IEA); GO_0033209 (EC: IDA, PMID: 10848577); GO_0034097 (EC: ISS); GO_0034240 (EC: IEA); GO_0035458 (EC: IMP, PMID: 18035482); GO_0042493 (EC: IEA); GO_0042542 (EC: IEA); GO_0042802 (EC: IPI, PMID: 8605877); GO_0042803 (EC: IDA, PMID: 9630226); GO_0042981 (EC: TAS, PMID: 12108949); GO_0043124 (EC: IMP, PMID: 10848577); GO_0043330 (EC: IEA); GO_0043434 (EC: ISS); GO_0043542 (EC: IMP, Qualifier: NOT, PMID: 16585190); GO_0045893 (EC: IDA, PMID: 10973496); GO_0045944 (EC: IDA, PMID: 10820245); GO_0045944 (EC: IMP, PMID: 18035482); GO_0048661 (EC: ISS); GO_0051591 (EC: ISS); GO_0051607 (EC: IEA); GO_0060333 (EC: IDA); GO_0060333 (EC: ISS); GO_0060333 (EC: TAS); GO_0060334 (EC: TAS); GO_0060337 (EC: ISS); GO_0060337 (EC: TAS); GO_0060338 (EC: TAS); GO_0060397 (EC: TAS); GO_0061326 (EC: IMP); GO_0072136 (EC: ISS); GO_0072162 (EC: ISS); GO_0072308 (EC: ISS) PMID: 1496401; 1502203; 7510216; 7514165; 7543024; 7657660; 7690989; 7885841; 8125298; 8232552; 8549654; 8605877; 8608597; 8621447; 8631962; 8889548; 8943351; 8986769; 9037008; 9069288; 9121453; 9135145; 9205132; 9284918; 9344858; 9355737; 9373245; 9452495; 9484840; 9584171; 9630226; 9724754; 9804857; 9843502; 9880553; 9925928; 9989503; 10067896; 10358045; 10358079; 10446176; 10464260; 10490649; 10490982; 10506573; 10602027; 10652206; 10692450; 10702714; 10764778; 10792030; 10805787; 10820245; 10848577; 10848598; 10851046; 10851062; 10918587; 10954736; 10961983; 10964507; 10973496; 10982844; 11152457; 11226159; 11238845; 11248027; 11257227; 11278462; 11278865; 11294897; 11301323; 11418623; 11438544; 11442634; 11452125; 11520787; 11594781; 11675348; 11722592; 11752148; 11777927; 11804954; 11815625; 11835405; 11839738; 11843291; 11886859; 11909852; 11909970; 11923478; 11927559; 11932384; 11972023; 11981818; 12039028; 12048190; 12070153; 12108949; 12130529; 12138178; 12161037; 12165521; 12167251; 12171910; 12191570; 12223098; 12232043; 12232802; 12270932; 12356736; 12388709; 12403783; 12426389; 12447867; 12459177; 12477932; 12539042; 12551969; 12590259; 12610144; 12629155; 12634403; 12637327; 12722480; 12734330; 12748293; 12759242; 12777975; 12788789; 12804771; 12807916; 12817007; 12832402; 12846741; 12855573; 12855578; 12856330; 12867595; 12917439; 12923054; 12948935; 12960323; 12963127; 12967644; 14499622; 14500749; 14517261; 14557668; 14599788; 14600148; 14623896; 14654078; 14654702; 14656722; 14657353; 14674010; 14688135; 14690454; 14702039; 14704793; 14746803; 14751560; 14755057; 14963018; 14976049; 14978237; 15010467; 15055356; 15123634; 15140960; 15146197; 15165826; 15210729; 15213094; 15217838; 15221897; 15280488; 15284024; 15284440; 15322115; 15467722; 15489334; 15494521; 15527154; 15604419; 15638726; 15650219; 15695802; 15778351; 15780933; 15784679; 15795279; 15824515; 15825084; 15894584; 15919942; 15979846; 15996661; 15998520; 16009940; 16077199; 16148108; 16148142; 16189514; 16195225; 16195385; 16223733; 16236267; 16254375; 16257975; 16260419; 16273093; 16298512; 16306601; 16318585; 16335966; 16344560; 16388135; 16467883; 16481475; 16501077; 16511123; 16512786; 16531398; 16571725; 16572323; 16574066; 16585190; 16628196; 16703666; 16773129; 16799645; 16878149; 16897667; 16904741; 16918696; 16934001; 16935931; 16940534; 16951379; 16978698; 17030574; 17075845; 17145596; 17182865; 17196131; 17227821; 17237409; 17266440; 17287281; 17346710; 17351669; 17353931; 17371985; 17386941; 17427945; 17442890; 17475642; 17486072; 17490620; 17523873; 17538964; 17561467; 17596301; 17617740; 17620599; 17640695; 17680769; 17686504; 17703412; 17726060; 17804871; 17878351; 17897103; 17909067; 17918184; 17923090; 17928350; 17933493; 17938255; 17983380; 17986321; 18003888; 18029348; 18035482; 18037959; 18062835; 18218993; 18225539; 18280748; 18305014; 18305569; 18338947; 18348986; 18370868; 18381204; 18401423; 18424756; 18463151; 18483262; 18500930; 18566411; 18579584; 18586252; 18591661; 18633131; 18660489; 18676680; 18723680; 18771758; 18775329; 18787082; 18787531; 18789440; 18803832; 18818378; 18832710; 18950845; 18989459; 19007958; 19012493; 19017763; 19041714; 19046253; 19074829; 19088846; 19100922; 19124747; 19131965; 19170196; 19171783; 19211553; 19223260; 19231233; 19258923; 19279332; 19333953; 19342095; 19351818; 19380416; 19393742; 19404407; 19423540; 19424608; 19434718; 19436109; 19437244; 19439556; 19453261; 19464956; 19471022; 19478064; 19479051; 19502801; 19508864; 19515782; 19553685; 19561067; 19574556; 19582813; 19594299; 19596857; 19604093; 19622834; 19625176; 19646959; 19647793; 19652026; 19656875; 19667270; 19691533; 19692168; 19781967; 19801665; 19802007; 19834108; 19853614; 19857525; 19891767; 19913121; 19915063; 19915608; 19935876; 20011528; 20045654; 20065083; 20093796; 20098684; 20103601; 20180146; 20195357; 20211142; 20225206; 20331378; 20345984; 20347693; 20353823; 20379614; 20380698; 20403236; 20406964; 20428775; 20438785; 20457620; 20503287; 20519510; 20523058; 20562129; 20568281; 20576130; 20588308; 20624457; 20628086; 20628624; 20662656; 20798561; 20802378; 20810735; 20814891; 20829351; 20832538; 20833730; 20841510; 20936779; 20937132; 20937272; 20949125; 20974984; 20980339; 21056555; 21057861; 21079652; 21084836; 21091911; 21099673; 21115047; 21139048; 21207025; 21288140; 21303487; 21307288; 21311224; 21321110; 21346151; 21354905; 21362620; 21368418; 21372127; 21385873; 21466707; 21477834; 21533215; 21571862; 21572044; 21576370; 21593149; 21674123; 21689637; 21690236; 21697347; 21714643; 21727188; 21734056; 21752694; 21772053; 21795355; 21796151; 21886773; 21890473; 21903422; 21906983; 21937453; 21988832; 22002246; 22022391; 22025054; 22038351; 22065572; 22115721; 22174846; 22178447; 22193460; 22194871; 22195034; 22217266; 22242177; 22253910; 22262126; 22320867; 22326919; 22381273; 22383882; 22401175; 22407921; 22425562; 22437822; 22474288; 22479354; 22488367; 22505724; 22514085; 22526675; 22535619; 22539792; 22558273; 22573496; 22647704; 22674974; 22693070; 22730530; 22748021; 22748593; 22757586; 22797925; 22805310; 22808166; 22811740; 22828446; 22833565; 22838736; 22844427; 22863883; 22920460; 22939629; 22942432; 22973045; 23000965; 23043228; 23068100; 23072252; 23076242; 23086340; 23108375; 23128233; 23153456; 23154639; 23180800; 23240025; 23271704; 23274199; 23306614; 23349666; 23363816; 23378427; 23383273; 23401241; 23403048; 23452095; 23471820; 23486482; 23487038; 23534974; 23541320; 23554911; 23582260; 23585528; 23588992; 23609054; 23621408; 23703473; 23704922; 23708675; 23740952; 23741352; 23756862; 23856440; 23910645; 23920124; 23940278; 23941832; 23956138; 23958647; 23984931; 24449862 signal transducer and activator of transcription 1, 91kDa Ensembl:ENSG00000115415 HGNC:11362 HPRD:02777 MIM:600555 Vega:OTTHUMG00000132699 Other designations: signal transducer and activator of transcription 1-alpha/beta|signal transducer and activator of transcription-1|transcription factor ISGF-3 components p91/p84 STAT1 OGG:3000006774 Bin Zhao, Yue Liu, Oliver He APRF HIES WEB: http://www.ncbi.nlm.nih.gov/gene STAT3 signal transducer and activator of transcription 3 (acute-phase response factor) 6774 17q21.31 9606 17 Official from a nomenclature committee GO_0000122 (EC: TAS, PMID: 8675499); GO_0001103 (EC: IPI); GO_0001659 (EC: ISS); GO_0001754 (EC: ISS); GO_0003677 (EC: ISS); GO_0003700 (EC: TAS, PMID: 7512451); GO_0004871 (EC: IEA); GO_0004879 (EC: IDA, PMID: 17324931); GO_0005509 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10688651); GO_0005634 (EC: IDA); GO_0005634 (EC: ISS); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005737 (EC: ISS); GO_0005829 (EC: TAS); GO_0005886 (EC: ISS); GO_0006355 (EC: IDA, PMID: 15664994); GO_0006357 (EC: ISS); GO_0006606 (EC: IDA, PMID: 18234692); GO_0006928 (EC: TAS, PMID: 9670957); GO_0006953 (EC: IEA); GO_0007165 (EC: TAS, PMID: 10205054); GO_0007259 (EC: TAS, PMID: 15664994); GO_0007399 (EC: TAS, PMID: 10205054); GO_0008134 (EC: IPI, PMID: 15664994); GO_0008283 (EC: IEA); GO_0016032 (EC: IEA); GO_0016310 (EC: ISS); GO_0019221 (EC: NAS, PMID: 15664994); GO_0019827 (EC: IEA); GO_0019901 (EC: ISS); GO_0019903 (EC: IPI, PMID: 12359225); GO_0019953 (EC: ISS); GO_0030522 (EC: IDA, PMID: 17324931); GO_0031730 (EC: IEA); GO_0032355 (EC: IDA, PMID: 12552091); GO_0032870 (EC: IDA, PMID: 12552091); GO_0035259 (EC: IEA); GO_0040014 (EC: IEA); GO_0042493 (EC: IEA); GO_0042593 (EC: ISS); GO_0042755 (EC: ISS); GO_0043565 (EC: IEA); GO_0044212 (EC: IDA, PMID: 17324931); GO_0045471 (EC: IEA); GO_0045747 (EC: ISS); GO_0045893 (EC: ISS); GO_0045944 (EC: IDA, PMID: 17324931); GO_0046983 (EC: ISS); GO_0048011 (EC: TAS); GO_0048708 (EC: ISS); GO_0060019 (EC: ISS); GO_0060396 (EC: IDA, PMID: 10925297); GO_0060397 (EC: IDA, PMID: 12552091); GO_0060397 (EC: ISS); GO_0060397 (EC: TAS); GO_0060548 (EC: IEA); GO_0070102 (EC: IDA, PMID: 12359225); GO_2001223 (EC: IEA) PMID: 3031469; 7512451; 7624343; 7701321; 7719938; 8140422; 8272872; 8608603; 8626374; 8626489; 8631962; 8657134; 8675499; 8889548; 8921406; 8923468; 9162009; 9211920; 9343414; 9373245; 9388192; 9398404; 9440692; 9484840; 9566874; 9584171; 9630560; 9647732; 9670957; 9714332; 9724754; 9756944; 9864141; 9872331; 9917912; 9923604; 9989503; 10037026; 10205054; 10358079; 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15615703; 15629435; 15638726; 15643501; 15649887; 15650183; 15653507; 15659654; 15664994; 15665295; 15673499; 15677471; 15677474; 15682485; 15688010; 15735682; 15735720; 15735721; 15736426; 15764709; 15809078; 15821101; 15837065; 15845643; 15870198; 15878791; 15882975; 15894558; 15895073; 15905571; 15912144; 15917293; 15923602; 15935090; 15936715; 15944400; 15950906; 15951569; 15958548; 15979846; 15994929; 16007214; 16036105; 16061629; 16061651; 16081048; 16082218; 16098628; 16107692; 16125646; 16140268; 16142329; 16174774; 16186805; 16192633; 16231698; 16236134; 16236267; 16260903; 16273093; 16278387; 16285960; 16298512; 16306601; 16331268; 16377083; 16381901; 16382134; 16401721; 16407171; 16425286; 16432158; 16503733; 16512876; 16524883; 16531398; 16557588; 16568091; 16571725; 16619044; 16636048; 16651533; 16685378; 16709613; 16732314; 16807407; 16825495; 16828865; 16835372; 16840717; 16841088; 16861352; 16871275; 16877361; 16887796; 16904741; 16926159; 16931573; 16935931; 16946298; 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20196786; 20197401; 20199106; 20200543; 20204302; 20209132; 20211142; 20213502; 20222910; 20229017; 20232316; 20237496; 20301786; 20331378; 20331635; 20348091; 20351189; 20356901; 20359118; 20368117; 20371693; 20379614; 20380698; 20388777; 20399615; 20406964; 20422486; 20431064; 20438785; 20446017; 20447714; 20456494; 20459702; 20463008; 20463292; 20473906; 20483734; 20484656; 20490271; 20490331; 20503287; 20507639; 20514402; 20515335; 20516069; 20516148; 20519510; 20546860; 20558345; 20562100; 20568281; 20585009; 20618440; 20627814; 20628086; 20628624; 20634891; 20652679; 20661303; 20663948; 20668024; 20686606; 20691278; 20709283; 20716621; 20797623; 20802378; 20807804; 20816194; 20826784; 20830236; 20830487; 20860602; 20872151; 20873541; 20873543; 20881637; 20886065; 20888416; 20929863; 20930550; 20939893; 20942237; 20943775; 20962850; 20974051; 20977777; 20978825; 21058221; 21068102; 21072187; 21072904; 21085192; 21098664; 21098725; 21102463; 21115047; 21122157; 21131551; 21138684; 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23504318; 23514705; 23526220; 23531596; 23531921; 23533997; 23545262; 23548897; 23555696; 23555719; 23563237; 23573315; 23583378; 23590971; 23590999; 23591770; 23604529; 23612755; 23613996; 23614738; 23618357; 23622344; 23623921; 23628554; 23633489; 23636127; 23636231; 23639951; 23650499; 23653350; 23659370; 23665025; 23665320; 23673666; 23674871; 23676499; 23677069; 23681230; 23703790; 23704922; 23716595; 23725032; 23734190; 23736381; 23740979; 23741012; 23756862; 23768868; 23782265; 23788661; 23791019; 23807222; 23820254; 23824569; 23824571; 23830147; 23856509; 23861822; 23874455; 23902772; 23904224; 23907460; 23911788; 23919497; 23920124; 23923047; 23926297; 23941832; 23941877; 23953057; 23956138; 23962558; 23966384; 23982944; 23984931; 23995109; 24004609; 24005672; 24027425; 24036113; 24048798; 24067369; 24082147; 24101550; 24114793; 24122993; 24123009; 24127267; 24135280; 24157808; 24158981; 24159173; 24184145; 24211205; 24218138; 24307657; 24315995; 24328557; 24342613; 24374144; 24395800; 24462277 signal transducer and activator of transcription 3 (acute-phase response factor) Ensembl:ENSG00000168610 HGNC:11364 HPRD:00026 MIM:102582 Vega:OTTHUMG00000150645 Other designations: DNA-binding protein APRF|acute-phase response factor|signal transducer and activator of transcription 3 STAT3 OGG:3000006782 Bin Zhao, Yue Liu, Oliver He STCH WEB: http://www.ncbi.nlm.nih.gov/gene HSPA13 heat shock protein 70kDa family, member 13 6782 21q11 9606 21 Official from a nomenclature committee GO_0005524 (EC: IEA); GO_0005783 (EC: IEA); GO_0043231 (EC: TAS, PMID: 8131751); GO_0070062 (EC: IDA, PMID: 19199708) PMID: 8125298; 8131751; 8825657; 8889548; 8889549; 10675567; 10830953; 11319647; 12107410; 12477932; 14702039; 15489334; 16087163; 16189514; 16713569; 18793616; 19199708; 19793966; 21139048; 21900206; 21988832; 22190034; 23303189 heat shock protein 70kDa family, member 13 Ensembl:ENSG00000155304 HGNC:11375 HPRD:03061 MIM:601100 Vega:OTTHUMG00000074261 Other designations: heat shock 70 kDa protein 13|microsomal stress 70 protein ATPase core|microsomal stress-70 protein ATPase core|stress 70 protein chaperone, microsome-associated, 60kD|stress 70 protein chaperone, microsome-associated, 60kDa|stress-70 protein chaperone microsome-associated 60 kDa protein HSPA13 OGG:3000006794 Bin Zhao, Yue Liu, Oliver He LKB1 PJS hLKB1 WEB: http://www.ncbi.nlm.nih.gov/gene STK11 serine/threonine kinase 11 6794 19p13.3 9606 19 Official from a nomenclature committee GO_0000287 (EC: IDA, PMID: 12805220); GO_0001558 (EC: ISS); GO_0001894 (EC: IEA); GO_0001944 (EC: ISS); GO_0002039 (EC: IDA, PMID: 11430832); GO_0004674 (EC: IDA, PMID: 11430832); GO_0004674 (EC: TAS); GO_0005515 (EC: IPI, PMID: 12595760); GO_0005524 (EC: IDA, PMID: 12805220); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA, PMID: 11430832); GO_0005739 (EC: IDA, PMID: 11430832); GO_0005829 (EC: ISS); GO_0005829 (EC: TAS); GO_0006112 (EC: TAS); GO_0006468 (EC: IDA, PMID: 12805220); GO_0006914 (EC: IEA); GO_0006974 (EC: IEA); GO_0007050 (EC: IDA, PMID: 12805220); GO_0007050 (EC: TAS); GO_0007286 (EC: IEA); GO_0007409 (EC: IEA); GO_0008285 (EC: IMP, PMID: 17216128); GO_0008286 (EC: TAS); GO_0010212 (EC: ISS); GO_0016020 (EC: ISS); GO_0030010 (EC: ISS); GO_0030111 (EC: IEA); GO_0030275 (EC: IEA); GO_0030295 (EC: IDA, PMID: 19892943); GO_0030308 (EC: ISS); GO_0030511 (EC: IMP, PMID: 18311138); GO_0032147 (EC: IDA, PMID: 18854309); GO_0032147 (EC: IEA); GO_0032403 (EC: IEA); GO_0033762 (EC: IEA); GO_0033993 (EC: IEA); GO_0036398 (EC: IEA); GO_0036399 (EC: IEA); GO_0042304 (EC: TAS); GO_0042593 (EC: ISS); GO_0043276 (EC: IMP, PMID: 19622832); GO_0044281 (EC: TAS); GO_0045059 (EC: IEA); GO_0045722 (EC: IEA); GO_0046777 (EC: IDA, PMID: 11430832); GO_0050731 (EC: IEA); GO_0050772 (EC: IEA); GO_0050852 (EC: IEA); GO_0051291 (EC: IEA); GO_0051645 (EC: IEA); GO_0051896 (EC: IEA); GO_0060070 (EC: IEA); GO_0060770 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867); GO_0072332 (EC: IDA, PMID: 11430832) PMID: 8889548; 8988175; 9425897; 9428765; 9537235; 9760200; 9837816; 10208439; 10362809; 10408777; 10508479; 10642499; 10642527; 11297520; 11430832; 11445556; 11668633; 11733352; 11741830; 11853558; 12097271; 12218179; 12234250; 12477932; 12489981; 12533684; 12552571; 12595760; 12753905; 12805220; 12847291; 12879020; 12912948; 14511394; 14511408; 14517247; 14517248; 14668798; 14676191; 14702039; 14976552; 14985505; 15077168; 15121768; 15183188; 15188174; 15231735; 15287029; 15292028; 15331174; 15485651; 15489334; 15561763; 15607222; 15608654; 15617552; 15731909; 15733851; 15774015; 15800014; 15987703; 16054041; 16169070; 16287113; 16311241; 16396636; 16407220; 16407837; 16540748; 16580634; 16582077; 16648371; 16822578; 16882735; 16912160; 16927138; 16953221; 17010524; 17026623; 17098823; 17108107; 17114342; 17212587; 17216128; 17234589; 17244606; 17319781; 17344591; 17384680; 17573348; 17575127; 17599048; 17637250; 17641416; 17676035; 17711506; 17766436; 17884763; 17921699; 17928927; 17950019; 18000088; 18029348; 18199157; 18245474; 18256292; 18303014; 18311138; 18321849; 18403917; 18483235; 18495044; 18594528; 18600394; 18676680; 18681789; 18687677; 18794113; 18854309; 18854318; 19029933; 19056867; 19068194; 19145097; 19165201; 19170196; 19177591; 19204826; 19229701; 19250387; 19287990; 19340305; 19351817; 19369417; 19386264; 19407487; 19414597; 19463221; 19507030; 19513107; 19520843; 19584313; 19615099; 19615732; 19622832; 19625176; 19692168; 19724060; 19727776; 19892943; 19908348; 20010869; 20018878; 20020146; 20057966; 20082862; 20193846; 20207041; 20227367; 20301443; 20354225; 20357370; 20368287; 20368693; 20400510; 20418665; 20423848; 20424326; 20428811; 20435009; 20452353; 20489196; 20497868; 20559149; 20562859; 20623358; 20668229; 20682687; 20686846; 20722467; 20818976; 20864035; 20881644; 20939895; 20956321; 20974850; 21048031; 21102257; 21118512; 21150337; 21191146; 21191700; 21192934; 21241696; 21396365; 21450399; 21532627; 21572398; 21706049; 21816872; 21832049; 21860411; 21876548; 21994947; 22005930; 22118009; 22168747; 22226967; 22265968; 22270359; 22384927; 22412893; 22457270; 22460425; 22487816; 22543132; 22575644; 22635025; 22775437; 22814264; 22848740; 22928647; 22939624; 22942091; 22983157; 22986809; 22988252; 23027127; 23044421; 23074285; 23086944; 23207623; 23322200; 23367447; 23393134; 23399955; 23415580; 23430953; 23451056; 23526220; 23572524; 23592276; 23612973; 23637231; 23645358; 23648482; 23679304; 23706335; 23788249; 23810581; 23861764; 23878245; 23892522; 24074562; 24154639; 24285539; 24362629 serine/threonine kinase 11 Ensembl:ENSG00000118046 HGNC:11389 HPRD:03740 MIM:602216 Vega:OTTHUMG00000180118 Other designations: liver kinase B1|polarization-related protein LKB1|renal carcinoma antigen NY-REN-19|serine/threonine-protein kinase 11|serine/threonine-protein kinase LKB1|serine/threonine-protein kinase STK11 STK11 OGG:3000006819 Bin Zhao, Yue Liu, Oliver He ST1C1 ST1C2 SULT1C1 humSULTC2 WEB: http://www.ncbi.nlm.nih.gov/gene SULT1C2 sulfotransferase family, cytosolic, 1C, member 2 6819 2q12.3 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0005737 (EC: TAS, PMID: 9169148); GO_0005829 (EC: TAS); GO_0006805 (EC: TAS); GO_0008146 (EC: IDA); GO_0009308 (EC: TAS, PMID: 9169148); GO_0044281 (EC: TAS); GO_0050427 (EC: TAS); GO_0051923 (EC: IDA) PMID: 7642552; 9034160; 9169148; 9635888; 9852044; 10481272; 10720750; 10783263; 11077054; 11154739; 11535246; 11740338; 12477932; 15489334; 16341674; 16507781; 16804942; 17425406; 18029348; 19343046; 19898482; 20453000; 20819778; 21044950; 21139048; 21988832 sulfotransferase family, cytosolic, 1C, member 2 Ensembl:ENSG00000198203 HGNC:11456 HPRD:03858 MIM:602385 Vega:OTTHUMG00000153215 Other designations: SULT1C#1|sulfotransferase 1C1|sulfotransferase 1C2|sulfotransferase family, cytosolic, 1C, member 1 SULT1C2 OGG:3000006868 Bin Zhao, Yue Liu, Oliver He ADAM18 CD156B CSVP NISBD TACE WEB: http://www.ncbi.nlm.nih.gov/gene ADAM17 ADAM metallopeptidase domain 17 6868 2p25 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0001666 (EC: IDA, PMID: 18276953); GO_0001934 (EC: IMP, PMID: 18625725); GO_0002446 (EC: IC, PMID: 16034137); GO_0002467 (EC: ISS, PMID: 10433800); GO_0002690 (EC: IC, PMID: 16034137); GO_0004222 (EC: IDA); GO_0004222 (EC: IMP, PMID: 9034190); GO_0004222 (EC: TAS); GO_0005112 (EC: IDA); GO_0005138 (EC: IPI, PMID: 16034137); GO_0005178 (EC: IPI, PMID: 14970227); GO_0005515 (EC: IPI, PMID: 10527948); GO_0005737 (EC: IDA); GO_0005886 (EC: TAS); GO_0005887 (EC: IDA, PMID: 17786981); GO_0005911 (EC: IDA, Qualifier: colocalizes_with, PMID: 14970227); GO_0005925 (EC: IDA, Qualifier: colocalizes_with, PMID: 14970227); GO_0006509 (EC: IDA, PMID: 17786981); GO_0006509 (EC: IMP, PMID: 12743035); GO_0006915 (EC: TAS); GO_0007155 (EC: IDA, PMID: 14970227); GO_0007173 (EC: IDA, PMID: 12743035); GO_0007173 (EC: TAS); GO_0007219 (EC: IEA); GO_0007220 (EC: IDA); GO_0008237 (EC: IDA, PMID: 12777399); GO_0008237 (EC: IMP, PMID: 12535668); GO_0008237 (EC: TAS); GO_0008270 (EC: IEA); GO_0008284 (EC: IMP, PMID: 18373975); GO_0009986 (EC: IDA, PMID: 18383040); GO_0010820 (EC: IMP, PMID: 18373975); GO_0015629 (EC: IDA, PMID: 17010968); GO_0016324 (EC: IDA, PMID: 16034137); GO_0017124 (EC: IEA); GO_0022617 (EC: TAS); GO_0030165 (EC: IPI, PMID: 12207026); GO_0030183 (EC: ISS, PMID: 10433800); GO_0030198 (EC: TAS); GO_0030307 (EC: IMP, PMID: 18373975); GO_0030335 (EC: IMP, PMID: 18373975); GO_0030511 (EC: ISS, PMID: 10433800); GO_0030574 (EC: TAS); GO_0031293 (EC: TAS); GO_0031659 (EC: IDA, PMID: 18483258); GO_0032496 (EC: IDA, PMID: 18383040); GO_0032587 (EC: IDA, Qualifier: colocalizes_with, PMID: 14970227); GO_0032717 (EC: IMP, PMID: 16034137); GO_0032722 (EC: IMP, PMID: 16034137); GO_0033025 (EC: ISS, PMID: 10433800); GO_0033077 (EC: ISS, PMID: 10433800); GO_0033627 (EC: IDA, PMID: 14970227); GO_0035313 (EC: IEP, PMID: 14970227); GO_0035625 (EC: IMP, PMID: 17655843); GO_0042493 (EC: ISS, PMID: 10433800); GO_0045121 (EC: IDA, PMID: 17010968); GO_0045741 (EC: IDA, PMID: 18483258); GO_0045741 (EC: IMP, PMID: 17655843); GO_0048011 (EC: TAS); GO_0048536 (EC: ISS, PMID: 10433800); GO_0048870 (EC: ISS, PMID: 10433800); GO_0051088 (EC: IDA, PMID: 14625290); GO_0051088 (EC: IMP, PMID: 18676862); GO_0051272 (EC: ISS, PMID: 10433800); GO_0055099 (EC: IDA, PMID: 17786981); GO_0060397 (EC: TAS); GO_0097190 (EC: TAS) PMID: 8889548; 9034190; 9034191; 9520379; 9574564; 9620803; 9774383; 9806848; 9920899; 10224132; 10433800; 10527948; 10799478; 10860581; 10882063; 11733179; 11741929; 11823465; 11988096; 12044879; 12058067; 12135369; 12147693; 12207026; 12441351; 12474981; 12477932; 12535668; 12568494; 12606576; 12621058; 12668732; 12706122; 12711607; 12714588; 12730960; 12743035; 12755693; 12777399; 12810728; 12832423; 12947092; 12972643; 14532978; 14625290; 14970227; 15066987; 15102849; 15146197; 15182369; 15280379; 15308656; 15309730; 15337756; 15534001; 15691827; 15784625; 15983030; 16034137; 16079149; 16148149; 16179345; 16210695; 16246259; 16279945; 16332693; 16336275; 16376986; 16478662; 16619241; 16641105; 16806063; 16900751; 16912185; 16942750; 16982746; 17010968; 17081983; 17155946; 17170699; 17227756; 17360351; 17405915; 17438092; 17608729; 17655843; 17714581; 17786981; 17942404; 17986144; 17999917; 18029348; 18167350; 18171982; 18238782; 18276953; 18281553; 18355445; 18373975; 18383040; 18396294; 18426733; 18442814; 18483258; 18490652; 18493210; 18600307; 18625725; 18636124; 18638486; 18676862; 18713734; 18818406; 18824549; 18922903; 18978678; 18979631; 19003995; 19082505; 19091752; 19124506; 19150341; 19154693; 19171023; 19253070; 19278423; 19296470; 19298600; 19299578; 19324423; 19376560; 19435795; 19482949; 19515085; 19535569; 19541935; 19564338; 19595713; 19633828; 19666115; 19704010; 19762488; 19772640; 19819120; 19843672; 19875451; 19913121; 19949420; 19959661; 20026129; 20059578; 20070837; 20118276; 20180536; 20184396; 20188673; 20221248; 20300049; 20300969; 20359533; 20379614; 20506406; 20551051; 20627730; 20628086; 20634891; 20679348; 20807704; 20811902; 20819075; 20863729; 20871631; 20922190; 21102583; 21153921; 21170088; 21175594; 21240579; 21268712; 21300824; 21359495; 21365281; 21386996; 21407195; 21423656; 21480393; 21501859; 21777519; 21837402; 21865167; 21890473; 21906983; 21925169; 21932060; 21949123; 22010916; 22018416; 22105359; 22139867; 22157716; 22200661; 22268729; 22319627; 22367719; 22384041; 22438584; 22479555; 22506015; 22550340; 22575642; 22613720; 22665490; 22668812; 22677042; 22689693; 22770404; 22772468; 22833676; 22927435; 22933306; 22934512; 22965144; 22967992; 23000965; 23011796; 23076445; 23105116; 23341882; 23349873; 23356982; 23384719; 23389772; 23415892; 23416080; 23441135; 23460612; 23475633; 23479224; 23487023; 23500026; 23521534; 23526433; 23545805; 23557259; 23563789; 23585341; 23625205; 23674691; 23684931; 23729230; 23746173; 23897050; 24044434; 24121505; 24189063; 24227843; 24286866 ADAM metallopeptidase domain 17 Ensembl:ENSG00000151694 HGNC:195 HPRD:04703 MIM:603639 Vega:OTTHUMG00000090425 Other designations: ADAM metallopeptidase domain 18|TNF-alpha convertase|TNF-alpha converting enzyme|disintegrin and metalloproteinase domain-containing protein 17|snake venom-like protease|tumor necrosis factor, alpha, converting enzyme ADAM17 OGG:3000006876 Bin Zhao, Yue Liu, Oliver He SM22 SMCC TAGLN1 WS3-10 WEB: http://www.ncbi.nlm.nih.gov/gene TAGLN transgelin 6876 11q23.2 9606 11 Official from a nomenclature committee GO_0003779 (EC: IEA); GO_0005515 (EC: IPI); GO_0005737 (EC: IEA); GO_0007517 (EC: TAS, PMID: 9615232); GO_0030855 (EC: IDA) PMID: 1520290; 1872880; 7788527; 8117285; 8125298; 9242426; 9276683; 9384215; 9615232; 11053353; 11773051; 12200029; 12477932; 12521938; 15489334; 16009940; 17082327; 17305610; 17353931; 17629319; 18245174; 18291675; 18378184; 18446369; 19011151; 19188659; 19329940; 19724680; 19796641; 19848416; 19913121; 20012321; 20066125; 20098441; 20336793; 20379614; 20540360; 20628086; 20705054; 20707403; 21044950; 21051832; 21092460; 21139048; 21677441; 21763649; 21943158; 22245152; 22257561; 22365974; 22939629; 23138394; 23174934; 23331552; 23538046; 23824909 transgelin Ensembl:ENSG00000149591 HGNC:11553 HPRD:02891 MIM:600818 Vega:OTTHUMG00000167067 Other designations: 22 kDa actin-binding protein|SM22-alpha|smooth muscle protein 22-alpha|transgelin variant 2 TAGLN OGG:3000006880 Bin Zhao, Yue Liu, Oliver He MGC:5067 STAF31/32 TAF2G TAFII-31 TAFII-32 TAFII31 TAFII32 TAFIID32 WEB: http://www.ncbi.nlm.nih.gov/gene TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa 6880 AD-004 5q13.2 9606 5 Official from a nomenclature committee GO_0000125 (EC: IDA, PMID: 9674425); GO_0002039 (EC: IPI, PMID: 11278372); GO_0003677 (EC: IDA, PMID: 15601843); GO_0003713 (EC: IDA, PMID: 11564863); GO_0003713 (EC: IMP, PMID: 11278372); GO_0004402 (EC: IDA, Qualifier: contributes_to, PMID: 11564863); GO_0005515 (EC: IPI, PMID: 15489227); GO_0005654 (EC: TAS); GO_0005669 (EC: IDA, PMID: 14580349); GO_0006325 (EC: TAS); GO_0006366 (EC: TAS); GO_0006367 (EC: TAS); GO_0006368 (EC: TAS); GO_0006974 (EC: IC, PMID: 11278372); GO_0010467 (EC: TAS); GO_0016032 (EC: TAS); GO_0030307 (EC: IMP, PMID: 15899866); GO_0030914 (EC: IDA, PMID: 11564863); GO_0032435 (EC: IDA, PMID: 11278372); GO_0033276 (EC: IDA, PMID: 15899866); GO_0033613 (EC: IPI, PMID: 19251649); GO_0043066 (EC: IMP, PMID: 15899866); GO_0043966 (EC: IDA, PMID: 11564863); GO_0044212 (EC: IDA, PMID: 19251649); GO_0045944 (EC: IDA, PMID: 11278372); GO_0046982 (EC: IEA); GO_0050821 (EC: IDA, PMID: 15899866); GO_0060760 (EC: IMP, PMID: 15489227); GO_0070555 (EC: IMP, PMID: 15489227); GO_0070742 (EC: IPI, PMID: 19251649); GO_0070761 (EC: IDA, PMID: 17636026); GO_0071339 (EC: IDA, PMID: 15960975); GO_1902166 (EC: IC, PMID: 15899866) PMID: 1939271; 2449431; 7597030; 7667268; 7761466; 7809597; 7835343; 7836461; 7933101; 8121496; 8401585; 8680883; 8764009; 8764062; 8849451; 8946909; 9045704; 9054383; 9153318; 9171108; 9177216; 9405375; 9611234; 9674425; 9792714; 9885574; 10191103; 10449590; 10810093; 10821850; 10931946; 11005381; 11278372; 11406595; 11564863; 12101418; 12453419; 12477932; 12601814; 12660246; 12837753; 14580349; 15081896; 15489227; 15489334; 15601843; 15641800; 15899866; 15932940; 15960975; 16079131; 16169070; 16189514; 16713569; 17081983; 17636026; 17643375; 17884155; 17967894; 18250150; 19240132; 19251649; 19471022; 19615732; 19643037; 20186459; 20195357; 20946988; 21139048; 21693764; 21729782; 21832049; 21890473; 21963094; 21988832; 22053931; 22505724; 22696218; 22939629; 23000965; 23246961 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa Ensembl:ENSG00000085231 HGNC:11542 HPRD:15983 MIM:600822 Vega:OTTHUMG00000099359 Other designations: RNA polymerase II TBP-associated factor subunit G|transcription initiation factor TFIID 31 kD subunit|transcription initiation factor TFIID 31 kDa subunit|transcription initiation factor TFIID 32 kDa subunit|transcription initiation factor TFIID subunit 9 TAF9 OGG:3000007040 Bin Zhao, Yue Liu, Oliver He CED DPD1 LAP TGFB TGFbeta WEB: http://www.ncbi.nlm.nih.gov/gene TGFB1 transforming growth factor, beta 1 7040 19q13.1 20140408 9606 19 protein-coding Official from a nomenclature committee GO_0000060 (EC: IDA); GO_0000122 (EC: IEA); GO_0000165 (EC: IMP); GO_0001657 (EC: IEA); GO_0001666 (EC: IEA); GO_0001837 (EC: IEA); GO_0001933 (EC: IDA, PMID: 8053900); GO_0001934 (EC: IDA, PMID: 18625725); GO_0002028 (EC: IEA); GO_0002062 (EC: IDA, PMID: 15040835); GO_0002244 (EC: IDA, PMID: 15451575); GO_0002248 (EC: TAS, PMID: 9639571); GO_0002460 (EC: IEA); GO_0002513 (EC: IEA); GO_0002576 (EC: TAS); GO_0003823 (EC: IPI, PMID: 16754747); GO_0005114 (EC: IDA, PMID: 11157754); GO_0005114 (EC: IPI, PMID: 1333888); GO_0005515 (EC: IPI, PMID: 10092230); GO_0005576 (EC: TAS); GO_0005578 (EC: ISS); GO_0005615 (EC: IDA, PMID: 19734317); GO_0005634 (EC: IDA, PMID: 18040277); GO_0005737 (EC: IDA, PMID: 18040277); GO_0005796 (EC: TAS); GO_0005886 (EC: TAS); GO_0005902 (EC: IDA, Qualifier: colocalizes_with, PMID: 19366691); GO_0006468 (EC: ISS); GO_0006611 (EC: IDA, PMID: 17438144); GO_0006754 (EC: IDA, PMID: 10513816); GO_0006796 (EC: IDA, PMID: 10513816); GO_0006874 (EC: IEA); GO_0006954 (EC: IDA); GO_0007050 (EC: IDA, PMID: 14555988); GO_0007093 (EC: IDA, PMID: 15334054); GO_0007173 (EC: IDA, PMID: 18625725); GO_0007179 (EC: IDA, PMID: 11157754); GO_0007179 (EC: TAS); GO_0007182 (EC: IDA); GO_0007183 (EC: IDA, PMID: 17438144); GO_0007184 (EC: IDA, PMID: 15334054); GO_0007406 (EC: IEA); GO_0007435 (EC: IEP, PMID: 18080134); GO_0007492 (EC: IEA); GO_0007565 (EC: IEA); GO_0007568 (EC: IEA); GO_0007596 (EC: TAS); GO_0008083 (EC: IEA); GO_0008156 (EC: IMP, PMID: 11158066); GO_0008284 (EC: IDA, PMID: 10513816); GO_0008285 (EC: IDA, PMID: 15334054); GO_0008354 (EC: IEA); GO_0009314 (EC: IEA); GO_0009611 (EC: IEP, PMID: 18040277); GO_0009749 (EC: IEA); GO_0009790 (EC: IEA); GO_0009817 (EC: IEA); GO_0009986 (EC: IMP, PMID: 19366691); GO_0010575 (EC: TAS, PMID: 19506300); GO_0010628 (EC: IDA, PMID: 18625725); GO_0010718 (EC: IDA, PMID: 17999987); GO_0010718 (EC: NAS); GO_0010742 (EC: IC, PMID: 15219857); GO_0010763 (EC: IDA, PMID: 18555217); GO_0010800 (EC: IDA, PMID: 18625725); GO_0010862 (EC: IDA, PMID: 19736306); GO_0010936 (EC: IDA); GO_0016049 (EC: IEA); GO_0016202 (EC: ISS); GO_0017015 (EC: IDA, PMID: 15334054); GO_0019048 (EC: TAS); GO_0019049 (EC: IDA, PMID: 15334054); GO_0019058 (EC: TAS); GO_0019899 (EC: IPI, PMID: 19366691); GO_0022408 (EC: IDA, PMID: 18593713); GO_0030168 (EC: TAS); GO_0030198 (EC: TAS); GO_0030214 (EC: IDA, PMID: 17324121); GO_0030279 (EC: IEA); GO_0030308 (EC: IDA, PMID: 15334054); GO_0030334 (EC: TAS, PMID: 19018011); GO_0030335 (EC: IDA, PMID: 19736306); GO_0030424 (EC: IEA); GO_0030501 (EC: IEP, PMID: 17401695); GO_0030512 (EC: TAS); GO_0031065 (EC: IEA); GO_0031093 (EC: TAS); GO_0031100 (EC: IEA); GO_0031334 (EC: IDA, PMID: 19366691); GO_0031536 (EC: IEA); GO_0031663 (EC: IDA); GO_0032270 (EC: IDA, PMID: 15219857); GO_0032355 (EC: IDA, PMID: 18039789); GO_0032570 (EC: IDA, PMID: 18039789); GO_0032740 (EC: IDA, PMID: 18453574); GO_0032801 (EC: IDA, PMID: 17878231); GO_0032930 (EC: IDA); GO_0032943 (EC: IEA); GO_0032967 (EC: IDA, PMID: 19734317); GO_0032967 (EC: IMP, PMID: 11158066); GO_0033138 (EC: IDA, PMID: 18625725); GO_0033280 (EC: IEA); GO_0034616 (EC: IEA); GO_0035066 (EC: IEA); GO_0035307 (EC: IDA, PMID: 14555988); GO_0042130 (EC: IEA); GO_0042306 (EC: ISS); GO_0042307 (EC: IDA, PMID: 19366691); GO_0042482 (EC: IEA); GO_0042493 (EC: IEA); GO_0042552 (EC: IEA); GO_0042803 (EC: IEA); GO_0043011 (EC: IEA); GO_0043025 (EC: IEA); GO_0043029 (EC: IEA); GO_0043065 (EC: IEA); GO_0043406 (EC: IDA, PMID: 18625725); GO_0043491 (EC: IMP); GO_0043536 (EC: IDA, PMID: 18555217); GO_0043537 (EC: IDA, PMID: 18555217); GO_0043552 (EC: IDA, PMID: 18625725); GO_0043932 (EC: IEP, PMID: 17401695); GO_0045066 (EC: IEA); GO_0045216 (EC: IDA, PMID: 18505915); GO_0045599 (EC: IDA, PMID: 15040835); GO_0045662 (EC: IDA, PMID: 9770491); GO_0045786 (EC: IDA, PMID: 11502704); GO_0045892 (EC: IDA, PMID: 15702480); GO_0045893 (EC: IDA, PMID: 14517293); GO_0045893 (EC: ISS); GO_0045930 (EC: IDA, PMID: 14555988); GO_0045944 (EC: IDA, PMID: 18832382); GO_0046732 (EC: TAS); GO_0046982 (EC: IEA); GO_0047485 (EC: IEA); GO_0048298 (EC: IDA, PMID: 14988498); GO_0048535 (EC: ISS); GO_0048565 (EC: IEA); GO_0048642 (EC: IDA, PMID: 9770491); GO_0048839 (EC: IEA); GO_0050679 (EC: IEA); GO_0050680 (EC: IDA, PMID: 9950587); GO_0050680 (EC: IMP, PMID: 16943770); GO_0050714 (EC: IDA, PMID: 18505915); GO_0050765 (EC: IEA); GO_0050777 (EC: IEA); GO_0050921 (EC: IDA, PMID: 18555217); GO_0051092 (EC: IEA); GO_0051098 (EC: ISS); GO_0051101 (EC: ISS); GO_0051152 (EC: IEA); GO_0051280 (EC: IEA); GO_0051781 (EC: IEA); GO_0051897 (EC: IDA, PMID: 18625725); GO_0060325 (EC: IEA); GO_0060364 (EC: IEA); GO_0060389 (EC: IDA, PMID: 11157754); GO_0060391 (EC: IDA, PMID: 19366691); GO_0060744 (EC: IEA); GO_0060751 (EC: IEA); GO_0060762 (EC: IEA); GO_0061035 (EC: IEA); GO_0070306 (EC: IEA); GO_0070723 (EC: IDA, PMID: 17878231); GO_0071158 (EC: IEA); GO_0071407 (EC: IDA); GO_0071549 (EC: IEA); GO_0072562 (EC: IDA); GO_0085029 (EC: IDA, PMID: 19734317); GO_0090190 (EC: IEA); GO_0097191 (EC: IDA, PMID: 15334054); GO_1900126 (EC: IDA, PMID: 17324121); GO_1901666 (EC: IDA); GO_2000679 (EC: IDA) PMID: 1281686; 1326540; 1333888; 1550960; 2119582; 2909528; 2982829; 3162913; 3457014; 3459257; 3470709; 3487831; 3861940; 7495302; 7513640; 7638106; 7686157; 7695626; 7798269; 7803268; 7852346; 7935686; 8053900; 8093006; 8106553; 8235612; 8242742; 8264131; 8294518; 8336945; 8370410; 8424942; 8424943; 8471846; 8551249; 8568261; 8599089; 8617200; 8679613; 8811049; 9150447; 9383706; 9389648; 9434787; 9521216; 9639571; 9660815; 9670843; 9675033; 9770491; 9783545; 9813058; 9865696; 9895299; 9918798; 9934696; 9950587; 9987082; 10025398; 10085302; 10092230; 10376933; 10383378; 10431160; 10457363; 10513816; 10631145; 10652271; 10716993; 10746731; 10843814; 10887155; 10930463; 10973241; 11008076; 11062463; 11100470; 11157754; 11158066; 11172812; 11176807; 11192323; 11233912; 11266927; 11266928; 11267084; 11267423; 11278302; 11316069; 11345594; 11357939; 11374867; 11389394; 11391236; 11391238; 11401606; 11404167; 11436536; 11453244; 11456401; 11483955; 11496247; 11502704; 11528523; 11557193; 11568166; 11576951; 11604083; 11694328; 11715070; 11740340; 11746498; 11750277; 11769974; 11771728; 11776328; 11784716; 11796824; 11800227; 11803605; 11810274; 11824477; 11826761; 11830340; 11836565; 11839086; 11867550; 11876742; 11876761; 11906036; 11906646; 11908736; 11911944; 11912197; 11924651; 11925630; 11928807; 11934870; 11960000; 11966931; 11970960; 11981433; 11991670; 11991675; 11992481; 11998866; 12000722; 12009575; 12015308; 12020803; 12021923; 12032592; 12036913; 12041672; 12046078; 12050565; 12055267; 12057905; 12060054; 12061838; 12062452; 12068984; 12081893; 12081894; 12082048; 12085100; 12089714; 12095061; 12097320; 12099698; 12101112; 12107734; 12117671; 12133353; 12140283; 12150293; 12151385; 12160532; 12161098; 12161428; 12163012; 12163055; 12164325; 12168782; 12170265; 12171249; 12172787; 12174377; 12175481; 12176809; 12182464; 12186868; 12189134; 12202226; 12202478; 12202987; 12207584; 12209716; 12219028; 12223346; 12232842; 12234017; 12352892; 12358597; 12358852; 12366695; 12370400; 12370804; 12374793; 12376363; 12379307; 12382579; 12393416; 12393612; 12397374; 12410804; 12411321; 12413771; 12420205; 12421823; 12431651; 12431652; 12432546; 12438348; 12441075; 12451269; 12453980; 12454225; 12457461; 12477932; 12478192; 12479636; 12485831; 12485877; 12489179; 12489185; 12491092; 12493411; 12493741; 12500218; 12507818; 12514788; 12515830; 12525765; 12529270; 12531695; 12531696; 12531888; 12540377; 12547711; 12548199; 12559970; 12560323; 12560674; 12569017; 12572925; 12579267; 12579348; 12589095; 12590978; 12591385; 12595498; 12595908; 12598898; 12601022; 12607775; 12615364; 12626500; 12630751; 12637138; 12649573; 12654639; 12667558; 12669309; 12675860; 12682078; 12700666; 12707335; 12723985; 12727482; 12743121; 12746254; 12747448; 12751024; 12753290; 12754205; 12758167; 12772773; 12775566; 12787424; 12794244; 12795790; 12802498; 12810668; 12815042; 12817760; 12821938; 12824005; 12838101; 12843182; 12850832; 12857600; 12858019; 12858451; 12859695; 12867422; 12874450; 12875973; 12879019; 12879228; 12893825; 12894997; 12898374; 12902338; 12909463; 12911534; 12911563; 12917425; 12938093; 12938195; 12943995; 12944979; 12953061; 12960355; 12974899; 13678774; 13679381; 14504277; 14504444; 14507446; 14510802; 14514699; 14514772; 14517293; 14525983; 14529885; 14531781; 14531804; 14532743; 14555988; 14557872; 14566095; 14576166; 14576954; 14583433; 14585325; 14595120; 14596813; 14597484; 14600158; 14604900; 14607332; 14607563; 14607699; 14608199; 14612292; 14612931; 14614718; 14625191; 14633126; 14633628; 14633705; 14634021; 14635011; 14636845; 14637150; 14641541; 14642613; 14643949; 14644155; 14648590; 14667198; 14672557; 14675189; 14675394; 14676209; 14679171; 14697238; 14697748; 14699019; 14704634; 14707053; 14712482; 14720431; 14722617; 14725686; 14726452; 14727154; 14732719; 14737114; 14751563; 14755254; 14756669; 14757763; 14760152; 14767644; 14871809; 14872501; 14969768; 14976204; 14978126; 14988407; 14988498; 14991065; 14993265; 14999526; 15000149; 15001984; 15003992; 15006917; 15009097; 15009106; 15009180; 15018667; 15020570; 15030461; 15033015; 15033492; 15034041; 15034927; 15040835; 15041164; 15041717; 15044465; 15044491; 15049387; 15057277; 15063762; 15066699; 15068691; 15084245; 15086490; 15100259; 15100460; 15102678; 15102771; 15104684; 15113633; 15114294; 15120189; 15132952; 15133024; 15133032; 15135368; 15159307; 15161830; 15166495; 15170816; 15170937; 15175276; 15178409; 15180953; 15184872; 15187087; 15187109; 15189946; 15191521; 15192047; 15192088; 15194285; 15200451; 15200452; 15203191; 15207246; 15212689; 15214940; 15215809; 15219857; 15220111; 15221033; 15225617; 15231647; 15240008; 15247230; 15247411; 15248227; 15257453; 15269821; 15271980; 15284289; 15288191; 15294900; 15297631; 15305380; 15308875; 15316224; 15334054; 15337504; 15342556; 15342643; 15351436; 15353478; 15354859; 15359164; 15361124; 15361128; 15361357; 15365652; 15367225; 15368517; 15372625; 15373772; 15377500; 15387373; 15450129; 15451575; 15458467; 15467747; 15479754; 15488704; 15489334; 15494412; 15498571; 15498766; 15522940; 15529502; 15536170; 15539010; 15546338; 15552843; 15569360; 15574511; 15592292; 15593052; 15593053; 15596839; 15598443; 15599305; 15599395; 15599946; 15603866; 15604209; 15606694; 15609398; 15613484; 15621151; 15622443; 15623538; 15623763; 15632190; 15637079; 15641096; 15650893; 15654963; 15661045; 15663966; 15665522; 15671065; 15690532; 15694998; 15698546; 15702480; 15703175; 15705190; 15708894; 15712349; 15716278; 15718915; 15721312; 15723707; 15730046; 15732863; 15735739; 15738684; 15750822; 15753900; 15754021; 15761148; 15763337; 15767424; 15769917; 15770661; 15773449; 15777850; 15778389; 15778431; 15784411; 15787639; 15788474; 15790343; 15794197; 15799969; 15800982; 15802940; 15803361; 15811853; 15818397; 15824172; 15833881; 15834029; 15837559; 15838283; 15838328; 15841043; 15842590; 15843517; 15845540; 15848524; 15848527; 15854667; 15856020; 15857508; 15860935; 15878096; 15879087; 15880049; 15881652; 15895394; 15896309; 15901906; 15905358; 15910294; 15913806; 15913903; 15916738; 15917409; 15917723; 15925543; 15927846; 15932621; 15935652; 15935832; 15938776; 15941661; 15941974; 15942255; 15943594; 15944607; 15945506; 15946939; 15951295; 15951665; 15955247; 15957132; 15982639; 16003239; 16014625; 16023325; 16029542; 16030091; 16044414; 16046050; 16046504; 16055706; 16082716; 16086840; 16095497; 16098131; 16100012; 16100774; 16111879; 16113310; 16133992; 16135802; 16135988; 16144297; 16144346; 16146757; 16148664; 16158060; 16162149; 16179583; 16179614; 16179804; 16179826; 16183136; 16184401; 16187293; 16187311; 16193177; 16207846; 16209640; 16210002; 16219695; 16222707; 16223572; 16223775; 16236363; 16243534; 16245329; 16251192; 16253118; 16253647; 16258727; 16258965; 16259606; 16260615; 16263699; 16270194; 16272332; 16277007; 16285938; 16287542; 16289860; 16292494; 16297654; 16298544; 16301119; 16307809; 16310402; 16323703; 16324212; 16327802; 16330131; 16335952; 16336267; 16343799; 16344560; 16350816; 16367920; 16369764; 16378061; 16378062; 16378074; 16387180; 16387590; 16400883; 16403803; 16407286; 16412560; 16413503; 16414983; 16423881; 16423922; 16424284; 16425360; 16428771; 16433832; 16456143; 16461080; 16463783; 16467160; 16482098; 16484622; 16488890; 16493441; 16495290; 16496359; 16499994; 16504679; 16521228; 16524740; 16540751; 16541418; 16543220; 16543493; 16549165; 16552334; 16554035; 16563223; 16563228; 16564125; 16567828; 16570020; 16571622; 16609882; 16617095; 16619041; 16619184; 16620985; 16621788; 16622033; 16622736; 16635219; 16635548; 16637060; 16638864; 16641085; 16646981; 16671880; 16675485; 16675963; 16677601; 16685022; 16690986; 16698802; 16702209; 16704031; 16704689; 16712948; 16718633; 16720864; 16722148; 16730575; 16730947; 16732186; 16733295; 16734133; 16754688; 16754747; 16778279; 16780585; 16785237; 16792132; 16798416; 16799085; 16803995; 16804000; 16807529; 16815840; 16816361; 16820791; 16820871; 16824159; 16824504; 16828225; 16828470; 16835828; 16837650; 16843825; 16849317; 16872485; 16873204; 16875935; 16877343; 16896935; 16904244; 16916603; 16916659; 16920945; 16921482; 16931622; 16933058; 16934609; 16938461; 16941960; 16943770; 16951150; 16962335; 16962935; 16966185; 16969385; 16971953; 16980081; 16987065; 16987066; 16989156; 16990280; 16990569; 16998703; 17003485; 17014924; 17017182; 17018615; 17018616; 17018785; 17021946; 17023672; 17023741; 17032917; 17035001; 17035229; 17044077; 17047091; 17052957; 17059371; 17067743; 17071067; 17072955; 17074098; 17074765; 17076676; 17080483; 17088559; 17097497; 17100549; 17114344; 17137775; 17138053; 17139467; 17145161; 17145371; 17146441; 17151785; 17157157; 17157217; 17164348; 17173255; 17184296; 17187359; 17192829; 17194537; 17198270; 17198275; 17203972; 17205957; 17209781; 17213232; 17214746; 17217620; 17217840; 17220333; 17230494; 17234915; 17237561; 17242066; 17257312; 17261758; 17261759; 17264880; 17268554; 17277740; 17285762; 17288590; 17290010; 17292826; 17293864; 17303584; 17305717; 17312920; 17314099; 17319955; 17324121; 17325209; 17327236; 17332318; 17333284; 17338374; 17341608; 17341610; 17341683; 17346099; 17347580; 17348207; 17359969; 17360530; 17360654; 17361195; 17365852; 17367219; 17368597; 17369174; 17369289; 17371954; 17373677; 17374177; 17376051; 17376924; 17381064; 17382930; 17392271; 17394006; 17400536; 17401617; 17401695; 17404043; 17405902; 17409139; 17415413; 17417945; 17418380; 17418594; 17424886; 17428349; 17433803; 17438144; 17456311; 17459720; 17468136; 17469184; 17471240; 17471513; 17476473; 17483238; 17485238; 17486072; 17498265; 17515815; 17520266; 17522998; 17524861; 17530715; 17540773; 17544674; 17545053; 17548703; 17554369; 17557241; 17557799; 17560118; 17562261; 17567933; 17570736; 17574548; 17579118; 17579298; 17580335; 17587163; 17588962; 17591977; 17594488; 17596875; 17597658; 17598964; 17601559; 17605296; 17612762; 17615257; 17620406; 17621264; 17622752; 17623674; 17624411; 17625450; 17626784; 17627086; 17627763; 17635914; 17637743; 17637750; 17638910; 17640324; 17641021; 17644809; 17649947; 17651146; 17653872; 17654453; 17654516; 17656362; 17656680; 17657504; 17657819; 17662305; 17664003; 17664181; 17669238; 17671518; 17673695; 17680270; 17680535; 17687390; 17689884; 17690184; 17690329; 17692120; 17692821; 17700165; 17703412; 17704440; 17707032; 17711410; 17713555; 17714959; 17720884; 17766609; 17768235; 17768377; 17785866; 17802821; 17823083; 17827158; 17848193; 17848599; 17875052; 17875924; 17876891; 17878231; 17882904; 17884818; 17889117; 17889143; 17889927; 17892594; 17906455; 17911416; 17915216; 17916352; 17920062; 17922404; 17924060; 17927862; 17928287; 17938236; 17947678; 17953753; 17961177; 17965799; 17967972; 17974160; 17974504; 17975134; 17975199; 17982242; 17986101; 17988266; 17989584; 17989610; 17990985; 17999987; 18001570; 18003620; 18024258; 18024394; 18028462; 18029191; 18036644; 18039529; 18039789; 18040277; 18041006; 18055455; 18058229; 18058470; 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23204521; 23207623; 23208491; 23209731; 23220173; 23222298; 23223528; 23226264; 23232296; 23239467; 23242839; 23243310; 23245944; 23249950; 23258796; 23260996; 23275154; 23277357; 23280075; 23284751; 23285029; 23291965; 23295196; 23298711; 23306609; 23319603; 23322881; 23325483; 23333936; 23334061; 23344525; 23352789; 23352795; 23357697; 23358854; 23359369; 23361571; 23362262; 23363776; 23378223; 23382382; 23390194; 23393376; 23399816; 23403314; 23416372; 23416968; 23419524; 23420368; 23421960; 23424236; 23426367; 23428182; 23434344; 23435990; 23437118; 23437179; 23447672; 23459932; 23463512; 23464518; 23466425; 23467611; 23468994; 23479725; 23481710; 23483604; 23486522; 23500081; 23503840; 23515048; 23536722; 23546898; 23548068; 23548835; 23554457; 23555036; 23567513; 23576639; 23581259; 23583521; 23589287; 23614931; 23618868; 23619257; 23623844; 23631855; 23638863; 23640911; 23645040; 23651239; 23653379; 23657067; 23657402; 23668958; 23684116; 23685151; 23690936; 23704908; 23705641; 23717436; 23727026; 23731614; 23741351; 23747893; 23748363; 23762097; 23762330; 23764028; 23770288; 23770290; 23779087; 23781096; 23783250; 23792459; 23792503; 23792529; 23793025; 23801826; 23804438; 23824844; 23824952; 23828577; 23830915; 23831640; 23839959; 23861796; 23872147; 23873179; 23884197; 23892434; 23904169; 23904263; 23911408; 23921128; 23923066; 23926107; 23936495; 23937428; 23940283; 23946447; 23951322; 23958565; 23965869; 23975370; 23990681; 23996684; 24005672; 24014274; 24015303; 24026183; 24049142; 24056369; 24067469; 24080022; 24106276; 24123012; 24129188; 24129565; 24133214; 24145170; 24162774; 24170657; 24183998; 24195511; 24240172; 24305876; 24316888; 24324267; 24511106; 24597264; 24597398 transforming growth factor, beta 1 HGNC:11766 HPRD:01821 MIM:190180 TGFB1 OGG:3000007042 Bin Zhao, Yue Liu, Oliver He LDS4 TGF-beta2 WEB: http://www.ncbi.nlm.nih.gov/gene TGFB2 transforming growth factor, beta 2 7042 1q41 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0000902 (EC: IDA, PMID: 15896309); GO_0001502 (EC: IEA); GO_0001525 (EC: TAS, PMID: 9611771); GO_0001540 (EC: IDA, PMID: 16227582); GO_0001654 (EC: IDA, PMID: 15944186); GO_0001666 (EC: IMP, PMID: 12411310); GO_0001837 (EC: IDA, PMID: 10092230); GO_0001837 (EC: TAS, PMID: 14679171); GO_0001942 (EC: IDA, PMID: 10433821); GO_0001942 (EC: ISS); GO_0001974 (EC: IEA); GO_0002576 (EC: TAS); GO_0003007 (EC: IDA, PMID: 10092230); GO_0004702 (EC: IDA, PMID: 12958365); GO_0005102 (EC: IMP, PMID: 16227582); GO_0005114 (EC: IDA, PMID: 11157754); GO_0005114 (EC: IPI, PMID: 1333888); GO_0005125 (EC: TAS, PMID: 9611771); GO_0005160 (EC: IDA, PMID: 10092230); GO_0005515 (EC: IPI, PMID: 10930463); GO_0005515 (EC: IPI, Qualifier: contributes_to, PMID: 11157754); GO_0005576 (EC: IDA, PMID: 16227582); GO_0005576 (EC: TAS, PMID: 2119582); GO_0005615 (EC: IEA); GO_0006468 (EC: IDA, PMID: 18358889); GO_0007050 (EC: IDA, PMID: 18223299); GO_0007179 (EC: IDA, PMID: 11157754); GO_0007184 (EC: IDA, PMID: 17192487); GO_0007267 (EC: TAS, PMID: 3322813); GO_0007411 (EC: IEA); GO_0007435 (EC: IEP, PMID: 18080134); GO_0007507 (EC: IDA, PMID: 15896309); GO_0007596 (EC: TAS); GO_0008083 (EC: IEA); GO_0008219 (EC: IDA, PMID: 16227582); GO_0008283 (EC: TAS, PMID: 3322813); GO_0008284 (EC: IDA, PMID: 15896309); GO_0008285 (EC: IDA, PMID: 15944186); GO_0008347 (EC: IDA, PMID: 18431253); GO_0009611 (EC: IEP, PMID: 16891397); GO_0009790 (EC: TAS, PMID: 2119582); GO_0010002 (EC: IDA, PMID: 15896309); GO_0010628 (EC: IEA); GO_0010634 (EC: IDA, PMID: 17960115); GO_0010693 (EC: IDA, PMID: 18358889); GO_0010718 (EC: IDA, PMID: 17999987); GO_0010936 (EC: IDA); GO_0014068 (EC: IDA, PMID: 18223299); GO_0016049 (EC: IEA); GO_0016477 (EC: IDA, PMID: 10092230); GO_0022601 (EC: IEP, PMID: 18039789); GO_0023014 (EC: IDA, PMID: 12958365); GO_0030097 (EC: ISS); GO_0030168 (EC: TAS); GO_0030198 (EC: TAS); GO_0030199 (EC: IDA, PMID: 16891397); GO_0030307 (EC: IDA, PMID: 15896309); GO_0030308 (EC: IDA, PMID: 18358889); GO_0030424 (EC: ISS); GO_0030593 (EC: ISS); GO_0030593 (EC: TAS, PMID: 9611771); GO_0031012 (EC: IDA, PMID: 18049952); GO_0031069 (EC: ISS); GO_0031093 (EC: TAS); GO_0032147 (EC: IDA, PMID: 17192487); GO_0032570 (EC: IDA, PMID: 18039789); GO_0032874 (EC: IDA, PMID: 17192487); GO_0032909 (EC: IMP, PMID: 12411310); GO_0033630 (EC: IDA, PMID: 17960115); GO_0042060 (EC: ISS); GO_0042416 (EC: ISS); GO_0042476 (EC: NAS, PMID: 18078367); GO_0042493 (EC: IDA); GO_0042637 (EC: IDA, PMID: 15955085); GO_0042803 (EC: IDA, PMID: 2119582); GO_0043025 (EC: ISS); GO_0043525 (EC: IDA, PMID: 16227582); GO_0045216 (EC: IDA, PMID: 18505915); GO_0045726 (EC: IDA, PMID: 17960115); GO_0045778 (EC: IEP, PMID: 17401695); GO_0045787 (EC: ISS); GO_0045823 (EC: IDA, PMID: 15896309); GO_0046982 (EC: TAS, PMID: 9611771); GO_0048103 (EC: ISS); GO_0048566 (EC: IEP); GO_0048663 (EC: IEA); GO_0048666 (EC: ISS); GO_0048699 (EC: TAS, PMID: 15944186); GO_0050680 (EC: IDA, PMID: 17217916); GO_0050680 (EC: IMP, PMID: 16943770); GO_0050714 (EC: IDA, PMID: 18505915); GO_0050777 (EC: TAS, PMID: 9611771); GO_0050778 (EC: ISS); GO_0051781 (EC: IEA); GO_0051795 (EC: IDA, PMID: 15955085); GO_0051891 (EC: IDA, PMID: 15896309); GO_0060038 (EC: IDA, PMID: 15896309); GO_0060317 (EC: IDA, PMID: 10092230); GO_0060325 (EC: IEA); GO_0060389 (EC: IDA, PMID: 11157754); GO_0070237 (EC: IEA); GO_0097191 (EC: IDA, PMID: 17217916); GO_2001241 (EC: IEA) PMID: 1333888; 1631557; 1641027; 1764261; 2119582; 2850146; 3162414; 3226728; 3322813; 3457014; 3476488; 7513640; 7852346; 8093006; 8106553; 9493905; 9611771; 9675033; 10092230; 10433821; 10457363; 10861501; 10930463; 11157754; 11241554; 11278302; 11483955; 11488419; 11528528; 11716069; 11795478; 11796824; 11895345; 11991670; 12011061; 12015308; 12021923; 12060054; 12060393; 12062452; 12064833; 12411310; 12420205; 12477932; 12489185; 12545247; 12607775; 12706107; 12772773; 12802400; 12867422; 12911534; 12958365; 14507446; 14510802; 14679171; 14702039; 15009106; 15113633; 15247411; 15290353; 15389580; 15489334; 15695166; 15816823; 15857508; 15896309; 15944186; 15955085; 16210002; 16227582; 16260601; 16463680; 16467496; 16608413; 16778279; 16885354; 16891397; 16943770; 16998703; 17192487; 17201588; 17217916; 17401695; 17431704; 17453002; 17532297; 17611697; 17651146; 17679942; 17703412; 17827158; 17960115; 17999987; 18039789; 18040277; 18043895; 18049952; 18078367; 18080134; 18174230; 18223299; 18239623; 18292822; 18348727; 18358889; 18384390; 18431253; 18457978; 18498721; 18505915; 18563556; 18694919; 19031438; 19062040; 19161338; 19212830; 19249525; 19258923; 19438810; 19444386; 19453261; 19472023; 19572226; 19651985; 19710942; 19834535; 19913121; 19937272; 19959123; 19965872; 20059631; 20134268; 20142847; 20201926; 20237496; 20301312; 20485444; 20503287; 20543478; 20585394; 20587546; 20628086; 20628624; 20630504; 20634891; 20734064; 20875417; 20881960; 21034224; 21087804; 21087928; 21088899; 21106846; 21139048; 21161068; 21207416; 21212630; 21305699; 21360509; 21411746; 21446058; 21585337; 21642622; 21693611; 21738403; 21917933; 21946350; 22180604; 22464821; 22487836; 22504005; 22582395; 22653295; 22706080; 22736943; 22739237; 22772368; 22772371; 22786655; 22823397; 22955109; 23099432; 23102774; 23249391; 23257207; 23297089; 23306609; 23322721; 23387555; 23651239; 23668958; 23687438; 24045946; 24314882 transforming growth factor, beta 2 Ensembl:ENSG00000092969 HGNC:11768 HPRD:01828 MIM:190220 Vega:OTTHUMG00000039521 TGFB2 OGG:3000007057 Bin Zhao, Yue Liu, Oliver He THBS THBS-1 TSP TSP-1 TSP1 WEB: http://www.ncbi.nlm.nih.gov/gene THBS1 thrombospondin 1 7057 15q15 9606 15 Official from a nomenclature committee GO_0000187 (EC: IMP, PMID: 17413041); GO_0001666 (EC: NAS, PMID: 9304800); GO_0001786 (EC: IDA, PMID: 18940719); GO_0001937 (EC: IDA, PMID: 17996481); GO_0001937 (EC: IMP, PMID: 17413041); GO_0001948 (EC: NAS, PMID: 6438154); GO_0001953 (EC: IDA, PMID: 17416590); GO_0001968 (EC: IDA, PMID: 6693501); GO_0002040 (EC: IMP, PMID: 17879962); GO_0002544 (EC: IEP, PMID: 18674744); GO_0002576 (EC: TAS); GO_0002581 (EC: IDA, PMID: 16882710); GO_0002605 (EC: IDA, PMID: 16882710); GO_0003151 (EC: IEA); GO_0003197 (EC: IEA); GO_0003417 (EC: IEA); GO_0005178 (EC: IMP, PMID: 17413041); GO_0005509 (EC: NAS, PMID: 9304800); GO_0005515 (EC: IPI, PMID: 11134179); GO_0005576 (EC: TAS); GO_0005577 (EC: IDA, PMID: 3997886); GO_0005615 (EC: IDA); GO_0005783 (EC: ISS); GO_0006955 (EC: IEP, PMID: 18674744); GO_0006986 (EC: IEA); GO_0007050 (EC: IDA, PMID: 17596205); GO_0007155 (EC: NAS, PMID: 9304800); GO_0007596 (EC: TAS); GO_0008201 (EC: IDA, PMID: 101549); GO_0009612 (EC: IEA); GO_0009749 (EC: IDA, PMID: 18096704); GO_0009897 (EC: IDA, PMID: 6777381); GO_0009986 (EC: IDA, PMID: 2435757); GO_0010595 (EC: IDA, PMID: 18555217); GO_0010596 (EC: IDA, PMID: 18555217); GO_0010748 (EC: IDA, PMID: 17416590); GO_0010751 (EC: IDA, PMID: 17416590); GO_0010754 (EC: IDA, PMID: 17416590); GO_0010757 (EC: IDA, PMID: 6438154); GO_0010759 (EC: ISS); GO_0010763 (EC: IDA, PMID: 18555217); GO_0010811 (EC: IEA); GO_0016477 (EC: IDA, PMID: 18555217); GO_0016525 (EC: IDA, PMID: 17596205); GO_0016529 (EC: ISS); GO_0017134 (EC: IDA, PMID: 17996481); GO_0018149 (EC: IDA, PMID: 3997886); GO_0030141 (EC: IDA, PMID: 101549); GO_0030168 (EC: TAS); GO_0030169 (EC: IDA, PMID: 6693501); GO_0030194 (EC: IDA, PMID: 3997886); GO_0030198 (EC: TAS); GO_0030335 (EC: IDA, PMID: 15700281); GO_0030335 (EC: IMP, PMID: 17413041); GO_0030511 (EC: IDA, PMID: 18555217); GO_0031012 (EC: IDA, Qualifier: colocalizes_with); GO_0031012 (EC: ISS, Qualifier: colocalizes_with); GO_0031012 (EC: TAS, PMID: 9304800); GO_0031091 (EC: IDA, PMID: 6777381); GO_0031093 (EC: TAS); GO_0032026 (EC: IDA, PMID: 6777381); GO_0032570 (EC: TAS, PMID: 9304800); GO_0032695 (EC: IDA, PMID: 16882710); GO_0032914 (EC: ISS); GO_0033574 (EC: IEA); GO_0034605 (EC: NAS, PMID: 9304800); GO_0034976 (EC: ISS); GO_0040037 (EC: IDA, PMID: 17996481); GO_0042327 (EC: IMP, PMID: 17413041); GO_0042493 (EC: IEP, PMID: 19738618); GO_0042535 (EC: IDA, PMID: 18726995); GO_0042802 (EC: NAS, PMID: 9304800); GO_0043032 (EC: IDA, PMID: 18757424); GO_0043066 (EC: IDA, PMID: 18653767); GO_0043154 (EC: IDA, PMID: 18653767); GO_0043236 (EC: IDA, PMID: 6693501); GO_0043394 (EC: TAS, PMID: 9304800); GO_0043536 (EC: IDA, PMID: 18555217); GO_0043537 (EC: IDA, PMID: 18555217); GO_0043652 (EC: IDA, PMID: 16882710); GO_0045727 (EC: IDA, PMID: 15700281); GO_0045766 (EC: IMP, PMID: 17413041); GO_0048266 (EC: ISS); GO_0050431 (EC: ISS); GO_0050431 (EC: TAS, PMID: 9304800); GO_0050921 (EC: IDA, PMID: 18555217); GO_0051592 (EC: IDA, PMID: 18757424); GO_0051895 (EC: TAS, PMID: 9304800); GO_0051897 (EC: IDA, PMID: 18653767); GO_0051918 (EC: IDA, PMID: 6438154); GO_0070051 (EC: IDA, PMID: 6693501); GO_0070052 (EC: IDA, PMID: 6693501); GO_0070062 (EC: IDA, PMID: 19056867); GO_0071356 (EC: IEA); GO_0071363 (EC: IEA); GO_1902043 (EC: IDA, PMID: 18726995); GO_2000353 (EC: IDA, PMID: 18726995); GO_2000379 (EC: IDA, PMID: 18757424); GO_2001237 (EC: TAS, PMID: 17879962) PMID: 101549; 1350660; 1550960; 2010551; 2335352; 2341158; 2430973; 2435757; 2478219; 2522013; 2544587; 2745554; 2918029; 3030396; 3084490; 3402455; 3461443; 3571333; 3997886; 6338048; 6438154; 6693501; 6777381; 7521539; 7775583; 8288588; 8408036; 8463250; 8550562; 8751720; 9045712; 9169439; 9304800; 9328841; 9334164; 9419208; 9459346; 9478926; 9657149; 9840442; 9867861; 10397731; 10398144; 10487979; 10698186; 10749676; 10772961; 10900205; 10922378; 10982388; 11023976; 11067851; 11094060; 11134179; 11358957; 11606713; 11773026; 11801541; 11820799; 11882904; 11920574; 11964147; 11980922; 11986954; 12054567; 12147243; 12147682; 12220191; 12358136; 12391027; 12443715; 12444143; 12450399; 12477932; 12482844; 12530526; 12553016; 12598312; 12609716; 12643280; 12658547; 12676576; 12679131; 12718556; 12759541; 12782324; 12824298; 12878157; 12902472; 12909644; 12927044; 12947001; 12964017; 14555767; 14557872; 14559817; 14561896; 14568985; 14583433; 14683523; 14718574; 14963009; 14991768; 15007078; 15014436; 15034804; 15037654; 15095410; 15113588; 15140581; 15166498; 15217952; 15258909; 15292271; 15342643; 15347840; 15356163; 15456750; 15503824; 15522326; 15583827; 15634279; 15634883; 15665307; 15696166; 15700281; 15730804; 15792551; 15799029; 15817447; 15820829; 15833768; 15855645; 15890262; 15907858; 15908066; 15927849; 15945504; 16006654; 16037098; 16100012; 16141331; 16147889; 16148025; 16150726; 16166434; 16263699; 16270194; 16335952; 16344560; 16388804; 16465407; 16478297; 16495290; 16618977; 16650813; 16684956; 16732887; 16740002; 16835379; 16882710; 16951312; 16962673; 17106256; 17175378; 17198740; 17289869; 17363705; 17374440; 17378161; 17413041; 17416590; 17487836; 17507668; 17572512; 17596205; 17620335; 17638877; 17706282; 17709727; 17879962; 17917789; 17996481; 18021253; 18035072; 18057090; 18089612; 18096704; 18178577; 18208671; 18222489; 18226512; 18275041; 18319354; 18321763; 18336597; 18384112; 18413367; 18425817; 18499674; 18515748; 18555217; 18641687; 18653767; 18661355; 18674744; 18675774; 18676351; 18688696; 18700275; 18712840; 18726995; 18757424; 18788631; 18853485; 18855616; 18855618; 18940719; 19056867; 19239428; 19250552; 19271751; 19322201; 19351925; 19383251; 19396698; 19414528; 19422532; 19435835; 19447890; 19485899; 19509293; 19531495; 19542224; 19570906; 19581582; 19584238; 19661269; 19687096; 19698122; 19706610; 19710505; 19715883; 19721725; 19732880; 19738618; 19747478; 19762163; 19805200; 19826414; 19906510; 19913121; 19958625; 19959938; 19998449; 20016205; 20056600; 20103648; 20182908; 20203415; 20204299; 20300551; 20346360; 20360068; 20372793; 20449626; 20452482; 20453000; 20458281; 20467328; 20470445; 20485444; 20492458; 20494556; 20498063; 20546609; 20625903; 20628086; 20655775; 20673868; 20705333; 20876797; 20923780; 20927579; 21107877; 21139048; 21142150; 21148423; 21152035; 21157449; 21161418; 21193465; 21217824; 21296375; 21307796; 21317461; 21343308; 21378271; 21402050; 21420687; 21437286; 21474793; 21501375; 21518247; 21526452; 21531776; 21565611; 21659549; 21762961; 21822266; 21845757; 21883885; 21899841; 22011138; 22014686; 22024541; 22028325; 22028813; 22035632; 22037878; 22136730; 22194599; 22198906; 22207555; 22231149; 22238753; 22247259; 22268819; 22308318; 22311024; 22318901; 22383169; 22403705; 22583901; 22592401; 22672426; 22796565; 22971480; 22982001; 23030305; 23085760; 23119050; 23145312; 23202046; 23315169; 23350987; 23380452; 23528972; 23614916; 23660684; 23667531; 23995838; 24314882 thrombospondin 1 HGNC:11785 HPRD:01765 MIM:188060 Other designations: thrombospondin-1|thrombospondin-1p180 THBS1 OGG:3000007076 Bin Zhao, Yue Liu, Oliver He CLGI EPA EPO HCI TIMP WEB: http://www.ncbi.nlm.nih.gov/gene TIMP1 TIMP metallopeptidase inhibitor 1 7076 RP1-230G1.3 Xp11.3-p11.23 9606 X Official from a nomenclature committee GO_0002020 (EC: IEA); GO_0002576 (EC: TAS); GO_0005515 (EC: IPI, PMID: 16917503); GO_0005576 (EC: NAS, PMID: 1653055); GO_0005576 (EC: TAS); GO_0005604 (EC: IEA); GO_0007568 (EC: IEA); GO_0007596 (EC: TAS); GO_0008191 (EC: IDA, PMID: 12714508); GO_0008284 (EC: TAS, PMID: 3839290); GO_0010951 (EC: IDA, PMID: 12714508); GO_0022617 (EC: TAS); GO_0030168 (EC: TAS); GO_0030198 (EC: TAS); GO_0031093 (EC: TAS); GO_0034097 (EC: IEA); GO_0043066 (EC: IEA); GO_0043249 (EC: IEA); GO_0043434 (EC: IEA); GO_0046872 (EC: IEA); GO_0051045 (EC: IDA, PMID: 12714508); GO_1901164 (EC: IMP) PMID: 1420137; 1653055; 1730286; 2163605; 2171551; 2251898; 2921031; 3010309; 3460333; 3688834; 3839290; 3903517; 7507419; 8757599; 9063449; 9286280; 9288970; 9778693; 10071915; 10233411; 10441576; 10623524; 11279011; 11598182; 11606052; 11705862; 11762702; 11796725; 11876751; 11935340; 11940298; 12032189; 12034345; 12063180; 12081564; 12082592; 12147251; 12150976; 12218659; 12376362; 12406369; 12452001; 12475252; 12477932; 12479097; 12496489; 12538453; 12612199; 12614934; 12620441; 12626459; 12634064; 12651627; 12704667; 12714508; 12717827; 12771930; 12791318; 12834347; 12846741; 12861139; 12869573; 12873541; 12904305; 12921631; 12951656; 12970724; 14517716; 14605322; 14622947; 14630798; 14648584; 14652000; 14661256; 14669348; 14688084; 14710472; 14734567; 14871825; 14962256; 14973177; 14983226; 15028476; 15051730; 15073104; 15161657; 15225209; 15248826; 15277439; 15287862; 15313474; 15340161; 15363817; 15363818; 15465038; 15479729; 15485866; 15489334; 15494493; 15515157; 15516987; 15530852; 15557756; 15616792; 15754326; 15754388; 15797648; 15818737; 15841325; 15867221; 15888067; 15890357; 15896974; 15944607; 16005367; 16019435; 16042227; 16061701; 16100012; 16103240; 16107690; 16169070; 16188099; 16191301; 16219294; 16248458; 16263699; 16269968; 16280123; 16288711; 16289162; 16303743; 16335952; 16372907; 16407831; 16410344; 16474379; 16496359; 16555295; 16615041; 16631927; 16740002; 16754484; 16767366; 16772717; 16786122; 16840178; 16864898; 16877361; 16880228; 16917503; 16931892; 16935611; 16940985; 16960901; 16996520; 17008230; 17009408; 17012236; 17045024; 17050530; 17071711; 17072372; 17114213; 17136882; 17162914; 17182940; 17192464; 17202148; 17205957; 17209789; 17222415; 17226791; 17299802; 17301822; 17340613; 17350093; 17380436; 17409012; 17456311; 17478562; 17489740; 17493602; 17543340; 17549663; 17564313; 17572998; 17589947; 17634538; 17660250; 17703334; 17726014; 17763191; 17786346; 17878270; 17893005; 17899257; 17920311; 17928006; 17998244; 18025061; 18034264; 18042068; 18049028; 18063811; 18159069; 18214300; 18217401; 18236174; 18273688; 18291374; 18292822; 18298349; 18385523; 18391843; 18395263; 18474748; 18477480; 18487063; 18502033; 18630499; 18634035; 18636124; 18645261; 18683786; 18692810; 18704317; 18787947; 18850474; 18854176; 18945772; 18984437; 19012952; 19019896; 19020757; 19036126; 19134356; 19141395; 19246282; 19288452; 19331801; 19336475; 19358835; 19383295; 19383343; 19383344; 19387352; 19390929; 19430729; 19464975; 19506087; 19513566; 19524176; 19551542; 19560452; 19596921; 19608737; 19609944; 19629003; 19637058; 19653096; 19717938; 19723139; 19723899; 19728856; 19747478; 19758569; 19766963; 19781774; 19796534; 19814619; 19863693; 19875168; 19887890; 19889076; 19904223; 19911067; 19913121; 19927649; 20021931; 20030715; 20039537; 20041335; 20051489; 20095885; 20111696; 20164040; 20193458; 20215736; 20298300; 20305574; 20361393; 20371206; 20388222; 20423842; 20450704; 20452482; 20459644; 20484597; 20514432; 20533294; 20545111; 20545310; 20556397; 20584750; 20587546; 20595097; 20616161; 20628086; 20628624; 20646231; 20654099; 20655547; 20673868; 20685094; 20707923; 20798956; 20838751; 20853162; 20854182; 20889295; 20921293; 21041986; 21086628; 21094936; 21115936; 21128246; 21139048; 21163810; 21165404; 21167221; 21211402; 21283828; 21427648; 21437624; 21437772; 21454617; 21463121; 21487066; 21506705; 21524282; 21535601; 21547130; 21586274; 21684102; 21709637; 21720458; 21731773; 21745383; 21763297; 21786179; 21858035; 21860087; 21881840; 21882477; 21903858; 21906983; 21928345; 21946941; 21963094; 21963718; 21969093; 21987572; 21993004; 21995626; 22016393; 22020222; 22051851; 22110238; 22122951; 22139647; 22177802; 22199358; 22200256; 22200690; 22200710; 22204652; 22223664; 22257687; 22268729; 22286923; 22289852; 22291969; 22305865; 22364921; 22397869; 22402936; 22427646; 22457727; 22465225; 22516898; 22532131; 22544540; 22547904; 22558080; 22645431; 22667130; 22671570; 22706255; 22712305; 22718114; 22739984; 22788708; 22820628; 22859303; 22883459; 22901654; 22906271; 22957045; 22965799; 22971139; 22975753; 22985578; 23000965; 23016931; 23043898; 23057632; 23060593; 23064462; 23107442; 23122949; 23158994; 23175213; 23179318; 23223421; 23318123; 23388475; 23407481; 23412981; 23457635; 23509357; 23522389; 23525523; 23548070; 23555182; 23557756; 23563628; 23583449; 23592002; 23650722; 23660069; 23673111; 23763354; 23768069; 23815085; 23817219; 23834019; 23881388; 23893334; 23967215; 23993112; 24039251; 24174628; 24330623; 24479343 TIMP metallopeptidase inhibitor 1 Ensembl:ENSG00000102265 HGNC:11820 HPRD:02371 MIM:305370 Vega:OTTHUMG00000021447 Other designations: TIMP-1|collagenase inhibitor|erythroid potentiating activity|erythroid-potentiating activity|fibroblast collagenase inhibitor|metalloproteinase inhibitor 1|tissue inhibitor of metalloproteinases 1 TIMP1 OGG:3000007098 Bin Zhao, Yue Liu, Oliver He CD283 IIAE2 WEB: http://www.ncbi.nlm.nih.gov/gene TLR3 toll-like receptor 3 7098 4q35 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0002224 (EC: TAS); GO_0002282 (EC: IEA); GO_0002756 (EC: TAS); GO_0003725 (EC: IDA, PMID: 16111635); GO_0003725 (EC: NAS, PMID: 12054664); GO_0004872 (EC: TAS, PMID: 10426995); GO_0004888 (EC: NAS, PMID: 12054664); GO_0005515 (EC: IPI, PMID: 16858407); GO_0005737 (EC: IDA, PMID: 19740627); GO_0005765 (EC: IDA, PMID: 17897319); GO_0005789 (EC: TAS); GO_0005887 (EC: TAS, PMID: 9435236); GO_0006954 (EC: IEA); GO_0006972 (EC: NAS, PMID: 12054664); GO_0007165 (EC: TAS, PMID: 10426995); GO_0007249 (EC: TAS); GO_0007250 (EC: NAS, PMID: 12054664); GO_0007252 (EC: IDA, PMID: 19740627); GO_0008584 (EC: IEA); GO_0009597 (EC: NAS, PMID: 12054664); GO_0009986 (EC: IDA, Qualifier: NOT, PMID: 19740627); GO_0010008 (EC: TAS); GO_0016020 (EC: NAS, PMID: 12054664); GO_0032722 (EC: IDA, PMID: 19740627); GO_0032728 (EC: ISS); GO_0032735 (EC: ISS); GO_0032755 (EC: IDA, PMID: 19740627); GO_0032757 (EC: IDA, PMID: 17128265); GO_0032760 (EC: ISS); GO_0034123 (EC: IDA, PMID: 17128265); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034346 (EC: IEA); GO_0035458 (EC: IEA); GO_0035666 (EC: TAS); GO_0035690 (EC: IEA); GO_0036020 (EC: TAS); GO_0042346 (EC: IDA, PMID: 19740627); GO_0042742 (EC: TAS, PMID: 10426995); GO_0043065 (EC: IEA); GO_0043123 (EC: IEA); GO_0043330 (EC: IDA); GO_0045078 (EC: IDA, PMID: 16286015); GO_0045080 (EC: IEA); GO_0045087 (EC: TAS, PMID: 15356140); GO_0045356 (EC: IDA, PMID: 16286015); GO_0045359 (EC: IDA, PMID: 16286015); GO_0045359 (EC: IMP, PMID: 12054664); GO_0045671 (EC: NAS, PMID: 12133979); GO_0045944 (EC: ISS); GO_0046330 (EC: IEA); GO_0050729 (EC: IC, PMID: 19740627); GO_0051092 (EC: IEA); GO_0051607 (EC: TAS, PMID: 15356140); GO_0052033 (EC: IEA); GO_0071260 (EC: IEP, PMID: 19593445); GO_0071346 (EC: IEA); GO_0071360 (EC: IEA); GO_0097191 (EC: IDA); GO_0097527 (EC: IDA) PMID: 9435236; 10066798; 10426995; 10820283; 11561001; 11607032; 11782555; 12054664; 12133979; 12477932; 12509442; 12539043; 12609980; 12646618; 12672806; 12692549; 12855817; 14519765; 14557267; 14575692; 14729660; 14982987; 14987294; 15064760; 15107846; 15119015; 15153468; 15212709; 15226270; 15315972; 15340161; 15356140; 15502848; 15579900; 15652398; 15731229; 15737993; 15767394; 15778392; 15845391; 15935884; 15961631; 15972671; 16029432; 16035096; 16043704; 16111635; 16115877; 16144834; 16146574; 16160153; 16286015; 16289658; 16293707; 16344560; 16399790; 16424203; 16473828; 16482523; 16484229; 16533755; 16585585; 16628196; 16720699; 16847112; 16858407; 16877304; 16914605; 16935934; 16950283; 17043099; 17085778; 17128265; 17142768; 17142772; 17150911; 17178723; 17209042; 17254392; 17292969; 17301562; 17314152; 17434873; 17449641; 17521732; 17525119; 17534115; 17573354; 17602875; 17626075; 17660379; 17703412; 17786279; 17805015; 17851256; 17872438; 17878161; 17897319; 17908959; 17939877; 17947455; 17962643; 17962701; 17963596; 17964520; 17982077; 18021446; 18029758; 18172197; 18204787; 18253710; 18262679; 18325643; 18367536; 18385087; 18394314; 18437017; 18442983; 18508883; 18541719; 18544529; 18562533; 18566014; 18566393; 18568036; 18684960; 18686608; 18715647; 18725521; 18753640; 18775079; 18776324; 18776592; 18779317; 18810425; 18813073; 18818748; 18832709; 18849495; 18946062; 18949355; 18978302; 18988918; 19001446; 19016379; 19019335; 19035519; 19055649; 19120481; 19134117; 19164128; 19231996; 19234180; 19247444; 19254290; 19258923; 19265130; 19299748; 19362356; 19378782; 19423540; 19437550; 19475618; 19494321; 19505919; 19522763; 19527514; 19542247; 19593445; 19597128; 19625408; 19628747; 19631980; 19646728; 19656899; 19740627; 19741468; 19748983; 19752565; 19758322; 19769802; 19779021; 19795416; 19810822; 19833099; 19855253; 19878930; 19887600; 19890046; 19902255; 19914718; 19948350; 19951172; 19966137; 19966777; 20009359; 20047764; 20100933; 20124101; 20194452; 20197609; 20200155; 20227302; 20237496; 20309865; 20331378; 20367642; 20381870; 20406303; 20406964; 20422193; 20438785; 20452482; 20472559; 20483009; 20483744; 20483774; 20503287; 20514466; 20523058; 20588308; 20595247; 20604744; 20636339; 20639488; 20651983; 20673868; 20685081; 20691286; 20819670; 20832341; 20855885; 20957750; 20977567; 20978888; 21061265; 21079408; 21093032; 21129170; 21132533; 21148036; 21173679; 21179282; 21189260; 21216866; 21220319; 21223583; 21239167; 21245912; 21255094; 21266579; 21367858; 21398612; 21454254; 21474651; 21481769; 21498625; 21515789; 21563279; 21623661; 21646299; 21691053; 21695056; 21708001; 21712495; 21722947; 21730023; 21735101; 21802664; 21829730; 21839239; 21843566; 21844166; 21847628; 21903422; 21911421; 21911422; 21911501; 21911973; 21931545; 21949112; 21952237; 21960283; 21978158; 21990957; 21998457; 22016778; 22024499; 22030901; 22038398; 22039520; 22057682; 22065573; 22070917; 22102050; 22147891; 22174453; 22200507; 22205631; 22205660; 22260507; 22310660; 22323545; 22415225; 22421267; 22421964; 22457005; 22466005; 22479513; 22504413; 22537752; 22549436; 22552940; 22568929; 22572822; 22579623; 22590509; 22591330; 22611194; 22685032; 22745793; 22759966; 22762377; 22771581; 22825813; 22849850; 22851595; 22864531; 22865861; 22912896; 22944378; 22948160; 22950839; 22960172; 22989785; 23053995; 23056170; 23056470; 23076446; 23103873; 23115281; 23151015; 23166319; 23179584; 23220997; 23240626; 23245579; 23255072; 23255358; 23269203; 23290562; 23353987; 23369718; 23396947; 23404408; 23425350; 23467704; 23489702; 23497334; 23534905; 23541683; 23548575; 23647955; 23668802; 23673618; 23716670; 23717201; 23721942; 23723066; 23844087; 23908180; 23946637; 23962979; 24070541; 24198284 toll-like receptor 3 HGNC:11849 HPRD:04324 MIM:603029 TLR3 OGG:3000007099 Bin Zhao, Yue Liu, Oliver He ARMD10 CD284 TLR-4 TOLL WEB: http://www.ncbi.nlm.nih.gov/gene TLR4 toll-like receptor 4 7099 9q33.1 9606 9 Official from a nomenclature committee GO_0000187 (EC: ISS); GO_0001530 (EC: IMP, PMID: 16514062); GO_0001530 (EC: NAS, PMID: 10835634); GO_0001875 (EC: IDA, PMID: 19252480); GO_0002224 (EC: TAS); GO_0002322 (EC: IEA); GO_0002537 (EC: IEA); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0004872 (EC: TAS, PMID: 10426995); GO_0004888 (EC: NAS, PMID: 11970998); GO_0005515 (EC: IPI, PMID: 11441107); GO_0005737 (EC: IDA, PMID: 19740627); GO_0005886 (EC: IDA, PMID: 19740627); GO_0005886 (EC: TAS); GO_0005887 (EC: IDA, PMID: 15027902); GO_0006955 (EC: TAS, PMID: 10426995); GO_0007249 (EC: TAS); GO_0007252 (EC: IDA, PMID: 19740627); GO_0009897 (EC: IDA, PMID: 16514062); GO_0010008 (EC: TAS); GO_0010572 (EC: ISS, PMID: 16514062); GO_0016046 (EC: NAS, PMID: 11254600); GO_0030890 (EC: IEA); GO_0031663 (EC: IDA, Qualifier: NOT, PMID: 10880523); GO_0031663 (EC: IGI, PMID: 10880523); GO_0032496 (EC: IC, PMID: 16514062); GO_0032496 (EC: IDA, PMID: 12594207); GO_0032497 (EC: IDA, PMID: 19252480); GO_0032609 (EC: IEA); GO_0032689 (EC: ISS); GO_0032700 (EC: ISS); GO_0032707 (EC: ISS); GO_0032715 (EC: ISS); GO_0032720 (EC: ISS); GO_0032722 (EC: IDA, PMID: 19740627); GO_0032727 (EC: ISS); GO_0032728 (EC: ISS); GO_0032729 (EC: ISS); GO_0032732 (EC: ISS); GO_0032733 (EC: ISS); GO_0032735 (EC: ISS); GO_0032755 (EC: IDA, PMID: 19740627); GO_0032757 (EC: IDA, PMID: 19740627); GO_0032760 (EC: ISS); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0035666 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042088 (EC: NAS, PMID: 11970998); GO_0042116 (EC: IMP, PMID: 10835634); GO_0042346 (EC: IDA, PMID: 19740627); GO_0042535 (EC: IDA, PMID: 17951129); GO_0042742 (EC: TAS, PMID: 10426995); GO_0043123 (EC: IEA); GO_0045084 (EC: IDA, PMID: 15027902); GO_0045087 (EC: TAS, PMID: 15356140); GO_0045348 (EC: IEA); GO_0045359 (EC: IEA); GO_0045416 (EC: IDA, PMID: 17951129); GO_0045429 (EC: IEA); GO_0045671 (EC: NAS, PMID: 12133979); GO_0045944 (EC: ISS); GO_0046330 (EC: IEA); GO_0046696 (EC: IDA, PMID: 19252480); GO_0048471 (EC: IDA, PMID: 15027902); GO_0050729 (EC: IC, PMID: 19740627); GO_0050829 (EC: IC, PMID: 16514062); GO_0051092 (EC: IDA, PMID: 12594207); GO_0051770 (EC: ISS); GO_0060729 (EC: ISS); GO_0060907 (EC: IEA); GO_0070373 (EC: ISS); GO_0070374 (EC: IEA); GO_0070430 (EC: IEA); GO_0070434 (EC: IEA); GO_0071222 (EC: ISS); GO_0071223 (EC: IEA); GO_0071260 (EC: IEP, PMID: 19593445) PMID: 9237759; 9435236; 9625770; 10359581; 10426995; 10465784; 10524757; 10734131; 10835634; 10880523; 10952994; 11081518; 11104518; 11254600; 11441107; 11466383; 11477091; 11490012; 11494169; 11514453; 11526399; 11529488; 11544529; 11561001; 11688988; 11706042; 11728442; 11743586; 11751856; 11782555; 11835533; 11836257; 11841848; 11842086; 11877429; 11893689; 11912201; 11923281; 11932926; 11932927; 11964313; 11970998; 11976338; 12045108; 12055604; 12089142; 12117914; 12124407; 12133979; 12165534; 12174084; 12193670; 12196527; 12270725; 12324469; 12324481; 12391239; 12397216; 12402214; 12404174; 12406828; 12411706; 12438323; 12444143; 12447442; 12477932; 12477953; 12495941; 12525572; 12552467; 12588460; 12591474; 12592402; 12594207; 12599057; 12622779; 12630564; 12646618; 12717385; 12724322; 12730365; 12734376; 12738639; 12742999; 12773175; 12773319; 12777373; 12782302; 12794153; 12796470; 12810071; 12832426; 12846053; 12855579; 12865424; 12874320; 12897738; 12923493; 12925853; 12941697; 12942028; 12957699; 12960171; 12964127; 14517278; 14519765; 14551607; 14556004; 14557267; 14563652; 14565959; 14578307; 14597728; 14600154; 14610481; 14625308; 14638766; 14651524; 14693986; 14699116; 14699155; 14706103; 14709406; 14715415; 14735148; 14738464; 14739370; 14764071; 14764599; 14987294; 15007351; 15016407; 15022344; 15027902; 15039334; 15041961; 15044215; 15069085; 15081257; 15087412; 15107846; 15132988; 15138173; 15143473; 15148609; 15155619; 15175334; 15175649; 15187145; 15190267; 15194649; 15207785; 15213237; 15225640; 15247281; 15258789; 15273551; 15276183; 15277575; 15292002; 15302104; 15305230; 15321997; 15337750; 15340161; 15341923; 15351720; 15356101; 15356140; 15356557; 15358455; 15367917; 15373967; 15385480; 15452251; 15456896; 15489631; 15509550; 15516360; 15520404; 15525557; 15528333; 15547160; 15557191; 15576653; 15591473; 15610077; 15614130; 15623538; 15632890; 15644417; 15647432; 15650037; 15655821; 15661045; 15665723; 15670831; 15691841; 15694388; 15695310; 15696495; 15699327; 15728517; 15752733; 15760452; 15760459; 15770725; 15778388; 15790341; 15796767; 15809303; 15829498; 15843568; 15845500; 15852007; 15863460; 15864121; 15866212; 15866876; 15875057; 15879290; 15882292; 15883205; 15905704; 15910421; 15910856; 15919371; 15927851; 15932772; 15953129; 15972671; 15973118; 16002719; 16006099; 16010583; 16019531; 16024789; 16044857; 16051275; 16085746; 16107886; 16135957; 16142747; 16146574; 16157088; 16157451; 16202743; 16213463; 16215326; 16219107; 16219455; 16239565; 16239841; 16246938; 16266379; 16266460; 16267105; 16270639; 16290232; 16301860; 16304445; 16338228; 16338476; 16343635; 16344560; 16357190; 16371473; 16385250; 16388712; 16393227; 16395111; 16397127; 16436969; 16437636; 16439361; 16441767; 16443229; 16461792; 16463649; 16467847; 16469362; 16487240; 16508260; 16514062; 16517732; 16523497; 16525349; 16552356; 16556150; 16567359; 16581829; 16585591; 16603631; 16606645; 16613760; 16629651; 16651628; 16706818; 16714144; 16717116; 16731773; 16738534; 16740140; 16751411; 16754682; 16754684; 16754725; 16779724; 16780707; 16785528; 16786156; 16802353; 16803995; 16818785; 16829202; 16830219; 16836908; 16837493; 16840031; 16843693; 16849487; 16878026; 16879054; 16879199; 16879239; 16888192; 16890863; 16907704; 16933467; 16936080; 16950283; 16954131; 16955390; 16961803; 16969132; 16971956; 16973891; 16982657; 16988837; 16990552; 17008589; 17015691; 17038528; 17044867; 17045043; 17055575; 17056597; 17057796; 17062130; 17083795; 17086894; 17096074; 17100621; 17100625; 17100974; 17101559; 17111814; 17121827; 17124436; 17130564; 17143969; 17151549; 17156435; 17157899; 17172927; 17179672; 17206636; 17220311; 17228323; 17229603; 17235555; 17237368; 17258210; 17258734; 17264400; 17292969; 17301271; 17301562; 17301819; 17304101; 17309585; 17309748; 17314284; 17314700; 17322885; 17324405; 17328955; 17332447; 17333217; 17344072; 17362744; 17381056; 17381401; 17384648; 17389503; 17389921; 17390084; 17395901; 17404865; 17414051; 17417801; 17431743; 17448042; 17449325; 17456342; 17462092; 17465679; 17476680; 17482427; 17493663; 17513785; 17524268; 17529905; 17530716; 17538633; 17545720; 17549384; 17555409; 17556642; 17559631; 17565323; 17579019; 17579031; 17587646; 17588655; 17592300; 17592301; 17595233; 17597463; 17599732; 17600225; 17623651; 17624583; 17625598; 17629003; 17652449; 17660297; 17675516; 17681703; 17699831; 17703412; 17707233; 17709420; 17709532; 17713436; 17718424; 17720800; 17724596; 17767165; 17803912; 17827066; 17849054; 17850411; 17854755; 17855767; 17855803; 17872459; 17877764; 17877801; 17878380; 17892476; 17908769; 17909078; 17914947; 17916356; 17921137; 17925445; 17927684; 17928056; 17934216; 17942642; 17947706; 17951129; 17956467; 17956942; 17962701; 17964520; 17964870; 17967488; 17977838; 17982277; 17992260; 17992634; 17996871; 17999935; 18000954; 18001295; 18008256; 18025155; 18029454; 18031543; 18034244; 18034897; 18040078; 18042837; 18044001; 18054497; 18056968; 18062119; 18062835; 18067993; 18070880; 18082569; 18084608; 18089358; 18092352; 18097881; 18172114; 18174680; 18178854; 18180278; 18180796; 18182917; 18192488; 18209079; 18209571; 18213697; 18221795; 18234118; 18234474; 18251133; 18252714; 18268386; 18275280; 18286551; 18288881; 18292749; 18295348; 18297073; 18298826; 18299127; 18304834; 18306470; 18307517; 18312481; 18325643; 18326860; 18338763; 18344712; 18345485; 18348860; 18360565; 18368233; 18381796; 18382655; 18385087; 18394314; 18395849; 18403647; 18408113; 18415752; 18422738; 18424732; 18437214; 18452992; 18458086; 18462799; 18493210; 18495130; 18509450; 18517079; 18519568; 18522803; 18523439; 18541719; 18543224; 18544275; 18546014; 18549457; 18549840; 18559343; 18565796; 18586872; 18590761; 18596029; 18608206; 18618036; 18622013; 18622290; 18633131; 18634146; 18634786; 18641349; 18649875; 18650420; 18650783; 18666712; 18670786; 18680223; 18680520; 18686608; 18690351; 18698233; 18712040; 18714935; 18723631; 18725521; 18728522; 18755634; 18763053; 18763295; 18769358; 18771998; 18773284; 18775079; 18782768; 18785522; 18806258; 18809506; 18810425; 18818748; 18825409; 18826495; 18826950; 18832719; 18835634; 18845299; 18846558; 18849341; 18925411; 18927069; 18928988; 18930806; 18936436; 18942754; 18945182; 18946062; 18948841; 18950592; 18972554; 18975326; 18978678; 18983635; 18987746; 18996347; 19001446; 19006850; 19012493; 19015224; 19015258; 19017994; 19029192; 19033535; 19035500; 19035519; 19037967; 19046305; 19048480; 19050632; 19060757; 19061090; 19064998; 19067129; 19067670; 19085953; 19096003; 19106585; 19108989; 19109197; 19112167; 19118102; 19120486; 19124725; 19131814; 19134118; 19135114; 19140875; 19148143; 19148938; 19150884; 19159017; 19164128; 19181857; 19189651; 19191896; 19195606; 19200604; 19201903; 19215923; 19218437; 19238444; 19239434; 19247692; 19252480; 19254290; 19258923; 19264973; 19265114; 19265483; 19267370; 19275590; 19277200; 19280717; 19289835; 19295440; 19306954; 19317913; 19318560; 19321453; 19336370; 19336475; 19351596; 19368968; 19376887; 19380025; 19390489; 19395279; 19395541; 19398177; 19405031; 19407153; 19412184; 19412702; 19422935; 19423540; 19426173; 19430824; 19436306; 19445369; 19445990; 19447045; 19453261; 19455302; 19473079; 19483297; 19493410; 19494321; 19494325; 19496069; 19500628; 19502387; 19505919; 19509286; 19513622; 19522765; 19527514; 19528164; 19528814; 19531762; 19539691; 19541348; 19542021; 19543401; 19545686; 19546479; 19548630; 19554026; 19556306; 19556696; 19561617; 19564644; 19564704; 19566553; 19572373; 19573080; 19575238; 19578796; 19584052; 19586676; 19590686; 19592497; 19593445; 19596916; 19597734; 19614650; 19622038; 19627277; 19628747; 19631641; 19638314; 19643479; 19646345; 19646728; 19656901; 19660727; 19664207; 19691982; 19692168; 19706440; 19710105; 19723394; 19729601; 19730000; 19735472; 19737468; 19740627; 19741468; 19750015; 19754671; 19758312; 19760027; 19763595; 19764566; 19769961; 19771452; 19772581; 19773279; 19773677; 19779605; 19796532; 19796535; 19796680; 19809335; 19809507; 19810822; 19811440; 19816595; 19824106; 19826413; 19839752; 19840833; 19841637; 19844258; 19844589; 19846529; 19846881; 19847953; 19855253; 19858308; 19888805; 19891659; 19892918; 19902255; 19912257; 19913121; 19913922; 19915052; 19922963; 19924287; 19928913; 19929430; 19948740; 19948975; 19953283; 19956541; 19956717; 19960069; 20001205; 20002809; 20007708; 20007974; 20011079; 20011698; 20016852; 20018893; 20026833; 20026892; 20030948; 20037584; 20039305; 20047764; 20048342; 20056178; 20059631; 20063104; 20067961; 20067962; 20078877; 20079790; 20083228; 20085599; 20092898; 20093834; 20098705; 20105294; 20109750; 20120936; 20124101; 20125114; 20140262; 20145198; 20145615; 20146922; 20153491; 20164024; 20169003; 20170964; 20177675; 20179247; 20187300; 20194452; 20196781; 20197549; 20200442; 20201793; 20207250; 20212095; 20214986; 20222908; 20226000; 20227302; 20228668; 20228685; 20233331; 20237496; 20237756; 20299682; 20306049; 20307689; 20308035; 20331879; 20332463; 20348497; 20351099; 20357250; 20357716; 20360984; 20363151; 20364327; 20375613; 20379791; 20381257; 20384861; 20388081; 20399512; 20400193; 20400509; 20402671; 20403143; 20406964; 20412715; 20430725; 20438785; 20441696; 20442853; 20448286; 20452482; 20463618; 20472010; 20483368; 20485444; 20492496; 20496780; 20497256; 20503287; 20504212; 20504769; 20505764; 20506307; 20510162; 20518842; 20521908; 20525286; 20525894; 20556833; 20568250; 20575099; 20577092; 20587312; 20587548; 20595247; 20596538; 20596954; 20598754; 20604744; 20614721; 20616112; 20618976; 20620409; 20626741; 20628086; 20634913; 20636402; 20646321; 20646366; 20646633; 20660289; 20661259; 20664479; 20671584; 20673868; 20681284; 20685742; 20692469; 20702616; 20711192; 20711470; 20714796; 20717938; 20721625; 20725790; 20730440; 20736788; 20797905; 20799043; 20802145; 20805788; 20807077; 20818954; 20818961; 20819643; 20819670; 20819778; 20826579; 20835611; 20843333; 20848773; 20862798; 20865702; 20878353; 20880684; 20886065; 20887801; 20929567; 20933442; 20940109; 20945369; 20951669; 20952467; 20956019; 20964862; 20974832; 20977567; 20978888; 20979736; 20980751; 21033154; 21037101; 21037509; 21039068; 21042230; 21044745; 21046243; 21048031; 21050493; 21054580; 21054877; 21056683; 21059221; 21061265; 21063844; 21079743; 21081146; 21091668; 21092506; 21097451; 21099280; 21103885; 21125016; 21127066; 21129170; 21151974; 21152870; 21167252; 21168672; 21169414; 21175809; 21189260; 21191086; 21206505; 21211341; 21214494; 21220426; 21220427; 21220755; 21221801; 21236243; 21236709; 21238472; 21239179; 21246489; 21248470; 21253969; 21255012; 21262374; 21293887; 21298446; 21303685; 21306745; 21323660; 21329689; 21330606; 21356084; 21363926; 21377387; 21393102; 21398611; 21403649; 21406030; 21412052; 21417682; 21420934; 21424379; 21443084; 21455638; 21457584; 21460221; 21466684; 21468605; 21515468; 21518510; 21527067; 21538184; 21543336; 21553150; 21559380; 21563195; 21570715; 21571945; 21586524; 21602844; 21612766; 21616060; 21625017; 21628465; 21628510; 21632720; 21646346; 21649525; 21673343; 21677444; 21704385; 21704886; 21715681; 21721932; 21726670; 21729627; 21730023; 21730052; 21738462; 21752694; 21762706; 21768115; 21775336; 21776015; 21781537; 21782178; 21789185; 21789730; 21813858; 21820713; 21822168; 21827211; 21827576; 21829704; 21843566; 21852034; 21854645; 21864388; 21878171; 21883620; 21897371; 21897866; 21900253; 21902816; 21903422; 21905500; 21909400; 21911421; 21921986; 21923667; 21924074; 21924775; 21931695; 21942553; 21943186; 21949112; 21949133; 21950140; 21952248; 21968286; 21969092; 21976223; 21988832; 21990957; 21994256; 22005560; 22005564; 22011399; 22014880; 22015781; 22021706; 22022564; 22030478; 22032785; 22037282; 22046231; 22057691; 22067623; 22070100; 22085193; 22088250; 22092594; 22095710; 22100911; 22127462; 22127564; 22128242; 22131235; 22139835; 22145357; 22156348; 22166855; 22173288; 22174696; 22180778; 22194611; 22219617; 22221660; 22225630; 22229967; 22230402; 22238472; 22244044; 22251522; 22251849; 22265692; 22271762; 22272615; 22286521; 22288713; 22300618; 22302853; 22305616; 22308961; 22320262; 22330637; 22333167; 22348075; 22360682; 22372604; 22383676; 22384232; 22393779; 22396536; 22402138; 22427667; 22429552; 22433852; 22440522; 22441122; 22442690; 22447928; 22450324; 22451944; 22453525; 22461445; 22461698; 22466961; 22468087; 22474023; 22479513; 22485159; 22487528; 22499954; 22525209; 22533660; 22535679; 22537674; 22552381; 22555057; 22556042; 22560646; 22564191; 22571967; 22580394; 22582869; 22583829; 22593572; 22608210; 22613713; 22645142; 22648929; 22661708; 22662111; 22672741; 22679141; 22697069; 22699754; 22703024; 22717291; 22730532; 22733781; 22735756; 22749378; 22749779; 22753132; 22761186; 22763977; 22773901; 22775464; 22778396; 22792416; 22795952; 22807450; 22831837; 22851489; 22857799; 22870312; 22870324; 22872782; 22892989; 22906770; 22911652; 22915070; 22918682; 22927965; 22929539; 22938142; 22940059; 22948021; 22951730; 22952638; 22956123; 22962435; 22964479; 22964787; 22965987; 22970235; 22983353; 22984080; 22985132; 22987288; 22996386; 22999059; 23000519; 23021866; 23027874; 23028414; 23035361; 23053976; 23055527; 23059983; 23062767; 23065292; 23065466; 23071313; 23083518; 23084080; 23086127; 23086480; 23091345; 23093310; 23103560; 23106544; 23108090; 23121518; 23129427; 23141927; 23142582; 23163570; 23170831; 23170858; 23179584; 23179660; 23200752; 23200920; 23201091; 23209313; 23211828; 23212905; 23234648; 23239500; 23239925; 23239997; 23241898; 23251661; 23252918; 23259689; 23272070; 23275193; 23281696; 23285751; 23289411; 23289617; 23297396; 23311681; 23316065; 23318418; 23322736; 23338716; 23347362; 23355465; 23356143; 23365080; 23380629; 23398566; 23402610; 23407387; 23411097; 23414695; 23417037; 23417289; 23425749; 23436141; 23437218; 23437263; 23455503; 23455702; 23457721; 23460645; 23465595; 23467413; 23470644; 23497941; 23504385; 23510418; 23525077; 23554896; 23555011; 23565226; 23574398; 23589304; 23592020; 23592986; 23611610; 23612767; 23629657; 23633568; 23639307; 23651260; 23665674; 23671673; 23673286; 23677465; 23678609; 23680697; 23690937; 23691015; 23692033; 23727604; 23738004; 23747880; 23752129; 23755898; 23761639; 23766695; 23786414; 23798430; 23799413; 23802631; 23821954; 23828139; 23836485; 23853092; 23855294; 23864765; 23871732; 23879541; 23880187; 23888080; 23888605; 23908180; 23910802; 23921128; 23936050; 23936790; 23949880; 23962979; 23980810; 23985798; 24021278; 24030146; 24044965; 24068665; 24076166; 24080332; 24084649; 24106112; 24172224; 24178299; 24277938; 24298017; 24307174 toll-like receptor 4 Ensembl:ENSG00000136869 HGNC:11850 HPRD:04325 MIM:603030 Vega:OTTHUMG00000021046 Other designations: hToll|homolog of Drosophila toll TLR4 OGG:3000007112 Bin Zhao, Yue Liu, Oliver He CMD1T LAP2 LEMD4 PRO0868 TP WEB: http://www.ncbi.nlm.nih.gov/gene TMPO thymopoietin 7112 12q22 20140408 9606 12 protein-coding Official from a nomenclature committee GO_0000785 (EC: IDA, PMID: 17284516); GO_0003677 (EC: IEA); GO_0005515 (EC: IPI, PMID: 17474147); GO_0005521 (EC: TAS, PMID: 8530026); GO_0005634 (EC: IDA, PMID: 17284516); GO_0005634 (EC: TAS, PMID: 8530026); GO_0005635 (EC: TAS, PMID: 8530026); GO_0005637 (EC: IEA); GO_0006355 (EC: IEA); GO_0016021 (EC: IEA); GO_0031965 (EC: IDA) PMID: 302007; 2158125; 6364989; 7517549; 7703909; 8324822; 8530026; 8619474; 8743987; 9110174; 9461618; 9490046; 9707448; 10393804; 10430029; 10806084; 10984438; 11034899; 11435115; 11500367; 11591818; 12475961; 12477932; 12538639; 12950172; 15302935; 15489334; 15546916; 16083285; 16129885; 16196087; 16247757; 16344560; 16606692; 16713569; 16760672; 17081983; 17207965; 17213199; 17227891; 17284516; 17314511; 17364180; 17474147; 17558393; 17620599; 18029348; 18403046; 19135240; 19394292; 19454010; 19471022; 19727227; 19913121; 19928837; 19929986; 20237496; 20301486; 20360068; 20462248; 20562859; 20628086; 21139048; 21252943; 21549307; 21679440; 21693764; 21890473; 21906983; 21907836; 21963094; 21987572; 21990273; 22113938; 22145905; 22268729; 22412018; 22505724; 22751105; 22939629; 22990118; 23000965; 23182705; 23184937; 23463506; 23673662; 23752268; 24457600 thymopoietin Ensembl:ENSG00000120802 HGNC:11875 HPRD:01777 MIM:188380 Vega:OTTHUMG00000170210 Other designations: LEM domain containing 4|TP alpha|TP beta/gamma|lamina-associated polypeptide 2|thymopoietin-related peptide isoform alpha|thymopoietin-related peptide isoforms beta/gamma TMPO OGG:3000007113 Bin Zhao, Yue Liu, Oliver He PP9284 PRSS10 WEB: http://www.ncbi.nlm.nih.gov/gene TMPRSS2 transmembrane protease, serine 2 7113 21q22.3 20140408 9606 21 protein-coding Official from a nomenclature committee GO_0004252 (EC: IEA); GO_0005044 (EC: IEA); GO_0005887 (EC: TAS, PMID: 9325052); GO_0008236 (EC: TAS, PMID: 9325052); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 8125298; 9325052; 10485450; 10830953; 11169526; 11245484; 11322890; 11414763; 12477932; 15065083; 15342556; 15489334; 15537383; 16575875; 16585160; 16820092; 16973594; 17032499; 17207965; 17367471; 17390040; 17584912; 17632455; 17654723; 17804708; 18029348; 18065961; 18172298; 18385909; 18474293; 18483239; 18519767; 18519769; 18562527; 18583469; 18676740; 18694509; 18922926; 19029822; 19056867; 19147579; 19158246; 19190343; 19242826; 19396154; 19465903; 19494719; 19584163; 19597533; 19649210; 19664128; 19762545; 19933109; 20068566; 20118910; 20382709; 20442300; 20631123; 20798944; 20800881; 20878952; 21036922; 21040948; 21068237; 21123387; 21169414; 21325420; 21377967; 21499238; 21584900; 21600800; 21676887; 21677539; 21680704; 21731703; 21743434; 21743959; 21802835; 21937078; 22076164; 22222211; 22313860; 22558251; 22674214; 22736790; 22860005; 22930729; 22993300; 23192872; 23352841; 23447416; 23472063; 23535644; 23536651; 23701505; 23850495; 24027332; 24195515; 24227843; 24292212; 24297949 transmembrane protease, serine 2 Ensembl:ENSG00000184012 HGNC:11876 HPRD:03637 MIM:602060 Vega:OTTHUMG00000086762 Other designations: epitheliasin|serine protease 10|transmembrane protease serine 2 TMPRSS2 OGG:3000007124 Bin Zhao, Yue Liu, Oliver He DIF TNF-alpha TNFA TNFSF2 WEB: http://www.ncbi.nlm.nih.gov/gene TNF tumor necrosis factor 7124 DADB-70P7.1 6p21.3 20140408 9606 6 protein-coding Official from a nomenclature committee GO_0000060 (EC: IDA, PMID: 16280327); GO_0000122 (EC: IDA, PMID: 15345745); GO_0000165 (EC: IMP); GO_0000185 (EC: IDA, PMID: 15310755); GO_0000187 (EC: IDA, PMID: 10748004); GO_0001666 (EC: IEA); GO_0001775 (EC: IEA); GO_0001819 (EC: IDA, PMID: 17922812); GO_0001891 (EC: ISS); GO_0001934 (EC: IDA, PMID: 10748004); GO_0002020 (EC: IPI, PMID: 12777399); GO_0002037 (EC: IEA); GO_0002439 (EC: IMP, PMID: 14512626); GO_0002740 (EC: IDA, PMID: 10443688); GO_0002876 (EC: IEA); GO_0002925 (EC: IEA); GO_0003009 (EC: IEA); GO_0005125 (EC: IDA, PMID: 10748004); GO_0005164 (EC: IDA, PMID: 14512626); GO_0005515 (EC: IPI, PMID: 11878931); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 10443688); GO_0005886 (EC: TAS); GO_0005887 (EC: IDA, PMID: 18355445); GO_0006006 (EC: IEA); GO_0006915 (EC: TAS); GO_0006919 (EC: IDA, PMID: 16723520); GO_0006927 (EC: IDA, PMID: 3883195); GO_0006954 (EC: IDA, PMID: 10748004); GO_0006959 (EC: IEA); GO_0007254 (EC: IEA); GO_0008285 (EC: IEA); GO_0008625 (EC: IDA, PMID: 10521396); GO_0008625 (EC: NAS); GO_0008630 (EC: IEA); GO_0008652 (EC: IEA); GO_0009612 (EC: IEA); GO_0009615 (EC: IDA, PMID: 10490959); GO_0009651 (EC: TAS, PMID: 18355445); GO_0009887 (EC: IEA); GO_0009897 (EC: ISS); GO_0009986 (EC: IDA, PMID: 18355445); GO_0010629 (EC: IDA, PMID: 15345745); GO_0010693 (EC: IEA); GO_0010888 (EC: NAS, PMID: 16464856); GO_0014823 (EC: IEA); GO_0019722 (EC: IEA); GO_0030198 (EC: IEA); GO_0030316 (EC: IEA); GO_0030730 (EC: IDA, PMID: 19032770); GO_0031334 (EC: IDA, PMID: 12813029); GO_0031622 (EC: ISS); GO_0031663 (EC: IDA); GO_0032715 (EC: IDA, PMID: 10443688); GO_0032722 (EC: IDA, PMID: 10490959); GO_0032729 (EC: IEA); GO_0032741 (EC: IEA); GO_0032755 (EC: IEA); GO_0032800 (EC: IDA, PMID: 10443688); GO_0033138 (EC: IDA, PMID: 17389591); GO_0033209 (EC: IMP, PMID: 10748004); GO_0034116 (EC: IDA, PMID: 10604883); GO_0042346 (EC: IDA, PMID: 17922812); GO_0042493 (EC: IEA); GO_0042802 (EC: IDA, PMID: 14512626); GO_0043065 (EC: IDA, PMID: 16723520); GO_0043068 (EC: IDA, PMID: 16611992); GO_0043122 (EC: IDA, PMID: 10748004); GO_0043123 (EC: IDA, PMID: 15310755); GO_0043242 (EC: IDA, PMID: 17389591); GO_0043243 (EC: IDA, PMID: 12813029); GO_0043280 (EC: IDA, PMID: 11577081); GO_0043406 (EC: IDA, PMID: 12813029); GO_0043491 (EC: IMP); GO_0043507 (EC: IDA, PMID: 17389591); GO_0043525 (EC: IEA); GO_0044130 (EC: IEA); GO_0044212 (EC: IDA, PMID: 17350185); GO_0045071 (EC: IDA, PMID: 10490959); GO_0045080 (EC: IDA, PMID: 10490959); GO_0045121 (EC: IDA, PMID: 17010968); GO_0045416 (EC: IDA); GO_0045429 (EC: IDA, PMID: 8383325); GO_0045599 (EC: NAS, PMID: 16464856); GO_0045668 (EC: IEA); GO_0045672 (EC: IDA, PMID: 17888176); GO_0045840 (EC: IEA); GO_0045892 (EC: IDA, PMID: 16895791); GO_0045893 (EC: IDA, PMID: 10748004); GO_0045944 (EC: IDA, PMID: 15345745); GO_0045944 (EC: IGI, PMID: 16803872); GO_0045994 (EC: IEA); GO_0046325 (EC: IEA); GO_0046330 (EC: IEA); GO_0048566 (EC: IEP); GO_0048661 (EC: IDA, PMID: 16518841); GO_0050715 (EC: IDA, PMID: 10443688); GO_0050796 (EC: IDA, PMID: 8383325); GO_0050806 (EC: IEA); GO_0050830 (EC: IEA); GO_0050901 (EC: IDA, PMID: 10820279); GO_0050995 (EC: IDA, PMID: 19032770); GO_0051023 (EC: IEA); GO_0051044 (EC: IDA, PMID: 18373975); GO_0051091 (EC: IDA, PMID: 10748004); GO_0051092 (EC: IDA, PMID: 10383454); GO_0051222 (EC: IDA, PMID: 15310755); GO_0051384 (EC: IDA, PMID: 10443688); GO_0051533 (EC: IDA, PMID: 16803872); GO_0051798 (EC: IEA); GO_0051897 (EC: IEA); GO_0055037 (EC: ISS); GO_0060557 (EC: IDA, PMID: 1690216); GO_0060559 (EC: IDA, PMID: 1690216); GO_0060664 (EC: IEA); GO_0060693 (EC: IEA); GO_0061048 (EC: IDA, PMID: 17350185); GO_0070374 (EC: NAS, PMID: 18606301); GO_0071230 (EC: IEA); GO_0071316 (EC: IDA, PMID: 18676776); GO_0071407 (EC: IDA); GO_0071677 (EC: NAS); GO_0071803 (EC: IDA, PMID: 15220135); GO_0097190 (EC: TAS); GO_0097191 (EC: IDA, PMID: 11577081); GO_0097527 (EC: IDA, PMID: 11101870); GO_1902043 (EC: IEA); GO_2000010 (EC: IDA, PMID: 19366699); GO_2000343 (EC: IDA); GO_2001240 (EC: IDA, PMID: 10666185) PMID: 1279199; 1310388; 1331108; 1380260; 1402651; 1548758; 1550865; 1690216; 1905933; 1918997; 1918999; 1964681; 1993354; 2009860; 2158863; 2170559; 2413547; 2537468; 2551905; 2848815; 2922050; 2995927; 3001529; 3031624; 3139842; 3351931; 3417634; 3464978; 3552045; 3555974; 3856324; 3883195; 3932069; 6392892; 7494249; 7511078; 7523444; 7526541; 7536422; 7561697; 7664431; 7693046; 7695626; 7704970; 7706435; 7739525; 7758105; 7815507; 7818827; 7852363; 7859743; 7930591; 7935762; 7966397; 8182064; 8267288; 8288897; 8336080; 8336118; 8381971; 8383325; 8482849; 8499947; 8590321; 8597870; 8707350; 8724035; 8764000; 8806809; 8852605; 8869635; 8870842; 9034191; 9108403; 9110146; 9223523; 9225992; 9226228; 9230816; 9269771; 9269777; 9278385; 9334723; 9344703; 9378998; 9438495; 9442056; 9449720; 9488135; 9552007; 9568681; 9639071; 9651389; 9658081; 9670843; 9730685; 9744279; 9828130; 9920899; 10202016; 10205166; 10339575; 10369255; 10376933; 10383454; 10388525; 10415019; 10438928; 10443688; 10450718; 10490959; 10521396; 10604883; 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24338609; 24340926; 24371310; 24403490; 24409675; 24459820; 24611333; 24611335 tumor necrosis factor Ensembl:ENSG00000232810 HGNC:11892 HPRD:01855 MIM:191160 Vega:OTTHUMG00000031194 Other designations: APC1 protein|TNF, macrophage-derived|TNF, monocyte-derived|TNF-a|cachectin|tumor necrosis factor ligand superfamily member 2|tumor necrosis factor-alpha TNF OGG:3000007157 Bin Zhao, Yue Liu, Oliver He BCC7 LFS1 P53 TRP53 WEB: http://www.ncbi.nlm.nih.gov/gene TP53 tumor protein p53 7157 17p13.1 9606 17 Official from a nomenclature committee GO_0000060 (EC: IEA); GO_0000122 (EC: IBA); GO_0000122 (EC: IDA, PMID: 15340061); GO_0000122 (EC: ISS, PMID: 19749791); GO_0000733 (EC: IDA, PMID: 8183576); GO_0000785 (EC: IBA); GO_0000790 (EC: IDA, PMID: 15710329); GO_0000979 (EC: IEA); GO_0001077 (EC: IEA); GO_0001085 (EC: IPI, PMID: 18549481); GO_0001228 (EC: IDA, PMID: 17146433); GO_0001701 (EC: IEA); GO_0001756 (EC: IEA); GO_0001836 (EC: IEA); GO_0002020 (EC: IPI, PMID: 11923872); GO_0002039 (EC: IBA); GO_0002309 (EC: IEA); GO_0002326 (EC: IEA); GO_0002360 (EC: IEA); GO_0002931 (EC: IEA); GO_0003677 (EC: IMP, PMID: 2144364); GO_0003682 (EC: IDA, PMID: 16322561); GO_0003684 (EC: IBA); GO_0003700 (EC: IDA, PMID: 18549481); GO_0005507 (EC: IDA, PMID: 7824276); GO_0005515 (EC: IPI, PMID: 10196247); GO_0005524 (EC: IDA, PMID: 8183576); GO_0005634 (EC: IDA); GO_0005654 (EC: IDA, PMID: 11080164); GO_0005654 (EC: TAS); GO_0005657 (EC: IBA); GO_0005669 (EC: IDA, Qualifier: colocalizes_with, PMID: 15053879); GO_0005730 (EC: IDA, PMID: 12080348); GO_0005737 (EC: IDA, PMID: 14744935); GO_0005739 (EC: IDA, PMID: 12667443); GO_0005759 (EC: IEA); GO_0005783 (EC: IEA); GO_0005829 (EC: IBA); GO_0005829 (EC: IDA, PMID: 14963330); GO_0006284 (EC: TAS, PMID: 15116721); GO_0006289 (EC: IMP, PMID: 7663514); GO_0006302 (EC: IEA); GO_0006355 (EC: IDA, PMID: 7587074); GO_0006461 (EC: IDA, PMID: 12915590); GO_0006915 (EC: TAS); GO_0006974 (EC: IDA, PMID: 14744935); GO_0006977 (EC: TAS); GO_0006978 (EC: IMP, PMID: 7958916); GO_0006983 (EC: IDA, PMID: 14744935); GO_0007050 (EC: IDA, PMID: 15149599); GO_0007050 (EC: IMP, PMID: 10962037); GO_0007179 (EC: IEA); GO_0007219 (EC: TAS); GO_0007265 (EC: IEP, PMID: 9054499); GO_0007275 (EC: IMP, PMID: 10065150); GO_0007369 (EC: IEA); GO_0007406 (EC: IEA); GO_0007417 (EC: IEA); GO_0007569 (EC: IMP, PMID: 12080348); GO_0007596 (EC: TAS); GO_0008104 (EC: IDA, PMID: 16507995); GO_0008134 (EC: IPI, PMID: 15053879); GO_0008156 (EC: IEA); GO_0008270 (EC: TAS, PMID: 10065153); GO_0008283 (EC: TAS, PMID: 10065150); GO_0008285 (EC: ISS); GO_0008340 (EC: ISS); GO_0009303 (EC: IEA); GO_0009651 (EC: IEA); GO_0010165 (EC: IBA); GO_0010332 (EC: IMP, PMID: 7958916); GO_0010666 (EC: IEA); GO_0016032 (EC: IEA); GO_0016363 (EC: IDA, PMID: 11080164); GO_0016604 (EC: IDA, Qualifier: colocalizes_with, PMID: 10360174); GO_0016605 (EC: IDA, PMID: 12006491); GO_0019899 (EC: IPI, PMID: 10666337); GO_0019901 (EC: IPI, PMID: 11546806); GO_0019903 (EC: IPI); GO_0030154 (EC: TAS, PMID: 10065150); GO_0030308 (EC: IMP, PMID: 8986812); GO_0030330 (EC: IDA, PMID: 15149599); GO_0030330 (EC: IMP); GO_0030512 (EC: IEA); GO_0030971 (EC: IPI); GO_0031065 (EC: IBA); GO_0031497 (EC: IDA, PMID: 16322561); GO_0031571 (EC: IMP, PMID: 7958916); GO_0031625 (EC: IPI, PMID: 10415337); GO_0032461 (EC: IDA, PMID: 12667443); GO_0033077 (EC: IEA); GO_0034103 (EC: IEA); GO_0034613 (EC: IDA, PMID: 15340061); GO_0034644 (EC: IBA); GO_0035033 (EC: IEA); GO_0035035 (EC: IPI, PMID: 10518217); GO_0035264 (EC: IEA); GO_0035690 (EC: IEP); GO_0042149 (EC: IDA, PMID: 14744935); GO_0042771 (EC: IDA, PMID: 14654789); GO_0042802 (EC: IPI, PMID: 16291740); GO_0042981 (EC: IDA, PMID: 14744935); GO_0043065 (EC: IDA, PMID: 12667443); GO_0043066 (EC: IDA, PMID: 16131611); GO_0043066 (EC: IEA); GO_0043234 (EC: IDA, PMID: 9529249); GO_0043525 (EC: IBA); GO_0044212 (EC: IDA, PMID: 15710329); GO_0045892 (EC: ISS, PMID: 19749791); GO_0045893 (EC: IDA, PMID: 16322561); GO_0045893 (EC: IMP); GO_0045944 (EC: IDA, PMID: 11672523); GO_0045944 (EC: IGI, PMID: 16061649); GO_0045944 (EC: IMP, PMID: 17146433); GO_0046677 (EC: IEP); GO_0046902 (EC: TAS, PMID: 15116721); GO_0046982 (EC: IPI, PMID: 10837489); GO_0047485 (EC: IPI, PMID: 11861836); GO_0048147 (EC: IMP, PMID: 10962037); GO_0048568 (EC: IEA); GO_0050731 (EC: ISS, PMID: 19749791); GO_0051087 (EC: IPI, PMID: 18086682); GO_0051097 (EC: TAS, PMID: 7663514); GO_0051262 (EC: TAS, PMID: 15116721); GO_0051402 (EC: IEA); GO_0051721 (EC: IPI, PMID: 17245430); GO_0070245 (EC: ISS); GO_0071158 (EC: IMP); GO_0071456 (EC: IEP); GO_0071479 (EC: IMP); GO_0071850 (EC: IEA); GO_0072332 (EC: IMP, PMID: 12172011); GO_0090200 (EC: IDA, PMID: 12667443); GO_0090343 (EC: IEA); GO_0090399 (EC: IMP, PMID: 19951988); GO_0090403 (EC: IMP, PMID: 19951988); GO_0097193 (EC: TAS, PMID: 16462759); GO_0097252 (EC: IDA, PMID: 7720704); GO_0097371 (EC: IEA); GO_1900740 (EC: TAS); GO_1901525 (EC: IEA); GO_1902108 (EC: IEA); GO_2000378 (EC: IEA); GO_2000379 (EC: IMP); GO_2001244 (EC: IMP, PMID: 14963330) PMID: 1088347; 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22214662; 22214764; 22216266; 22216294; 22217266; 22217299; 22220854; 22223137; 22227409; 22227579; 22230478; 22230750; 22231431; 22233820; 22234063; 22235305; 22236162; 22242180; 22243433; 22244827; 22245141; 22246403; 22249259; 22249977; 22252757; 22253229; 22254155; 22258307; 22261536; 22262171; 22262183; 22262409; 22263566; 22264786; 22265402; 22265415; 22266186; 22266309; 22266850; 22266861; 22266868; 22267390; 22267755; 22275381; 22276141; 22277327; 22280536; 22282309; 22283740; 22286760; 22287741; 22289634; 22290440; 22291954; 22292621; 22293932; 22294769; 22299208; 22301190; 22302483; 22303479; 22309998; 22311583; 22319594; 22323293; 22324744; 22330136; 22331460; 22331725; 22334068; 22334079; 22334668; 22335907; 22335944; 22336889; 22336942; 22340598; 22345153; 22348878; 22349816; 22353881; 22354696; 22354970; 22357201; 22357944; 22361354; 22361592; 22362889; 22365966; 22366412; 22367371; 22370482; 22372375; 22373952; 22374402; 22374670; 22374672; 22376288; 22378745; 22381680; 22383394; 22384858; 22389383; 22389451; 22389628; 22391559; 22391565; 22392074; 22393962; 22395445; 22395499; 22395505; 22395508; 22396072; 22396451; 22398042; 22399500; 22401965; 22405092; 22406215; 22410433; 22410801; 22411991; 22416758; 22417132; 22417303; 22420423; 22421154; 22421763; 22422199; 22425911; 22427364; 22427654; 22427690; 22428663; 22430213; 22431589; 22431922; 22433872; 22434242; 22440256; 22440942; 22441365; 22444248; 22446329; 22446679; 22448750; 22451655; 22459764; 22459898; 22466965; 22467874; 22469844; 22479585; 22480684; 22483988; 22484427; 22487818; 22493095; 22495821; 22496369; 22499945; 22502699; 22503977; 22505350; 22508983; 22509368; 22510504; 22510560; 22510592; 22511763; 22514277; 22514644; 22515118; 22516242; 22523600; 22524816; 22525470; 22532853; 22534503; 22534828; 22540896; 22545084; 22546833; 22547059; 22548738; 22549273; 22549949; 22551440; 22551548; 22552282; 22555846; 22556425; 22562509; 22563078; 22564437; 22570471; 22574148; 22575263; 22575647; 22576742; 22577164; 22578566; 22579650; 22580601; 22586326; 22588298; 22588717; 22591662; 22592924; 22593196; 22593484; 22595792; 22607092; 22607702; 22609107; 22609129; 22609775; 22611192; 22611237; 22613405; 22615843; 22616991; 22621920; 22622028; 22624712; 22627629; 22628410; 22628563; 22631671; 22634494; 22641095; 22641442; 22647703; 22648906; 22652532; 22652861; 22653586; 22653678; 22659184; 22660439; 22664917; 22666537; 22668018; 22669068; 22669776; 22672907; 22673192; 22673234; 22675167; 22675170; 22675488; 22678923; 22683204; 22683628; 22685613; 22688387; 22689594; 22692183; 22696478; 22698402; 22698404; 22699455; 22700878; 22700930; 22706378; 22707142; 22710110; 22711357; 22712299; 22712728; 22714709; 22715097; 22723347; 22726440; 22728651; 22729835; 22729911; 22729912; 22730327; 22732402; 22733133; 22736329; 22737255; 22744426; 22747700; 22759751; 22761580; 22761954; 22763759; 22765508; 22768103; 22768805; 22772468; 22773013; 22773829; 22773839; 22777350; 22777358; 22777360; 22780299; 22782351; 22784258; 22787160; 22787161; 22790665; 22791815; 22797063; 22797073; 22797925; 22800615; 22801382; 22801474; 22802528; 22802529; 22803606; 22806321; 22807444; 22810507; 22811390; 22819212; 22819825; 22820403; 22824800; 22825821; 22825850; 22829776; 22829934; 22836579; 22841759; 22842154; 22843046; 22843172; 22844323; 22845047; 22847613; 22848370; 22851211; 22855178; 22855598; 22856646; 22859066; 22859294; 22859938; 22861165; 22862424; 22863952; 22864287; 22868530; 22869143; 22869710; 22869713; 22870275; 22874878; 22880004; 22886512; 22886602; 22886769; 22893124; 22894933; 22895816; 22898080; 22899716; 22899882; 22901123; 22901126; 22901221; 22902550; 22904680; 22905155; 22905229; 22906635; 22907436; 22908277; 22911014; 22911296; 22911849; 22912861; 22914606; 22914926; 22915551; 22915647; 22918438; 22919278; 22922869; 22923510; 22927405; 22927443; 22929185; 22933333; 22933706; 22934707; 22939624; 22941060; 22945757; 22948151; 22952705; 22955915; 22962266; 22964580; 22965952; 22965953; 22972749; 22975381; 22982291; 22983008; 22983585; 22984579; 22985798; 22989750; 22990118; 22990386; 22990545; 22991139; 22993345; 22994752; 22995373; 22998186; 22999923; 23009112; 23011884; 23012405; 23013791; 23020228; 23025236; 23026641; 23027126; 23028042; 23028800; 23029043; 23029260; 23034174; 23038753; 23040663; 23042265; 23042398; 23043633; 23045280; 23047509; 23049793; 23049825; 23052192; 23053979; 23054019; 23056559; 23060298; 23063560; 23065429; 23068099; 23071787; 23072722; 23073555; 23077249; 23079576; 23089923; 23092908; 23092970; 23095338; 23096687; 23100276; 23102701; 23102841; 23106581; 23110309; 23112865; 23114628; 23115335; 23118962; 23121011; 23124483; 23124863; 23125046; 23128792; 23129176; 23131771; 23133524; 23133535; 23134341; 23135266; 23139272; 23146687; 23148227; 23149933; 23150668; 23158659; 23159155; 23162013; 23165746; 23166734; 23167333; 23167335; 23167364; 23167810; 23168175; 23168703; 23168708; 23169665; 23170979; 23172776; 23175693; 23177619; 23178494; 23178529; 23178973; 23184057; 23187810; 23188674; 23192640; 23197232; 23199549; 23200676; 23201157; 23206596; 23207172; 23207289; 23208500; 23210340; 23210739; 23213260; 23214297; 23219661; 23220852; 23222509; 23224600; 23224642; 23228226; 23232572; 23235459; 23242140; 23242655; 23243274; 23243311; 23244080; 23246487; 23246812; 23246961; 23253087; 23255126; 23255232; 23255396; 23255406; 23259501; 23261415; 23261448; 23261524; 23262097; 23263379; 23268317; 23268330; 23268708; 23268996; 23269546; 23269799; 23272046; 23273944; 23273978; 23284306; 23285001; 23287481; 23287532; 23289390; 23291854; 23291982; 23291986; 23292286; 23292895; 23293969; 23297687; 23299342; 23306062; 23306555; 23313511; 23315175; 23316052; 23317197; 23317213; 23317414; 23317892; 23318437; 23318444; 23319048; 23319609; 23319651; 23324352; 23324739; 23328582; 23329847; 23335286; 23341181; 23341460; 23343762; 23343766; 23344532; 23354312; 23354912; 23356234; 23356517; 23356739; 23358872; 23359201; 23359294; 23360829; 23360998; 23361940; 23363223; 23370271; 23374541; 23376231; 23378270; 23379189; 23380758; 23382381; 23382584; 23383273; 23384026; 23386643; 23387809; 23388101; 23388179; 23388826; 23392172; 23397771; 23398456; 23401182; 23401530; 23402884; 23403321; 23404110; 23404342; 23404471; 23409163; 23412343; 23412385; 23416147; 23416275; 23416979; 23417151; 23421999; 23422071; 23423487; 23423975; 23429506; 23431171; 23433851; 23435014; 23435420; 23435461; 23437037; 23442362; 23447676; 23449391; 23451161; 23452320; 23453606; 23455382; 23455922; 23456460; 23462994; 23468244; 23470568; 23471665; 23472201; 23478443; 23482364; 23483203; 23483263; 23487038; 23487462; 23492369; 23492773; 23497522; 23499753; 23504554; 23507139; 23510323; 23514281; 23515929; 23516071; 23516500; 23519249; 23519469; 23521708; 23522190; 23524907; 23525475; 23525797; 23528269; 23528315; 23534750; 23536279; 23536437; 23543742; 23545415; 23545901; 23547411; 23550211; 23555186; 23555710; 23558569; 23559007; 23559009; 23563200; 23564481; 23571142; 23571737; 23572512; 23572574; 23573956; 23574746; 23575399; 23576507; 23576563; 23578198; 23578831; 23580068; 23583237; 23583409; 23583620; 23583669; 23585871; 23586029; 23588418; 23589328; 23589839; 23595149; 23595658; 23596757; 23599430; 23602568; 23603558; 23604351; 23607988; 23608226; 23608884; 23609977; 23612020; 23612969; 23612976; 23613387; 23613399; 23613406; 23620080; 23620409; 23620777; 23624524; 23624687; 23624782; 23624843; 23626008; 23630584; 23632916; 23639512; 23640975; 23643883; 23649769; 23649806; 23649808; 23650532; 23650552; 23652204; 23653000; 23653187; 23657012; 23663243; 23665236; 23665932; 23667851; 23670029; 23670238; 23671280; 23676490; 23677994; 23678008; 23678541; 23683469; 23684722; 23686119; 23686257; 23687300; 23687381; 23702906; 23706820; 23706821; 23708675; 23715779; 23716179; 23717592; 23718721; 23720736; 23722592; 23727578; 23727990; 23728348; 23729685; 23733769; 23736031; 23739040; 23742673; 23743335; 23744327; 23745682; 23747015; 23747308; 23747528; 23748877; 23752197; 23759592; 23760493; 23762372; 23764844; 23772552; 23775119; 23775793; 23785149; 23785201; 23786219; 23786650; 23788249; 23790165; 23793604; 23794094; 23796514; 23796712; 23799027; 23799104; 23800173; 23800953; 23802716; 23804139; 23811687; 23812725; 23812727; 23817390; 23818345; 23818355; 23818364; 23826318; 23835407; 23835706; 23836507; 23837945; 23841076; 23844043; 23844254; 23845906; 23851436; 23852341; 23860773; 23863845; 23870121; 23870475; 23873310; 23878395; 23880211; 23880345; 23880760; 23881403; 23886144; 23894400; 23896410; 23907539; 23908595; 23908596; 23915071; 23916609; 23918540; 23933584; 23935506; 23936455; 23942113; 23946421; 23954287; 23954291; 23954467; 23959174; 23959540; 23960076; 23962557; 23965232; 23966169; 23966171; 23966406; 23966881; 23967302; 23971040; 23973262; 23973461; 23977882; 23981578; 23982177; 23990016; 23991992; 23994832; 24001612; 24003224; 24006363; 24006461; 24008423; 24012673; 24014029; 24022481; 24023291; 24023325; 24025248; 24026986; 24029231; 24032713; 24038938; 24042100; 24043769; 24044511; 24045667; 24046089; 24052075; 24053468; 24056649; 24061453; 24067370; 24067899; 24067978; 24074410; 24076372; 24078252; 24091621; 24099634; 24101517; 24113167; 24113472; 24120139; 24122997; 24129246; 24134839; 24143256; 24145651; 24163369; 24164297; 24183724; 24190973; 24200963; 24209622; 24219989; 24220032; 24231352; 24239288; 24240685; 24241536; 24248600; 24256616; 24272483; 24285725; 24289924; 24314634; 24316591; 24323028; 24344030; 24361594; 24379070; 24379358; 24403473; 24434386; 24449575; 24617039 tumor protein p53 Ensembl:ENSG00000141510 HGNC:11998 HPRD:01859 MIM:191170 Vega:OTTHUMG00000162125 Other designations: antigen NY-CO-13|cellular tumor antigen p53|mutant tumor protein 53|p53 tumor suppressor|phosphoprotein p53|transformation-related protein 53|tumor protein 53 TP53 gene OGG:3000007184 Bin Zhao, Yue Liu, Oliver He ECGP GP96 GRP94 HEL-S-125m HEL35 TRA1 WEB: http://www.ncbi.nlm.nih.gov/gene HSP90B1 heat shock protein 90kDa beta (Grp94), member 1 7184 12q24.2-q24.3 9606 12 Official from a nomenclature committee GO_0001666 (EC: IDA, PMID: 15620698); GO_0002224 (EC: TAS); GO_0003723 (EC: IDA, PMID: 11958450); GO_0005509 (EC: TAS, PMID: 10497210); GO_0005515 (EC: IPI, PMID: 11907036); GO_0005524 (EC: IEA); GO_0005576 (EC: TAS); GO_0005783 (EC: IDA); GO_0005783 (EC: TAS, PMID: 16130169); GO_0005788 (EC: IDA, PMID: 10497210); GO_0005788 (EC: TAS); GO_0005789 (EC: IDA, PMID: 10497210); GO_0005829 (EC: IDA, PMID: 9596688); GO_0005886 (EC: IEA); GO_0006457 (EC: IEA); GO_0006987 (EC: TAS); GO_0015031 (EC: NAS, PMID: 15845869); GO_0019903 (EC: IDA, PMID: 19000834); GO_0030433 (EC: IMP, PMID: 18264092); GO_0030496 (EC: IDA, PMID: 15166316); GO_0030968 (EC: TAS); GO_0031247 (EC: IDA, PMID: 19000834); GO_0042470 (EC: IEA); GO_0043066 (EC: IMP, PMID: 10497210); GO_0043066 (EC: TAS, PMID: 16130169); GO_0043666 (EC: IDA, PMID: 19000834); GO_0044267 (EC: TAS); GO_0045087 (EC: TAS); GO_0046790 (EC: IPI, PMID: 11958450); GO_0048471 (EC: IDA, PMID: 10497210); GO_0050750 (EC: IDA, PMID: 15082773); GO_0051082 (EC: IEA); GO_0051208 (EC: NAS, PMID: 15192333); GO_0070062 (EC: IDA, PMID: 19199708); GO_0071318 (EC: IDA, PMID: 19000834); GO_0071682 (EC: TAS) PMID: 1512535; 1923827; 2377606; 2378869; 2546060; 2924290; 7523574; 7768954; 8460400; 8617772; 9006956; 9596688; 9694898; 10049727; 10497210; 10887119; 11557039; 11584270; 11726552; 11861214; 11907036; 11912201; 11958450; 12167617; 12397072; 12470827; 12471035; 12475965; 12477932; 12643545; 12654781; 12665801; 12754519; 14499622; 14500642; 15082718; 15082773; 15107540; 15166316; 15192333; 15257553; 15489334; 15576338; 15620698; 15637761; 15728573; 15845869; 15952740; 15962384; 16015374; 16130169; 16257961; 16263699; 16269234; 16288044; 16335966; 16497268; 16630554; 16754684; 17081065; 17082602; 17347446; 17431395; 17545519; 17558393; 17612505; 17726464; 17805476; 17936703; 18029348; 18155754; 18178560; 18190237; 18239673; 18264092; 18273841; 18331622; 18340425; 18411291; 18482745; 18554719; 18662321; 18781797; 18816836; 18941243; 19000834; 19135240; 19199708; 19212831; 19343720; 19578160; 19615732; 19697319; 19724918; 19752220; 19875450; 19895174; 19913121; 20000738; 20159978; 20176102; 20195357; 20232284; 20237496; 20300187; 20351288; 20352117; 20510162; 20562859; 20599762; 20628086; 20704820; 20721957; 20811636; 20839070; 20936779; 21081666; 21110914; 21139048; 21145461; 21208614; 21319273; 21343306; 21472681; 21559462; 21565611; 21637029; 21642380; 21708117; 21739154; 21774995; 21890473; 21900206; 21906983; 21963094; 21988832; 21992474; 21998592; 22079093; 22174317; 22178446; 22190034; 22245095; 22268729; 22270544; 22304920; 22363530; 22427667; 22532561; 22554506; 22653265; 22672426; 22724016; 22777994; 22863883; 22938940; 22939629; 23000965; 23035116; 23077236; 23097496; 23109341; 23182705; 23190606; 23208072; 23266770; 23349634; 23428871; 23431407; 23455922; 23503679; 23589305; 23703321; 23755898; 23798571; 23862649; 24244333; 24457600; 24511009 heat shock protein 90kDa beta (Grp94), member 1 Ensembl:ENSG00000166598 HGNC:12028 HPRD:01860 MIM:191175 Vega:OTTHUMG00000170118 Other designations: 94 kDa glucose-regulated protein|endoplasmin|endothelial cell (HBMEC) glycoprotein|epididymis luminal protein 35|epididymis secretory sperm binding protein Li 125m|heat shock protein 90 kDa beta member 1|stress-inducible tumor rejection antigen gp96|tumor rejection antigen (gp96) 1|tumor rejection antigen 1 HSP90B1 OGG:3000007186 Bin Zhao, Yue Liu, Oliver He MGC:45012 TRAP TRAP3 WEB: http://www.ncbi.nlm.nih.gov/gene TRAF2 TNF receptor-associated factor 2 7186 9q34 9606 9 Official from a nomenclature committee GO_0002726 (EC: IMP, PMID: 15125833); GO_0004842 (EC: IDA, PMID: 15258597); GO_0004871 (EC: NAS, PMID: 8702708); GO_0005164 (EC: IPI, PMID: 11279055); GO_0005174 (EC: ISS); GO_0005515 (EC: IPI, PMID: 10514511); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005938 (EC: IEA); GO_0006461 (EC: TAS, PMID: 8702708); GO_0006915 (EC: TAS); GO_0006919 (EC: TAS); GO_0007165 (EC: TAS, PMID: 8702708); GO_0007250 (EC: IMP, PMID: 15125833); GO_0008270 (EC: IEA); GO_0009898 (EC: ISS); GO_0019899 (EC: IPI, PMID: 16636664); GO_0019903 (EC: IPI, PMID: 15696169); GO_0030163 (EC: IEA); GO_0031435 (EC: IEA); GO_0031625 (EC: IPI, PMID: 11279055); GO_0031996 (EC: IPI, PMID: 11279055); GO_0032403 (EC: IEA); GO_0032743 (EC: IMP, PMID: 15125833); GO_0033209 (EC: IDA, PMID: 11907583); GO_0034351 (EC: IEA); GO_0035631 (EC: ISS); GO_0042802 (EC: IPI, PMID: 16189514); GO_0042981 (EC: IDA, PMID: 11907583); GO_0043507 (EC: IDA, PMID: 11907583); GO_0043623 (EC: ISS); GO_0045087 (EC: TAS); GO_0045121 (EC: IEA); GO_0046625 (EC: IDA); GO_0050870 (EC: IC, PMID: 15125833); GO_0051023 (EC: IEA); GO_0051091 (EC: IMP, PMID: 12296995); GO_0051092 (EC: IDA, PMID: 11279055); GO_0051092 (EC: IMP, PMID: 12296995); GO_0051291 (EC: IEA); GO_0051865 (EC: IDA); GO_0051865 (EC: TAS, PMID: 16378096); GO_0070207 (EC: IPI); GO_0070534 (EC: IDA, PMID: 15258597); GO_0090073 (EC: IMP, PMID: 11278723); GO_0097190 (EC: TAS); GO_2001238 (EC: IMP); GO_2001239 (EC: TAS) PMID: 7639698; 7758105; 8069916; 8125298; 8548810; 8565075; 8612133; 8627180; 8643514; 8662842; 8692885; 8702708; 8710854; 8875942; 8943045; 8985011; 8999898; 9020361; 9104814; 9153189; 9162022; 9168896; 9208847; 9244310; 9275204; 9353251; 9384571; 9418902; 9461607; 9464265; 9488716; 9500555; 9582383; 9607925; 9685412; 9692890; 9705938; 9712898; 9718306; 9733516; 9774460; 9774977; 9794406; 9827693; 9852070; 9990007; 10025951; 10037686; 10075662; 10206649; 10339433; 10346818; 10352240; 10411888; 10477597; 10490605; 10514511; 10521462; 10523862; 10544141; 10581243; 10617615; 10650002; 10753917; 10759890; 10764746; 10809768; 10837247; 10880535; 10882101; 10892748; 10903733; 10911999; 10980203; 10990461; 11035039; 11057907; 11064452; 11112773; 11181075; 11278268; 11278723; 11279055; 11340079; 11359906; 11384837; 11435475; 11466612; 11479302; 11562359; 11607847; 11728344; 11777919; 11784851; 11798190; 11804591; 11805080; 11821416; 11882293; 11907088; 11907583; 11909853; 11932422; 11971184; 12005438; 12136106; 12169272; 12220533; 12296995; 12411322; 12411493; 12477932; 12529173; 12547194; 12571250; 12591926; 12637493; 12796506; 12842894; 12843613; 12867425; 12887920; 12917689; 12917690; 12917691; 14517219; 14557256; 14585990; 14633987; 14644197; 14702039; 14741690; 14743216; 14982987; 15084608; 15121867; 15125833; 15208311; 15258597; 15265700; 15308666; 15310755; 15327770; 15383523; 15485634; 15485837; 15489334; 15670770; 15670977; 15696169; 15707590; 15708970; 15743837; 15861135; 15941918; 15944293; 16009713; 16153868; 16189514; 16214042; 16227629; 16260598; 16263936; 16282325; 16291755; 16304992; 16311516; 16341674; 16378096; 16446357; 16603398; 16611992; 16636664; 16713569; 16876162; 16891304; 16936264; 17015619; 17314283; 17379600; 17384642; 17389591; 17544371; 17599408; 17626074; 17724081; 17851586; 17923499; 18022363; 18024283; 18029348; 18069092; 18230756; 18271526; 18292192; 18312353; 18362156; 18362886; 18671942; 18776134; 18787502; 18818748; 18827186; 18950704; 18981220; 18990758; 19019335; 19150425; 19151112; 19234489; 19243308; 19287455; 19336370; 19380743; 19453261; 19506082; 19527514; 19573080; 19584093; 19586614; 19667091; 19690440; 19773279; 19795416; 19810754; 19815509; 19815541; 19937093; 20005846; 20047764; 20056178; 20064526; 20133937; 20138174; 20184394; 20237496; 20333651; 20348096; 20368287; 20385093; 20447407; 20448643; 20449947; 20562859; 20568250; 20577214; 20585848; 20614026; 20628086; 20676093; 20732415; 20856938; 20949042; 20972266; 20974987; 21041452; 21041727; 21071692; 21078302; 21078624; 21119000; 21139048; 21229359; 21266470; 21282461; 21282507; 21289304; 21325409; 21331077; 21421854; 21620750; 21653699; 21793045; 21810480; 21864338; 21886773; 21890473; 21903422; 21906983; 21921033; 21963094; 21987572; 21988832; 22029577; 22078441; 22167321; 22170762; 22179575; 22184250; 22195745; 22212761; 22271254; 22343716; 22505724; 22525270; 22550173; 22585859; 22685297; 22711886; 22732732; 22792062; 22847298; 22863753; 23000965; 23007157; 23051914; 23088713; 23142077; 23160117; 23188828; 23301098; 23319823; 23357418; 23381138; 23405219; 23414308; 23453969; 23524849; 23543740; 23595117; 23608757; 23624947; 23638224; 23690480; 23743189; 23754945; 23775076; 23885119; 23890813; 23918987; 23972990; 24008839; 24434549; 24457600 TNF receptor-associated factor 2 Ensembl:ENSG00000127191 HGNC:12032 HPRD:03538 MIM:601895 Vega:OTTHUMG00000020952 Other designations: E3 ubiquitin-protein ligase TRAF2|tumor necrosis factor type 2 receptor associated protein 3|tumor necrosis factor type 2 receptor-associated protein 3 TRAF2 OGG:3000007187 Bin Zhao, Yue Liu, Oliver He CAP-1 CAP1 CD40bp CRAF1 IIAE5 LAP1 WEB: http://www.ncbi.nlm.nih.gov/gene TRAF3 TNF receptor-associated factor 3 7187 14q32.32 9606 14 Official from a nomenclature committee GO_0001817 (EC: ISS); GO_0002224 (EC: ISS); GO_0002224 (EC: TAS); GO_0002756 (EC: TAS); GO_0004842 (EC: IEA); GO_0004871 (EC: TAS, PMID: 7530216); GO_0005515 (EC: IPI, PMID: 10791955); GO_0005739 (EC: IEA); GO_0005768 (EC: IEA); GO_0005829 (EC: TAS); GO_0006915 (EC: IEA); GO_0007165 (EC: TAS, PMID: 7530216); GO_0008270 (EC: IEA); GO_0009898 (EC: ISS); GO_0019901 (EC: IEA); GO_0030162 (EC: IMP); GO_0031625 (EC: IPI, PMID: 11279055); GO_0031996 (EC: IPI, PMID: 11279055); GO_0032088 (EC: IMP); GO_0032480 (EC: TAS); GO_0032648 (EC: ISS); GO_0033209 (EC: IMP); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0035631 (EC: ISS); GO_0035666 (EC: TAS); GO_0042981 (EC: IEA); GO_0045087 (EC: TAS); GO_0050688 (EC: ISS) PMID: 7527023; 7530216; 7533327; 7859281; 8565075; 8612133; 8626767; 8662842; 8663299; 8710854; 9122217; 9162022; 9168896; 9275204; 9384571; 9388227; 9418902; 9464265; 9488716; 9550380; 9582383; 9718306; 9774460; 9774977; 9794406; 9852070; 9990007; 10025951; 10037686; 10199393; 10207006; 10352240; 10514511; 10523862; 10557073; 10635328; 10644711; 10764746; 10781837; 10791955; 10799510; 10809768; 10837247; 10862698; 10903733; 10984535; 11035039; 11098060; 11226259; 11261798; 11278268; 11279055; 11384837; 11435475; 11562359; 11607847; 11728344; 11950878; 12005438; 12089335; 12136149; 12169272; 12220533; 12270937; 12471121; 12477932; 12529173; 12571250; 12637493; 12860972; 14517219; 14572659; 14716302; 14743216; 14982987; 15084608; 15208311; 15280356; 15383523; 15485634; 15489334; 15514968; 15585864; 15708970; 15941918; 15944293; 16009714; 16260598; 16280329; 16306936; 16311516; 16429118; 16582590; 16858409; 17544371; 17586463; 17608743; 17626074; 17692805; 17823124; 17878343; 17991829; 18042799; 18275617; 18607851; 18614628; 19023125; 19074885; 19419966; 19667091; 19693093; 19893624; 19913121; 19937093; 19954665; 19996094; 20008286; 20056178; 20080758; 20097753; 20138174; 20161788; 20174559; 20185819; 20237496; 20348096; 20504251; 20585848; 20614026; 20628086; 20800603; 20832341; 21041452; 21041727; 21084666; 21139048; 21200404; 21228035; 21660053; 21703539; 21864338; 21885437; 21890473; 21903422; 21906983; 21963094; 21988832; 22011580; 22017431; 22022264; 22079989; 22330071; 22469134; 22709905; 22715070; 22792062; 22901541; 22908223; 22945920; 23303668; 23308279; 23329887; 23333941; 23334419; 23381138; 23524849; 23543740; 23612708; 23717208; 23962979; 23986588; 24260396 TNF receptor-associated factor 3 Ensembl:ENSG00000131323 HGNC:12033 HPRD:03539 MIM:601896 Vega:OTTHUMG00000171902 Other designations: CD40 associated protein 1|CD40 binding protein|CD40 receptor associated factor 1|LMP1-associated protein 1 TRAF3 OGG:3000007266 Bin Zhao, Yue Liu, Oliver He DJ11 DJC7 TPR2 TTC2 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC7 DnaJ (Hsp40) homolog, subfamily C, member 7 7266 17q11.2 9606 17 GO_0005515 (EC: IPI); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005856 (EC: IEA); GO_0006457 (EC: TAS, PMID:8836031); GO_0031072 (EC: IPI, PMID:12853476); GO_0070062 (EC: IDA, PMID:19056867); GO_0070389 (EC: IDA, PMID:12853476) PMID:8836031; 10567422; 11076863; 11147971; 11230166; 11573955; 12477932; 12853476; 15189447; 15231748; 15342556; 15489334; 15489336; 15592455; 15761153; 16381901; 17043677; 18029348; 18620420; 19056867; 19875381; 20473970; 20562859; 20661446; 20936779; 21139048; 21145461; 21890473; 21906983; 21963094; 21987572; 22118674; 22190034; 22337587; 22623428; 22863883; 22944692; 22990118; 23000965; 23261415; 23438482; 23455922 DnaJ (Hsp40) homolog, subfamily C, member 7 Ensembl:ENSG00000168259 HGNC:12392 MIM:601964 Vega:OTTHUMG00000180862 Other designations: TPR repeat protein 2|dnaJ homolog subfamily C member 7|tetratricopeptide repeat domain 2|tetratricopeptide repeat protein 2 DNAJC7 OGG:3000007291 Bin Zhao, Yue Liu, Oliver He ACS3 BPES2 BPES3 CRS CRS1 SCS TWIST bHLHa38 WEB: http://www.ncbi.nlm.nih.gov/gene TWIST1 twist family bHLH transcription factor 1 7291 7p21.2 9606 7 Official from a nomenclature committee GO_0000122 (EC: IMP, PMID: 17690110); GO_0000981 (EC: IDA, PMID: 17332325); GO_0001503 (EC: TAS, PMID: 11001584); GO_0001649 (EC: IEA); GO_0001701 (EC: IEA); GO_0001764 (EC: IEA); GO_0001843 (EC: IEA); GO_0003180 (EC: IMP); GO_0003183 (EC: IEA); GO_0003203 (EC: IEA); GO_0003253 (EC: IEA); GO_0005515 (EC: IPI, PMID: 18504427); GO_0005634 (EC: IDA, PMID: 10749989); GO_0006366 (EC: IDA, PMID: 17332325); GO_0007517 (EC: IEA); GO_0008134 (EC: IPI, PMID: 15545268); GO_0010628 (EC: IMP, PMID: 17003487); GO_0010718 (EC: IMP, PMID: 18297062); GO_0014067 (EC: IMP, PMID: 17003487); GO_0019904 (EC: IEA); GO_0030500 (EC: IMP, PMID: 19597909); GO_0032000 (EC: IMP); GO_0032720 (EC: IEA); GO_0032760 (EC: IMP); GO_0033128 (EC: IMP, PMID: 17690110); GO_0035067 (EC: IEA); GO_0035115 (EC: IEA); GO_0035116 (EC: IEA); GO_0035359 (EC: IEA); GO_0042473 (EC: TAS, PMID: 11001584); GO_0042476 (EC: IEA); GO_0042733 (EC: TAS, PMID: 11001584); GO_0042803 (EC: IEA); GO_0043066 (EC: IEA); GO_0043425 (EC: IPI, PMID: 10749989); GO_0043433 (EC: IEA); GO_0043518 (EC: IMP, PMID: 17690110); GO_0045668 (EC: IMP, PMID: 16888803); GO_0045766 (EC: NAS, PMID: 17987801); GO_0045944 (EC: IDA, PMID: 17332325); GO_0045944 (EC: IMP, PMID: 12270142); GO_0046982 (EC: IEA); GO_0048642 (EC: IEA); GO_0048701 (EC: IMP, PMID: 8988166); GO_0050679 (EC: IEA); GO_0060021 (EC: IEA); GO_0060363 (EC: TAS, PMID: 11001584); GO_0060900 (EC: IMP, PMID: 17070479); GO_0061029 (EC: IMP, PMID: 17070479); GO_0070888 (EC: IDA, PMID: 17332325); GO_0071363 (EC: IEA); GO_0071456 (EC: IMP, PMID: 18297062); GO_0071639 (EC: IMP); GO_2000147 (EC: IMP, PMID: 17332325); GO_2000147 (EC: NAS, PMID: 17332324); GO_2000276 (EC: IEA); GO_2000679 (EC: IMP, PMID: 12270142); GO_2000773 (EC: IMP, PMID: 17690110); GO_2000778 (EC: IMP); GO_2000780 (EC: IMP, PMID: 17690110); GO_2000793 (EC: IMP); GO_2000802 (EC: IEA) PMID: 1433226; 7296937; 7987323; 8968762; 8988166; 8988167; 8995765; 9073070; 9215678; 9259286; 9343420; 9934984; 10025406; 10465122; 10485844; 10749989; 11001584; 11062344; 11474656; 11748846; 11754069; 11854168; 11948912; 11977182; 12015302; 12142027; 12218784; 12270142; 12477932; 12553906; 12690205; 12791045; 12853948; 14513358; 14724576; 15210113; 15313894; 15489334; 15545268; 15555546; 15607966; 15735646; 15880747; 15900593; 15958559; 16229805; 16293629; 16322226; 16412561; 16502419; 16540516; 16737925; 16831897; 16888803; 17003487; 17070479; 17157810; 17236203; 17332324; 17332325; 17343269; 17394502; 17403902; 17414280; 17487558; 17512904; 17690110; 17785550; 17886095; 17893140; 17925286; 17967182; 17987801; 18062917; 18172301; 18231738; 18255367; 18297062; 18349132; 18353781; 18391499; 18440840; 18480983; 18504427; 18519689; 18549475; 18598946; 18663125; 18974133; 19051271; 19064546; 19094228; 19276370; 19345188; 19373776; 19381684; 19412634; 19453261; 19470737; 19513566; 19534813; 19597909; 19609939; 19644484; 19802001; 19816777; 19821482; 19851501; 19860490; 19863427; 19893041; 19954024; 20007935; 20019840; 20025748; 20079104; 20140954; 20219012; 20301368; 20388391; 20400975; 20400976; 20496080; 20505321; 20562331; 20564230; 20628624; 20634891; 20643727; 20646316; 20696219; 20714342; 20804746; 20818389; 20838384; 20857420; 20920982; 20943789; 20970163; 21083641; 21123820; 21138866; 21199805; 21208645; 21316706; 21317430; 21324165; 21333765; 21389145; 21397860; 21461979; 21464926; 21478681; 21502402; 21503964; 21532573; 21539816; 21559372; 21559426; 21594904; 21677079; 21732143; 21740802; 21748764; 21796367; 21822911; 21834956; 21854747; 21864967; 21866569; 21883379; 21884981; 21914771; 21919891; 21931630; 21983900; 21994965; 22002117; 22006115; 22006371; 22007485; 22020939; 22050045; 22056872; 22060274; 22102471; 22110753; 22155737; 22166980; 22178381; 22184289; 22241470; 22245869; 22253230; 22266852; 22272264; 22288519; 22290439; 22331730; 22349827; 22354994; 22360285; 22407364; 22457607; 22515221; 22532563; 22544111; 22576709; 22581441; 22581828; 22654667; 22668877; 22797064; 22820497; 22847601; 22896337; 22899291; 22961111; 22965800; 22974478; 22974479; 22975381; 22982861; 22983574; 23029385; 23052737; 23056278; 23095743; 23150175; 23158991; 23161342; 23167357; 23222305; 23232513; 23251661; 23329645; 23354436; 23375009; 23429988; 23500436; 23530115; 23613408; 23623921; 23664538; 23682613; 23684708; 23691243; 23696034; 23741524; 23775496; 23815808; 23825006; 23845905; 23873099; 23889968; 23928864; 23935104; 23990016; 23994666; 24051309; 24085799; 24148247; 24150986; 24157255; 24457449 twist family bHLH transcription factor 1 Ensembl:ENSG00000122691 HGNC:12428 HPRD:03374 MIM:601622 Vega:OTTHUMG00000090821 Other designations: B-HLH DNA binding protein|H-twist|TWIST homolog of drosophila|class A basic helix-loop-helix protein 38|craniosynostosis|twist basic helix-loop-helix transcription factor 1|twist homolog 1|twist-related protein 1 TWIST1 OGG:3000007296 Bin Zhao, Yue Liu, Oliver He GRIM-12 TR TR1 TRXR1 TXNR WEB: http://www.ncbi.nlm.nih.gov/gene TXNRD1 thioredoxin reductase 1 7296 12q23-q24.1 9606 12 Official from a nomenclature committee GO_0001707 (EC: IEA); GO_0004791 (EC: EXP); GO_0005515 (EC: IPI, PMID: 19820694); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005739 (EC: IEA); GO_0005829 (EC: TAS); GO_0007165 (EC: NAS, PMID: 8921404); GO_0008283 (EC: IEA); GO_0009055 (EC: IEA); GO_0015035 (EC: IEA); GO_0015949 (EC: TAS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0045454 (EC: IEA); GO_0050660 (EC: IEA); GO_0050661 (EC: IEA); GO_0055086 (EC: TAS) PMID: 2064786; 7589432; 8554614; 8577704; 8650234; 8921404; 8999974; 9177183; 9207062; 9671710; 9774665; 10383413; 10432307; 10786696; 11353774; 11375392; 11410332; 11737861; 11782468; 11953436; 12214272; 12435734; 12477932; 12574159; 12668662; 12949356; 12968334; 13679440; 14607844; 14676218; 14980707; 15123685; 15183196; 15199063; 15489334; 15592455; 15824742; 15879598; 16009940; 16169070; 16344560; 16424062; 16481328; 16750198; 16815975; 16868544; 16977661; 17382897; 17512005; 17601350; 17634480; 18029348; 18042542; 18163424; 18187038; 18267104; 18382651; 18483336; 18835810; 18977241; 18996185; 19020731; 19059456; 19124506; 19322201; 19555664; 19595745; 19620238; 19654027; 19766715; 19820694; 19896490; 20160040; 20536427; 20584310; 20877624; 20920480; 21139048; 21172426; 21206984; 21593104; 21693764; 21890473; 21906983; 21963094; 21988832; 22053931; 22230366; 22505724; 22863883; 22939629; 22977247; 23000965; 23063346; 23223577; 23413027; 23512591; 23603921; 24515614 thioredoxin reductase 1 Ensembl:ENSG00000198431 HGNC:12437 HPRD:03068 MIM:601112 Vega:OTTHUMG00000166481 Other designations: KM-102-derived reductase-like factor|gene associated with retinoic and IFN-induced mortality 12 protein|gene associated with retinoic and interferon-induced mortality 12 protein|oxidoreductase|thioredoxin reductase 1, cytoplasmic|thioredoxin reductase GRIM-12|thioredoxin reductase TR1 TXNRD1 OGG:3000007298 Bin Zhao, Yue Liu, Oliver He HST422 TMS TS WEB: http://www.ncbi.nlm.nih.gov/gene TYMS thymidylate synthetase 7298 OK/SW-cl.29 18p11.32 9606 18 Official from a nomenclature committee GO_0000082 (EC: TAS); GO_0000083 (EC: TAS); GO_0000166 (EC: IEA); GO_0000278 (EC: TAS); GO_0003729 (EC: IEA); GO_0004799 (EC: TAS); GO_0005542 (EC: IEA); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0005730 (EC: IEA); GO_0005737 (EC: IDA); GO_0005739 (EC: IDA); GO_0005743 (EC: IDA); GO_0005759 (EC: IDA); GO_0005829 (EC: TAS); GO_0005976 (EC: IEA); GO_0006139 (EC: TAS, PMID: 2987839); GO_0006206 (EC: TAS); GO_0006231 (EC: IEA); GO_0006235 (EC: IEA); GO_0006260 (EC: NAS, PMID: 15504738); GO_0006281 (EC: NAS, PMID: 15504738); GO_0007568 (EC: IEA); GO_0007623 (EC: IEA); GO_0008144 (EC: IEA); GO_0009157 (EC: TAS, PMID: 2987839); GO_0009636 (EC: IEA); GO_0019088 (EC: IEA); GO_0019860 (EC: IEA); GO_0031100 (EC: IEA); GO_0032570 (EC: IEA); GO_0033189 (EC: IEA); GO_0034097 (EC: IEA); GO_0042493 (EC: IEA); GO_0042803 (EC: IEA); GO_0044281 (EC: TAS); GO_0045471 (EC: IEA); GO_0046078 (EC: IEA); GO_0046134 (EC: TAS); GO_0046653 (EC: IEA); GO_0046683 (EC: IEP, PMID: 16079077); GO_0048015 (EC: NAS, PMID: 15504738); GO_0048037 (EC: IEA); GO_0048589 (EC: IEA); GO_0051216 (EC: IEA); GO_0051384 (EC: IEA); GO_0051593 (EC: IEA); GO_0055086 (EC: TAS); GO_0060574 (EC: IEA) PMID: 1720706; 2243092; 2532645; 2656695; 2987839; 3839505; 8125298; 8449516; 8845352; 9148948; 11102983; 11251009; 11251164; 11278511; 11316879; 11329255; 11445856; 11697906; 11747337; 11799066; 11804689; 11937185; 11989786; 11992400; 12018454; 12067974; 12084458; 12084459; 12084460; 12084461; 12084462; 12147691; 12215845; 12220503; 12239455; 12466474; 12477932; 12530000; 12576451; 12576452; 12604405; 12640689; 12684695; 12706868; 12782596; 12845668; 12859954; 12907731; 12972956; 14519634; 14519641; 14576935; 14578129; 14586640; 14656021; 14702180; 14745930; 14760062; 14967037; 14970324; 14977639; 15093541; 15115918; 15161716; 15198953; 15213713; 15231747; 15244514; 15251465; 15259039; 15260847; 15284183; 15316940; 15355920; 15386366; 15386371; 15457444; 15459215; 15489334; 15504738; 15510613; 15571262; 15571263; 15571283; 15579479; 15585623; 15598787; 15677700; 15682292; 15713801; 15735113; 15736425; 15788669; 15797993; 15817609; 15897576; 15930032; 15952572; 15953655; 15985285; 15993511; 15999119; 16030402; 16045580; 16051637; 16077970; 16079077; 16130010; 16132996; 16141798; 16162288; 16182121; 16188144; 16219137; 16234002; 16242255; 16259621; 16284371; 16317430; 16328059; 16328315; 16333305; 16334126; 16365025; 16424979; 16447238; 16456808; 16467096; 16575011; 16580699; 16596248; 16609021; 16617381; 16622263; 16675565; 16722845; 16723031; 16773218; 16920564; 16929515; 17000685; 17018589; 17065089; 17181924; 17187508; 17201138; 17203168; 17220568; 17273745; 17290389; 17311259; 17317154; 17367411; 17369151; 17372271; 17377791; 17385677; 17395259; 17410198; 17417073; 17439323; 17449906; 17454638; 17512053; 17546637; 17549369; 17551301; 17581305; 17596206; 17655928; 17659576; 17661145; 17684410; 17684476; 17688376; 17716232; 17854149; 17891500; 17971770; 18095031; 18098291; 18174236; 18177869; 18192902; 18203297; 18221821; 18245544; 18267032; 18274813; 18281538; 18285546; 18299612; 18322994; 18336674; 18365142; 18370400; 18381794; 18406541; 18427977; 18430179; 18448328; 18458991; 18498133; 18505590; 18510611; 18540691; 18584349; 18589584; 18593893; 18597678; 18600534; 18607581; 18629514; 18635682; 18636124; 18642643; 18669903; 18676680; 18676755; 18677108; 18704422; 18722050; 18728661; 18781797; 18785313; 18830263; 18855534; 18976010; 18983896; 18985814; 18988749; 18989779; 18990369; 18992148; 19020309; 19020759; 19020767; 19048631; 19064578; 19074750; 19082493; 19147506; 19154585; 19159907; 19161160; 19162321; 19170196; 19190136; 19295264; 19306093; 19307503; 19332728; 19339270; 19339911; 19374805; 19384296; 19426394; 19427504; 19444465; 19460136; 19471022; 19493349; 19513514; 19546880; 19568409; 19571608; 19619240; 19621386; 19625176; 19632929; 19636001; 19651439; 19672780; 19692168; 19722231; 19724871; 19738201; 19748501; 19750576; 19751277; 19774638; 19822515; 19837268; 19850635; 19858398; 19858780; 19885596; 19888426; 19898266; 19913121; 19917450; 19956635; 19998340; 20012317; 20047592; 20061047; 20101025; 20112501; 20122156; 20151707; 20165956; 20177420; 20180013; 20216541; 20235210; 20237949; 20306339; 20310006; 20331623; 20368715; 20371218; 20372850; 20372856; 20381446; 20385995; 20387074; 20447923; 20453000; 20458436; 20501373; 20504250; 20515563; 20530282; 20531375; 20544798; 20565774; 20570913; 20571234; 20580582; 20615890; 20628086; 20628382; 20628391; 20634891; 20638924; 20647221; 20647341; 20651387; 20665215; 20670920; 20714149; 20714877; 20734048; 20737570; 20815815; 20819423; 20824655; 20837458; 20932673; 20944490; 20962453; 20966539; 20970877; 21036767; 21043562; 21048041; 21057378; 21064161; 21111509; 21131780; 21139048; 21167658; 21188629; 21206062; 21245530; 21254360; 21262916; 21269855; 21282454; 21321092; 21347782; 21362378; 21460376; 21463130; 21471424; 21550658; 21570215; 21603981; 21605004; 21618517; 21643952; 21716147; 21730794; 21788964; 21811101; 21824439; 21848426; 21890473; 21900206; 21906983; 21919605; 21947036; 21948461; 21956592; 21963094; 21965773; 21987572; 22006578; 22074251; 22110208; 22143355; 22166040; 22172489; 22233820; 22270332; 22307944; 22384047; 22388795; 22397721; 22407825; 22486600; 22496803; 22502681; 22505724; 22551903; 22576918; 22580655; 22593457; 22623428; 22641663; 22713864; 22763757; 22819905; 22825513; 22863883; 22866924; 22882943; 22887475; 22895141; 22901148; 22938428; 22939629; 23000965; 23098521; 23148637; 23217244; 23249808; 23263912; 23336575; 23350714; 23468971; 23523421; 23645741; 23652803; 23675481; 23710599; 23722170; 23726796; 23736036; 23810585; 23838799; 23930679; 24067998; 24100087; 24123038 thymidylate synthetase Ensembl:ENSG00000176890 HGNC:12441 HPRD:01774 MIM:188350 Vega:OTTHUMG00000131473 Other designations: TSase|thymidylate synthase TYMS OGG:3000007329 Bin Zhao, Yue Liu, Oliver He C358B7.1 P18 UBC9 WEB: http://www.ncbi.nlm.nih.gov/gene UBE2I ubiquitin-conjugating enzyme E2I 7329 LA16c-358B7.1 16p13.3 9606 16 Official from a nomenclature committee GO_0000122 (EC: IMP, PMID: 19955185); GO_0000795 (EC: TAS, PMID: 8610150); GO_0001650 (EC: IEA); GO_0004842 (EC: TAS, PMID: 19955185); GO_0005515 (EC: IPI, PMID: 10871618); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA, PMID: 14752048); GO_0005654 (EC: TAS); GO_0005737 (EC: IDA); GO_0006464 (EC: TAS, PMID: 8798754); GO_0006511 (EC: TAS, PMID: 8565643); GO_0007059 (EC: IEA); GO_0007067 (EC: IEA); GO_0008022 (EC: IEA); GO_0008134 (EC: IPI, PMID: 19744555); GO_0010469 (EC: IEA); GO_0016032 (EC: IEA); GO_0016605 (EC: IDA, PMID: 9885291); GO_0016925 (EC: IDA, PMID: 19955185); GO_0016925 (EC: IEA); GO_0016925 (EC: TAS); GO_0019789 (EC: IDA, Qualifier: contributes_to, PMID: 19955185); GO_0019899 (EC: IPI, PMID: 17087506); GO_0030425 (EC: IEA); GO_0033145 (EC: IEA); GO_0043161 (EC: IEA); GO_0043398 (EC: IEA); GO_0043425 (EC: IEA); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0045202 (EC: IEA); GO_0045892 (EC: IDA, PMID: 16631117); GO_0051091 (EC: IEA); GO_0071535 (EC: IPI, PMID: 19407830) PMID: 8565643; 8610150; 8668125; 8668529; 8733011; 8798622; 8798754; 8824223; 8921390; 8940097; 9067428; 9197546; 9223484; 9257699; 9261152; 9333025; 9334332; 9353268; 9488727; 9497385; 9514881; 9563508; 9855622; 9885291; 9920803; 10377438; 10380882; 10383460; 10497239; 10535925; 10655495; 10694430; 10737800; 10759568; 10788439; 10806190; 10871618; 10961991; 11025202; 11085938; 11112409; 11157797; 11278381; 11278694; 11367701; 11384992; 11447110; 11451954; 11583632; 11709548; 11735126; 11779867; 11792325; 11812797; 11842083; 11853669; 11867732; 11877416; 11927605; 11960997; 12021447; 12023963; 12072434; 12082530; 12110916; 12150977; 12177000; 12192048; 12200128; 12354770; 12356736; 12419227; 12477932; 12565873; 12615929; 12620973; 12621041; 12633878; 12641448; 12674497; 12679040; 12727872; 12761287; 12788062; 12813045; 12887893; 12924945; 14516784; 14517060; 14517261; 14527952; 14531806; 14556380; 14578449; 14609633; 14673145; 14702039; 14752048; 14765993; 15087395; 15105549; 15123615; 15192080; 15210726; 15231748; 15246872; 15312759; 15327968; 15378033; 15489334; 15539951; 15546615; 15588942; 15592428; 15604093; 15608651; 15611122; 15611636; 15613319; 15616553; 15635413; 15637059; 15637079; 15666801; 15723523; 15735760; 15802564; 15806172; 15809060; 15820677; 15829507; 15876874; 15881673; 15882978; 15896780; 15931224; 15952105; 15958389; 15983381; 16029420; 16061479; 16098147; 16120648; 16148010; 16154161; 16166628; 16169070; 16189514; 16212558; 16248985; 16421094; 16421255; 16455055; 16455490; 16469311; 16494873; 16524884; 16566921; 16620772; 16631117; 16713569; 16730941; 16732283; 16998888; 17005699; 17036045; 17037517; 17087506; 17087659; 17105732; 17261810; 17283066; 17297476; 17314004; 17336575; 17353931; 17391059; 17466333; 17491593; 17498654; 17533377; 17548468; 17646165; 17671234; 17698038; 17704809; 17709345; 17823119; 17956732; 17967884; 17987106; 18087039; 18211895; 18321803; 18359863; 18408014; 18455188; 18538659; 18624398; 18625722; 18628979; 18655774; 18660489; 18684836; 18691969; 18706886; 18819927; 18946085; 19218564; 19287951; 19343802; 19358266; 19407830; 19471022; 19549727; 19553542; 19597476; 19616115; 19640976; 19684601; 19727227; 19744555; 19760037; 19765634; 19766626; 19836047; 19843541; 19859084; 19946338; 19955185; 19965618; 20016594; 20016603; 20023705; 20209145; 20351170; 20359522; 20360068; 20501649; 20555024; 20561671; 20671745; 20696768; 20797634; 20805487; 20863840; 20936779; 20972456; 21047957; 21070824; 21113135; 21120624; 21139048; 21139563; 21147068; 21174150; 21203974; 21216249; 21288202; 21319273; 21336309; 21344391; 21467194; 21510985; 21518904; 21693764; 21795333; 21829513; 21836637; 21880185; 21890473; 21906983; 21940674; 21949651; 21965678; 21971700; 21988832; 21998312; 22114711; 22155184; 22162396; 22194619; 22214662; 22403398; 22407595; 22411991; 22464730; 22578841; 22614022; 22623531; 22731716; 22797925; 22825850; 22863883; 22910413; 22939629; 23000965; 23128241; 23131550; 23155000; 23187003; 23264041; 23381475; 23395904; 23404503; 23417673; 23455924; 23470653; 23628505; 23686912; 23788427; 23860269; 23861967; 23871147; 23990779; 24068740; 24086615; 24260396; 24362530 ubiquitin-conjugating enzyme E2I Ensembl:ENSG00000103275 HGNC:12485 HPRD:09045 MIM:601661 Vega:OTTHUMG00000047845 Other designations: SUMO-1-protein ligase|SUMO-conjugating enzyme UBC9|SUMO-protein ligase|ubiquitin carrier protein 9|ubiquitin carrier protein I|ubiquitin conjugating enzyme 9|ubiquitin-conjugating enzyme E2I (UBC9 homolog, yeast)|ubiquitin-conjugating enzyme E2I (homologous to yeast UBC9)|ubiquitin-conjugating enzyme UbcE2A|ubiquitin-like protein SUMO-1 conjugating enzyme|ubiquitin-protein ligase E2I|ubiquitin-protein ligase I UBE2I OGG:3000007352 Bin Zhao, Yue Liu, Oliver He SLC25A9 WEB: http://www.ncbi.nlm.nih.gov/gene UCP3 uncoupling protein 3 (mitochondrial, proton carrier) 7352 11q13.4 9606 11 Official from a nomenclature committee GO_0000303 (EC: IEA); GO_0001666 (EC: IEA); GO_0005215 (EC: TAS, PMID: 9196039); GO_0005515 (EC: IPI); GO_0005739 (EC: TAS, PMID: 9180264); GO_0005743 (EC: TAS); GO_0006629 (EC: TAS, PMID: 10935638); GO_0006631 (EC: IEA); GO_0006839 (EC: IEA); GO_0007568 (EC: IEA); GO_0007584 (EC: IEA); GO_0007585 (EC: TAS, PMID: 9180264); GO_0009409 (EC: IEA); GO_0014823 (EC: IEA); GO_0015992 (EC: TAS); GO_0016021 (EC: IEA); GO_0017077 (EC: IEA); GO_0022904 (EC: TAS); GO_0032868 (EC: IEA); GO_0032870 (EC: IEA); GO_0044237 (EC: TAS); GO_0044281 (EC: TAS); GO_0051384 (EC: IEA) PMID: 9180264; 9196039; 9305858; 9325252; 9480760; 9498661; 9769326; 10329378; 10620491; 10748196; 10772343; 10785390; 10935638; 10958796; 11126413; 11151767; 11238538; 11319649; 11683368; 11842047; 11875702; 11920154; 11994670; 12051710; 12075570; 12145158; 12145475; 12170470; 12217879; 12351640; 12395215; 12477932; 12612210; 12634927; 12670931; 12720538; 12734183; 12756473; 12824081; 12843208; 14671191; 14702039; 14708035; 15045692; 15120704; 15211595; 15346230; 15489334; 15496137; 15520825; 15564896; 15870396; 15910756; 15959859; 15978856; 16006788; 16046300; 16178820; 16215931; 16337086; 16344560; 16352674; 16373902; 16622580; 16631432; 16644712; 16741147; 16752430; 16966355; 17150099; 17351641; 17502873; 17512314; 17544366; 17571165; 17587402; 17676309; 17728536; 17786284; 17786291; 17870627; 18059082; 18167556; 18191161; 18223008; 18249216; 18305572; 18348082; 18426825; 18426866; 18484143; 18648851; 18660489; 18676680; 18755175; 18825612; 18924534; 18956255; 18996102; 19039313; 19056482; 19056576; 19073146; 19155787; 19170196; 19336475; 19369366; 19413708; 19468707; 19491387; 19578796; 19625176; 19653005; 19680556; 19692168; 19710539; 19753844; 19769793; 19876004; 19913121; 19913848; 19948975; 20031128; 20186155; 20416077; 20468064; 20538960; 20628086; 20679960; 20694293; 20734064; 20802238; 20877624; 21047682; 21074158; 21175267; 21336965; 21544083; 21613221; 21751002; 21775425; 21897112; 22241057; 22774401; 22811361; 23165529; 23266187; 23365654; 23412863; 23505621; 23521650; 23560041; 23639961; 24124336 uncoupling protein 3 (mitochondrial, proton carrier) Ensembl:ENSG00000175564 HGNC:12519 HPRD:03623 MIM:602044 Vega:OTTHUMG00000168109 Other designations: mitochondrial uncoupling protein 3|solute carrier family 25 member 9 UCP3 OGG:3000007357 Bin Zhao, Yue Liu, Oliver He GCS GLCT1 WEB: http://www.ncbi.nlm.nih.gov/gene UGCG UDP-glucose ceramide glucosyltransferase 7357 9q31 9606 9 Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0006665 (EC: TAS); GO_0006679 (EC: TAS, PMID: 8643456); GO_0006687 (EC: TAS); GO_0006688 (EC: TAS, PMID: 8643456); GO_0008120 (EC: IEA); GO_0008544 (EC: TAS, PMID: 9545298); GO_0016020 (EC: TAS, PMID: 8643456); GO_0016021 (EC: IEA); GO_0044281 (EC: TAS) PMID: 1533793; 8643456; 8901638; 9545298; 9605861; 10945987; 11335714; 11915344; 12477932; 12489486; 12873973; 14766899; 15263008; 15489334; 15661399; 15747776; 16500619; 17709137; 18155680; 18560890; 19693666; 20533270; 20540746; 20843709; 21278235; 21380926; 21558327; 21617856; 21756066; 21832049; 21890473; 22270805; 22936806; 23133636; 23555901; 24510559 UDP-glucose ceramide glucosyltransferase HGNC:12524 HPRD:04190 MIM:602874 Other designations: GLCT-1|UDP-glucose:N-acylsphingosine D-glucosyltransferase|ceramide glucosyltransferase|glucosylceramide synthase UGCG OGG:3000007364 Bin Zhao, Yue Liu, Oliver He UDPGT 2B9 UDPGT2B7 UDPGTH2 UGT2B9 WEB: http://www.ncbi.nlm.nih.gov/gene UGT2B7 UDP glucuronosyltransferase 2 family, polypeptide B7 7364 4q13 9606 4 Official from a nomenclature committee GO_0001972 (EC: IDA, Qualifier: NOT); GO_0005789 (EC: IEA); GO_0006629 (EC: TAS, PMID: 2159463); GO_0008209 (EC: IDA, PMID: 17442341); GO_0015020 (EC: IDA, PMID: 17442341); GO_0016020 (EC: TAS, PMID: 2159463); GO_0016021 (EC: IEA); GO_0052695 (EC: IDA, PMID: 17442341) PMID: 2159463; 7835904; 8125298; 8674824; 10024527; 10222050; 10748067; 10779377; 10833461; 11186130; 11883901; 12185559; 12477932; 12623074; 12629580; 12695355; 12746330; 12811366; 14660172; 14871856; 15001974; 15318931; 15319348; 15320866; 15472229; 15489334; 15611481; 15615884; 15689421; 15815621; 16103897; 16397224; 16466707; 16580900; 16595916; 16849011; 17115150; 17178267; 17241877; 17263731; 17329852; 17339869; 17363580; 17429314; 17440429; 17442341; 17446261; 17579197; 17670842; 17687269; 17706742; 17724700; 17924828; 17965522; 17978490; 18052087; 18161889; 18315786; 18496127; 18569595; 18597651; 18622261; 18622263; 18641546; 18647858; 18719619; 18946804; 19116784; 19225446; 19244109; 19289110; 19343046; 19352303; 19408577; 19424794; 19494809; 19574343; 19628728; 19644937; 19730281; 19779319; 19898482; 19956635; 20008037; 20056642; 20064729; 20142249; 20147615; 20216122; 20297805; 20379614; 20565459; 20567810; 20634197; 20679960; 20734064; 20814162; 20860463; 20973683; 21044367; 21056984; 21123165; 21415305; 21856742; 21881541; 21988832; 22028316; 22092298; 22188362; 22240840; 22462748; 22676193; 23099353; 23131697; 23223495; 23230132; 23251661; 23263737; 23700788; 23726609 UDP glucuronosyltransferase 2 family, polypeptide B7 Ensembl:ENSG00000171234 HGNC:12554 HPRD:02508 MIM:600068 Vega:OTTHUMG00000129404 Other designations: 3,4-catechol estrogen specific|3,4-catechol estrogen-specific UDPGT|UDP glucuronosyltransferase 2B7|UDP-glucuronosyltransferase 2B7|UDP-glucuronosyltransferase 2B9|UDP-glucuronyltransferase, family 2, beta-7|UDPGT 2B7|UDPGTh-2 UGT2B7 OGG:3000007376 Bin Zhao, Yue Liu, Oliver He LXR-b LXRB NER NER-I RIP15 UNR WEB: http://www.ncbi.nlm.nih.gov/gene NR1H2 nuclear receptor subfamily 1, group H, member 2 7376 19q13.3 9606 19 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0001133 (EC: IEA); GO_0003677 (EC: TAS, PMID: 7926814); GO_0003707 (EC: IEA); GO_0004879 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12393874); GO_0005634 (EC: IDA, PMID: 12393874); GO_0005654 (EC: TAS); GO_0005737 (EC: IDA, PMID: 12393874); GO_0006367 (EC: TAS); GO_0008270 (EC: IEA); GO_0010467 (EC: TAS); GO_0010745 (EC: IC, PMID: 17693624); GO_0010867 (EC: IMP, PMID: 17186944); GO_0010875 (EC: IMP, PMID: 17186944); GO_0010884 (EC: IEA); GO_0010887 (EC: IMP, PMID: 17693624); GO_0032270 (EC: IMP, PMID: 17186944); GO_0032369 (EC: IMP, PMID: 17693624); GO_0032376 (EC: IDA, PMID: 16141411); GO_0042632 (EC: IEA); GO_0043565 (EC: IEA); GO_0044255 (EC: IEA); GO_0045723 (EC: IMP, PMID: 17186944); GO_0045861 (EC: IEA); GO_0045892 (EC: IDA, PMID: 12393874); GO_0045944 (EC: IDA, PMID: 16141411); GO_0045944 (EC: IMP, PMID: 17186944); GO_0046965 (EC: IEA); GO_0048384 (EC: IEA); GO_0048550 (EC: IMP, PMID: 17693624); GO_0051006 (EC: IMP, PMID: 17186944); GO_0060336 (EC: NAS); GO_0090108 (EC: IEA); GO_0090187 (EC: IEA); GO_0090340 (EC: IEA); GO_2000188 (EC: ISS) PMID: 7625741; 7760852; 7782080; 7926814; 7971966; 9874807; 10187832; 11158331; 11546778; 12040022; 12198243; 12393874; 12477932; 12663743; 12724417; 12736258; 12819202; 12957674; 14643652; 14699103; 14702039; 15489334; 15539633; 15548517; 15604093; 15774904; 16141411; 16189514; 16219912; 16298468; 16344560; 16354658; 16482468; 16524875; 16567856; 16904112; 16973760; 17045963; 17108812; 17110595; 17135302; 17186944; 17218271; 17391100; 17396233; 17405904; 17626048; 17693624; 17724434; 17766241; 17845217; 17900622; 17936707; 18026184; 18081155; 18182682; 18221307; 18372238; 18597895; 18636124; 18660489; 18782758; 18854425; 19060904; 19105208; 19242521; 19292929; 19303409; 19426978; 19436111; 19481530; 19796621; 19837721; 19913121; 19933273; 19948975; 20159957; 20176747; 20219900; 20364260; 20628086; 20655109; 20836841; 20855565; 20939869; 21042792; 21315073; 21331046; 21356276; 21507939; 21900206; 21937108; 21951066; 21988832; 22027013; 22029530; 22257474; 22367754; 22610535; 22723445; 22766509; 22939629; 22969086; 22990668; 23018104; 23223141; 23455924; 23838803; 23867501; 23987069; 24100084; 24398515 nuclear receptor subfamily 1, group H, member 2 Ensembl:ENSG00000131408 HGNC:7965 HPRD:02660 MIM:600380 Vega:OTTHUMG00000183036 Other designations: LX receptor beta|liver X nuclear receptor beta|nuclear orphan receptor LXR-beta|nuclear receptor NER|oxysterols receptor LXR-beta|steroid hormone-nuclear receptor NER|ubiquitously-expressed nuclear receptor NR1H2 OGG:3000007392 Bin Zhao, Yue Liu, Oliver He FIP bHLHb12 WEB: http://www.ncbi.nlm.nih.gov/gene USF2 upstream transcription factor 2, c-fos interacting 7392 19q13 9606 19 Official from a nomenclature committee GO_0000430 (EC: IC, PMID: 8576131); GO_0000432 (EC: IMP, PMID: 7852331); GO_0000432 (EC: ISS); GO_0000978 (EC: IEA); GO_0003690 (EC: IEA); GO_0003700 (EC: IEA); GO_0003705 (EC: IMP, PMID: 8576131); GO_0005515 (EC: IPI, PMID: 19505873); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0006351 (EC: IEA); GO_0006366 (EC: IMP, PMID: 8576131); GO_0007595 (EC: IEA); GO_0019086 (EC: IC, PMID: 8576131); GO_0042803 (EC: IPI, PMID: 8576131); GO_0043425 (EC: IPI, PMID: 8576131); GO_0043565 (EC: IDA, PMID: 8576131); GO_0045944 (EC: IMP, PMID: 8576131); GO_0046982 (EC: IPI, PMID: 8576131); GO_0055088 (EC: ISS) PMID: 1450663; 1589769; 7852331; 8576131; 8619474; 8954795; 9053857; 9070273; 9099698; 9108421; 9110174; 10434034; 11058604; 11583024; 11945176; 11948912; 12477932; 12611894; 12663044; 12791656; 12857727; 12917334; 12970752; 14502648; 15014447; 15042619; 15057824; 15187018; 15242350; 15276216; 15358760; 15489334; 15741164; 15767439; 15864740; 16199862; 16386222; 16870626; 16943425; 17081983; 17353931; 17379962; 17823260; 17846119; 18165439; 18167349; 18817855; 18845576; 18970934; 19074828; 19087304; 19089909; 19505873; 19730683; 19846536; 20180799; 20626032; 20814220; 20936779; 21139048; 21653943; 21813151; 21890473; 21921026; 22891280; 22966206; 23560079 upstream transcription factor 2, c-fos interacting Ensembl:ENSG00000105698 HGNC:12594 HPRD:02668 MIM:600390 Vega:OTTHUMG00000183182 Other designations: FOS-interacting protein|c-fos interacting protein|class B basic helix-loop-helix protein 12|major late transcription factor 2|upstream stimulatory factor 2 USF2 OGG:3000007410 Bin Zhao, Yue Liu, Oliver He VAV-2 WEB: http://www.ncbi.nlm.nih.gov/gene VAV2 vav 2 guanine nucleotide exchange factor 7410 9q34.1 9606 9 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0005085 (EC: EXP); GO_0005085 (EC: TAS); GO_0005089 (EC: IEA); GO_0005154 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11390470); GO_0005829 (EC: TAS); GO_0005886 (EC: IEA); GO_0007165 (EC: TAS, PMID: 7762982); GO_0007264 (EC: TAS); GO_0007411 (EC: TAS); GO_0007596 (EC: TAS); GO_0016477 (EC: IEA); GO_0030032 (EC: IEA); GO_0030168 (EC: TAS); GO_0038095 (EC: TAS); GO_0038096 (EC: TAS); GO_0043065 (EC: TAS); GO_0043087 (EC: EXP); GO_0043087 (EC: TAS); GO_0043552 (EC: IEA); GO_0045087 (EC: TAS); GO_0046872 (EC: IEA); GO_0048011 (EC: TAS); GO_0051056 (EC: TAS); GO_0097190 (EC: TAS) PMID: 7762982; 8621483; 8986718; 9115846; 9269777; 9399639; 9438848; 10022833; 10618391; 10938113; 10982832; 11076863; 11080163; 11262396; 11313921; 11390470; 11448999; 11516622; 11606575; 11756498; 11909943; 12376548; 12376551; 12454019; 12477932; 12787561; 12810717; 14702039; 15345594; 15479739; 15489336; 15618286; 15848800; 15850391; 16273093; 16381901; 16397238; 17234718; 17686471; 18067320; 18271526; 18654987; 18729074; 18829495; 19322201; 19451809; 19531499; 19826000; 19911011; 20140013; 20140222; 20298788; 20463313; 20598377; 20808760; 20940296; 21810271; 22554804; 22750419; 22939629; 22946057; 23033535; 23033540; 23382691; 23402756; 23615439; 23724134 vav 2 guanine nucleotide exchange factor Ensembl:ENSG00000160293 HGNC:12658 HPRD:02694 MIM:600428 Vega:OTTHUMG00000020882 Other designations: guanine nucleotide exchange factor VAV2|vav 2 oncogene VAV2 OGG:3000007412 Bin Zhao, Yue Liu, Oliver He CD106 INCAM-100 WEB: http://www.ncbi.nlm.nih.gov/gene VCAM1 vascular cell adhesion molecule 1 7412 1p32-p31 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0001666 (EC: IEA); GO_0002102 (EC: IDA, PMID: 15220135); GO_0002526 (EC: IEA); GO_0002544 (EC: IEA); GO_0005178 (EC: IDA, PMID: 1377228); GO_0005178 (EC: IMP, PMID: 19738201); GO_0005615 (EC: IDA, PMID: 9290466); GO_0005769 (EC: IDA); GO_0005783 (EC: IDA); GO_0005794 (EC: IDA); GO_0005886 (EC: TAS); GO_0005902 (EC: IDA, PMID: 12082081); GO_0007155 (EC: IDA, PMID: 16809613); GO_0007157 (EC: IDA, PMID: 1715889); GO_0007159 (EC: IDA, PMID: 1381355); GO_0007507 (EC: IEA); GO_0007568 (EC: IEA); GO_0007584 (EC: IEA); GO_0008131 (EC: IDA); GO_0009308 (EC: IDA); GO_0009897 (EC: IDA, PMID: 1377228); GO_0009986 (EC: IDA, PMID: 1715889); GO_0010043 (EC: IEA); GO_0010212 (EC: IEA); GO_0016021 (EC: IEA); GO_0016032 (EC: IEA); GO_0019221 (EC: TAS); GO_0022614 (EC: IEP, PMID: 12082081); GO_0030175 (EC: IDA, PMID: 12082081); GO_0030183 (EC: IC, PMID: 1715889); GO_0030198 (EC: TAS); GO_0032496 (EC: IEA); GO_0035094 (EC: IEA); GO_0035924 (EC: IEA); GO_0042102 (EC: IDA, PMID: 1381355); GO_0042383 (EC: IEA); GO_0045177 (EC: IDA, PMID: 12082081); GO_0045471 (EC: IEA); GO_0050776 (EC: TAS); GO_0050839 (EC: IDA, PMID: 1377228); GO_0050839 (EC: IPI, PMID: 12082081); GO_0050901 (EC: IEP, PMID: 2688898); GO_0055114 (EC: IDA); GO_0060326 (EC: IEA); GO_0060333 (EC: TAS); GO_0060710 (EC: IEA); GO_0071065 (EC: IDA, PMID: 15220135); GO_0071333 (EC: IEA); GO_0071356 (EC: IEA) PMID: 1281211; 1377228; 1379595; 1381355; 1699207; 1707234; 1707873; 1713772; 1715583; 1715889; 2688898; 7521694; 7531291; 7534402; 7539925; 7545397; 7691867; 7884872; 8125298; 8607877; 8825878; 8977311; 9117345; 9184636; 9269771; 9290466; 9443894; 9603478; 9792375; 9973426; 10209034; 10377075; 10438935; 10477700; 10556825; 10602408; 10623819; 10944555; 11123288; 11517385; 11520773; 11776680; 11817523; 11847011; 11882338; 11904449; 11922919; 11929779; 11935152; 11961404; 11963839; 11983205; 12006387; 12082081; 12086338; 12097820; 12105209; 12115600; 12172318; 12172576; 12193695; 12351381; 12387879; 12393616; 12433638; 12477932; 12493764; 12587980; 12601490; 12643440; 12650924; 12673844; 12682249; 12700137; 12704784; 12714597; 12759453; 12788528; 12871600; 12940514; 12958610; 12969778; 14534081; 14550782; 14592496; 14615367; 14684616; 14691297; 14741380; 14748068; 14762656; 14984317; 15009098; 15059493; 15078922; 15080580; 15116247; 15175347; 15194470; 15220135; 15225366; 15265790; 15299708; 15304054; 15308572; 15340161; 15489334; 15489374; 15489375; 15525877; 15548573; 15661077; 15661918; 15666579; 15710215; 15784173; 15805138; 15806475; 15845907; 15979542; 16002075; 16015337; 16127297; 16184405; 16230423; 16242117; 16317091; 16327982; 16335952; 16344560; 16498082; 16585601; 16644735; 16722038; 16790997; 16809613; 16874958; 16902065; 16914554; 16977262; 16987074; 17008592; 17022986; 17090406; 17115186; 17116732; 17126824; 17142773; 17167725; 17192354; 17255534; 17258924; 17292586; 17303384; 17334226; 17352405; 17430469; 17431880; 17437524; 17497038; 17517105; 17521609; 17530710; 17531998; 17560459; 17564956; 17586618; 17597073; 17599409; 17616653; 17657162; 17678915; 17702963; 17703412; 17706337; 17706953; 17714716; 17891599; 17906965; 17922685; 17943642; 17962718; 17963163; 17964973; 17983593; 18078450; 18160848; 18197885; 18212564; 18227515; 18284603; 18326231; 18383329; 18406566; 18420209; 18421029; 18449421; 18462748; 18473733; 18482273; 18490752; 18504269; 18554449; 18564921; 18574676; 18582564; 18597403; 18600396; 18613029; 18618671; 18628303; 18633131; 18636124; 18656701; 18666029; 18676680; 18676870; 18692491; 18707907; 18761738; 18778820; 18787016; 18787184; 18791689; 18813849; 18828734; 18834676; 18846968; 18930765; 18974842; 19002703; 19021457; 19022587; 19028820; 19057841; 19074885; 19131662; 19134480; 19136619; 19170196; 19208843; 19210349; 19225544; 19229069; 19236760; 19237221; 19242838; 19247692; 19249917; 19258923; 19281832; 19342863; 19353432; 19379571; 19391499; 19399399; 19407977; 19407978; 19417018; 19422386; 19423540; 19452728; 19479237; 19520742; 19526283; 19540498; 19542447; 19554506; 19559392; 19573080; 19597294; 19604093; 19625176; 19692168; 19717975; 19729601; 19738201; 19771922; 19773279; 19812370; 19887846; 19913121; 19948975; 20039412; 20056178; 20112284; 20164172; 20184510; 20197690; 20217071; 20219985; 20233927; 20237496; 20360250; 20405289; 20406964; 20416077; 20430730; 20438785; 20447702; 20482449; 20485444; 20503287; 20508517; 20536507; 20568250; 20573493; 20602615; 20603037; 20628086; 20685094; 20714774; 20851866; 20864106; 20880684; 20929696; 20935502; 20966071; 21030716; 21037509; 21073443; 21099224; 21144825; 21162967; 21172429; 21177856; 21183871; 21184654; 21214384; 21236267; 21381877; 21520070; 21540635; 21562063; 21594636; 21632263; 21641584; 21804483; 21808112; 21833088; 21843619; 21895545; 21900123; 22001052; 22014578; 22031842; 22093255; 22137570; 22137794; 22183741; 22195873; 22209080; 22209338; 22269951; 22298164; 22324942; 22366735; 22374129; 22384064; 22448134; 22463742; 22497223; 22505707; 22539325; 22552687; 22591361; 22593994; 22623428; 22664325; 22694757; 22717098; 22719189; 22734001; 22740338; 22742445; 22874466; 22879387; 22905988; 22976263; 23042271; 23057424; 23058024; 23117931; 23185512; 23232649; 23242661; 23285079; 23313051; 23336423; 23344094; 23349048; 23396735; 23463506; 23665024; 23677452; 23679262; 23704882; 23792525; 23934855; 24045955; 24157824; 24282904 vascular cell adhesion molecule 1 Ensembl:ENSG00000162692 HGNC:12663 HPRD:01888 MIM:192225 Vega:OTTHUMG00000010982 Other designations: CD106 antigen|vascular cell adhesion protein 1 VCAM1 OGG:3000007422 Bin Zhao, Yue Liu, Oliver He MVCD1 VEGF VPF WEB: http://www.ncbi.nlm.nih.gov/gene VEGFA vascular endothelial growth factor A 7422 RP1-261G23.1 6p12 20140408 9606 6 protein-coding Official from a nomenclature committee GO_0000122 (EC: IDA, PMID: 18093989); GO_0001525 (EC: IDA, PMID: 11427521); GO_0001541 (EC: ISS); GO_0001569 (EC: ISS); GO_0001570 (EC: TAS, PMID: 15015550); GO_0001666 (EC: IDA, PMID: 16490744); GO_0001701 (EC: ISS); GO_0001822 (EC: ISS); GO_0001934 (EC: IDA, PMID: 18386220); GO_0001938 (EC: IDA, PMID: 10022831); GO_0001938 (EC: ISS); GO_0001968 (EC: IDA, PMID: 14570917); GO_0002042 (EC: IDA, PMID: 18059339); GO_0002052 (EC: ISS); GO_0002053 (EC: ISS); GO_0002092 (EC: IDA); GO_0002575 (EC: IDA, PMID: 17082651); GO_0002576 (EC: TAS); GO_0002687 (EC: TAS, PMID: 1312256); GO_0003007 (EC: ISS); GO_0003151 (EC: ISS); GO_0003169 (EC: ISS); GO_0005125 (EC: IDA, PMID: 18440775); GO_0005125 (EC: ISS); GO_0005161 (EC: IPI, PMID: 17470632); GO_0005172 (EC: IPI, PMID: 10471394); GO_0005515 (EC: IPI, PMID: 10543948); GO_0005576 (EC: TAS); GO_0005578 (EC: NAS, PMID: 14570917); GO_0005615 (EC: IDA, PMID: 16490744); GO_0005615 (EC: ISS); GO_0005737 (EC: IDA, PMID: 17082651); GO_0006357 (EC: IMP, PMID: 18093989); GO_0007399 (EC: TAS, PMID: 15351965); GO_0007498 (EC: ISS); GO_0007595 (EC: ISS); GO_0007596 (EC: TAS); GO_0008083 (EC: IDA); GO_0008083 (EC: ISS); GO_0008201 (EC: IDA, PMID: 15001987); GO_0008201 (EC: IMP, PMID: 14570917); GO_0008284 (EC: IDA, PMID: 7929439); GO_0008360 (EC: IDA, PMID: 10527820); GO_0009986 (EC: IDA, PMID: 17470632); GO_0010595 (EC: IDA, PMID: 10022831); GO_0010628 (EC: IDA, PMID: 18386220); GO_0016020 (EC: IEA); GO_0030141 (EC: IDA, PMID: 17082651); GO_0030168 (EC: TAS); GO_0030224 (EC: IDA); GO_0030225 (EC: IDA); GO_0030324 (EC: ISS); GO_0030335 (EC: IDA, PMID: 17470632); GO_0030855 (EC: ISS); GO_0030949 (EC: IDA, PMID: 1312256); GO_0031077 (EC: ISS); GO_0031093 (EC: TAS); GO_0031334 (EC: IDA, PMID: 16489009); GO_0031954 (EC: IDA, PMID: 17470632); GO_0032147 (EC: IDA, PMID: 18059339); GO_0032793 (EC: IDA); GO_0033138 (EC: IDA, PMID: 18440775); GO_0035148 (EC: IDA, PMID: 19033661); GO_0035767 (EC: IDA, PMID: 18440775); GO_0035924 (EC: IDA, PMID: 18440775); GO_0036303 (EC: ISS); GO_0038033 (EC: IDA, PMID: 18440775); GO_0038091 (EC: IDA, PMID: 17470632); GO_0038190 (EC: ISS); GO_0040007 (EC: ISS); GO_0042056 (EC: IDA, PMID: 17082651); GO_0042462 (EC: ISS); GO_0042802 (EC: IPI, PMID: 12207021); GO_0042803 (EC: ISS); GO_0043066 (EC: IMP, PMID: 10066377); GO_0043117 (EC: IDA, PMID: 16109918); GO_0043129 (EC: ISS); GO_0043154 (EC: IDA, PMID: 18386220); GO_0043183 (EC: IPI, PMID: 1312256); GO_0043184 (EC: IPI, PMID: 10022831); GO_0043406 (EC: IDA, PMID: 18440775); GO_0043536 (EC: IDA, PMID: 18440775); GO_0045766 (EC: IDA, PMID: 18440775); GO_0045766 (EC: IMP, PMID: 18275976); GO_0045785 (EC: IDA, PMID: 19674970); GO_0045944 (EC: IDA, PMID: 18059339); GO_0045944 (EC: IMP, PMID: 18093989); GO_0046982 (EC: IDA, PMID: 8702615); GO_0048010 (EC: IDA); GO_0048010 (EC: TAS); GO_0048018 (EC: IPI, PMID: 17470632); GO_0048469 (EC: ISS); GO_0048593 (EC: ISS); GO_0048739 (EC: ISS); GO_0048754 (EC: ISS); GO_0048842 (EC: ISS); GO_0048844 (EC: ISS); GO_0050679 (EC: ISS); GO_0050731 (EC: IDA, PMID: 10022831); GO_0050840 (EC: IC, PMID: 14570917); GO_0050918 (EC: IDA, PMID: 19275959); GO_0050927 (EC: IDA, PMID: 12744932); GO_0050930 (EC: IDA, PMID: 19275959); GO_0050930 (EC: NAS, PMID: 12744932); GO_0051272 (EC: IDA, PMID: 10527820); GO_0051781 (EC: IEA); GO_0051894 (EC: IDA, PMID: 16489009); GO_0060319 (EC: ISS); GO_0060749 (EC: ISS); GO_0060754 (EC: IDA, PMID: 19275959); GO_0060948 (EC: ISS); GO_0060982 (EC: ISS); GO_0061418 (EC: TAS); GO_0061419 (EC: IMP, PMID: 19652095); GO_0071456 (EC: IDA, PMID: 10575000); GO_0071456 (EC: TAS); GO_0071542 (EC: ISS); GO_0071679 (EC: ISS); GO_0090037 (EC: IDA, PMID: 18059339); GO_0090050 (EC: IDA); GO_0090190 (EC: ISS); GO_0090259 (EC: ISS); GO_1900086 (EC: IDA); GO_1900745 (EC: IDA, PMID: 18386220); GO_1901727 (EC: IDA); GO_1902336 (EC: ISS); GO_1902533 (EC: IDA) PMID: 1312256; 1417831; 1550962; 1567395; 1711045; 1791831; 2479986; 2479987; 2584205; 7518352; 7525053; 7678805; 7681362; 7759509; 7829517; 7929439; 8621427; 8631822; 8641698; 8702615; 8786112; 8889548; 9012504; 9012841; 9054410; 9202027; 9207067; 9323936; 9336848; 9351807; 9393862; 9450968; 9529250; 9634701; 9674707; 9684805; 9716565; 9792673; 9878851; 9922142; 10022831; 10066377; 10067980; 10196157; 10409677; 10464055; 10471394; 10527820; 10543948; 10575000; 10585578; 10626738; 10748121; 10873597; 11016853; 11032698; 11069235; 11115828; 11122379; 11133233; 11146397; 11196464; 11352659; 11427521; 11461089; 11563986; 11642726; 11686329; 11705851; 11705867; 11731620; 11741977; 11742492; 11744618; 11748975; 11751905; 11783119; 11784713; 11784722; 11796824; 11806247; 11809675; 11809713; 11815711; 11819817; 11824377; 11831981; 11832343; 11834731; 11836562; 11839635; 11847008; 11866530; 11866538; 11867956; 11875709; 11877311; 11877669; 11882460; 11891801; 11908876; 11912213; 11912219; 11920479; 11921018; 11930687; 11930688; 11940485; 11956584; 11956638; 11957147; 11959648; 11960372; 11961297; 11961303; 11964077; 11964307; 11972026; 11978184; 11978667; 11980898; 11986311; 11986954; 11999550; 12012273; 12014632; 12016145; 12023772; 12038454; 12039075; 12042276; 12058259; 12062186; 12067896; 12067976; 12085210; 12086892; 12089333; 12102661; 12105188; 12114504; 12117969; 12119553; 12124351; 12127077; 12133473; 12133520; 12133521; 12141529; 12149254; 12151344; 12151391; 12163680; 12168088; 12168808; 12168898; 12174362; 12174901; 12187074; 12197476; 12207021; 12208766; 12209585; 12209725; 12213806; 12213874; 12213878; 12215337; 12232762; 12235106; 12239588; 12358602; 12391145; 12391545; 12393542; 12400015; 12406876; 12407018; 12413884; 12425822; 12427739; 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20382636; 20383146; 20388088; 20388222; 20388348; 20388479; 20389299; 20395257; 20395351; 20396703; 20396759; 20396799; 20398057; 20400478; 20406100; 20413783; 20413880; 20414936; 20416077; 20417690; 20420808; 20422320; 20422487; 20424473; 20430742; 20430845; 20442584; 20443868; 20444917; 20446021; 20449668; 20452482; 20453000; 20453883; 20465445; 20465852; 20470445; 20471067; 20471686; 20471768; 20473646; 20477880; 20482220; 20485168; 20485444; 20489156; 20489684; 20492336; 20497701; 20501856; 20502414; 20502715; 20504760; 20510681; 20514415; 20522805; 20529820; 20531372; 20532559; 20538805; 20540786; 20543462; 20545903; 20546613; 20549300; 20551700; 20552269; 20552697; 20554972; 20555002; 20556584; 20561442; 20562294; 20563637; 20566589; 20568250; 20571438; 20571754; 20571871; 20580871; 20587967; 20591524; 20592375; 20592377; 20593045; 20593288; 20599538; 20602615; 20615131; 20618614; 20619094; 20621071; 20621078; 20628086; 20628624; 20629312; 20631454; 20631636; 20632925; 20635170; 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21711965; 21712445; 21724588; 21726930; 21730794; 21734015; 21737794; 21740084; 21743435; 21744122; 21757152; 21757650; 21757917; 21761115; 21761458; 21763962; 21763969; 21763972; 21766497; 21769478; 21771176; 21773953; 21774929; 21782227; 21782870; 21782909; 21797753; 21798757; 21799753; 21802218; 21809353; 21809368; 21813166; 21814723; 21826315; 21830391; 21831507; 21832278; 21832283; 21837996; 21845872; 21845875; 21851000; 21851923; 21853312; 21854110; 21856421; 21866460; 21867616; 21872252; 21873429; 21876459; 21881842; 21882634; 21886838; 21897119; 21902756; 21905000; 21905955; 21906274; 21912077; 21913973; 21917937; 21918901; 21918972; 21923031; 21935869; 21938405; 21939655; 21939755; 21944175; 21948244; 21950586; 21953277; 21959110; 21959987; 21964530; 21965736; 21968684; 21978756; 21979585; 21982816; 21983449; 21984182; 21985298; 21986500; 21986923; 21987221; 21988832; 21994955; 21998580; 22004076; 22009797; 22012426; 22014666; 22016416; 22020326; 22020917; 22024063; 22028446; 22030397; 22034877; 22040304; 22051188; 22051879; 22053594; 22053610; 22058001; 22064697; 22067973; 22073279; 22082308; 22084166; 22086907; 22094096; 22095559; 22095586; 22097317; 22098148; 22098246; 22098296; 22103490; 22104143; 22105769; 22111836; 22116346; 22120617; 22124604; 22125641; 22125837; 22126484; 22128293; 22128802; 22129133; 22139971; 22147251; 22147779; 22158497; 22159356; 22161247; 22162628; 22167330; 22170854; 22171127; 22174163; 22174934; 22178239; 22178822; 22183311; 22184869; 22185591; 22186244; 22189703; 22194599; 22197408; 22198599; 22199270; 22199311; 22203927; 22203935; 22206010; 22209065; 22209952; 22210436; 22222630; 22227235; 22227305; 22227643; 22230112; 22230399; 22230402; 22231433; 22233184; 22251524; 22257487; 22259987; 22260074; 22268049; 22270366; 22270936; 22274866; 22275161; 22287745; 22289522; 22292637; 22296200; 22307775; 22307787; 22308085; 22311631; 22314268; 22315135; 22318385; 22318724; 22319020; 22320189; 22321253; 22328776; 22337942; 22344539; 22350794; 22355348; 22363824; 22368191; 22370607; 22380724; 22382924; 22385323; 22385934; 22386962; 22392094; 22392487; 22392726; 22395988; 22397762; 22399811; 22402207; 22402885; 22402934; 22407444; 22409847; 22417860; 22429695; 22431315; 22433249; 22437209; 22452999; 22455137; 22460086; 22461367; 22471664; 22472004; 22475441; 22475893; 22479202; 22489699; 22493900; 22494072; 22497886; 22506349; 22510875; 22511716; 22513751; 22517242; 22521084; 22527851; 22528855; 22534113; 22541785; 22542989; 22547925; 22548401; 22552325; 22553402; 22558473; 22558480; 22564870; 22568177; 22569438; 22573202; 22577248; 22580375; 22581182; 22581719; 22587628; 22590832; 22594508; 22609636; 22612323; 22612467; 22613408; 22622799; 22635523; 22640261; 22643235; 22644871; 22645074; 22652447; 22652457; 22659165; 22659470; 22659681; 22670172; 22674805; 22675957; 22677927; 22685266; 22689615; 22689881; 22690749; 22692760; 22694909; 22696064; 22697069; 22699049; 22699054; 22699060; 22699782; 22699808; 22705563; 22711306; 22729570; 22729710; 22730813; 22733742; 22735262; 22740248; 22762535; 22763125; 22768249; 22771446; 22773844; 22776467; 22781068; 22786655; 22789536; 22790437; 22791116; 22795057; 22796052; 22800355; 22813402; 22818823; 22819906; 22833169; 22836100; 22840423; 22848663; 22849380; 22850906; 22853925; 22854047; 22855059; 22855159; 22864531; 22864925; 22865486; 22869459; 22872519; 22872931; 22875307; 22876972; 22877565; 22882209; 22899753; 22901144; 22901561; 22906062; 22915033; 22915086; 22925497; 22926658; 22927437; 22930318; 22931643; 22935455; 22942646; 22944463; 22948895; 22951014; 22956610; 22957090; 22961433; 22962287; 22963269; 22965144; 22992725; 22993129; 22993299; 22994042; 22994764; 23005896; 23015149; 23020605; 23025904; 23029477; 23038639; 23039092; 23040494; 23053181; 23058011; 23059773; 23060442; 23061744; 23062326; 23062640; 23064377; 23065156; 23065202; 23065534; 23068100; 23073296; 23077562; 23086295; 23086340; 23086933; 23093658; 23094709; 23098361; 23098453; 23102786; 23104639; 23104894; 23108136; 23114032; 23117246; 23118492; 23128854; 23129289; 23137522; 23145112; 23151382; 23155231; 23155236; 23155356; 23160675; 23161411; 23166713; 23167810; 23168996; 23169005; 23169435; 23172303; 23176363; 23177780; 23181555; 23182805; 23192572; 23201159; 23204297; 23206462; 23211130; 23212515; 23213275; 23217559; 23220088; 23221067; 23222716; 23224211; 23225320; 23227881; 23232696; 23236677; 23236888; 23239744; 23243026; 23250775; 23254909; 23254958; 23257745; 23263486; 23264084; 23264219; 23265127; 23269488; 23269798; 23272057; 23272609; 23279742; 23280079; 23285958; 23288726; 23290762; 23293030; 23293323; 23295255; 23302311; 23313225; 23315815; 23317892; 23321169; 23321170; 23326384; 23326500; 23328414; 23329570; 23332132; 23332617; 23334331; 23335070; 23335846; 23339636; 23340303; 23346798; 23350126; 23350655; 23352645; 23353010; 23359195; 23364276; 23367565; 23369005; 23370341; 23374220; 23374253; 23383089; 23384557; 23390884; 23398358; 23401860; 23403511; 23404377; 23405237; 23408906; 23413901; 23421785; 23421942; 23428182; 23429328; 23429999; 23430447; 23435217; 23444216; 23449351; 23454149; 23454747; 23455636; 23459872; 23462604; 23465821; 23467576; 23470436; 23475388; 23481572; 23485997; 23499421; 23511629; 23522390; 23542734; 23545315; 23548900; 23552871; 23553563; 23554900; 23555666; 23559636; 23569009; 23572336; 23586368; 23588859; 23589053; 23592000; 23599627; 23602531; 23605255; 23608225; 23613250; 23613251; 23613412; 23618468; 23620752; 23625573; 23639731; 23644986; 23648010; 23649946; 23650550; 23651239; 23656623; 23661335; 23667446; 23673188; 23679262; 23679318; 23687977; 23688054; 23690937; 23695013; 23698113; 23699597; 23711375; 23714383; 23719599; 23722461; 23725153; 23725155; 23728502; 23737289; 23737650; 23745581; 23748230; 23749886; 23754270; 23754948; 23756256; 23759331; 23761723; 23765166; 23767832; 23780896; 23790363; 23794239; 23831623; 23831629; 23838139; 23838428; 23840094; 23848209; 23851330; 23860526; 23861821; 23867510; 23870474; 23877020; 23884416; 23884772; 23884891; 23886195; 23886210; 23904001; 23906304; 23907576; 23913375; 23922493; 23926105; 23929745; 23933698; 23950980; 23953100; 23953866; 23976881; 23982876; 23992143; 23998120; 24005038; 24016866; 24021340; 24021586; 24024441; 24043765; 24048796; 24052076; 24067461; 24120473; 24123039; 24222145; 24225154; 24254563; 24263190; 24274376; 24284961; 24321896; 24341227; 24400721; 24403492; 24510998; 24511001 vascular endothelial growth factor A Ensembl:ENSG00000112715 HGNC:12680 HPRD:01889 MIM:192240 Vega:OTTHUMG00000014745 Other designations: vascular permeability factor VEGFA OGG:3000007458 Bin Zhao, Yue Liu, Oliver He WBSCR1 WSCR1 eIF-4H WEB: http://www.ncbi.nlm.nih.gov/gene EIF4H eukaryotic translation initiation factor 4H 7458 7q11.23 9606 7 GO_0000166 (EC: IEA); GO_0003723 (EC: TAS, PMID:8812460); GO_0003743 (EC: IEA); GO_0005515 (EC: IPI, PMID:19203580); GO_0005829 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0006446 (EC: TAS, PMID:9516461); GO_0008135 (EC: TAS, PMID:9516461); GO_0010467 (EC: TAS); GO_0016032 (EC: IEA); GO_0016281 (EC: TAS, PMID:9516461); GO_0019953 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0048471 (EC: IEA); GO_0048589 (EC: IEA) PMID:7584026; 7584028; 8812460; 9516461; 10585411; 11003705; 11418588; 12477932; 12588972; 12665801; 12690205; 12853948; 15078951; 15489334; 15592455; 16014927; 16094384; 16189514; 18448541; 18719248; 19203580; 19369421; 19738201; 19847924; 20360068; 20473909; 20549515; 21139048; 21427765; 21906983; 22505724; 22863883; 22939629; 23776612; 24250222 eukaryotic translation initiation factor 4H Ensembl:ENSG00000106682 HGNC:12741 HPRD:11940 MIM:603431 Vega:OTTHUMG00000023025 Other designations: Williams-Beuren syndrome chromosome region 1 EIF4H OGG:3000007494 Bin Zhao, Yue Liu, Oliver He TREB5 XBP-1 XBP2 WEB: http://www.ncbi.nlm.nih.gov/gene XBP1 X-box binding protein 1 7494 22q12.1|22q12 9606 22 Official from a nomenclature committee GO_0003677 (EC: TAS, PMID: 1718857); GO_0003700 (EC: IEA); GO_0005634 (EC: IDA); GO_0005654 (EC: TAS); GO_0006366 (EC: IEA); GO_0006955 (EC: TAS, PMID: 1718857); GO_0006987 (EC: TAS); GO_0030968 (EC: TAS); GO_0031017 (EC: IEA); GO_0042493 (EC: IEA); GO_0043565 (EC: IEA); GO_0044267 (EC: TAS); GO_0051602 (EC: IEA); GO_0060096 (EC: IEA); GO_0060691 (EC: IEA); GO_0071236 (EC: IEA); GO_1900103 (EC: IMP, PMID: 16645094) PMID: 1718857; 1903538; 2196176; 2321018; 8349596; 8657566; 9563853; 10591208; 10652269; 11076863; 11256614; 11779464; 11813207; 12067985; 12477932; 12586069; 12713871; 12805554; 12949534; 12954762; 14576841; 14634507; 14702039; 15063770; 15149721; 15184063; 15298659; 15331160; 15351732; 15380296; 15461802; 15489334; 15489336; 15598891; 15882996; 15892135; 15927087; 15936534; 16002735; 16009131; 16154272; 16342282; 16381901; 16461360; 16645094; 16958950; 17026957; 17034899; 17092596; 17418411; 17442311; 17660348; 17884689; 17898050; 17906960; 17928342; 17932454; 18082745; 18191223; 18192112; 18386815; 18417469; 18552212; 18583979; 18635891; 18676680; 18775308; 18840095; 18840627; 19009018; 19122331; 19154631; 19170196; 19176362; 19237300; 19265690; 19321437; 19380033; 19389935; 19403667; 19412428; 19416856; 19420237; 19435892; 19470730; 19471022; 19530237; 19543371; 19564049; 19622636; 19625176; 19669932; 19692168; 19722195; 19735688; 19751410; 19941857; 19958799; 20013084; 20170659; 20211142; 20368688; 20421453; 20688044; 20955178; 20980528; 21050047; 21061914; 21085187; 21129256; 21129257; 21138464; 21138840; 21233347; 21385877; 21423203; 21660045; 21693764; 21858728; 21906983; 21924241; 21963094; 22002058; 22370484; 22427205; 22445760; 22469468; 22505724; 22644804; 22669460; 22679299; 22787145; 22925926; 22960999; 23184933; 23277279; 23335490; 23421912; 23447676; 23470653; 23510626; 23560553; 23661758; 23737521; 24027308; 24029229; 24165480 X-box binding protein 1 Ensembl:ENSG00000100219 HGNC:12801 HPRD:01908 MIM:194355 Vega:OTTHUMG00000151094 Other designations: X-box-binding protein 1|tax-responsive element-binding protein 5 XBP1 OGG:3000007804 Bin Zhao, Yue Liu, Oliver He APOER2 HSZ75190 LRP-8 MCI1 WEB: http://www.ncbi.nlm.nih.gov/gene LRP8 low density lipoprotein receptor-related protein 8, apolipoprotein e receptor 7804 RP5-1024G6.8 1p34 9606 1 Official from a nomenclature committee GO_0000122 (EC: ISS); GO_0001523 (EC: TAS); GO_0004888 (EC: TAS, PMID: 8626535); GO_0005509 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12950167); GO_0005576 (EC: IEA); GO_0005875 (EC: IEA); GO_0005886 (EC: TAS); GO_0005901 (EC: IDA, PMID: 11369809); GO_0006508 (EC: NAS, PMID: 11152697); GO_0006629 (EC: NAS, PMID: 11152697); GO_0006897 (EC: IDA, PMID: 8626535); GO_0006898 (EC: IDA, PMID: 8626535); GO_0007165 (EC: TAS, PMID: 10380922); GO_0007596 (EC: TAS); GO_0007603 (EC: TAS); GO_0008035 (EC: IEA); GO_0014069 (EC: IEA); GO_0016021 (EC: IC, PMID: 11152697); GO_0019221 (EC: NAS, PMID: 11152697); GO_0019894 (EC: IEA); GO_0021541 (EC: ISS); GO_0021819 (EC: IEA); GO_0030229 (EC: IDA, PMID: 8626535); GO_0030425 (EC: IEA); GO_0032793 (EC: ISS); GO_0034185 (EC: IC, PMID: 8626535); GO_0038025 (EC: ISS); GO_0038026 (EC: ISS); GO_0042493 (EC: IEA); GO_0043025 (EC: IEA); GO_0043235 (EC: IDA); GO_0050731 (EC: ISS); GO_0050804 (EC: ISS); GO_0061003 (EC: ISS); GO_0061098 (EC: ISS); GO_0071363 (EC: IEA); GO_0071397 (EC: IEA); GO_1900006 (EC: ISS) PMID: 8626535; 9079678; 10218790; 10231386; 10380922; 10508213; 10571240; 10827173; 11152697; 11369809; 12167620; 12169628; 12399018; 12426372; 12477932; 12621059; 12670700; 12681505; 12807892; 12824284; 12871934; 12899622; 12950167; 14702039; 14732905; 15313836; 15459198; 15489334; 15950758; 16034672; 16332682; 16481437; 16642433; 16951405; 17470198; 17614163; 17847002; 18039658; 18089558; 18489431; 18592168; 19056482; 19116273; 19282863; 19439088; 19661487; 19720620; 19913121; 19948739; 20208369; 20331378; 20493228; 20628086; 21157031; 21316997; 21347244; 21554715; 21601501; 21906983; 21963094; 22109552; 22170052; 22404453; 22419519; 22589174; 22889673; 23192594; 23524007; 23739027 low density lipoprotein receptor-related protein 8, apolipoprotein e receptor HGNC:6700 HPRD:04002 MIM:602600 Other designations: ApoE receptor 2|low-density lipoprotein receptor-related protein 8 LRP8 OGG:3000007832 Bin Zhao, Yue Liu, Oliver He PC3 TIS21 WEB: http://www.ncbi.nlm.nih.gov/gene BTG2 BTG family, member 2 7832 1q32 9606 1 Official from a nomenclature committee GO_0001077 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11136725); GO_0006281 (EC: TAS, PMID: 8944033); GO_0006479 (EC: IEA); GO_0006974 (EC: IDA, PMID: 8944033); GO_0008285 (EC: IMP); GO_0008306 (EC: IEA); GO_0009612 (EC: IEA); GO_0009952 (EC: IEA); GO_0014070 (EC: IEA); GO_0017148 (EC: IDA); GO_0021542 (EC: IEA); GO_0021954 (EC: IEA); GO_0031175 (EC: IMP, PMID: 18773938); GO_0035914 (EC: IEA); GO_0043434 (EC: IEA); GO_0043524 (EC: IEA); GO_0051602 (EC: IEA); GO_0060213 (EC: IDA, PMID: 18337750); GO_0070062 (EC: IDA, PMID: 19056867); GO_2000178 (EC: IEA) PMID: 1713584; 8663146; 8891336; 8944033; 9712883; 9828097; 10200315; 10341341; 10617598; 10669755; 11136725; 11237868; 11267995; 11377414; 11429045; 11470758; 11814693; 11856371; 11930152; 11989967; 12135500; 12360398; 12477932; 12771185; 15056715; 15378000; 15489334; 15542835; 15741235; 15788397; 16418486; 16710414; 16782888; 16997058; 17353931; 17371797; 18029348; 18196550; 18288394; 18337750; 18393292; 18773938; 18840609; 18854154; 18974182; 19056867; 19117054; 19203451; 19468252; 19546886; 19615363; 19728149; 20020054; 20398657; 20553615; 20569234; 21120602; 21172304; 21173166; 22266859; 22392501; 22493435; 22562501; 22614007; 22975506; 23089312; 23299537; 23857284; 23907596; 24047462; 24308156; 24440351 BTG family, member 2 Ensembl:ENSG00000159388 HGNC:1131 HPRD:03357 MIM:601597 Vega:OTTHUMG00000035834 Other designations: B-cell translocation gene 2|NGF-inducible anti-proliferative protein PC3|nerve growth factor-inducible anti-proliferative|pheochromacytoma cell-3|protein BTG2 BTG2 OGG:3000007873 Bin Zhao, Yue Liu, Oliver He ARMET ARP WEB: http://www.ncbi.nlm.nih.gov/gene MANF mesencephalic astrocyte-derived neurotrophic factor 7873 3p21.1 9606 3 Official from a nomenclature committee GO_0002014 (EC: IEA); GO_0003674 (EC: ND); GO_0005575 (EC: ND); GO_0005615 (EC: IEA); GO_0006986 (EC: IEA); GO_0008083 (EC: IEA); GO_0008150 (EC: ND); GO_0044822 (EC: IDA); GO_0048471 (EC: IEA) PMID: 8649854; 8971156; 9174057; 9230196; 10767373; 12477932; 12665801; 12794311; 14699964; 15146197; 15489334; 18561914; 18718866; 19258449; 19399876; 19641128; 20186704; 20685313; 21047780; 21139048; 21890473; 23000965; 23255601 mesencephalic astrocyte-derived neurotrophic factor Ensembl:ENSG00000145050 HGNC:15461 HPRD:03558 MIM:601916 Vega:OTTHUMG00000156897 Other designations: arginine-rich, mutated in early stage tumors MANF OGG:3000007965 Bin Zhao, Yue Liu, Oliver He JTV-1 JTV1 P38 WEB: http://www.ncbi.nlm.nih.gov/gene AIMP2 aminoacyl tRNA synthetase complex-interacting multifunctional protein 2 7965 PRO0992 7p22 9606 7 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 16189514); GO_0005634 (EC: IEA); GO_0005829 (EC: TAS); GO_0006418 (EC: TAS); GO_0006915 (EC: IEA); GO_0008285 (EC: IEA); GO_0010467 (EC: TAS); GO_0031398 (EC: IEA); GO_0060510 (EC: IEA) PMID: 600859; 1651330; 8052601; 8078941; 8188258; 8449960; 8666379; 9278442; 9878398; 10913161; 11714285; 12477932; 12690205; 12729910; 12783850; 12819782; 12853948; 15479637; 15489334; 16049031; 16055448; 16125937; 16135753; 16189514; 16714300; 17512523; 18676680; 18695251; 18781797; 19060904; 19170196; 19584093; 19625176; 19692168; 19738201; 21044950; 21110914; 21139048; 21209200; 21483803; 21832049; 21890473; 21900206; 21988832; 22190034; 22285955; 22532625; 22562359; 22751010; 22863883; 22939629; 23000965; 23455922; 23815603; 23824909; 23974709; 24250222 aminoacyl tRNA synthetase complex-interacting multifunctional protein 2 Ensembl:ENSG00000106305 HGNC:20609 HPRD:02915 MIM:600859 Vega:OTTHUMG00000122077 Other designations: ARS-interacting multi-functional protein 2|aminoacyl tRNA synthase complex-interacting multifunctional protein 2|multisynthase complex auxiliary component p38|multisynthetase complex auxiliary component p38|protein JTV-1 AIMP2 OGG:3000008309 Bin Zhao, Yue Liu, Oliver He BCOX BRCACOX BRCOX THCCox WEB: http://www.ncbi.nlm.nih.gov/gene ACOX2 acyl-CoA oxidase 2, branched chain 8309 3p14.3 9606 3 GO_0003995 (EC: IEA); GO_0003997 (EC: TAS); GO_0005102 (EC: IPI); GO_0005777 (EC: IDA, PMID:2079609); GO_0005782 (EC: TAS); GO_0006699 (EC: TAS); GO_0008206 (EC: TAS); GO_0016402 (EC: TAS); GO_0033540 (EC: TAS); GO_0033791 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0050660 (EC: IEA) PMID:2079609; 8387517; 8943006; 8993592; 9070889; 12477932; 15489334; 16756494; 20178365; 20379614; 21343950 acyl-CoA oxidase 2, branched chain Ensembl:ENSG00000168306 HGNC:120 HPRD:09037 MIM:601641 Vega:OTTHUMG00000159154 Other designations: 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase|3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase|THCA-CoA oxidase|acyl-Coenzyme A oxidase 2, branched chain|peroxisomal acyl-coenzyme A oxidase 2|peroxisomal branched chain acyl-CoA oxidase|trihydroxycoprostanoyl-CoA oxidase ACOX2 OGG:3000008310 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene ACOX3 acyl-CoA oxidase 3, pristanoyl 8310 4p15.3 9606 4 GO_0003995 (EC: IEA); GO_0005102 (EC: IPI); GO_0005739 (EC: IEA); GO_0005777 (EC: IDA, PMID:8993592); GO_0005782 (EC: TAS); GO_0016402 (EC: TAS); GO_0033540 (EC: IEA); GO_0033540 (EC: TAS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0050660 (EC: IEA) PMID:8125298; 8387517; 8993592; 9271077; 12477932; 15231748; 15489334; 15599942; 16344560; 16756494; 20178365; 20677014; 20877624; 21659360; 21906983; 22505724 acyl-CoA oxidase 3, pristanoyl Other designations: BRCACox|acyl-Coenzyme A oxidase 3, pristanoyl|branched-chain acyl-CoA oxidase|peroxisomal acyl-coenzyme A oxidase 3|pristanoyl-CoA oxidase ACOX3 OGG:3000008337 Bin Zhao, Yue Liu, Oliver He H2A H2A.2 H2A/O H2A/q H2AFO H2a-615 HIST2H2AA WEB: http://www.ncbi.nlm.nih.gov/gene HIST2H2AA3 histone cluster 2, H2aa3 8337 1q21.2 9606 1 Official from a nomenclature committee PMID: 2071153; 6326092; 8179821; 8543049; 8858345; 9439656; 9566873; 11080476; 11181995; 11375490; 11689053; 12408966; 12477932; 12628926; 14657027; 14759373; 14992727; 15010469; 15078818; 15386022; 15489334; 15527963; 15635413; 15823041; 16159877; 16319397; 16322561; 16359901; 16457589; 16702407; 16710414; 18688256; 19615732; 20525793; 20599239; 20639865; 20972266; 21041483; 21139048; 21179169; 21443952; 21693764; 21726816; 21772249; 21832049; 21890473; 21906983; 21963094; 21987572; 22053931; 22505724; 22810585; 22980979; 23000965; 23349634; 24457600 histone cluster 2, H2aa3 HGNC:4736 HPRD:08851 MIM:142720 Other designations: H2A histone family, member O|histone 2, H2aa3|histone H2A type 2-A HIST2H2AA3 OGG:3000008339 Bin Zhao, Yue Liu, Oliver He H2B.1A H2B/a H2BFA dJ221C16.8 WEB: http://www.ncbi.nlm.nih.gov/gene HIST1H2BG histone cluster 1, H2bg 8339 6p21.3 20140408 9606 6 protein-coding Official from a nomenclature committee PMID: 422550; 1916825; 8620898; 8814229; 9119399; 9439656; 9566873; 9973324; 11080476; 11689053; 11790298; 11859126; 12408966; 12477932; 12757711; 12860195; 14574404; 14595808; 14657027; 15019208; 15161933; 15489334; 16196087; 16283522; 16307923; 16319397; 16457587; 16627869; 16713563; 16916647; 18247557; 18457437; 20639865; 21130743; 21139048; 21890473; 21906983; 21907836; 21963094; 21987572; 22053931; 22505724; 22616001; 22623428; 23000965 histone cluster 1, H2bg Ensembl:ENSG00000187990 HGNC:4746 HPRD:11897 MIM:602798 Vega:OTTHUMG00000014446 Other designations: H2B histone family, member A|histone 1, H2bg|histone H2B type 1-C/E/F/G/I|histone H2B.1 A|histone H2B.a HIST1H2BG OGG:3000008431 The protein encoded by this gene is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. The gene product is a member of the nuclear hormone receptor family, a group of transcription factors regulated by small hydrophobic hormones, a subset of which do not have known ligands and are referred to as orphan nuclear receptors. The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. In addition, interaction with estrogen receptors has been demonstrated, leading to inhibition of function. Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function. [provided by RefSeq, Jul 2008] NCBI-Human-GeneID:8431 OMIM:604630 SHP1 nuclear receptor subfamily 0, group B, member 2 NR0B2 (mol) NCBI-Human-GeneID:8431 http://www.ncbi.nlm.nih.gov/gene/8431 OGG:3000008517 Bin Zhao, Yue Liu, Oliver He AMCBX1 FIP-3 FIP3 Fip3p IKK-gamma IP IP1 IP2 IPD2 NEMO ZC2HC9 WEB: http://www.ncbi.nlm.nih.gov/gene IKBKG inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma 8517 Xq28 9606 X GO_0000187 (EC: TAS); GO_0001782 (EC: IEA); GO_0002224 (EC: TAS); GO_0002755 (EC: TAS); GO_0002756 (EC: TAS); GO_0004871 (EC: TAS, PMID:9927690); GO_0005515 (EC: IPI, PMID:11113112); GO_0005622 (EC: IDA); GO_0005634 (EC: IDA, PMID:14651848); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006351 (EC: IEA); GO_0006915 (EC: TAS, PMID:9927690); GO_0006954 (EC: TAS, PMID:18626576); GO_0006955 (EC: TAS, PMID:9751060); GO_0006974 (EC: IDA, PMID:14651848); GO_0007249 (EC: TAS, PMID:18626576); GO_0007250 (EC: IEA); GO_0007254 (EC: TAS); GO_0008385 (EC: TAS, PMID:18626576); GO_0008385 (EC: TAS, Qualifier: colocalizes_with, PMID:16831874); GO_0009615 (EC: TAS, PMID:18626576); GO_0016032 (EC: IEA); GO_0019904 (EC: IPI, PMID:15341735); GO_0032481 (EC: TAS); GO_0034134 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0034146 (EC: TAS); GO_0034162 (EC: TAS); GO_0034166 (EC: TAS); GO_0035666 (EC: TAS); GO_0035872 (EC: TAS); GO_0038095 (EC: TAS); GO_0038123 (EC: TAS); GO_0038124 (EC: TAS); GO_0042803 (EC: IDA); GO_0043123 (EC: TAS); GO_0045087 (EC: TAS, PMID:18626576); GO_0045944 (EC: IDA); GO_0046872 (EC: IEA); GO_0046982 (EC: IDA); GO_0050852 (EC: NAS, PMID:15125833); GO_0050852 (EC: TAS, PMID:16831874); GO_0051092 (EC: IDA, PMID:15620648); GO_0051092 (EC: TAS, PMID:18626576); GO_0051403 (EC: TAS); GO_0070423 (EC: TAS) PMID:9744859; 9751060; 9891086; 9927690; 10087442; 10364167; 10723127; 10733566; 10755617; 10839543; 10880512; 10944468; 10962024; 10962033; 10968790; 10980203; 11002417; 11047757; 11057907; 11064457; 11080499; 11113112; 11224521; 11242109; 11256614; 11262391; 11389905; 11410370; 11418127; 11485410; 11495908; 11551959; 11590134; 11673821; 11709543; 11830587; 11864612; 11877453; 11971901; 11971985; 12045264; 12133833; 12138192; 12192055; 12244103; 12435599; 12459277; 12477932; 12486103; 12530972; 12612076; 12657630; 12808104; 12867425; 12917689; 12917690; 12917691; 12943667; 14585847; 14585990; 14597638; 14651848; 14653779; 14684825; 14695475; 14726382; 14743216; 14748687; 14754897; 14764716; 15043934; 15100680; 15125833; 15184390; 15218148; 15229184; 15231748; 15276183; 15327770; 15341735; 15356572; 15371500; 15456791; 15474016; 15489334; 15578091; 15601829; 15601896; 15620648; 15670770; 15749833; 15802604; 15833158; 15870263; 16051665; 16126728; 16148947; 16227629; 16267042; 16301747; 16311516; 16319058; 16360037; 16379012; 16424386; 16497931; 16543241; 16547522; 16583354; 16603398; 16611882; 16627981; 16684768; 16697380; 16737960; 16794254; 16831874; 16874300; 16906147; 17000764; 17043643; 17047224; 17135271; 17145747; 17244613; 17314097; 17314283; 17363905; 17363973; 17401323; 17401626; 17468758; 17568778; 17626013; 17693255; 17702576; 17728323; 17766391; 17891179; 17910706; 17932497; 17939994; 17942533; 17948050; 17977820; 17997719; 18029035; 18029348; 18037881; 18079694; 18180283; 18187620; 18201555; 18207244; 18212736; 18216269; 18266324; 18266467; 18287044; 18313693; 18347055; 18350553; 18429822; 18511905; 18583959; 18617513; 18620544; 18625728; 18626576; 18685082; 18841575; 18851874; 18931663; 18949366; 18952891; 18957422; 19033441; 19064727; 19149237; 19185524; 19285159; 19303852; 19305025; 19327867; 19365808; 19373245; 19373254; 19404319; 19422324; 19453261; 19494296; 19531477; 19603533; 19609363; 19656162; 19656241; 19675569; 19687056; 19763089; 19815509; 19820708; 19854204; 19875381; 19880420; 19897484; 19948975; 19956647; 20005846; 20010814; 20026645; 20065354; 20098747; 20161788; 20164171; 20167598; 20211142; 20301198; 20301645; 20353939; 20368414; 20380930; 20412081; 20434027; 20484576; 20499091; 20529958; 20542322; 20586999; 20724660; 20837477; 20890435; 20923877; 20932475; 20932476; 20959607; 20970423; 21057728; 21097508; 21109981; 21113135; 21131783; 21139048; 21153314; 21184742; 21212807; 21217772; 21220427; 21286028; 21309033; 21383699; 21458669; 21474709; 21486954; 21512573; 21513986; 21518757; 21538482; 21606198; 21622571; 21622647; 21703539; 21704885; 21709223; 21722947; 21777808; 21790911; 21803029; 21811235; 21862579; 21862596; 21890473; 21896478; 21903422; 21906983; 21963094; 21988832; 22054014; 22081069; 22099304; 22118674; 22176836; 22300264; 22341466; 22505724; 22513115; 22517901; 22525270; 22547678; 22605335; 22607974; 22732732; 22848449; 22863883; 22901541; 22939629; 22990857; 23000965; 23000966; 23007157; 23028469; 23032186; 23032187; 23102662; 23123196; 23131831; 23453969; 23483900; 23506214; 23524849; 23575687; 23690623; 23732909; 23746843; 23776175; 23807287; 23950712; 23986494; 24030825; 24100029; 24109239; 24240172; 24266532; 24270572 inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma Ensembl:ENSG00000073009 HGNC:5961 HPRD:02217 MIM:300248 Vega:OTTHUMG00000024234 Other designations: I-kappa-B kinase subunit gamma|IKKAP1|IKKG|IkB kinase gamma subunit|NF-kappa-B essential modifier|NF-kappa-B essential modulator|NFkappaB essential modulator|ikB kinase subunit gamma|ikB kinase-associated protein 1|incontinentia pigmenti|inhibitor of nuclear factor kappa-B kinase subunit gamma IKBKG OGG:3000008529 Bin Zhao, Yue Liu, Oliver He CPF2 WEB: http://www.ncbi.nlm.nih.gov/gene CYP4F2 cytochrome P450, family 4, subfamily F, polypeptide 2 8529 19p13.12 9606 19 GO_0000038 (EC: IDA, PMID:18433732); GO_0001676 (EC: IDA, PMID:18433732); GO_0003091 (EC: IEP, PMID:10660572); GO_0003095 (EC: IEP, PMID:10660572); GO_0005506 (EC: IEA); GO_0005515 (EC: IPI, PMID:17474147); GO_0005737 (EC: IDA, PMID:10660572); GO_0005789 (EC: TAS); GO_0006690 (EC: TAS); GO_0006691 (EC: TAS); GO_0006805 (EC: TAS); GO_0008217 (EC: IMP, PMID:18391101); GO_0008392 (EC: IDA); GO_0016324 (EC: IDA, PMID:10660572); GO_0017144 (EC: IMP); GO_0018685 (EC: IDA, PMID:18433732); GO_0019369 (EC: IDA, PMID:10660572); GO_0019369 (EC: TAS); GO_0019373 (EC: IDA); GO_0020037 (EC: IEA); GO_0030195 (EC: IMP, PMID:19297518); GO_0032304 (EC: IMP, PMID:18391101); GO_0032305 (EC: IMP, PMID:17341693); GO_0036101 (EC: IDA, PMID:10492403); GO_0042360 (EC: IDA); GO_0042371 (EC: IMP, PMID:19297518); GO_0043231 (EC: IDA, PMID:10660572); GO_0044281 (EC: TAS); GO_0047057 (EC: IMP, PMID:19297518); GO_0050051 (EC: IDA, PMID:8026587); GO_0052869 (EC: IDA, PMID:10660572); GO_0052871 (EC: IDA); GO_0052872 (EC: IDA); GO_0055078 (EC: IEP, PMID:10660572); GO_0055114 (EC: IDA); GO_0097267 (EC: TAS) PMID:8026587; 8424651; 9068972; 9618440; 9799565; 10492403; 10660572; 10860554; 11162441; 11715494; 12477932; 12736711; 15057824; 15128046; 15489334; 16733892; 17142457; 17284776; 17341693; 17474147; 18065749; 18235092; 18250228; 18391101; 18433732; 18574070; 18662666; 18787519; 18971550; 19097922; 19207028; 19270263; 19279555; 19297518; 19297519; 19300499; 19343046; 19545555; 19578179; 19741565; 19794411; 19913121; 19957603; 19958090; 20072124; 20130494; 20149073; 20182420; 20227456; 20421126; 20442691; 20499136; 20504253; 20553802; 20555338; 20628086; 20653676; 20833655; 20861217; 21063236; 21084764; 21127708; 21150635; 21475774; 21562135; 21625857; 21729881; 21883387; 21887457; 21906983; 22188360; 22198820; 22393834; 22437554; 22452429; 22484021; 22528326; 22534826; 22549502; 22854539; 22855348; 23013706; 23018470; 23132553; 23215885; 23281178; 23510058; 23726967; 24138531 cytochrome P450, family 4, subfamily F, polypeptide 2 Ensembl:ENSG00000186115 HGNC:2645 HPRD:05112 MIM:604426 Vega:OTTHUMG00000185995 Other designations: CYPIVF2|cytochrome P450 4F2|cytochrome P450, subfamily IVF, polypeptide 2|cytochrome P450-LTB-omega|leukotriene B4 omega-hydroxylase|leukotriene-B(4) 20-monooxygenase 1|leukotriene-B(4) omega-hydroxylase 1|leukotriene-B4 20-monooxygenase CYP4F2 OGG:3000008542 Bin Zhao, Yue Liu, Oliver He APO-L APOL APOL-I FSGS4 WEB: http://www.ncbi.nlm.nih.gov/gene APOL1 apolipoprotein L, 1 8542 RP1-68O2.2 22q13.1 20140408 9606 22 protein-coding Official from a nomenclature committee GO_0005254 (EC: IDA, PMID: 16020735); GO_0005515 (EC: IPI, PMID: 12621437); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID: 17192540); GO_0006821 (EC: IDA, PMID: 16020735); GO_0006869 (EC: IEA); GO_0008203 (EC: IEA); GO_0008289 (EC: IDA, PMID: 16020735); GO_0019835 (EC: IDA, PMID: 12621437); GO_0031224 (EC: IC, PMID: 16020735); GO_0031640 (EC: IDA, PMID: 12621437); GO_0034361 (EC: IDA, PMID: 17154273); GO_0034364 (EC: IDA, PMID: 9325276); GO_0042157 (EC: IEA); GO_0045087 (EC: IDA, PMID: 17192540); GO_0072562 (EC: IDA); GO_1902476 (EC: IDA, PMID: 16020735) PMID: 9325276; 10591208; 10946010; 11290834; 11374903; 11944986; 12477932; 12621437; 12837283; 14718574; 15489334; 15500911; 15604524; 15949655; 16020735; 16335952; 16344560; 17154273; 17192540; 17360487; 17845074; 18505729; 18632255; 18850207; 18927493; 19239905; 19324878; 19913121; 20483474; 20602615; 20628086; 20635188; 20647424; 20668430; 20805508; 20855565; 21080072; 21486385; 21537348; 21698141; 21910715; 21931123; 21968148; 21997392; 21997394; 21997396; 21997397; 21997398; 22119407; 22135313; 22239288; 22357707; 22487534; 22495294; 22569246; 22691369; 22695330; 22832513; 22878977; 22956460; 23082501; 23107266; 23300552; 23438974; 23520206; 23766536; 23768513; 24206458 apolipoprotein L, 1 Ensembl:ENSG00000100342 HGNC:618 HPRD:04774 MIM:603743 Vega:OTTHUMG00000030427 Other designations: apolipoprotein L1 APOL1 OGG:3000008544 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene PIR pirin (iron-binding nuclear protein) 8544 Xp22.2 9606 X Official from a nomenclature committee GO_0003712 (EC: IMP); GO_0005515 (EC: IPI, PMID: 10362352); GO_0005634 (EC: IDA, PMID: 9079676); GO_0005737 (EC: IDA); GO_0006355 (EC: IEA); GO_0006366 (EC: TAS, PMID: 9079676); GO_0008127 (EC: IDA, PMID: 15951572); GO_0030224 (EC: IMP); GO_0046872 (EC: IDA) PMID: 9079676; 10362352; 12477932; 12876364; 14573596; 15231748; 15489334; 15951572; 16344560; 17213182; 19766747; 20010624; 20089166; 20711196; 21514450; 22939629; 23716661; 24272884 pirin (iron-binding nuclear protein) Other designations: pirin|probable quercetin 2,3-dioxygenase PIR|probable quercetinase PIR OGG:3000008575 Bin Zhao, Yue Liu, Oliver He DYT16 PACT RAX WEB: http://www.ncbi.nlm.nih.gov/gene PRKRA protein kinase, interferon-inducible double stranded RNA dependent activator 8575 HSD14 2q31.2 9606 2 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 16424907); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006468 (EC: IEA); GO_0006955 (EC: TAS, PMID: 9687506); GO_0008047 (EC: TAS, PMID: 9687506); GO_0008285 (EC: TAS, PMID: 9687506); GO_0009615 (EC: TAS, PMID: 9687506); GO_0010467 (EC: TAS); GO_0030422 (EC: IDA, PMID: 17452327); GO_0034599 (EC: IEA); GO_0042473 (EC: IEA); GO_0042474 (EC: IEA); GO_0042803 (EC: IPI, PMID: 17452327); GO_0043085 (EC: TAS, PMID: 9687506); GO_0044822 (EC: IDA); GO_0048471 (EC: IEA); GO_0048705 (EC: IEA); GO_2001244 (EC: IEA) PMID: 8125298; 9010216; 9687506; 10336432; 11230166; 11238927; 11256614; 11526399; 11985496; 12368348; 12477932; 12874289; 14702039; 15299031; 15489334; 15815621; 16169070; 16424907; 16861340; 16982605; 17081983; 17125937; 17353931; 17452327; 18243799; 18420150; 18936160; 19441135; 19580324; 19604093; 19913121; 20379614; 20468071; 20588308; 20628086; 20628624; 21139048; 21145461; 21501829; 21526770; 21595004; 21790829; 21882225; 21900206; 21903422; 21988832; 22025453; 22214662; 22473766; 22505724; 22586326; 22961479; 22990118; 23455922; 23472185; 23550157; 23602568; 23658827; 23661684; 23844083; 23870315; 24067967; 24457600 protein kinase, interferon-inducible double stranded RNA dependent activator Ensembl:ENSG00000180228 HGNC:9438 HPRD:04573 MIM:603424 Vega:OTTHUMG00000132576 Other designations: PKR-associated protein X|PKR-associating protein X|interferon-inducible double stranded RNA-dependent protein kinase activator A|interferon-inducible double-stranded RNA-dependent protein kinase activator A|protein activator of the interferon-induced protein kinase|protein kinase, interferon-inducible double stranded RNA-dependent activator|protein kinase, interferon-inducible double-stranded RNA-dependent activator PRKRA OGG:3000008637 Bin Zhao, Yue Liu, Oliver He 4E-BP3 4EBP3 WEB: http://www.ncbi.nlm.nih.gov/gene EIF4EBP3 eukaryotic translation initiation factor 4E binding protein 3 8637 5q31.3 9606 5 GO_0005515 (EC: IPI, PMID:15153109); GO_0008190 (EC: IEA); GO_0016281 (EC: NAS, PMID:9593750); GO_0030371 (EC: NAS, PMID:9593750); GO_0045947 (EC: NAS, PMID:9593750) PMID:9593750; 11865047; 12477932; 12482586; 14507920; 14557257; 15153109; 15489334; 16189514; 16271312; 17316564; 19615732; 20621385; 21088106; 21145461; 22684010 eukaryotic translation initiation factor 4E binding protein 3 Ensembl:ENSG00000243056 HGNC:3290 HPRD:09149 MIM:603483 Vega:OTTHUMG00000129498 Other designations: eIF4E-binding protein 3|eukaryotic initiation factor 4E-binding protein 3|eukaryotic translation initiation factor 4E-binding protein 3 EIF4EBP3 OGG:3000008647 ABC16 BRIC2 BSEP PFIC-2 PFIC2 PGY4 SPGP ATP-binding cassette, sub-family B (MDR/TAP), member 11 8647 GO_0000139 (EC: IBA); GO_0005215 (EC: TAS, PMID:9806540); GO_0005524 (EC: IEA); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:9806540); GO_0006699 (EC: TAS); GO_0006810 (EC: TAS, PMID:9806540); GO_0008206 (EC: TAS); GO_0008554 (EC: TAS, PMID:9806540); GO_0015126 (EC: IBA); GO_0015432 (EC: TAS, PMID:9806540); GO_0015721 (EC: TAS); GO_0015722 (EC: IBA); GO_0016020 (EC: TAS, PMID:9806540); GO_0016021 (EC: IBA); GO_0016324 (EC: IBA); GO_0035725 (EC: TAS, PMID:9806540); GO_0042626 (EC: IBA); GO_0044281 (EC: TAS); GO_0046581 (EC: IBA); GO_0055085 (EC: IBA); GO_0070062 (EC: IDA, PMID:19056867) PMID:9545351; 9806540; 10579978; 11172067; 11495894; 11600213; 11745042; 11783115; 11815775; 11829140; 12825874; 14762791; 14999697; 15077010; 15159385; 15300568; 15471871; 15791618; 16039748; 16290310; 16749857; 16763017; 16871584; 16890614; 16941683; 17264802; 17622941; 18176959; 18270374; 18395098; 18521185; 18660489; 18668439; 18676680; 18692205; 18987030; 19056867; 19060910; 19101985; 19170196; 19343046; 19408031; 19571440; 19625176; 19669124; 19692168; 19821532; 19833092; 19845854; 19888660; 19898482; 19913121; 19937311; 20010382; 20028269; 20147439; 20163776; 20232290; 20301474; 20379614; 20414253; 20447715; 20453000; 20628086; 20683201; 20702406; 20723035; 20855565; 20857261; 20858683; 20883210; 21139048; 21386085; 21490445; 21691112; 21766090; 21811948; 21909109; 21988832; 22001757; 22098322; 22161577; 22673116; 22681771; 23022423; 23279303; 23750872; 23876151; 23929842; 24058526; 24366234; 24378332 ATP-binding cassette, sub-family B (MDR/TAP), member 11 http://omim.org/entry/603201 Other designations: ABC member 16, MDR/TAP subfamily|ATP-binding cassette sub-family B member 11|bile salt export pump|progressive familial intrahepatic cholestasis 2|sister p-glycoprotein ABCB11 OGG:3000008661 Bin Zhao, Yue Liu, Oliver He EIF3 EIF3S10 P167 TIF32 eIF3-p170 eIF3-theta p180 p185 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3A eukaryotic translation initiation factor 3, subunit A 8661 10q26 9606 10 GO_0001731 (EC: IEA); GO_0001732 (EC: IDA, PMID:17581632); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005198 (EC: NAS, PMID:9150439); GO_0005515 (EC: IPI, PMID:11169732); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005737 (EC: IDA); GO_0005737 (EC: NAS, PMID:9150439); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: TAS); GO_0006446 (EC: IEA); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:2110361; 8590280; 8816444; 8995409; 8995410; 9054404; 9150439; 9341143; 9418880; 9790534; 9804427; 9822659; 9925932; 10444591; 10611228; 11102443; 11169732; 11384103; 11590142; 12124384; 12477932; 12588972; 12812986; 12878157; 12904573; 14519125; 15946946; 16385451; 16497727; 16541103; 16582619; 16829125; 17322308; 17353931; 17361185; 17381544; 17403899; 17581632; 18000879; 18029348; 18354498; 18423202; 18502210; 18568671; 18599441; 18628297; 18725400; 18781797; 19245811; 19327350; 19454010; 19615732; 19738201; 20020773; 20056645; 20068067; 20360068; 20399188; 20562859; 20647036; 20818067; 20936779; 21078624; 21139048; 21319273; 21610145; 21625209; 21890473; 21906983; 21963094; 22022972; 22053931; 22108332; 22145905; 22190034; 22268729; 22505724; 22623428; 22634302; 22863883; 22939629; 22952844; 23000965; 23127338; 23184937; 23393223; 23437357; 23455922; 23463506; 23530232; 23623729; 23766293; 23862649; 23921387; 24457600; 24515614 eukaryotic translation initiation factor 3, subunit A Ensembl:ENSG00000107581 HGNC:3271 HPRD:03618 MIM:602039 Vega:OTTHUMG00000019144 Other designations: EIF3, p180 subunit|centrosomin homolog|cytoplasmic protein p167|eIF-3-theta|eIF3 p167|eIF3 p180|eIF3 p185|eukaryotic translation initiation factor 3 subunit 10|eukaryotic translation initiation factor 3 subunit A|eukaryotic translation initiation factor 3, subunit 10 (theta, 150/170kD)|eukaryotic translation initiation factor 3, subunit 10 (theta, 170kD)|eukaryotic translation initiation factor 3, subunit 10 theta, 150/170kDa|eukaryotic translation initiation factor 3, subunit 10, 170kD EIF3A OGG:3000008662 Bin Zhao, Yue Liu, Oliver He EIF3-ETA EIF3-P110 EIF3-P116 EIF3S9 PRT1 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3B eukaryotic translation initiation factor 3, subunit B 8662 7p22.3 9606 7 GO_0000166 (EC: IEA); GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, PMID:8995410); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005515 (EC: IPI, PMID:11169732); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: IDA, PMID:8995410); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0031369 (EC: IEA); GO_0032947 (EC: TAS, PMID:17322308); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS); GO_0070062 (EC: IDA) PMID:7693677; 8889548; 8995409; 8995410; 9388245; 9822659; 9847074; 11169732; 11331597; 12477932; 12588972; 12690205; 14519125; 14688252; 14702039; 15047060; 15302935; 15489334; 15592455; 15946946; 16159877; 16196087; 16286006; 16541103; 17053147; 17081983; 17190833; 17322308; 17403899; 17581632; 18423202; 18457437; 18599441; 18628297; 18781797; 19245811; 19454010; 19615732; 19738201; 20020773; 20060839; 20360068; 20508642; 20862284; 20972266; 21045808; 21081666; 21139048; 21890473; 21906983; 21963094; 21987572; 22145905; 22190034; 22234522; 22268729; 22505724; 22623428; 22863883; 22939629; 22990118; 23000965; 23184937; 23398456; 23455922; 23463506; 23575475; 24457600 eukaryotic translation initiation factor 3, subunit B Ensembl:ENSG00000106263 HGNC:3280 HPRD:06795 MIM:603917 Vega:OTTHUMG00000022839 Other designations: eIF-3-eta|eIF3 p110|eIF3 p116|eukaryotic translation initiation factor 3 subunit 9|eukaryotic translation initiation factor 3 subunit B|eukaryotic translation initiation factor 3, subunit 9 (eta, 116kD)|eukaryotic translation initiation factor 3, subunit 9 eta, 116kDa|hPrt1|prt1 homolog EIF3B OGG:3000008663 Bin Zhao, Yue Liu, Oliver He EIF3CL EIF3S8 eIF3-p110 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3C eukaryotic translation initiation factor 3, subunit C 8663 16p11.2 9606 16 GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005515 (EC: IPI, PMID:18628297); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: IEA); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0031369 (EC: IEA); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:8995409; 8995410; 9822659; 10493829; 10504338; 12477932; 12514125; 12588972; 14519125; 14702039; 15047060; 15146197; 15231748; 15302935; 15489334; 15840729; 15946946; 16083285; 16097034; 16169070; 16196087; 16286006; 16341674; 16964243; 17081983; 17322308; 17361185; 17403899; 17581632; 18599441; 18628297; 18781797; 19245811; 19615732; 19850743; 19915574; 20020773; 20360068; 20508642; 20972266; 21081666; 21102463; 21145461; 21209461; 21319273; 21890473; 21900206; 21906983; 21963094; 21987572; 22016036; 22145905; 22190034; 22505724; 22863883; 22939629; 23000965; 23128233; 23455922; 23463506; 23733421; 23862649; 24092755; 24515614 eukaryotic translation initiation factor 3, subunit C Ensembl:ENSG00000184110 HGNC:3279 HPRD:04889 MIM:603916 Vega:OTTHUMG00000099443 Other designations: cell migration-inducing protein 17|eIF3 p110|eukaryotic translation initiation factor 3 subunit 8|eukaryotic translation initiation factor 3 subunit C|eukaryotic translation initiation factor 3, subunit 8 (110kD)|eukaryotic translation initiation factor 3, subunit 8, 110kDa EIF3C OGG:3000008664 Bin Zhao, Yue Liu, Oliver He EIF3S7 eIF3-p66 eIF3-zeta WEB: http://www.ncbi.nlm.nih.gov/gene EIF3D eukaryotic translation initiation factor 3, subunit D 8664 RP5-1119A7.12-003 22q13.1 9606 22 GO_0001731 (EC: IEA); GO_0001732 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005515 (EC: IPI, PMID:11369516); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: IEA); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:8995409; 8995410; 9341143; 9822659; 10591208; 11331597; 11369516; 11590142; 12477932; 12588972; 14519125; 15047060; 15461802; 15489334; 15592455; 17322308; 17353931; 17361185; 17403899; 17474147; 17581632; 18571626; 18599441; 18628297; 19615732; 19738201; 20171186; 20360068; 20890303; 21139048; 21145461; 21890473; 21900206; 21906983; 21963094; 22145905; 22190034; 22505724; 22586326; 22863883; 22939629; 22944692; 23000965; 23455922; 24092755; 24457600 eukaryotic translation initiation factor 3, subunit D Ensembl:ENSG00000100353 HGNC:3278 HPRD:04888 MIM:603915 Vega:OTTHUMG00000150599 Other designations: eIF-3-zeta|eIF3 p66|eukaryotic translation initiation factor 3 subunit 7|eukaryotic translation initiation factor 3 subunit D|eukaryotic translation initiation factor 3, subunit 7 zeta, 66/67kDa|translation initiation factor eIF3 p66 subunit EIF3D OGG:3000008665 Bin Zhao, Yue Liu, Oliver He EIF3S5 eIF3-p47 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3F eukaryotic translation initiation factor 3, subunit F 8665 11p15.4 9606 11 GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0003743 (EC: TAS, PMID:9341143); GO_0004843 (EC: IDA); GO_0005515 (EC: IPI, PMID:18354498); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0005852 (EC: TAS, PMID:9341143); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: IEA); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0016579 (EC: IDA); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS) PMID:8995409; 8995410; 9341143; 9822659; 12446680; 12477932; 12588972; 14519125; 14702039; 15231748; 15489334; 15862967; 16159877; 16169070; 16189514; 16196087; 16286006; 16537434; 16541103; 16712791; 17207965; 17322308; 17353931; 17361185; 17403899; 17581632; 17918192; 18354498; 18381585; 18599441; 18628297; 18724935; 19073596; 19237569; 19245811; 19454010; 19615732; 19738201; 19854136; 20360068; 20800221; 21081666; 21124883; 21139048; 21832049; 21963094; 22145905; 22190034; 22268729; 22457825; 22505724; 22797925; 22863883; 22939629; 23275563; 23463506; 24457600 eukaryotic translation initiation factor 3, subunit F Ensembl:ENSG00000175390 HGNC:3275 HPRD:04887 MIM:603914 Other designations: deubiquitinating enzyme eIF3f|eIF-3-epsilon|eIF3-epsilon|eukaryotic translation initiation factor 3 subunit F|eukaryotic translation initiation factor 3, subunit 5 (epsilon, 47kD)|eukaryotic translation initiation factor 3, subunit 5 epsilon, 47kDa EIF3F OGG:3000008666 Bin Zhao, Yue Liu, Oliver He EIF3-P42 EIF3S4 eIF3-delta eIF3-p44 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3G eukaryotic translation initiation factor 3, subunit G 8666 19p13.2 9606 19 GO_0000166 (EC: IEA); GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005515 (EC: IPI, PMID:14688252); GO_0005634 (EC: IEA); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: IEA); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0048471 (EC: IEA) PMID:8889549; 8995409; 8995410; 9341143; 9822659; 9973622; 10887144; 12477932; 12588972; 14519125; 14688252; 15231747; 15302935; 15489334; 16243297; 17094969; 17322308; 17353931; 17361185; 17403899; 17581632; 18599441; 18628297; 19471022; 19615732; 20360068; 20406461; 21044950; 21139048; 21145461; 21832049; 21890473; 21900206; 21906983; 22190034; 22493286; 22863883; 22939629; 23398456; 23402259; 23463506; 24080033 eukaryotic translation initiation factor 3, subunit G Ensembl:ENSG00000130811 HGNC:3274 HPRD:04886 MIM:603913 Vega:OTTHUMG00000180396 Other designations: eIF-3 RNA-binding subunit|eIF-3-delta|eIF3 p42|eIF3 p44|eukaryotic translation initiation factor 3 RNA-binding subunit|eukaryotic translation initiation factor 3 subunit 4|eukaryotic translation initiation factor 3 subunit G|eukaryotic translation initiation factor 3 subunit p42|eukaryotic translation initiation factor 3, subunit 4 (delta, 44kD)|eukaryotic translation initiation factor 3, subunit 4 delta, 44kDa EIF3G OGG:3000008667 Bin Zhao, Yue Liu, Oliver He EIF3S3 eIF3-gamma eIF3-p40 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3H eukaryotic translation initiation factor 3, subunit H 8667 8q24.11 9606 8 GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005515 (EC: IPI, PMID:12812986); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: TAS, PMID:9341143); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0070062 (EC: IDA, PMID:19056867) PMID:8125298; 8995409; 8995410; 9341143; 9822659; 11733359; 12477932; 12588972; 12812986; 14519125; 14578863; 14702039; 14997205; 15489334; 16159877; 16189514; 16196087; 16226712; 16263121; 16286006; 16344560; 16652384; 17043677; 17081983; 17322308; 17353931; 17361185; 17403899; 17581632; 18029348; 18187620; 18372905; 18544531; 18599441; 18628297; 19056867; 19060904; 19204574; 19615732; 20016921; 20020773; 20360068; 20437058; 20508642; 20659471; 20862326; 21139048; 21319273; 21761138; 21890473; 21906983; 21963094; 22108332; 22190034; 22505724; 22863883; 22939629; 22969067; 22990118; 23000965; 23184937; 23398456; 23402259; 23455922; 23463506; 24163370 eukaryotic translation initiation factor 3, subunit H HGNC:3273 HPRD:04885 MIM:603912 Other designations: eIF-3-gamma|eIF3 p40 subunit|eukaryotic translation initiation factor 3 subunit 3|eukaryotic translation initiation factor 3 subunit H|eukaryotic translation initiation factor 3, subunit 2 (beta, 36kD)|eukaryotic translation initiation factor 3, subunit 3 (gamma, 40kD)|eukaryotic translation initiation factor 3, subunit 3 gamma, 40kDa EIF3H OGG:3000008668 Bin Zhao, Yue Liu, Oliver He EIF3S2 PRO2242 TRIP-1 TRIP1 eIF3-beta eIF3-p36 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3I eukaryotic translation initiation factor 3, subunit I 8668 RP4-675E8.1 1p34.1 9606 1 GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, PMID:17581632); GO_0005515 (EC: IPI, PMID:14688252); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: IEA); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS); GO_0070062 (EC: IDA) PMID:7566156; 7566158; 8125298; 8995409; 8995410; 9368056; 9599024; 9813058; 9822659; 10706629; 11781097; 12477932; 12588972; 14519125; 14688252; 15047060; 15231747; 15489334; 15592455; 15604093; 16159877; 16196087; 16236267; 16341674; 16541103; 16929481; 17314511; 17322308; 17353931; 17361185; 17403899; 17581632; 17620599; 18599441; 18624398; 18628297; 18781797; 19059401; 19329541; 19615732; 19738201; 20020773; 20360068; 20508642; 20972266; 21139048; 21145461; 21319273; 21378021; 21890473; 21906983; 21963094; 21987572; 22022972; 22053931; 22145905; 22174317; 22190034; 22505724; 22586326; 22623428; 22863883; 22939629; 22990118; 23000965; 23349634; 23398456; 23402259; 23455922; 23463506; 23602568; 24163370; 24457600 eukaryotic translation initiation factor 3, subunit I Ensembl:ENSG00000084623 HGNC:3272 HPRD:04884 MIM:603911 Vega:OTTHUMG00000007364 Other designations: TGF-beta receptor-interacting protein 1|TGFbeta receptor-interacting protein 1|eIF-3-beta|eIF3 p36|eukaryotic translation initiation factor 3 subunit 2|eukaryotic translation initiation factor 3 subunit I|eukaryotic translation initiation factor 3, subunit 2 (beta, 36kD)|eukaryotic translation initiation factor 3, subunit 2 beta, 36kDa|predicted protein of HQ2242 EIF3I OGG:3000008669 Bin Zhao, Yue Liu, Oliver He EIF3S1 eIF3-alpha eIF3-p35 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3J eukaryotic translation initiation factor 3, subunit J 8669 PRO0391 15q21.1 9606 15 GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0005515 (EC: IPI, PMID:14688252); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: TAS); GO_0006446 (EC: IEA); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA); GO_0044267 (EC: TAS) PMID:9822659; 10672017; 11560931; 12477932; 14519125; 14688252; 14702039; 15146197; 15489334; 15703437; 15946946; 16169070; 16766523; 16964243; 17081983; 17190833; 17322308; 17403899; 17588516; 18599441; 18628297; 18658124; 19471022; 19615732; 20060839; 20360068; 21139048; 21890473; 22025682; 22113938; 22190034; 22804784; 22863883; 23000965; 23455922; 24163370 eukaryotic translation initiation factor 3, subunit J Ensembl:ENSG00000104131 HGNC:3270 HPRD:04883 MIM:603910 Vega:OTTHUMG00000131158 Other designations: eukaryotic translation initiation factor 3 subunit J|eukaryotic translation initiation factor 3, subunit 1 (alpha, 35kD) EIF3J OGG:3000008672 Bin Zhao, Yue Liu, Oliver He eIF-4G 3 eIF4G 3 eIF4GII WEB: http://www.ncbi.nlm.nih.gov/gene EIF4G3 eukaryotic translation initiation factor 4 gamma, 3 8672 RP11-190H11.1 1p36.12 9606 1 GO_0000339 (EC: TAS, PMID:9418880); GO_0001934 (EC: IEA); GO_0003743 (EC: IEA); GO_0005829 (EC: TAS); GO_0006446 (EC: TAS, PMID:9418880); GO_0007283 (EC: IEA); GO_0008135 (EC: TAS, PMID:9418880); GO_0016032 (EC: IEA); GO_0016281 (EC: TAS, PMID:9418880); GO_0019221 (EC: TAS); GO_0044822 (EC: IDA); GO_0045727 (EC: IEA); GO_0060903 (EC: IEA) PMID:8125298; 9418880; 9857202; 9878069; 10022874; 10737800; 10872469; 11172724; 12477932; 12663812; 12975586; 14507913; 15016848; 15146197; 15361857; 15489334; 16344560; 16964243; 17081983; 17353931; 18654987; 19615732; 19805454; 20020773; 20379614; 21139048; 21182205; 21890473; 21900206; 21906983; 21963094; 22505724; 22586326; 22939629; 22990118; 23000965 eukaryotic translation initiation factor 4 gamma, 3 Ensembl:ENSG00000075151 HGNC:3298 HPRD:06802 MIM:603929 Vega:OTTHUMG00000002624 Other designations: eIF-4-gamma 3|eIF-4-gamma II|eukaryotic translation initiation factor 4 gamma 3 EIF4G3 OGG:3000008717 Bin Zhao, Yue Liu, Oliver He Hs.89862 WEB: http://www.ncbi.nlm.nih.gov/gene TRADD TNFRSF1A-associated via death domain 8717 16q22 9606 16 Official from a nomenclature committee GO_0004871 (EC: IEA); GO_0005164 (EC: IEA); GO_0005515 (EC: IPI, PMID: 1040062); GO_0005634 (EC: IEA); GO_0005737 (EC: IDA, PMID: 11684708); GO_0005829 (EC: TAS); GO_0005856 (EC: IEA); GO_0006915 (EC: TAS); GO_0006919 (EC: TAS); GO_0007165 (EC: TAS, PMID: 7758105); GO_0008625 (EC: TAS, PMID: 8612133); GO_0019900 (EC: IPI, PMID: 8612133); GO_0031264 (EC: TAS, PMID: 18309324); GO_0032403 (EC: IEA); GO_0033209 (EC: TAS, PMID: 8612133); GO_0042802 (EC: IPI, PMID: 11684708); GO_0043065 (EC: TAS, PMID: 18309324); GO_0043123 (EC: IEP, PMID: 12761501); GO_0043235 (EC: IDA, PMID: 8612133); GO_0045121 (EC: IEA); GO_0051092 (EC: TAS, PMID: 18309324); GO_0051291 (EC: IEA); GO_0051798 (EC: IEA); GO_0060090 (EC: IPI, PMID: 8612133); GO_0070513 (EC: IPI, PMID: 8612133); GO_0097190 (EC: TAS); GO_0097191 (EC: IMP, PMID: 16611992); GO_0097191 (EC: TAS, PMID: 18309324); GO_2001239 (EC: TAS) PMID: 1040062; 7758105; 8565075; 8612133; 8621670; 8681376; 8702708; 8934525; 8943045; 9020361; 9082980; 9356494; 9427646; 9430227; 9560245; 9714541; 9915703; 9916731; 9916988; 10187805; 10356400; 10400625; 10544141; 10848577; 10892748; 10911999; 10980203; 11032752; 11035039; 11112409; 11112773; 11181075; 11226577; 11435712; 11479302; 11684708; 11821416; 11934887; 12045187; 12107169; 12417987; 12446787; 12477932; 12576460; 12604596; 12665801; 12753742; 12761501; 12796506; 12887920; 12911633; 14585990; 14644197; 14660619; 14702039; 14743216; 15103018; 15247912; 15310755; 15485837; 15489334; 15707590; 15761471; 16006552; 16227624; 16344560; 16603398; 16611992; 17051333; 17235653; 17540176; 17702576; 17922260; 18174230; 18198944; 18309324; 18661484; 18776134; 18939944; 18990758; 19151112; 19176810; 19287455; 19336370; 19379743; 19453261; 19573080; 19773279; 19781631; 19815541; 19854717; 20005846; 20568250; 20628368; 21068102; 21421854; 21724995; 21906983; 22099304; 22170762; 22179575; 22297296; 22510408; 22561347; 23732909; 23908590; 23955153; 23982205; 24130170; 24250222; 24374337 TNFRSF1A-associated via death domain HGNC:12030 HPRD:04610 MIM:603500 Other designations: TNFR1-associated death domain protein|tumor necrosis factor receptor type 1 associated death domain protein|tumor necrosis factor receptor type 1-associated DEATH domain protein|tumor necrosis factor receptor-1-associated protein TRADD OGG:3000008743 Bin Zhao, Yue Liu, Oliver He APO2L Apo-2L CD253 TL2 TRAIL WEB: http://www.ncbi.nlm.nih.gov/gene TNFSF10 tumor necrosis factor (ligand) superfamily, member 10 8743 3q26 20140408 9606 3 protein-coding Official from a nomenclature committee GO_0005102 (EC: TAS, PMID: 8663110); GO_0005125 (EC: IEA); GO_0005164 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10549288); GO_0005576 (EC: TAS); GO_0005615 (EC: IEA); GO_0005887 (EC: TAS, PMID: 8663110); GO_0006915 (EC: TAS); GO_0006919 (EC: TAS); GO_0006955 (EC: IEA); GO_0007165 (EC: TAS, PMID: 8663110); GO_0007267 (EC: TAS, PMID: 8777713); GO_0008584 (EC: IEA); GO_0032868 (EC: IEA); GO_0043065 (EC: IDA); GO_0043123 (EC: IEP, PMID: 12761501); GO_0043280 (EC: IDA); GO_0046872 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19199708); GO_0090200 (EC: IDA); GO_0097190 (EC: TAS); GO_2001238 (EC: IDA); GO_2001239 (EC: TAS) PMID: 8663110; 8777713; 8793301; 9082980; 9242610; 9311998; 9314565; 9325248; 9430226; 9520411; 9613612; 9754559; 9830064; 10485660; 10542098; 10549288; 10651627; 10894160; 10960444; 11022932; 11027498; 11059770; 11094155; 11095979; 11243698; 11385301; 11466352; 11553609; 11568006; 11677236; 11739488; 11781716; 11830480; 11844843; 11852102; 11877293; 11936954; 11940602; 11956660; 11964312; 11994437; 12029096; 12036888; 12082620; 12082629; 12097384; 12097388; 12118245; 12140294; 12198154; 12221720; 12351634; 12359235; 12398939; 12407100; 12414956; 12421926; 12421985; 12421989; 12429913; 12439929; 12445619; 12447876; 12477932; 12488957; 12496482; 12517970; 12532461; 12539042; 12556488; 12574346; 12576447; 12592338; 12604406; 12642868; 12663665; 12707267; 12715915; 12738989; 12761501; 12761581; 12767990; 12787570; 12808117; 12813457; 12839575; 12874246; 12907654; 12915532; 12915677; 12920112; 12927928; 12934102; 12969966; 14534533; 14601052; 14637151; 14644197; 14645705; 14647456; 14670183; 14675194; 14691451; 14715264; 14726404; 14729397; 14742697; 15030996; 15033706; 15041704; 15064358; 15077162; 15093732; 15094456; 15110168; 15137068; 15201983; 15205263; 15241475; 15251327; 15256058; 15257094; 15285015; 15286701; 15292354; 15308561; 15326479; 15339846; 15361826; 15451437; 15459016; 15459191; 15475369; 15489334; 15498932; 15509531; 15511228; 15520016; 15531913; 15539085; 15557763; 15558024; 15569667; 15607733; 15615731; 15619633; 15634757; 15637055; 15653751; 15655781; 15671071; 15681838; 15688023; 15757891; 15760909; 15767553; 15774464; 15792357; 15806163; 15809718; 15828026; 15884050; 15887227; 15916713; 15962328; 15990565; 15996036; 16007425; 16026644; 16037944; 16040132; 16041267; 16046522; 16082383; 16116625; 16166346; 16169070; 16174727; 16178278; 16180223; 16199534; 16206163; 16215673; 16226105; 16229016; 16245299; 16288714; 16289694; 16344560; 16368536; 16382051; 16436464; 16449964; 16455983; 16459719; 16478725; 16514644; 16518756; 16574768; 16607283; 16627981; 16645643; 16731632; 16751802; 16785986; 16807984; 16820090; 16831934; 16857810; 16863850; 16887991; 16941746; 16950202; 16951203; 17012835; 17070520; 17079165; 17110373; 17187253; 17195089; 17278883; 17314102; 17352408; 17356300; 17384675; 17420249; 17431115; 17431792; 17479107; 17495957; 17513605; 17525260; 17540725; 17544413; 17548900; 17553352; 17554866; 17558561; 17571163; 17579120; 17583676; 17617740; 17638906; 17683987; 17686764; 17697742; 17701086; 17702740; 17703232; 17765202; 17767167; 17803681; 17881904; 17884184; 17895594; 17900262; 17907960; 17913827; 17932312; 17938258; 17940338; 17947462; 17956986; 17982483; 17983809; 18006822; 18006832; 18006836; 18031928; 18057577; 18063697; 18089811; 18174230; 18178561; 18187663; 18202704; 18220834; 18233993; 18243765; 18266928; 18266968; 18284918; 18287563; 18314443; 18330721; 18338379; 18339897; 18341587; 18343496; 18348311; 18362888; 18362891; 18375389; 18385934; 18413764; 18424742; 18430896; 18451172; 18474604; 18483205; 18491232; 18502726; 18519235; 18522940; 18566412; 18599181; 18599488; 18640940; 18644981; 18723061; 18726983; 18772312; 18780288; 18802096; 18814951; 18834856; 18838202; 18922903; 18942021; 19050264; 19058836; 19074436; 19074831; 19106633; 19147771; 19197243; 19199708; 19203346; 19212626; 19221598; 19223770; 19236007; 19261616; 19265041; 19270498; 19281785; 19289465; 19294332; 19305384; 19309556; 19349211; 19361506; 19379558; 19385057; 19398149; 19404407; 19406930; 19407827; 19412666; 19418484; 19427028; 19435900; 19449143; 19453261; 19470406; 19476940; 19481529; 19519609; 19533303; 19540229; 19573080; 19587531; 19597472; 19629467; 19632771; 19671825; 19674787; 19690337; 19724854; 19749795; 19767219; 19773279; 19782681; 19802013; 19812265; 19854352; 19890662; 19896469; 19948942; 19954364; 19954896; 19956887; 19962668; 19962958; 19967427; 20007807; 20042498; 20119620; 20123409; 20150555; 20154087; 20189551; 20204286; 20237496; 20308427; 20334827; 20339295; 20354842; 20372797; 20379197; 20393185; 20394499; 20400979; 20417200; 20424169; 20430391; 20443055; 20560677; 20568250; 20580220; 20580868; 20628624; 20638129; 20638385; 20671119; 20734142; 20802294; 20811726; 20819778; 20838376; 20839416; 20852190; 20862322; 20961336; 20977779; 21047948; 21059290; 21064084; 21086019; 21107885; 21120579; 21125311; 21156789; 21160038; 21167276; 21183948; 21209944; 21211989; 21248767; 21255088; 21279373; 21291526; 21305500; 21308719; 21317160; 21368892; 21381010; 21426505; 21435442; 21437625; 21437722; 21454681; 21465464; 21480222; 21482133; 21483669; 21485546; 21525012; 21538027; 21554547; 21603612; 21622121; 21670755; 21695716; 21697087; 21706325; 21732015; 21760914; 21769428; 21769834; 21802664; 21822306; 21824395; 21846721; 21859711; 21864851; 21926463; 21941373; 21952139; 21988644; 21993926; 22023762; 22034880; 22072062; 22110611; 22159760; 22194780; 22202560; 22266862; 22310286; 22320196; 22322844; 22328338; 22345097; 22354145; 22384114; 22392486; 22398750; 22408249; 22449797; 22462553; 22471587; 22496450; 22542907; 22554587; 22585859; 22698523; 22719861; 22729471; 22783581; 22883061; 22898820; 22899350; 22914768; 22922789; 22948392; 23014529; 23018355; 23053497; 23071256; 23085529; 23096115; 23142077; 23228130; 23247197; 23258590; 23277172; 23290504; 23306613; 23319802; 23375756; 23384657; 23392805; 23408429; 23426404; 23428290; 23437333; 23441146; 23456625; 23457619; 23468057; 23472162; 23481489; 23492767; 23579274; 23615398; 23636231; 23667901; 23674352; 23686163; 23699397; 23699656; 23703388; 23732517; 23774624; 23792015; 23932896; 23937794; 23959437; 23974204; 23981753; 24019170; 24078627; 24100030; 24167941; 24184557; 24223304; 24299309; 24344047 tumor necrosis factor (ligand) superfamily, member 10 Ensembl:ENSG00000121858 HGNC:11925 HPRD:04670 MIM:603598 Vega:OTTHUMG00000156917 Other designations: Apo-2 ligand|TNF-related apoptosis inducing ligand TRAIL|chemokine tumor necrosis factor ligand superfamily member 10|tumor necrosis factor (ligand) family, member 10|tumor necrosis factor apoptosis-inducing ligand splice variant delta|tumor necrosis factor ligand superfamily member 10 TNFSF10 OGG:3000008800 Bin Zhao, Yue Liu, Oliver He PEX11-ALPHA PMP28 hsPEX11p WEB: http://www.ncbi.nlm.nih.gov/gene PEX11A peroxisomal biogenesis factor 11 alpha 8800 15q26.1 9606 15 Official from a nomenclature committee GO_0005515 (EC: IPI); GO_0005777 (EC: IDA, PMID: 18782765); GO_0005778 (EC: TAS); GO_0005779 (EC: IDA, PMID: 9714566); GO_0007031 (EC: IMP, PMID: 9792670); GO_0007165 (EC: IMP, PMID: 9792670); GO_0016557 (EC: IEA); GO_0016559 (EC: IDA); GO_0042803 (EC: IDA); GO_0043234 (EC: IDA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0044375 (EC: IDA); GO_0050873 (EC: IEA) PMID: 9714566; 9792670; 9922452; 10704444; 11839773; 12417726; 12477932; 14702039; 15489334; 16344560; 16567422; 17220199; 18782765; 20531392; 20826455; 21419861 peroxisomal biogenesis factor 11 alpha Ensembl:ENSG00000166821 HGNC:8852 HPRD:04843 MIM:603866 Vega:OTTHUMG00000149809 Other designations: 28 kDa peroxisomal integral membrane protein|peroxin-11A|peroxisomal biogenesis factor 11A|peroxisomal membrane protein 11A|protein PEX11 homolog alpha PEX11A OGG:3000008817 Bin Zhao, Yue Liu, Oliver He FGF-18 ZFGF5 WEB: http://www.ncbi.nlm.nih.gov/gene FGF18 fibroblast growth factor 18 8817 UNQ420/PRO856 5q34 9606 5 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0001957 (EC: IEA); GO_0001958 (EC: IEA); GO_0002063 (EC: IEA); GO_0005105 (EC: IDA, PMID: 16384934); GO_0005111 (EC: IDA, PMID: 16384934); GO_0005576 (EC: TAS); GO_0005615 (EC: TAS, PMID: 9742123); GO_0005730 (EC: IDA); GO_0007165 (EC: TAS, PMID: 9742123); GO_0007173 (EC: TAS); GO_0007267 (EC: TAS, PMID: 9742123); GO_0007399 (EC: IEA); GO_0008083 (EC: IEA); GO_0008284 (EC: IEA); GO_0008286 (EC: TAS); GO_0008543 (EC: TAS); GO_0009653 (EC: TAS, PMID: 9742123); GO_0030324 (EC: IEA); GO_0030949 (EC: IEA); GO_0032332 (EC: IEA); GO_0038095 (EC: TAS); GO_0045087 (EC: TAS); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0070374 (EC: IEA) PMID: 1697263; 9660775; 9742123; 10353607; 10579907; 10629055; 10751172; 11076863; 11124520; 11256614; 11294897; 12477932; 12975309; 15199049; 15489334; 15489336; 15749088; 16019430; 16381901; 16384934; 16597617; 16756958; 17128416; 17133345; 17360555; 17890768; 18978678; 19197348; 19453261; 19727229; 19909293; 20507176; 21048031; 21319186; 21988832; 24018557 fibroblast growth factor 18 Ensembl:ENSG00000156427 HGNC:3674 HPRD:04766 MIM:603726 Vega:OTTHUMG00000130464 FGF18 OGG:3000008829 Bin Zhao, Yue Liu, Oliver He BDCA4 CD304 NP1 NRP VEGF165R WEB: http://www.ncbi.nlm.nih.gov/gene NRP1 neuropilin 1 8829 RP11-342D11.1 10p12 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0001569 (EC: ISS); GO_0001764 (EC: ISS); GO_0001938 (EC: TAS); GO_0002042 (EC: ISS); GO_0002116 (EC: NAS, PMID: 19909241); GO_0005021 (EC: ISS); GO_0005021 (EC: NAS, PMID: 19909241); GO_0005515 (EC: IPI, PMID: 16763549); GO_0005576 (EC: IEA); GO_0005829 (EC: IDA); GO_0005883 (EC: IEA); GO_0005886 (EC: IDA); GO_0005886 (EC: TAS); GO_0007155 (EC: IEA); GO_0007165 (EC: TAS, PMID: 9288753); GO_0007267 (EC: TAS, PMID: 9288753); GO_0007411 (EC: NAS, PMID: 19909241); GO_0007411 (EC: TAS); GO_0007413 (EC: IEA); GO_0007507 (EC: IEA); GO_0008201 (EC: IEA); GO_0009611 (EC: IEA); GO_0009887 (EC: TAS, PMID: 9529250); GO_0009986 (EC: IEA); GO_0010595 (EC: TAS); GO_0014911 (EC: TAS); GO_0015026 (EC: TAS); GO_0016021 (EC: IEA); GO_0016358 (EC: IEA); GO_0017154 (EC: NAS, PMID: 19909241); GO_0019838 (EC: IPI, PMID: 9529250); GO_0019838 (EC: TAS); GO_0019955 (EC: NAS, PMID: 19909241); GO_0021636 (EC: IEA); GO_0021675 (EC: ISS); GO_0030424 (EC: ISS); GO_0030426 (EC: IEA); GO_0031290 (EC: ISS); GO_0031410 (EC: TAS); GO_0035729 (EC: IMP); GO_0035767 (EC: IMP); GO_0043025 (EC: IEA); GO_0043235 (EC: TAS); GO_0043524 (EC: IEA); GO_0046872 (EC: IEA); GO_0048008 (EC: IMP); GO_0048010 (EC: IMP); GO_0048010 (EC: TAS); GO_0048012 (EC: IMP); GO_0048842 (EC: ISS); GO_0048843 (EC: IEA); GO_0048846 (EC: ISS); GO_0050731 (EC: IMP); GO_0050918 (EC: ISS); GO_0060301 (EC: TAS); GO_0060385 (EC: ISS); GO_0060627 (EC: TAS); GO_0060666 (EC: IEA); GO_0061549 (EC: ISS); GO_0071526 (EC: NAS, PMID: 19909241); GO_0071679 (EC: ISS); GO_0090259 (EC: ISS); GO_0097102 (EC: ISS); GO_0097490 (EC: ISS); GO_0097491 (EC: ISS); GO_1902285 (EC: ISS); GO_1902336 (EC: ISS); GO_2001237 (EC: IEA) PMID: 9288753; 9331348; 9529250; 9856463; 9883722; 10196546; 10329017; 10409677; 10414980; 10520994; 10520995; 10688880; 10748121; 10842181; 11112349; 11166270; 11256614; 11333271; 11604131; 11807987; 11953749; 11976715; 11986311; 12216067; 12456642; 12477932; 12517344; 12577308; 12730958; 12883660; 14500350; 14514674; 14600159; 14760080; 15126502; 15160992; 15161648; 15166498; 15233640; 15239958; 15489334; 15522955; 15550623; 15613413; 15695515; 15920019; 15956974; 15978582; 16159877; 16330548; 16335952; 16344560; 16371354; 16377081; 16385451; 16423422; 16424390; 16513643; 16648151; 16763549; 16809290; 16847823; 16849452; 16990775; 17015762; 17017185; 17088944; 17222790; 17369353; 17369861; 17376520; 17575273; 17726369; 17891484; 17917967; 17974973; 18000534; 18065694; 18088455; 18164591; 18223683; 18231921; 18272814; 18284215; 18325345; 18403014; 18443354; 18628209; 18638267; 18704117; 18708346; 18785001; 18922901; 18974107; 18984674; 18996601; 19037249; 19054571; 19086053; 19270265; 19364973; 19460752; 19474288; 19480842; 19486891; 19499532; 19736548; 19805273; 19837659; 19857463; 19909241; 20026901; 20043119; 20053475; 20085644; 20201926; 20215856; 20363638; 20588308; 20631636; 20675371; 20950431; 20956519; 21063027; 21111525; 21139048; 21186301; 21245381; 21306301; 21338642; 21401950; 21525791; 21586748; 21653826; 21682944; 21852397; 21890473; 21897119; 21906983; 21939755; 21951945; 21978468; 21988832; 22025255; 22052678; 22134529; 22251373; 22318724; 22393126; 22627768; 22875653; 22885184; 23145112; 23175449; 23185562; 23222303; 23288161; 23297363; 23398358; 23447383; 23452854; 23455922; 23551578; 23585340; 23621014; 23685409; 23793025; 24079887 neuropilin 1 Ensembl:ENSG00000099250 HGNC:8004 HPRD:03642 MIM:602069 Vega:OTTHUMG00000019343 Other designations: neuropilin-1|transmembrane receptor|vascular endothelial cell growth factor 165 receptor NRP1 OGG:3000008837 Bin Zhao, Yue Liu, Oliver He CASH CASP8AP1 CLARP Casper FLAME FLAME-1 FLAME1 FLIP I-FLICE MRIT c-FLIP c-FLIPL c-FLIPR c-FLIPS WEB: http://www.ncbi.nlm.nih.gov/gene CFLAR CASP8 and FADD-like apoptosis regulator 8837 2q33-q34 9606 2 Official from a nomenclature committee GO_0002020 (EC: IPI, PMID: 9208847); GO_0004197 (EC: IKR, Qualifier: NOT); GO_0005515 (EC: IPI, PMID: 11741985); GO_0005737 (EC: IDA, PMID: 18073330); GO_0005829 (EC: TAS); GO_0006915 (EC: IMP); GO_0006915 (EC: TAS); GO_0007519 (EC: ISS); GO_0008047 (EC: IDA, PMID: 9208847); GO_0014732 (EC: ISS); GO_0014842 (EC: ISS); GO_0014866 (EC: ISS); GO_0016032 (EC: IEA); GO_0031264 (EC: IDA); GO_0031265 (EC: IEA); GO_0035877 (EC: IBA); GO_0043066 (EC: IEA); GO_0043085 (EC: IDA, PMID: 9208847); GO_0043123 (EC: IEP, PMID: 12761501); GO_0043403 (EC: ISS); GO_0051092 (EC: ISS); GO_0060544 (EC: IDA); GO_0097190 (EC: TAS); GO_0097342 (EC: IDA); GO_1901740 (EC: ISS); GO_1902042 (EC: IMP, PMID: 18202225); GO_2001237 (EC: IDA, PMID: 9208847); GO_2001237 (EC: IMP); GO_2001239 (EC: TAS) PMID: 8889548; 9208847; 9211860; 9217161; 9219695; 9228018; 9289491; 9325248; 9326610; 9380701; 9560245; 9575181; 9880531; 9990034; 10069390; 10200473; 10227994; 10329646; 10837247; 11002417; 11161814; 11193041; 11741985; 11830587; 11877293; 11940602; 11965497; 12031968; 12060768; 12097160; 12115181; 12215447; 12220669; 12393527; 12407100; 12432255; 12477932; 12477972; 12496285; 12496481; 12496482; 12552004; 12556488; 12574377; 12592338; 12716387; 12746452; 12761501; 12820373; 12887920; 13679070; 14562111; 14578361; 14637155; 14662022; 14759258; 15024054; 15078899; 15096587; 15183989; 15258564; 15273717; 15280356; 15297424; 15304499; 15334061; 15354734; 15459191; 15485835; 15489334; 15540114; 15557152; 15644494; 15653751; 15686714; 15701649; 15701651; 15722350; 15731171; 15760909; 15761846; 15815586; 15832422; 15843523; 15864316; 15886205; 15899875; 15917295; 15956881; 16014121; 16052233; 16052516; 16077198; 16211288; 16246840; 16247474; 16298825; 16304056; 16403915; 16436054; 16441226; 16472594; 16537561; 16611896; 16712791; 16720717; 16740746; 16901543; 17003335; 17047155; 17056549; 17070520; 17106251; 17110930; 17159907; 17272514; 17353931; 17376892; 17440816; 17441421; 17450141; 17513603; 17559541; 17573774; 17581950; 17638906; 17646662; 17659339; 17697742; 17726263; 17762208; 17912957; 17922291; 17932249; 17982483; 17988665; 18073330; 18084329; 18189268; 18202225; 18243739; 18257744; 18264131; 18314443; 18339897; 18391984; 18398344; 18414015; 18509086; 18559494; 18593367; 18603835; 18726983; 18767116; 18820704; 18823309; 18838202; 18840411; 18976975; 19090833; 19109151; 19115040; 19161534; 19177145; 19203346; 19223508; 19243385; 19249545; 19282655; 19321593; 19339247; 19343040; 19363595; 19372246; 19398149; 19409438; 19433309; 19439735; 19476635; 19543235; 19573080; 19604093; 19710364; 19728335; 19734124; 19773279; 19798106; 19802016; 19808964; 19816511; 19838173; 19890350; 19896469; 19906927; 19913121; 19949310; 19956887; 20016063; 20087343; 20218968; 20224598; 20227749; 20335528; 20372864; 20449949; 20453000; 20484045; 20508645; 20561424; 20568250; 20595005; 20628086; 20628624; 20689807; 20696707; 20802294; 20812013; 20876284; 20876774; 20882347; 20975036; 21048031; 21071136; 21107885; 21153369; 21307400; 21324892; 21394196; 21403465; 21435442; 21454681; 21474069; 21480219; 21483669; 21525012; 21562857; 21638304; 21691254; 21737329; 21803845; 21822306; 21856935; 21868755; 21890473; 21912376; 21988832; 22027693; 22072062; 22126763; 22190004; 22219201; 22266862; 22288650; 22322857; 22345097; 22393362; 22504646; 22683265; 22753273; 22781394; 22842544; 22864571; 22884570; 22948392; 23028678; 23142077; 23167276; 23230268; 23235765; 23247197; 23255321; 23256568; 23319802; 23322903; 23371318; 23483900; 23518915; 23519470; 23615398; 23696271; 23853530 CASP8 and FADD-like apoptosis regulator Ensembl:ENSG00000003402 HGNC:1876 HPRD:04671 MIM:603599 Vega:OTTHUMG00000132819 Other designations: FADD-like anti-apoptotic molecule|FADD-like antiapoptotic molecule 1|MACH-related inducer of toxicity|caspase homolog|caspase-eight-related protein|caspase-like apoptosis regulatory protein|caspase-related inducer of apoptosis|cellular FLICE-like inhibitory protein|inhibitor of FLICE|usurpin beta CFLAR OGG:3000008851 Bin Zhao, Yue Liu, Oliver He CDK5P35 CDK5R NCK5A p23 p25 p35 p35nck5a WEB: http://www.ncbi.nlm.nih.gov/gene CDK5R1 cyclin-dependent kinase 5, regulatory subunit 1 (p35) 8851 17q11.2 9606 17 Official from a nomenclature committee GO_0000079 (EC: TAS, PMID: 7592934); GO_0001764 (EC: ISS); GO_0004672 (EC: TAS, PMID: 7592934); GO_0004693 (EC: IEA); GO_0005509 (EC: ISS); GO_0005515 (EC: IPI, PMID: 10721722); GO_0005634 (EC: ISS); GO_0005737 (EC: ISS); GO_0005829 (EC: TAS); GO_0005886 (EC: IEA); GO_0007158 (EC: ISS); GO_0007213 (EC: ISS); GO_0007411 (EC: ISS); GO_0007411 (EC: TAS); GO_0007413 (EC: ISS); GO_0007420 (EC: ISS); GO_0007420 (EC: NAS, PMID: 10915792); GO_0008283 (EC: TAS, PMID: 8090221); GO_0009790 (EC: ISS); GO_0014069 (EC: ISS); GO_0016020 (EC: ISS); GO_0016301 (EC: ISS); GO_0016533 (EC: IEA); GO_0016534 (EC: IEA); GO_0018105 (EC: IDA, PMID: 12832520); GO_0018107 (EC: IDA, PMID: 12832520); GO_0019901 (EC: IPI, PMID: 12832520); GO_0021549 (EC: IEA); GO_0021722 (EC: IEA); GO_0021766 (EC: IEA); GO_0021819 (EC: IEA); GO_0030182 (EC: ISS); GO_0030424 (EC: ISS); GO_0030425 (EC: ISS); GO_0030426 (EC: ISS); GO_0030517 (EC: IEA); GO_0031175 (EC: ISS); GO_0031594 (EC: ISS); GO_0032956 (EC: IEA); GO_0033136 (EC: IEA); GO_0035235 (EC: ISS); GO_0043025 (EC: ISS); GO_0043197 (EC: ISS); GO_0043292 (EC: ISS); GO_0043525 (EC: ISS); GO_0043539 (EC: IDA, PMID: 12832520); GO_0043539 (EC: ISS); GO_0045296 (EC: ISS); GO_0045664 (EC: NAS, PMID: 10721722); GO_0045892 (EC: IMP); GO_0046875 (EC: IEA); GO_0048013 (EC: ISS); GO_0048471 (EC: IDA, PMID: 12832520); GO_0061001 (EC: ISS); GO_0070507 (EC: IEA); GO_0090314 (EC: IEA) PMID: 7556643; 7592934; 8090221; 9010203; 9038181; 9933594; 10604467; 10721722; 10753743; 10830966; 10915792; 11113134; 11168528; 11389014; 11583627; 11604394; 11741927; 11784720; 11882646; 12037672; 12084709; 12223541; 12226093; 12230554; 12477932; 12491158; 12688339; 12826674; 12832492; 12832520; 12859671; 14521924; 14702039; 14976144; 15013773; 15123618; 15175076; 15342635; 15489224; 15489334; 15492003; 15536496; 15689152; 15741232; 15917097; 16189514; 16407256; 16425041; 16678793; 17036052; 17060323; 17121855; 17207965; 17491008; 17493033; 17496813; 17591690; 17762160; 18053171; 18247371; 18325333; 18829967; 19081376; 19154537; 19638632; 19874574; 19913121; 19953087; 20097924; 20354813; 20518484; 20618441; 20628086; 21130530; 21220307; 21544067; 21625387; 21772061; 21832049; 22654103; 22964075; 23151508; 23455922; 23602568; 24085300 cyclin-dependent kinase 5, regulatory subunit 1 (p35) Ensembl:ENSG00000176749 HGNC:1775 HPRD:04586 MIM:603460 Vega:OTTHUMG00000132814 Other designations: CDK5 activator 1|TPKII regulatory subunit|cyclin-dependent kinase 5 activator 1|cyclin-dependent kinase 5 regulatory subunit 1|neuronal CDK5 activator|regulatory partner for CDK5 kinase|tau protein kinase II 23kDa subunit CDK5R1 OGG:3000008856 PXR nuclear receptor subfamily 1 group I member 2 orphan nuclear receptor PXR pregnane X nuclear receptor variant 2 pregnane X receptor rphan nuclear receptor PAR1 NR1I2 OGG:3000008870 Bin Zhao, Yue Liu, Oliver He DIF-2 DIF2 GLY96 IEX-1 IEX-1L IEX1 PRG1 WEB: http://www.ncbi.nlm.nih.gov/gene IER3 immediate early response 3 8870 DADB-118P11.5 6p21.3 9606 6 Official from a nomenclature committee GO_0001562 (EC: IEA); GO_0003085 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15451437); GO_0005634 (EC: IDA); GO_0006282 (EC: IEA); GO_0006915 (EC: TAS, PMID: 9196025); GO_0007095 (EC: IEA); GO_0008630 (EC: IEA); GO_0009653 (EC: TAS, PMID: 9196025); GO_0016021 (EC: IEA); GO_0043066 (EC: IEA); GO_0045732 (EC: IEA); GO_0045820 (EC: IEA); GO_0046822 (EC: IEA); GO_0050728 (EC: IEA); GO_1901029 (EC: IEA); GO_2000377 (EC: IEA); GO_2001020 (EC: IMP) PMID: 8125298; 8603392; 8653710; 9196025; 9588170; 9703517; 9781666; 9791001; 9878538; 10448082; 11455449; 11782530; 11844788; 11910304; 12032839; 12356731; 12477932; 12510147; 12682234; 12743274; 12761504; 15120418; 15451437; 15489334; 15767410; 15781630; 15855159; 16344560; 16456541; 16567805; 16702430; 16960879; 16973576; 17704804; 18026799; 18482256; 18564103; 19152102; 19285955; 19690192; 19773435; 19837266; 19851445; 20587610; 20713914; 20848476; 20934684; 21112119; 21250941; 21518511; 21832049; 21906983; 22085302; 23455636; 24311782 immediate early response 3 Ensembl:ENSG00000137331 HGNC:5392 HPRD:04295 MIM:602996 Vega:OTTHUMG00000031265 Other designations: PACAP-responsive gene 1 protein|anti-death protein|differentiation-dependent gene 2 protein|expressed in pancreatic carcinoma|gly96, mouse, homolog of|immediate early protein GLY96|immediate early response 3 protein|immediately early gene X-1|protein DIF-2|radiation-inducible immediate-early gene IEX-1 IER3 OGG:3000008876 Bin Zhao, Yue Liu, Oliver He HDLCQ8 Tiff66 WEB: http://www.ncbi.nlm.nih.gov/gene VNN1 vanin 1 8876 6q23-q24 9606 6 Official from a nomenclature committee GO_0002526 (EC: ISS, PMID: 14966568); GO_0002544 (EC: ISS, PMID: 14966568); GO_0005886 (EC: IEA); GO_0006928 (EC: TAS, PMID: 9790769); GO_0006954 (EC: ISS, PMID: 15282320); GO_0006979 (EC: TAS, PMID: 17145956); GO_0015939 (EC: IDA, PMID: 11491533); GO_0016021 (EC: TAS, PMID: 17145956); GO_0016337 (EC: ISS, PMID: 11491533); GO_0017159 (EC: IDA, PMID: 11491533); GO_0031225 (EC: IEA); GO_0033089 (EC: ISS, PMID: 11491533); GO_0034235 (EC: TAS, PMID: 17145956); GO_0045087 (EC: ISS, PMID: 14966568); GO_1902176 (EC: ISS, PMID: 15282320) PMID: 8934567; 9790769; 10567687; 11491533; 12477932; 14574404; 14702039; 14966568; 15084671; 15282320; 15489334; 16335952; 17145956; 17312006; 18043751; 19322213; 20571492; 20641033; 21325602; 21544065; 21550219; 21907259; 23185446; 23978960; 24140347 vanin 1 Ensembl:ENSG00000112299 HGNC:12705 HPRD:04651 MIM:603570 Vega:OTTHUMG00000015587 Other designations: pantetheinase|pantetheine hydrolase|vanin-1|vannin 1|vascular non-inflammatory molecule 1 VNN1 OGG:3000008879 Bin Zhao, Yue Liu, Oliver He S1PL SPL WEB: http://www.ncbi.nlm.nih.gov/gene SGPL1 sphingosine-1-phosphate lyase 1 8879 10q21 9606 10 Official from a nomenclature committee GO_0001553 (EC: IEA); GO_0001570 (EC: IEA); GO_0001822 (EC: IEA); GO_0005515 (EC: IPI); GO_0005783 (EC: IDA, PMID: 14570870); GO_0005789 (EC: TAS); GO_0006665 (EC: TAS); GO_0006672 (EC: IDA, PMID: 14570870); GO_0007283 (EC: IEA); GO_0008117 (EC: IDA, PMID: 14570870); GO_0008117 (EC: NAS, PMID: 11018465); GO_0008209 (EC: IEA); GO_0008210 (EC: IEA); GO_0009791 (EC: IEA); GO_0010761 (EC: IEA); GO_0016831 (EC: IEA); GO_0019752 (EC: IEA); GO_0030097 (EC: IEA); GO_0030148 (EC: TAS); GO_0030149 (EC: NAS, PMID: 11018465); GO_0030170 (EC: IEA); GO_0030176 (EC: NAS, PMID: 11018465); GO_0033327 (EC: IEA); GO_0040014 (EC: IEA); GO_0044281 (EC: TAS); GO_0048008 (EC: IEA); GO_0048705 (EC: IEA); GO_0060021 (EC: IEA); GO_0060325 (EC: IEA); GO_0097194 (EC: IDA, PMID: 14570870) PMID: 2061324; 9464245; 10574462; 11018465; 12477932; 14570870; 14702039; 15342556; 15489334; 16385451; 16777052; 17090686; 17373700; 18029348; 18172856; 19119317; 19322201; 20519401; 21139048; 21184844; 21304987; 21368890; 21565611; 21890473; 21903422; 21906983; 21963094; 22190034; 22784711; 23000965; 23455922; 23956138; 24255178 sphingosine-1-phosphate lyase 1 Ensembl:ENSG00000166224 HGNC:10817 HPRD:07224 MIM:603729 Vega:OTTHUMG00000018421 Other designations: SP-lyase 1|SPL 1|hSPL|sphingosine-1-phosphate aldolase SGPL1 OGG:3000008884 Bin Zhao, Yue Liu, Oliver He SMVT WEB: http://www.ncbi.nlm.nih.gov/gene SLC5A6 solute carrier family 5 (sodium/multivitamin and iodide cotransporter), member 6 8884 2p23 9606 2 Official from a nomenclature committee GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID: 9516450); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0006768 (EC: TAS); GO_0006810 (EC: TAS, PMID: 9516450); GO_0008523 (EC: IEA); GO_0012506 (EC: IEA); GO_0015878 (EC: IEA); GO_0015887 (EC: IEA); GO_0015939 (EC: TAS); GO_0016020 (EC: TAS, PMID: 9516450); GO_0031526 (EC: IEA); GO_0044281 (EC: TAS); GO_0055085 (EC: TAS) PMID: 9516450; 10329687; 10334869; 11834205; 11955628; 12477932; 12646417; 14702039; 15123239; 15561972; 16303743; 16344560; 16749865; 16751776; 16959947; 17135299; 17904341; 19211916; 19898482; 20962270; 20980265; 21139048; 21183659; 21570947; 21890473; 21906983; 21963094; 21988832; 22015582; 22304562; 22732670; 22927035; 23000965; 23142496 solute carrier family 5 (sodium/multivitamin and iodide cotransporter), member 6 Ensembl:ENSG00000138074 HGNC:11041 HPRD:04934 MIM:604024 Vega:OTTHUMG00000097075 Other designations: Na(+)-dependent multivitamin transporter|Na+-dependent multivitamin transporter|sodium-dependent multivitamin transporter|solute carrier family 5 (sodium-dependent vitamin transporter), member 6|solute carrier family 5 member 6 SLC5A6 OGG:3000008890 Bin Zhao, Yue Liu, Oliver He EIF-2B EIF2B EIF2Bdelta WEB: http://www.ncbi.nlm.nih.gov/gene EIF2B4 eukaryotic translation initiation factor 2B, subunit 4 delta, 67kDa 8890 2p23.3 9606 2 GO_0001541 (EC: IMP, PMID:15507143); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:16289705); GO_0005085 (EC: IDA, Qualifier: contributes_to, PMID:11323413); GO_0005085 (EC: IMP, Qualifier: contributes_to, PMID:15054402); GO_0005515 (EC: IPI, PMID:15060152); GO_0005737 (EC: IDA, PMID:11323413); GO_0005829 (EC: TAS); GO_0005851 (EC: IDA, PMID:11323413); GO_0006412 (EC: TAS); GO_0006413 (EC: IDA, PMID:16289705); GO_0006413 (EC: TAS); GO_0006417 (EC: NAS, PMID:12556349); GO_0006446 (EC: IBA); GO_0009408 (EC: ISS); GO_0009408 (EC: TAS, PMID:12499492); GO_0009749 (EC: ISS); GO_0010467 (EC: TAS); GO_0014003 (EC: IMP, PMID:15217090); GO_0019509 (EC: IBA, Qualifier: NOT); GO_0031369 (EC: ISS); GO_0032057 (EC: ISS); GO_0042552 (EC: IMP, PMID:14566705); GO_0043087 (EC: IDA, PMID:11323413); GO_0043087 (EC: IMP, PMID:15054402); GO_0043434 (EC: ISS); GO_0044267 (EC: TAS); GO_0045947 (EC: IBA); GO_0046523 (EC: IBA, Qualifier: NOT); GO_0051716 (EC: IDA, PMID:8626696) PMID:7982969; 8626696; 8887689; 8929216; 9446619; 10805739; 10858531; 10931946; 11323413; 11835386; 12477932; 12499492; 12556349; 12707859; 14566705; 15054402; 15060152; 15217090; 15489334; 15507143; 16288713; 16289705; 18005052; 18061208; 18160716; 18263758; 18330844; 18539998; 18632786; 19158808; 19460752; 20016818; 20301435; 20434207; 20532202; 20709751; 20734064; 21139048; 21503715; 21890473; 21906983; 22505724; 22737209; 22939629; 23000965; 23382691 eukaryotic translation initiation factor 2B, subunit 4 delta, 67kDa Ensembl:ENSG00000115211 HGNC:3260 HPRD:09459 MIM:606687 Vega:OTTHUMG00000151927 Other designations: eIF-2B GDP-GTP exchange factor subunit delta|eukaryotic translation initiation factor 2B subunit 4 delta|translation initiation factor eIF-2B subunit delta|translation initiation factor eIF-2b delta subunit EIF2B4 OGG:3000008891 Bin Zhao, Yue Liu, Oliver He EIF-2B EIF2Bgamma WEB: http://www.ncbi.nlm.nih.gov/gene EIF2B3 eukaryotic translation initiation factor 2B, subunit 3 gamma, 58kDa 8891 RP5-882O7.2 1p34.1 9606 1 GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:10900014); GO_0005085 (EC: IDA, Qualifier: contributes_to, PMID:11323413); GO_0005085 (EC: IMP, Qualifier: contributes_to, PMID:15054402); GO_0005515 (EC: IPI, PMID:15060152); GO_0005737 (EC: IDA, PMID:11323413); GO_0005829 (EC: TAS); GO_0005851 (EC: IDA, PMID:11323413); GO_0006412 (EC: TAS); GO_0006413 (EC: IDA, PMID:10900014); GO_0006413 (EC: TAS); GO_0008135 (EC: IDA, Qualifier: contributes_to, PMID:10900014); GO_0009408 (EC: ISS); GO_0009408 (EC: TAS, PMID:12499492); GO_0009749 (EC: ISS); GO_0010467 (EC: TAS); GO_0014003 (EC: IMP, PMID:15217090); GO_0016779 (EC: IEA); GO_0032057 (EC: ISS); GO_0043087 (EC: IDA, PMID:11323413); GO_0043087 (EC: IMP, PMID:15054402); GO_0043434 (EC: ISS); GO_0044267 (EC: TAS); GO_0051716 (EC: IDA, PMID:8626696) PMID:8626696; 8889549; 10737800; 10805739; 10858531; 10900014; 11076863; 11230166; 11323413; 11835386; 12477932; 12499492; 12707859; 14702039; 15054402; 15060152; 15217090; 15489334; 15489336; 16169070; 16288713; 16289705; 16344560; 16381901; 16710414; 17353931; 18263758; 18632786; 20301435; 20379614; 21139048; 21484434; 21890473; 21906983; 21963094; 21987572; 22268729; 22312164; 22863883; 22939629; 23000965; 23956138 eukaryotic translation initiation factor 2B, subunit 3 gamma, 58kDa Ensembl:ENSG00000070785 HGNC:3259 HPRD:09379 MIM:606273 Vega:OTTHUMG00000008585 Other designations: eIF-2B GDP-GTP exchange factor subunit gamma|translation initiation factor eIF-2B subunit gamma EIF2B3 OGG:3000008892 Bin Zhao, Yue Liu, Oliver He EIF-2Bbeta EIF2B WEB: http://www.ncbi.nlm.nih.gov/gene EIF2B2 eukaryotic translation initiation factor 2B, subunit 2 beta, 39kDa 8892 14q24.3 9606 14 GO_0001541 (EC: IMP, PMID:15507143); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:16289705); GO_0005085 (EC: IDA, Qualifier: contributes_to, PMID:11323413); GO_0005085 (EC: IMP, Qualifier: contributes_to, PMID:15054402); GO_0005515 (EC: IPI, PMID:15060152); GO_0005524 (EC: IDA, PMID:11323413); GO_0005525 (EC: IDA, PMID:11323413); GO_0005737 (EC: IDA, PMID:11323413); GO_0005829 (EC: TAS); GO_0005851 (EC: IDA, PMID:11323413); GO_0006412 (EC: TAS); GO_0006413 (EC: IDA, PMID:16289705); GO_0006413 (EC: TAS); GO_0006446 (EC: IBA); GO_0006446 (EC: TAS, PMID:15060152); GO_0007417 (EC: IMP, PMID:15776425); GO_0009408 (EC: ISS); GO_0009408 (EC: TAS, PMID:12499492); GO_0009749 (EC: ISS); GO_0010467 (EC: TAS); GO_0014003 (EC: IMP, PMID:15217090); GO_0019509 (EC: IBA, Qualifier: NOT); GO_0042552 (EC: IMP, PMID:14566705); GO_0043087 (EC: IDA, PMID:11323413); GO_0043087 (EC: IMP, PMID:15054402); GO_0043434 (EC: ISS); GO_0044267 (EC: TAS); GO_0046523 (EC: IBA, Qualifier: NOT); GO_0051716 (EC: IDA, PMID:8626696) PMID:7596406; 8619474; 8626696; 8887689; 9110174; 9446619; 10805739; 10858531; 11323413; 11704758; 11959995; 12477932; 12499492; 12508121; 12707859; 14566705; 14993275; 15054402; 15060152; 15217090; 15489334; 15507143; 15776425; 16169070; 16225457; 16289705; 17878805; 18029348; 18263758; 18632786; 19913121; 20301435; 20434207; 20628086; 20734064; 21139048; 21795329; 21832049; 21890473; 21988832; 22053931; 22285377; 22729508; 22863883; 22939629; 23000965; 23956138 eukaryotic translation initiation factor 2B, subunit 2 beta, 39kDa Ensembl:ENSG00000119718 HGNC:3258 HPRD:05923 MIM:606454 Vega:OTTHUMG00000171764 Other designations: S20I15|S20III15|eIF-2B GDP-GTP exchange factor subunit beta|translation initiation factor eIF-2B subunit beta EIF2B2 OGG:3000008893 Bin Zhao, Yue Liu, Oliver He CACH CLE EIF-2B EIF2Bepsilon LVWM WEB: http://www.ncbi.nlm.nih.gov/gene EIF2B5 eukaryotic translation initiation factor 2B, subunit 5 epsilon, 82kDa 8893 3q27.1 9606 3 GO_0001541 (EC: IMP, PMID:15507143); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:16289705); GO_0003743 (EC: NAS, PMID:8688466); GO_0005085 (EC: IDA, Qualifier: contributes_to, PMID:11323413); GO_0005085 (EC: IMP, PMID:15054402); GO_0005085 (EC: ISS); GO_0005515 (EC: IPI, PMID:15060152); GO_0005634 (EC: ISS); GO_0005737 (EC: IDA, PMID:11323413); GO_0005829 (EC: TAS); GO_0005851 (EC: IDA, PMID:11323413); GO_0006412 (EC: TAS); GO_0006413 (EC: IDA, PMID:16289705); GO_0006413 (EC: TAS); GO_0009408 (EC: IMP, PMID:15723074); GO_0009408 (EC: ISS); GO_0009408 (EC: TAS, PMID:12499492); GO_0009749 (EC: ISS); GO_0010467 (EC: TAS); GO_0014002 (EC: IMP, PMID:15723074); GO_0014003 (EC: IMP, PMID:15217090); GO_0031369 (EC: ISS); GO_0032057 (EC: ISS); GO_0034976 (EC: IMP, PMID:16041584); GO_0035690 (EC: IDA, PMID:8626696); GO_0042552 (EC: IMP, PMID:14566705); GO_0043087 (EC: IDA, PMID:11323413); GO_0043087 (EC: IMP, PMID:15054402); GO_0043087 (EC: ISS); GO_0043434 (EC: ISS); GO_0044267 (EC: TAS); GO_0045948 (EC: ISS); GO_0048708 (EC: IMP, PMID:15723074) PMID:8626696; 8688466; 9446619; 9468292; 10441579; 10805739; 10858531; 11323413; 11500362; 11704758; 12133000; 12325082; 12477932; 12499492; 12707859; 14566705; 14572143; 14702039; 14993275; 15054402; 15060152; 15217090; 15302935; 15489334; 15507143; 15723074; 16041584; 16097034; 16289705; 16730941; 17081983; 17353931; 17439913; 17646634; 18263758; 18294360; 18562513; 18565837; 18632786; 18854154; 19913121; 20301435; 20628086; 20734064; 20975056; 21204011; 21307862; 21503715; 21832049; 21890473; 21906983; 22472876; 22939629; 23956138 eukaryotic translation initiation factor 2B, subunit 5 epsilon, 82kDa Ensembl:ENSG00000145191 HGNC:3261 HPRD:04898 MIM:603945 Vega:OTTHUMG00000156840 Other designations: eIF-2B GDP-GTP exchange factor subunit epsilon|translation initiation factor eIF-2B subunit epsilon EIF2B5 OGG:3000008894 Bin Zhao, Yue Liu, Oliver He EIF2 EIF2B EIF2beta PPP1R67 eIF-2-beta WEB: http://www.ncbi.nlm.nih.gov/gene EIF2S2 eukaryotic translation initiation factor 2, subunit 2 beta, 38kDa 8894 20q11.2 9606 20 GO_0001701 (EC: IEA); GO_0002176 (EC: IEA); GO_0003723 (EC: TAS, PMID:3044606); GO_0003743 (EC: IDA, PMID:16289705); GO_0005515 (EC: IPI, PMID:16288713); GO_0005829 (EC: TAS); GO_0005850 (EC: TAS, PMID:3044606); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0008135 (EC: TAS, PMID:10805737); GO_0008584 (EC: IEA); GO_0010467 (EC: TAS); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0046872 (EC: IEA) PMID:1104615; 3044606; 8024572; 9079663; 9395514; 9442054; 9446619; 9933616; 10620360; 10648795; 10805737; 10805739; 11092890; 11739746; 11780052; 11959995; 12477932; 12588972; 12901717; 15489334; 15635413; 16169070; 16288713; 16289705; 16932749; 17081983; 18423202; 18639529; 18781797; 18850631; 20000738; 20434207; 20972266; 21139048; 21145461; 21832049; 21890473; 21906983; 21907836; 22113938; 22174317; 22678362; 22813744; 22863883; 22939629; 22976474; 22990118; 23000965; 23455922; 24250222; 24457600 eukaryotic translation initiation factor 2, subunit 2 beta, 38kDa Ensembl:ENSG00000125977 HGNC:3266 HPRD:04882 MIM:603908 Vega:OTTHUMG00000032287 Other designations: eukaryotic translation initiation factor 2 subunit 2|eukaryotic translation initiation factor 2 subunit beta|protein phosphatase 1, regulatory subunit 67 EIF2S2 OGG:3000008935 Bin Zhao, Yue Liu, Oliver He PRAP RA70 SAPS SCAP2 SKAP-HOM SKAP55R WEB: http://www.ncbi.nlm.nih.gov/gene SKAP2 src kinase associated phosphoprotein 2 8935 7p15.2 9606 7 Official from a nomenclature committee GO_0005070 (EC: TAS, PMID: 9671755); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA, PMID: 11390434); GO_0006461 (EC: TAS, PMID: 9671755); GO_0007165 (EC: TAS, PMID: 9837776); GO_0008285 (EC: IEA); GO_0009967 (EC: TAS, PMID: 9671755); GO_0042113 (EC: IEA) PMID: 8125298; 9671755; 9755858; 9837776; 10469599; 10527689; 10942756; 11063873; 11301322; 11390434; 12477932; 12690205; 12853948; 12893833; 15166227; 15489334; 15761153; 17081983; 17952125; 19380743; 19430480; 19807924; 19913121; 20378605; 20628086; 21719704; 21832049; 21906983; 22745667; 23128233; 23161539 src kinase associated phosphoprotein 2 Ensembl:ENSG00000005020 HGNC:15687 HPRD:05558 MIM:605215 Vega:OTTHUMG00000023495 Other designations: Fyn-associated phosphoprotein SKAP55 homologue|Pyk2/RAFTK-associated protein|SKAP-55HOM|SKAP55 homolog|retinoic acid-induced protein 70|src family associated phosphoprotein 2|src family-associated phosphoprotein 2|src kinase-associated phosphoprotein 2|src kinase-associated phosphoprotein 55-related protein|src kinase-associated phosphoprotein of 55-related protein|src-associated adapter protein with PH and SH3 domains|src-associated adaptor protein SKAP2 OGG:3000009068 Bin Zhao, Yue Liu, Oliver He ANG3 ANGPT3 ARP1 AngY UNQ162 dJ595C2.2 WEB: http://www.ncbi.nlm.nih.gov/gene ANGPTL1 angiopoietin-like 1 9068 PSEC0154 1q25.2 9606 1 GO_0005102 (EC: IEA); GO_0005615 (EC: IDA, PMID:10025962); GO_0007169 (EC: IEA); GO_0070062 (EC: IDA, PMID:19199708) PMID:8125298; 8889548; 9286704; 10025962; 10051567; 10318855; 10473614; 12477932; 12624729; 15284220; 15489334; 15542434; 15940350; 15950186; 16303743; 16710414; 18182823; 18644593; 19199708; 20819778; 23434592 angiopoietin-like 1 Ensembl:ENSG00000116194 HGNC:489 HPRD:04851 MIM:603874 Vega:OTTHUMG00000035075 Other designations: ANG-3|angioarrestin|angiopoietin 3|angiopoietin Y1|angiopoietin-3|angiopoietin-like protein 1|angiopoietin-related protein 1|dJ595C2.2 (angiopoietin Y1) ANGPTL1 OGG:3000009086 Bin Zhao, Yue Liu, Oliver He eIF-4C WEB: http://www.ncbi.nlm.nih.gov/gene EIF1AY eukaryotic translation initiation factor 1A, Y-linked 9086 Yq11.223 9606 Y GO_0003743 (EC: IEA); GO_0005515 (EC: IPI, PMID:12569173) PMID:9381176; 10747295; 12477932; 12569173; 12815422; 14660691; 15064832; 15252450; 15342556; 15489334; 15613541; 16713569; 16936303; 18029348; 19605777; 20031959; 20823116; 21139048; 21145461; 21890473; 21906983; 22158087; 22365286; 22505724; 23000965; 23602568; 24319994 eukaryotic translation initiation factor 1A, Y-linked Ensembl:ENSG00000198692 HGNC:3252 HPRD:02455 MIM:400014 Vega:OTTHUMG00000036544 Other designations: eIF-1A Y isoform|eukaryotic translation initiation factor 1A, Y chromosome|eukaryotic translation initiation factor 1A, Y-chromosomal|eukaryotic translation initiation factor 4C EIF1AY OGG:3000009133 Bin Zhao, Yue Liu, Oliver He HsT17299 WEB: http://www.ncbi.nlm.nih.gov/gene CCNB2 cyclin B2 9133 15q22.2 9606 15 Official from a nomenclature committee GO_0000079 (EC: IEA); GO_0000086 (EC: TAS); GO_0000278 (EC: TAS); GO_0001701 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15232106); GO_0005654 (EC: TAS); GO_0005813 (EC: IDA); GO_0005829 (EC: TAS); GO_0007067 (EC: IEA); GO_0007077 (EC: TAS); GO_0015630 (EC: IDA); GO_0016020 (EC: IEA); GO_0019901 (EC: IEA); GO_0040007 (EC: IEA); GO_0043029 (EC: IEA); GO_0048538 (EC: IEA); GO_0051726 (EC: TAS) PMID: 1717476; 7474080; 7474100; 7494303; 7666531; 7737117; 8070405; 8125298; 9094673; 9356466; 9520381; 9539739; 9560267; 9926943; 10958988; 11076863; 11230166; 11256614; 11531413; 11878934; 11960377; 12477932; 12482752; 12727876; 14702039; 14718574; 15232106; 15489334; 15489336; 16381901; 17289878; 17388661; 17533373; 17549666; 18591933; 18692784; 19223528; 19454010; 19664331; 19738611; 19786724; 20360068; 20660152; 20972266; 21139048; 21161946; 21890473; 22916037; 22939629; 23282137; 23455922; 23602568 cyclin B2 Ensembl:ENSG00000157456 HGNC:1580 HPRD:04131 MIM:602755 Vega:OTTHUMG00000132715 Other designations: G2/mitotic-specific cyclin-B2 CCNB2 gene OGG:3000009144 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene SYNGR2 synaptogyrin 2 9144 UNQ352/PRO615 17q25.3 9606 17 Official from a nomenclature committee GO_0006605 (EC: IEA); GO_0008021 (EC: IEA); GO_0016021 (EC: NAS, PMID: 9760194); GO_0070062 (EC: IDA) PMID: 9446595; 9760194; 12477932; 12975309; 15489334; 17255364; 21139048; 21890473; 23000965 synaptogyrin 2 Other designations: cellugyrin|synaptogyrin-2 SYNGR2 OGG:3000009159 Bin Zhao, Yue Liu, Oliver He LPC PC7 PC8 SPC7 WEB: http://www.ncbi.nlm.nih.gov/gene PCSK7 proprotein convertase subtilisin/kexin type 7 9159 11q23-q24 9606 11 Official from a nomenclature committee GO_0004252 (EC: IBA); GO_0016486 (EC: NAS, PMID: 9341152); GO_0030173 (EC: IDA, PMID: 9341152) PMID: 7819324; 8125298; 8564950; 8615762; 8940009; 8995623; 9094426; 9341152; 9521771; 9820811; 10037747; 10050053; 10362256; 10409610; 10452538; 10715106; 10964928; 11051545; 11063880; 11104692; 11380615; 11723118; 12071862; 12084516; 12354117; 12477932; 14702039; 17242158; 18343183; 19322201; 20164418; 21075846; 21149283; 21209099; 21805236; 21805237; 21943158; 22294700; 22679642; 23390091; 23686857; 23775089 proprotein convertase subtilisin/kexin type 7 HGNC:8748 HPRD:05339 MIM:604872 Other designations: lymphoma proprotein convertase|prohormone convertase 7|prohormone convertase PC7|proprotein convertase 7|proprotein convertase 8|proprotein convertase PC7|subtilisin/kexin-like protease PC7 PCSK7 OGG:3000009175 Bin Zhao, Yue Liu, Oliver He LZK MEKK13 MLK WEB: http://www.ncbi.nlm.nih.gov/gene MAP3K13 mitogen-activated protein kinase kinase kinase 13 9175 3q27 9606 3 Official from a nomenclature committee GO_0000186 (EC: IDA, PMID: 11726277); GO_0004674 (EC: IDA, PMID: 9353328); GO_0004709 (EC: IDA, PMID: 11726277); GO_0005515 (EC: IPI, PMID: 11726277); GO_0005524 (EC: IEA); GO_0006468 (EC: IDA, PMID: 11726277); GO_0007254 (EC: IDA, PMID: 11726277); GO_0008385 (EC: IDA, Qualifier: colocalizes_with, PMID: 12492477); GO_0016020 (EC: IDA, PMID: 9353328); GO_0019901 (EC: ISS, PMID: 9353328); GO_0042802 (EC: IPI, PMID: 11163770); GO_0042803 (EC: IDA, PMID: 11163770); GO_0046777 (EC: IDA, PMID: 9353328); GO_0046872 (EC: IEA); GO_0051092 (EC: IDA, PMID: 12492477) PMID: 8274451; 9353328; 11163770; 11726277; 12186766; 12477932; 12492477; 14702039; 15489334; 20379614; 21988832; 22505724; 22623531; 22837378 mitogen-activated protein kinase kinase kinase 13 Ensembl:ENSG00000073803 HGNC:6852 HPRD:05372 MIM:604915 Vega:OTTHUMG00000156673 Other designations: leucine zipper-bearing kinase|mixed lineage kinase MAP3K13 OGG:3000009188 Bin Zhao, Yue Liu, Oliver He GUA GURDB RH-II/GU RH-II/GuA WEB: http://www.ncbi.nlm.nih.gov/gene DDX21 DEAD (Asp-Glu-Ala-Asp) box helicase 21 9188 10q21 9606 10 Official from a nomenclature committee GO_0003725 (EC: IEA); GO_0004004 (EC: TAS, PMID: 8614622); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0006200 (EC: TAS, PMID: 8614622); GO_0009615 (EC: IEA); GO_0043330 (EC: IEA); GO_0044822 (EC: IDA) PMID: 8614622; 9177271; 10860663; 11237763; 11790298; 11823437; 11891046; 12477932; 12777385; 14559904; 15164054; 15302935; 15367657; 15489334; 15635413; 15840729; 15848144; 16045751; 16159877; 16385451; 16565220; 17081983; 17353931; 18029348; 18180292; 18781797; 19394292; 19454010; 19596686; 19710015; 19738201; 20020773; 20360068; 20431927; 20462248; 20800221; 20873769; 21044950; 21139048; 21145461; 21149631; 21182205; 21252943; 21319273; 21385873; 21726808; 21890473; 21907836; 22108332; 22113938; 22174317; 22178446; 22268729; 22446626; 22586326; 22623428; 22751105; 22939629; 22952844; 23000965; 23145133; 23151878; 23184937; 23277564; 23398456; 23419719; 23455922; 23503679; 23602568; 24457600 DEAD (Asp-Glu-Ala-Asp) box helicase 21 Ensembl:ENSG00000165732 HGNC:2744 HPRD:05895 MIM:606357 Vega:OTTHUMG00000018366 Other designations: DEAD (Asp-Glu-Ala-Asp) box polypeptide 21|DEAD box protein 21|DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 21|Gu protein|RH II/Gu|RNA helicase II/Gu alpha|gu-alpha|nucleolar RNA helicase 2|nucleolar RNA helicase Gu|nucleolar RNA helicase II DDX21 OGG:3000009221 Bin Zhao, Yue Liu, Oliver He NOPP130 NOPP140 NS5ATP13 P130 WEB: http://www.ncbi.nlm.nih.gov/gene NOLC1 nucleolar and coiled-body phosphoprotein 1 9221 10q24.32 9606 10 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 17620599); GO_0005524 (EC: IEA); GO_0005525 (EC: IEA); GO_0005730 (EC: IDA); GO_0005737 (EC: IEA); GO_0006364 (EC: TAS, PMID: 7657714); GO_0007000 (EC: IEA); GO_0007049 (EC: TAS, PMID: 7657714); GO_0007067 (EC: TAS, PMID: 7657714); GO_0015030 (EC: IEA); GO_0044822 (EC: IDA) PMID: 7584026; 7584028; 7657714; 8125298; 8630004; 8657117; 8889548; 8972203; 9013635; 9016786; 9553145; 9679133; 10567578; 11571651; 12167624; 12446766; 12477932; 12777385; 14702039; 15144186; 15146197; 15161933; 15302935; 15324660; 15385968; 16341674; 16344560; 16385451; 16964243; 17001309; 17038328; 17081983; 17342744; 17353931; 17531812; 17620599; 18029348; 18253863; 18790693; 19129172; 19381672; 19471022; 19541936; 19608861; 20360068; 21139048; 21264300; 21266110; 21693764; 21832049; 21890473; 21906983; 22178446; 22190034; 22586326; 22751105; 22863883; 22906532; 22939629; 22952844; 23000965; 23188192; 23398456; 23455922; 24218616; 24457600 nucleolar and coiled-body phosphoprotein 1 Ensembl:ENSG00000166197 HGNC:15608 MIM:602394 Vega:OTTHUMG00000018944 Other designations: 140 kDa nucleolar phosphoprotein|HCV NS5A trans-regulated protein 13|HCV NS5A-transactivated protein 13|hepatitis C virus NS5A-transactivated protein 13|nucleolar 130 kDa protein|nucleolar and coiled-body phosphprotein 1|nucleolar phosphoprotein p130|nucleolar protein p130 NOLC1 OGG:3000009400 Bin Zhao, Yue Liu, Oliver He RECQ5 WEB: http://www.ncbi.nlm.nih.gov/gene RECQL5 RecQ protein-like 5 9400 17q25 9606 17 Official from a nomenclature committee GO_0000993 (EC: IDA); GO_0003676 (EC: IEA); GO_0003678 (EC: IDA); GO_0003678 (EC: NAS, PMID: 10710432); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005654 (EC: NAS, PMID: 10710432); GO_0005730 (EC: IDA); GO_0005737 (EC: IDA); GO_0005737 (EC: NAS, PMID: 10710432); GO_0006259 (EC: NAS, PMID: 10710432); GO_0006260 (EC: IMP); GO_0006281 (EC: IMP); GO_0006310 (EC: IEA); GO_0007067 (EC: IMP); GO_0008026 (EC: IEA); GO_0016591 (EC: IDA); GO_0031965 (EC: IDA); GO_0032508 (EC: IDA); GO_0032508 (EC: NAS, PMID: 10710432); GO_0032508 (EC: TAS, PMID: 9878247); GO_0034244 (EC: IDA); GO_0051304 (EC: IMP) PMID: 9878247; 10471747; 10710432; 12477932; 15241474; 15342556; 15489334; 16169070; 16344560; 17003056; 18003859; 18029348; 18290761; 18419580; 18562274; 19270065; 19570979; 20081208; 20231364; 20348101; 20643585; 21145461; 21402780; 21890473; 21988832; 22633600; 22645136; 22939629; 22973052; 22990118; 23180761; 23627586; 23748380 RecQ protein-like 5 Ensembl:ENSG00000108469 HGNC:9950 HPRD:04806 MIM:603781 Vega:OTTHUMG00000179795 Other designations: ATP-dependent DNA helicase Q5|DNA helicase, RecQ-like type 5 RECQL5 OGG:3000009415 Bin Zhao, Yue Liu, Oliver He D6D DES6 FADSD6 LLCDL2 SLL0262 TU13 WEB: http://www.ncbi.nlm.nih.gov/gene FADS2 fatty acid desaturase 2 9415 11q12.2 9606 11 Official from a nomenclature committee GO_0004768 (EC: IEA); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0005887 (EC: TAS, PMID: 9867867); GO_0006636 (EC: IEA); GO_0016020 (EC: TAS, PMID: 9867867); GO_0020037 (EC: IEA); GO_0033559 (EC: TAS); GO_0036109 (EC: TAS); GO_0043651 (EC: TAS); GO_0044281 (EC: TAS) PMID: 9445487; 9867867; 10860662; 12147235; 12477932; 12562861; 12713571; 12851727; 12951357; 14702039; 16196087; 16303743; 16344560; 16670158; 16713569; 16893529; 16908951; 17284757; 17852835; 17984066; 18320251; 18479586; 18626191; 18842780; 18936223; 18937842; 19060906; 19060910; 19060911; 19144731; 19148276; 19352218; 19546342; 19776639; 19809313; 19875987; 19913121; 19948371; 20045144; 20335541; 20339536; 20364269; 20379614; 20395685; 20427696; 20484448; 20562440; 20565855; 20615514; 20628086; 20644632; 20686565; 20691134; 20694148; 20714348; 20948998; 20972250; 20980488; 21040914; 21106917; 21139048; 21414826; 21560298; 21605700; 21629299; 21733300; 21793953; 21818279; 21829377; 21890473; 21917437; 21980057; 21987572; 22001757; 22140540; 22194195; 22286219; 22359512; 22505724; 22619218; 22629455; 22748975; 22877655; 22916037; 22960237; 23000965; 23128233; 23160180; 23211517; 23221573; 23362303; 23378610; 23414387; 23464991; 23555103; 23667444; 23737301; 23844124 fatty acid desaturase 2 Ensembl:ENSG00000134824 HGNC:3575 HPRD:05854 MIM:606149 Vega:OTTHUMG00000163794 Other designations: delta(6) desaturase|delta(6) fatty acid desaturase|delta-6 desaturase|delta-6 fatty acid desaturase|delta-6-desaturase|linoleoyl-CoA desaturase (delta-6-desaturase)-like 2 FADS2 OGG:3000009420 Bin Zhao, Yue Liu, Oliver He CBAS3 CP7B SPG5A WEB: http://www.ncbi.nlm.nih.gov/gene CYP7B1 cytochrome P450, family 7, subfamily B, polypeptide 1 9420 8q21.3 9606 8 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006699 (EC: IEA); GO_0006699 (EC: TAS); GO_0006805 (EC: TAS); GO_0008203 (EC: IEA); GO_0008206 (EC: TAS); GO_0008219 (EC: IEA); GO_0008396 (EC: IEA); GO_0016125 (EC: TAS); GO_0020037 (EC: IEA); GO_0033147 (EC: IEA); GO_0033783 (EC: IEA); GO_0044281 (EC: TAS); GO_0050679 (EC: IEA); GO_0060740 (EC: IEA) PMID:7987300; 9559267; 9802883; 10588945; 12477932; 12721789; 14521990; 15003524; 15007371; 15128046; 15181079; 15698543; 15751070; 16630558; 17467270; 17680536; 18055760; 18252231; 18331353; 18676680; 18790053; 18855023; 19170196; 19187859; 19343046; 19363635; 19439420; 19625176; 19687010; 19692168; 19732851; 19913121; 20628086; 21214876; 21452256; 21541746; 21567895; 21890473; 22174851; 23180418; 23393555; 23400010 cytochrome P450, family 7, subfamily B, polypeptide 1 Ensembl:ENSG00000172817 HGNC:2652 HPRD:04753 MIM:603711 Vega:OTTHUMG00000164387 Other designations: 25-hydroxycholesterol 7-alpha-hydroxylase|cytochrome P450 7B1|cytochrome P450, subfamily VIIB (oxysterol 7 alpha-hydroxylase), polypeptide 1|oxysterol 7-alpha-hydroxylase|oxysterol 7alpha-hydroxylase CYP7B1 OGG:3000009439 Bin Zhao, Yue Liu, Oliver He ARC130 CRSP130 CRSP133 CRSP3 DRIP130 MRT18 SUR-2 SUR2 WEB: http://www.ncbi.nlm.nih.gov/gene MED23 mediator complex subunit 23 9439 RP5-914N13.2 6q22.33-q24.1 9606 6 Official from a nomenclature committee GO_0003713 (EC: TAS, PMID: 9989412); GO_0005515 (EC: IPI, PMID: 17438371); GO_0005654 (EC: TAS); GO_0005667 (EC: IDA, PMID: 9989412); GO_0006355 (EC: IDA, PMID: 9989412); GO_0006357 (EC: TAS, PMID: 9989412); GO_0006367 (EC: TAS); GO_0010467 (EC: TAS); GO_0016592 (EC: IEA) PMID: 9989412; 10235266; 10235267; 10353252; 10574462; 10823961; 10993082; 11076863; 11230166; 11416138; 11834832; 11867769; 11934987; 12089346; 12242338; 12421765; 12477932; 12543799; 14574404; 14638676; 14657022; 14759369; 15175163; 15489336; 15572696; 15893730; 15989967; 16147992; 16204234; 16239144; 16381901; 16799563; 16964286; 17438371; 18418385; 18660489; 18691967; 19322201; 19913121; 20098423; 20133760; 20508642; 20628086; 20720539; 21139048; 21729782; 21868677; 21890473; 21906983; 22505724; 22797925; 22939629; 22988093; 23022380; 23275444; 23322298; 23340209; 23602568 mediator complex subunit 23 Ensembl:ENSG00000112282 HGNC:2372 HPRD:05436 MIM:605042 Vega:OTTHUMG00000015565 Other designations: 130 kDa transcriptional co-activator|133 kDa transcriptional co-activator|activator-recruited cofactor 130 kDa component|cofactor required for Sp1 transcriptional activation subunit 3|mediator of RNA polymerase II transcription subunit 23|vitamin D3 receptor interacting protein MED23 OGG:3000009451 Bin Zhao, Yue Liu, Oliver He PEK PERK WRS WEB: http://www.ncbi.nlm.nih.gov/gene EIF2AK3 eukaryotic translation initiation factor 2-alpha kinase 3 9451 2p12 9606 2 GO_0001501 (EC: ISS); GO_0001503 (EC: IMP, PMID:12086964); GO_0002063 (EC: ISS); GO_0004672 (EC: TAS, PMID:10026192); GO_0004674 (EC: ISS); GO_0004674 (EC: TAS); GO_0004694 (EC: IDA, PMID:10026192); GO_0004694 (EC: IMP, PMID:12086964); GO_0005515 (EC: IPI, PMID:11907036); GO_0005524 (EC: IEA); GO_0005737 (EC: ISS); GO_0005783 (EC: IC, PMID:11907036); GO_0005783 (EC: ISS); GO_0005783 (EC: TAS, PMID:12086964); GO_0005789 (EC: ISS); GO_0005789 (EC: NAS, PMID:11907036); GO_0005789 (EC: TAS); GO_0006412 (EC: IEA); GO_0006468 (EC: ISS); GO_0006919 (EC: ISS); GO_0006983 (EC: IDA, PMID:10677345); GO_0006987 (EC: TAS); GO_0007029 (EC: ISS); GO_0007595 (EC: IEA); GO_0009967 (EC: IEA); GO_0016021 (EC: IEA); GO_0017148 (EC: TAS, PMID:12086964); GO_0019217 (EC: IEA); GO_0019722 (EC: ISS); GO_0019899 (EC: IPI); GO_0019903 (EC: IPI); GO_0030073 (EC: ISS); GO_0030282 (EC: ISS); GO_0030968 (EC: IDA, PMID:10677345); GO_0030968 (EC: TAS, PMID:19816510); GO_0031018 (EC: IMP, PMID:12086964); GO_0031642 (EC: ISS); GO_0032057 (EC: TAS, PMID:10677345); GO_0032092 (EC: IEA); GO_0032933 (EC: IEA); GO_0034976 (EC: IMP, PMID:19061639); GO_0042802 (EC: IPI, PMID:11907036); GO_0044267 (EC: TAS); GO_0045444 (EC: IEA); GO_0046777 (EC: IDA, PMID:10026192); GO_0046777 (EC: IMP, PMID:12086964); GO_0048009 (EC: ISS); GO_0051260 (EC: IMP, PMID:11907036); GO_0070059 (EC: IEA) PMID:1677563; 8099443; 9819435; 10026192; 10542257; 10575235; 10677345; 10848580; 10932183; 11555640; 11907036; 12014989; 12086964; 12370288; 12446770; 12446838; 12477932; 12610133; 14517290; 15146197; 15220213; 15234121; 15483661; 15489334; 15650164; 16147992; 16148948; 16288713; 16344560; 16720581; 17229688; 17785458; 17823375; 18063576; 18216498; 18426796; 18451152; 18664456; 18787411; 19009018; 19029953; 19061639; 19586904; 19816510; 19837917; 19913121; 20072656; 20103619; 20202148; 20348950; 20371724; 20379614; 20457808; 20463975; 20628086; 20709135; 20800603; 20881960; 21385877; 21419175; 21464971; 21518408; 21648287; 21685912; 21709020; 22028037; 22072062; 22169477; 22246806; 22253692; 22354021; 22446326; 22795130; 22813743; 22915762; 22917505; 22956602; 23103912; 23110043; 23116876; 23160380; 23471998; 23585173; 23592989; 23759358; 24103755; 24114838; 24457600 eukaryotic translation initiation factor 2-alpha kinase 3 Ensembl:ENSG00000172071 HGNC:3255 HPRD:04942 MIM:604032 Vega:OTTHUMG00000155046 Other designations: PRKR-like endoplasmic reticulum kinase|eukaryotic translation initiation factor 2 alpha kinase 3|hsPEK|pancreatic EIF2-alpha kinase EIF2AK3 OGG:3000009470 Bin Zhao, Yue Liu, Oliver He 4E-LP 4EHP EIF4EL3 IF4e WEB: http://www.ncbi.nlm.nih.gov/gene EIF4E2 eukaryotic translation initiation factor 4E family member 2 9470 2q37.1 9606 2 GO_0000339 (EC: TAS, PMID:9582349); GO_0001701 (EC: IEA); GO_0003743 (EC: IEA); GO_0005515 (EC: IPI, PMID:16189514); GO_0005829 (EC: TAS); GO_0005845 (EC: IDA, PMID:17368478); GO_0008135 (EC: TAS, PMID:9582349); GO_0017148 (EC: IMP); GO_0019221 (EC: TAS); GO_0031625 (EC: IPI, PMID:14623119); GO_0044822 (EC: IDA) PMID:9582349; 9653160; 11042152; 12477932; 14623119; 14702039; 15094042; 15153109; 15489334; 16189514; 16344560; 17289916; 17353931; 17368478; 17369309; 17979178; 19060904; 19615732; 20379614; 20467438; 20531386; 21079520; 21139048; 21832049; 21890473; 22751931; 23940030; 24250222; 24255178 eukaryotic translation initiation factor 4E family member 2 Ensembl:ENSG00000135930 HGNC:3293 HPRD:05798 MIM:605895 Vega:OTTHUMG00000133256 Other designations: eIF-4E type 2|eIF4E-like cap-binding protein|eIF4E-like protein 4E-LP|eukaryotic translation initiation factor 4E homologous protein|eukaryotic translation initiation factor 4E type 2|eukaryotic translation initiation factor 4E-like 3|mRNA cap-binding protein type 3 EIF4E2 OGG:3000009517 Bin Zhao, Yue Liu, Oliver He HSN1C LCB2 LCB2A NSAN1C SPT2 hLCB2a WEB: http://www.ncbi.nlm.nih.gov/gene SPTLC2 serine palmitoyltransferase, long chain base subunit 2 9517 14q24.3 9606 14 Official from a nomenclature committee GO_0004758 (EC: IDA, PMID: 19416851); GO_0005739 (EC: IEA); GO_0005789 (EC: TAS); GO_0006665 (EC: TAS); GO_0006686 (EC: IEA); GO_0016021 (EC: IEA); GO_0017059 (EC: IDA, PMID: 19416851); GO_0030148 (EC: TAS, PMID: 19416851); GO_0030170 (EC: IEA); GO_0044281 (EC: TAS); GO_0046511 (EC: IEA); GO_0046512 (EC: IEA); GO_0046513 (EC: IEA) PMID: 7506601; 8889549; 8921873; 9363775; 9628581; 10722674; 10737800; 12207934; 12445191; 12477932; 12508121; 15489334; 16147992; 17081983; 17194770; 17331073; 19416851; 20877624; 20920666; 21139048; 21890473; 21906983; 23658386 serine palmitoyltransferase, long chain base subunit 2 Ensembl:ENSG00000100596 HGNC:11278 HPRD:05755 MIM:605713 Vega:OTTHUMG00000171540 Other designations: LCB 2|SPT 2|long chain base biosynthesis protein 2a|serine palmitoyltransferase 2|serine palmitoyltransferase, subunit II|serine-palmitoyl-CoA transferase 2 SPTLC2 OGG:3000009518 Bin Zhao, Yue Liu, Oliver He GDF-15 MIC-1 MIC1 NAG-1 PDF PLAB PTGFB WEB: http://www.ncbi.nlm.nih.gov/gene GDF15 growth differentiation factor 15 9518 19p13.11 9606 19 Official from a nomenclature committee GO_0005125 (EC: IEA); GO_0005576 (EC: TAS, PMID: 9326641); GO_0005615 (EC: IEA); GO_0007165 (EC: TAS, PMID: 9326641); GO_0007179 (EC: TAS, PMID: 9348093); GO_0007267 (EC: TAS, PMID: 9326641); GO_0008083 (EC: IEA) PMID: 8125298; 9326641; 9348093; 9375789; 9426002; 9593718; 10524241; 10777512; 10811612; 11102463; 11134143; 11141057; 11259636; 11278594; 11445565; 11895857; 11994274; 12011055; 12082608; 12090982; 12139236; 12477932; 12514175; 12624183; 12855642; 12894347; 12900512; 12941831; 14575402; 14662774; 14726168; 15073115; 15316060; 15342369; 15670751; 15677629; 15757899; 15900300; 16154591; 16286461; 16388506; 16397141; 16484622; 16699947; 16741990; 16775185; 17050687; 17192395; 17328047; 17548705; 17637746; 17721544; 17908975; 17909264; 17982462; 18029348; 18264720; 18359786; 18398830; 18550273; 18624398; 18657084; 18676680; 18754039; 18801729; 18824595; 19047680; 19060904; 19074584; 19100681; 19125423; 19133249; 19152406; 19168526; 19170196; 19302795; 19341722; 19357976; 19375854; 19401523; 19470878; 19505289; 19505919; 19515791; 19521960; 19625176; 19692168; 19695766; 19913121; 19946339; 20024638; 20031597; 20067113; 20104227; 20130018; 20160200; 20167682; 20193126; 20215826; 20237496; 20357380; 20385121; 20431030; 20534737; 20576287; 20628086; 20800603; 20854422; 20855664; 20860541; 20884666; 20937742; 20966402; 20975101; 21097678; 21245963; 21312063; 21336029; 21437897; 21475976; 21487066; 21503121; 21504622; 21535154; 21548946; 21586550; 21616994; 21645023; 21773947; 21803025; 21809352; 21865063; 21881845; 21906983; 22023041; 22064648; 22144502; 22160844; 22180562; 22231869; 22301101; 22341306; 22365732; 22384099; 22484283; 22505696; 22511768; 22723347; 22815297; 22872134; 22975449; 23071585; 23146921; 23154866; 23262134; 23328263; 23335088; 23468844; 23503457; 23799024; 23836903; 23850849; 23996089; 24136234; 24345755 growth differentiation factor 15 Ensembl:ENSG00000130513 HGNC:30142 HPRD:05608 MIM:605312 Vega:OTTHUMG00000183360 Other designations: NRG-1|NSAID (nonsteroidal anti-inflammatory drug)-activated protein 1|NSAID-activated gene 1 protein|NSAID-regulated gene 1 protein|PTGF-beta|growth/differentiation factor 15|macrophage inhibitory cytokine 1|placental TGF-beta|placental bone morphogenetic protein|prostate differentiation factor GDF15 OGG:3000009636 Bin Zhao, Yue Liu, Oliver He G1P2 IFI15 IP17 UCRP hUCRP WEB: http://www.ncbi.nlm.nih.gov/gene ISG15 ISG15 ubiquitin-like modifier 9636 1p36.33 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 16872604); GO_0005576 (EC: IDA); GO_0005829 (EC: TAS); GO_0016032 (EC: IEA); GO_0019221 (EC: TAS); GO_0019941 (EC: IEA); GO_0031386 (EC: IEA); GO_0031397 (EC: IDA, PMID: 18305167); GO_0032020 (EC: IDA, PMID: 16122702); GO_0032020 (EC: IMP); GO_0032480 (EC: TAS); GO_0032649 (EC: IMP); GO_0034340 (EC: IDA); GO_0042742 (EC: IMP); GO_0045071 (EC: IMP, PMID: 19357168); GO_0045087 (EC: TAS); GO_0045648 (EC: IEA); GO_0051607 (EC: IMP, PMID: 19357168); GO_0060337 (EC: TAS) PMID: 1373138; 1695131; 2005397; 2440890; 2477469; 3087979; 3350799; 3476954; 7490683; 7526157; 8550581; 8889548; 8892645; 10476939; 10508226; 10866800; 11157743; 11788588; 12055236; 12067988; 12477932; 12539042; 14976209; 15131269; 15489334; 15670748; 15684817; 15917233; 16009940; 16112642; 16122702; 16139798; 16169070; 16189514; 16254333; 16424026; 16428300; 16434471; 16641915; 16815975; 16872604; 16884686; 17069755; 17097911; 17222803; 17289916; 17353931; 17653289; 17692280; 17719635; 18057259; 18287095; 18305167; 18356159; 18566215; 18583345; 18597038; 18606809; 18627608; 18953482; 19043203; 19073728; 19074853; 19357168; 19378789; 19430494; 19656964; 19694548; 19846672; 19913121; 19956859; 19959962; 20035788; 20093371; 20133869; 20157543; 20164219; 20219937; 20308324; 20542004; 20581239; 20628086; 20628624; 20639253; 20946978; 20975683; 21139048; 21245344; 21298066; 21399617; 21544738; 21757684; 21808041; 21906983; 21994560; 22093708; 22100648; 22185919; 22405323; 22647704; 22693631; 22706304; 22729740; 22740306; 22762019; 22859821; 22939629; 23212917; 23229543; 23588721; 23824909; 24386835 ISG15 ubiquitin-like modifier Ensembl:ENSG00000187608 HGNC:4053 HPRD:00958 MIM:147571 Vega:OTTHUMG00000040777 ISG15 OGG:3000009641 Bin Zhao, Yue Liu, Oliver He IKK-E IKK-i IKKE IKKI WEB: http://www.ncbi.nlm.nih.gov/gene IKBKE inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase epsilon 9641 RP11-534L20.1 1q32.1 9606 1 GO_0002224 (EC: TAS); GO_0002756 (EC: TAS); GO_0004704 (EC: IDA, PMID:10882136); GO_0005515 (EC: IPI, PMID:14743216); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006468 (EC: IDA, PMID:10882136); GO_0006955 (EC: NAS, PMID:10421793); GO_0008384 (EC: IEA); GO_0008630 (EC: IMP); GO_0010008 (EC: TAS); GO_0016605 (EC: IDA); GO_0032480 (EC: TAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0035666 (EC: TAS); GO_0038061 (EC: IDA, PMID:10882136); GO_0043123 (EC: IEP, PMID:12761501); GO_0045087 (EC: TAS) PMID:8590280; 8889548; 9914500; 10421793; 10759890; 10882136; 11470787; 11839743; 11902829; 11959143; 12133833; 12477932; 12676577; 12692549; 12736252; 12761501; 14560022; 14702039; 14743216; 15276183; 15367631; 15489227; 15489334; 15550384; 15556946; 15661910; 15695821; 15767399; 15879144; 15939554; 16177806; 16281057; 16299251; 16344560; 16380379; 16393995; 16710414; 16731946; 16840782; 16888014; 16914100; 17003035; 17327220; 17328045; 17353931; 17468758; 17568778; 17574021; 17599067; 17823124; 18029348; 18353649; 18434448; 18636086; 18636090; 19153231; 19380491; 19481526; 19497997; 19786281; 19820708; 19913121; 19940156; 20188669; 20449947; 20581830; 20588308; 20628086; 20634891; 21171089; 21179067; 21200404; 21212807; 21221132; 21271611; 21464307; 21685032; 21718646; 21885437; 21903422; 21906983; 21908616; 21987572; 22065572; 22072751; 22079989; 22266464; 22330135; 22505724; 22531926; 22532683; 22552702; 22787218; 22851696; 22939624; 22942254; 23007157; 23096996; 23157677; 23308279; 23365428; 23453969; 23478265; 23535865; 23691078; 23816933; 23873932; 23950712 inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase epsilon Ensembl:ENSG00000143466 HGNC:14552 HPRD:05442 MIM:605048 Vega:OTTHUMG00000036346 Other designations: I-kappa-B kinase epsilon|IKK-epsilon|IKK-related kinase epsilon|inducible I kappa-B kinase|inducible IkappaB kinase|inhibitor of nuclear factor kappa-B kinase subunit epsilon IKBKE OGG:3000009648 Bin Zhao, Yue Liu, Oliver He GCC185 RANBP2L4 REN53 WEB: http://www.ncbi.nlm.nih.gov/gene GCC2 GRIP and coiled-coil domain containing 2 9648 2q12.3 9606 2 Official from a nomenclature committee GO_0000042 (EC: IEA); GO_0005515 (EC: IPI, PMID: 16885419); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA); GO_0005794 (EC: IDA); GO_0005802 (EC: IDA, PMID: 16885419); GO_0006622 (EC: IMP, PMID: 16885419); GO_0016020 (EC: IEA); GO_0031023 (EC: IMP, PMID: 17543864); GO_0034067 (EC: IMP, PMID: 16885419); GO_0034453 (EC: IMP, PMID: 17543864); GO_0034499 (EC: IMP, PMID: 16885419); GO_0042147 (EC: IMP, PMID: 17488291); GO_0042802 (EC: IPI, PMID: 18243103); GO_0043001 (EC: IMP, Qualifier: NOT, PMID: 16885419); GO_0070861 (EC: IMP, PMID: 17488291); GO_0071955 (EC: IMP, PMID: 17488291); GO_0090161 (EC: IMP, PMID: 16885419) PMID: 8889548; 9205841; 10508479; 11149944; 12200376; 12446665; 12477932; 12972563; 14702039; 15489334; 15522892; 15654769; 15815621; 16344560; 16885419; 16964243; 17488291; 17543864; 18029348; 18243103; 18946081; 19013454; 19615732; 19703403; 21139048; 21875948; 21890473; 22159419; 22939629; 23000965 GRIP and coiled-coil domain containing 2 Ensembl:ENSG00000135968 HGNC:23218 HPRD:11001 MIM:612711 Vega:OTTHUMG00000153214 Other designations: 185 kDa Golgi coiled-coil protein|CLL-associated antigen KW-11|CTCL tumor antigen se1-1|GCC protein, 185-kD|GRIP and coiled-coil domain-containing protein 2|Golgi coiled-coil protein GCC185|Ran-binding protein 2-like 4|renal carcinoma antigen NY-REN-53 GCC2 OGG:3000009669 Bin Zhao, Yue Liu, Oliver He IF2 WEB: http://www.ncbi.nlm.nih.gov/gene EIF5B eukaryotic translation initiation factor 5B 9669 2q11.2 9606 2 GO_0003743 (EC: IDA, PMID:10432305); GO_0003743 (EC: NAS, PMID:10200264); GO_0003924 (EC: IEA); GO_0005515 (EC: IPI, PMID:12569173); GO_0005525 (EC: IEA); GO_0005829 (EC: TAS); GO_0006412 (EC: TAS); GO_0006413 (EC: TAS); GO_0006446 (EC: IDA, PMID:10432305); GO_0006446 (EC: NAS, PMID:10200264); GO_0010467 (EC: TAS); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA) PMID:8621719; 9872452; 10200264; 10432305; 11699879; 12477932; 12514125; 12569173; 14702039; 15302935; 16097034; 16964243; 17081983; 17161026; 17361185; 17568775; 18572216; 19135240; 19738201; 20195357; 20211142; 20562859; 21139048; 21145461; 21151833; 21697471; 21890473; 21907836; 21926972; 21963094; 22108332; 22113938; 22586326; 22678362; 22863883; 22939629; 22990118; 23000965; 24250222 eukaryotic translation initiation factor 5B Ensembl:ENSG00000158417 HGNC:30793 HPRD:07304 MIM:606086 Vega:OTTHUMG00000153242 Other designations: eIF-5B|translation initiation factor IF-2|translation initiation factor IF2 EIF5B OGG:3000009695 Bin Zhao, Yue Liu, Oliver He EDEM WEB: http://www.ncbi.nlm.nih.gov/gene EDEM1 ER degradation enhancer, mannosidase alpha-like 1 9695 3p26.1 9606 3 GO_0004571 (EC: IDA, Qualifier: NOT, PMID:12610306); GO_0005509 (EC: IEA); GO_0005515 (EC: IPI, PMID:16449189); GO_0005789 (EC: TAS); GO_0006457 (EC: TAS); GO_0006987 (EC: TAS); GO_0018279 (EC: TAS); GO_0030176 (EC: ISS); GO_0030433 (EC: ISS); GO_0030968 (EC: TAS); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS); GO_0051787 (EC: IDA, PMID:19524542) PMID:9039502; 11375934; 12477932; 12610305; 12610306; 15146197; 15489334; 15579471; 16449189; 16629899; 17353931; 17360537; 17380188; 17499246; 18303019; 18452703; 19266160; 19322201; 19524542; 19934218; 20065073; 21062743; 21388347; 21632540; 21917589; 22678362; 22905195; 23233672 ER degradation enhancer, mannosidase alpha-like 1 Ensembl:ENSG00000134109 HGNC:18967 HPRD:09644 MIM:607673 Vega:OTTHUMG00000154896 Other designations: ER degradation-enhancing alpha-mannosidase-like 1|ER degradation-enhancing alpha-mannosidase-like protein 1 EDEM1 OGG:3000009709 Bin Zhao, Yue Liu, Oliver He HERP Mif1 SUP WEB: http://www.ncbi.nlm.nih.gov/gene HERPUD1 homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1 9709 16q13 9606 16 Official from a nomenclature committee GO_0003674 (EC: ND); GO_0005789 (EC: IDA, PMID: 10922362); GO_0005789 (EC: TAS); GO_0006511 (EC: IEA); GO_0006874 (EC: IEA); GO_0006986 (EC: IEP, PMID: 10708769); GO_0006987 (EC: TAS); GO_0016021 (EC: IEA); GO_0030968 (EC: TAS); GO_0031396 (EC: IEA); GO_0032092 (EC: IEA); GO_0043154 (EC: IEA); GO_0044267 (EC: TAS) PMID: 7584026; 8125298; 8619474; 9110174; 10708769; 10922362; 11112790; 11799129; 12153396; 12370023; 12477932; 14550564; 15489334; 16169070; 16189514; 16289116; 16344560; 16713569; 16940180; 17020760; 17310145; 17420289; 18042451; 18307982; 18656546; 19251110; 19447887; 19788048; 20031564; 20054003; 20147634; 20604806; 20694148; 20838585; 20936779; 21139048; 21149444; 21832049; 21900206; 21906983; 21963094; 21965653; 23372434; 23505323; 23867461; 24120520 homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1 Ensembl:ENSG00000051108 HGNC:13744 HPRD:07456 MIM:608070 Vega:OTTHUMG00000133276 Other designations: MMS-inducible|homocysteine-inducible endoplasmic reticulum stress-inducible ubiquitin-like domain member 1 protein|homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein|methyl methanesulfonate (MMF)-inducible fragment protein 1 HERPUD1 OGG:3000009768 Bin Zhao, Yue Liu, Oliver He NS5ATP9 OEATC OEATC-1 OEATC1 PAF PAF15 p15(PAF) p15/PAF p15PAF WEB: http://www.ncbi.nlm.nih.gov/gene KIAA0101 KIAA0101 9768 L5 15q22.31 20140408 9606 15 protein-coding Official from a nomenclature committee GO_0003682 (EC: IDA); GO_0005515 (EC: IPI); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA); GO_0006260 (EC: IDA); GO_0006974 (EC: IDA); GO_0009411 (EC: IDA); GO_0019985 (EC: IMP); GO_0048471 (EC: IDA); GO_0051297 (EC: IMP); GO_0051726 (EC: IMP) PMID: 7788527; 11313979; 12477932; 15334068; 15489334; 15789362; 16288740; 16646990; 17207965; 17213182; 17875765; 18068894; 18727915; 18781797; 19219066; 20118010; 20639865; 20972266; 21070969; 21139048; 21263028; 21628590; 21673012; 21689861; 21890473; 21906983; 21963094; 22053931; 22096502; 22505724; 22576474; 22863883; 22939629; 23000965; 23157749; 23209346; 23240630; 23593430; 23698777; 24055345; 24145239; 24197986 KIAA0101 Ensembl:ENSG00000166803 HGNC:28961 HPRD:13778 MIM:610696 Vega:OTTHUMG00000133017 Other designations: HCV NS5A-transactivated protein 9|PCNA-associated factor|PCNA-associated factor of 15 kDa|hepatitis C virus NS5A-transactivated protein 9|overexpressed in anaplastic thyroid carcinoma 1 KIAA0101 OGG:3000009775 Bin Zhao, Yue Liu, Oliver He DDX48 MUK34 NMP265 NUK34 RCPS eIF4AIII WEB: http://www.ncbi.nlm.nih.gov/gene EIF4A3 eukaryotic translation initiation factor 4A3 9775 17q25.3 9606 17 GO_0000184 (EC: IMP, PMID:16209946); GO_0000184 (EC: TAS); GO_0000288 (EC: TAS); GO_0000289 (EC: TAS); GO_0000398 (EC: IC, PMID:11991638); GO_0003729 (EC: IDA); GO_0004004 (EC: IDA, PMID:10523622); GO_0005515 (EC: IPI, PMID:10523622); GO_0005524 (EC: IDA, PMID:10523622); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA, PMID:10523622); GO_0005829 (EC: TAS); GO_0006200 (EC: IDA, PMID:10523622); GO_0006364 (EC: IEA); GO_0008143 (EC: IDA, PMID:10523622); GO_0010467 (EC: TAS); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016607 (EC: IEA); GO_0017148 (EC: IDA, PMID:10523622); GO_0019221 (EC: TAS); GO_0035145 (EC: IDA, PMID:16601204); GO_0044822 (EC: IDA); GO_0045727 (EC: IMP, PMID:18423201); GO_0051028 (EC: IEA); GO_0071013 (EC: IDA, PMID:11991638) PMID:7788527; 10523622; 10623621; 11991638; 12127692; 12477932; 14730019; 14973490; 15024115; 15034551; 15324660; 15489334; 15635413; 15796914; 16159877; 16170325; 16189514; 16196087; 16209946; 16344560; 16452507; 16601204; 16923391; 16931718; 17190602; 17361185; 17456004; 17606899; 17632064; 17643375; 18337751; 18423201; 18427545; 18781797; 18954305; 18974867; 19417104; 19435936; 19471022; 19738201; 19884259; 20360068; 20371770; 20639865; 20972266; 21081666; 21110914; 21139048; 21145460; 21145461; 21319273; 21576267; 21853274; 21890473; 21906983; 21963094; 21987572; 22053931; 22178446; 22268729; 22365833; 22505724; 22623428; 22863883; 22939629; 22952844; 22961380; 23000965; 23084401; 23602568; 24218557; 24360810; 24457600 eukaryotic translation initiation factor 4A3 Ensembl:ENSG00000141543 HGNC:18683 HPRD:06482 MIM:608546 Vega:OTTHUMG00000177538 Other designations: ATP-dependent RNA helicase DDX48|ATP-dependent RNA helicase eIF4A-3|DEAD (Asp-Glu-Ala-Asp) box polypeptide 48|DEAD box protein 48|NMP 265|eIF-4A-III|eIF4A-III|eukaryotic initiation factor 4A-III|eukaryotic initiation factor 4A-like NUK-34|eukaryotic translation initiation factor 4A|hNMP 265|nuclear matrix protein 265 EIF4A3 OGG:3000009804 Bin Zhao, Yue Liu, Oliver He MAS20 MOM19 TOM20 WEB: http://www.ncbi.nlm.nih.gov/gene TOMM20 translocase of outer mitochondrial membrane 20 homolog (yeast) 9804 RP4-597N16.2 1q42 9606 1 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 14557246); GO_0005739 (EC: IDA); GO_0005742 (EC: NAS, PMID: 7498524); GO_0005742 (EC: TAS, PMID: 14557246); GO_0006626 (EC: IDA, PMID: 14557246); GO_0006626 (EC: TAS); GO_0015450 (EC: IDA, PMID: 14557246); GO_0016021 (EC: IEA); GO_0044267 (EC: TAS); GO_0051082 (EC: IDA, PMID: 14557246); GO_0071806 (EC: IDA, PMID: 14557246) PMID: 7498524; 7584026; 7584028; 7589431; 9119086; 9211931; 9748310; 9756929; 10548729; 10980201; 10982837; 11027586; 11913975; 12477932; 14557246; 14699115; 15489334; 15644312; 15733919; 16169070; 16710414; 17081983; 18029348; 19322201; 20686565; 20877624; 21771790; 21890473; 21906983; 21963094; 22280891; 22610502; 22939629; 23000965; 23165776; 23251661; 23275563; 23885119; 24250222 translocase of outer mitochondrial membrane 20 homolog (yeast) Ensembl:ENSG00000173726 HGNC:20947 HPRD:03507 MIM:601848 Vega:OTTHUMG00000039619 Other designations: mitochondrial 20 kDa outer membrane protein|mitochondrial import receptor subunit TOM20 homolog|outer mitochondrial membrane receptor Tom20|translocase of outer mitochondrial membrane 20 homolog type II TOMM20 OGG:3000009829 Bin Zhao, Yue Liu, Oliver He DJC6 PARK19 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC6 DnaJ (Hsp40) homolog, subfamily C, member 6 9829 1p31.3 9606 1 GO_0004725 (EC: IEA); GO_0005829 (EC: TAS); GO_0006892 (EC: TAS); GO_0017124 (EC: IEA); GO_0061024 (EC: TAS) PMID:8524399; 9455477; 9455484; 11031247; 11147971; 11252894; 11470803; 12477932; 12732633; 15342556; 15489334; 15502813; 16710414; 18489706; 19165527; 19851296; 20198315; 22216198; 22365833; 22563501; 22647716; 23211418 DnaJ (Hsp40) homolog, subfamily C, member 6 Ensembl:ENSG00000116675 HGNC:15469 HPRD:16326 MIM:608375 Vega:OTTHUMG00000009066 Other designations: DnaJ (Hsp40) homolog, subfamily B, member 6|auxilin|putative tyrosine-protein phosphatase auxilin DNAJC6 OGG:3000009871 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene SEC24D SEC24 family member D 9871 4q26 9606 4 Official from a nomenclature committee GO_0000139 (EC: IEA); GO_0002474 (EC: TAS); GO_0003674 (EC: ND); GO_0005789 (EC: TAS); GO_0005829 (EC: TAS); GO_0006886 (EC: IEA); GO_0006888 (EC: NAS, PMID: 10329445); GO_0006888 (EC: TAS); GO_0008270 (EC: IEA); GO_0012507 (EC: TAS); GO_0018279 (EC: TAS); GO_0019886 (EC: TAS); GO_0030127 (EC: NAS, PMID: 10329445); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS); GO_0044281 (EC: TAS); GO_0048208 (EC: TAS); GO_0048471 (EC: IEA); GO_0061024 (EC: TAS) PMID: 9872452; 10075675; 10329445; 11031247; 11252894; 12477932; 14702039; 15231748; 15580264; 16189514; 16344560; 17210573; 20332099; 20379614; 20889976; 21890473; 21906983; 22404651; 22863883; 22939629; 24250222 SEC24 family member D Other designations: SEC24 family, member D|SEC24 related gene family, member D|SEC24-related protein D|protein transport protein Sec24D SEC24D OGG:3000009891 Bin Zhao, Yue Liu, Oliver He ARK5 WEB: http://www.ncbi.nlm.nih.gov/gene NUAK1 NUAK family, SNF1-like kinase, 1 9891 12q23.3 9606 12 Official from a nomenclature committee GO_0002039 (EC: IPI); GO_0004674 (EC: IDA, PMID: 19927127); GO_0005515 (EC: IPI, PMID: 19927127); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005737 (EC: IDA); GO_0006974 (EC: IEA); GO_0007155 (EC: IEA); GO_0015630 (EC: IDA); GO_0030155 (EC: IDA); GO_0035507 (EC: IDA); GO_0042127 (EC: TAS); GO_0046872 (EC: IEA); GO_2000772 (EC: IDA, PMID: 19927127) PMID: 9628581; 12409306; 12477932; 13679856; 14702039; 14976552; 15060171; 15273717; 15354411; 16044163; 16306228; 16488889; 17353931; 18254724; 19322201; 19927127; 20354225; 20602751; 20978832; 21317932; 21750233; 21832049; 22105900; 22460906; 23063350; 23080069; 23215946; 23419831; 23516026; 23934065; 23940030 NUAK family, SNF1-like kinase, 1 Ensembl:ENSG00000074590 HGNC:14311 HPRD:12171 MIM:608130 Vega:OTTHUMG00000169763 Other designations: AMP-activated protein kinase family member 5|AMPK-related protein kinase 5|NUAK family SNF1-like kinase 1|omphalocele kinase 1 NUAK1 OGG:3000009926 Bin Zhao, Yue Liu, Oliver He FAM34A FAM34A1 NET8 WEB: http://www.ncbi.nlm.nih.gov/gene LPGAT1 lysophosphatidylglycerol acyltransferase 1 9926 1q32 9606 1 Official from a nomenclature committee GO_0003674 (EC: ND); GO_0005737 (EC: IDA, PMID: 10942595); GO_0005789 (EC: TAS); GO_0006644 (EC: TAS); GO_0008150 (EC: ND); GO_0016021 (EC: IEA); GO_0016746 (EC: IEA); GO_0036148 (EC: TAS); GO_0044281 (EC: TAS); GO_0046474 (EC: TAS) PMID: 9039502; 9637538; 10942595; 12477932; 15485873; 15489334; 17207965; 19322201; 21890473; 21903422; 21906983; 23362303; 23464991; 23505186 lysophosphatidylglycerol acyltransferase 1 Ensembl:ENSG00000123684 HGNC:28985 HPRD:14304 MIM:610473 Vega:OTTHUMG00000037120 Other designations: acyl-CoA:lysophosphatidylglycerol acyltransferase 1|family with sequence similarity 34, member A LPGAT1 OGG:3000009939 Bin Zhao, Yue Liu, Oliver He BOV-1A BOV-1B BOV-1C C1DELq21.1 DEL1q21.1 MDS014 RBM8 RBM8B TAR Y14 ZNRP ZRNP1 WEB: http://www.ncbi.nlm.nih.gov/gene RBM8A RNA binding motif protein 8A 9939 HSPC114 1q21.1 9606 1 Official from a nomenclature committee GO_0000166 (EC: IEA); GO_0000184 (EC: IMP, PMID: 16209946); GO_0000184 (EC: TAS); GO_0000381 (EC: IMP); GO_0000398 (EC: IC, PMID: 11991638); GO_0000398 (EC: TAS); GO_0003723 (EC: NAS, PMID: 11013075); GO_0003729 (EC: NAS, PMID: 11030346); GO_0005515 (EC: IPI, PMID: 10662555); GO_0005634 (EC: IDA); GO_0005634 (EC: NAS, PMID: 11013075); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: NAS, PMID: 11030346); GO_0005829 (EC: TAS); GO_0006366 (EC: TAS); GO_0006369 (EC: TAS); GO_0006406 (EC: TAS); GO_0006417 (EC: IEA); GO_0008380 (EC: TAS); GO_0010467 (EC: TAS); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0016607 (EC: IEA); GO_0031124 (EC: TAS); GO_0035145 (EC: IDA, PMID: 16601204); GO_0044822 (EC: IDA); GO_0071013 (EC: IDA, PMID: 11991638) PMID: 9222511; 9933612; 10662555; 11004516; 11013075; 11030346; 11042152; 11118221; 11447110; 11546873; 11546874; 11696323; 11707068; 11707413; 11991638; 12054603; 12093754; 12226669; 12477932; 12718880; 12730685; 12781131; 12944400; 14625303; 14730019; 15302935; 15489334; 15635413; 16083285; 16100109; 16159877; 16170325; 16189514; 16209946; 16303743; 16344560; 16452507; 16501559; 16601204; 16931718; 16964243; 17081983; 17456004; 18026120; 18029348; 18243119; 18503751; 19254694; 19410547; 19417104; 19471022; 19615732; 20098747; 20301781; 20371770; 21139048; 21145460; 21209085; 21832049; 22355610; 22365833; 22366785; 22939629; 22944692; 23084401; 23115303; 23602568; 23817415; 23940030; 23970407; 24244333; 24457600 RNA binding motif protein 8A Ensembl:ENSG00000131795 HGNC:9905 HPRD:05609 MIM:605313 Vega:OTTHUMG00000013736 Other designations: BOV-1|RNA binding motif protein 8B|RNA-binding motif protein 8A|RNA-binding protein 8A|RNA-binding protein Y14|binder of OVCA1-1|ribonucleoprotein RBM8|ribonucleoprotein RBM8A RBM8A OGG:3000009965 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene FGF19 fibroblast growth factor 19 9965 UNQ334/PRO533 11q13.1 9606 11 Official from a nomenclature committee GO_0001755 (EC: IEA); GO_0005104 (EC: IPI, PMID: 10525310); GO_0005515 (EC: IPI, PMID: 18829467); GO_0005576 (EC: TAS); GO_0007173 (EC: TAS); GO_0007399 (EC: TAS, PMID: 9931477); GO_0007507 (EC: IEA); GO_0008083 (EC: IEA); GO_0008284 (EC: IGI, PMID: 18187602); GO_0008286 (EC: TAS); GO_0008543 (EC: IGI, PMID: 18187602); GO_0008543 (EC: IPI, PMID: 10525310); GO_0008543 (EC: TAS); GO_0038095 (EC: TAS); GO_0045087 (EC: TAS); GO_0046326 (EC: IDA, PMID: 17623664); GO_0046330 (EC: IDA, PMID: 12815072); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0070374 (EC: IDA, PMID: 17623664); GO_0070858 (EC: IDA, PMID: 12815072) PMID: 9931477; 10525310; 10579907; 10652257; 11110663; 11294897; 11956156; 12057932; 12477932; 12792807; 12815072; 12975309; 14730967; 14976145; 15199049; 15340161; 15489334; 16597617; 17000708; 17339340; 17599042; 17623664; 17711860; 18187602; 18559909; 18829467; 19185005; 19233843; 19237543; 19681655; 20013647; 20018895; 20093562; 20453838; 20691689; 21397858; 21436455; 21437243; 21574752; 21653700; 21691104; 21747170; 21953282; 22166511; 22267484; 22396169; 22442730; 22561792; 23038264; 23064887; 23205607; 23329754; 23456506; 23940810; 24321096 fibroblast growth factor 19 Other designations: FGF-19 FGF19 OGG:3000009970 This gene encodes a member of the nuclear receptor superfamily, and is a key regulator of xenobiotic and endobiotic metabolism. The protein binds to DNA as a monomer or a heterodimer with the retinoid X receptor and regulates the transcription of target genes involved in drug metabolism and bilirubin clearance, such as cytochrome P450 family members. Unlike most nuclear receptors, this transcriptional regulator is constitutively active in the absence of ligand but is regulated by both agonists and inverse agonists. Ligand binding results in translocation of this protein to the nucleus, where it activates or represses target gene transcription. These ligands include bilirubin, a variety of foreign compounds, steroid hormones, and prescription drugs. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] https://omim.org/entry/603881 CAR Constitutive Activator Of Retinoid Response Constitutive Androstane Receptor MB67 Nuclear Receptor Subfamily 1 Group I Member 3 NR1I3 OGG:3000009971 nuclear receptor subfamily 1, group H, member 4 RXR-interacting protein 14 bile acid receptor farnesoid X nuclear receptor farnesoid X-activated receptor farnesol receptor HRR-1 retinoid X receptor-interacting protein 14 NR1H4 OGG:3000009972 Bin Zhao, Yue Liu, Oliver He HNUP153 N153 WEB: http://www.ncbi.nlm.nih.gov/gene NUP153 nucleoporin 153kDa 9972 6p22.3 9606 6 Official from a nomenclature committee GO_0000278 (EC: TAS); GO_0003677 (EC: IEA); GO_0005215 (EC: TAS, PMID: 8110839); GO_0005487 (EC: IDA); GO_0005515 (EC: IPI, PMID: 11896061); GO_0005643 (EC: IDA, PMID: 12802065); GO_0005654 (EC: TAS); GO_0005730 (EC: IDA); GO_0005737 (EC: IDA); GO_0005975 (EC: TAS); GO_0007077 (EC: TAS); GO_0008270 (EC: IEA); GO_0008645 (EC: TAS); GO_0010827 (EC: TAS); GO_0015031 (EC: IEA); GO_0015758 (EC: TAS); GO_0016032 (EC: TAS); GO_0017056 (EC: IMP, PMID: 15229283); GO_0019221 (EC: TAS); GO_0031965 (EC: IDA); GO_0034399 (EC: IDA, PMID: 11839768); GO_0042405 (EC: IDA, PMID: 11839768); GO_0042802 (EC: IPI); GO_0043495 (EC: IMP, PMID: 12802065); GO_0044281 (EC: TAS); GO_0044615 (EC: IDA, PMID: 11839768); GO_0046718 (EC: IEA); GO_0046832 (EC: IDA); GO_0051028 (EC: IEA); GO_0051292 (EC: IMP, PMID: 12802065); GO_0055085 (EC: TAS); GO_0075732 (EC: IEA) PMID: 7603572; 8110839; 9114010; 9275187; 9847314; 10069809; 10202161; 10601273; 10629106; 10668806; 10749866; 10891500; 11024021; 11073998; 11238447; 11266456; 11567018; 11574060; 11598013; 11777942; 11839768; 11896061; 12138183; 12163599; 12191473; 12192048; 12228227; 12477932; 12802065; 12894213; 12917407; 14578343; 14718558; 15229283; 15302935; 15522285; 15632149; 15659641; 16133350; 16344560; 16543150; 16964243; 17081983; 17255949; 17314511; 17426026; 17615301; 17916694; 18029348; 18068677; 18187620; 18391951; 18854154; 19158386; 19369352; 19454010; 19471022; 19596686; 19615732; 20126445; 20360068; 20561986; 20658144; 20936779; 21139048; 21145461; 21182205; 21318276; 21327100; 21327106; 21489275; 21555518; 21593146; 21693764; 21858095; 21890473; 21906983; 21963094; 21983083; 22075984; 22082286; 22110128; 22118420; 22174692; 22249246; 22412018; 22505724; 22510057; 22586326; 22939629; 23000965; 23007389; 23251661; 23523133; 23752268 nucleoporin 153kDa Ensembl:ENSG00000124789 HGNC:8062 HPRD:04899 MIM:603948 Vega:OTTHUMG00000014312 Other designations: 153 kDa nucleoporin|nuclear pore complex protein Nup153|nuclear pore complex protein hnup153|nucleoporin Nup153 NUP153 OGG:3000009994 Bin Zhao, Yue Liu, Oliver He CED-4 FLASH RIP25 WEB: http://www.ncbi.nlm.nih.gov/gene CASP8AP2 caspase 8 associated protein 2 9994 RP11-63K6.3 6q15 9606 6 GO_0003677 (EC: IEA); GO_0003714 (EC: IDA, PMID:12477726); GO_0005123 (EC: TAS, PMID:10235259); GO_0005515 (EC: IPI, PMID:12477726); GO_0005634 (EC: IDA, PMID:12477726); GO_0005737 (EC: IDA, PMID:12477726); GO_0005739 (EC: IDA, PMID:17245429); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0006919 (EC: IMP, PMID:17245429); GO_0006919 (EC: ISS); GO_0007049 (EC: IEA); GO_0007165 (EC: TAS, PMID:10235259); GO_0008625 (EC: IMP, PMID:17245429); GO_0008625 (EC: ISS); GO_0008656 (EC: ISS); GO_0016505 (EC: ISS); GO_0016605 (EC: IDA, PMID:17245429); GO_0032184 (EC: IDA); GO_0036337 (EC: IMP, PMID:17245429); GO_0071260 (EC: IEP, PMID:19593445); GO_0097190 (EC: TAS, PMID:10235259) PMID:10235259; 10537104; 10718198; 11340079; 12168954; 12477726; 12477932; 14702039; 15069192; 15342556; 15489334; 15561718; 15592525; 15698540; 15840729; 16627760; 17003125; 17003126; 17245429; 17370265; 17696945; 18038312; 18408764; 18677100; 19406988; 19414860; 19471022; 19546234; 19573080; 19593445; 19615980; 19773279; 19854135; 20109966; 20237496; 20697732; 20801175; 20936779; 21139048; 21245389; 21338522; 21693764; 21696825; 21725362; 21906983; 21988832; 22216762; 22427918; 22595458; 23071092; 23086935; 23673342; 23953914 caspase 8 associated protein 2 HGNC:1510 HPRD:06048 MIM:606880 Other designations: CASP8 associated protein 2|CASP8-associated protein 2|FLASH homolog RIP25|FLICE associated huge|FLICE-associated huge protein|human FLASH CASP8AP2 OGG:3000010005 Bin Zhao, Yue Liu, Oliver He HNAACTE PTE-1 PTE-2 PTE1 PTE2 hACTE-III hTE WEB: http://www.ncbi.nlm.nih.gov/gene ACOT8 acyl-CoA thioesterase 8 10005 RP3-337O18.2 20q13.12 9606 20 GO_0005102 (EC: IPI); GO_0005515 (EC: IPI); GO_0005739 (EC: IEA); GO_0005782 (EC: IDA, PMID:10092594); GO_0005782 (EC: IMP, PMID:14709540); GO_0005782 (EC: TAS); GO_0006637 (EC: IDA, PMID:9299485); GO_0006699 (EC: TAS); GO_0008206 (EC: TAS); GO_0016032 (EC: IEA); GO_0016290 (EC: IDA, PMID:9299485); GO_0016559 (EC: IDA, PMID:15194431); GO_0033540 (EC: TAS); GO_0033559 (EC: TAS); GO_0033882 (EC: IEA); GO_0036109 (EC: TAS); GO_0043649 (EC: IDA, PMID:16141203); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0047617 (EC: IDA, PMID:10092594); GO_0052815 (EC: IDA, PMID:9299485) PMID:9153233; 9299485; 10092594; 10799608; 10807905; 10944470; 11549316; 11755680; 11780052; 12477932; 14702039; 14709540; 15194431; 15489334; 16009940; 16103133; 16141203; 16335799; 16756494; 16940157; 17314511; 17624024; 20178365; 21139048; 21824805; 22002062; 22190034; 22810585; 23540296; 24457600 acyl-CoA thioesterase 8 Ensembl:ENSG00000101473 HGNC:15919 HPRD:06998 MIM:608123 Vega:OTTHUMG00000033045 Other designations: HIV-Nef associated acyl-CoA thioesterase|acyl-coenzyme A thioesterase 8|choloyl-CoA hydrolase|choloyl-coenzyme A thioesterase|long-chain fatty-acyl-CoA hydrolase|palmitoyl-CoA hydrolase|peroxisomal acyl-CoA thioesterase 1|peroxisomal acyl-coenzyme A thioester hydrolase 1|peroxisomal long-chain acyl-CoA thioesterase 1|thioesterase II|thioesterase III ACOT8 OGG:3000010018 Bin Zhao, Yue Liu, Oliver He BAM BIM BOD WEB: http://www.ncbi.nlm.nih.gov/gene BCL2L11 BCL2-like 11 (apoptosis facilitator) 10018 2q13 9606 2 Official from a nomenclature committee GO_0001701 (EC: IEA); GO_0001782 (EC: IEA); GO_0001783 (EC: IEA); GO_0001822 (EC: IEA); GO_0002262 (EC: IEA); GO_0005515 (EC: IPI, PMID: 14596824); GO_0005741 (EC: TAS); GO_0005829 (EC: IDA); GO_0005829 (EC: TAS); GO_0005874 (EC: IDA, Qualifier: colocalizes_with); GO_0006915 (EC: TAS, PMID: 10381623); GO_0006919 (EC: IDA); GO_0007160 (EC: IEA); GO_0007283 (EC: IEA); GO_0007420 (EC: IEA); GO_0008017 (EC: IDA, Qualifier: contributes_to); GO_0008017 (EC: IEA); GO_0008584 (EC: IEA); GO_0008630 (EC: IDA, PMID: 11546872); GO_0012505 (EC: IEA); GO_0019898 (EC: IEA); GO_0030879 (EC: IEA); GO_0032464 (EC: IDA); GO_0034976 (EC: IDA); GO_0035148 (EC: IEA); GO_0042475 (EC: IEA); GO_0043029 (EC: IEA); GO_0043065 (EC: IMP, PMID: 17289999); GO_0043065 (EC: TAS); GO_0043280 (EC: IEA); GO_0043525 (EC: IEA); GO_0043583 (EC: IEA); GO_0045787 (EC: IEA); GO_0046620 (EC: IEA); GO_0048011 (EC: TAS); GO_0048066 (EC: IEA); GO_0048070 (EC: IEA); GO_0048536 (EC: IEA); GO_0048538 (EC: IEA); GO_0048563 (EC: IEA); GO_0060139 (EC: IEA); GO_0060154 (EC: IEA); GO_0070242 (EC: IEA); GO_0090200 (EC: IGI); GO_0090200 (EC: IMP, PMID: 17289999); GO_0097140 (EC: IDA); GO_0097141 (EC: IDA); GO_0097190 (EC: TAS); GO_0097192 (EC: IEA); GO_0097193 (EC: TAS); GO_1900740 (EC: TAS); GO_1902110 (EC: IEA); GO_1902263 (EC: IEA); GO_2000271 (EC: IDA, PMID: 11997495); GO_2001244 (EC: IMP); GO_2001244 (EC: TAS) PMID: 8918887; 8929531; 9430630; 9463381; 9731710; 10198631; 10381623; 10576740; 10837489; 11050388; 11210187; 11301022; 11435715; 11546872; 11583631; 11734221; 11859372; 11997495; 12019181; 12095614; 12118373; 12198137; 12376548; 12388545; 12477932; 12486001; 12591950; 12787561; 12818176; 12844146; 14527951; 14555991; 14561217; 14596824; 14676826; 14681225; 14732682; 14764673; 14769789; 14970329; 14996839; 15014070; 15030401; 15096481; 15146197; 15147734; 15193260; 15378010; 15459900; 15486195; 15489334; 15509554; 15653751; 15661735; 15688014; 15694340; 15711598; 15721256; 15728578; 15731037; 15731089; 15767553; 15824087; 15843898; 15899862; 15989957; 16022280; 16051596; 16091744; 16148027; 16183168; 16213503; 16260615; 16282323; 16373335; 16476732; 16478725; 16697956; 16773715; 16810067; 16888645; 16951744; 17051334; 17062728; 17067554; 17074758; 17105963; 17151701; 17158029; 17188240; 17203211; 17207965; 17218274; 17251431; 17276340; 17289999; 17486061; 17499214; 17525735; 17531220; 17538248; 17637819; 17653091; 17686764; 17692808; 17698840; 17716672; 17717606; 17927446; 18006817; 18063582; 18064628; 18089817; 18165867; 18182577; 18195012; 18246127; 18251703; 18345036; 18348176; 18354037; 18391004; 18398508; 18413764; 18420585; 18508762; 18549468; 18651223; 18668139; 18677096; 18715233; 18715501; 18758461; 18806830; 18812174; 18925930; 18949058; 18981303; 19050264; 19052714; 19064725; 19100522; 19101511; 19141860; 19148187; 19150432; 19285955; 19300516; 19305426; 19308286; 19330811; 19332026; 19336552; 19403302; 19407828; 19494111; 19541822; 19573080; 19574221; 19587239; 19622586; 19622774; 19641506; 19737817; 19773279; 19773546; 19805519; 19850739; 19881544; 19893569; 19914305; 20010785; 20066663; 20074640; 20082325; 20086250; 20160166; 20206402; 20231287; 20237869; 20332261; 20348947; 20404322; 20431602; 20697841; 20700448; 20705940; 20819778; 20821734; 20841506; 20855536; 20861305; 20877573; 20878914; 20885957; 20959405; 21041309; 21130142; 21148306; 21148799; 21151127; 21247487; 21333317; 21339291; 21367852; 21375523; 21378313; 21415216; 21478148; 21481848; 21507240; 21533175; 21555518; 21613222; 21625639; 21655183; 21659544; 21671007; 21673341; 21729544; 21732363; 21808067; 21832049; 21899728; 21924351; 21937453; 21958719; 21984578; 21988832; 22071694; 22076535; 22081075; 22093624; 22131152; 22145099; 22160382; 22245094; 22270368; 22349704; 22388891; 22391963; 22426421; 22430213; 22516966; 22572381; 22609401; 22622039; 22628193; 22645134; 22742832; 22762551; 22788963; 22802411; 22819074; 22895567; 22905229; 23012423; 23047821; 23138847; 23152053; 23152504; 23235460; 23243017; 23270470; 23295054; 23301543; 23358890; 23382048; 23394612; 23402819; 23441183; 23500081; 23532334; 23633923; 23648111; 23681223; 23737756; 23770605; 23824909; 23874387; 23912711; 24074954; 24227856; 24239173 BCL2-like 11 (apoptosis facilitator) Ensembl:ENSG00000153094 HGNC:994 HPRD:04828 MIM:603827 Vega:OTTHUMG00000131256 Other designations: bcl-2 interacting mediator of cell death|bcl-2 interacting protein Bim|bcl-2-like protein 11|bcl-2-related ovarian death agonist BCL2L11 OGG:3000010020 Bin Zhao, Yue Liu, Oliver He DMRV GLCNE IBM2 NM Uae1 WEB: http://www.ncbi.nlm.nih.gov/gene GNE glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase 10020 9p13.3 9606 9 Official from a nomenclature committee GO_0005524 (EC: IEA); GO_0005737 (EC: TAS, PMID: 9305888); GO_0005829 (EC: IEA); GO_0006045 (EC: IEA); GO_0006047 (EC: IEA); GO_0006054 (EC: TAS, PMID: 9305888); GO_0007155 (EC: TAS, PMID: 10334995); GO_0008761 (EC: IEA); GO_0009103 (EC: IEA); GO_0009384 (EC: IEA); GO_0016787 (EC: IEA); GO_0046380 (EC: IEA); GO_0046835 (EC: TAS, PMID: 9305888); GO_0046872 (EC: IEA) PMID: 2443758; 2808337; 8439453; 8789455; 8889548; 9305887; 9305888; 10330343; 10334995; 10356312; 10431835; 11326336; 11528398; 11749051; 11916006; 12177386; 12325084; 12409274; 12473753; 12473769; 12473780; 12477932; 12497639; 12612874; 12743242; 12811782; 12913203; 12921793; 12927803; 14707127; 14972325; 15136692; 15146476; 15164053; 15342556; 15489334; 15670773; 15748884; 15833430; 15987957; 16810679; 16847058; 17118363; 17597614; 17698786; 17704511; 17718674; 18029348; 18373408; 18560563; 18653764; 18698493; 18815882; 19322201; 19841673; 19845164; 19917666; 20059379; 20175955; 20300792; 20301343; 20301439; 20346669; 21131200; 21139048; 21584309; 21708040; 21868336; 21906983; 21910480; 21963094; 22049060; 22196754; 22231866; 22343627; 22349865; 22507750; 22863883; 22883483; 23000965; 23238814; 23437777; 23549799; 24005727 glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase Ensembl:ENSG00000159921 HGNC:23657 HPRD:04825 MIM:603824 Vega:OTTHUMG00000019899 Other designations: N-acylmannosamine kinase|UDP-GlcNAc-2-epimerase/ManAc kinase|UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase|UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase|bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase GNE OGG:3000010049 Bin Zhao, Yue Liu, Oliver He DJ4 DnaJ HHDJ1 HSJ-2 HSJ2 LGMD1D LGMD1E MRJ MSJ-1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6 10049 tcag7.555 7q36.3 9606 7 GO_0001671 (EC: IDA, PMID:11896048); GO_0003677 (EC: IEA); GO_0005515 (EC: IPI, PMID:10954706); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0006457 (EC: IDA, PMID:11896048); GO_0030018 (EC: IDA); GO_0030036 (EC: IEA); GO_0030198 (EC: IEA); GO_0031072 (EC: IDA, PMID:10954706); GO_0032781 (EC: IDA, PMID:11896048); GO_0034504 (EC: IEA); GO_0043154 (EC: IDA, PMID:11896048); GO_0045109 (EC: IDA, PMID:10954706); GO_0045892 (EC: IEA); GO_0048471 (EC: IDA, PMID:10954706); GO_0051087 (EC: IDA, PMID:11896048); GO_0060710 (EC: IEA); GO_0060715 (EC: IEA); GO_0060717 (EC: IEA) PMID:8125298; 10319584; 10954706; 11076863; 11147971; 11230166; 11256614; 11896048; 12069690; 12477932; 12690205; 12853948; 12974469; 14702039; 15182641; 15342353; 15489334; 15489336; 16196087; 16260608; 16381901; 16919237; 17081983; 17314511; 18029348; 18163532; 18184612; 18328103; 18373498; 18457437; 18624398; 18976975; 19002655; 20020773; 20159555; 20301582; 20301672; 20308539; 20372789; 20522561; 21139048; 21145461; 21832049; 21890473; 21906983; 21963094; 21988832; 22334415; 22366786; 22455953; 22504047; 22505724; 22710984; 23000965; 23133382; 23394708; 23455922; 23612975; 23667531; 23752268; 24047968; 24250222 DnaJ (Hsp40) homolog, subfamily B, member 6 Ensembl:ENSG00000105993 HGNC:14888 HPRD:07107 MIM:611332 Vega:OTTHUMG00000157242 Other designations: DnaJ-like 2 protein|dnaJ homolog subfamily B member 6|heat shock protein J2|limb girdle muscular dystrophy 1D (autosomal dominant) DNAJB6 OGG:3000010053 Bin Zhao, Yue Liu, Oliver He AP1-mu2 HSMU1B MU-1B MU1B mu2 WEB: http://www.ncbi.nlm.nih.gov/gene AP1M2 adaptor-related protein complex 1, mu 2 subunit 10053 19p13.2 9606 19 Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0005765 (EC: TAS); GO_0005829 (EC: TAS); GO_0006605 (EC: TAS, PMID: 10338135); GO_0006892 (EC: TAS); GO_0006903 (EC: TAS, PMID: 10338135); GO_0016032 (EC: TAS); GO_0019886 (EC: TAS); GO_0030131 (EC: IEA); GO_0030659 (EC: TAS); GO_0030665 (EC: IEA); GO_0032588 (EC: TAS); GO_0050690 (EC: TAS); GO_0061024 (EC: TAS) PMID: 7569928; 8125298; 8810314; 9714795; 9794796; 9882340; 10338135; 10535737; 10640811; 10887964; 11031247; 11157985; 11222723; 11252894; 11573956; 11694590; 12010461; 12086608; 12134076; 12477932; 14702039; 15182197; 15489334; 15569716; 16189514; 16343431; 16574660; 17145811; 17207965; 17220478; 17261850; 17381423; 18356317; 21048031; 21139048; 21163940; 21762802; 21890473; 21906983; 23000965; 23956138 adaptor-related protein complex 1, mu 2 subunit Ensembl:ENSG00000129354 HGNC:558 HPRD:06296 MIM:607309 Vega:OTTHUMG00000180584 Other designations: AP-1 complex subunit mu-2|AP-mu chain family member mu1B|HA1 47 kDa subunit 2|adaptor protein complex AP-1 mu-2 subunit|adaptor protein complex AP-1 subunit mu-2|adaptor-related protein complex 1 mu-2 subunit|adaptor-related protein complex 1 subunit mu-2|clathrin assembly protein complex 1 medium chain 2|clathrin assembly protein complex 1 mu-2 medium chain 2|clathrin coat assembly protein AP47 2|clathrin coat associated protein AP47 2|clathrin-associated adaptor medium chain mu2|golgi adaptor AP-1 47 kDa protein|golgi adaptor HA1/AP1 adaptin mu-2 subunit|mu-adaptin 2|mu1B-adaptin AP1M2 OGG:3000010125 Bin Zhao, Yue Liu, Oliver He CALDAG-GEFI CALDAG-GEFII RASGRP V hRasGRP1 WEB: http://www.ncbi.nlm.nih.gov/gene RASGRP1 RAS guanyl releasing protein 1 (calcium and DAG-regulated) 10125 15q14 9606 15 Official from a nomenclature committee GO_0000139 (EC: IEA); GO_0001816 (EC: IEA); GO_0002437 (EC: IEA); GO_0005085 (EC: TAS); GO_0005509 (EC: IEA); GO_0005789 (EC: IEA); GO_0005829 (EC: TAS); GO_0005886 (EC: TAS); GO_0007165 (EC: TAS, PMID: 9789079); GO_0007265 (EC: TAS, PMID: 9582122); GO_0007596 (EC: TAS); GO_0008289 (EC: TAS, PMID: 9582122); GO_0014066 (EC: IEA); GO_0016020 (EC: TAS, PMID: 9582122); GO_0030154 (EC: IEA); GO_0030168 (EC: TAS); GO_0032252 (EC: IEA); GO_0032862 (EC: IEA); GO_0038095 (EC: TAS); GO_0042629 (EC: IEA); GO_0043303 (EC: IEA); GO_0045087 (EC: TAS); GO_0047496 (EC: IEA) PMID: 9582122; 9789079; 10087292; 11257115; 12477932; 12845332; 14583629; 15829980; 16344560; 17190838; 17283063; 17353931; 17576779; 17658605; 17702895; 17878389; 18711365; 18760455; 18840781; 19058789; 19100522; 19465406; 19960345; 20467438; 20670164; 21815871; 21829393; 21856938; 21966541; 21968647; 21976405; 22116551; 22939629; 22961080; 23128233 RAS guanyl releasing protein 1 (calcium and DAG-regulated) Ensembl:ENSG00000172575 HGNC:9878 HPRD:04909 MIM:603962 Vega:OTTHUMG00000172379 Other designations: RAS guanyl nucleotide-releasing protein 1|RAS guanyl-releasing protein 1|calcium and DAG-regulated guanine nucleotide exchange factor II|guanine nucleotide exchange factor, calcium- and DAG-regulated, Rap1A|ras activator RasGRP RASGRP1 OGG:3000010209 Bin Zhao, Yue Liu, Oliver He A121 EIF-1 EIF1A ISO1 SUI1 WEB: http://www.ncbi.nlm.nih.gov/gene EIF1 eukaryotic translation initiation factor 1 10209 17q21.2 9606 17 GO_0003743 (EC: NAS, PMID:10347211); GO_0005737 (EC: TAS, PMID:10347211); GO_0006446 (EC: TAS, PMID:10347211); GO_0006950 (EC: NAS, PMID:10347211); GO_0008135 (EC: TAS, PMID:10347211); GO_0009048 (EC: IEA); GO_0044822 (EC: IDA) PMID:7904817; 8889549; 10208429; 10228174; 10347211; 10754390; 11073994; 12477932; 15489334; 15592455; 16169070; 20921384; 21139048; 21832049; 21890473; 21900206; 21906983; 21963094; 22053931; 22505724; 22813744; 22939629; 23000965; 23293029; 24250222 eukaryotic translation initiation factor 1 HGNC:3249 HPRD:15449 Other designations: protein translation factor SUI1 homolog|sui1iso1 EIF1 OGG:3000010218 Bin Zhao, Yue Liu, Oliver He AngX CDT6 dJ647M16.1 WEB: http://www.ncbi.nlm.nih.gov/gene ANGPTL7 angiopoietin-like 7 10218 RP4-647M16.2 1p36 9606 1 GO_0005576 (EC: IEA); GO_0006979 (EC: TAS, PMID:8026862) PMID:8026862; 8144038; 9727400; 11426320; 11682471; 12107410; 12477932; 12975309; 15340161; 15489334; 16710414; 17695521; 18421092; 21199193; 21697133; 21832049 angiopoietin-like 7 Ensembl:ENSG00000171819 HGNC:24078 HPRD:10818 Vega:OTTHUMG00000002002 Other designations: angiopoietin-like factor (CDT6)|angiopoietin-like protein 7|angiopoietin-related protein 7|cornea-derived transcript 6 protein ANGPTL7 OGG:3000010243 Bin Zhao, Yue Liu, Oliver He GEPH GPH GPHRYN HKPX1 MOCODC WEB: http://www.ncbi.nlm.nih.gov/gene GPHN gephyrin 10243 14q23.3 20140408 9606 14 protein-coding Official from a nomenclature committee GO_0005524 (EC: IEA); GO_0005737 (EC: IEA); GO_0005856 (EC: IEA); GO_0005886 (EC: TAS); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0006777 (EC: IEA); GO_0007529 (EC: IEA); GO_0016740 (EC: TAS); GO_0030054 (EC: IEA); GO_0032324 (EC: TAS); GO_0044281 (EC: TAS); GO_0045211 (EC: IEA); GO_0046872 (EC: IEA); GO_0061598 (EC: IEA); GO_0061599 (EC: IEA) PMID: 1319186; 1657993; 7546736; 9473484; 9990024; 10037506; 10325225; 10607391; 10718198; 10839351; 10900017; 10947798; 11095995; 11418245; 11554796; 11727829; 12097491; 12477932; 12535948; 12684523; 12754701; 12967995; 14622920; 14751928; 14760703; 15489334; 16964243; 17293395; 17347650; 18315564; 18334916; 18403029; 19615732; 19874574; 19913121; 20206270; 20301437; 20360068; 20379614; 20468064; 20622020; 20628086; 21071388; 21094642; 21139048; 21404332; 21726808; 21829170; 21988832; 22270318; 22778260; 22863883; 23077067; 23290196; 23393157; 23408424; 24128675; 24297911 gephyrin Ensembl:ENSG00000171723 HGNC:15465 HPRD:04893 MIM:603930 Vega:OTTHUMG00000029785 GPHN OGG:3000010273 Bin Zhao, Yue Liu, Oliver He CHIP HSPABP2 NY-CO-7 SDCCAG7 UBOX1 WEB: http://www.ncbi.nlm.nih.gov/gene STUB1 STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase 10273 LA16c-313D11.6 16p13.3 9606 16 Official from a nomenclature committee GO_0000151 (EC: IDA, PMID: 16275660); GO_0000209 (EC: IDA, PMID: 15781469); GO_0000209 (EC: IMP, PMID: 19713937); GO_0004842 (EC: IDA, PMID: 15466472); GO_0004842 (EC: IMP, PMID: 19713937); GO_0004842 (EC: TAS, PMID: 16307917); GO_0005515 (EC: IPI, PMID: 11146632); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA); GO_0006281 (EC: IEA); GO_0006511 (EC: IMP, PMID: 19713937); GO_0006515 (EC: IDA, PMID: 16831871); GO_0007179 (EC: TAS); GO_0019899 (EC: IPI, PMID: 16280320); GO_0019900 (EC: IPI, PMID: 17512523); GO_0030512 (EC: TAS); GO_0030544 (EC: IDA, PMID: 10330192); GO_0030579 (EC: IDA, PMID: 15781469); GO_0030674 (EC: TAS, PMID: 16307917); GO_0030911 (EC: IDA, PMID: 11146632); GO_0031371 (EC: TAS, PMID: 16307917); GO_0031398 (EC: IDA, PMID: 11146632); GO_0031625 (EC: IEA); GO_0031943 (EC: IDA, PMID: 11146632); GO_0032436 (EC: IDA, PMID: 11146632); GO_0034450 (EC: ISS); GO_0042405 (EC: IDA, PMID: 16831871); GO_0042803 (EC: ISS); GO_0043161 (EC: IDA, PMID: 15781469); GO_0045111 (EC: IDA); GO_0046332 (EC: IDA, PMID: 15781469); GO_0051604 (EC: TAS, PMID: 16307917); GO_0051787 (EC: IDA, PMID: 16831871); GO_0051865 (EC: IDA, PMID: 16307917); GO_0051879 (EC: IDA, PMID: 11146632); GO_0070534 (EC: IDA, PMID: 16307917); GO_0071218 (EC: IDA, PMID: 16831871); GO_0090035 (EC: IDA, PMID: 16831871) PMID: 9610721; 10330192; 11146632; 11146634; 11157797; 11557750; 11676916; 11743028; 11805346; 12150907; 12200376; 12239347; 12477932; 12559985; 12574167; 12837759; 14532117; 14532270; 14612456; 14701756; 14962978; 15001357; 15046863; 15107424; 15189447; 15198682; 15215316; 15254225; 15302935; 15358145; 15447663; 15456869; 15466472; 15489334; 15525661; 15538384; 15611333; 15694383; 15708501; 15761032; 15761153; 15781469; 15911628; 15936278; 16037132; 16038411; 16111477; 16135753; 16169070; 16169850; 16207813; 16275660; 16280320; 16293251; 16307917; 16621797; 16682404; 16712791; 16714300; 16720573; 16725394; 16740632; 16809764; 16831871; 16895519; 16964243; 17081983; 17127076; 17157513; 17178836; 17209571; 17239458; 17304350; 17317785; 17324930; 17512523; 17545168; 17595347; 17666403; 17873020; 17875712; 17962192; 17963781; 18042044; 18094050; 18223694; 18292230; 18313385; 18388150; 18411298; 18436529; 18457437; 18485199; 18541707; 18655187; 18678647; 18718056; 18784277; 18818696; 18955503; 18988734; 19011619; 19056735; 19098309; 19103148; 19153604; 19165527; 19196961; 19198599; 19237536; 19240029; 19306926; 19362296; 19406989; 19465479; 19471022; 19478201; 19483080; 19524548; 19536328; 19648119; 19706771; 19713937; 19818709; 19875381; 19892702; 19913553; 19940151; 20029029; 20146531; 20151404; 20349136; 20413784; 20466727; 20588253; 20618441; 20661446; 20675402; 20677910; 20704274; 20724525; 20729196; 20811636; 20924358; 20943656; 20947504; 20947508; 20959453; 20974249; 20974815; 21044950; 21124777; 21139048; 21157430; 21209460; 21220432; 21268072; 21272160; 21293491; 21325980; 21358815; 21360678; 21454478; 21518764; 21549100; 21625540; 21652633; 21710689; 21767636; 21775628; 21793045; 21855799; 21860411; 21898230; 21911421; 21942715; 21988832; 21995445; 22038067; 22090276; 22101235; 22118674; 22128174; 22190034; 22190037; 22254155; 22271573; 22350907; 22350919; 22407479; 22427670; 22433856; 22492994; 22535373; 22543587; 22551455; 22670667; 22734001; 22824801; 22842904; 22863883; 22895543; 22939629; 23023377; 23109339; 23134341; 23237806; 23246967; 23256568; 23271055; 23322406; 23344957; 23410750; 23412384; 23431407; 23455922; 23482560; 23493285; 23554879; 23560854; 23602568; 23629654; 23679257; 23686137; 23729439; 23764847; 23865999; 23880665; 23904609; 23963841; 23973223; 23990462; 24023840; 24043303; 24250222; 24509416 STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase Ensembl:ENSG00000103266 HGNC:11427 HPRD:06232 MIM:607207 Vega:OTTHUMG00000121140 Other designations: CLL-associated antigen KW-8|E3 ubiquitin-protein ligase CHIP|STIP1 homology and U box-containing protein 1|antigen NY-CO-7|carboxy terminus of Hsp70-interacting protein|heat shock protein A binding protein 2 (c-terminal)|serologically defined colon cancer antigen 7 STUB1 OGG:3000010289 Bin Zhao, Yue Liu, Oliver He GC20 WEB: http://www.ncbi.nlm.nih.gov/gene EIF1B eukaryotic translation initiation factor 1B 10289 3p22.1 9606 3 GO_0003743 (EC: IEA); GO_0005575 (EC: ND); GO_0006446 (EC: NAS, PMID:7904817); GO_0044822 (EC: IDA) PMID:7904817; 8125298; 10931946; 12477932; 15489334; 17353931; 19322201; 21139048; 21890473; 21906983; 21988832; 22053931; 22939629; 23000965; 23275563 eukaryotic translation initiation factor 1B Ensembl:ENSG00000114784 HGNC:30792 HPRD:17032 Vega:OTTHUMG00000131388 Other designations: eukaryotic translation initiation factor 1b|protein translation factor SUI1 homolog GC20|translation factor sui1 homolog EIF1B OGG:3000010382 Bin Zhao, Yue Liu, Oliver He DYT4 TUBB4 TUBB5 beta-5 WEB: http://www.ncbi.nlm.nih.gov/gene TUBB4A tubulin, beta 4A class IVa 10382 19p13.3 9606 19 Official from a nomenclature committee GO_0000086 (EC: TAS); GO_0000278 (EC: TAS); GO_0003924 (EC: IEA); GO_0005200 (EC: IEA); GO_0005515 (EC: IPI); GO_0005525 (EC: IEA); GO_0005829 (EC: TAS); GO_0005874 (EC: IDA); GO_0005929 (EC: IEA); GO_0006457 (EC: TAS); GO_0007017 (EC: IEA); GO_0033269 (EC: IEA); GO_0043025 (EC: IEA); GO_0043209 (EC: IEA); GO_0044267 (EC: TAS); GO_0051084 (EC: TAS); GO_0051258 (EC: IEA) PMID: 3782288; 6462917; 6865944; 7790358; 8432555; 8619814; 8653701; 10908577; 11076968; 11120798; 12221128; 12477932; 12486001; 12840015; 12852856; 14702039; 15121898; 15188402; 15324660; 15331610; 15489334; 15691386; 15698476; 16196087; 16303743; 16462731; 16526095; 16565220; 16944923; 17360745; 17620599; 17627938; 18029348; 18553364; 18613978; 18781797; 19167051; 19299461; 19773279; 20171186; 20195357; 20473970; 20639865; 20972266; 21110914; 21139048; 21145461; 21151833; 21525035; 21839816; 21890473; 21906983; 21956287; 21963094; 21987572; 22174317; 22266860; 22268729; 22505724; 22586326; 22797925; 22863883; 23000965; 23142642; 23190606; 23246001; 23349634; 23424103; 23455922; 23463506; 23503679; 23582646; 23595291; 23703321; 23956138 tubulin, beta 4A class IVa Ensembl:ENSG00000104833 HGNC:20774 HPRD:04045 MIM:602662 Vega:OTTHUMG00000181829 Other designations: dystonia 4, torsion (autosomal dominant)|tubulin beta-4 chain|tubulin beta-4A chain|tubulin, beta, 5 TUBB4A OGG:3000010401 Bin Zhao, Yue Liu, Oliver He ZMIZ5 WEB: http://www.ncbi.nlm.nih.gov/gene PIAS3 protein inhibitor of activated STAT, 3 10401 1q21 9606 1 Official from a nomenclature committee GO_0003676 (EC: IEA); GO_0005515 (EC: IPI, PMID: 11060035); GO_0005634 (EC: IEA); GO_0005737 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0008022 (EC: IPI, PMID: 14715251); GO_0008270 (EC: IEA); GO_0009725 (EC: IEA); GO_0010628 (EC: IEA); GO_0015459 (EC: IEA); GO_0016925 (EC: IEA); GO_0016925 (EC: ISS); GO_0019789 (EC: IEA); GO_0019899 (EC: IPI, PMID: 17087506); GO_0030425 (EC: IEA); GO_0033235 (EC: IDA, PMID: 17696781); GO_0045202 (EC: IEA); GO_0045838 (EC: IEA); GO_0047485 (EC: IEA) PMID: 9388184; 9724754; 10319586; 11060035; 11071847; 11117529; 11390395; 11429412; 11477070; 11709556; 12208521; 12387893; 12477932; 12804609; 12869526; 14630083; 14691252; 14702039; 14715251; 15138572; 15140884; 15171715; 15231748; 15489334; 15907835; 16029420; 16098628; 16368885; 16455055; 16522640; 16524884; 16679534; 17032498; 17087506; 17533377; 17565989; 17696781; 17987106; 18037959; 18212042; 18408014; 18550668; 18681895; 19217413; 19308990; 19322201; 19471022; 19569236; 19760037; 19903771; 20159969; 20231901; 20351170; 20516148; 20935639; 20936779; 21288202; 21317457; 21497567; 21532337; 21693764; 21733403; 21900206; 21906983; 21963094; 21988832; 22321011; 22584572; 22649547; 23092970; 23322197; 23704280; 23959540 protein inhibitor of activated STAT, 3 Ensembl:ENSG00000131788 HGNC:16861 HPRD:09068 MIM:605987 Vega:OTTHUMG00000013750 Other designations: E3 SUMO-protein ligase PIAS3|protein inhibitor of activated STAT protein 3|zinc finger, MIZ-type containing 5 PIAS3 OGG:3000010404 Bin Zhao, Yue Liu, Oliver He LDP PGCP WEB: http://www.ncbi.nlm.nih.gov/gene CPQ carboxypeptidase Q 10404 8q22.2 9606 8 Official from a nomenclature committee GO_0004180 (EC: IEA); GO_0005615 (EC: IDA, PMID: 10206990); GO_0005737 (EC: IDA, PMID: 10206990); GO_0005764 (EC: ISS); GO_0005783 (EC: ISS); GO_0005794 (EC: ISS); GO_0006508 (EC: IDA, PMID: 10206990); GO_0006590 (EC: ISS); GO_0042246 (EC: ISS); GO_0042803 (EC: IDA, PMID: 12675526); GO_0043171 (EC: IDA, PMID: 10206990); GO_0046872 (EC: IEA); GO_0070573 (EC: IDA, PMID: 10206990) PMID: 10206990; 12477932; 12591738; 12675526; 16303743; 16344560; 17214548; 20201926; 20379614; 20802479; 23725790; 23728906 carboxypeptidase Q Ensembl:ENSG00000104324 HGNC:16910 HPRD:07140 Vega:OTTHUMG00000164690 Other designations: Ser-Met dipeptidase|aminopeptidase|blood plasma glutamate carboxypeptidase|lysosomal dipeptidase CPQ OGG:3000010417 Bin Zhao, Yue Liu, Oliver He DIL-1 DIL1 M-SPONDIN MINDIN WEB: http://www.ncbi.nlm.nih.gov/gene SPON2 spondin 2, extracellular matrix protein 10417 UNQ435/PRO866 4p16.3 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0005578 (EC: IEA); GO_0007155 (EC: IEA); GO_0007411 (EC: TAS, PMID: 10512675); GO_0045087 (EC: IEA); GO_0046872 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 10512675; 12477932; 12975309; 14702039; 15094111; 15489334; 16303743; 16344560; 16368877; 18239089; 19056867; 19153605; 19903741; 20379614; 21098016; 21632881; 22615945 spondin 2, extracellular matrix protein Ensembl:ENSG00000159674 HGNC:11253 HPRD:16174 MIM:605918 Vega:OTTHUMG00000089002 Other designations: differentially expressed in cancerous and non-cancerous lung cells 1|spondin-2 SPON2 OGG:3000010419 Bin Zhao, Yue Liu, Oliver He HRMT1L5 IBP72 JBP1 SKB1 SKB1Hs WEB: http://www.ncbi.nlm.nih.gov/gene PRMT5 protein arginine methyltransferase 5 10419 14q11.2 9606 14 Official from a nomenclature committee GO_0000122 (EC: IEA); GO_0000387 (EC: IMP, PMID: 17709427); GO_0000387 (EC: TAS); GO_0003682 (EC: IEA); GO_0005515 (EC: IPI, PMID: 16087681); GO_0005634 (EC: IDA); GO_0005634 (EC: NAS, PMID: 18404153); GO_0005737 (EC: IDA); GO_0005829 (EC: IDA, PMID: 18984161); GO_0005829 (EC: TAS); GO_0006351 (EC: IEA); GO_0006355 (EC: IBA); GO_0007088 (EC: TAS, PMID: 9843966); GO_0008168 (EC: IDA, PMID: 15369763); GO_0008283 (EC: TAS, PMID: 9843966); GO_0008469 (EC: IBA); GO_0010467 (EC: TAS); GO_0016070 (EC: TAS); GO_0018216 (EC: IMP, PMID: 17709427); GO_0019918 (EC: IMP, PMID: 17709427); GO_0034660 (EC: TAS); GO_0034709 (EC: IDA, PMID: 18984161); GO_0035243 (EC: IMP, PMID: 17709427); GO_0035246 (EC: IDA, PMID: 15369763); GO_0042118 (EC: IMP); GO_0043021 (EC: IPI, PMID: 17709427); GO_0043985 (EC: NAS, PMID: 18404153) PMID: 9556550; 9843966; 10531356; 10734105; 11152681; 11713266; 11720283; 11747828; 11756452; 12101096; 12358155; 12477932; 12665801; 12718890; 12972618; 14559996; 14583623; 14702039; 15130578; 15324660; 15369763; 15485929; 15489334; 15654770; 15670829; 15701830; 15737618; 16087681; 16169070; 16300736; 16428440; 16699504; 16712789; 16969126; 16980624; 17409432; 17437848; 17452440; 17573539; 17620599; 17627275; 17643375; 17707232; 17709427; 17925232; 17974993; 18029348; 18347060; 18404153; 18562274; 18694959; 18781797; 18984161; 18992153; 19032343; 19086919; 19167051; 19188441; 19234465; 19380743; 19520849; 19738201; 19741270; 20195544; 20360068; 20421892; 20473970; 20495075; 20811636; 20951943; 21081503; 21081666; 21118156; 21139048; 21145461; 21159818; 21262773; 21316606; 21385873; 21592330; 21700716; 21890473; 21906983; 21907836; 21917714; 21963094; 21975038; 21987572; 22143770; 22169276; 22179613; 22193545; 22199349; 22231400; 22266372; 22268729; 22269951; 22354994; 22365833; 22586326; 22708516; 22726390; 22797925; 22863883; 22939629; 22952863; 23071334; 23084401; 23133559; 23184937; 23246001; 23261437; 23292799; 23398456; 23455922; 23455924; 23569248; 23671120; 23862649; 23904475; 23912080; 24121109; 24163370; 24189068 protein arginine methyltransferase 5 Ensembl:ENSG00000100462 HGNC:10894 HPRD:04955 MIM:604045 Vega:OTTHUMG00000028709 Other designations: 72 kDa ICln-binding protein|HMT1 hnRNP methyltransferase-like 5|SKB1 homolog|histone-arginine N-methyltransferase PRMT5|jak-binding protein 1|protein arginine N-methyltransferase 5|shk1 kinase-binding protein 1 homolog PRMT5 OGG:3000010437 Bin Zhao, Yue Liu, Oliver He GILT IFI-30 IP30 WEB: http://www.ncbi.nlm.nih.gov/gene IFI30 interferon, gamma-inducible protein 30 10437 19p13.1 20140408 9606 19 protein-coding Official from a nomenclature committee GO_0005576 (EC: IEA); GO_0005737 (EC: IDA); GO_0005764 (EC: IDA, PMID: 10639150); GO_0005886 (EC: IDA); GO_0016667 (EC: IMP, PMID: 10639150); GO_0019221 (EC: TAS); GO_0019886 (EC: TAS); GO_0030054 (EC: IDA); GO_0042590 (EC: ISS); GO_0043202 (EC: TAS); GO_0043231 (EC: IDA); GO_0048147 (EC: IEA); GO_0050821 (EC: IEA); GO_0060333 (EC: TAS) PMID: 16170; 1069150; 3136170; 10639150; 10852914; 11491538; 12021307; 12198183; 12477932; 18029348; 18343923; 18410276; 19240061; 20668223; 21701784; 23246037 interferon, gamma-inducible protein 30 Ensembl:ENSG00000216490 HGNC:5398 HPRD:05234 MIM:604664 Vega:OTTHUMG00000183373 Other designations: gamma-interferon-inducible lysosomal thiol reductase|gamma-interferon-inducible protein IP-30|interferon gamma-inducible protein 30 preproprotein|legumaturain IFI30 OGG:3000010480 Bin Zhao, Yue Liu, Oliver He B5 PCID1 TANGO7 hfl-B5 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3M eukaryotic translation initiation factor 3, subunit M 10480 GA17 11p13 9606 11 GO_0001731 (EC: IEA); GO_0002183 (EC: IBA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0005515 (EC: IPI, PMID:18599441); GO_0005852 (EC: IDA, PMID:17322308); GO_0006413 (EC: IC, PMID:17322308); GO_0006446 (EC: IEA); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA) PMID:8125298; 12477932; 14702039; 15231747; 15919898; 15919899; 16169070; 17322308; 17353931; 17719568; 18599441; 18781797; 19471022; 19483676; 19615732; 20360068; 20379614; 20508642; 20676407; 20838379; 20972266; 21139048; 21832049; 21890473; 21906983; 21963094; 22022972; 22053931; 22174317; 22190034; 22505724; 22678362; 22863883; 22939629; 23000965; 23402259; 23455922; 23602568 eukaryotic translation initiation factor 3, subunit M HGNC:24460 HPRD:09969 MIM:609641 Other designations: B5 receptor|PCI domain containing 1 (herpesvirus entry mediator)|PCI domain-containing protein 1|dendritic cell protein|eukaryotic translation initiation factor 3 subunit M|fetal lung protein B5|transport and golgi organization 7 homolog EIF3M OGG:3000010525 Bin Zhao, Yue Liu, Oliver He GRP-170 Grp170 HSP12A ORP-150 ORP150 WEB: http://www.ncbi.nlm.nih.gov/gene HYOU1 hypoxia up-regulated 1 10525 11q23.1-q23.3 9606 11 Official from a nomenclature committee GO_0002931 (EC: IEA); GO_0005524 (EC: IEA); GO_0005576 (EC: TAS); GO_0005783 (EC: TAS, PMID: 9020069); GO_0005788 (EC: TAS); GO_0006950 (EC: TAS, PMID: 9020069); GO_0006987 (EC: TAS); GO_0030968 (EC: TAS); GO_0044267 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19199708); GO_0071682 (EC: TAS) PMID: 8125298; 8878445; 9006956; 9020069; 9645760; 10037731; 10837345; 10965054; 11231630; 11690552; 12477932; 12553534; 12754519; 15240565; 15342556; 15952740; 16263699; 16335952; 16543725; 17131193; 17330988; 17353931; 17481612; 18404158; 19106412; 19199708; 19225868; 19812200; 19913121; 20000738; 20626887; 20628086; 21139048; 21296878; 21319273; 21890473; 21903422; 21906983; 22190034; 22268729; 22586326; 22863883; 22939629; 23097496; 23645669; 23757447; 23862649; 24457600 hypoxia up-regulated 1 Ensembl:ENSG00000149428 HGNC:16931 HPRD:03448 MIM:601746 Vega:OTTHUMG00000166354 Other designations: 150 kDa oxygen-regulated protein|170 kDa glucose-regulated protein|hypoxia up-regulated protein 1|oxygen regulated protein (150kD) HYOU1 OGG:3000010539 Bin Zhao, Yue Liu, Oliver He GLRX4 GRX3 GRX4 PICOT TXNL2 TXNL3 WEB: http://www.ncbi.nlm.nih.gov/gene GLRX3 glutaredoxin 3 10539 HUSSY-22 10q26 9606 10 Official from a nomenclature committee GO_0002026 (EC: ISS); GO_0005080 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10636891); GO_0005938 (EC: IEA); GO_0009055 (EC: IEA); GO_0010614 (EC: ISS); GO_0015035 (EC: IEA); GO_0030018 (EC: IEA); GO_0044822 (EC: IDA); GO_0045454 (EC: IEA); GO_0046872 (EC: IEA); GO_0051536 (EC: IEA) PMID: 8125298; 10636891; 11124703; 11774602; 12477932; 14702039; 15231748; 15342556; 15489334; 16169070; 16189514; 16385451; 17353931; 18258855; 18528843; 19471022; 19738201; 19797004; 20170406; 20226171; 20498481; 20800603; 21123948; 21139048; 21160409; 21575136; 21890473; 21900206; 21906983; 22309771; 22623428; 22678362; 22863883; 23000965; 23415866; 23615448; 24250222 glutaredoxin 3 Ensembl:ENSG00000108010 HGNC:15987 HPRD:10153 MIM:612754 Vega:OTTHUMG00000019267 Other designations: PKC-interacting cousin of thioredoxin|PKC-theta-interacting protein|PKCq-interacting protein|glutaredoxin 4|glutaredoxin-3|thioredoxin-like protein 2 GLRX3 OGG:3000010542 Bin Zhao, Yue Liu, Oliver He HBXIP XIP WEB: http://www.ncbi.nlm.nih.gov/gene LAMTOR5 late endosomal/lysosomal adaptor, MAPK and MTOR activator 5 10542 1p13.3 9606 1 Official from a nomenclature committee GO_0005085 (EC: IDA, Qualifier: contributes_to); GO_0005515 (EC: IPI, PMID: 12773388); GO_0005764 (EC: IDA); GO_0005829 (EC: IDA, PMID: 12773388); GO_0008361 (EC: IMP); GO_0009615 (EC: TAS, PMID: 9499022); GO_0019079 (EC: IEA); GO_0032008 (EC: IMP); GO_0032947 (EC: IDA, Qualifier: contributes_to); GO_0043066 (EC: IDA, PMID: 12773388); GO_0043087 (EC: IDA); GO_0043154 (EC: IDA, PMID: 12773388); GO_0061462 (EC: IMP); GO_0071230 (EC: IMP); GO_0071986 (EC: IDA) PMID: 9499022; 11788598; 11925594; 12477932; 12773388; 14578865; 14702039; 15489334; 15955450; 16055925; 16169070; 16176273; 17050029; 17303008; 17428866; 18029348; 18032378; 18158869; 18976975; 19885569; 20811532; 20877624; 21139048; 21343296; 21651858; 21706058; 21988832; 22209835; 22293503; 22740693; 22939629; 22980980; 23266610; 23291272; 23352642; 23494474; 23537647; 23667255 late endosomal/lysosomal adaptor, MAPK and MTOR activator 5 Ensembl:ENSG00000134248 HGNC:17955 HPRD:09773 MIM:608521 Vega:OTTHUMG00000011568 Other designations: HBV X-interacting protein|HBx-interacting protein|hepatitis B virus x interacting protein|hepatitis B virus x-interacting protein (9.6kD)|late endosomal/lysosomal adaptor and MAPK and MTOR activator 5|ragulator complex protein LAMTOR5 LAMTOR5 OGG:3000010553 Bin Zhao, Yue Liu, Oliver He CC3 SDR44U1 TIP30 WEB: http://www.ncbi.nlm.nih.gov/gene HTATIP2 HIV-1 Tat interactive protein 2, 30kDa 10553 11p15.1 9606 11 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0003713 (EC: TAS, PMID: 9482853); GO_0005515 (EC: IPI, PMID: 15282309); GO_0005634 (EC: TAS, PMID: 9482853); GO_0005635 (EC: IDA, PMID: 15282309); GO_0005737 (EC: IDA); GO_0006357 (EC: TAS, PMID: 9482853); GO_0006915 (EC: IEA); GO_0016032 (EC: IEA); GO_0016491 (EC: IEA); GO_0030154 (EC: IEA); GO_0043066 (EC: TAS, PMID: 10611237); GO_0045765 (EC: IDA, PMID: 11313954); GO_0051170 (EC: IDA, PMID: 15282309) PMID: 8125298; 9174052; 9482853; 10395547; 10611237; 10698937; 10892349; 11313954; 12477932; 14695192; 15073177; 15124103; 15282309; 15342556; 15489334; 15493507; 15633220; 15728189; 16615932; 16799960; 17097132; 17997990; 18029348; 18519672; 18528861; 18537194; 18972434; 19010857; 19027726; 19104151; 19349353; 19798571; 19839715; 20374651; 21139048; 21150275; 21252234; 21543106; 21731680; 21890473; 21906983; 21963094; 21987572; 22490293; 22733137; 23000965; 23178973; 23251661; 23800048; 24037692 HIV-1 Tat interactive protein 2, 30kDa Ensembl:ENSG00000109854 HGNC:16637 HPRD:09288 MIM:605628 Vega:OTTHUMG00000166015 Other designations: 30 kDa HIV-1 TAT-interacting protein|HIV-1 TAT-interactive protein 2|Tat-interacting protein (30kD)|oxidoreductase HTATIP2|short chain dehydrogenase/reductase family 44U, member 1 HTATIP2 OGG:3000010580 Bin Zhao, Yue Liu, Oliver He CAP FLAF2 R85FL SH3D5 SH3P12 SORB1 WEB: http://www.ncbi.nlm.nih.gov/gene SORBS1 sorbin and SH3 domain containing 1 10580 RP11-476E15.1 10q23.33 9606 10 Official from a nomenclature committee GO_0001725 (EC: ISS); GO_0003779 (EC: TAS, PMID: 10085297); GO_0005070 (EC: IC, PMID: 11374898); GO_0005070 (EC: ISS, PMID: 9447983); GO_0005158 (EC: IDA, PMID: 11374898); GO_0005515 (EC: IPI, PMID: 11371513); GO_0005634 (EC: IDA, PMID: 11371513); GO_0005829 (EC: ISS, PMID: 9447983); GO_0005829 (EC: TAS); GO_0005899 (EC: IDA, Qualifier: colocalizes_with, PMID: 11374898); GO_0005913 (EC: ISS); GO_0005915 (EC: TAS, PMID: 10085297); GO_0005924 (EC: ISS); GO_0005925 (EC: IEA); GO_0006936 (EC: TAS); GO_0007160 (EC: TAS, PMID: 10085297); GO_0008092 (EC: TAS, PMID: 10085297); GO_0008286 (EC: ISS); GO_0009967 (EC: IC, PMID: 11374898); GO_0009967 (EC: ISS, PMID: 9447983); GO_0015758 (EC: ISS); GO_0016363 (EC: IEA); GO_0019901 (EC: IEA); GO_0032869 (EC: ISS, PMID: 11001060); GO_0043149 (EC: ISS); GO_0045121 (EC: ISS); GO_0045725 (EC: ISS, PMID: 11001060); GO_0046326 (EC: ISS, PMID: 11001060); GO_0046889 (EC: ISS, PMID: 11001060); GO_0048041 (EC: ISS); GO_0090004 (EC: ISS) PMID: 9447983; 9461600; 10085297; 10583506; 10718198; 11001060; 11076863; 11230166; 11371513; 11374898; 11481476; 11532984; 11557983; 11997497; 12079283; 12395215; 12421765; 12477932; 12504111; 12510380; 12650714; 12690089; 12765336; 12849814; 14627618; 14702039; 15031295; 15128873; 15489334; 15489336; 15716063; 15777793; 15939299; 16374509; 16381901; 16385451; 17082770; 17353931; 17462669; 17548467; 18029348; 18394047; 18660489; 19165527; 19282865; 19891780; 20129698; 20201926; 20379614; 20936779; 21041247; 21988832; 22094256; 22235335; 22745667; 23251661; 23382691; 23793025; 23892081; 24255178 sorbin and SH3 domain containing 1 Ensembl:ENSG00000095637 HGNC:14565 HPRD:05587 MIM:605264 Vega:OTTHUMG00000018812 Other designations: Fas-ligand associated factor 2|SH3 domain protein 5|c-Cbl associated protein|ponsin|sorbin and SH3 domain-containing protein 1 SORBS1 OGG:3000010586 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene MAB21L2 mab-21-like 2 (C. elegans) 10586 4q31 9606 4 Official from a nomenclature committee GO_0005634 (EC: IEA); GO_0007399 (EC: TAS, PMID: 10556287); GO_0008284 (EC: IEA); GO_0010172 (EC: IEA); GO_0043010 (EC: IEA) PMID: 10556287; 12477932; 14702039; 17207965; 21832049; 23602568 mab-21-like 2 (C. elegans) Other designations: protein mab-21-like 2 MAB21L2 OGG:3000010611 Bin Zhao, Yue Liu, Oliver He ENH ENH1 LIM WEB: http://www.ncbi.nlm.nih.gov/gene PDLIM5 PDZ and LIM domain 5 10611 L9 4q22 9606 4 Official from a nomenclature committee GO_0003779 (EC: ISS); GO_0005080 (EC: ISS); GO_0005829 (EC: ISS); GO_0008270 (EC: IEA); GO_0014069 (EC: ISS); GO_0015629 (EC: IDA); GO_0016020 (EC: ISS); GO_0030054 (EC: IEA); GO_0042805 (EC: ISS); GO_0043005 (EC: IEA); GO_0045211 (EC: IEA); GO_0051963 (EC: ISS); GO_0061001 (EC: ISS) PMID: 7698749; 8889548; 8940095; 10429367; 10737800; 10833443; 11076863; 11230166; 11256614; 12477932; 12665800; 14743183; 15334068; 15342556; 15346770; 15362566; 15489334; 15489336; 15555569; 16044170; 16189514; 16213469; 16344560; 16381901; 16549780; 16595163; 16713569; 17081983; 17287082; 18021463; 18197271; 18296710; 18456508; 18496208; 18496210; 19328558; 19448850; 19596686; 19636345; 19738201; 19767753; 20564319; 20878950; 21139048; 21266195; 21890473; 21906983; 22118674; 22589738; 22741436; 22863883; 22939629; 23031404; 24457600 PDZ and LIM domain 5 Ensembl:ENSG00000163110 HGNC:17468 HPRD:05799 MIM:605904 Vega:OTTHUMG00000130973 Other designations: PDZ and LIM domain protein 5|enigma homolog|enigma-like LIM domain protein|enigma-like PDZ and LIM domains protein PDLIM5 OGG:3000010635 Bin Zhao, Yue Liu, Oliver He PIR51 WEB: http://www.ncbi.nlm.nih.gov/gene RAD51AP1 RAD51 associated protein 1 10635 12p13.2-p13.1 20140408 9606 12 protein-coding Official from a nomenclature committee GO_0000724 (EC: NAS, PMID: 9396801); GO_0003690 (EC: IDA, PMID: 9396801); GO_0003697 (EC: IDA, PMID: 9396801); GO_0003723 (EC: IDA, PMID: 9396801); GO_0005515 (EC: IPI); GO_0005634 (EC: IC, PMID: 9396801); GO_0006281 (EC: NAS, PMID: 9396801); GO_0010569 (EC: IDA); GO_0071479 (EC: IDA) PMID: 8889548; 9396801; 12477932; 14702039; 14966907; 15489334; 16920159; 17207965; 17996710; 17996711; 18316552; 19615732; 19953087; 20201926; 20558539; 20871616; 21307306; 21832049; 21903585; 22375013; 22452920; 23263487 RAD51 associated protein 1 Ensembl:ENSG00000111247 HGNC:16956 MIM:603070 Vega:OTTHUMG00000168125 Other designations: RAD51-associated protein 1|RAD51-interacting protein RAD51AP1 OGG:3000010670 Bin Zhao, Yue Liu, Oliver He FIP-1 FIP1 RAGA WEB: http://www.ncbi.nlm.nih.gov/gene RRAGA Ras-related GTP binding A 10670 9p22.1 9606 9 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 11073942); GO_0005525 (EC: IDA, PMID: 14660641); GO_0005634 (EC: IDA, PMID: 11073942); GO_0005737 (EC: IDA, PMID: 11073942); GO_0005764 (EC: IDA); GO_0005765 (EC: IDA, PMID: 17897319); GO_0005794 (EC: IDA); GO_0006915 (EC: IEA); GO_0008219 (EC: IDA, PMID: 8995684); GO_0019048 (EC: IDA, PMID: 8995684); GO_0032008 (EC: NAS); GO_0034613 (EC: IMP); GO_0042803 (EC: IDA, PMID: 14660641); GO_0043231 (EC: IDA); GO_0045919 (EC: IDA, PMID: 8995684); GO_0046982 (EC: IPI, PMID: 11073942); GO_0051219 (EC: IDA, PMID: 8995684); GO_0071230 (EC: IMP) PMID: 7499430; 8995684; 9394008; 11073942; 12477932; 14660641; 14749727; 15164053; 15489334; 16189514; 17897319; 18029348; 18497260; 18685082; 19136632; 21816923; 21890473; 21981924; 23000965; 23151878; 23184942 Ras-related GTP binding A Ensembl:ENSG00000155876 HGNC:16963 HPRD:10205 MIM:612194 Vega:OTTHUMG00000019621 Other designations: adenovirus E3 14.7 kDa-interacting protein 1|adenovirus E3-14.7K interacting protein 1|rag A|ras-related GTP-binding protein A RRAGA OGG:3000010741 Bin Zhao, Yue Liu, Oliver He BOG RBBP10 WEB: http://www.ncbi.nlm.nih.gov/gene RBBP9 retinoblastoma binding protein 9 10741 20p11.2 9606 20 Official from a nomenclature committee GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005737 (EC: IDA); GO_0016787 (EC: IEA); GO_0042127 (EC: IEA) PMID: 9697699; 10449909; 11780052; 12296629; 12477932; 12730717; 14702039; 15489334; 18029348; 19004028; 20080647; 21044950; 21139048; 21689726; 21890473; 21933118; 22430187 retinoblastoma binding protein 9 Ensembl:ENSG00000089050 HGNC:9892 HPRD:04217 MIM:602908 Vega:OTTHUMG00000031972 Other designations: B5T overexpressed gene protein|B5T-overexpressed gene protein|RBBP-10|RBBP-9|putative hydrolase RBBP9|retinoblastoma-binding protein 10|retinoblastoma-binding protein 9|retinoma-binding protein 9 RBBP9 OGG:3000010747 Bin Zhao, Yue Liu, Oliver He MAP19 MASP-2 MASP1P1 sMAP WEB: http://www.ncbi.nlm.nih.gov/gene MASP2 mannan-binding lectin serine peptidase 2 10747 1p36.3-p36.2 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0001867 (EC: IDA, PMID: 17182967); GO_0001867 (EC: TAS); GO_0004252 (EC: IDA, PMID: 9087411); GO_0005509 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10946292); GO_0005576 (EC: TAS); GO_0006956 (EC: TAS); GO_0006958 (EC: IEA); GO_0008233 (EC: IDA, PMID: 10946292); GO_0045087 (EC: TAS); GO_0048306 (EC: IPI, PMID: 12421953); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 8018603; 9087411; 9777418; 10092804; 10330290; 10393416; 10639434; 10679061; 10878362; 10925294; 10946292; 11426320; 11532276; 11907111; 12421953; 12477932; 12538697; 12904520; 15117939; 15364579; 15746044; 16029433; 16040602; 16112196; 16344560; 16395704; 16710414; 17045845; 17096357; 17182967; 17252003; 17303612; 17565323; 17614162; 17709141; 17971300; 17984804; 18177377; 18221301; 18295674; 18400978; 18582923; 18596574; 18638656; 18842294; 18849076; 19050632; 19056867; 19234189; 19275590; 19307021; 19344414; 19405982; 19423540; 19737459; 19775369; 19817957; 19913121; 19948975; 20002787; 20042521; 20150204; 20406964; 20438785; 20467438; 20593422; 20628086; 20817870; 21198752; 21203938; 21489885; 21843573; 21871896; 21926545; 21974696; 22071314; 22173059; 22178059; 22236007; 22380611; 22511776; 22691502; 22966085; 23142462; 23220946; 23402018; 23785123; 23861212; 23911397; 23935922; 24227370 mannan-binding lectin serine peptidase 2 Ensembl:ENSG00000009724 HGNC:6902 HPRD:05484 MIM:605102 Vega:OTTHUMG00000002121 Other designations: MBL-associated plasma protein of 19 kD|MBL-associated serine protease 2|mannan-binding lectin serine peptidase 1 pseudogene 1|mannan-binding lectin serine protease 1 pseudogene 1|mannan-binding lectin serine protease 2|mannose-binding protein-associated serine protease 2|small MBL-associated protein MASP2 OGG:3000010769 Bin Zhao, Yue Liu, Oliver He SNK hPlk2 hSNK WEB: http://www.ncbi.nlm.nih.gov/gene PLK2 polo-like kinase 2 10769 5q12.1-q13.2 9606 5 Official from a nomenclature committee GO_0000082 (EC: IMP, PMID: 15242618); GO_0004674 (EC: IDA, PMID: 19001868); GO_0004871 (EC: IMP, PMID: 12761501); GO_0005515 (EC: IPI); GO_0005524 (EC: IEA); GO_0005622 (EC: ISS); GO_0005813 (EC: IDA, PMID: 15242618); GO_0005814 (EC: IDA, PMID: 19001868); GO_0006468 (EC: IDA); GO_0007052 (EC: IDA, PMID: 19001868); GO_0007093 (EC: ISS); GO_0007265 (EC: ISS); GO_0007613 (EC: ISS); GO_0030425 (EC: ISS); GO_0032436 (EC: IEA); GO_0032486 (EC: ISS); GO_0043066 (EC: ISS); GO_0043123 (EC: IMP, PMID: 12761501); GO_0046599 (EC: IDA, PMID: 19001868); GO_0046599 (EC: IMP, PMID: 15242618); GO_0048167 (EC: ISS); GO_0060291 (EC: ISS); GO_0060292 (EC: ISS) PMID: 8889549; 10523297; 10557092; 11039900; 11696980; 11716500; 12477932; 12651910; 12761501; 12897130; 12972611; 14702039; 15242618; 15489334; 16169070; 16203730; 16344560; 17671831; 17706602; 17912033; 19001868; 19004816; 19506885; 19597481; 19706541; 19834535; 19889641; 19953087; 20054236; 20056645; 20352051; 20360068; 20508983; 20531387; 21067440; 21340720; 21402713; 21832049; 21906983; 21963094; 21988832; 22100274; 22134238; 22138223; 22248692; 22289679; 22399798; 22828320; 22988096; 23466428; 23703673 polo-like kinase 2 Ensembl:ENSG00000145632 HGNC:19699 HPRD:06118 MIM:607023 Vega:OTTHUMG00000097047 Other designations: PLK-2|serine/threonine-protein kinase PLK2|serine/threonine-protein kinase SNK|serum-inducible kinase PLK2 OGG:3000010803 Bin Zhao, Yue Liu, Oliver He CC-CKR-9 CDw199 GPR-9-6 GPR28 WEB: http://www.ncbi.nlm.nih.gov/gene CCR9 chemokine (C-C motif) receptor 9 10803 3p21.3 9606 3 GO_0004950 (EC: TAS, PMID:10229797); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:10229797); GO_0006935 (EC: IEA); GO_0006955 (EC: IEA); GO_0006968 (EC: TAS, PMID:10544196); GO_0007186 (EC: TAS, PMID:10544196); GO_0007204 (EC: TAS, PMID:10229797); GO_0016493 (EC: IEA); GO_0070098 (EC: TAS, PMID:10229797) PMID:2834384; 10229797; 10498628; 10544196; 10602049; 10640743; 10702689; 10974041; 11046037; 12477932; 12816994; 14559839; 15489334; 15623660; 15717282; 16344560; 17205512; 17570212; 18240029; 18245518; 18245522; 18577758; 19423540; 19525985; 19756884; 20036838; 20056178; 20081876; 20190752; 20406964; 20438785; 20738854; 20947433; 21075690; 21344163; 21511186; 21637913; 21984373; 23326330 chemokine (C-C motif) receptor 9 Ensembl:ENSG00000173585 HGNC:1610 HPRD:09200 MIM:604738 Vega:OTTHUMG00000133450 Other designations: C-C chemokine receptor type 9|G protein-coupled receptor 28 CCR9 OGG:3000010857 Bin Zhao, Yue Liu, Oliver He HPR6.6 MPR WEB: http://www.ncbi.nlm.nih.gov/gene PGRMC1 progesterone receptor membrane component 1 10857 Xq22-q24 9606 X Official from a nomenclature committee GO_0005496 (EC: IEA); GO_0005515 (EC: IPI); GO_0005730 (EC: IDA); GO_0005783 (EC: IDA); GO_0005789 (EC: IEA); GO_0007411 (EC: IEA); GO_0016021 (EC: IEA); GO_0020037 (EC: IEA) PMID: 9705155; 11697142; 12477932; 12493773; 14523988; 15302935; 15489334; 15702432; 15782218; 15970648; 16234411; 16565220; 17081983; 17215244; 17276356; 17353931; 18029348; 18249431; 18319313; 18440126; 18479732; 18782852; 18818748; 18922159; 19019335; 19292867; 19417032; 19527514; 19797399; 20140262; 20164297; 20537145; 20538600; 21081644; 21109987; 21131300; 21139048; 21145461; 21148105; 21455559; 21825115; 21890473; 21900206; 21906983; 21918976; 22053931; 22190034; 22245528; 22492871; 22588913; 22939629; 23000965; 23116217; 23246001; 23455922; 23557589; 23798571 progesterone receptor membrane component 1 Ensembl:ENSG00000101856 HGNC:16090 HPRD:02338 MIM:300435 Vega:OTTHUMG00000022268 Other designations: membrane-associated progesterone receptor component 1|progesterone binding protein PGRMC1 OGG:3000010858 Bin Zhao, Yue Liu, Oliver He CP46 CYP46 WEB: http://www.ncbi.nlm.nih.gov/gene CYP46A1 cytochrome P450, family 46, subfamily A, polypeptide 1 10858 14q32.1 9606 14 GO_0005506 (EC: IEA); GO_0005783 (EC: TAS, PMID:10377398); GO_0005789 (EC: TAS); GO_0006699 (EC: TAS); GO_0006707 (EC: IDA, PMID:18621681); GO_0006805 (EC: IDA); GO_0006805 (EC: TAS); GO_0007399 (EC: TAS, PMID:10377398); GO_0008206 (EC: TAS); GO_0008395 (EC: TAS, PMID:10377398); GO_0016021 (EC: IEA); GO_0016125 (EC: TAS); GO_0020037 (EC: IDA, PMID:18621681); GO_0033781 (EC: IDA, PMID:18621681); GO_0044281 (EC: TAS) PMID:9717719; 10377398; 11111082; 11698143; 12123847; 12232784; 12477932; 12533083; 12533085; 14640697; 14702039; 15034781; 15106838; 15128046; 15165699; 15172102; 15286456; 15331159; 15450677; 15489334; 15936520; 15975088; 16013913; 16055229; 16157450; 16258842; 16734927; 16960449; 17335784; 17550732; 17854420; 18511756; 18621681; 18842294; 18976975; 19059217; 19161969; 19212968; 19286353; 19363267; 19553612; 19647891; 20193040; 20535486; 20667828; 20682755; 20693622; 21049985; 21386929; 21729100; 22185844; 22528464; 22977134; 23070465; 23167762; 23288837; 23604141 cytochrome P450, family 46, subfamily A, polypeptide 1 Ensembl:ENSG00000036530 HGNC:2641 HPRD:04970 MIM:604087 Vega:OTTHUMG00000171510 Other designations: CH24H|cholesterol 24-hydroxylase|cytochrome P450 46A1|cytochrome P450, subfamily 46 (cholesterol 24-hydroxylase) CYP46A1 OGG:3000010923 Bin Zhao, Yue Liu, Oliver He P15 PC4 p14 WEB: http://www.ncbi.nlm.nih.gov/gene SUB1 SUB1 homolog (S. cerevisiae) 10923 5p13.3 9606 5 Official from a nomenclature committee GO_0003697 (EC: IDA, PMID: 8062391); GO_0003713 (EC: IDA, PMID: 8062391); GO_0005515 (EC: IPI, PMID: 11389848); GO_0005634 (EC: IDA); GO_0005667 (EC: IDA, PMID: 8062391); GO_0005730 (EC: IDA); GO_0006351 (EC: IEA); GO_0006357 (EC: IDA, PMID: 8062391); GO_0044822 (EC: IDA); GO_0070062 (EC: IDA) PMID: 7628453; 7809103; 8062391; 8062392; 9360603; 9482861; 9632764; 9660784; 9660958; 9792714; 9885563; 10024883; 10887206; 11005381; 11279157; 11313979; 11389848; 11741883; 12477932; 12565890; 12590132; 14966284; 15199162; 15302935; 15489334; 15635413; 15893730; 16415882; 16982701; 17081983; 17130840; 17317687; 17361185; 17785449; 18029348; 18854154; 19038270; 19047459; 19322201; 19471022; 19525231; 19706510; 19738201; 19759913; 20080105; 20305379; 20360068; 21139048; 21193408; 21319273; 21586571; 21832049; 21890473; 21906983; 21907836; 21963094; 21987572; 22113938; 22174317; 22505724; 22939629; 23000965; 23184937; 23455922; 23602568 SUB1 homolog (S. cerevisiae) Ensembl:ENSG00000113387 HGNC:19985 HPRD:02737 MIM:600503 Vega:OTTHUMG00000131071 Other designations: activated RNA polymerase II transcription cofactor 4|activated RNA polymerase II transcriptional coactivator p15|positive cofactor 4 SUB1 OGG:3000010924 Bin Zhao, Yue Liu, Oliver He ASM3A ASML3a yR36GH4.1 WEB: http://www.ncbi.nlm.nih.gov/gene SMPDL3A sphingomyelin phosphodiesterase, acid-like 3A 10924 6q22.31 9606 6 Official from a nomenclature committee GO_0004767 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12442002); GO_0005615 (EC: IEA); GO_0006685 (EC: IEA); GO_0008150 (EC: ND); GO_0016798 (EC: IEA) PMID: 12442002; 12477932; 14574404; 15174051; 15489334; 16344560; 22810003 sphingomyelin phosphodiesterase, acid-like 3A Ensembl:ENSG00000172594 HGNC:17389 HPRD:10244 MIM:610728 Vega:OTTHUMG00000015490 Other designations: 0610010C24Rik|ASM-like phosphodiesterase 3a|acid sphingomyelinase-like phosphodiesterase 3a SMPDL3A OGG:3000010926 Bin Zhao, Yue Liu, Oliver He ASK CHIF DBF4A ZDBF1 WEB: http://www.ncbi.nlm.nih.gov/gene DBF4 DBF4 zinc finger 10926 7q21.3 9606 7 Official from a nomenclature committee GO_0000082 (EC: TAS); GO_0000278 (EC: TAS); GO_0003676 (EC: IEA); GO_0005654 (EC: TAS); GO_0006260 (EC: TAS); GO_0008047 (EC: TAS, PMID: 10373557); GO_0008270 (EC: IEA); GO_0043085 (EC: TAS, PMID: 10373557) PMID: 10373557; 10517317; 10523313; 10846177; 12015319; 12420215; 12441400; 12477932; 12535533; 12614612; 12791985; 12853948; 12968034; 14702039; 15226314; 15231747; 15302935; 15374998; 15489334; 15707391; 16826239; 16899510; 16912045; 17276990; 17768177; 18286467; 18503552; 18536724; 18714392; 19111665; 19744312; 19864417; 21036905; 21536671; 22123827; 22990118; 24240236 DBF4 zinc finger Ensembl:ENSG00000006634 HGNC:17364 HPRD:10371 MIM:604281 Vega:OTTHUMG00000131034 Other designations: DBF4 homolog|DBF4 zinc finger A|DBF4-type zinc finger-containing protein 1|activator of S phase kinase|chiffon homolog A|protein DBF4 homolog A|zinc finger, DBF-type containing 1 DBF4 OGG:3000010952 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene SEC61B Sec61 beta subunit 10952 9q22.32-q31.3 9606 9 Official from a nomenclature committee GO_0000060 (EC: IMP, PMID: 17215517); GO_0002474 (EC: TAS); GO_0002479 (EC: TAS); GO_0005515 (EC: IPI, PMID: 18555783); GO_0005783 (EC: IDA); GO_0006412 (EC: TAS); GO_0006614 (EC: TAS); GO_0010467 (EC: TAS); GO_0016020 (EC: IDA); GO_0016021 (EC: NAS, PMID: 8107851); GO_0030433 (EC: IDA, PMID: 8945469); GO_0030970 (EC: IMP, PMID: 17215517); GO_0031205 (EC: ISS); GO_0042590 (EC: TAS); GO_0043022 (EC: IEA); GO_0044267 (EC: TAS); GO_0044822 (EC: IDA); GO_0048408 (EC: IPI, PMID: 19602593) PMID: 8107851; 8125298; 8945469; 9512475; 9565615; 9585408; 9631292; 9792704; 10212142; 10508919; 10601334; 10799540; 12477932; 15164053; 15489334; 16015337; 16083285; 17081983; 17215517; 17360537; 18555783; 19602593; 19738201; 20516149; 20676083; 20937808; 21139048; 21182205; 21255561; 21343306; 22623428; 22645275; 22710939; 23129660; 23533635; 23606741; 23874384 Sec61 beta subunit Other designations: Sec61 complex, beta subunit|protein translocation complex beta|protein transport protein SEC61 beta subunit|protein transport protein Sec61 subunit beta SEC61B OGG:3000010965 Bin Zhao, Yue Liu, Oliver He CTE-IA CTE1A MTE1 PTE2 PTE2A ZAP128 WEB: http://www.ncbi.nlm.nih.gov/gene ACOT2 acyl-CoA thioesterase 2 10965 14q24.3 9606 14 GO_0000038 (EC: IDA, PMID:16940157); GO_0001676 (EC: IDA, PMID:16940157); GO_0005102 (EC: IPI); GO_0005739 (EC: IDA, PMID:16940157); GO_0006637 (EC: IDA, PMID:10944470); GO_0016290 (EC: IEA); GO_0047617 (EC: IDA, PMID:10944470) PMID:7596406; 8125298; 10944470; 12477932; 12665801; 14702039; 15007068; 15489334; 16103133; 16940157; 17353931; 19497300; 20178365; 20379614; 20877624; 21139048; 21890473; 21963094; 21987572 acyl-CoA thioesterase 2 Ensembl:ENSG00000119673 HGNC:18431 HPRD:10173 MIM:609972 Vega:OTTHUMG00000171608 Other designations: acyl-coenzyme A thioester hydrolase 2a|acyl-coenzyme A thioesterase 2, mitochondrial|long-chain acyl-CoA thioesterase 2|mitochondrial acyl-CoA thioesterase 1|peroxisomal long-chain acyl-coA thioesterase 2 ACOT2 OGG:3000011010 Bin Zhao, Yue Liu, Oliver He CRISP7 GLIPR RTVP1 WEB: http://www.ncbi.nlm.nih.gov/gene GLIPR1 GLI pathogenesis-related 1 11010 12q21.2 9606 12 Official from a nomenclature committee GO_0005576 (EC: IEA); GO_0005886 (EC: TAS); GO_0016021 (EC: IEA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS) PMID: 7607567; 8973356; 9482873; 11971968; 12477932; 14702039; 14871827; 15489334; 16712791; 16714093; 17207965; 17825796; 18030365; 18199537; 19483285; 19913121; 20356381; 20628086; 21045302; 21777672; 21922325; 21931216; 22025562; 23333597; 23714687 GLI pathogenesis-related 1 HGNC:17001 HPRD:04071 MIM:602692 Other designations: GLI pathogenesis-related 1 (glioma)|gliPR 1|glioma pathogenesis-related protein 1|protein RTVP-1|related to testis-specific, vespid, and pathogenesis proteins 1|testes-specific vespid and pathogenesis protein 1 GLIPR1 OGG:3000011014 Bin Zhao, Yue Liu, Oliver He ELP-1 ERD2.2 WEB: http://www.ncbi.nlm.nih.gov/gene KDELR2 KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 2 11014 tcag7.840 7p22.1 9606 7 Official from a nomenclature committee GO_0005046 (EC: TAS, PMID: 1316805); GO_0005783 (EC: TAS, PMID: 1316805); GO_0005789 (EC: IEA); GO_0005794 (EC: TAS, PMID: 1316805); GO_0005801 (EC: IEA); GO_0006621 (EC: IEA); GO_0006886 (EC: TAS, PMID: 1325562); GO_0016021 (EC: IEA); GO_0016192 (EC: IEA) PMID: 1316805; 1325562; 9118249; 11752456; 12071860; 12477932; 12690205; 12853948; 14702039; 15489334; 16344560; 17353931; 19322201; 21139048; 21890473; 24250222 KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 2 Ensembl:ENSG00000136240 HGNC:6305 HPRD:06598 MIM:609024 Vega:OTTHUMG00000023103 Other designations: (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 2|ER lumen protein retaining receptor 2|ERD-2-like protein|ERD2-like protein 1|KDEL endoplasmic reticulum protein retention receptor 2|KDEL receptor 2 KDELR2 OGG:3000011016 Bin Zhao, Yue Liu, Oliver He ATFA WEB: http://www.ncbi.nlm.nih.gov/gene ATF7 activating transcription factor 7 11016 12q13 9606 12 GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID:10376527); GO_0005634 (EC: NAS, PMID:8288576); GO_0005654 (EC: IEA); GO_0005737 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IDA, PMID:8288576); GO_0008134 (EC: IDA, PMID:10376527); GO_0016032 (EC: IEA); GO_0034399 (EC: IDA, PMID:17264123); GO_0043565 (EC: IEA); GO_0046872 (EC: IEA); GO_0051019 (EC: IDA, PMID:10376527) PMID:1694576; 7769693; 8288576; 8649858; 8889548; 8939888; 10376527; 10698518; 11278933; 11566021; 12477932; 12805554; 14643450; 15342556; 15735663; 15867431; 16147992; 16344560; 17081983; 17264123; 18029348; 18671972; 18950637; 19471022; 20189936; 20195357; 21693764; 21858082; 21890473; 21998595; 22242598; 22939629; 23000965; 23426901; 23793025 activating transcription factor 7 Ensembl:ENSG00000170653 HGNC:792 HPRD:06968 MIM:606371 Vega:OTTHUMG00000169776 Other designations: cyclic AMP-dependent transcription factor ATF-7|transcription factor ATF-A ATF7 OGG:3000011080 Bin Zhao, Yue Liu, Oliver He DNAJW DjB4 HLJ1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB4 DnaJ (Hsp40) homolog, subfamily B, member 4 11080 1p31.1 9606 1 GO_0005515 (EC: IPI); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005886 (EC: IDA); GO_0006457 (EC: IEA); GO_0006986 (EC: TAS, PMID:9546042); GO_0009408 (EC: TAS, PMID:9546042); GO_0051082 (EC: IEA) PMID:9546042; 11147971; 11371506; 12477932; 15489334; 15592455; 15661747; 15782117; 16009940; 16542645; 16788156; 18029348; 18794131; 20145123; 20360068; 20615403; 21345358; 21906983; 21963094; 21988832; 22145905; 22863883; 22939629; 23000965; 23306212; 23824909; 24318877 DnaJ (Hsp40) homolog, subfamily B, member 4 HGNC:14886 HPRD:07486 MIM:611327 Other designations: DnaJ-like heat shock protein 40|HSP40 homolog|dnaJ homolog subfamily B member 4|heat shock 40 kDa protein 1 homolog|heat shock protein 40 homolog|human liver DnaJ-like protein DNAJB4 OGG:3000011124 Bin Zhao, Yue Liu, Oliver He HFAF1s UBXD12 UBXN3A hFAF1 WEB: http://www.ncbi.nlm.nih.gov/gene FAF1 Fas (TNFRSF6) associated factor 1 11124 CGI-03 1p33 9606 1 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 15688372); GO_0005634 (EC: IDA, PMID: 15596450); GO_0005635 (EC: IEA); GO_0005829 (EC: IDA, PMID: 15596450); GO_0006915 (EC: IEA); GO_0007253 (EC: IMP, PMID: 14600157); GO_0008219 (EC: IMP, PMID: 15743842); GO_0019887 (EC: NAS, PMID: 11713579); GO_0019901 (EC: IDA, PMID: 11713579); GO_0019904 (EC: IEA); GO_0030155 (EC: IEA); GO_0031072 (EC: IDA, PMID: 15596450); GO_0031265 (EC: NAS, PMID: 12702723); GO_0031334 (EC: IMP, PMID: 15688372); GO_0031625 (EC: IDA, PMID: 18775313); GO_0034098 (EC: IDA, PMID: 18775313); GO_0042176 (EC: IMP, PMID: 15743842); GO_0043065 (EC: NAS, PMID: 10462485); GO_0043130 (EC: IDA, PMID: 18775313); GO_0043161 (EC: NAS, PMID: 15743842); GO_0045859 (EC: NAS, PMID: 11713579); GO_0048471 (EC: IDA, PMID: 11713579); GO_0051059 (EC: IPI, PMID: 14600157); GO_1902043 (EC: IEA) PMID: 8524870; 9740801; 10094392; 10462485; 10810093; 11243799; 11378439; 11527403; 11713579; 12087183; 12372427; 12477932; 12702723; 12832043; 12963981; 14600157; 14702039; 15207703; 15231748; 15489334; 15592455; 15596450; 15688372; 15743842; 16169070; 16807242; 17046979; 17684021; 17999750; 18573343; 18775313; 18790738; 19013454; 19174780; 19422935; 19471022; 19615732; 19722279; 19913121; 20057067; 20124726; 20195546; 20237496; 20379614; 20628086; 20639865; 20886065; 21076409; 21139048; 21282461; 21295280; 21411632; 21414298; 21645854; 21849551; 21890473; 21900206; 21906983; 21914798; 21963094; 21978668; 21987572; 22053931; 22064162; 22102026; 22350894; 22505724; 22730322; 22863883; 22876279; 22939629; 23000965; 23293021; 23314748; 23383273; 23720822 Fas (TNFRSF6) associated factor 1 Ensembl:ENSG00000185104 HGNC:3578 HPRD:05124 MIM:604460 Other designations: FAS-associated factor 1|TNFRSF6-associated factor 1|UBX domain protein 3A|UBX domain-containing protein 12|UBX domain-containing protein 3A FAF1 OGG:3000011145 Bin Zhao, Yue Liu, Oliver He AdPLA H-REV107-1 HRASLS3 HREV107 HREV107-1 HREV107-3 HRSL3 WEB: http://www.ncbi.nlm.nih.gov/gene PLA2G16 phospholipase A2, group XVI 11145 11q12.3 9606 11 Official from a nomenclature committee GO_0004623 (EC: IDA); GO_0005515 (EC: IPI, PMID: 17374643); GO_0005575 (EC: ND); GO_0005783 (EC: IEA); GO_0005829 (EC: TAS); GO_0006644 (EC: IDA); GO_0006644 (EC: TAS); GO_0008970 (EC: IEA); GO_0016021 (EC: IEA); GO_0016042 (EC: IEA); GO_0036149 (EC: TAS); GO_0036150 (EC: TAS); GO_0036151 (EC: TAS); GO_0036152 (EC: TAS); GO_0044281 (EC: TAS); GO_0045786 (EC: IEA); GO_0046474 (EC: TAS); GO_0048471 (EC: IEA); GO_0052739 (EC: IEA); GO_0052740 (EC: IEA) PMID: 9771974; 10508479; 11337467; 11526504; 11973642; 12054741; 12477932; 15489334; 16189514; 16713569; 17003497; 17374643; 18614531; 19136964; 19615464; 20501645; 21139048; 21890473; 21963094; 22605381; 22923616 phospholipase A2, group XVI Ensembl:ENSG00000176485 HGNC:17825 HPRD:13671 MIM:613867 Other designations: Ca-independent phospholipase A1/2|H-rev 107 protein homolog|HRAS-like suppressor 1|HRAS-like suppressor 3|adipose-specific PLA2|adipose-specific phospholipase A2|group XVI phospholipase A1/A2|group XVI phospholipase A2|renal carcinoma antigen NY-REN-65 PLA2G16 OGG:3000011163 Bin Zhao, Yue Liu, Oliver He DIPP2 DIPP2alpha DIPP2beta WEB: http://www.ncbi.nlm.nih.gov/gene NUDT4 nudix (nucleoside diphosphate linked moiety X)-type motif 4 11163 HDCMB47P 12q21 9606 12 Official from a nomenclature committee GO_0005622 (EC: TAS, PMID: 10777568); GO_0005829 (EC: TAS); GO_0008486 (EC: IDA, PMID: 10777568); GO_0009187 (EC: TAS, PMID: 10777568); GO_0019722 (EC: TAS, PMID: 10777568); GO_0019935 (EC: TAS, PMID: 10777568); GO_0030515 (EC: ISS); GO_0035556 (EC: NAS, PMID: 10777568); GO_0043647 (EC: TAS); GO_0044281 (EC: TAS); GO_0046831 (EC: TAS, PMID: 10777568); GO_0046872 (EC: IEA); GO_0046907 (EC: TAS, PMID: 10777568); GO_0050072 (EC: ISS, Qualifier: NOT); GO_0052840 (EC: TAS); GO_0052843 (EC: IEA); GO_0052844 (EC: IEA); GO_0052845 (EC: IEA); GO_0052846 (EC: IEA); GO_0052847 (EC: IEA); GO_0052848 (EC: IEA) PMID: 8125298; 9455484; 10777568; 11376937; 12121577; 12370170; 12477932; 15252450; 15489334; 18976975 nudix (nucleoside diphosphate linked moiety X)-type motif 4 Ensembl:ENSG00000173598 HGNC:8051 HPRD:14850 MIM:609229 Vega:OTTHUMG00000170155 Other designations: DIPP-2|diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2|diphosphoinositol polyphosphate phosphohydrolase 2|diphosphoinositol polyphosphate phosphohydrolase type 2 NUDT4 OGG:3000011164 Bin Zhao, Yue Liu, Oliver He YSA1 YSA1H YSAH1 hYSAH1 WEB: http://www.ncbi.nlm.nih.gov/gene NUDT5 nudix (nucleoside diphosphate linked moiety X)-type motif 5 11164 HSPC115 10p14 9606 10 Official from a nomenclature committee GO_0000287 (EC: IDA, PMID: 18462755); GO_0005622 (EC: NAS, PMID: 10567213); GO_0005829 (EC: TAS); GO_0009117 (EC: NAS, PMID: 10567213); GO_0009191 (EC: IDA, PMID: 18462755); GO_0017110 (EC: IEA); GO_0019144 (EC: IDA, PMID: 10567213); GO_0019303 (EC: NAS, PMID: 10567213); GO_0030515 (EC: ISS); GO_0034656 (EC: TAS); GO_0044281 (EC: TAS); GO_0047631 (EC: EXP); GO_0050072 (EC: ISS, Qualifier: NOT); GO_0055086 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 10373642; 10567213; 10722730; 11042152; 12477932; 12717453; 15489334; 15592455; 16002790; 16169070; 16716086; 17052728; 17261271; 18462755; 19056867; 19699693; 20144704; 20176146; 20360068; 21139048; 21389046; 21768126; 21890473; 21900206; 21906983; 21963094; 22200976; 22351996; 22505724; 22863883; 22939629; 23000965; 23184937 nudix (nucleoside diphosphate linked moiety X)-type motif 5 Ensembl:ENSG00000165609 HGNC:8052 HPRD:14851 MIM:609230 Other designations: 8-oxo-dGDP phosphatase|ADP-sugar pyrophosphatase NUDT5 OGG:3000011283 Bin Zhao, Yue Liu, Oliver He CPF8 CYPIVF8 WEB: http://www.ncbi.nlm.nih.gov/gene CYP4F8 cytochrome P450, family 4, subfamily F, polypeptide 8 11283 19p13.1 9606 19 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006690 (EC: TAS); GO_0006693 (EC: TAS, PMID:10405341); GO_0006805 (EC: TAS); GO_0016021 (EC: IEA); GO_0018685 (EC: TAS, PMID:10405341); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA) PMID:9068972; 10405341; 10791960; 11448449; 12464258; 14702039; 15128046; 15789615; 16112640; 16344560; 17353931; 19343046; 21281786; 22228203 cytochrome P450, family 4, subfamily F, polypeptide 8 HGNC:2648 HPRD:08518 MIM:611545 Other designations: cytochrome P450 4F8|cytochrome P450, subfamily IVF, polypeptide 8|flavoprotein-linked monooxygenase|microsomal monooxygenase CYP4F8 OGG:3000011332 Bin Zhao, Yue Liu, Oliver He ACH1 ACT BACH CTE-II LACH LACH1 hBACH WEB: http://www.ncbi.nlm.nih.gov/gene ACOT7 acyl-CoA thioesterase 7 11332 RP1-120G22.10 1p36 9606 1 GO_0000062 (EC: IDA, PMID:10578051); GO_0005515 (EC: IPI, PMID:10578051); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005739 (EC: IEA); GO_0005829 (EC: IDA, PMID:10578051); GO_0009062 (EC: IEA); GO_0015937 (EC: IDA, PMID:10578051); GO_0016290 (EC: IDA, PMID:10578051); GO_0036042 (EC: IDA, PMID:10578051); GO_0036114 (EC: IDA, PMID:10578051); GO_0036116 (EC: IDA, PMID:10578051); GO_0042803 (EC: IPI, PMID:10578051); GO_0043005 (EC: IEA); GO_0044297 (EC: IEA); GO_0051792 (EC: IDA, PMID:10578051); GO_0070062 (EC: IDA, PMID:19056867); GO_1900535 (EC: IDA, PMID:10578051) PMID:10578051; 12435388; 12477932; 14702039; 15489334; 15592755; 15731883; 16103133; 16710414; 16713569; 18029348; 19056867; 19305408; 19724895; 19851296; 20198315; 21044950; 21110914; 21139048; 21319273; 21890473; 21906983; 21963094; 22053931; 22505724; 22863883; 23000965 acyl-CoA thioesterase 7 Ensembl:ENSG00000097021 HGNC:24157 HPRD:12517 MIM:602587 Vega:OTTHUMG00000001295 Other designations: CTE-IIa|acyl-CoA thioesterase 2|acyl-CoA thioesterase, long chain|brain acyl CoA hydrolase|brain acyl-CoA hydrolase|cytosolic acyl coenzyme A thioester hydrolase|long chain acyl-CoA thioester hydrolase ACOT7 OGG:3000011343 Bin Zhao, Yue Liu, Oliver He HU-K5 HUK5 MAGL MGL WEB: http://www.ncbi.nlm.nih.gov/gene MGLL monoglyceride lipase 11343 3q21.3 9606 3 Official from a nomenclature committee GO_0004622 (EC: TAS, PMID: 9495531); GO_0005789 (EC: TAS); GO_0005886 (EC: TAS); GO_0006629 (EC: TAS, PMID: 9495531); GO_0006633 (EC: IEA); GO_0006644 (EC: TAS); GO_0006954 (EC: TAS, PMID: 9495531); GO_0007596 (EC: TAS); GO_0008289 (EC: IEA); GO_0009966 (EC: ISS); GO_0019369 (EC: ISS); GO_0019433 (EC: IEA); GO_0019433 (EC: TAS); GO_0030168 (EC: TAS); GO_0036155 (EC: TAS); GO_0042803 (EC: IPI, PMID: 19957260); GO_0044281 (EC: TAS); GO_0045202 (EC: IEA); GO_0046464 (EC: ISS); GO_0046474 (EC: TAS); GO_0047372 (EC: ISS); GO_0047372 (EC: TAS); GO_0050727 (EC: ISS); GO_0051930 (EC: ISS); GO_0060292 (EC: IEA); GO_2000124 (EC: ISS) PMID: 8619474; 8889548; 9110174; 9495531; 11470505; 12477932; 14702039; 15342556; 15489334; 16169070; 16344560; 16806233; 17621164; 18452279; 18721756; 19014633; 19233690; 19913121; 19957260; 19962385; 20079333; 20464001; 20628086; 20855465; 20976246; 21118518; 21308848; 21543155; 21802006; 22349814; 22664939; 22827915; 23455058; 23509962; 23553709; 24368842 monoglyceride lipase Ensembl:ENSG00000074416 HGNC:17038 HPRD:17574 MIM:609699 Vega:OTTHUMG00000159641 Other designations: lysophospholipase homolog|monoacylglycerol lipase MGLL OGG:3000022809 Bin Zhao, Yue Liu, Oliver He ATFX HMFN0395 WEB: http://www.ncbi.nlm.nih.gov/gene ATF5 activating transcription factor 5 22809 19q13.3 9606 19 GO_0003700 (EC: IEA); GO_0003714 (EC: TAS, PMID:10373550); GO_0005515 (EC: IPI, PMID:10373550); GO_0005634 (EC: IDA); GO_0005667 (EC: IEA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0006351 (EC: IEA); GO_0006357 (EC: IEA); GO_0009791 (EC: IEA); GO_0021891 (EC: IEA); GO_0031072 (EC: IEA); GO_0035264 (EC: IEA); GO_0043066 (EC: IEA); GO_0043565 (EC: IEA); GO_0048712 (EC: IEA) PMID:1371974; 8889548; 10373550; 11087824; 11278933; 12477932; 12812986; 14702039; 15221005; 15342556; 15358120; 15489334; 15890932; 16164412; 16170340; 16300731; 16344560; 17346882; 18029348; 18055463; 18195013; 18276110; 18332083; 18458088; 18701499; 18832568; 19167516; 19251251; 19285020; 19531563; 20379614; 20423929; 21212266; 21521685; 21791614; 21972289; 21988832; 22442021; 22528486; 23018213; 23275563; 23661758; 23876217; 24250222 activating transcription factor 5 Ensembl:ENSG00000169136 HGNC:790 HPRD:05906 MIM:606398 Vega:OTTHUMG00000183065 Other designations: cAMP-dependent transcription factor ATF-5|cyclic AMP-dependent transcription factor ATF-5|transcription factor ATFx ATF5 OGG:3000022826 Bin Zhao, Yue Liu, Oliver He HSPC331 SPF31 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC8 DnaJ (Hsp40) homolog, subfamily C, member 8 22826 HSPC315 1p35.3 9606 1 GO_0000398 (EC: TAS); GO_0005654 (EC: TAS); GO_0008380 (EC: TAS); GO_0010467 (EC: TAS) PMID:11147971; 11790298; 12226669; 12234937; 12477932; 15489334; 15635413; 16159877; 16344560; 16710414; 17332742; 18850631; 19471022; 20098747; 20360068; 20379614; 21139048; 21693764; 21832049; 21890473; 22863883; 22939629; 22944692; 23602568; 23940030; 24163370 DnaJ (Hsp40) homolog, subfamily C, member 8 Ensembl:ENSG00000126698 HGNC:15470 HPRD:13236 Vega:OTTHUMG00000003538 Other designations: dnaJ homolog subfamily C member 8|splicing protein spf31 DNAJC8 OGG:3000022843 Bin Zhao, Yue Liu, Oliver He CaMKP-N POPX1 PP2CH caMKN WEB: http://www.ncbi.nlm.nih.gov/gene PPM1E protein phosphatase, Mg2+/Mn2+ dependent, 1E 22843 17q22 9606 17 Official from a nomenclature committee GO_0004722 (EC: IDA); GO_0005515 (EC: IPI, PMID: 11864573); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005739 (EC: IEA); GO_0006469 (EC: IDA, PMID: 11864573); GO_0035690 (EC: IDA); GO_0035970 (EC: IDA); GO_0043234 (EC: IDA, PMID: 11864573); GO_0046872 (EC: IEA); GO_0051496 (EC: IDA, PMID: 11864573) PMID: 10470851; 11726284; 11864573; 12477932; 15496589; 15680915; 17043677; 17897624; 17903297; 18029348; 20801214; 23620142; 23666239 protein phosphatase, Mg2+/Mn2+ dependent, 1E HGNC:19322 HPRD:17888 Other designations: ca(2+)/calmodulin-dependent protein kinase phosphatase N|caMKP-nucleus|nuclear calmodulin-dependent protein kinase phosphatase|partner of PIX 1|partner of PIX-alpha|partner of PIXA|protein phosphatase 1E|protein phosphatase 1E (PP2C domain containing) PPM1E OGG:3000022861 Bin Zhao, Yue Liu, Oliver He CARD7 CIDED CLR17.1 DEFCAP DEFCAP-L/S NAC NALP1 PP1044 SLEV1 VAMAS1 WEB: http://www.ncbi.nlm.nih.gov/gene NLRP1 NLR family, pyrin domain containing 1 22861 17p13.2 9606 17 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 11472070); GO_0005524 (EC: IDA, PMID: 15212762); GO_0005622 (EC: IC, PMID: 11076957); GO_0005634 (EC: IDA, PMID: 17164409); GO_0005829 (EC: TAS); GO_0006915 (EC: NAS, PMID: 11076957); GO_0006919 (EC: IDA, PMID: 15212762); GO_0006919 (EC: NAS, PMID: 11076957); GO_0008656 (EC: NAS, PMID: 11076957); GO_0019899 (EC: IPI, PMID: 11076957); GO_0019904 (EC: IPI, PMID: 16575408); GO_0032495 (EC: ISS); GO_0035872 (EC: TAS); GO_0042742 (EC: ISS); GO_0045087 (EC: TAS); GO_0050718 (EC: ISS); GO_0050727 (EC: IC, PMID: 15212762); GO_0051402 (EC: IDA, PMID: 15212762); GO_0072558 (EC: IDA, PMID: 12191486); GO_0072558 (EC: TAS) PMID: 8619474; 8781126; 9110174; 10231032; 11076957; 11113115; 11250163; 11270363; 11472070; 11592035; 12191486; 12477932; 12563287; 14527388; 14691733; 14702039; 15107016; 15174051; 15212762; 15749123; 16575408; 17164409; 17377159; 17418785; 17620097; 17637824; 18263805; 18348116; 18854154; 18946481; 19001869; 19074885; 19120479; 19223160; 19337385; 19727120; 19913121; 20152874; 20370570; 20379614; 20403135; 20502346; 20574744; 20628086; 20697295; 20800603; 21098108; 21149496; 21245836; 21252346; 21331694; 21376416; 21946017; 21976003; 22087307; 22117610; 22227487; 22235789; 22507623; 22524199; 22665479; 23053059; 23253924; 23349227; 23374100; 23380025; 23382179; 23508996; 23563199; 23940760; 24008734 NLR family, pyrin domain containing 1 Ensembl:ENSG00000091592 HGNC:14374 HPRD:07364 MIM:606636 Vega:OTTHUMG00000132419 Other designations: NACHT, LRR and PYD containing protein 1|NACHT, LRR and PYD domains-containing protein 1|NACHT, leucine rich repeat and PYD (pyrin domain) containing 1|NACHT, leucine rich repeat and PYD containing 1|caspase recruitment domain protein 7|caspase recruitment domain-containing protein 7|death effector filament-forming Ced-4-like apoptosis protein|nucleotide-binding domain and caspase recruitment domain|nucleotide-binding oligomerization domain, leucine rich repeat and pyrin domain containing 1 NLRP1 OGG:3000022926 Bin Zhao, Yue Liu, Oliver He ATF6A WEB: http://www.ncbi.nlm.nih.gov/gene ATF6 activating transcription factor 6 22926 1q22-q23 9606 1 GO_0000139 (EC: TAS); GO_0003700 (EC: IEA); GO_0003713 (EC: TAS, PMID:10866666); GO_0005515 (EC: IPI, PMID:16469704); GO_0005634 (EC: TAS, PMID:10564271); GO_0005635 (EC: TAS, PMID:10866666); GO_0005654 (EC: TAS); GO_0005789 (EC: TAS); GO_0006351 (EC: IEA); GO_0006357 (EC: TAS, PMID:10564271); GO_0006457 (EC: TAS, PMID:10564271); GO_0006950 (EC: TAS, PMID:10866666); GO_0006987 (EC: TAS); GO_0006990 (EC: TAS, PMID:9837962); GO_0007165 (EC: TAS, PMID:9271374); GO_0016021 (EC: IEA); GO_0030968 (EC: TAS, PMID:19816510); GO_0043565 (EC: IEA); GO_0044267 (EC: TAS) PMID:2516827; 8889548; 9271374; 9837962; 10564271; 10866666; 11158310; 11163209; 11256944; 11287625; 11483355; 11805088; 11821395; 11909875; 12014989; 12076252; 12097557; 12477932; 12713871; 12782636; 12805554; 12949534; 14699159; 14765107; 15063770; 15299016; 15342556; 15489334; 15598891; 15899857; 16196087; 16469704; 16505252; 16710414; 17092596; 17101776; 17327457; 17440018; 17442311; 17522056; 17686766; 18022401; 18635891; 18650380; 18840095; 19122331; 19304306; 19420237; 19667116; 19693772; 19722195; 19723703; 19772629; 19816510; 19822759; 19913121; 20160352; 20219975; 20628086; 20732420; 20800603; 20936779; 21106748; 21131360; 21150130; 21211013; 21329801; 21329806; 21345978; 21355074; 21385877; 21454619; 21521793; 21693764; 21809331; 21832049; 21841196; 21906983; 21963094; 21988832; 22013072; 22102412; 22146569; 22268729; 22354938; 22577136; 22872700; 22917505; 22956602; 23011799; 23037953; 23382691; 23661758; 23864652; 23924739; 24043630 activating transcription factor 6 Ensembl:ENSG00000118217 HGNC:791 HPRD:16118 MIM:605537 Vega:OTTHUMG00000023961 Other designations: cAMP-dependent transcription factor ATF-6 alpha|cyclic AMP-dependent transcription factor ATF-6 alpha ATF6 OGG:3000022977 Bin Zhao, Yue Liu, Oliver He AFAR2 WEB: http://www.ncbi.nlm.nih.gov/gene AKR7A3 aldo-keto reductase family 7, member A3 (aflatoxin aldehyde reductase) 22977 1p36.13 9606 1 Official from a nomenclature committee GO_0004032 (EC: IEA); GO_0004033 (EC: TAS, PMID: 10383892); GO_0005739 (EC: IEA); GO_0005829 (EC: TAS, PMID: 10383892); GO_0006081 (EC: TAS, PMID: 10383892); GO_0009055 (EC: TAS, PMID: 10383892); GO_0046223 (EC: IEA); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 10383892; 12477932; 12879023; 15489334; 16189514; 16341674; 16710414; 19056867; 20453000; 21044950; 23824909 aldo-keto reductase family 7, member A3 (aflatoxin aldehyde reductase) HGNC:390 HPRD:07089 MIM:608477 Other designations: AFB1 aldehyde reductase 2|AFB1-AR 2|aflatoxin B1 aldehyde reductase 2|aflatoxin B1 aldehyde reductase member 3 AKR7A3 OGG:3000022996 Bin Zhao, Yue Liu, Oliver He C1orf34 DEME-6 WEB: http://www.ncbi.nlm.nih.gov/gene TTC39A tetratricopeptide repeat domain 39A 22996 1p32.3 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0003674 (EC: ND); GO_0005575 (EC: ND); GO_0008150 (EC: ND) PMID: 9455484; 9461476; 12477932 tetratricopeptide repeat domain 39A Ensembl:ENSG00000085831 HGNC:18657 Vega:OTTHUMG00000008193 Other designations: TPR repeat protein 39A|differentially expressed in MCF7 with estradiol protein 6|tetratricopeptide repeat protein 39A TTC39A OGG:3000023210 Bin Zhao, Yue Liu, Oliver He PSR PTDSR PTDSR1 WEB: http://www.ncbi.nlm.nih.gov/gene JMJD6 jumonji domain containing 6 23210 17q25 9606 17 Official from a nomenclature committee GO_0001822 (EC: IEA); GO_0002040 (EC: ISS); GO_0003723 (EC: TAS); GO_0003727 (EC: IDA); GO_0004872 (EC: IEA); GO_0005506 (EC: IDA); GO_0005515 (EC: IPI, PMID: 19574390); GO_0005634 (EC: IDA, PMID: 14729065); GO_0005654 (EC: IDA); GO_0005730 (EC: IDA); GO_0005886 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0006397 (EC: IEA); GO_0007166 (EC: IEA); GO_0007507 (EC: IEA); GO_0008380 (EC: IEA); GO_0018395 (EC: IDA, PMID: 19574390); GO_0030324 (EC: IEA); GO_0033077 (EC: IEA); GO_0033746 (EC: IDA, PMID: 17947579); GO_0033749 (EC: IDA, PMID: 17947579); GO_0042116 (EC: IEA); GO_0042802 (EC: IDA, PMID: 17534701); GO_0042802 (EC: IPI); GO_0043654 (EC: IEA); GO_0048024 (EC: IMP, PMID: 19574390); GO_0048821 (EC: IEA); GO_0060041 (EC: IEA); GO_0070078 (EC: IDA, PMID: 17947579); GO_0070079 (EC: IDA, PMID: 17947579); GO_0070782 (EC: IEA); GO_0070815 (EC: IDA, PMID: 19574390) PMID: 9628581; 10811223; 11877474; 12477932; 12559004; 12898702; 14645848; 14702039; 14729065; 15072554; 15193161; 15345036; 15453906; 15469976; 15489334; 15622002; 16983801; 17534701; 17947579; 18564434; 19492415; 19574390; 20574068; 20679243; 20684070; 21139048; 21300889; 21890473; 21906983; 21963094; 22189873; 22505724; 22621393; 22701020; 22863883; 23303181; 23455924; 23595221; 23688307; 23776548; 24360279 jumonji domain containing 6 Ensembl:ENSG00000070495 HGNC:19355 HPRD:05371 MIM:604914 Vega:OTTHUMG00000169267 Other designations: bifunctional arginine demethylase and lysyl-hydroxylase JMJD6|histone arginine demethylase JMJD6|jmjC domain-containing protein 6|jumonji domain-containing protein 6|lysyl-hydroxylase JMJD6|peptide-lysine 5-dioxygenase JMJD6|phosphatidylserine receptor JMJD6 OGG:3000023234 Bin Zhao, Yue Liu, Oliver He HDJC9 JDD1 SB73 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC9 DnaJ (Hsp40) homolog, subfamily C, member 9 23234 10q22.2 9606 10 GO_0035176 (EC: IEP) PMID:10231032; 11444854; 12477932; 14702039; 17182002; 19410544; 19710015; 19862764; 20099975; 20379614; 21139048; 21145461; 21531385; 21906983; 21963094; 22939629; 23000965; 24457600 DnaJ (Hsp40) homolog, subfamily C, member 9 HGNC:19123 HPRD:13237 MIM:611206 Other designations: DnaJ protein SB73|dnaJ homolog subfamily C member 9 DNAJC9 OGG:3000023317 Bin Zhao, Yue Liu, Oliver He RME8 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC13 DnaJ (Hsp40) homolog, subfamily C, member 13 23317 3q22.1 9606 3 GO_0005765 (EC: IDA, PMID:17897319); GO_0070062 (EC: IDA, PMID:19056867) PMID:9734811; 12438707; 12477932; 14702039; 15051737; 15302935; 15489334; 15538384; 15840729; 16179350; 17897319; 18256511; 18307993; 19056867; 19874558; 21139048; 21145461; 21674799; 21900206; 21906983; 21963094; 22507240; 23402259; 24250222 DnaJ (Hsp40) homolog, subfamily C, member 13 Ensembl:ENSG00000138246 HGNC:30343 HPRD:10915 MIM:614334 Vega:OTTHUMG00000159674 Other designations: DnaJ domain-containing protein RME-8|RME-8|dnaJ homolog subfamily C member 13|required for receptor-mediated endocytosis 8 DNAJC13 OGG:3000023341 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC16 DnaJ (Hsp40) homolog, subfamily C, member 16 23341 RP4-680D5.1 1p36.1 9606 1 GO_0016021 (EC: IEA); GO_0045454 (EC: IEA) PMID:10231032; 12168954; 12477932; 14702039; 15489334; 16710414; 16751776; 19773279; 21906983; 21963094 DnaJ (Hsp40) homolog, subfamily C, member 16 Other designations: dnaJ homolog subfamily C member 16|novel DnaJ domain-containing protein DNAJC16 OGG:3000023452 Bin Zhao, Yue Liu, Oliver He ARP2 HARP WEB: http://www.ncbi.nlm.nih.gov/gene ANGPTL2 angiopoietin-like 2 23452 RP11-1M19.1 9q34 9606 9 GO_0005102 (EC: TAS, PMID:10473614); GO_0005615 (EC: TAS, PMID:10473614); GO_0007275 (EC: TAS, PMID:10473614); GO_0070062 (EC: IDA, PMID:19056867) PMID:8619474; 9110174; 10473614; 12477932; 12624729; 12975309; 15164053; 15489334; 16303743; 17207965; 17347581; 18593905; 19056867; 19723494; 20304962; 21983347; 22281496; 22345152; 22556334; 22966088; 23333801; 23469106; 23602322 angiopoietin-like 2 Ensembl:ENSG00000136859 HGNC:490 HPRD:05415 MIM:605001 Vega:OTTHUMG00000020695 Other designations: angiopoietin-like protein 2|angiopoietin-related protein 2 ANGPTL2 OGG:3000023475 Bin Zhao, Yue Liu, Oliver He HEL-S-90n QPRTase WEB: http://www.ncbi.nlm.nih.gov/gene QPRT quinolinate phosphoribosyltransferase 23475 16p11.2 9606 16 Official from a nomenclature committee GO_0004514 (EC: IDA, PMID: 17868694); GO_0005829 (EC: TAS); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0009435 (EC: IEA); GO_0019674 (EC: TAS); GO_0034213 (EC: IDA, PMID: 3409840); GO_0042803 (EC: IDA, PMID: 17868694); GO_0044281 (EC: TAS); GO_0051259 (EC: IDA, PMID: 17868694) PMID: 3409840; 9473669; 10721107; 12477932; 14704851; 15489334; 16189514; 17868694; 19321014; 21139048; 21963094; 21988832; 22505724; 23000965 quinolinate phosphoribosyltransferase HGNC:9755 HPRD:06950 MIM:606248 Other designations: QAPRTase|epididymis secretory sperm binding protein Li 90n|nicotinate-nucleotide pyrophosphorylase (carboxylating)|nicotinate-nucleotide pyrophosphorylase [carboxylating] QPRT OGG:3000023581 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CASP14 caspase 14, apoptosis-related cysteine peptidase 23581 19p13.1 9606 19 GO_0004197 (EC: IBA); GO_0005634 (EC: IEA); GO_0005737 (EC: IBA); GO_0008544 (EC: TAS, PMID:10203698); GO_0008630 (EC: IBA); GO_0031424 (EC: TAS, PMID:18309324); GO_0045095 (EC: IEA); GO_0070268 (EC: TAS, PMID:18309324); GO_0097192 (EC: IBA) PMID:1286667; 9792675; 9823333; 10203698; 11062009; 11121154; 11175259; 12181750; 12200134; 12445205; 12477932; 15331408; 15489334; 15619438; 16061209; 16061862; 16168224; 16341674; 16854378; 17207965; 17359582; 17436577; 17558860; 18309324; 18424262; 18762957; 19269008; 19414860; 19573080; 19615732; 19747408; 19773279; 19960512; 20237496; 20402676; 20533828; 20562859; 21139048; 21145461; 21539619; 21567094; 21800051; 21930782; 22354994; 22548721; 22825846; 22876114; 23349634; 23362869; 23377137; 23408445; 23580611; 23750785; 24244333 caspase 14, apoptosis-related cysteine peptidase Other designations: CASP-14|apoptosis-related cysteine protease|caspase 14, apoptosis-related cysteine protease|caspase-14 CASP14 OGG:3000023586 Bin Zhao, Yue Liu, Oliver He RIG-I RIGI RLR-1 WEB: http://www.ncbi.nlm.nih.gov/gene DDX58 DEAD (Asp-Glu-Ala-Asp) box polypeptide 58 23586 RP11-334P12.2 9p12 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0002230 (EC: IMP, PMID: 19609254); GO_0003690 (EC: IEA); GO_0003725 (EC: IDA, PMID: 19576794); GO_0003725 (EC: IMP, PMID: 19211564); GO_0003725 (EC: TAS, PMID: 17079289); GO_0003727 (EC: IMP, PMID: 19211564); GO_0005515 (EC: IPI, PMID: 16127453); GO_0005524 (EC: IEA); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005923 (EC: IDA, PMID: 19122199); GO_0008026 (EC: IEA); GO_0008270 (EC: IDA, PMID: 18243112); GO_0009597 (EC: IDA, PMID: 17079289); GO_0009615 (EC: TAS); GO_0015629 (EC: IDA, PMID: 19122199); GO_0016032 (EC: IEA); GO_0030334 (EC: IDA, PMID: 19122199); GO_0032480 (EC: TAS); GO_0032587 (EC: IDA, PMID: 19122199); GO_0032727 (EC: IDA, PMID: 19576794); GO_0032727 (EC: IMP, PMID: 19609254); GO_0032728 (EC: IDA, PMID: 17079289); GO_0032728 (EC: IMP, PMID: 19211564); GO_0034344 (EC: TAS); GO_0039528 (EC: TAS); GO_0039529 (EC: IMP, PMID: 19211564); GO_0042802 (EC: IPI); GO_0042993 (EC: IDA, PMID: 17079289); GO_0043330 (EC: IEA); GO_0045087 (EC: IMP, PMID: 19609254); GO_0045087 (EC: TAS); GO_0045944 (EC: IDA, PMID: 17079289); GO_0051091 (EC: IC, PMID: 17079289) PMID: 11002417; 11890704; 12477932; 14702039; 15164053; 15181474; 15208624; 15219805; 15297736; 15370293; 15612946; 15708988; 15737993; 15767399; 16009940; 16116171; 16125763; 16127453; 16153868; 16177806; 16182584; 16188996; 16281057; 16306043; 16585524; 16707574; 16797201; 16946700; 17038589; 17038590; 17053203; 17079289; 17093192; 17182220; 17190814; 17307033; 17392790; 17403696; 17516545; 17541283; 17600090; 17719635; 17878351; 17911629; 18021446; 18214119; 18242112; 18243112; 18250407; 18258269; 18268020; 18428149; 18446221; 18550535; 18617992; 18632970; 18635538; 18636086; 18650396; 18684960; 18724357; 18849341; 18948594; 18977754; 18981155; 19017631; 19044019; 19122199; 19154402; 19164550; 19193793; 19201382; 19211564; 19234166; 19324880; 19374188; 19374189; 19419966; 19454348; 19454678; 19478455; 19484123; 19574455; 19576794; 19591957; 19609254; 19615405; 19620789; 19628239; 19628240; 19631370; 19675569; 19846522; 19859543; 19881509; 19890046; 19893624; 19902255; 19922606; 19948350; 19996094; 20001730; 20007272; 20034464; 20042593; 20071582; 20130065; 20144762; 20167631; 20331378; 20400512; 20403326; 20406818; 20410276; 20434986; 20484300; 20492658; 20511549; 20519382; 20581823; 20595247; 20639488; 20805493; 20818395; 20926691; 21068236; 21084468; 21113677; 21187441; 21203974; 21224412; 21233210; 21245912; 21248047; 21288362; 21292167; 21336305; 21501829; 21632559; 21659521; 21690088; 21691053; 21695051; 21811588; 21835791; 21890623; 21899695; 21903422; 21906983; 21910972; 21947008; 21971670; 21978001; 21979817; 22000018; 22000019; 22020100; 22022264; 22067459; 22114345; 22235281; 22301134; 22301138; 22328336; 22402283; 22430200; 22504413; 22607805; 22629479; 22705106; 22745133; 22776165; 22787226; 22862800; 22908223; 22911572; 22912574; 22915805; 22992810; 23000965; 23055530; 23056170; 23060457; 23063562; 23118418; 23185463; 23209422; 23262976; 23264040; 23284052; 23325848; 23333445; 23388719; 23399697; 23434273; 23498958; 23499489; 23592984; 23611287; 23653683; 23671710; 23684307; 23744645; 23772026; 23843640; 23870315; 23950712; 24334410; 24360797; 24391215 DEAD (Asp-Glu-Ala-Asp) box polypeptide 58 Ensembl:ENSG00000107201 HGNC:19102 HPRD:13131 MIM:609631 Vega:OTTHUMG00000019746 Other designations: DEAD box protein 58|DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide|RIG-1|RIG-I-like receptor 1|RNA helicase RIG-I|probable ATP-dependent RNA helicase DDX58|retinoic acid inducible gene I|retinoic acid-inducible gene 1 protein|retinoic acid-inducible gene I protein DDX58 OGG:3000023594 Bin Zhao, Yue Liu, Oliver He ORC6L WEB: http://www.ncbi.nlm.nih.gov/gene ORC6 origin recognition complex, subunit 6 23594 16q12 20140408 9606 16 protein-coding Official from a nomenclature committee GO_0000082 (EC: TAS); GO_0000278 (EC: TAS); GO_0000808 (EC: IDA, PMID: 17716973); GO_0003677 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15232106); GO_0005654 (EC: TAS); GO_0005664 (EC: IEA); GO_0006260 (EC: TAS); GO_0006261 (EC: IEA) PMID: 8266075; 10436018; 10523313; 10945994; 11076863; 11095689; 11125146; 11323433; 11593009; 11931757; 12004060; 12045100; 12169736; 12477932; 12614612; 14702039; 15226314; 15232106; 15489334; 15489336; 15684404; 15707391; 15910003; 16381901; 17081983; 17716973; 18234858; 18761675; 19112505; 19471022; 19541634; 21358632; 21461783; 21502537; 21832049; 21906983; 21963094; 22505724; 23000965; 24250222 origin recognition complex, subunit 6 Ensembl:ENSG00000091651 HGNC:17151 HPRD:06237 MIM:607213 Vega:OTTHUMG00000132539 Other designations: origin recognition complex subunit 6 ORC6 OGG:3000023597 Bin Zhao, Yue Liu, Oliver He ACATE2 MT-ACT48 MTACT48 WEB: http://www.ncbi.nlm.nih.gov/gene ACOT9 acyl-CoA thioesterase 9 23597 CGI-16 Xp22.11 9606 X GO_0003986 (EC: ISS); GO_0005739 (EC: ISS); GO_0006637 (EC: ISS) PMID:10383425; 10810093; 12477932; 14702039; 16103133; 18781797; 20186120; 20360068; 21139048; 21890473; 21906983; 21963094; 22114354; 22268729; 22323290; 22797925; 23956138 acyl-CoA thioesterase 9 Ensembl:ENSG00000123130 HGNC:17152 HPRD:06438 MIM:300862 Vega:OTTHUMG00000021257 Other designations: acyl-CoA thioester hydrolase 9|acyl-Coenzyme A thioesterase 2, mitochondrial|acyl-coenzyme A thioesterase 9, mitochondrial|mitochondrial Acyl-CoA Thioesterase ACOT9 OGG:3000023645 Bin Zhao, Yue Liu, Oliver He GADD34 WEB: http://www.ncbi.nlm.nih.gov/gene PPP1R15A protein phosphatase 1, regulatory subunit 15A 23645 19q13.2 9606 19 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 11564868); GO_0005783 (EC: IEA); GO_0005829 (EC: TAS); GO_0006417 (EC: IEA); GO_0006915 (EC: IEA); GO_0006974 (EC: TAS, PMID: 9153226); GO_0007050 (EC: TAS, PMID: 9153226); GO_0007179 (EC: TAS); GO_0019901 (EC: IPI, PMID: 11517336); GO_0030512 (EC: TAS); GO_0030968 (EC: IEA) PMID: 8125298; 9153226; 9413226; 10434033; 10490642; 10631107; 11104688; 11517336; 11564868; 12016208; 12168790; 12477932; 12556489; 12724406; 12813455; 14635187; 14670976; 14702039; 14718519; 15231748; 15541008; 16169070; 16337513; 16344560; 16455055; 17273797; 18362886; 18794359; 19131336; 19776135; 19901557; 20040105; 20467438; 20800603; 21145461; 21518769; 21988832; 22145905; 23412101; 24092754 protein phosphatase 1, regulatory subunit 15A Ensembl:ENSG00000087074 HGNC:14375 HPRD:06572 MIM:611048 Vega:OTTHUMG00000183330 Other designations: growth arrest and DNA damage-inducible protein GADD34|growth arrest and DNA-damage-inducible 34|myeloid differentiation primary response protein MyD116 homolog|protein phosphatase 1 regulatory subunit 15A|protein phosphatase 1, regulatory (inhibitor) subunit 15A PPP1R15A OGG:3000023659 Bin Zhao, Yue Liu, Oliver He ACS GXVPLA2 LLPL LPLA2 LYPLA3 WEB: http://www.ncbi.nlm.nih.gov/gene PLA2G15 phospholipase A2, group XV 23659 UNQ341/PRO540 16q22.1 9606 16 Official from a nomenclature committee GO_0004622 (EC: TAS, PMID: 10092508); GO_0005543 (EC: TAS, PMID: 10092508); GO_0005576 (EC: IEA); GO_0005739 (EC: IEA); GO_0005764 (EC: ISS); GO_0005764 (EC: NAS, PMID: 11790796); GO_0006672 (EC: IEA); GO_0008374 (EC: ISS); GO_0009062 (EC: TAS, PMID: 10092508); GO_0046470 (EC: IEA); GO_0047499 (EC: ISS) PMID: 8125298; 10092508; 10230407; 10395961; 11790796; 12477932; 12975309; 14702039; 14754907; 15340161; 15489334; 16169070; 16303743; 16973413; 18029348; 18983494; 19461040; 19913121; 20628086; 20877624; 21906983; 22268729 phospholipase A2, group XV Ensembl:ENSG00000103066 HGNC:17163 HPRD:07128 MIM:609362 Vega:OTTHUMG00000137554 Other designations: 1-O-acylceramide synthase|LCAT-like lysophospholipase|group XV phospholipase A2|lysophospholipase 3 (lysosomal phospholipase A2)|lysosomal phospholipase A2 PLA2G15 OGG:3000023753 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene SDF2L1 stromal cell-derived factor 2-like 1 23753 UNQ1941/PRO4424 22q11.21 9606 22 Official from a nomenclature committee GO_0005788 (EC: IEA); GO_0016020 (EC: IEA) PMID: 10591208; 11162531; 12477932; 12975309; 15461802; 15489334; 16396496; 18781797; 19710015; 20811636; 21139048; 21145461; 22190034; 22268729; 22863883; 23444373; 24457600 stromal cell-derived factor 2-like 1 Other designations: OTTHUMT00000075032|PWP1-interacting protein 8|SDF2-like 1|SDF2-like protein 1|dihydropyrimidinase-like 2|stromal cell-derived factor 2-like protein 1 SDF2L1 OGG:3000023766 Bin Zhao, Yue Liu, Oliver He ATG8D WEB: http://www.ncbi.nlm.nih.gov/gene GABARAPL3 GABA(A) receptors associated protein like 3, pseudogene 23766 15q26.1 9606 15 Official from a nomenclature committee GO_0000421 (EC: IEA); GO_0005783 (EC: IEA); GO_0005794 (EC: IEA); GO_0005874 (EC: IEA); GO_0006914 (EC: IEA); GO_0031410 (EC: IEA); GO_0032590 (EC: IEA); GO_0032839 (EC: IEA); GO_0044297 (EC: IEA) PMID: 11414770; 22446963 GABA(A) receptors associated protein like 3, pseudogene HGNC:4069 GABARAPL3 OGG:3000025822 Bin Zhao, Yue Liu, Oliver He Hsc40 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB5 DnaJ (Hsp40) homolog, subfamily B, member 5 25822 RP11-392A14.5 9p13.3 9606 9 GO_0000122 (EC: IEA); GO_0005515 (EC: IPI); GO_0005634 (EC: IEA); GO_0005829 (EC: IEA); GO_0006457 (EC: IEA); GO_0006986 (EC: IEP, PMID:10570961); GO_0051082 (EC: IEA) PMID:7566098; 10570961; 11147971; 12477932; 14702039; 15456869; 18457437; 18555775; 21078624; 21139048; 23000965 DnaJ (Hsp40) homolog, subfamily B, member 5 Ensembl:ENSG00000137094 HGNC:14887 MIM:611328 Vega:OTTHUMG00000019840 Other designations: dnaJ homolog subfamily B member 5|heat shock cognate 40|heat shock protein Hsp40-2|heat shock protein Hsp40-3|heat shock protein cognate 40 DNAJB5 OGG:3000025833 Bin Zhao, Yue Liu, Oliver He Epoc-1 OCT-11 OCT11 OTF-11 PLA-1 PLA1 Skn-1a WEB: http://www.ncbi.nlm.nih.gov/gene POU2F3 POU class 2 homeobox 3 25833 11q23.3 9606 11 Official from a nomenclature committee GO_0003700 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12624109); GO_0005634 (EC: IDA); GO_0005667 (EC: IEA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0006351 (EC: IEA); GO_0006357 (EC: TAS, PMID: 10473598); GO_0008544 (EC: TAS, PMID: 10473598); GO_0030216 (EC: IEA); GO_0042060 (EC: IEA); GO_0043565 (EC: IDA, PMID: 9242494); GO_0043922 (EC: IDA, PMID: 14645924); GO_0045944 (EC: IEA); GO_0046983 (EC: IEA) PMID: 8441607; 9242494; 10473598; 11429405; 12477932; 12624109; 14645924; 14702039; 15077167; 16005513; 16147992; 16607278; 17195013; 17562024; 17989732; 18029348; 18479461; 20379614; 20888799; 21074976; 21906983; 23000965 POU class 2 homeobox 3 Ensembl:ENSG00000137709 HGNC:19864 HPRD:09582 MIM:607394 Vega:OTTHUMG00000166140 Other designations: POU domain transcription factor OCT11a|POU domain, class 2, transcription factor 3|octamer-binding protein 11|octamer-binding transcription factor 11|transcription factor PLA-1|transcription factor Skn-1 POU2F3 OGG:3000025987 Bin Zhao, Yue Liu, Oliver He E2IG4 LRRC54 TSK WEB: http://www.ncbi.nlm.nih.gov/gene TSKU tsukushi, small leucine rich proteoglycan 25987 UNQ850/PRO1788 11q13.5 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0005615 (EC: IEA); GO_0010468 (EC: IEA); GO_0021540 (EC: IEA); GO_0021670 (EC: IEA); GO_0021960 (EC: IEA); GO_0030178 (EC: IEA); GO_0061073 (EC: IEA) PMID: 11085516; 12477932; 12975309; 14702039; 15231748; 15489334; 16303743; 16344560; 19710929; 22880013; 22995554 tsukushi, small leucine rich proteoglycan Ensembl:ENSG00000182704 HGNC:28850 HPRD:12152 MIM:608015 Vega:OTTHUMG00000165238 Other designations: E2-induced gene 4 protein|leucine rich repeat containing 54|leucine-rich repeat-containing protein 54|tsukushi homolog|tsukushi small leucine rich proteoglycan homolog|tsukushin TSKU OGG:3000026027 Bin Zhao, Yue Liu, Oliver He BFIT STARD14 THEA THEM1 WEB: http://www.ncbi.nlm.nih.gov/gene ACOT11 acyl-CoA thioesterase 11 26027 1p32.3 9606 1 GO_0005737 (EC: IC, PMID:11696000); GO_0006631 (EC: NAS, PMID:11696000); GO_0008289 (EC: IEA); GO_0009266 (EC: ISS); GO_0009409 (EC: ISS, PMID:11696000); GO_0035556 (EC: NAS, PMID:11696000); GO_0047617 (EC: TAS, PMID:11696000); GO_0070062 (EC: IDA, PMID:19056867) PMID:8125298; 9734811; 11696000; 12477932; 14702039; 15489334; 16103133; 16344560; 19056867; 19913121; 20379614; 20470824; 20628086; 21738568; 22897136 acyl-CoA thioesterase 11 Ensembl:ENSG00000162390 HGNC:18156 HPRD:07075 MIM:606803 Vega:OTTHUMG00000009891 Other designations: START domain containing 14|StAR-related lipid transfer (START) domain containing 14|acyl-CoA thioester hydrolase 11|acyl-coenzyme A thioesterase 11|adipose-associated thioesterase|brown fat-inducible thioesterase|thioesterase superfamily member 1|thioesterase, adipose associated ACOT11 OGG:3000026061 Bin Zhao, Yue Liu, Oliver He 2-HPCL HPCL HPCL2 PHYH2 WEB: http://www.ncbi.nlm.nih.gov/gene HACL1 2-hydroxyacyl-CoA lyase 1 26061 HSPC279 3p25.1 9606 3 Official from a nomenclature committee GO_0000287 (EC: IEA); GO_0001561 (EC: IDA, PMID: 10468558); GO_0001561 (EC: TAS); GO_0005102 (EC: IPI); GO_0005777 (EC: IDA, PMID: 10468558); GO_0005782 (EC: TAS); GO_0016830 (EC: IDA, PMID: 10468558); GO_0016830 (EC: TAS); GO_0030976 (EC: IDA, PMID: 10468558); GO_0042802 (EC: IPI, PMID: 16189514); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0048037 (EC: IDA, PMID: 15644336); GO_0051259 (EC: IDA) PMID: 10468558; 11042152; 12477932; 14561759; 14702039; 15489334; 15644336; 16189514; 16344560; 16756494; 17370265; 20178365; 21708296; 21890473; 21900206; 21906983; 21963094; 22002062; 22939629; 23000965 2-hydroxyacyl-CoA lyase 1 Ensembl:ENSG00000131373 HGNC:17856 HPRD:09183 MIM:604300 Vega:OTTHUMG00000129862 Other designations: 1600020H07Rik|2-hydroxyphytanol-CoA lyase|2-hydroxyphytanoyl-CoA lyase|phytanoyl-CoA 2-hydroxylase 2|phytanoyl-CoA hydroxylase 2 HACL1 OGG:3000026286 Bin Zhao, Yue Liu, Oliver He ARFGAP1 WEB: http://www.ncbi.nlm.nih.gov/gene ARFGAP3 ADP-ribosylation factor GTPase activating protein 3 26286 AL049757.1 22q13.2 9606 22 Official from a nomenclature committee GO_0000139 (EC: IEA); GO_0005737 (EC: IDA); GO_0005794 (EC: IDA); GO_0005829 (EC: IDA, PMID: 11172815); GO_0006886 (EC: NAS, PMID: 11172815); GO_0008060 (EC: IDA, PMID: 11172815); GO_0008270 (EC: IEA); GO_0008565 (EC: NAS, PMID: 11172815); GO_0009306 (EC: IEP, PMID: 11172815); GO_0016192 (EC: NAS, PMID: 11172815); GO_0032312 (EC: IEA); GO_0043547 (EC: IDA, PMID: 11172815) PMID: 8076819; 10591208; 10704287; 11172815; 12477932; 12529303; 14702039; 15461802; 15489334; 15761153; 17081983; 17760859; 18029348; 19015319; 19299515; 20379614; 21139048; 21647875; 21832049; 21890473; 21988832; 23000965; 24250222 ADP-ribosylation factor GTPase activating protein 3 Ensembl:ENSG00000242247 HGNC:661 HPRD:06444 MIM:612439 Vega:OTTHUMG00000150718 Other designations: ADP-ribosylation factor GTPase activating protein 1|ADP-ribosylation factor GTPase-activating protein 3|ARF GAP 3 ARFGAP3 OGG:3000026291 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene FGF21 fibroblast growth factor 21 26291 UNQ3115/PRO10196 19q13.33 9606 19 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 18829467); GO_0005576 (EC: IEA); GO_0007165 (EC: TAS, PMID: 10858549); GO_0007267 (EC: TAS, PMID: 10858549); GO_0008083 (EC: IEA); GO_0008284 (EC: IEA); GO_0010988 (EC: NAS); GO_0045716 (EC: NAS); GO_0046326 (EC: IDA, PMID: 17623664); GO_0070374 (EC: IDA, PMID: 17623664); GO_0090080 (EC: IEA) PMID: 10858549; 12477932; 12975309; 15199049; 15340161; 15902306; 17068132; 17452648; 17623664; 17926232; 18252893; 18559909; 18680716; 18722685; 18829467; 18840768; 19059246; 19117008; 19318452; 19322201; 19401423; 19487637; 19528204; 19531592; 19681655; 19699495; 19702724; 19720803; 19926712; 19953087; 20332535; 20362303; 20451522; 20452080; 20566462; 20566587; 20629328; 20675007; 20682689; 20717167; 21060863; 21123446; 21206918; 21309058; 21373720; 21502324; 21505329; 21521346; 21521350; 21525989; 21596453; 21664250; 21691104; 21696361; 21712364; 21750278; 21767451; 21812521; 21820356; 21849508; 21889884; 21926274; 21926972; 21949781; 21988350; 21988832; 22013098; 22046277; 22136913; 22152380; 22190000; 22233381; 22248288; 22293928; 22344195; 22378787; 22398021; 22438225; 22442730; 22523080; 22529197; 22539584; 22701542; 22740503; 22881230; 23123503; 23129782; 23270727; 23283977; 23372041; 23533568; 23545215; 23626003; 23636237; 23667629; 23759753; 23768789; 23782039; 23824729; 23887638; 24142477; 24184811 fibroblast growth factor 21 FGF21 OGG:3000026512 Bin Zhao, Yue Liu, Oliver He DBI-1 DDX26 DDX26A DICE1 HDB INT6 Notchl2 WEB: http://www.ncbi.nlm.nih.gov/gene INTS6 integrator complex subunit 6 26512 RP11-24B19.2 13q14.3 9606 13 Official from a nomenclature committee GO_0004888 (EC: TAS, PMID: 10467397); GO_0005515 (EC: IPI, PMID: 16239144); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0007165 (EC: TAS, PMID: 10467397); GO_0015629 (EC: IDA); GO_0016180 (EC: IDA, PMID: 16239144); GO_0032039 (EC: IDA, PMID: 16239144) PMID: 10467397; 11939413; 12477932; 12527901; 14702039; 15057823; 15254679; 15489334; 16007164; 16239144; 16271964; 17310990; 18029348; 18854154; 20133760; 21906983; 21963094; 22360420; 23280823; 24250222; 24457600 integrator complex subunit 6 Ensembl:ENSG00000102786 HGNC:14879 HPRD:05063 MIM:604331 Other designations: DEAD box protein|DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 26|RNA helicase HDB|protein deleted in cancer 1 INTS6 OGG:3000026973 Bin Zhao, Yue Liu, Oliver He CHP1 WEB: http://www.ncbi.nlm.nih.gov/gene CHORDC1 cysteine and histidine-rich domain (CHORD) containing 1 26973 11q14.3 9606 11 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 19875381); GO_0005575 (EC: ND); GO_0006950 (EC: IEA); GO_0008270 (EC: IEA); GO_0010824 (EC: IEA); GO_0051879 (EC: IPI, PMID: 19875381); GO_0061077 (EC: ISS); GO_1900034 (EC: ISS); GO_2000299 (EC: IEA) PMID: 8125298; 8889548; 10571178; 12477932; 12965203; 14702039; 15642353; 16083881; 16344560; 17207965; 18854154; 19875381; 19910486; 20360068; 20800603; 21139048; 21890473; 21906983; 21963094; 22190034; 22833565; 22863883; 23000965; 23184943; 24250222 cysteine and histidine-rich domain (CHORD) containing 1 HGNC:14525 HPRD:05072 MIM:604353 Other designations: CHORD-containing protein 1|CHP-1|chord domain-containing protein 1|cysteine and histidine-rich domain (CHORD)-containing 1|cysteine and histidine-rich domain (CHORD)-containing, zinc-binding protein 1|cysteine and histidine-rich domain-containing protein 1|protein morgana CHORDC1 OGG:3000027000 Bin Zhao, Yue Liu, Oliver He MPHOSPH11 MPP11 ZRF1 ZUO1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC2 DnaJ (Hsp40) homolog, subfamily C, member 2 27000 7q22 9606 7 GO_0003677 (EC: IEA); GO_0003682 (EC: IDA); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA); GO_0005829 (EC: IDA, PMID:16002468); GO_0006260 (EC: IEA); GO_0006351 (EC: IEA); GO_0016568 (EC: IEA); GO_0030308 (EC: IEA); GO_0030544 (EC: IPI, PMID:16002468); GO_0031965 (EC: IDA); GO_0042393 (EC: IDA); GO_0043130 (EC: IDA); GO_0044822 (EC: IDA); GO_0045893 (EC: IDA); GO_0051083 (EC: TAS, PMID:16002468); GO_2000279 (EC: IEA) PMID:8885239; 11034098; 12477932; 12800198; 14696097; 14702039; 15802566; 16002468; 16344560; 17081983; 18029348; 18399720; 20231810; 21139048; 21179169; 21906983; 22433847; 22733129; 24449271 DnaJ (Hsp40) homolog, subfamily C, member 2 Ensembl:ENSG00000105821 HGNC:13192 MIM:605502 Vega:OTTHUMG00000157202 Other designations: M-phase phosphoprotein 11|dnaJ homolog subfamily C member 2|zuotin related factor 1|zuotin-related factor 1 DNAJC2 OGG:3000027102 Bin Zhao, Yue Liu, Oliver He HCR HRI WEB: http://www.ncbi.nlm.nih.gov/gene EIF2AK1 eukaryotic translation initiation factor 2-alpha kinase 1 27102 PRO1362 7p22 9606 7 GO_0004694 (EC: IDA, PMID:11036079); GO_0005524 (EC: IEA); GO_0005737 (EC: IEA); GO_0006950 (EC: IEP, PMID:11036079); GO_0008285 (EC: IEA); GO_0009605 (EC: IEP, PMID:11036079); GO_0010999 (EC: IEA); GO_0020037 (EC: ISS); GO_0042803 (EC: ISS); GO_0045993 (EC: NAS, PMID:11036079); GO_0046501 (EC: IEA); GO_0046777 (EC: ISS); GO_0046986 (EC: ISS) PMID:1677563; 7709427; 9819435; 10542257; 10718198; 10931946; 11036079; 11076863; 11101152; 11230166; 11256614; 12391722; 12477932; 12690205; 12767237; 12853948; 14702039; 15489334; 15489336; 16381901; 17081983; 19133234; 19851296; 20071449; 20198315; 21139048; 21906983; 21963094; 22939624; 22990118; 23357686; 23392680; 23874749; 24250222 eukaryotic translation initiation factor 2-alpha kinase 1 Ensembl:ENSG00000086232 HGNC:24921 HPRD:10684 MIM:613635 Vega:OTTHUMG00000090689 Other designations: heme regulated initiation factor 2 alpha kinase|heme sensitive initiation factor 2a kinase|heme-controlled repressor|heme-regulated eukaryotic initiation factor eIF-2-alpha kinase|heme-regulated inhibitor|heme-regulated initiation factor 2-alpha kinase|heme-regulated repressor|hemin-sensitive initiation factor 2-alpha kinase EIF2AK1 OGG:3000027178 Bin Zhao, Yue Liu, Oliver He FIL1 FIL1(ZETA) FIL1Z IL-1F7 IL-1H IL-1H4 IL-1RP1 IL-37 IL1F7 IL1H4 IL1RP1 WEB: http://www.ncbi.nlm.nih.gov/gene IL37 interleukin 37 27178 2q12-q14.1 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0005125 (EC: IEA); GO_0005149 (EC: NAS, PMID: 10744718); GO_0005149 (EC: TAS, PMID: 10625660); GO_0005576 (EC: NAS, PMID: 10625660); GO_0005576 (EC: TAS, PMID: 10744718); GO_0005615 (EC: IEA); GO_0005634 (EC: IEA); GO_0005829 (EC: IEA); GO_0006954 (EC: IEA); GO_0006955 (EC: NAS, PMID: 10625660) PMID: 8188271; 9169134; 10512743; 10625660; 10744718; 10860666; 11093146; 11145836; 11278614; 11466363; 11574262; 11991722; 11991723; 12096920; 12381835; 12477932; 12496389; 15489334; 15527767; 15815621; 17207965; 18390730; 18484691; 19874811; 20141484; 20237496; 20935647; 21072596; 21394384; 21873195; 22646996; 23159404; 23171316; 23182761; 23600829; 23932459 interleukin 37 Ensembl:ENSG00000125571 HGNC:15563 HPRD:05695 MIM:605510 Vega:OTTHUMG00000131345 IL37 OGG:3000027241 Bin Zhao, Yue Liu, Oliver He B1 C18 D1 PTHB1 WEB: http://www.ncbi.nlm.nih.gov/gene BBS9 Bardet-Biedl syndrome 9 27241 7p14 9606 7 Official from a nomenclature committee GO_0003674 (EC: ND); GO_0005515 (EC: IPI, PMID: 17574030); GO_0005737 (EC: IEA); GO_0005815 (EC: IEA); GO_0007601 (EC: IEA); GO_0015031 (EC: IEA); GO_0030030 (EC: IEA); GO_0034464 (EC: IDA, PMID: 17574030); GO_0045444 (EC: ISS); GO_0050896 (EC: IEA); GO_0060170 (EC: IEA) PMID: 10221542; 12477932; 12618763; 12690205; 14702039; 15489334; 16380913; 17574030; 18029348; 18349106; 20161521; 20301537; 20379614; 20801516; 22479622; 23160099; 24250222 Bardet-Biedl syndrome 9 Ensembl:ENSG00000122507 HGNC:30000 HPRD:16262 MIM:607968 Vega:OTTHUMG00000128659 Other designations: PTH-responsive osteosarcoma B1 protein|bardet-Biedl syndrome 9 protein|parathyroid hormone-responsive B1 gene protein|protein PTHB1 BBS9 OGG:3000027242 Bin Zhao, Yue Liu, Oliver He BM-018 CD358 DR6 WEB: http://www.ncbi.nlm.nih.gov/gene TNFRSF21 tumor necrosis factor receptor superfamily, member 21 27242 UNQ437/PRO868 6p21.1 9606 6 Official from a nomenclature committee GO_0001783 (EC: ISS); GO_0002250 (EC: ISS); GO_0005515 (EC: IPI, PMID: 19225519); GO_0005886 (EC: TAS); GO_0005887 (EC: IDA, PMID: 19654028); GO_0006915 (EC: IMP); GO_0006959 (EC: ISS); GO_0030424 (EC: IEA); GO_0030889 (EC: ISS); GO_0031226 (EC: ISS); GO_0031642 (EC: IMP); GO_0042130 (EC: ISS); GO_0042552 (EC: ISS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0048713 (EC: ISS); GO_0050852 (EC: ISS); GO_0051402 (EC: ISS); GO_0071356 (EC: IDA, PMID: 19654028); GO_0097252 (EC: ISS); GO_2000663 (EC: ISS); GO_2000666 (EC: ISS); GO_2001180 (EC: ISS) PMID: 9714541; 11485735; 11714751; 11753679; 12477932; 12975309; 14574404; 14702039; 15301860; 15489334; 15623156; 16378686; 17962943; 18029348; 19165232; 19225519; 19322201; 19654028; 20237496; 20819778; 21337622; 21501873; 21900206; 22297296; 22525750; 22567163; 22761420; 24374337 tumor necrosis factor receptor superfamily, member 21 Ensembl:ENSG00000146072 HGNC:13469 HPRD:05759 MIM:605732 Vega:OTTHUMG00000014796 Other designations: TNFR-related death receptor 6|death receptor 6|tumor necrosis factor receptor superfamily member 21 TNFRSF21 OGG:3000027244 Bin Zhao, Yue Liu, Oliver He PA26 SEST1 WEB: http://www.ncbi.nlm.nih.gov/gene SESN1 sestrin 1 27244 RP11-787I22.2 6q21 9606 6 Official from a nomenclature committee GO_0005634 (EC: IEA); GO_0006974 (EC: TAS, PMID: 9926927); GO_0007050 (EC: IEA); GO_0008285 (EC: TAS, PMID: 9926927) PMID: 7938006; 8889548; 9926927; 12477932; 12607115; 14702039; 15105503; 16751804; 18692468; 18703169; 19704005; 20800603; 21067298; 21890473; 21906983; 23000965; 23274085; 23535732; 24250222 sestrin 1 Ensembl:ENSG00000080546 HGNC:21595 HPRD:07310 MIM:606103 Vega:OTTHUMG00000015338 Other designations: p53 activated gene 26|p53 regulated PA26 nuclear protein|sestrin-1 SESN1 OGG:3000027286 Bin Zhao, Yue Liu, Oliver He BPP CBPS PMGX RESDX SRPUL WEB: http://www.ncbi.nlm.nih.gov/gene SRPX2 sushi-repeat containing protein, X-linked 2 27286 RP11-524D16__A.1 Xq21.33-q23 20140408 9606 X protein-coding Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0005102 (EC: IPI, PMID: 18718938); GO_0005515 (EC: IPI, PMID: 18718938); GO_0005615 (EC: IDA); GO_0005737 (EC: IDA, PMID: 19065654); GO_0009986 (EC: ISS); GO_0016337 (EC: IDA, PMID: 19065654); GO_0030054 (EC: IEA); GO_0036458 (EC: IDA); GO_0042325 (EC: IDA, PMID: 19065654); GO_0042802 (EC: IDA); GO_0048870 (EC: IDA, PMID: 19065654); GO_0051965 (EC: IDA); GO_0060076 (EC: ISS); GO_0090050 (EC: ISS); GO_0097060 (EC: ISS) PMID: 209648; 9864177; 11375929; 11822025; 12477932; 15342556; 15489334; 15772651; 16303743; 16344560; 16497722; 17942002; 18029348; 18718938; 19065654; 19667118; 20236627; 20858596; 22242148; 23115050; 23933820; 24179158 sushi-repeat containing protein, X-linked 2 Ensembl:ENSG00000102359 HGNC:30668 HPRD:06726 MIM:300642 Vega:OTTHUMG00000022003 Other designations: sushi repeat-containing protein SRPX2|sushi-repeat protein up-regulated in leukemia|sushi-repeat protein upregulated in leukemia|sushi-repeat-containing protein, X-linked 2 SRPX2 OGG:3000027329 Bin Zhao, Yue Liu, Oliver He ANG-5 ANGPT5 ANL3 FHBL2 WEB: http://www.ncbi.nlm.nih.gov/gene ANGPTL3 angiopoietin-like 3 27329 UNQ153/PRO179 1p31.3 9606 1 GO_0004857 (EC: ISS); GO_0004859 (EC: IDA, PMID:17110602); GO_0005178 (EC: IPI, PMID:11877390); GO_0005615 (EC: IDA, PMID:17110602); GO_0006071 (EC: IDA, PMID:12565906); GO_0006631 (EC: IDA, PMID:12565906); GO_0006644 (EC: IDA, PMID:17110602); GO_0007160 (EC: IPI, PMID:11877390); GO_0007165 (EC: IDA, PMID:11877390); GO_0007229 (EC: NAS, PMID:11877390); GO_0008083 (EC: IDA, PMID:11877390); GO_0008203 (EC: IDA, PMID:17110602); GO_0009395 (EC: IDA, PMID:17110602); GO_0009725 (EC: IEA); GO_0009986 (EC: IDA, PMID:12565906); GO_0010519 (EC: IDA, PMID:17110602); GO_0019915 (EC: IDA, PMID:12565906); GO_0030335 (EC: IDA, PMID:11877390); GO_0042632 (EC: IDA, PMID:17110602); GO_0045766 (EC: IDA, PMID:11877390); GO_0048844 (EC: ISS); GO_0050996 (EC: IDA, PMID:12565906); GO_0051005 (EC: IDA, PMID:17110602); GO_0055088 (EC: IDA, PMID:17110602); GO_0055090 (EC: IDA, PMID:17110602); GO_0055091 (EC: IDA, PMID:17110602); GO_0070328 (EC: IGI); GO_0070328 (EC: ISS) PMID:10644446; 11877390; 12477932; 12518032; 12565906; 12672813; 12909640; 12975309; 15094378; 15340161; 15489334; 16335952; 16505486; 16531751; 17110602; 17207965; 17681148; 18063851; 18193043; 18193044; 18279878; 18535744; 18596051; 18804459; 19028676; 19060906; 19075393; 19148283; 19282754; 19318355; 19474742; 19487539; 19540497; 19542565; 19656773; 19826106; 19890028; 19936222; 20139978; 20160193; 20360639; 20570916; 20571754; 20595410; 20679960; 20686565; 20714348; 20837471; 20855565; 20864672; 20942659; 20972250; 21691831; 21983347; 22062970; 22095935; 22155345; 22247256; 22286219; 22659251; 22732211; 22896670; 22916037; 23314748; 23661675; 23839332 angiopoietin-like 3 Ensembl:ENSG00000132855 HGNC:491 HPRD:10381 MIM:604774 Vega:OTTHUMG00000009146 Other designations: angiopoietin 5|angiopoietin-related protein 3 ANGPTL3 OGG:3000027335 Bin Zhao, Yue Liu, Oliver He EIF3-p28 EIF3S12 HSPC029 M9 MSTP001 PLAC-24 PLAC24 PRO1474 PTD001 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3K eukaryotic translation initiation factor 3, subunit K 27335 ARG134 19q13.2 9606 19 GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005515 (EC: IPI); GO_0005634 (EC: IEA); GO_0005829 (EC: TAS); GO_0005852 (EC: IDA, PMID:17322308); GO_0006412 (EC: TAS); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006413 (EC: TAS); GO_0006446 (EC: IEA); GO_0010467 (EC: TAS); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA); GO_0043022 (EC: IEA); GO_0044267 (EC: TAS) PMID:11042152; 12006665; 12477932; 12588972; 14519125; 15180986; 15327989; 15489334; 16189514; 17081983; 17207965; 17322308; 17353931; 17403899; 17581632; 18029348; 18577580; 18599441; 18628297; 19471022; 19615732; 19738201; 20360068; 21139048; 21693764; 21890473; 21906983; 21963094; 21987572; 21988832; 22053931; 22190034; 22505724; 22623428; 22678362; 22779921; 22863883; 22939629; 23000965; 23349634; 23463506; 24036361; 24250222 eukaryotic translation initiation factor 3, subunit K Ensembl:ENSG00000178982 HGNC:24656 HPRD:11740 MIM:609596 Vega:OTTHUMG00000180865 Other designations: eIF-3 p25|eIF-3 p28|eukaryotic translation initiation factor 3 subunit 12|eukaryotic translation initiation factor 3 subunit K|eukaryotic translation initiation factor 3, subunit 12|muscle specific|muscle-specific gene M9 protein EIF3K OGG:3000029028 Bin Zhao, Yue Liu, Oliver He ANCCA CT137 PRO2000 WEB: http://www.ncbi.nlm.nih.gov/gene ATAD2 ATPase family, AAA domain containing 2 29028 L16 8q24.13 20140408 9606 8 protein-coding Official from a nomenclature committee GO_0005524 (EC: IEA); GO_0005634 (EC: IEA); GO_0006200 (EC: IDA, PMID: 17998543); GO_0006351 (EC: IEA); GO_0016887 (EC: IDA, PMID: 17998543); GO_0045893 (EC: IDA, PMID: 17998543); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 12477932; 14702039; 15302935; 15334068; 15342556; 15489334; 16712791; 17081983; 17998543; 18029348; 19056867; 19318566; 19471022; 19843847; 20374707; 20855524; 20864510; 21139048; 21252943; 21693764; 21890473; 21906983; 22178446; 22586326; 22771493; 22914773; 23000965; 23393560; 23752268 ATPase family, AAA domain containing 2 Ensembl:ENSG00000156802 HGNC:30123 HPRD:10678 MIM:611941 Vega:OTTHUMG00000165090 Other designations: AAA nuclear coregulator cancer-associated protein|ATPase family AAA domain-containing protein 2 ATAD2 OGG:3000029078 Bin Zhao, Yue Liu, Oliver He C6orf66 HRPAP20 My013 bA22L21.1 WEB: http://www.ncbi.nlm.nih.gov/gene NDUFAF4 NADH dehydrogenase (ubiquinone) complex I, assembly factor 4 29078 HSPC125 6q16.1 9606 6 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 19463981); GO_0005516 (EC: IEA); GO_0005739 (EC: IDA); GO_0031966 (EC: IDA, PMID: 19463981); GO_0032981 (EC: IMP, PMID: 18179882) PMID: 11042152; 12477932; 14574404; 14871833; 15342556; 15489334; 16344560; 17001319; 17909269; 18029348; 18179882; 19352385; 19463981; 20877624; 21890473; 21906983; 21963094; 22939629; 23670274; 24250222 NADH dehydrogenase (ubiquinone) complex I, assembly factor 4 Ensembl:ENSG00000123545 HGNC:21034 HPRD:10795 MIM:611776 Vega:OTTHUMG00000015246 Other designations: NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, assembly factor 4|NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4|hormone-regulated proliferation-associated protein of 20 kDa|hormone-regulated proliferation-associated protein, 20 kDa NDUFAF4 OGG:3000029089 Bin Zhao, Yue Liu, Oliver He PIG50 WEB: http://www.ncbi.nlm.nih.gov/gene UBE2T ubiquitin-conjugating enzyme E2T (putative) 29089 HSPC150 1q32.1 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0003682 (EC: IDA, PMID: 17938197); GO_0004842 (EC: IDA, PMID: 16916645); GO_0005524 (EC: IEA); GO_0005634 (EC: TAS, PMID: 17938197); GO_0005654 (EC: TAS); GO_0006281 (EC: IMP, PMID: 16916645); GO_0006281 (EC: TAS); GO_0006513 (EC: IDA, PMID: 16916645); GO_0006974 (EC: IMP, PMID: 16916645); GO_0031625 (EC: IPI, PMID: 16916645); GO_0035519 (EC: IDA); GO_0044314 (EC: IDA); GO_0051865 (EC: IDA, PMID: 16916645); GO_0070534 (EC: IDA); GO_0070936 (EC: IDA); GO_0070979 (EC: IDA); GO_0085020 (EC: IDA) PMID: 10931946; 11042152; 12477932; 12938929; 14702039; 15489334; 16196087; 16710414; 16916645; 17203973; 17938197; 18029348; 18667844; 18781797; 19111657; 19471022; 19549727; 19589784; 19690564; 19887602; 20639865; 21139048; 21693764; 21722982; 21775430; 21890473; 21906983; 21963094; 22053931; 22287633; 22505724; 22939629; 23000965; 23535733; 23936387; 24250222; 24389026 ubiquitin-conjugating enzyme E2T (putative) Ensembl:ENSG00000077152 HGNC:25009 HPRD:13704 MIM:610538 Vega:OTTHUMG00000041392 Other designations: HSPC150 protein similar to ubiquitin-conjugating enzyme|cell proliferation-inducing gene 50 protein|ubiquitin carrier protein T|ubiquitin conjugating enzyme|ubiquitin-conjugating enzyme E2 T|ubiquitin-protein ligase T UBE2T OGG:3000029103 Bin Zhao, Yue Liu, Oliver He DNAJD1 HSD18 MCJ WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC15 DnaJ (Hsp40) homolog, subfamily C, member 15 29103 GIG22 13q14.1 9606 13 GO_0005743 (EC: IEA); GO_0015031 (EC: IEA); GO_0016021 (EC: IEA) PMID:11358853; 12477932; 14729589; 15057823; 15489334; 16049974; 17283040; 18029348; 18324624; 19322201; 19734545; 20877624; 23263864 DnaJ (Hsp40) homolog, subfamily C, member 15 Ensembl:ENSG00000120675 HGNC:20325 HPRD:13238 MIM:615339 Vega:OTTHUMG00000016813 Other designations: DNAJ domain-containing|DnaJ (Hsp40) homolog, subfamily D, member 1|cell growth-inhibiting gene 22 protein|dnaJ homolog subfamily C member 15|methylation-controlled J protein DNAJC15 OGG:3000029108 Bin Zhao, Yue Liu, Oliver He ASC CARD5 TMS TMS-1 TMS1 WEB: http://www.ncbi.nlm.nih.gov/gene PYCARD PYD and CARD domain containing 29108 16p11.2 20140408 9606 16 protein-coding Official from a nomenclature committee GO_0001773 (EC: IMP); GO_0002020 (EC: IEA); GO_0002218 (EC: IDA); GO_0002230 (EC: IEA); GO_0002277 (EC: ISS); GO_0002588 (EC: ISS); GO_0002821 (EC: IMP); GO_0005515 (EC: IPI, PMID: 11786556); GO_0005576 (EC: IEA); GO_0005634 (EC: IDA); GO_0005634 (EC: ISS); GO_0005730 (EC: IDA); GO_0005737 (EC: IDA); GO_0005737 (EC: NAS, PMID: 12019269); GO_0005739 (EC: IDA, PMID: 14730312); GO_0005783 (EC: IEA); GO_0005829 (EC: TAS); GO_0006915 (EC: TAS, PMID: 10567338); GO_0006919 (EC: NAS, PMID: 12019269); GO_0006954 (EC: IEA); GO_0007165 (EC: NAS, PMID: 12019269); GO_0008385 (EC: IDA, Qualifier: colocalizes_with, PMID: 12486103); GO_0008385 (EC: TAS, PMID: 12656673); GO_0008656 (EC: NAS, PMID: 12019269); GO_0010803 (EC: IMP, PMID: 14730312); GO_0030838 (EC: ISS); GO_0031647 (EC: ISS); GO_0032088 (EC: IMP, PMID: 16585594); GO_0032090 (EC: IPI, PMID: 15030775); GO_0032314 (EC: IEA); GO_0032611 (EC: IEA); GO_0032688 (EC: IMP, PMID: 19158675); GO_0032729 (EC: ISS); GO_0032755 (EC: ISS); GO_0032760 (EC: IMP, PMID: 16982856); GO_0033209 (EC: IDA, PMID: 12656673); GO_0035872 (EC: TAS); GO_0042104 (EC: ISS); GO_0042771 (EC: IMP, PMID: 14730312); GO_0042803 (EC: IDA, PMID: 15030775); GO_0043025 (EC: IEA); GO_0043065 (EC: IDA, PMID: 12646168); GO_0043124 (EC: IDA, PMID: 12486103); GO_0043280 (EC: IDA, PMID: 15030775); GO_0044325 (EC: IEA); GO_0044351 (EC: ISS); GO_0045087 (EC: TAS); GO_0046330 (EC: IMP); GO_0050718 (EC: IDA, PMID: 15030775); GO_0050727 (EC: IEA); GO_0050766 (EC: ISS); GO_0050829 (EC: IMP, PMID: 16982856); GO_0050870 (EC: IMP); GO_0051091 (EC: IDA, PMID: 19494289); GO_0051092 (EC: IDA, PMID: 12646168); GO_0051607 (EC: IDA); GO_0070374 (EC: IMP); GO_0071222 (EC: IDA, PMID: 12486103); GO_0071347 (EC: IDA, PMID: 12486103); GO_0071356 (EC: IDA, PMID: 12486103); GO_0071901 (EC: IDA, PMID: 12486103); GO_0072332 (EC: IMP, PMID: 14730312); GO_0072558 (EC: IDA, PMID: 12191486); GO_0072559 (EC: IDA, PMID: 15030775); GO_0090197 (EC: IMP); GO_0090200 (EC: IDA, PMID: 14730312); GO_0097169 (EC: IDA, PMID: 19158676); GO_2000406 (EC: ISS); GO_2000484 (EC: IMP, PMID: 16982856); GO_2000778 (EC: IMP, PMID: 16982856); GO_2001056 (EC: IDA, PMID: 19158676); GO_2001181 (EC: IMP, PMID: 16982856); GO_2001238 (EC: IDA, PMID: 16964285); GO_2001242 (EC: IDA, PMID: 14730312) PMID: 10567338; 10847592; 11103776; 11103777; 11250163; 11374873; 11498534; 11733524; 11786556; 11967258; 12019269; 12054656; 12191486; 12477932; 12486103; 12553049; 12615073; 12646168; 12656673; 12776200; 12800194; 12949795; 14499617; 14634131; 14643031; 14702039; 14730312; 14985395; 15020601; 15030775; 15041718; 15456791; 15489334; 15641782; 15701651; 16037825; 16189514; 16425203; 16585594; 16715133; 16777061; 16848908; 16964285; 16982856; 17048097; 17178784; 17339483; 17418785; 17599361; 17964261; 17986858; 18263805; 18311798; 18348116; 18701507; 18791131; 18945969; 19158675; 19158676; 19158679; 19201894; 19223547; 19234215; 19258216; 19324871; 19443857; 19494289; 19636848; 19661336; 19759015; 19759850; 20020448; 20140741; 20148899; 20500518; 20808838; 20926535; 21036703; 21058222; 21104989; 21270336; 21487011; 21832064; 21890473; 22230750; 22286270; 22295065; 22732093; 22931929; 22934972; 23064206; 23066025; 23090995; 23110696; 23209292; 23839215 PYD and CARD domain containing Ensembl:ENSG00000103490 HGNC:16608 HPRD:06020 MIM:606838 Vega:OTTHUMG00000176753 Other designations: apoptosis-associated speck-like protein containing a CARD|caspase recruitment domain-containing protein 5|target of methylation-induced silencing 1 PYCARD OGG:3000029110 Bin Zhao, Yue Liu, Oliver He NAK T2K WEB: http://www.ncbi.nlm.nih.gov/gene TBK1 TANK-binding kinase 1 29110 12q14.1 20140408 9606 12 protein-coding Official from a nomenclature committee GO_0002224 (EC: TAS); GO_0002756 (EC: TAS); GO_0003676 (EC: IEA); GO_0004672 (EC: NAS, PMID: 10581243); GO_0004674 (EC: TAS); GO_0005515 (EC: IPI, PMID: 14743216); GO_0005524 (EC: IEA); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006954 (EC: TAS); GO_0007249 (EC: TAS); GO_0009615 (EC: TAS); GO_0010008 (EC: TAS); GO_0010629 (EC: IEA); GO_0016032 (EC: IEA); GO_0032480 (EC: TAS); GO_0032481 (EC: TAS); GO_0032606 (EC: TAS); GO_0032727 (EC: IDA, PMID: 16127453); GO_0032728 (EC: IDA, PMID: 16127453); GO_0033138 (EC: NAS); GO_0034138 (EC: TAS); GO_0034142 (EC: TAS); GO_0035666 (EC: TAS); GO_0043123 (EC: IEP, PMID: 12761501); GO_0045087 (EC: TAS); GO_0045359 (EC: IEA); GO_0045944 (EC: IDA, PMID: 16127453); GO_0050830 (EC: IEA); GO_0051219 (EC: IPI, PMID: 14530355); GO_0051607 (EC: IEA) PMID: 7706279; 8601309; 9721103; 10581243; 10783893; 10990461; 11839743; 12133833; 12477932; 12568715; 12692549; 12702806; 12761501; 14530355; 14560022; 14702039; 14743216; 15276183; 15367631; 15485837; 15489227; 15489334; 15556946; 15619605; 15661910; 15695821; 15841462; 16051665; 16127453; 16153868; 16155125; 16223731; 16281057; 16344560; 16380379; 16393995; 16394098; 16537515; 16887178; 16888014; 16914100; 16973572; 17018283; 17327220; 17526488; 17568778; 17599067; 17823124; 17991829; 18307994; 18353649; 18508731; 18583960; 18614628; 18636086; 18977754; 19017982; 19153231; 19160540; 19307177; 19380831; 19419966; 19615732; 19656901; 19820708; 19847166; 19953087; 19955181; 19958770; 20098747; 20174559; 20304918; 20331378; 20449947; 20462248; 20562859; 20588308; 20628368; 21048031; 21074459; 21139048; 21204785; 21270402; 21332394; 21364999; 21447600; 21464307; 21492457; 21617041; 21813773; 21832049; 21868362; 21885437; 21903422; 21906983; 21911421; 21931631; 21939555; 21963094; 21987572; 21988832; 22072751; 22079989; 22127978; 22261722; 22306015; 22330071; 22388039; 22394562; 22505724; 22610919; 22619329; 22745133; 22787218; 22792062; 22851595; 22851696; 22908223; 22939624; 22945920; 23007157; 23028469; 23096996; 23157677; 23209807; 23286385; 23308279; 23395611; 23395801; 23453972; 23542348; 23649622; 23675467; 23717208; 23836654; 23950712; 23962979; 24027431; 24056301; 24062311; 24250222; 24255178; 24449872 TANK-binding kinase 1 Ensembl:ENSG00000183735 HGNC:11584 HPRD:05322 MIM:604834 Vega:OTTHUMG00000168796 Other designations: NF-kB-activating kinase|NF-kappa-B-activating kinase|serine/threonine-protein kinase TBK1 TBK1 OGG:3000029118 Bin Zhao, Yue Liu, Oliver He GRTH WEB: http://www.ncbi.nlm.nih.gov/gene DDX25 DEAD (Asp-Glu-Ala-Asp) box helicase 25 29118 11q24 9606 11 Official from a nomenclature committee GO_0003723 (EC: IEA); GO_0004004 (EC: ISS); GO_0005524 (EC: ISS); GO_0005634 (EC: ISS); GO_0005737 (EC: ISS); GO_0006200 (EC: ISS); GO_0006406 (EC: ISS); GO_0006417 (EC: ISS); GO_0007275 (EC: IEA); GO_0007286 (EC: ISS); GO_0033391 (EC: ISS) PMID: 10608860; 12477932; 15094194; 15096601; 15489334; 16293649; 17848414; 17889551; 19536092; 19875492; 20378615 DEAD (Asp-Glu-Ala-Asp) box helicase 25 Ensembl:ENSG00000109832 HGNC:18698 HPRD:06367 MIM:607663 Vega:OTTHUMG00000165859 Other designations: ATP-dependent RNA helicase DDX25|DEAD (Asp-Glu-Ala-Asp) box polypeptide 25|DEAD box protein 25|DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 25|gonadotropin-regulated testicular RNA helicase DDX25 OGG:3000029128 Bin Zhao, Yue Liu, Oliver He ICBP90 Np95 RNF106 hNP95 hUHRF1 huNp95 WEB: http://www.ncbi.nlm.nih.gov/gene UHRF1 ubiquitin-like with PHD and ring finger domains 1 29128 19p13.3 20140408 9606 19 protein-coding Official from a nomenclature committee GO_0000122 (EC: IDA); GO_0000790 (EC: IDA, PMID: 17673620); GO_0000790 (EC: ISS); GO_0000791 (EC: IDA); GO_0000792 (EC: IDA, PMID: 17967883); GO_0000987 (EC: IDA, PMID: 10646863); GO_0003700 (EC: TAS, PMID: 1868030); GO_0004842 (EC: IDA, PMID: 17967883); GO_0004842 (EC: ISS); GO_0005515 (EC: IPI, PMID: 15361834); GO_0005634 (EC: IDA, PMID: 10646863); GO_0005657 (EC: IDA, PMID: 17673620); GO_0006281 (EC: IEA); GO_0006351 (EC: IEA); GO_0007049 (EC: IEA); GO_0008270 (EC: IDA); GO_0008283 (EC: IEP, PMID: 15361834); GO_0008327 (EC: IDA, PMID: 15361834); GO_0010216 (EC: IMP, PMID: 17673620); GO_0010390 (EC: ISS); GO_0016363 (EC: ISS); GO_0016574 (EC: IDA, PMID: 17967883); GO_0031493 (EC: ISS); GO_0032270 (EC: IDA, PMID: 10646863); GO_0035064 (EC: IDA, PMID: 17967883); GO_0042393 (EC: IDA); GO_0042787 (EC: IDA); GO_0042802 (EC: ISS); GO_0044729 (EC: IDA, PMID: 17673620); GO_0045944 (EC: IC, PMID: 10646863); GO_0051865 (EC: IDA, PMID: 17967883); GO_2000373 (EC: IC, PMID: 10646863) PMID: 1868030; 8889549; 10646863; 11290415; 12477932; 12838312; 14702039; 14993289; 15009091; 15033738; 15057824; 15146197; 15178447; 15361834; 15964557; 16007129; 16195352; 16344560; 16964243; 17065439; 17067204; 17081983; 17370265; 17673620; 17934516; 17967883; 18005238; 18772889; 18781797; 18945682; 19056828; 19077538; 19270723; 19322201; 19328461; 19471022; 19491893; 19798101; 19800870; 19851296; 19943104; 20037778; 20198315; 20613874; 21045206; 21067293; 21139048; 21214517; 21252943; 21268065; 21296067; 21351083; 21489993; 21539450; 21611839; 21745816; 21777816; 21808300; 21890473; 21906983; 21963094; 22055183; 22064703; 22096602; 22100450; 22219067; 22285022; 22286757; 22294699; 22330138; 22411829; 22505724; 22552622; 22837395; 22939629; 22945642; 23000965; 23022729; 23023523; 23107467; 23161542; 23245651; 23281010; 23297342; 23463006; 23537643; 23677994; 23752590; 23943380; 24005809; 24013172; 24035451; 24134914; 24324066; 24368767; 24457600; 24469333; 24486181 ubiquitin-like with PHD and ring finger domains 1 HGNC:12556 HPRD:06992 MIM:607990 Other designations: E3 ubiquitin-protein ligase UHRF1|RING finger protein 106|inverted CCAAT box-binding protein of 90 kDa|nuclear phosphoprotein 95|nuclear protein 95|nuclear zinc finger protein Np95|transcription factor ICBP90|ubiquitin-like PHD and RING finger domain-containing protein 1|ubiquitin-like, containing PHD and RING finger domains, 1 UHRF1 OGG:3000029785 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CYP2S1 cytochrome P450, family 2, subfamily S, polypeptide 1 29785 UNQ891/PRO1906 19q13.1 9606 19 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA) PMID:7566098; 11181079; 12477932; 12711469; 12721789; 12975309; 14702039; 15128046; 15450424; 15489334; 17277313; 17280660; 17495422; 17529885; 19343046; 19368491; 19713358; 21139048; 21319273; 21430234; 22039172; 22232929; 22863683; 23224081; 23648403 cytochrome P450, family 2, subfamily S, polypeptide 1 Other designations: CYPIIS1|cytochrome P450 2S1|cytochrome P450 family member predicted from ESTs|cytochrome P540, subfamily IIS, polypeptide 1 CYP2S1 OGG:3000029896 Bin Zhao, Yue Liu, Oliver He AWMS1 HSU53209 WEB: http://www.ncbi.nlm.nih.gov/gene TRA2A transformer 2 alpha homolog (Drosophila) 29896 7p15.3 9606 7 Official from a nomenclature committee GO_0000166 (EC: IEA); GO_0000398 (EC: IDA, PMID: 9546399); GO_0005634 (EC: IDA, PMID: 9546399); GO_0005730 (EC: IDA); GO_0043231 (EC: IDA); GO_0044822 (EC: IDA) PMID: 8799144; 9546399; 9847074; 12477932; 12761501; 14729963; 14765198; 15324660; 15342556; 15489334; 16097034; 16964243; 17081983; 19322201; 19471022; 20508642; 21110914; 21139048; 21145461; 21382349; 21447598; 21890473; 21900206; 21906983; 21988832; 22094256; 22365833; 22939629; 22990118; 23000965; 23084401; 23255807; 23602568; 24457600 transformer 2 alpha homolog (Drosophila) Ensembl:ENSG00000164548 HGNC:16645 HPRD:04096 MIM:602718 Vega:OTTHUMG00000128459 Other designations: TRA-2 alpha|TRA2-alpha|Tra2alpha|htra-2 alpha|htra-2-alpha|putative MAPK activating protein PM24|transformer-2 alpha|transformer-2 protein homolog A|transformer-2 protein homolog alpha TRA2A OGG:3000029923 Bin Zhao, Yue Liu, Oliver He C7orf68 HIG-2 HIG2 WEB: http://www.ncbi.nlm.nih.gov/gene HILPDA hypoxia inducible lipid droplet-associated 29923 7q32.1 20140408 9606 7 protein-coding Official from a nomenclature committee GO_0001819 (EC: IDA); GO_0005102 (EC: IPI, PMID: 15930302); GO_0005515 (EC: IPI, PMID: 15930302); GO_0005615 (EC: IDA, PMID: 15930302); GO_0005811 (EC: IDA); GO_0006950 (EC: NAS, PMID: 10690527); GO_0008284 (EC: IDA, PMID: 15930302); GO_0009986 (EC: IDA, PMID: 15930302); GO_0010884 (EC: IDA); GO_0016021 (EC: IEA); GO_0030141 (EC: IDA, PMID: 15930302); GO_0035425 (EC: IDA, PMID: 15930302) PMID: 8125298; 10690527; 12477932; 12690205; 15489334; 15642117; 15930302; 18550099; 20134266; 20624928; 21124928; 21614900; 21906983; 23916472; 24250222 hypoxia inducible lipid droplet-associated Ensembl:ENSG00000135245 HGNC:28859 HPRD:17105 Vega:OTTHUMG00000157712 Other designations: hypoxia inducible gene 2|hypoxia-inducible gene 2 protein|hypoxia-inducible lipid droplet-associated protein|hypoxia-inducible protein 2 HILPDA OGG:3000029948 Bin Zhao, Yue Liu, Oliver He BDGI OKL38 WEB: http://www.ncbi.nlm.nih.gov/gene OSGIN1 oxidative stress induced growth inhibitor 1 29948 16q23.3 9606 16 Official from a nomenclature committee GO_0005575 (EC: ND); GO_0007275 (EC: IEA); GO_0008083 (EC: IDA, PMID: 11459809); GO_0030154 (EC: IEA); GO_0030308 (EC: IDA, PMID: 11459809) PMID: 8889548; 11459809; 12374686; 12477932; 14570898; 15489334; 15569677; 16924236; 17192422; 18499678; 18597759; 19578798; 19851296; 20198315; 20307321; 21737788; 21906983; 22912861 oxidative stress induced growth inhibitor 1 Ensembl:ENSG00000140961 HGNC:30093 HPRD:06412 MIM:607975 Vega:OTTHUMG00000137640 Other designations: bone marrow stromal cell-derived growth inhibitor|ovary, kidney and liver protein 38|oxidative stress-induced growth inhibitor 1|pregnancy-induced growth inhibitor OKL38 OSGIN1 OGG:3000049855 Bin Zhao, Yue Liu, Oliver He ZNF291 Zfp291 WEB: http://www.ncbi.nlm.nih.gov/gene SCAPER S-phase cyclin A-associated protein in the ER 49855 MSTP063 15q24 20140408 9606 15 protein-coding Official from a nomenclature committee GO_0005634 (EC: IEA); GO_0005783 (EC: IEA); GO_0046872 (EC: IEA) PMID: 10819331; 12421765; 12477932; 14702039; 15161980; 15840729; 17553665; 17698606; 18245951; 19596686; 21139048; 22505724; 24163370 S-phase cyclin A-associated protein in the ER Ensembl:ENSG00000140386 HGNC:13081 HPRD:11704 MIM:611611 Vega:OTTHUMG00000172655 Other designations: S phase cyclin A-associated protein in the ER|S phase cyclin A-associated protein in the endoplasmic reticulum|zinc finger protein 291 SCAPER OGG:3000050810 Bin Zhao, Yue Liu, Oliver He HDGF-2 HDGF2 HRP-3 WEB: http://www.ncbi.nlm.nih.gov/gene 50810 CGI-142 15q25.2 9606 15 NCBI-supplied GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IEA); GO_0008083 (EC: IEA); GO_0008283 (EC: NAS, PMID: 10581169) PMID: 10581169; 10810093; 12477932; 14702039; 15371438; 15489334; 15761153; 16337983; 18029348; 19237540; 21044950; 21706016; 21890473; 23000965; 23503679; 24012673 hepatoma-derived growth factor, related protein 3 Ensembl:ENSG00000166503 HPRD:17096 Vega:OTTHUMG00000172685 Other designations: hepatoma-derived growth factor 2|hepatoma-derived growth factor-related protein 3 HDGFRP3 OGG:3000051129 Bin Zhao, Yue Liu, Oliver He ANGPTL2 ARP4 FIAF HARP HFARP NL2 PGAR UNQ171 pp1158 WEB: http://www.ncbi.nlm.nih.gov/gene ANGPTL4 angiopoietin-like 4 51129 PP1158 19p13.3 9606 19 GO_0001525 (EC: IEA); GO_0001666 (EC: NAS, PMID:12707035); GO_0004857 (EC: ISS); GO_0005515 (EC: IPI); GO_0005576 (EC: IDA, PMID:10698685); GO_0005576 (EC: TAS); GO_0005578 (EC: IEA); GO_0005615 (EC: IDA, PMID:10698685); GO_0030154 (EC: IEA); GO_0043066 (EC: IDA, PMID:10698685); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0045766 (EC: TAS, PMID:11953136); GO_0051005 (EC: IDA, PMID:19542565); GO_0051260 (EC: IEA); GO_0070328 (EC: ISS); GO_0072562 (EC: IDA); GO_2000352 (EC: IEA) PMID:8125298; 10698685; 10866690; 11953136; 12015030; 12438262; 12477932; 12707035; 12975309; 14570927; 14583458; 15190076; 15284220; 15292369; 15489334; 15579652; 15837923; 15863837; 15870027; 16049480; 16081640; 16272564; 16303743; 16531751; 17049073; 17068295; 17088546; 17130448; 17207965; 17322881; 18029348; 18340008; 18394990; 18433990; 18442626; 18599063; 18634015; 18728224; 18809343; 18940399; 18974381; 19019854; 19028676; 19060906; 19074989; 19246456; 19270337; 19318355; 19342599; 19542565; 19628874; 19775228; 19826106; 19878569; 19890028; 19913121; 20025870; 20162021; 20454689; 20595396; 20628086; 20660728; 20664963; 20667978; 20686565; 20729546; 20829508; 20927337; 20972945; 21109191; 21151138; 21212665; 21217681; 21308352; 21397862; 21398697; 21421336; 21489049; 21518214; 21596930; 21674552; 21709421; 21714923; 21841165; 21860410; 21937683; 21966511; 22078753; 22086875; 22307217; 22458843; 22462789; 22549372; 22573825; 22639947; 22661548; 22729570; 22732211; 22773878; 22791755; 22820186; 22972030; 23056264; 23183503; 23208498; 23283507; 23319744; 23339868; 23387337; 23518684; 23617883; 23640487; 23959876; 23960078; 24317117 angiopoietin-like 4 Ensembl:ENSG00000167772 HGNC:16039 HPRD:16173 MIM:605910 Vega:OTTHUMG00000182273 Other designations: PPARG angiopoietin related protein|angiopoietin-related protein 4|fasting-induced adipose factor|hepatic angiopoietin-related protein|hepatic fibrinogen/angiopoietin-related protein|peroxisome proliferator-activated receptor (PPAR) gamma induced angiopoietin-related protein ANGPTL4 OGG:3000051141 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene INSIG2 insulin induced gene 2 51141 2q14.2 9606 2 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 12242332); GO_0005789 (EC: TAS); GO_0006641 (EC: IEA); GO_0006695 (EC: IEA); GO_0008134 (EC: IEA); GO_0010894 (EC: IEA); GO_0032868 (EC: IEA); GO_0032933 (EC: IDA, PMID: 12242332); GO_0032937 (EC: IDA, PMID: 12242332); GO_0042472 (EC: IEA); GO_0042474 (EC: IEA); GO_0044281 (EC: TAS); GO_0045717 (EC: IEA); GO_0060021 (EC: IEA); GO_0060363 (EC: IEA); GO_0070542 (EC: IEA) PMID: 12242332; 12477932; 12482938; 12624180; 12842885; 14702039; 16549805; 16606821; 16614226; 17137505; 17428920; 17465681; 17471297; 17489846; 18003761; 18070740; 18162505; 18195716; 18223638; 18239574; 18270535; 18319320; 18347269; 18398047; 18426866; 18464289; 18514965; 18570692; 18615239; 18660489; 18682847; 18839134; 18989534; 19105843; 19197259; 19197262; 19224890; 19263810; 19360016; 19399648; 19523229; 19617589; 19638338; 19740467; 19772594; 19815544; 19851442; 19913121; 19948975; 20007308; 20028541; 20045156; 20083228; 20092643; 20145255; 20373477; 20504252; 20538960; 20628086; 20645959; 20653998; 20712903; 20816152; 20816195; 20858904; 20877301; 20920244; 20955599; 21163096; 21443541; 21544599; 21978759; 22020349; 22143767; 22355322; 22504420; 22695173; 22968099; 24250222; 24371122 insulin induced gene 2 Other designations: INSIG-2|INSIG2 membrane protein|insulin induced protein 2|insulin-induced gene 2 protein INSIG2 OGG:3000051147 Bin Zhao, Yue Liu, Oliver He my036 p29ING4 WEB: http://www.ncbi.nlm.nih.gov/gene ING4 inhibitor of growth family, member 4 51147 My036 12p13.31 9606 12 Official from a nomenclature committee GO_0000123 (EC: IDA, PMID: 16387653); GO_0003713 (EC: IDA, PMID: 16387653); GO_0005515 (EC: IPI, PMID: 12750254); GO_0005634 (EC: IDA, PMID: 15029197); GO_0005654 (EC: TAS); GO_0006260 (EC: IDA, PMID: 16387653); GO_0006325 (EC: TAS); GO_0006473 (EC: IDA, PMID: 12750254); GO_0006915 (EC: IDA, PMID: 15251430); GO_0006978 (EC: IDA, PMID: 16387653); GO_0007050 (EC: IDA, PMID: 15251430); GO_0008270 (EC: IEA); GO_0008285 (EC: IDA, PMID: 12750254); GO_0035064 (EC: IDA, PMID: 16728974); GO_0043065 (EC: IDA, PMID: 16387653); GO_0043966 (EC: IDA, PMID: 16387653); GO_0043981 (EC: IDA, PMID: 16387653); GO_0043982 (EC: IDA, PMID: 16387653); GO_0043983 (EC: IDA, PMID: 16387653); GO_0043984 (EC: IDA, Qualifier: NOT, PMID: 16387653); GO_0045892 (EC: IDA, PMID: 15029197); GO_0045926 (EC: IDA, PMID: 12750254) PMID: 8889548; 10931946; 12477932; 12750254; 15029197; 15251430; 15342556; 15489334; 15528276; 15882981; 15897452; 15935570; 16096374; 16387653; 16728974; 16916647; 16920330; 16973615; 17157298; 17325660; 17363573; 17517644; 17848618; 17954561; 18381289; 18394746; 18399550; 18775696; 18779315; 18789575; 19034511; 19250543; 19430401; 19571607; 19775294; 20053357; 20211142; 20381459; 20445261; 20501848; 20705953; 20707719; 20716169; 20953165; 21056991; 21177815; 21310648; 21315418; 21454715; 21626442; 21890473; 21971889; 21988832; 22078444; 22144582; 22228137; 22334692; 22436625; 22767438; 23055189; 23056468; 23181555; 23455924; 23603392; 23624912; 24130172; 24157826 inhibitor of growth family, member 4 Ensembl:ENSG00000111653 HGNC:19423 HPRD:09774 MIM:608524 Vega:OTTHUMG00000141274 Other designations: brain my036 protein|candidate tumor suppressor p33 ING1 homolog|inhibitor of growth protein 4 ING4 OGG:3000051250 Bin Zhao, Yue Liu, Oliver He PRED31 WEB: http://www.ncbi.nlm.nih.gov/gene C6orf203 chromosome 6 open reading frame 203 51250 HSPC230 6q21 9606 6 Official from a nomenclature committee GO_0005739 (EC: IDA) PMID: 11042152; 11707072; 12107413; 12477932; 14574404; 14702039; 15489334; 16169070; 16344560; 20186120; 20877624; 21832049; 21988832; 24250222 chromosome 6 open reading frame 203 Ensembl:ENSG00000130349 HGNC:17971 HPRD:12873 Vega:OTTHUMG00000015307 Other designations: uncharacterized protein C6orf203 C6orf203 OGG:3000051277 Bin Zhao, Yue Liu, Oliver He RBJ RabJS WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC27 DnaJ (Hsp40) homolog, subfamily C, member 27 51277 2p23.3 9606 2 GO_0005525 (EC: IEA); GO_0005739 (EC: IEA); GO_0007264 (EC: IEA) PMID:9564038; 12477932; 14980719; 18391951; 20877624; 20881960; 20935630; 21980299; 22344219; 23449627 DnaJ (Hsp40) homolog, subfamily C, member 27 Ensembl:ENSG00000115137 HGNC:30290 HPRD:15221 MIM:613527 Vega:OTTHUMG00000125524 Other designations: Ras-associated protein Rap1|dnaJ homolog subfamily C member 27|rab and DnaJ domain-containing protein DNAJC27 OGG:3000051302 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CYP39A1 cytochrome P450, family 39, subfamily A, polypeptide 1 51302 6p21.1-p11.2 9606 6 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006699 (EC: IDA, PMID:10748047); GO_0006699 (EC: TAS); GO_0006707 (EC: IEA); GO_0006805 (EC: TAS); GO_0007586 (EC: TAS, PMID:10748047); GO_0008206 (EC: TAS); GO_0008387 (EC: IEA); GO_0008396 (EC: IDA, PMID:10748047); GO_0016125 (EC: TAS); GO_0020037 (EC: IEA); GO_0030573 (EC: IEA); GO_0033782 (EC: IEA); GO_0043231 (EC: TAS, PMID:10748047); GO_0044281 (EC: TAS) PMID:10748047; 11329013; 12477932; 15128046; 15489334; 19553612; 20453000; 21988832 cytochrome P450, family 39, subfamily A, polypeptide 1 Other designations: 24-hydroxycholesterol 7-alpha-hydroxylase|cytochrome P450, subfamily XXXIX (oxysterol 7 alpha-hydroxylase), polypeptide 1 CYP39A1 OGG:3000051311 Bin Zhao, Yue Liu, Oliver He CD288 WEB: http://www.ncbi.nlm.nih.gov/gene TLR8 toll-like receptor 8 51311 UNQ249/PRO286 Xp22 20140408 9606 X protein-coding Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0002224 (EC: TAS); GO_0002282 (EC: IEA); GO_0003677 (EC: IDA, PMID: 16123302); GO_0003723 (EC: TAS, PMID: 16123302); GO_0003725 (EC: IDA, PMID: 16111635); GO_0003727 (EC: IDA, PMID: 14976262); GO_0004872 (EC: NAS, PMID: 12032557); GO_0005789 (EC: TAS); GO_0006954 (EC: IEA); GO_0007249 (EC: IDA, PMID: 12032557); GO_0008144 (EC: IEA); GO_0009615 (EC: IDA, PMID: 12032557); GO_0010008 (EC: TAS); GO_0016021 (EC: IC, PMID: 12032557); GO_0016064 (EC: TAS, PMID: 16123302); GO_0034162 (EC: TAS); GO_0036020 (EC: TAS); GO_0045078 (EC: IDA, PMID: 16286015); GO_0045087 (EC: NAS, PMID: 12032557); GO_0045087 (EC: TAS); GO_0045089 (EC: IDA, PMID: 16123302); GO_0045356 (EC: IDA, PMID: 16286015); GO_0045359 (EC: IDA, PMID: 16286015); GO_0045416 (EC: IMP, PMID: 16188996); GO_0051607 (EC: IMP, PMID: 16188996); GO_0052033 (EC: IEA); GO_0071260 (EC: IEP, PMID: 19593445) PMID: 9435236; 11022119; 11022120; 11607792; 11782555; 11909637; 12032557; 12477932; 12724322; 12975309; 14625308; 14976262; 15276183; 15489334; 16008579; 16024789; 16025564; 16111635; 16123302; 16188996; 16286015; 16303743; 16482509; 16737960; 16857668; 16935934; 17023556; 17040905; 17090647; 17301562; 17698957; 17703412; 17724596; 17868034; 17932028; 17964520; 18394314; 18406377; 18431484; 18438411; 18605904; 18682521; 18686608; 18810425; 18818748; 18927625; 18942751; 18985439; 18985539; 19017992; 19019335; 19028959; 19164127; 19164128; 19258923; 19265114; 19381167; 19406482; 19437550; 19454678; 19505919; 19527497; 19527514; 19593445; 19614650; 19637197; 19841637; 19850743; 19913121; 19915052; 19924287; 20004021; 20100933; 20124101; 20190752; 20194452; 20227302; 20237413; 20237496; 20364151; 20399690; 20412752; 20503287; 20588308; 20595247; 20628086; 20652908; 20674764; 20829351; 20832340; 20946625; 20977567; 21061265; 21092001; 21321205; 21354862; 21499082; 21677671; 21734241; 21947541; 21977996; 22022576; 22065095; 22164301; 22196370; 22210629; 22243920; 22289837; 22340042; 22363482; 22393042; 22525943; 22730373; 22768144; 22795647; 22857391; 23221735; 23223421; 23369718; 23386618; 23425350; 23520111; 23685782; 23787171; 23906644; 24046015; 24227841; 24254490 toll-like receptor 8 Ensembl:ENSG00000101916 HGNC:15632 HPRD:02296 MIM:300366 Vega:OTTHUMG00000021145 TLR8 OGG:3000051330 Bin Zhao, Yue Liu, Oliver He CD266 FN14 TWEAKR WEB: http://www.ncbi.nlm.nih.gov/gene TNFRSF12A tumor necrosis factor receptor superfamily, member 12A 51330 16p13.3 9606 16 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0001726 (EC: IEA); GO_0005515 (EC: IPI); GO_0005886 (EC: IEA); GO_0006915 (EC: IEA); GO_0006928 (EC: TAS, PMID: 10551889); GO_0006931 (EC: IEA); GO_0007275 (EC: TAS, PMID: 10551889); GO_0009986 (EC: IEA); GO_0016021 (EC: IEA); GO_0043065 (EC: IDA); GO_0045773 (EC: IEA); GO_2001238 (EC: IMP) PMID: 10551889; 10751351; 11728344; 12445828; 12477932; 12496418; 12529173; 12651623; 14573547; 15140220; 15353286; 15489334; 15611130; 16341674; 16503147; 16526941; 16809572; 17018610; 17124496; 17383968; 17594693; 18505918; 19018248; 19241374; 19349318; 19573080; 19773279; 19828625; 19895311; 19963275; 20004376; 20189297; 20237496; 20487651; 20557950; 20568250; 20610643; 20628624; 20810696; 20844036; 20927042; 21153335; 21303425; 21435232; 21483105; 21525013; 21708117; 21828059; 21963094; 21982860; 21993017; 22055894; 22081603; 22521346; 22634180; 22637703; 22672874; 22767506; 22896023; 23107828; 23288170; 23300011; 23320797; 23438059; 23443741; 23469193; 23722548; 23775076; 23886137; 23999007; 24056367; 24122208 tumor necrosis factor receptor superfamily, member 12A Ensembl:ENSG00000006327 HGNC:18152 HPRD:05801 MIM:605914 Vega:OTTHUMG00000129001 Other designations: FGF-inducible 14|fibroblast growth factor-inducible immediate-early response protein 14|tumor necrosis factor receptor superfamily member 12A|tweak-receptor|type I transmembrane protein Fn14 TNFRSF12A OGG:3000051378 Bin Zhao, Yue Liu, Oliver He AGP4 ANG-3 ANG4 WEB: http://www.ncbi.nlm.nih.gov/gene ANGPT4 angiopoietin 4 51378 20p13 9606 20 GO_0001525 (EC: IEA); GO_0001935 (EC: IDA, Qualifier: NOT, PMID:10025962); GO_0005576 (EC: TAS); GO_0005615 (EC: IDA, PMID:10025962); GO_0007171 (EC: IDA, PMID:10051567); GO_0007596 (EC: TAS); GO_0010595 (EC: IDA, PMID:12958144); GO_0016525 (EC: IDA, PMID:16790085); GO_0030297 (EC: IDA, PMID:10051567); GO_0030971 (EC: IDA, PMID:10051567); GO_0043066 (EC: IDA, PMID:12958144); GO_0043536 (EC: IDA, PMID:15284220); GO_0043537 (EC: IDA, PMID:16790085); GO_0045766 (EC: IDA, PMID:15284220); GO_0050731 (EC: IDA, PMID:15851516); GO_0050900 (EC: TAS); GO_0071456 (EC: IEP, PMID:12958144) PMID:10025962; 10051567; 10218486; 10343124; 11076863; 11780052; 11856872; 12477932; 12624729; 12958144; 15198927; 15284220; 15489334; 15542434; 15851516; 16790085; 17724803; 19204726; 19913121; 20596041; 20628086; 20819778; 20823154; 21603628; 22267746 angiopoietin 4 Ensembl:ENSG00000101280 HGNC:487 HPRD:04747 MIM:603705 Vega:OTTHUMG00000031652 Other designations: ANG-4|angiopoietin-3|angiopoietin-4|dJ824F16.2 (angiopoietin 4) ANGPT4 OGG:3000051386 Bin Zhao, Yue Liu, Oliver He EIF3EIP EIF3S11 EIF3S6IP HSPC021 HSPC025 MSTP005 WEB: http://www.ncbi.nlm.nih.gov/gene EIF3L eukaryotic translation initiation factor 3, subunit L 51386 AL022311.1 22q 9606 22 GO_0001650 (EC: IEA); GO_0001731 (EC: IEA); GO_0003743 (EC: IC, Qualifier: contributes_to, PMID:17322308); GO_0003743 (EC: IDA, Qualifier: contributes_to, PMID:17581632); GO_0005515 (EC: IPI, PMID:18599441); GO_0005654 (EC: IEA); GO_0005852 (EC: IDA, PMID:17322308); GO_0006413 (EC: IC, PMID:17322308); GO_0006413 (EC: IDA, PMID:17581632); GO_0006446 (EC: IEA); GO_0016282 (EC: IEA); GO_0033290 (EC: IEA); GO_0044822 (EC: IDA) PMID:8125298; 11042152; 11590142; 11592397; 12393749; 12477932; 14702039; 15231747; 15231748; 15461802; 15489334; 16169070; 16189514; 16344560; 16522924; 17322308; 17353931; 17403899; 17581632; 18029348; 18599441; 18781797; 19167051; 19615732; 19738201; 20360068; 20508642; 21081666; 21139048; 21145461; 21890473; 21900206; 21906983; 21963094; 21987572; 22190034; 22505724; 22586326; 22623428; 22863883; 22939629; 23455922; 23463506; 23800076; 24250222; 24457600 eukaryotic translation initiation factor 3, subunit L Ensembl:ENSG00000100129 HGNC:18138 HPRD:10932 Vega:OTTHUMG00000150671 Other designations: eIEF associated protein HSPC021|eukaryotic translation initiation factor 3 subunit 6-interacting protein|eukaryotic translation initiation factor 3 subunit E-interacting protein|eukaryotic translation initiation factor 3 subunit L EIF3L OGG:3000051390 Bin Zhao, Yue Liu, Oliver He AIG-1 dJ95L4.1 WEB: http://www.ncbi.nlm.nih.gov/gene AIG1 androgen-induced 1 51390 RP1-95L4.1 6q24.2 9606 6 Official from a nomenclature committee GO_0005515 (EC: IPI); GO_0016021 (EC: IEA) PMID: 8125298; 8889548; 10810093; 11266118; 11329013; 12477932; 14574404; 14702039; 15489334; 16344560; 20379614; 21622095; 21988832 androgen-induced 1 Ensembl:ENSG00000146416 HGNC:21607 HPRD:16346 MIM:608514 Vega:OTTHUMG00000015721 Other designations: androgen-induced gene 1 protein AIG1 OGG:3000051477 Bin Zhao, Yue Liu, Oliver He INO1 INOS IPS IPS 1 IPS-1 WEB: http://www.ncbi.nlm.nih.gov/gene ISYNA1 inositol-3-phosphate synthase 1 51477 19p13.11 9606 19 Official from a nomenclature committee GO_0004512 (EC: TAS); GO_0005829 (EC: TAS); GO_0006021 (EC: IEA); GO_0008654 (EC: IEA); GO_0043647 (EC: TAS); GO_0044281 (EC: TAS) PMID: 12477932; 12941308; 14702039; 15024000; 15464731; 16169070; 16344560; 21044950; 21139048; 21890473; 21906983; 21988832; 22707096; 23535729; 23902760 inositol-3-phosphate synthase 1 Ensembl:ENSG00000105655 HGNC:29821 HPRD:17163 MIM:611670 Vega:OTTHUMG00000179027 Other designations: MI-1-P synthase|MIP synthase|myo-inositol 1-phosphate synthase A1 ISYNA1 OGG:3000051512 Bin Zhao, Yue Liu, Oliver He B99 WEB: http://www.ncbi.nlm.nih.gov/gene GTSE1 G-2 and S-phase expressed 1 51512 RP5-1163J1.2 22q13.2-q13.3 9606 22 Official from a nomenclature committee GO_0000085 (EC: NAS, PMID: 10974554); GO_0003674 (EC: ND); GO_0005515 (EC: IPI); GO_0005881 (EC: NAS, PMID: 10974554); GO_0006977 (EC: NAS, PMID: 10974554); GO_0007017 (EC: NAS, PMID: 10974554) PMID: 8125298; 8889548; 10591208; 10974554; 10984615; 12477932; 12750368; 14702039; 14707141; 15146197; 15231747; 15302935; 15461802; 15489334; 15790807; 15998911; 16344560; 16964243; 19531213; 19615732; 19913121; 20018861; 20577264; 20628086; 20800603; 21139048; 21693764; 21890473; 22292647; 22990118; 23236459; 24250222 G-2 and S-phase expressed 1 Ensembl:ENSG00000075218 HGNC:13698 HPRD:09593 MIM:607477 Vega:OTTHUMG00000150486 Other designations: G2 and S phase-expressed protein 1|protein B99 homolog GTSE1 OGG:3000051594 Bin Zhao, Yue Liu, Oliver He NAG SOPH WEB: http://www.ncbi.nlm.nih.gov/gene NBAS neuroblastoma amplified sequence 51594 2p24 9606 2 Official from a nomenclature committee GO_0000956 (EC: IMP); GO_0005737 (EC: IEA); GO_2000623 (EC: IMP) PMID: 9926938; 11329013; 11954550; 12477932; 12706883; 14702039; 16169070; 17028906; 19369418; 19407829; 20360068; 20379614; 20577004; 20585324; 21139048; 21697133; 21906983; 21963094; 23828042 neuroblastoma amplified sequence Ensembl:ENSG00000151779 HGNC:15625 HPRD:10473 MIM:608025 Vega:OTTHUMG00000121153 Other designations: NAG/BC035112 fusion|NAG/FAM49A fusion|neuroblastoma-amplified gene protein|neuroblastoma-amplified sequence NBAS OGG:3000051726 Bin Zhao, Yue Liu, Oliver He ABBP-2 ABBP2 DJ9 Dj-9 EDJ ERdj3 ERj3 ERj3p PRO1080 UNQ537 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB11 DnaJ (Hsp40) homolog, subfamily B, member 11 51726 PSEC0121 3q27.3 9606 3 GO_0005515 (EC: IPI, PMID:18923428); GO_0005634 (EC: IEA); GO_0005783 (EC: IDA); GO_0005783 (EC: TAS, PMID:16130169); GO_0005788 (EC: TAS); GO_0006457 (EC: IEA); GO_0006987 (EC: TAS); GO_0016556 (EC: IEA); GO_0030968 (EC: TAS); GO_0044267 (EC: TAS); GO_0051082 (EC: IEA) PMID:10827079; 11147971; 11584023; 12475965; 12477932; 12975309; 14702039; 15195998; 15489334; 15525676; 15544163; 16130169; 16169070; 16236267; 16303743; 17353931; 17976514; 18029348; 18303054; 18624398; 18923428; 19167051; 19322201; 19748898; 19913121; 20335166; 20418907; 20628086; 20811636; 21081666; 21139048; 21145461; 21150319; 21182205; 21673190; 21844235; 21890473; 21900206; 21906983; 21963094; 22190034; 22268729; 22678362; 22863883; 22939629; 22990118; 23097496; 23349634; 23378021; 23455922; 23752268; 23798571 DnaJ (Hsp40) homolog, subfamily B, member 11 Ensembl:ENSG00000090520 HGNC:14889 HPRD:07485 MIM:611341 Other designations: APOBEC1-binding protein 2|DnaJ protein 9|ER-associated DNAJ protein 3|ER-associated Hsp40 co-chaperone|ER-resident protein ERdj3|PWP1-interacting protein 4|dnaJ homolog subfamily B member 11|endoplasmic reticulum DNA J domain-containing protein 3 DNAJB11 OGG:3000053354 Bin Zhao, Yue Liu, Oliver He PANK WEB: http://www.ncbi.nlm.nih.gov/gene PANK1 pantothenate kinase 1 53354 10q23.31 9606 10 Official from a nomenclature committee GO_0004594 (EC: IEA); GO_0005524 (EC: IEA); GO_0005634 (EC: IEA); GO_0005829 (EC: TAS); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0009108 (EC: TAS); GO_0015937 (EC: IEA); GO_0015939 (EC: TAS); GO_0030118 (EC: IEA); GO_0044281 (EC: TAS); GO_0055037 (EC: IEA); GO_0071944 (EC: IEA) PMID: 2981478; 11479594; 11809413; 12379284; 12477932; 14523052; 15161933; 15164054; 15489334; 16385451; 17631502; 18029348; 18187620; 19060910; 19322201; 20379614; 20833636; 22912811; 23343762 pantothenate kinase 1 Ensembl:ENSG00000152782 HGNC:8598 HPRD:07549 MIM:606160 Other designations: pantothenic acid kinase 1 PANK1 OGG:3000054106 Bin Zhao, Yue Liu, Oliver He CD289 WEB: http://www.ncbi.nlm.nih.gov/gene TLR9 toll-like receptor 9 54106 UNQ5798/PRO19605 3p21.3 20140408 9606 3 protein-coding Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0002224 (EC: TAS); GO_0002237 (EC: TAS, PMID: 15356140); GO_0002755 (EC: IEA); GO_0004888 (EC: IEA); GO_0005149 (EC: IPI, PMID: 12925853); GO_0005576 (EC: NAS, PMID: 11130078); GO_0005737 (EC: IDA, PMID: 19740627); GO_0005764 (EC: ISS); GO_0005768 (EC: ISS); GO_0005783 (EC: ISS); GO_0005789 (EC: TAS); GO_0005886 (EC: IDA, PMID: 19740627); GO_0006954 (EC: IEA); GO_0007252 (EC: IDA, PMID: 19740627); GO_0008286 (EC: TAS); GO_0010008 (EC: TAS); GO_0016021 (EC: IEA); GO_0016323 (EC: IDA, PMID: 17128265); GO_0016324 (EC: IDA, PMID: 17128265); GO_0030277 (EC: ISS); GO_0032009 (EC: ISS); GO_0032088 (EC: IDA, PMID: 17128265); GO_0032715 (EC: ISS); GO_0032717 (EC: IDA, PMID: 17128265); GO_0032722 (EC: IDA, PMID: 19740627); GO_0032728 (EC: ISS); GO_0032733 (EC: ISS); GO_0032735 (EC: ISS); GO_0032741 (EC: ISS); GO_0032755 (EC: IDA, PMID: 19740627); GO_0032757 (EC: IDA, PMID: 17128265); GO_0032760 (EC: ISS); GO_0034122 (EC: IDA, PMID: 17128265); GO_0034123 (EC: IDA, PMID: 17128265); GO_0034162 (EC: TAS); GO_0035197 (EC: IMP, PMID: 15723075); GO_0036020 (EC: TAS); GO_0042346 (EC: IDA, PMID: 19740627); GO_0042742 (EC: NAS, PMID: 11130078); GO_0043123 (EC: IDA, PMID: 17128265); GO_0043507 (EC: IDA, PMID: 17128265); GO_0045078 (EC: IDA, PMID: 16286015); GO_0045087 (EC: TAS, PMID: 15356140); GO_0045356 (EC: IDA, PMID: 16286015); GO_0045359 (EC: IDA, PMID: 16286015); GO_0045944 (EC: ISS); GO_0046330 (EC: IC, PMID: 17128265); GO_0050707 (EC: IEA); GO_0050729 (EC: IC, PMID: 19740627); GO_0050829 (EC: IMP); GO_0051092 (EC: IDA, PMID: 17128265); GO_0051770 (EC: ISS) PMID: 9435236; 11022119; 11022120; 11130078; 11561001; 11564765; 11782555; 11867692; 11909637; 11970999; 11976718; 12477932; 12560217; 12573264; 12600829; 12660731; 12689944; 12724322; 12734363; 12778475; 12867418; 12925853; 12941697; 12975309; 14625308; 14694183; 14716310; 14751759; 14987294; 15107846; 15153500; 15207506; 15276183; 15294971; 15307186; 15356140; 15489334; 15585868; 15607737; 15631627; 15723075; 15730519; 15790341; 15860583; 15878652; 16002719; 16024265; 16024789; 16125159; 16164440; 16230478; 16237063; 16286015; 16371473; 16394009; 16424230; 16428738; 16437636; 16575840; 16608528; 16731773; 16779724; 16847112; 16849519; 16864658; 16920494; 16951309; 16971956; 16990271; 17000223; 17040905; 17075805; 17128265; 17142771; 17145922; 17192395; 17229603; 17258734; 17292969; 17295441; 17301562; 17325049; 17328813; 17344245; 17360657; 17373717; 17440926; 17469139; 17473064; 17474147; 17482427; 17516623; 17534115; 17573724; 17636117; 17703412; 17768129; 17854429; 17854755; 17878374; 17893430; 17894360; 17914947; 17932028; 17964520; 17984204; 17986857; 18036648; 18092352; 18160420; 18208876; 18215354; 18253698; 18262306; 18275280; 18312481; 18318750; 18332208; 18394314; 18406377; 18437017; 18524824; 18535206; 18539711; 18568766; 18595521; 18606688; 18633634; 18686608; 18763053; 18769358; 18776126; 18776592; 18806803; 18810425; 18818748; 18832675; 18841790; 18922969; 18946062; 19019335; 19033535; 19034349; 19050243; 19079358; 19096003; 19120473; 19129482; 19130296; 19201477; 19211891; 19247692; 19254290; 19258923; 19264973; 19275920; 19284650; 19289178; 19297619; 19299739; 19317913; 19319670; 19337058; 19362685; 19367581; 19390575; 19401392; 19406482; 19423540; 19459480; 19505919; 19513613; 19527514; 19539691; 19564354; 19578108; 19601804; 19618291; 19620253; 19627277; 19639721; 19714766; 19723394; 19724876; 19740627; 19745833; 19771452; 19789190; 19794067; 19796535; 19809335; 19810822; 19840968; 19844589; 19854217; 19855253; 19903791; 19906293; 19913121; 19914718; 19924287; 19948975; 19953283; 20026892; 20038537; 20041977; 20044998; 20054821; 20085599; 20100933; 20130217; 20132814; 20137629; 20181802; 20194452; 20197609; 20207250; 20227302; 20227772; 20237496; 20307689; 20331378; 20348497; 20363151; 20364327; 20375564; 20375566; 20399690; 20406964; 20422193; 20438785; 20442853; 20452482; 20497632; 20500814; 20503287; 20514021; 20559388; 20588308; 20592251; 20595247; 20604744; 20622911; 20628086; 20635795; 20646321; 20646633; 20659127; 20667457; 20673868; 20674764; 20696081; 20713890; 20797905; 20811701; 20819670; 20821041; 20843333; 20843814; 20935225; 20977567; 20978888; 20980519; 21048031; 21048937; 21050493; 21057083; 21059889; 21068441; 21086718; 21115235; 21129170; 21132533; 21155002; 21176371; 21191071; 21220755; 21223799; 21250838; 21258099; 21273385; 21287547; 21317915; 21324137; 21328884; 21391743; 21398612; 21425908; 21448350; 21457584; 21462132; 21483736; 21490291; 21499878; 21515789; 21527067; 21575365; 21595536; 21604257; 21607583; 21633947; 21682079; 21689850; 21703981; 21720175; 21734566; 21741080; 21748790; 21778270; 21778277; 21833528; 21843566; 21844166; 21850017; 21866115; 21876325; 21903422; 21908428; 21908957; 21911421; 21926972; 21929816; 21940676; 21968308; 21968713; 21977996; 21978158; 21990957; 22001237; 22014045; 22041559; 22046272; 22055432; 22057691; 22059466; 22065095; 22067623; 22070100; 22132241; 22169598; 22170068; 22174451; 22178715; 22196370; 22207622; 22211722; 22221660; 22228476; 22251233; 22269973; 22288832; 22344539; 22423970; 22488361; 22552867; 22554506; 22577991; 22594374; 22594608; 22613717; 22653776; 22662111; 22671429; 22672741; 22684144; 22691414; 22695187; 22701693; 22714906; 22768144; 22822061; 22836641; 22847512; 22853846; 22893852; 22898741; 22908309; 22931661; 22932083; 22948021; 22948541; 22952899; 22964787; 23009111; 23021866; 23043436; 23045477; 23071157; 23091345; 23103284; 23123793; 23133627; 23135998; 23179584; 23182970; 23183093; 23219390; 23221735; 23237868; 23266611; 23276930; 23289794; 23296704; 23369718; 23383065; 23406596; 23407387; 23425749; 23467704; 23472199; 23490285; 23497207; 23564191; 23593431; 23617757; 23651260; 23673637; 23677790; 23724117; 23752229; 23766695; 23776537; 23816930; 23827939; 23855294; 23893288; 23913633; 23957925; 23962979; 23967355; 23974872; 24004541; 24067965; 24080302; 24168509; 24269682 toll-like receptor 9 Ensembl:ENSG00000239732 HGNC:15633 HPRD:05685 MIM:605474 Vega:OTTHUMG00000158106 TLR9 OGG:3000054431 Bin Zhao, Yue Liu, Oliver He ERdj5 JPDI MTHr PDIA19 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC10 DnaJ (Hsp40) homolog, subfamily C, member 10 54431 UNQ495/PRO1012 2q32.1 9606 2 GO_0001671 (EC: ISS); GO_0001933 (EC: IDA, PMID:19122239); GO_0005515 (EC: IPI, PMID:19706418); GO_0005783 (EC: IDA, PMID:12411443); GO_0005788 (EC: IDA); GO_0006662 (EC: IEA); GO_0015035 (EC: IDA); GO_0015035 (EC: ISS); GO_0015036 (EC: ISS); GO_0016671 (EC: ISS); GO_0030433 (EC: IMP, PMID:18400946); GO_0030544 (EC: IPI); GO_0032781 (EC: ISS); GO_0034663 (EC: IDA, PMID:18400946); GO_0034975 (EC: IDA); GO_0034976 (EC: IDA, PMID:19122239); GO_0045454 (EC: IEA); GO_0051087 (EC: IDA, PMID:12411443); GO_0051117 (EC: IPI, PMID:12411443); GO_0051787 (EC: IDA, PMID:18400946); GO_0070059 (EC: IDA, PMID:19122239) PMID:12411443; 12446677; 12477932; 12975309; 14587667; 14702039; 15489334; 15815621; 16189514; 16303743; 16344560; 17353921; 18400946; 18653895; 19122239; 19706418; 19815549; 20347046; 21139048; 21145461; 21266254; 21329881; 21632540; 21890473; 21906983; 22229892; 22354994; 22797925; 23192594; 23363602; 23455922; 23769672 DnaJ (Hsp40) homolog, subfamily C, member 10 HGNC:24637 HPRD:09722 MIM:607987 Other designations: ER-resident protein ERdj5|J-domain-containing protein disulfide isomerase-like protein|dnaJ homolog subfamily C member 10|endoplasmic reticulum DNA J domain-containing protein 5|macrothioredoxin|protein disulfide isomerase family A, member 19 DNAJC10 OGG:3000054541 Bin Zhao, Yue Liu, Oliver He Dig2 REDD-1 REDD1 WEB: http://www.ncbi.nlm.nih.gov/gene DDIT4 DNA-damage-inducible transcript 4 54541 RP11-442H21.1 10q22.1 9606 10 Official from a nomenclature committee GO_0001666 (EC: IDA); GO_0001764 (EC: ISS); GO_0005622 (EC: IDA); GO_0005737 (EC: IDA, PMID: 12453409); GO_0005739 (EC: IEA); GO_0005829 (EC: IEA); GO_0007420 (EC: ISS); GO_0008283 (EC: ISS); GO_0010801 (EC: ISS); GO_0030182 (EC: ISS); GO_0032007 (EC: IMP); GO_0033137 (EC: ISS); GO_0042771 (EC: ISS); GO_0043241 (EC: IEA); GO_0045820 (EC: IEA); GO_0048011 (EC: ISS); GO_0051607 (EC: IEA); GO_0071889 (EC: IEA); GO_0072593 (EC: IEA); GO_1901216 (EC: ISS); GO_1902532 (EC: ISS) PMID: 11076863; 11230166; 11256614; 11884613; 12453409; 12477932; 14646594; 15146197; 15180327; 15489336; 15592522; 15632201; 15988001; 16169070; 16196087; 16258273; 16341674; 16381901; 16713569; 17005863; 17307335; 18029348; 18781797; 18796435; 18953439; 19114033; 19127203; 19210572; 19221489; 19557001; 19996311; 20166753; 20354178; 20374513; 20473305; 20639865; 20972266; 21123297; 21139048; 21258409; 21266827; 21414293; 21460850; 21540236; 21798997; 21890473; 21900206; 21906983; 21909097; 21963094; 21987572; 22053931; 22505724; 23000965; 23193052; 23528835 DNA-damage-inducible transcript 4 Ensembl:ENSG00000168209 HGNC:24944 HPRD:09662 MIM:607729 Vega:OTTHUMG00000183961 Other designations: DNA damage-inducible transcript 4 protein|HIF-1 responsive protein RTP801|protein regulated in development and DNA damage response 1 DDIT4 OGG:3000054658 Bin Zhao, Yue Liu, Oliver He BILIQTL1 GNT1 HUG-BR1 UDPGT UDPGT 1-1 UGT1 UGT1A WEB: http://www.ncbi.nlm.nih.gov/gene UGT1A1 UDP glucuronosyltransferase 1 family, polypeptide A1 54658 2q37 9606 2 Official from a nomenclature committee GO_0001889 (EC: IEA); GO_0001972 (EC: IDA); GO_0004857 (EC: IDA, PMID: 19996319); GO_0005496 (EC: IDA, PMID: 19996319); GO_0005789 (EC: TAS); GO_0005887 (EC: IEA); GO_0006778 (EC: TAS); GO_0006789 (EC: TAS, PMID: 1339448); GO_0006805 (EC: TAS); GO_0006953 (EC: IEA); GO_0007584 (EC: IEA); GO_0007586 (EC: NAS, PMID: 1898728); GO_0008202 (EC: IC, PMID: 19996319); GO_0008210 (EC: TAS, PMID: 8780690); GO_0015020 (EC: IDA, PMID: 18052087); GO_0015020 (EC: TAS); GO_0017144 (EC: IC, PMID: 19996319); GO_0019899 (EC: IDA); GO_0031100 (EC: IEA); GO_0032496 (EC: IEA); GO_0042167 (EC: TAS); GO_0042493 (EC: IEA); GO_0042573 (EC: IC); GO_0042594 (EC: IEA); GO_0042803 (EC: IPI); GO_0043086 (EC: IDA, PMID: 19996319); GO_0044281 (EC: TAS); GO_0045939 (EC: IC, PMID: 19996319); GO_0046483 (EC: IC, PMID: 19996319); GO_0046982 (EC: IPI); GO_0051552 (EC: IDA, PMID: 18052087); GO_0052695 (EC: TAS); GO_0052696 (EC: IDA); GO_0052697 (EC: IDA); GO_0070069 (EC: IEA); GO_0070980 (EC: IEA); GO_0071361 (EC: IEA); GO_0071385 (EC: IEA); GO_2001030 (EC: IDA, PMID: 18004212) PMID: 1339448; 1634050; 1634606; 1898728; 2108603; 3082969; 3141926; 7565971; 7715297; 7906695; 7936809; 7989045; 7989595; 8027054; 8226884; 8276413; 8280139; 8467709; 8514037; 8528206; 8706880; 8780690; 9039987; 9295054; 9375768; 9472029; 9497253; 9535849; 9621515; 9627603; 9639672; 10412811; 10498597; 10706110; 10748067; 10836148; 10946897; 11013440; 11061796; 11141380; 11156391; 11179460; 11370628; 11401924; 11434514; 11465080; 11764096; 11827650; 11855932; 11857560; 11878580; 11906189; 11915038; 11968090; 11987245; 12036456; 12078936; 12105841; 12139570; 12151360; 12185559; 12357057; 12402338; 12439228; 12477932; 12480553; 12480568; 12499798; 12502904; 12566446; 12602902; 12646172; 12677174; 12680285; 12695355; 12732365; 12732844; 12743455; 12800608; 12850481; 12850492; 12909459; 12925779; 12960109; 12969965; 12972027; 14550264; 14555305; 14586211; 14616765; 14647407; 14672974; 14871858; 15007088; 15049432; 15111762; 15179405; 15180166; 15247627; 15254716; 15280927; 15286088; 15297419; 15304120; 15318931; 15319294; 15319464; 15320866; 15388579; 15455371; 15472229; 15491385; 15519273; 15523087; 15557560; 15560369; 15572581; 15586176; 15684703; 15709212; 15710570; 15712364; 15746053; 15771689; 15815621; 15855726; 15857854; 15864124; 15864125; 15864130; 15867280; 15929176; 15931768; 16004608; 16135700; 16171463; 16210851; 16237771; 16255851; 16257834; 16257926; 16280036; 16399345; 16424820; 16456808; 16469709; 16513443; 16557566; 16609363; 16610035; 16636344; 16637266; 16712705; 16735790; 16771603; 16791115; 16792515; 16809730; 16849011; 16864595; 16865249; 16871576; 16896007; 16909274; 16951398; 16965601; 16969497; 16985250; 17000907; 17060921; 17138857; 17166930; 17185998; 17187418; 17192505; 17196409; 17229650; 17259171; 17273745; 17329852; 17372243; 17374650; 17406868; 17409981; 17426648; 17440429; 17459361; 17471158; 17478602; 17498780; 17506482; 17510208; 17530442; 17549067; 17555467; 17558305; 17576806; 17577039; 17578897; 17593033; 17611564; 17622938; 17627617; 17681105; 17700594; 17728214; 17762398; 17850628; 17888052; 17898154; 17909964; 17949292; 17952380; 17978490; 17981384; 17990575; 18004206; 18004212; 18043502; 18052087; 18081723; 18082937; 18161889; 18172616; 18181169; 18221820; 18223459; 18240903; 18300238; 18324905; 18335219; 18343383; 18349273; 18349289; 18375480; 18379174; 18392554; 18419642; 18430559; 18454993; 18491077; 18498916; 18509181; 18547414; 18558634; 18594531; 18597651; 18675828; 18685565; 18695635; 18756540; 18768784; 18781851; 18790042; 18797458; 18818748; 18832463; 18953066; 18981166; 18982743; 18990750; 18992148; 19019335; 19021734; 19077918; 19141701; 19204906; 19207584; 19217809; 19238116; 19243019; 19268007; 19279563; 19299905; 19303655; 19309288; 19325249; 19336732; 19343046; 19349540; 19349543; 19352303; 19356098; 19364970; 19371317; 19389676; 19390945; 19397531; 19406951; 19414484; 19419973; 19424794; 19430380; 19450125; 19482841; 19486253; 19513514; 19527514; 19546880; 19620808; 19636001; 19639031; 19674361; 19683255; 19712005; 19732760; 19771428; 19797611; 19830808; 19858149; 19858398; 19859999; 19861894; 19888426; 19891553; 19898482; 19913121; 19932091; 19948621; 19996319; 20028383; 20038727; 20057336; 20061399; 20063115; 20064729; 20070246; 20087647; 20096102; 20136364; 20140262; 20142249; 20173083; 20177420; 20197307; 20207827; 20214802; 20215562; 20216541; 20235787; 20297805; 20308029; 20335017; 20358470; 20371435; 20376058; 20377135; 20378551; 20381444; 20385995; 20389299; 20402064; 20430047; 20483464; 20485444; 20504240; 20528217; 20528568; 20529348; 20530282; 20546738; 20562211; 20562445; 20580994; 20600030; 20620155; 20628086; 20628391; 20639394; 20643254; 20647221; 20648548; 20650040; 20653675; 20679960; 20686835; 20709051; 20734064; 20823282; 20837016; 20860988; 20865252; 20890421; 20948202; 20975617; 21072184; 21080475; 21092520; 21150467; 21266593; 21272068; 21275655; 21317830; 21319362; 21342357; 21351260; 21411679; 21473286; 21513526; 21614935; 21646302; 21760472; 21771722; 21886157; 21911884; 21978357; 21983082; 21988832; 22050734; 22085899; 22169899; 22199302; 22212955; 22213983; 22214020; 22273851; 22299209; 22307138; 22318545; 22325916; 22340355; 22357454; 22367021; 22371261; 22398043; 22448797; 22450351; 22475179; 22511988; 22537951; 22558097; 22559977; 22648071; 22661630; 22676194; 22749334; 22808571; 22829544; 23014115; 23053265; 23130636; 23147267; 23148286; 23148825; 23207817; 23236239; 23281178; 23290513; 23303296; 23350445; 23371916; 23386248; 23461146; 23516488; 23517300; 23548653; 23580084; 23642732; 23647681; 23753274; 23781580; 23881212; 23892411; 23898114; 23926009; 23950218; 23964438; 24033692; 24195516; 24217933; 24341141; 24403462 UDP glucuronosyltransferase 1 family, polypeptide A1 Ensembl:ENSG00000242366 HGNC:12530 HPRD:08933 MIM:191740 Vega:OTTHUMG00000059117 Other designations: UDP glycosyltransferase 1 family, polypeptide A1|UDP-glucuronosyltransferase 1-1|UDP-glucuronosyltransferase 1-A|UDP-glucuronosyltransferase 1A1|UGT-1A|UGT1*1|UGT1-01|UGT1.1|bilirubin UDP-glucuronosyltransferase 1-1|bilirubin UDP-glucuronosyltransferase isozyme 1|bilirubin-specific UDPGT isozyme 1 UGT1A1 OGG:3000054788 Bin Zhao, Yue Liu, Oliver He DJ10 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB12 DnaJ (Hsp40) homolog, subfamily B, member 12 54788 10q22.1 9606 10 GO_0016021 (EC: IEA) PMID:8125298; 11147971; 12477932; 14702039; 15489334; 17207965; 17342744; 18029348; 18781797; 21139048; 21148293; 21150129; 21150319; 21890473; 21906983; 21963094; 21987572; 22939629; 23000965; 23956138; 24250222 DnaJ (Hsp40) homolog, subfamily B, member 12 Ensembl:ENSG00000148719 HGNC:14891 HPRD:07086 MIM:608376 Vega:OTTHUMG00000018436 Other designations: dnaJ homolog subfamily B member 12 DNAJB12 OGG:3000054905 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CYP2W1 cytochrome P450, family 2, subfamily W, polypeptide 1 54905 7p22.3 9606 7 GO_0004497 (EC: IEA); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0016705 (EC: IEA); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS) PMID:12477932; 15128046; 15489334; 16426568; 16677611; 17979506; 17998294; 20602611; 20805301; 21988832; 22591743; 22631658; 22993331; 23897914 cytochrome P450, family 2, subfamily W, polypeptide 1 Other designations: CYPIIW1|cytochrome P450 2W1 CYP2W1 OGG:3000054943 Bin Zhao, Yue Liu, Oliver He C21orf55 C21orf78 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC28 DnaJ (Hsp40) homolog, subfamily C, member 28 54943 21q22.11 9606 21 PMID:8125298; 10830953; 12036298; 12477932; 14702039; 15489334; 16344560; 21900206; 21906983; 24250222 DnaJ (Hsp40) homolog, subfamily C, member 28 Ensembl:ENSG00000177692 HGNC:1297 HPRD:10752 Vega:OTTHUMG00000065531 Other designations: dnaJ homolog subfamily C member 28 DNAJC28 OGG:3000054951 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene COMMD8 COMM domain containing 8 54951 MDS022 4p12 9606 4 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 15799966) PMID: 12477932; 14702039; 15489334; 15799966; 16169070; 17207965; 20379614; 21139048; 21890473; 21900206; 22939629; 23000965; 23563313; 24250222 COMM domain containing 8 Other designations: COMM domain-containing protein 8 COMMD8 OGG:3000055089 Bin Zhao, Yue Liu, Oliver He ATA3 NAT3 PAAT WEB: http://www.ncbi.nlm.nih.gov/gene SLC38A4 solute carrier family 38, member 4 55089 12q13 20140408 9606 12 protein-coding Official from a nomenclature committee GO_0005886 (EC: TAS); GO_0006811 (EC: TAS); GO_0006814 (EC: IEA); GO_0006865 (EC: TAS); GO_0015171 (EC: IEA); GO_0015293 (EC: IEA); GO_0016021 (EC: IEA); GO_0055085 (EC: TAS) PMID: 11342143; 11414754; 12477932; 12845534; 14702039; 15489334; 16148032; 16344560; 16712791; 18195088; 18703994; 19015196; 21917917; 22945694 solute carrier family 38, member 4 Ensembl:ENSG00000139209 HGNC:14679 HPRD:12159 MIM:608065 Vega:OTTHUMG00000169518 Other designations: N amino acid transporter 3|Na(+)-coupled neutral amino acid transporter 4|amino acid transporter A3|amino acid transporter system A3|sodium-coupled neutral amino acid transporter 4|system A amino acid transporter 3|system N amino acid transporter 3 SLC38A4 OGG:3000055109 Bin Zhao, Yue Liu, Oliver He GPATC7 GPATCH7 HSU84971 HUS84971 VG5Q WEB: http://www.ncbi.nlm.nih.gov/gene AGGF1 angiogenic factor with G patch and FHA domains 1 55109 5q13.3 20140408 9606 5 protein-coding Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0001570 (EC: TAS, PMID: 15905966); GO_0001938 (EC: IDA, PMID: 14961121); GO_0003676 (EC: IEA); GO_0005515 (EC: IPI, PMID: 14961121); GO_0005576 (EC: IDA, PMID: 14961121); GO_0005737 (EC: IDA, PMID: 14961121); GO_0006396 (EC: TAS, PMID: 15486042); GO_0007155 (EC: IDA, PMID: 14961121); GO_0045766 (EC: IDA, PMID: 14961121); GO_0048471 (EC: IDA, PMID: 14961121) PMID: 10737800; 12477932; 14702039; 14961121; 15486042; 15489334; 15905966; 16189514; 16443853; 16911369; 17103452; 17332742; 18564129; 19556247; 19615732; 20360068; 21576349; 22365833; 22990118; 23628701 angiogenic factor with G patch and FHA domains 1 Ensembl:ENSG00000164252 HGNC:24684 HPRD:07621 MIM:608464 Vega:OTTHUMG00000102132 Other designations: G patch domain-containing protein 7|angiogenic factor VG5Q|vasculogenesis gene on 5q protein AGGF1 OGG:3000055190 Bin Zhao, Yue Liu, Oliver He APS1 ASP1 DIPP3b DIPP3beta hDIPP3beta WEB: http://www.ncbi.nlm.nih.gov/gene NUDT11 nudix (nucleoside diphosphate linked moiety X)-type motif 11 55190 RP11-348F1.5 Xp11.22 9606 X Official from a nomenclature committee GO_0005622 (EC: IDA); GO_0005829 (EC: TAS); GO_0008486 (EC: ISS); GO_0043647 (EC: TAS); GO_0044281 (EC: TAS); GO_0046872 (EC: IEA); GO_0052840 (EC: IEA); GO_0052843 (EC: IEA); GO_0052844 (EC: IEA); GO_0052845 (EC: IEA); GO_0052846 (EC: IEA); GO_0052847 (EC: IEA); GO_0052848 (EC: IEA) PMID: 11076863; 11256614; 12105228; 12121577; 12370170; 12477932; 14702039; 15345747; 15489334; 15489336; 15772651; 16381901; 18264097; 18264098; 18854154; 19902474; 21071540; 21139048; 22730461 nudix (nucleoside diphosphate linked moiety X)-type motif 11 Ensembl:ENSG00000196368 HGNC:18011 HPRD:06667 MIM:300528 Vega:OTTHUMG00000021531 Other designations: DIPP-3-beta|DIPP3-beta|diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-beta|diadenosine hexaphosphate hydrolase (AMP-forming)|diphosphoinositol polyphosphate phosphohydrolase 3, beta|diphosphoinositol polyphosphate phosphohydrolase 3-beta|hAps1|nucleoside diphosphate-linked moiety X motif 11|nudix motif 11 NUDT11 OGG:3000055192 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC17 DnaJ (Hsp40) homolog, subfamily C, member 17 55192 15q15.1 9606 15 GO_0000166 (EC: IEA); GO_0003723 (EC: IEA) PMID:12477932; 14702039; 15489334; 16344560; 17081983; 19913121; 20628086; 21139048; 21890473 DnaJ (Hsp40) homolog, subfamily C, member 17 Other designations: dnaJ homolog subfamily C member 17 DNAJC17 OGG:3000055224 Bin Zhao, Yue Liu, Oliver He EKI2 HMFT1716 WEB: http://www.ncbi.nlm.nih.gov/gene ETNK2 ethanolamine kinase 2 55224 RP11-74C13.2 1q32.1 9606 1 Official from a nomenclature committee GO_0001701 (EC: IEA); GO_0001890 (EC: IEA); GO_0004305 (EC: IEA); GO_0005524 (EC: IEA); GO_0005575 (EC: ND); GO_0005829 (EC: TAS); GO_0006644 (EC: TAS); GO_0006646 (EC: IEA); GO_0006646 (EC: TAS); GO_0008150 (EC: ND); GO_0009791 (EC: IEA); GO_0035264 (EC: IEA); GO_0044281 (EC: TAS); GO_0046474 (EC: TAS) PMID: 11044454; 12477932; 14702039; 15161093; 16189514; 16861741; 18953568; 19060904; 19536175; 21177773; 24024966 ethanolamine kinase 2 Ensembl:ENSG00000143845 HGNC:25575 HPRD:13283 MIM:609859 Vega:OTTHUMG00000036061 Other designations: EKI 2|ethanolamine kinase-like protein ETNK2 OGG:3000055289 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene ACOXL acyl-CoA oxidase-like 55289 2q13 9606 2 GO_0003674 (EC: ND); GO_0003995 (EC: IEA); GO_0003997 (EC: IEA); GO_0005575 (EC: ND); GO_0005777 (EC: IEA); GO_0006635 (EC: IEA); GO_0008150 (EC: ND) PMID:12477932; 14702039; 15146197; 18758461; 19773279; 20332261; 20731705; 21145461; 21738478; 22197929; 22219177; 22566634; 22700719; 23222517; 23770605 acyl-CoA oxidase-like Other designations: acyl-CoA oxidase-like protein|acyl-coenzyme A oxidase-like protein ACOXL OGG:3000055304 Bin Zhao, Yue Liu, Oliver He C20orf38 LCB2B LCB3 SPT3 SPTLC2L dJ718P11 dJ718P11.1 hLCB2b WEB: http://www.ncbi.nlm.nih.gov/gene SPTLC3 serine palmitoyltransferase, long chain base subunit 3 55304 RP5-1077I2.1 20p12.1 20140408 9606 20 protein-coding Official from a nomenclature committee GO_0004758 (EC: IDA, PMID: 19416851); GO_0005789 (EC: TAS); GO_0006665 (EC: TAS); GO_0016021 (EC: IEA); GO_0017059 (EC: IDA, PMID: 17331073); GO_0030148 (EC: TAS, PMID: 19416851); GO_0030170 (EC: IEA); GO_0044281 (EC: TAS); GO_0046520 (EC: IDA, PMID: 19648650) PMID: 11780052; 12477932; 14702039; 15489334; 16303743; 17023427; 17331073; 19416851; 19648650; 19798445; 19913121; 20037589; 20379614; 20628086; 20920666; 21368711; 22359512; 23192594 serine palmitoyltransferase, long chain base subunit 3 Ensembl:ENSG00000172296 HGNC:16253 HPRD:12765 MIM:611120 Vega:OTTHUMG00000031899 Other designations: LCB 3|SPT 3|long chain base biosynthesis protein 2b|long chain base biosynthesis protein 3|serine palmitoyltransferase 3|serine palmitoyltransferase, long chain base subunit 2-like (aminotransferase 2)|serine-palmitoyl-CoA transferase 3 SPTLC3 OGG:3000055331 Bin Zhao, Yue Liu, Oliver He APHC PHCA WEB: http://www.ncbi.nlm.nih.gov/gene ACER3 alkaline ceramidase 3 55331 11q13.5 9606 11 Official from a nomenclature committee GO_0005789 (EC: TAS); GO_0006665 (EC: TAS); GO_0006672 (EC: IEA); GO_0008284 (EC: IMP); GO_0030148 (EC: TAS); GO_0030173 (EC: IDA, PMID: 11356846); GO_0030176 (EC: IDA, PMID: 11356846); GO_0044281 (EC: TAS); GO_0046512 (EC: IDA); GO_0070774 (EC: IDA, PMID: 11356846); GO_0071602 (EC: IDA, PMID: 11356846) PMID: 11356846; 12477932; 14702039; 15489334; 17207965; 18619555; 19322201; 19834535; 19913121; 20068046; 20379614; 20628086; 20706999 alkaline ceramidase 3 HGNC:16066 HPRD:17844 Other designations: alkCDase 3|alkaline CDase 3|alkaline dihydroceramidase SB89|alkaline phytoceramidase|phytoceramidase, alkaline ACER3 OGG:3000055350 Bin Zhao, Yue Liu, Oliver He HSA238982 WEB: http://www.ncbi.nlm.nih.gov/gene VNN3 vanin 3 55350 6q23.2 9606 6 Official from a nomenclature committee GO_0005575 (EC: ND); GO_0005615 (EC: IEA); GO_0005886 (EC: IEA); GO_0008150 (EC: ND); GO_0015939 (EC: IEA); GO_0017159 (EC: NAS, PMID: 11491533); GO_0031225 (EC: IEA) PMID: 10501839; 11491533; 12477932; 14574404; 16344560; 18805469; 19322213; 19932582 vanin 3 Ensembl:ENSG00000093134 HGNC:16431 HPRD:09420 MIM:606592 Vega:OTTHUMG00000015589 VNN3 OGG:3000055571 Bin Zhao, Yue Liu, Oliver He C2orf29 WEB: http://www.ncbi.nlm.nih.gov/gene CNOT11 CCR4-NOT transcription complex, subunit 11 55571 C40 2q11.2 9606 2 Official from a nomenclature committee GO_0000288 (EC: TAS); GO_0000289 (EC: TAS); GO_0003674 (EC: ND); GO_0005515 (EC: IPI); GO_0005634 (EC: IEA); GO_0005829 (EC: TAS); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0006417 (EC: IEA); GO_0008283 (EC: NAS, PMID: 10497265); GO_0010467 (EC: TAS); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0030014 (EC: IDA, PMID: 19558367); GO_0031047 (EC: IEA) PMID: 10497265; 12477932; 14702039; 15489334; 15815621; 19322201; 19558367; 20360068; 21139048; 21890473; 21906983; 21963094; 22505724; 23232451; 23303381; 23602568; 24250222 CCR4-NOT transcription complex, subunit 11 Ensembl:ENSG00000158435 HGNC:25217 HPRD:12812 Vega:OTTHUMG00000130686 Other designations: CCR4-NOT transcription complex subunit 11|UPF0760 protein C2orf29 CNOT11 OGG:3000055629 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene PNRC2 proline-rich nuclear receptor coactivator 2 55629 RP11-4M23.5 1p36.11 9606 1 Official from a nomenclature committee GO_0000184 (EC: IDA, PMID: 19150429); GO_0000932 (EC: IDA, PMID: 19150429); GO_0005515 (EC: IPI, PMID: 19150429); GO_0005634 (EC: IDA, PMID: 19150429); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0031087 (EC: TAS, PMID: 19150429) PMID: 10894149; 11042152; 11574675; 12477932; 14651967; 14702039; 15489334; 15604093; 16169070; 16344560; 16710414; 19150429; 21900206; 21906983; 23085078; 23251661 proline-rich nuclear receptor coactivator 2 PNRC2 OGG:3000055632 Bin Zhao, Yue Liu, Oliver He KIAA1333 PHF7B WEB: http://www.ncbi.nlm.nih.gov/gene G2E3 G2/M-phase specific E3 ubiquitin protein ligase 55632 14q12 9606 14 Official from a nomenclature committee GO_0000209 (EC: IEA); GO_0001824 (EC: IEA); GO_0004842 (EC: IEA); GO_0005730 (EC: IEA); GO_0005737 (EC: IEA); GO_0006915 (EC: IEA); GO_0008270 (EC: IEA); GO_2001243 (EC: IEA) PMID: 8125298; 10718198; 11483598; 12477932; 14667819; 14702039; 15489334; 16189514; 16344560; 17239372; 18029348; 18511420; 21139048; 21890473; 22939624; 23000965 G2/M-phase specific E3 ubiquitin protein ligase Ensembl:ENSG00000092140 HGNC:20338 HPRD:13851 MIM:611299 Vega:OTTHUMG00000140204 Other designations: G2/M phase-specific E3 ubiquitin-protein ligase|G2/M-phase specific E3 ubiquitin ligase|PHD finger protein 7B G2E3 OGG:3000055729 Bin Zhao, Yue Liu, Oliver He AM ATF-IP MCAF MCAF1 p621 WEB: http://www.ncbi.nlm.nih.gov/gene ATF7IP activating transcription factor 7 interacting protein 55729 12p13.1 9606 12 GO_0000122 (EC: IEA); GO_0003714 (EC: IEA); GO_0005515 (EC: IPI, PMID:12665582); GO_0005634 (EC: IDA, PMID:12665582); GO_0005667 (EC: IEA); GO_0006306 (EC: IDA, PMID:12665582); GO_0006351 (EC: IEA); GO_0016032 (EC: IEA); GO_0016887 (EC: IEA); GO_0045892 (EC: IDA, PMID:12665582); GO_0045893 (EC: IDA, PMID:12665582); GO_0045898 (EC: IDA, PMID:12665582) PMID:10777215; 10976766; 12477932; 12659632; 12665582; 12812986; 14536086; 14702039; 15231748; 15489334; 15691849; 16314315; 16344560; 16757475; 17081983; 18029348; 18842587; 19106100; 19394292; 19471022; 20543847; 20549333; 20936779; 21139048; 21693764; 21890473; 21906983; 21963094; 21987572; 21988832; 22939629; 23000965; 23359319; 23666240; 23935871; 24250222 activating transcription factor 7 interacting protein Ensembl:ENSG00000171681 HGNC:20092 HPRD:09811 MIM:613644 Vega:OTTHUMG00000168656 Other designations: ATF-interacting protein|ATF7-interacting protein|ATFa-associated modulator|MBD1-containing chromatin-associated factor 1|activating transcription factor 7-interacting protein 1 ATF7IP OGG:3000055735 Bin Zhao, Yue Liu, Oliver He dJ126A5.1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC11 DnaJ (Hsp40) homolog, subfamily C, member 11 55735 RP1-126A5.3 1p36.31 9606 1 GO_0005515 (EC: IPI, PMID:17500595); GO_0005743 (EC: IEA) PMID:8619474; 9110174; 12477932; 12964007; 14702039; 15489334; 16710414; 17207965; 17222547; 17500595; 17624330; 19808946; 20877624; 21139048; 21890473; 21900206; 21906983; 21987572; 22114354; 22268729; 24255178 DnaJ (Hsp40) homolog, subfamily C, member 11 Ensembl:ENSG00000007923 HGNC:25570 HPRD:07112 MIM:614827 Vega:OTTHUMG00000001443 Other designations: dnaJ homolog subfamily C member 11|novel DnaJ domain-containing protein DNAJC11 OGG:3000055741 Bin Zhao, Yue Liu, Oliver He C20orf31 C20orf49 bA4204.1 WEB: http://www.ncbi.nlm.nih.gov/gene EDEM2 ER degradation enhancer, mannosidase alpha-like 2 55741 UNQ573/PRO1135 20q11.22 9606 20 GO_0004571 (EC: IDA, Qualifier: NOT, PMID:15537790); GO_0005509 (EC: IEA); GO_0005576 (EC: IEA); GO_0005788 (EC: IEA); GO_0005789 (EC: TAS); GO_0006457 (EC: TAS); GO_0006986 (EC: IEA); GO_0018279 (EC: TAS); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS) PMID:8619474; 9110174; 11780052; 12477932; 12975309; 14702039; 15342556; 15489334; 15537790; 15579471; 16169070; 17499246; 18303019; 20802025; 21822266; 21906983; 22703881; 24250222 ER degradation enhancer, mannosidase alpha-like 2 Ensembl:ENSG00000088298 HGNC:15877 HPRD:09841 MIM:610302 Vega:OTTHUMG00000032322 Other designations: ER degradation-enhancing alpha-mannosidase-like 2|ER degradation-enhancing alpha-mannosidase-like protein 2|ER degradation-enhancing-mannosidase-like protein 2 EDEM2 OGG:3000055803 Bin Zhao, Yue Liu, Oliver He CENTA2 HSA272195 cent-b WEB: http://www.ncbi.nlm.nih.gov/gene ADAP2 ArfGAP with dual PH domains 2 55803 17q11.2 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0005515 (EC: IPI); GO_0005546 (EC: ISS, PMID: 12018390); GO_0005547 (EC: IDA, PMID: 14690521); GO_0005737 (EC: IDA, PMID: 14690521); GO_0005740 (EC: ISS, PMID: 12018390); GO_0005886 (EC: IDA, PMID: 14690521); GO_0007507 (EC: IEP, PMID: 16138909); GO_0008060 (EC: IEA); GO_0008270 (EC: IEA); GO_0030674 (EC: NAS, PMID: 14690521); GO_0032312 (EC: IEA); GO_0043325 (EC: ISS, PMID: 12018390); GO_0043533 (EC: IDA, PMID: 14690521) PMID: 8125298; 10843809; 12018390; 12477932; 14690521; 15489334; 16138909; 16169070; 17207965; 17632510; 18391951; 18482256; 18541383; 19266077; 19291764; 19953087; 20098747; 20379614; 20546612; 21832049; 23285209 ArfGAP with dual PH domains 2 Ensembl:ENSG00000184060 HGNC:16487 HPRD:16357 MIM:608635 Vega:OTTHUMG00000132868 Other designations: arf-GAP with dual PH domain-containing protein 2|centaurin beta|centaurin, alpha 2|centaurin-alpha 2 protein|centaurin-alpha-2|cnt-a2 ADAP2 OGG:3000055819 Bin Zhao, Yue Liu, Oliver He G1RZFP GOLIATH GP WEB: http://www.ncbi.nlm.nih.gov/gene RNF130 ring finger protein 130 55819 5q35.3 9606 5 Official from a nomenclature committee GO_0004842 (EC: IDA, PMID: 16549277); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA); GO_0006915 (EC: IEA); GO_0008270 (EC: IEA); GO_0012501 (EC: ISS, PMID: 13679316); GO_0016021 (EC: IEA) PMID: 7566098; 10806348; 12477932; 13679316; 15489334; 15761153; 16169070; 16549277; 16797685; 18029348; 19690564; 21139048; 21150319; 21347282; 22505724; 24250222 ring finger protein 130 Ensembl:ENSG00000113269 HGNC:18280 HPRD:11504 Vega:OTTHUMG00000130909 Other designations: E3 ubiquitin-protein ligase RNF130|g1-related zinc finger protein|goliath homolog RNF130 OGG:3000055856 Bin Zhao, Yue Liu, Oliver He PNAS-27 THEM2 WEB: http://www.ncbi.nlm.nih.gov/gene ACOT13 acyl-CoA thioesterase 13 55856 HT012 6p22.3 9606 6 GO_0005739 (EC: IEA); GO_0008152 (EC: IDA, PMID:16934754); GO_0047617 (EC: IDA, PMID:16934754); GO_0051289 (EC: IPI, PMID:16934754) PMID:8889548; 10931946; 12477932; 14574404; 14702039; 15489334; 16344560; 16934754; 17045243; 17704541; 18095154; 18624398; 19170545; 19405909; 19738201; 20877624; 21139048; 21319273; 22262880; 22939629; 23954868; 24250222 acyl-CoA thioesterase 13 Ensembl:ENSG00000112304 HGNC:20999 HPRD:07158 MIM:615652 Vega:OTTHUMG00000014359 Other designations: acyl-coenzyme A thioesterase 13|hypothalamus protein HT012|thioesterase superfamily member 2 ACOT13 OGG:3000056478 Bin Zhao, Yue Liu, Oliver He 4E-T Clast4 WEB: http://www.ncbi.nlm.nih.gov/gene EIF4ENIF1 eukaryotic translation initiation factor 4E nuclear import factor 1 56478 RP11-247I13.2 22q11.2 9606 22 GO_0005515 (EC: IPI, PMID:10856257); GO_0005634 (EC: TAS, PMID:10856257); GO_0005737 (EC: TAS, PMID:10856257); GO_0005829 (EC: IEA); GO_0008565 (EC: TAS, PMID:10856257); GO_0016605 (EC: IEA); GO_0016607 (EC: IEA); GO_0043231 (EC: IDA); GO_0044822 (EC: IDA) PMID:10856257; 12477932; 14651998; 14702039; 15345747; 15461802; 15489334; 15840819; 16147992; 16157702; 16189514; 16343815; 16344560; 16699599; 16713569; 17314511; 17567994; 18029348; 18343217; 19060904; 19850929; 22094256; 22505724; 22751931; 22966201; 23902945; 24255178 eukaryotic translation initiation factor 4E nuclear import factor 1 Ensembl:ENSG00000184708 HGNC:16687 HPRD:10456 MIM:607445 Vega:OTTHUMG00000030793 Other designations: 2610509L04Rik|eIF4E transporter|eIF4E-transporter|eukaryotic translation initiation factor 4E transporter EIF4ENIF1 OGG:3000056521 Bin Zhao, Yue Liu, Oliver He JDP1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC12 DnaJ (Hsp40) homolog, subfamily C, member 12 56521 RP11-57G10.2 10q22.1 9606 10 PMID:10760603; 12477932; 15164054; 15489334; 16385451; 16391838; 16712791; 17373700; 21832049; 22939629 DnaJ (Hsp40) homolog, subfamily C, member 12 Ensembl:ENSG00000108176 HGNC:28908 HPRD:06930 MIM:606060 Vega:OTTHUMG00000018339 Other designations: J domain containing protein 1 (JDP1)|J domain protein 1|dnaJ homolog subfamily C member 12|j domain-containing protein 1 DNAJC12 OGG:3000056603 Bin Zhao, Yue Liu, Oliver He CYP26A2 P450RAI-2 P450RAI2 RHFCA WEB: http://www.ncbi.nlm.nih.gov/gene CYP26B1 cytochrome P450, family 26, subfamily B, polypeptide 1 56603 2p13.2 9606 2 GO_0001709 (EC: ISS); GO_0001972 (EC: IDA, PMID:10823918); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006766 (EC: TAS); GO_0006805 (EC: TAS); GO_0007140 (EC: ISS); GO_0007283 (EC: ISS); GO_0008401 (EC: IDA, PMID:10823918); GO_0009954 (EC: ISS); GO_0010628 (EC: IEA); GO_0020037 (EC: NAS, PMID:10823918); GO_0030326 (EC: ISS); GO_0034653 (EC: IDA, PMID:10823918); GO_0043587 (EC: IEA); GO_0044281 (EC: TAS); GO_0048384 (EC: IEA); GO_0048387 (EC: TAS, PMID:14532297); GO_0055114 (EC: IDA, PMID:10823918); GO_0060349 (EC: IMP); GO_0071300 (EC: IEA); GO_2001037 (EC: IEA) PMID:10545224; 10823918; 11744378; 12101034; 12477932; 14532297; 15128046; 15489334; 15815621; 16574820; 16933217; 19322201; 19703508; 19884280; 19953087; 20375987; 20606468; 21482329; 21641851; 21945024; 22019272; 22020119; 22415012; 22666329; 22899867; 22965740; 22985482; 23298258; 23303528; 23320086; 23409080; 23554885; 23587162; 23837398 cytochrome P450, family 26, subfamily B, polypeptide 1 Ensembl:ENSG00000003137 HGNC:20581 HPRD:05550 MIM:605207 Vega:OTTHUMG00000129756 Other designations: cytochrome P450 26B1|cytochrome P450 retinoic acid-inactivating 2|cytochrome P450 retinoid metabolizing protein|cytochrome P450, subfamily XXVIB, polypeptide 1|retinoic acid-metabolizing cytochrome CYP26B1 OGG:3000056605 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene ERO1LB ERO1-like beta (S. cerevisiae) 56605 RP5-985L19.2 1q42.2-q43 9606 1 Official from a nomenclature committee GO_0003756 (EC: IEA); GO_0005515 (EC: IPI); GO_0005783 (EC: TAS, PMID: 10818100); GO_0005789 (EC: IEA); GO_0006457 (EC: TAS, PMID: 10818100); GO_0016491 (EC: NAS, PMID: 10818100); GO_0016671 (EC: IEA); GO_0051082 (EC: NAS, PMID: 10818100) PMID: 10818100; 11707400; 11847130; 12477932; 12752442; 14702039; 15161913; 15489334; 16012172; 16263699; 16677073; 16822866; 17207965; 18395550; 18996753; 19730683; 20379614; 20802462; 21091435; 21139048; 22268729; 22990118 ERO1-like beta (S. cerevisiae) Other designations: ERO1-L-beta|ERO1-like protein beta|endoplasmic oxidoreductin-1-like protein B|endoplasmic reticulum oxidoreductin-1-like protein B|oxidoreductin-1-L-beta ERO1LB OGG:3000056648 Bin Zhao, Yue Liu, Oliver He EIF-5A2 eIF5AII WEB: http://www.ncbi.nlm.nih.gov/gene EIF5A2 eukaryotic translation initiation factor 5A2 56648 3q26.2 9606 3 GO_0003746 (EC: IEA); GO_0005515 (EC: IPI, PMID:14622290); GO_0005643 (EC: IEA); GO_0005789 (EC: IEA); GO_0005829 (EC: TAS); GO_0006452 (EC: IEA); GO_0007283 (EC: NAS, PMID:11161802); GO_0008284 (EC: IGI, PMID:14622290); GO_0008612 (EC: TAS); GO_0010509 (EC: NAS, PMID:11161802); GO_0015031 (EC: IEA); GO_0043022 (EC: IEA); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS); GO_0045901 (EC: IEA); GO_0045905 (EC: IEA); GO_0051028 (EC: IEA) PMID:11161802; 11325856; 12477932; 14622290; 15205331; 15489334; 15635413; 16169419; 16189514; 16452303; 16519677; 16916647; 17876542; 17949776; 19054548; 19155439; 19298601; 20112425; 20434207; 20639865; 21139048; 21145461; 21319273; 21813470; 21890473; 21903422; 21906983; 21942715; 21963094; 21988832; 22053931; 22505724; 22927971; 23000965 eukaryotic translation initiation factor 5A2 Ensembl:ENSG00000163577 HGNC:3301 HPRD:10426 MIM:605782 Vega:OTTHUMG00000158958 Other designations: eIF-5A-2|eukaryotic initiation factor 5A|eukaryotic translation initiation factor 5A-2 EIF5A2 OGG:3000056649 Bin Zhao, Yue Liu, Oliver He CAPH2 MT-SP2 TMPRSS3 WEB: http://www.ncbi.nlm.nih.gov/gene TMPRSS4 transmembrane protease, serine 4 56649 UNQ776/PRO1570 11q23.3 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0004252 (EC: NAS, PMID: 10825129); GO_0005044 (EC: IEA); GO_0006508 (EC: NAS, PMID: 10825129); GO_0016021 (EC: NAS, PMID: 10825129) PMID: 8889548; 10825129; 12477932; 12975309; 14702039; 15342556; 15489334; 17207965; 17968309; 18029348; 19158246; 20118200; 20631123; 21637307; 22067904; 22692880; 22944691; 23420063; 24299317 transmembrane protease, serine 4 HGNC:11878 HPRD:05952 MIM:606565 Other designations: channel-activating protease 2|membrane-type serine protease 2|transmembrane protease serine 4|transmembrane serine protease 3|type II membrane serine protease TMPRSS4 OGG:3000056910 Bin Zhao, Yue Liu, Oliver He GTT1 WEB: http://www.ncbi.nlm.nih.gov/gene STARD7 StAR-related lipid transfer (START) domain containing 7 56910 2q11.2 9606 2 Official from a nomenclature committee GO_0005739 (EC: IEA); GO_0008289 (EC: IEA) PMID: 12477932; 14702039; 15013637; 15146197; 15489334; 17672918; 19679347; 20042613; 21622533; 21906983; 22063720; 22952907; 23247143; 23824909; 24250222 StAR-related lipid transfer (START) domain containing 7 Ensembl:ENSG00000084090 HGNC:18063 HPRD:18118 Vega:OTTHUMG00000130457 Other designations: START domain containing 7|START domain-containing protein 7|gestational trophoblastic tumor protein 1|stAR-related lipid transfer protein 7, mitochondrial STARD7 OGG:3000057153 Bin Zhao, Yue Liu, Oliver He CTL2 PP1292 WEB: http://www.ncbi.nlm.nih.gov/gene SLC44A2 solute carrier family 44 (choline transporter), member 2 57153 PSEC0210 19p13.1 9606 19 Official from a nomenclature committee GO_0004871 (EC: IMP, PMID: 12761501); GO_0005765 (EC: IDA, PMID: 17897319); GO_0005886 (EC: TAS); GO_0006644 (EC: TAS); GO_0006656 (EC: TAS); GO_0007165 (EC: IMP, PMID: 12761501); GO_0015220 (EC: TAS, PMID: 10677542); GO_0015871 (EC: TAS, PMID: 10677542); GO_0016021 (EC: TAS, PMID: 10677542); GO_0043123 (EC: IMP, PMID: 12761501); GO_0044281 (EC: TAS); GO_0046474 (EC: TAS); GO_0055085 (EC: TAS); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 8619474; 9110174; 10677542; 12477932; 12761501; 14702039; 14973250; 15489334; 15715662; 16303743; 16344560; 17897319; 17926100; 18029348; 19056867; 20037594; 20040764; 20410607; 20665236; 21048031; 21564101; 21906983; 22040064; 22211383; 22414054; 23398146; 24250222 solute carrier family 44 (choline transporter), member 2 Ensembl:ENSG00000129353 HGNC:17292 HPRD:16198 MIM:606106 Vega:OTTHUMG00000180585 Other designations: choline transporter-like protein 2|solute carrier family 44, member 2 SLC44A2 OGG:3000057216 Bin Zhao, Yue Liu, Oliver He LPP1 LTAP STB1 STBM STBM1 WEB: http://www.ncbi.nlm.nih.gov/gene VANGL2 VANGL planar cell polarity protein 2 57216 1q22-q23 9606 1 Official from a nomenclature committee GO_0001736 (EC: ISS); GO_0001843 (EC: ISS); GO_0001942 (EC: IEA); GO_0001947 (EC: ISS); GO_0003149 (EC: IEA); GO_0003150 (EC: IEA); GO_0003402 (EC: IEA); GO_0005886 (EC: TAS); GO_0005911 (EC: ISS); GO_0007266 (EC: IEA); GO_0009952 (EC: IEA); GO_0016021 (EC: IEA); GO_0016323 (EC: IEA); GO_0016324 (EC: ISS); GO_0016328 (EC: ISS); GO_0022007 (EC: IEA); GO_0032835 (EC: IEA); GO_0032956 (EC: IEA); GO_0035019 (EC: IEA); GO_0035058 (EC: ISS); GO_0035787 (EC: ISS); GO_0036342 (EC: IEA); GO_0042060 (EC: IEA); GO_0043507 (EC: IEA); GO_0045176 (EC: ISS); GO_0045197 (EC: IEA); GO_0048103 (EC: IEA); GO_0048105 (EC: IEA); GO_0048546 (EC: IEA); GO_0060028 (EC: IEA); GO_0060122 (EC: IEA); GO_0060187 (EC: IEA); GO_0060488 (EC: IEA); GO_0060489 (EC: IEA); GO_0060490 (EC: IEA); GO_0060993 (EC: IEA); GO_0090103 (EC: IEA); GO_0090177 (EC: IEA); GO_0090179 (EC: IEA) PMID: 10574462; 11431695; 12477932; 12490194; 15195140; 15489334; 16710414; 18034999; 18849982; 19577357; 19734545; 20223754; 20558380; 20738329; 21139048; 21142127; 23579212 VANGL planar cell polarity protein 2 Ensembl:ENSG00000162738 HGNC:15511 HPRD:02758 MIM:600533 Vega:OTTHUMG00000033122 Other designations: loop-tail protein 1 homolog|loop-tail-associated protein|strabismus 1|van Gogh-like protein 2|vang-like 2 (van gogh, Drosophila)|vang-like protein 2 VANGL2 OGG:3000057404 Bin Zhao, Yue Liu, Oliver He CYP-M WEB: http://www.ncbi.nlm.nih.gov/gene CYP20A1 cytochrome P450, family 20, subfamily A, polypeptide 1 57404 UNQ667/PRO1301 2q33.2 9606 2 GO_0004497 (EC: IEA); GO_0005506 (EC: IEA); GO_0016021 (EC: IEA); GO_0016705 (EC: IEA); GO_0020037 (EC: IEA) PMID:9890157; 11178272; 12477932; 12975309; 14702039; 15128046; 15191668; 19898482; 20966902; 21832049 cytochrome P450, family 20, subfamily A, polypeptide 1 Ensembl:ENSG00000119004 HGNC:20576 HPRD:07100 Vega:OTTHUMG00000132854 Other designations: cytochrome P450 20A1|cytochrome P450 monooxygenase CYP20A1 OGG:3000057506 Bin Zhao, Yue Liu, Oliver He CARDIF IPS-1 IPS1 VISA WEB: http://www.ncbi.nlm.nih.gov/gene MAVS mitochondrial antiviral signaling protein 57506 20p13 20140408 9606 20 protein-coding Official from a nomenclature committee GO_0001934 (EC: IDA, PMID: 16127453); GO_0002218 (EC: IMP, PMID: 18818105); GO_0002230 (EC: IDA, PMID: 16127453); GO_0002230 (EC: IMP, PMID: 19609254); GO_0004871 (EC: IMP, PMID: 12761501); GO_0005515 (EC: IPI, PMID: 16127453); GO_0005739 (EC: IDA); GO_0005741 (EC: IDA, PMID: 18818105); GO_0005741 (EC: TAS); GO_0005778 (EC: IDA); GO_0007165 (EC: IMP); GO_0016021 (EC: IEA); GO_0016032 (EC: IEA); GO_0019901 (EC: IPI, PMID: 16127453); GO_0031966 (EC: IDA); GO_0032480 (EC: TAS); GO_0032727 (EC: IDA, PMID: 16127453); GO_0032727 (EC: IMP, PMID: 19609254); GO_0032728 (EC: IDA, PMID: 16127453); GO_0032728 (EC: IMP, PMID: 19609254); GO_0032757 (EC: IDA, PMID: 16127453); GO_0032760 (EC: IDA, PMID: 16127453); GO_0033160 (EC: IDA, PMID: 18818105); GO_0039529 (EC: IEA); GO_0042742 (EC: IMP, PMID: 19631370); GO_0042993 (EC: IDA, PMID: 18818105); GO_0043123 (EC: IMP, PMID: 12761501); GO_0045071 (EC: IDA); GO_0045087 (EC: IMP, PMID: 19609254); GO_0045087 (EC: TAS); GO_0045944 (EC: IDA, PMID: 16127453); GO_0050700 (EC: IPI, PMID: 16127453); GO_0051091 (EC: IDA, PMID: 16127453); GO_0051607 (EC: IDA); GO_0060340 (EC: IDA, PMID: 16127453); GO_0071360 (EC: IMP, PMID: 16127453); GO_0071651 (EC: IDA, PMID: 16127453); GO_0071660 (EC: IDA, PMID: 16127453); GO_1900063 (EC: IMP) PMID: 10574462; 11002417; 11780052; 12477932; 12761501; 14702039; 15489334; 16125763; 16127453; 16153868; 16177806; 16239922; 16301520; 16341674; 16344560; 16585524; 16707574; 16731946; 16858409; 16914100; 16964243; 16984921; 17093192; 17911629; 18207245; 18307765; 18550535; 18692023; 18756281; 18818105; 18927075; 18977754; 18984593; 19028691; 19193783; 19351494; 19380491; 19419966; 19454348; 19546225; 19591957; 19609254; 19631370; 19644511; 19690333; 19701189; 19734229; 19881509; 19893624; 19902255; 19914245; 19996094; 20032188; 20044805; 20071582; 20080758; 20097753; 20127681; 20154210; 20159242; 20161788; 20406818; 20434986; 20483786; 20538852; 20554965; 20628368; 20661427; 20699220; 20711230; 20877624; 20962078; 21068253; 21127988; 21130742; 21139048; 21170385; 21187438; 21200404; 21203974; 21268286; 21285412; 21292167; 21421666; 21625535; 21782231; 21813773; 21865020; 21903422; 21957149; 22022264; 22079989; 22105485; 22114345; 22131337; 22341464; 22383950; 22427742; 22588174; 22623778; 22626058; 22674996; 22792062; 22870331; 22901541; 22908223; 22939629; 23028469; 23028806; 23087404; 23246644; 23308256; 23399697; 23460740; 23582325; 24048902; 24285545; 24391214 mitochondrial antiviral signaling protein HGNC:29233 HPRD:13847 MIM:609676 Other designations: CARD adapter inducing interferon beta|CARD adaptor inducing IFN-beta|IFN-B promoter stimulator 1|interferon beta promoter stimulator protein 1|mitochondrial antiviral-signaling protein|putative NF-kappa-B-activating protein 031N|virus-induced signaling adaptor|virus-induced-signaling adapter MAVS OGG:3000057546 Bin Zhao, Yue Liu, Oliver He PPM2C2 WEB: http://www.ncbi.nlm.nih.gov/gene PDP2 pyruvate dehyrogenase phosphatase catalytic subunit 2 57546 16q22.1 9606 16 Official from a nomenclature committee GO_0004724 (EC: IEA); GO_0004741 (EC: IEA); GO_0005759 (EC: TAS); GO_0006090 (EC: TAS); GO_0010510 (EC: TAS); GO_0035970 (EC: IEA); GO_0044237 (EC: TAS); GO_0044281 (EC: TAS); GO_0046872 (EC: IEA) PMID: 8889548; 9651365; 10718198; 11577086; 12477932; 12676647; 15489334; 17207965; 20208177; 20525856; 20877624; 20972266; 21890473 pyruvate dehyrogenase phosphatase catalytic subunit 2 Ensembl:ENSG00000172840 HGNC:30263 HPRD:15112 MIM:615499 Vega:OTTHUMG00000137512 Other designations: PDPC 2|[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial|protein phosphatase 2C, magnesium-dependent, catalytic subunit 2|pyruvate dehydrogenase phosphatase catalytic subunit 2|pyruvate dehydrogenase phosphatase isoenzyme 2|pyruvate dehydrogenase phosphatase, catalytic subunit 2 PDP2 gene OGG:3000057600 Bin Zhao, Yue Liu, Oliver He FNIPL MAPO1 WEB: http://www.ncbi.nlm.nih.gov/gene FNIP2 folliculin interacting protein 2 57600 4q32.1 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0000122 (EC: IDA); GO_0001932 (EC: IDA, PMID: 18663353); GO_0005515 (EC: IPI, PMID: 18403135); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA); GO_0005815 (EC: IDA); GO_0005886 (EC: IDA); GO_0006468 (EC: IDA, PMID: 18663353); GO_0008630 (EC: ISS); GO_0033138 (EC: IDA, PMID: 19914239) PMID: 10819331; 12477932; 14702039; 18029348; 18403135; 18663353; 19914239; 20379614; 23201403 folliculin interacting protein 2 Ensembl:ENSG00000052795 HGNC:29280 MIM:612768 Vega:OTTHUMG00000161983 Other designations: FNIP1-like protein|O6-methylguanine-induced apoptosis 1 protein|folliculin-interacting protein 2 FNIP2 OGG:3000057761 Bin Zhao, Yue Liu, Oliver He C20orf97 NIPK SINK SKIP3 TRB3 WEB: http://www.ncbi.nlm.nih.gov/gene TRIB3 tribbles pseudokinase 3 57761 RP5-1103G7.7 20p13-p12.2 9606 20 Official from a nomenclature committee GO_0003714 (EC: ISS); GO_0004860 (EC: IEA); GO_0005515 (EC: IPI, PMID: 12743605); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005634 (EC: ISS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005829 (EC: TAS); GO_0005886 (EC: TAS); GO_0006351 (EC: IEA); GO_0006468 (EC: IEA); GO_0006469 (EC: IDA, PMID: 12791994); GO_0007173 (EC: TAS); GO_0008286 (EC: TAS); GO_0008543 (EC: TAS); GO_0010827 (EC: ISS, PMID: 12791994); GO_0016301 (EC: IDA, Qualifier: NOT, PMID: 12743605); GO_0019901 (EC: IPI, PMID: 12791994); GO_0019901 (EC: ISS); GO_0031625 (EC: ISS, PMID: 16794074); GO_0032092 (EC: ISS, PMID: 16794074); GO_0032869 (EC: ISS, PMID: 12791994); GO_0034976 (EC: IDA, PMID: 15775988); GO_0038095 (EC: TAS); GO_0043405 (EC: IDA, PMID: 15299019); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0045087 (EC: TAS); GO_0045599 (EC: ISS, PMID: 17576771); GO_0045717 (EC: ISS, PMID: 16794074); GO_0045892 (EC: IMP, PMID: 15775988); GO_0048011 (EC: TAS); GO_0048015 (EC: TAS); GO_0051443 (EC: ISS, PMID: 16794074); GO_0055106 (EC: ISS); GO_0070059 (EC: IDA, PMID: 15775988) PMID: 8125298; 11780052; 12477932; 12736262; 12743605; 12791994; 13679039; 14702039; 15299019; 15489334; 15775988; 15781252; 16123373; 16129579; 16147992; 16169070; 16715410; 16794074; 16887816; 16966378; 17112672; 17369260; 17576771; 17576816; 17707795; 17872950; 18029348; 18187772; 18276110; 18408768; 18436806; 18660489; 18984671; 19139803; 19180501; 19291425; 19389115; 19389818; 19505541; 19904274; 19913121; 20064487; 20139130; 20393693; 20461355; 20592469; 20606298; 20628086; 20693163; 21130836; 21203563; 21220698; 21435438; 21492415; 21572435; 21704407; 21832049; 21864376; 21896644; 21935927; 22274752; 22577090; 22912727; 22977230; 23185332; 23319603; 23349842; 23455924; 23550039; 23632994; 23695665 tribbles pseudokinase 3 Ensembl:ENSG00000101255 HGNC:16228 HPRD:09836 MIM:607898 Vega:OTTHUMG00000031627 Other designations: TRB-3|neuronal cell death inducible putative kinase|neuronal cell death-inducible putative kinase|p65-interacting inhibitor of NF-kappa-B|p65-interacting inhibitor of NF-kappaB|tribbles homolog 3 TRIB3 OGG:3000057834 Bin Zhao, Yue Liu, Oliver He CYPIVF11 WEB: http://www.ncbi.nlm.nih.gov/gene CYP4F11 cytochrome P450, family 4, subfamily F, polypeptide 11 57834 19p13.1 9606 19 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0006954 (EC: TAS, PMID:10964514); GO_0016021 (EC: IEA); GO_0020037 (EC: TAS, PMID:10964514); GO_0044281 (EC: TAS); GO_0055114 (EC: TAS, PMID:10964514); GO_0070330 (EC: IEA) PMID:8889548; 9068972; 10964514; 12477932; 14702039; 15057824; 15128046; 15489334; 18065749; 18976975; 19812349; 20379614; 20689807; 21906983; 21988832; 24138531 cytochrome P450, family 4, subfamily F, polypeptide 11 Ensembl:ENSG00000171903 HGNC:13265 HPRD:07101 MIM:611517 Vega:OTTHUMG00000182294 Other designations: cytochrome P450 4F11|cytochrome P450, subfamily IVF, polypeptide 11 CYP4F11 OGG:3000059272 Bin Zhao, Yue Liu, Oliver He ACEH WEB: http://www.ncbi.nlm.nih.gov/gene ACE2 angiotensin I converting enzyme 2 59272 UNQ868/PRO1885 Xp22 20140408 9606 X protein-coding Official from a nomenclature committee GO_0001618 (EC: IDA, PMID: 18343844); GO_0001817 (EC: IC, PMID: 15380922); GO_0001948 (EC: IPI, PMID: 18343844); GO_0002003 (EC: TAS); GO_0002005 (EC: IC, PMID: 10924499); GO_0003051 (EC: IMP, PMID: 18258853); GO_0003081 (EC: IC, PMID: 10924499); GO_0003081 (EC: IMP, PMID: 18258853); GO_0004175 (EC: IDA, PMID: 15283675); GO_0004180 (EC: IDA, PMID: 10924499); GO_0005576 (EC: IDA, PMID: 10969042); GO_0005615 (EC: IDA, PMID: 18258853); GO_0005886 (EC: TAS); GO_0008237 (EC: IDA, Qualifier: NOT, PMID: 10924499); GO_0008241 (EC: IDA, Qualifier: NOT, PMID: 10924499); GO_0008270 (EC: TAS, PMID: 10924499); GO_0009615 (EC: IDA, PMID: 18343844); GO_0009986 (EC: IDA, PMID: 18343844); GO_0016021 (EC: IEA); GO_0017046 (EC: IEA); GO_0019229 (EC: IC, PMID: 15380922); GO_0032800 (EC: IMP, PMID: 18258853); GO_0042127 (EC: TAS, PMID: 17703127); GO_0042312 (EC: IC, PMID: 15380922); GO_0044267 (EC: TAS); GO_0045121 (EC: TAS, PMID: 18279660); GO_0046718 (EC: TAS, PMID: 15165741); GO_0046813 (EC: IDA, PMID: 18343844); GO_0050727 (EC: IC, PMID: 15380922); GO_0070062 (EC: IDA, PMID: 19056867); GO_2000379 (EC: IC, PMID: 15380922) PMID: 10924499; 10969042; 11815627; 12025971; 12075344; 12459472; 12477932; 12967627; 12975309; 14647384; 14670965; 14754895; 15084671; 15141377; 15151696; 15165741; 15231706; 15233982; 15276642; 15283675; 15361769; 15380922; 15452268; 15489334; 15640278; 15671045; 15769906; 15791205; 15897467; 15937940; 15979045; 15983030; 16001071; 16006956; 16055515; 16088128; 16166094; 16166518; 16211375; 16215952; 16283142; 16315782; 16338465; 16459167; 16510163; 16574921; 16647014; 16690935; 16866021; 16912312; 16962475; 17037534; 17037543; 17037544; 17037581; 17079315; 17303661; 17473847; 17504232; 17703127; 17897017; 17906677; 18022600; 18029348; 18070603; 18164957; 18208662; 18223023; 18223027; 18223028; 18258853; 18279660; 18310257; 18343844; 18389211; 18441099; 18448527; 18490652; 18496132; 18502721; 18554741; 18560893; 18660448; 18753062; 18814896; 18926157; 18931070; 19020433; 19021774; 19034303; 19051693; 19056867; 19067252; 19077419; 19077694; 19136547; 19141296; 19164471; 19164480; 19212105; 19286756; 19286757; 19289653; 19297479; 19411314; 19461648; 19684612; 19700132; 19716087; 19864379; 19901337; 19913121; 19924243; 19926873; 19934006; 20060185; 20117248; 20117991; 20134095; 20142028; 20160196; 20204277; 20224560; 20349406; 20484496; 20541774; 20559404; 20592051; 20628086; 20660625; 20674894; 20679547; 20692300; 20703229; 20798044; 20813695; 20831027; 20854388; 21052031; 21068237; 21072744; 21115782; 21189404; 21265092; 21316680; 21346373; 21411533; 21457402; 21490025; 21670585; 21814048; 21864606; 21880865; 21946695; 21952934; 21963832; 21993363; 22025374; 22033511; 22048948; 22179088; 22291007; 22297693; 22475818; 22523556; 22629438; 22647782; 22718567; 22749485; 22750422; 23091417; 23144053; 23230080; 23328447; 23545945; 23630610; 23893738; 24014829; 24100303; 24147777; 24172901; 24191856; 24227843 angiotensin I converting enzyme 2 Ensembl:ENSG00000130234 HGNC:13557 HPRD:02274 MIM:300335 Vega:OTTHUMG00000021177 Other designations: ACE-related carboxypeptidase|angiotensin I converting enzyme (peptidyl-dipeptidase A) 2|angiotensin-converting enzyme 2|angiotensin-converting enzyme homolog|metalloprotease MPROT15|peptidyl-dipeptidase A ACE2 OGG:3000060312 Bin Zhao, Yue Liu, Oliver He AFAP AFAP-110 AFAP110 WEB: http://www.ncbi.nlm.nih.gov/gene AFAP1 actin filament associated protein 1 60312 4p16 9606 4 Official from a nomenclature committee GO_0003779 (EC: IEA); GO_0005737 (EC: IEA); GO_0005856 (EC: IEA) PMID: 7545969; 9619827; 9655255; 10666339; 11607843; 11641786; 12134071; 12477932; 14755689; 15146197; 15345747; 16344560; 16751776; 17520695; 18029348; 21150319; 23333711 actin filament associated protein 1 Ensembl:ENSG00000196526 HGNC:24017 HPRD:09747 MIM:608252 Vega:OTTHUMG00000125515 Other designations: 110 kDa actin filament-associated protein|actin filament-associated protein 1|actin filament-associated protein, 110 kDa AFAP1 OGG:3000063934 Bin Zhao, Yue Liu, Oliver He MIPU1 WEB: http://www.ncbi.nlm.nih.gov/gene ZNF667 zinc finger protein 667 63934 19q13.43 9606 19 Official from a nomenclature committee GO_0003677 (EC: IEA); GO_0005634 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0046872 (EC: IEA) PMID: 12477932; 14702039; 15489334; 16344560; 17397802; 20379614; 21139048; 21900206; 23080069; 24250222 zinc finger protein 667 Ensembl:ENSG00000198046 HGNC:28854 HPRD:08592 MIM:611024 Vega:OTTHUMG00000181941 Other designations: myocardial ischemic preconditioning upregulated 1 ortholog ZNF667 OGG:3000064081 Bin Zhao, Yue Liu, Oliver He MAWBP MAWDBP WEB: http://www.ncbi.nlm.nih.gov/gene PBLD phenazine biosynthesis-like protein domain containing 64081 10q21.3 20140408 9606 10 protein-coding Official from a nomenclature committee GO_0003674 (EC: ND); GO_0005515 (EC: IPI, PMID: 17929853); GO_0005737 (EC: IDA, PMID: 17929853); GO_0009058 (EC: IEA); GO_0010633 (EC: IMP); GO_0010719 (EC: IMP); GO_0016853 (EC: IEA); GO_0030277 (EC: IMP, PMID: 17929853); GO_0030512 (EC: IMP); GO_0050680 (EC: IMP); GO_0060392 (EC: IGI); GO_0060394 (EC: IMP); GO_0070062 (EC: IDA, PMID: 19056867) PMID: 1286669; 11355021; 12477932; 14702039; 15489334; 15806103; 16189514; 16385451; 16712791; 17929853; 19056867; 19850743; 20395239; 20548946; 23687415; 23824909 phenazine biosynthesis-like protein domain containing Ensembl:ENSG00000108187 HGNC:23301 HPRD:14366 MIM:612189 Vega:OTTHUMG00000073949 Other designations: MAWD-binding protein|phenazine biosynthesis-like domain-containing protein PBLD OGG:3000064215 Bin Zhao, Yue Liu, Oliver He DNAJL1 ERdj1 HTJ1 MTJ1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC1 DnaJ (Hsp40) homolog, subfamily C, member 1 64215 RP11-399C16.1 10p12.31 9606 10 GO_0001671 (EC: TAS, PMID:14668352); GO_0003677 (EC: IEA); GO_0003682 (EC: IEA); GO_0005515 (EC: IPI, PMID:14668352); GO_0005783 (EC: ISS); GO_0005789 (EC: IEA); GO_0006417 (EC: IEA); GO_0006457 (EC: IEA); GO_0016021 (EC: IEA); GO_0031965 (EC: IEA); GO_0032781 (EC: TAS, PMID:14668352); GO_0045861 (EC: TAS, PMID:14668352); GO_0050708 (EC: IDA, PMID:14668352); GO_0051087 (EC: IEA) PMID:10777498; 12477932; 14667819; 14668352; 14702039; 15164054; 15489334; 16271702; 16385451; 18029348; 22412018; 23535729; 23535730 DnaJ (Hsp40) homolog, subfamily C, member 1 Ensembl:ENSG00000136770 HGNC:20090 HPRD:09922 MIM:611207 Vega:OTTHUMG00000017800 Other designations: DnaJ-like protein|dnaJ homolog subfamily C member 1|dnaJ protein homolog MTJ1 DNAJC1 OGG:3000064241 Bin Zhao, Yue Liu, Oliver He GBD4 STSL WEB: http://www.ncbi.nlm.nih.gov/gene ABCG8 ATP-binding cassette, sub-family G (WHITE), member 8 64241 2p21 9606 2 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 16870176); GO_0005524 (EC: IDA, Qualifier: contributes_to, PMID: 16893193); GO_0005886 (EC: TAS); GO_0006200 (EC: IDA, PMID: 16893193); GO_0007584 (EC: IEA); GO_0007588 (EC: IGI, PMID: 14504269); GO_0010949 (EC: IMP, PMID: 11099417); GO_0015914 (EC: IEA); GO_0015918 (EC: TAS); GO_0016021 (EC: IEA); GO_0016324 (EC: IMP, PMID: 14504269); GO_0016887 (EC: IDA, Qualifier: contributes_to, PMID: 16893193); GO_0017127 (EC: IGI, Qualifier: contributes_to, PMID: 14504269); GO_0030299 (EC: IC, PMID: 12208868); GO_0033344 (EC: IGI, PMID: 14504269); GO_0042493 (EC: IEA); GO_0042632 (EC: IMP, PMID: 11099417); GO_0044281 (EC: TAS); GO_0045796 (EC: IMP, PMID: 11099417); GO_0046982 (EC: IPI, PMID: 16870176); GO_0055085 (EC: TAS) PMID: 11099417; 11452359; 11590207; 11668628; 11893785; 12111378; 12124998; 12150943; 12208867; 12208868; 12220438; 12477932; 14504269; 14703505; 15175352; 15262185; 15311998; 15331430; 15520451; 15611112; 15816807; 15930516; 16472606; 16518588; 16870176; 16893193; 16980816; 17055487; 17098593; 17102949; 17403900; 17612515; 17626266; 17632509; 17690481; 17827468; 18007013; 18457353; 18522623; 18581044; 18641716; 18660489; 18676680; 18850127; 18977479; 19005228; 19012522; 19018975; 19019257; 19056482; 19060906; 19060911; 19111681; 19170196; 19217458; 19270375; 19306529; 19343046; 19692168; 19692220; 19878569; 19936222; 20163776; 20170916; 20172523; 20210363; 20235787; 20370913; 20379614; 20403997; 20413122; 20497293; 20529992; 20581104; 20592455; 20594224; 20679960; 20686565; 20837016; 20854103; 21039838; 21062971; 21274884; 21988832; 22378727; 22548731; 22655090; 22869156; 22898925; 23179156; 23241408; 23406058; 23556150; 23707316; 23726366; 23790976; 23840693 ATP-binding cassette, sub-family G (WHITE), member 8 Ensembl:ENSG00000143921 HGNC:13887 HPRD:05679 MIM:605460 Vega:OTTHUMG00000128756 Other designations: ATP-binding cassette sub-family G member 8|ATP-binding cassette, subfamily G, member 8|sterolin 2|sterolin-2 ABCG8 OGG:3000064327 Bin Zhao, Yue Liu, Oliver He ACHP C7orf2 DIF14 PPD2 TPT ZRS WEB: http://www.ncbi.nlm.nih.gov/gene LMBR1 limb development membrane protein 1 64327 tcag7.573 7q36 9606 7 Official from a nomenclature committee GO_0016021 (EC: IEA); GO_0042733 (EC: IEA) PMID: 8533803; 9847074; 10329000; 10945466; 11076863; 11090342; 11333865; 11606546; 12032320; 12477932; 12491086; 12690205; 12837695; 12853948; 14702039; 14727139; 15489334; 15489336; 16344560; 16381901; 17152067; 17300748; 18698406; 19136951; 20068592; 20379614; 20446115; 21139048; 21906983; 22495965; 22786669 limb development membrane protein 1 Ensembl:ENSG00000105983 HGNC:13243 HPRD:05700 MIM:605522 Other designations: differentiation-related gene 14 protein|limb region 1 homolog|limb region 1 protein homolog LMBR1 OGG:3000064332 Bin Zhao, Yue Liu, Oliver He IKBZ INAP MAIL WEB: http://www.ncbi.nlm.nih.gov/gene NFKBIZ nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, zeta 64332 3p12-q12 9606 3 Official from a nomenclature committee GO_0005634 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0006954 (EC: IEA) PMID: 11278262; 11356851; 12477932; 12565889; 14702039; 15241416; 15522867; 15618216; 16344560; 16513645; 16622025; 17447895; 18362142; 18436238; 18813073; 18850010; 19595668; 19707556; 19783680; 19798075; 20211142; 20650996; 21224476; 21833088; 21988832; 22059479; 23869088; 24027435 nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, zeta Ensembl:ENSG00000144802 HGNC:29805 HPRD:09217 MIM:608004 Vega:OTTHUMG00000159194 Other designations: I-kappa-B-zeta|IL-1 inducible nuclear ankyrin-repeat protein|Ikappa B-zeta variant 3|IkappaB-zeta|NF-kappa-B inhibitor zeta|ikB-zeta|ikappaBzeta|molecule possessing ankyrin repeats induced by lipopolysaccharide NFKBIZ OGG:3000064344 Bin Zhao, Yue Liu, Oliver He HIF-3A IPAS MOP7 PASD7 bHLHe17 WEB: http://www.ncbi.nlm.nih.gov/gene HIF3A hypoxia inducible factor 3, alpha subunit 64344 19q13.32 9606 19 Official from a nomenclature committee GO_0003677 (EC: IEA); GO_0003700 (EC: IEA); GO_0003713 (EC: IDA, PMID: 11573933); GO_0003714 (EC: IDA, PMID: 11573933); GO_0004871 (EC: IEA); GO_0005654 (EC: TAS); GO_0005829 (EC: TAS); GO_0006357 (EC: IDA, PMID: 11573933); GO_0006366 (EC: IEA); GO_0046983 (EC: IEA); GO_0061418 (EC: TAS); GO_0071456 (EC: IDA, Qualifier: NOT, PMID: 11573933); GO_0071456 (EC: TAS) PMID: 8889548; 11573933; 11734856; 12119283; 12477932; 12538644; 14702039; 15319539; 15474027; 16126907; 16182248; 16344560; 16775626; 17121608; 17998805; 18029348; 19694616; 20416395; 20551700; 21069422; 21404626; 21479871; 23451260; 23485455 hypoxia inducible factor 3, alpha subunit Ensembl:ENSG00000124440 HGNC:15825 HPRD:17104 MIM:609976 Vega:OTTHUMG00000141296 Other designations: HIF3-alpha-1|PAS domain-containing protein 7|basic-helix-loop-helix-PAS protein MOP7|class E basic helix-loop-helix protein 17|hypoxia-inducible factor 3-alpha|inhibitory PAS domain protein|member of PAS protein 7 HIF3A OGG:3000064782 Bin Zhao, Yue Liu, Oliver He ISG20L1 pp12744 WEB: http://www.ncbi.nlm.nih.gov/gene AEN apoptosis enhancing nuclease 64782 SBBI58 15q26.1 9606 15 Official from a nomenclature committee GO_0003676 (EC: IEA); GO_0004527 (EC: IDA, PMID: 16171785); GO_0005634 (EC: IDA); GO_0005654 (EC: IDA, PMID: 16171785); GO_0005730 (EC: IDA); GO_0010212 (EC: IDA, PMID: 16171785); GO_0031965 (EC: IDA); GO_0042771 (EC: IDA, PMID: 18264133); GO_0090305 (EC: IDA, PMID: 16171785) PMID: 12477932; 14702039; 16171785; 17207965; 18029348; 18264133; 18816836; 20429933; 21906983 apoptosis enhancing nuclease Ensembl:ENSG00000181026 HGNC:25722 HPRD:08573 MIM:610177 Vega:OTTHUMG00000148681 Other designations: apoptosis-enhancing nuclease|interferon stimulated exonuclease gene 20kDa-like 1|interferon-stimulated 20 kDa exonuclease-like 1 AEN OGG:3000064787 Bin Zhao, Yue Liu, Oliver He EPS8R2 WEB: http://www.ncbi.nlm.nih.gov/gene EPS8L2 EPS8-like 2 64787 PP13181 11p15.5 9606 11 Official from a nomenclature committee GO_0003779 (EC: IDA, PMID: 14565974); GO_0005089 (EC: IDA, Qualifier: contributes_to, PMID: 14565974); GO_0005737 (EC: IDA); GO_0005886 (EC: IDA); GO_0007266 (EC: IDA, PMID: 14565974); GO_0030676 (EC: IDA, Qualifier: contributes_to, PMID: 14565974); GO_0032314 (EC: IDA, PMID: 14565974); GO_0032319 (EC: IDA, PMID: 14565974); GO_0032587 (EC: IDA, PMID: 14565974); GO_0035023 (EC: IDA, PMID: 14565974); GO_0043234 (EC: IDA, PMID: 14565974); GO_0070062 (EC: IDA, PMID: 19056867); GO_1900029 (EC: IGI, PMID: 14565974) PMID: 8125298; 12477932; 12620401; 14565974; 14702039; 15489334; 15498874; 16083285; 18029348; 19056867; 21832049; 21900206; 21988832 EPS8-like 2 Ensembl:ENSG00000177106 HGNC:21296 HPRD:10940 MIM:614988 Vega:OTTHUMG00000165165 Other designations: EPS8-like protein 2|EPS8-related protein 2|epidermal growth factor receptor kinase substrate 8-like protein 2|epidermal growth factor receptor pathway substrate 8-related protein 2 EPS8L2 OGG:3000064816 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CYP3A43 cytochrome P450, family 3, subfamily A, polypeptide 43 64816 7q21.1 9606 7 GO_0004497 (EC: ISS); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA) PMID:9890157; 11137287; 11160876; 11243885; 11266076; 11726664; 12477932; 12853948; 14695544; 14759258; 15128046; 15548719; 15894682; 16314882; 16848237; 18566991; 19343046; 19789190; 20529763; 20715157; 21081028; 21533175 cytochrome P450, family 3, subfamily A, polypeptide 43 Other designations: cytochrome P450 3A43|cytochrome P450, subfamily IIIA, polypeptide 43 CYP3A43 OGG:3000064838 Bin Zhao, Yue Liu, Oliver He FRCP1 WEB: http://www.ncbi.nlm.nih.gov/gene FNDC4 fibronectin type III domain containing 4 64838 UNQ6389/PRO21134 2p23.3 9606 2 Official from a nomenclature committee GO_0005783 (EC: ISS); GO_0005886 (EC: ISS); GO_0016021 (EC: IEA) PMID: 12384288; 12477932; 12975309; 14702039; 15489334; 15815621; 19913121; 20383146; 20628086; 20705733; 21988832; 22267201; 23022100; 23505323 fibronectin type III domain containing 4 Ensembl:ENSG00000115226 HGNC:20239 HPRD:09965 MIM:611905 Vega:OTTHUMG00000097787 Other designations: fibronectin type III domain-containing protein 4|fibronectin type III repeat-containing protein 1 FNDC4 OGG:3000065992 Bin Zhao, Yue Liu, Oliver He C20orf116 UFBP1 dJ1187M17.3 WEB: http://www.ncbi.nlm.nih.gov/gene DDRGK1 DDRGK domain containing 1 65992 20p13 9606 20 Official from a nomenclature committee GO_0005515 (EC: IPI); GO_0005783 (EC: IDA) PMID: 11780052; 12477932; 15489334; 17207965; 17353931; 20018847; 20036718; 20228063; 20637204; 21139048; 21494687; 21659334; 21832049; 21890473; 22939629; 23675531; 24250222 DDRGK domain containing 1 Ensembl:ENSG00000198171 HGNC:16110 HPRD:12741 Vega:OTTHUMG00000031732 Other designations: DDRGK domain-containing protein 1|Dashurin|UFM1-binding protein 1 containing a PCI domain DDRGK1 OGG:3000066002 Bin Zhao, Yue Liu, Oliver He F22329_1 WEB: http://www.ncbi.nlm.nih.gov/gene CYP4F12 cytochrome P450, family 4, subfamily F, polypeptide 12 66002 UNQ568/PRO1129 19p13.1 9606 19 GO_0000038 (EC: ISS); GO_0001676 (EC: ISS); GO_0003091 (EC: ISS); GO_0003095 (EC: ISS); GO_0005506 (EC: IEA); GO_0005737 (EC: ISS); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0008392 (EC: ISS); GO_0016021 (EC: IEA); GO_0016324 (EC: ISS); GO_0017144 (EC: ISS); GO_0018685 (EC: ISS); GO_0019369 (EC: ISS); GO_0019373 (EC: ISS); GO_0020037 (EC: IEA); GO_0030195 (EC: ISS); GO_0036101 (EC: ISS); GO_0042360 (EC: ISS); GO_0042371 (EC: ISS); GO_0043231 (EC: ISS); GO_0044281 (EC: TAS); GO_0047057 (EC: ISS); GO_0050051 (EC: ISS); GO_0055078 (EC: ISS); GO_0055114 (EC: ISS); GO_0070330 (EC: IEA) PMID:1116264; 9068972; 11162607; 11162645; 12477932; 12975309; 14702039; 15128046; 15548388; 16112640; 16303743; 16344560; 18065749; 21906983; 21988832 cytochrome P450, family 4, subfamily F, polypeptide 12 Ensembl:ENSG00000186204 HGNC:18857 HPRD:07102 MIM:611485 Vega:OTTHUMG00000164477 Other designations: CYPIVF12|cytochrome P450 4F12|cytochrome P450, subfamily IVF, polypeptide 12 CYP4F12 OGG:3000079071 Bin Zhao, Yue Liu, Oliver He FACE FAE LCE WEB: http://www.ncbi.nlm.nih.gov/gene ELOVL6 ELOVL fatty acid elongase 6 79071 4q25 9606 4 Official from a nomenclature committee GO_0005515 (EC: IPI); GO_0005783 (EC: IDA); GO_0005789 (EC: TAS); GO_0016747 (EC: IEA); GO_0019367 (EC: IDA); GO_0019432 (EC: TAS); GO_0030176 (EC: IEA); GO_0035338 (EC: TAS); GO_0042759 (EC: IDA); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS) PMID: 8889549; 8944226; 11567032; 12477932; 14702039; 15342556; 15489334; 15815621; 16344560; 18660489; 19259639; 20332099; 20732626; 20937905; 21544602; 21701577; 21906983; 22753171; 23251661 ELOVL fatty acid elongase 6 Ensembl:ENSG00000170522 HGNC:15829 HPRD:13269 MIM:611546 Vega:OTTHUMG00000132547 Other designations: 3-keto acyl-CoA synthase ELOVL6|ELOVL FA elongase 6|ELOVL family member 6, elongation of long chain fatty acids (FEN1/Elo2, SUR4/Elo3-like, yeast)|elongation of very long chain fatty acids protein 6|fatty acid elongase 2|fatty acyl-CoA elongase|hELO2|long-chain fatty-acyl elongase|very-long-chain 3-oxoacyl-CoA synthase 6 ELOVL6 OGG:3000079094 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CHAC1 ChaC, cation transport regulator homolog 1 (E. coli) 79094 15q15.1 9606 15 Official from a nomenclature committee GO_0005112 (EC: ISS); GO_0005515 (EC: IPI, PMID: 16189514); GO_0005794 (EC: IEA); GO_0005802 (EC: ISS); GO_0005829 (EC: IDA, PMID: 19109178); GO_0006986 (EC: IEA); GO_0007219 (EC: IEA); GO_0010955 (EC: IMP); GO_0022008 (EC: ISS); GO_0045746 (EC: IMP); GO_0070059 (EC: IMP, PMID: 19109178) PMID: 8889548; 12477932; 15489334; 16189514; 16341674; 19109178; 21890473; 21906983; 22108517; 22589738; 23000965; 23070364; 23342279 ChaC, cation transport regulator homolog 1 (E. coli) Other designations: ChaC, cation transport regulator-like 1|blocks Notch protein|botch|cation transport regulator-like protein 1|gamma-GCT acting on glutathione homolog 1 CHAC1 OGG:3000079174 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CRELD2 cysteine-rich with EGF-like domains 2 79174 CITF22-1A6.1 22q13.33 9606 22 Official from a nomenclature committee GO_0005509 (EC: IEA); GO_0005515 (EC: IPI); GO_0005615 (EC: IEA); GO_0005783 (EC: IEA); GO_0005794 (EC: IEA) PMID: 8125298; 12137942; 12477932; 12975309; 14702039; 15340161; 15489334; 16238698; 16919896; 21900206; 21963094; 21988832; 23455924 cysteine-rich with EGF-like domains 2 Other designations: cysteine-rich with EGF-like domain protein 2 CRELD2 OGG:3000079789 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CLMN calmin (calponin-like, transmembrane) 79789 14q32.13 20140408 9606 14 protein-coding Official from a nomenclature committee GO_0003779 (EC: IEA); GO_0005737 (EC: IEA); GO_0008285 (EC: IEA); GO_0016021 (EC: IEA); GO_0031175 (EC: IEA) PMID: 9455484; 10574461; 11386753; 12477932; 12508121; 14702039; 16712791; 20195266; 20339536; 22747683; 23080069; 23535033 calmin (calponin-like, transmembrane) Other designations: calmin|calponin like transmembrane domain protein|calponin-like transmembrane domain protein CLMN OGG:3000079792 Bin Zhao, Yue Liu, Oliver He DF5L DFNA5L GSDMDC1 WEB: http://www.ncbi.nlm.nih.gov/gene GSDMD gasdermin D 79792 FKSG10 8q24.3 20140408 9606 8 protein-coding Official from a nomenclature committee GO_0031668 (EC: IEA) PMID: 12477932; 14702039; 15289881; 15489334; 15592455; 16421571; 17350798; 19051310; 21139048; 21890473; 21906983; 23000965 gasdermin D Ensembl:ENSG00000104518 HGNC:25697 HPRD:11014 Vega:OTTHUMG00000165132 Other designations: gasdermin domain containing 1|gasdermin domain-containing protein 1|gasdermin-D GSDMD OGG:3000079799 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene UGT2A3 UDP glucuronosyltransferase 2 family, polypeptide A3 79799 UNQ2559/PRO6239 4q13.2 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0015020 (EC: IDA, PMID: 19858781); GO_0016021 (EC: IEA); GO_0052695 (EC: IDA, PMID: 19858781) PMID: 8125298; 12477932; 12975309; 15342556; 18523138; 19858781; 20379614; 20819778 UDP glucuronosyltransferase 2 family, polypeptide A3 Other designations: UDP-glucuronosyltransferase 2A3|UDPGT 2A3 UGT2A3 OGG:3000079882 Bin Zhao, Yue Liu, Oliver He MSUT-2 NY-REN-37 SUT2 UKp68 WEB: http://www.ncbi.nlm.nih.gov/gene ZC3H14 zinc finger CCCH-type containing 14 79882 14q31.3 9606 14 Official from a nomenclature committee GO_0005515 (EC: IPI, PMID: 19273536); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: IDA, PMID: 19303045); GO_0005737 (EC: IEA); GO_0016607 (EC: IEA); GO_0044822 (EC: IDA); GO_0046872 (EC: IEA) PMID: 10508479; 12477932; 14702039; 16159877; 16189514; 16344560; 17630287; 18029348; 19273536; 19303045; 19471022; 20658987; 21139048; 21355046; 21734151; 21890473; 21906983; 22505724; 22586326; 22939629; 23000965; 24163370; 24250222; 24457600 zinc finger CCCH-type containing 14 Ensembl:ENSG00000100722 HGNC:20509 HPRD:13348 MIM:613279 Vega:OTTHUMG00000170803 Other designations: mammalian suppressor of tau pathology-2|nuclear protein UKp68|renal carcinoma antigen NY-REN-37|zinc finger CCCH domain-containing protein 14 ZC3H14 OGG:3000079962 Bin Zhao, Yue Liu, Oliver He wus WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC22 DnaJ (Hsp40) homolog, subfamily C, member 22 79962 12q13.12 9606 12 GO_0016021 (EC: IEA) PMID:12477932; 14702039; 17558392; 19460752; 21906983 DnaJ (Hsp40) homolog, subfamily C, member 22 Ensembl:ENSG00000178401 HGNC:25802 HPRD:08580 Vega:OTTHUMG00000169487 Other designations: dnaJ homolog subfamily C member 22|wurst homolog DNAJC22 OGG:3000079982 Bin Zhao, Yue Liu, Oliver He EGNR9427 PRO34683 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB14 DnaJ (Hsp40) homolog, subfamily B, member 14 79982 UNQ9427/PRO34683 4q23 9606 4 GO_0016021 (EC: IEA) PMID:12477932; 12975309; 14702039; 15489334; 15815621; 16344560; 21139048; 21832049; 23018488 DnaJ (Hsp40) homolog, subfamily B, member 14 Ensembl:ENSG00000164031 HGNC:25881 HPRD:07013 Vega:OTTHUMG00000131049 Other designations: dnaJ homolog subfamily B member 14 DNAJB14 OGG:3000080063 Bin Zhao, Yue Liu, Oliver He MCAF2 WEB: http://www.ncbi.nlm.nih.gov/gene ATF7IP2 activating transcription factor 7 interacting protein 2 80063 16p13.13 9606 16 GO_0005634 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA) PMID:8125298; 12477932; 14702039; 15489334; 15691849; 18029348; 20195266 activating transcription factor 7 interacting protein 2 Ensembl:ENSG00000166669 HGNC:20397 HPRD:16517 MIM:613645 Vega:OTTHUMG00000129749 Other designations: ATF7-interacting protein 2|MBD1-containing chromatin associated factor 2|MBD1-containing chromatin-associated factor 2|activating transcription factor 7-interacting protein 2 ATF7IP2 OGG:3000080235 Bin Zhao, Yue Liu, Oliver He GPI-MT-IV PIG-Z SMP3 WEB: http://www.ncbi.nlm.nih.gov/gene PIGZ phosphatidylinositol glycan anchor biosynthesis, class Z 80235 3q29 9606 3 Official from a nomenclature committee GO_0000026 (EC: IMP, PMID: 15208306); GO_0000030 (EC: IGI, PMID: 15208306); GO_0005783 (EC: IDA, PMID: 15208306); GO_0005789 (EC: IEA); GO_0006506 (EC: IEA); GO_0006506 (EC: IGI, PMID: 15208306); GO_0006506 (EC: IMP, PMID: 15208306); GO_0016021 (EC: IEA); GO_0097502 (EC: IGI, PMID: 15208306); GO_0097502 (EC: IMP, PMID: 15208306) PMID: 11356840; 12200473; 12477932; 12655644; 14702039; 15208306; 15489334; 16344560 phosphatidylinositol glycan anchor biosynthesis, class Z Ensembl:ENSG00000119227 HGNC:30596 HPRD:18076 MIM:611671 Vega:OTTHUMG00000155522 Other designations: GPI mannosyltransferase 4|GPI mannosyltransferase IV|SMP3 mannosyltransferase|dol-P-Man dependent GPI mannosyltransferase|phosphatidylinositol glycan, class Z|phosphatidylinositol-glycan biosynthesis class Z protein PIGZ OGG:3000080255 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene SLC35F5 solute carrier family 35, member F5 80255 UNQ2545/PRO6097 2q14.1 9606 2 Official from a nomenclature committee GO_0006810 (EC: IEA); GO_0016021 (EC: IEA) PMID: 12477932; 12975309; 21139048; 21963094 solute carrier family 35, member F5 Other designations: HCV NS5A-transactivated protein 3|hepatitis C virus NS5A-transactivated protein 3|solute carrier family 35 member F5 SLC35F5 OGG:3000080267 Bin Zhao, Yue Liu, Oliver He C1orf22 WEB: http://www.ncbi.nlm.nih.gov/gene EDEM3 ER degradation enhancer, mannosidase alpha-like 3 80267 1q25 9606 1 GO_0004569 (EC: IEA); GO_0004571 (EC: IEA); GO_0005509 (EC: IEA); GO_0005788 (EC: IEA); GO_0005789 (EC: TAS); GO_0006457 (EC: TAS); GO_0006516 (EC: IEA); GO_0006986 (EC: IEA); GO_0018279 (EC: TAS); GO_0043161 (EC: IEA); GO_0043687 (EC: TAS); GO_0044267 (EC: TAS) PMID:8125298; 11318611; 12477932; 14702039; 15537790; 15579471; 16344560; 16431915; 16710414; 17499246; 18303019; 20360068; 21890473; 22190034; 22268729; 23251661 ER degradation enhancer, mannosidase alpha-like 3 Ensembl:ENSG00000116406 HGNC:16787 HPRD:10724 MIM:610214 Vega:OTTHUMG00000035387 Other designations: ER degradation-enhancing -mannosidase-like protein 3|ER degradation-enhancing alpha-mannosidase-like 3|ER degradation-enhancing alpha-mannosidase-like protein 3|alpha-1,2-mannosidase EDEM3 EDEM3 OGG:3000080331 Bin Zhao, Yue Liu, Oliver He CLN4 CLN4B CSP DNAJC5A NCL WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC5 DnaJ (Hsp40) homolog, subfamily C, member 5 80331 20q13.33 9606 20 GO_0001948 (EC: IEA); GO_0005739 (EC: IDA); GO_0005765 (EC: IDA, PMID:17897319); GO_0005886 (EC: IDA); GO_0005886 (EC: TAS); GO_0007268 (EC: TAS); GO_0007269 (EC: TAS); GO_0008021 (EC: IEA); GO_0008219 (EC: IEA); GO_0042470 (EC: IEA); GO_0043008 (EC: IEA); GO_0043524 (EC: IEA); GO_0061202 (EC: TAS) PMID:2663281; 3284607; 8764987; 10194413; 11214971; 11604405; 11780052; 12039948; 12477932; 14570907; 14702039; 14997482; 15489334; 15610015; 15972823; 16469739; 16751776; 17897319; 18029348; 18314541; 18596047; 19098309; 20301601; 20453918; 21139048; 21674799; 21820099; 21890473; 21906983; 21963094; 21987572; 22073189; 22235333; 22902780; 22939629; 22978711; 23000965; 23535732; 24250222 DnaJ (Hsp40) homolog, subfamily C, member 5 Ensembl:ENSG00000101152 HGNC:16235 HPRD:08539 MIM:611203 Vega:OTTHUMG00000033007 Other designations: cysteine string protein alpha|dnaJ homolog subfamily C member 5 DNAJC5 OGG:3000081575 Bin Zhao, Yue Liu, Oliver He VERGE WEB: http://www.ncbi.nlm.nih.gov/gene APOLD1 apolipoprotein L domain containing 1 81575 12p13.1 9606 12 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0001666 (EC: IEA); GO_0005576 (EC: IEA); GO_0005886 (EC: IEA); GO_0006869 (EC: IEA); GO_0008289 (EC: IEA); GO_0016021 (EC: IEA); GO_0030154 (EC: IEA); GO_0042118 (EC: IEA); GO_0042157 (EC: IEA); GO_0045601 (EC: IEA) PMID: 8125298; 11076863; 11230166; 12477932; 14702039; 15102925; 15489334; 15489336; 16344560; 16381901; 19738201; 19913121; 20628086; 24250222 apolipoprotein L domain containing 1 Ensembl:ENSG00000178878 HGNC:25268 HPRD:13153 MIM:612456 Vega:OTTHUMG00000153561 Other designations: apolipoprotein L domain-containing protein 1|vascular early response gene protein APOLD1 OGG:3000083452 Bin Zhao, Yue Liu, Oliver He SMC2 WEB: http://www.ncbi.nlm.nih.gov/gene RAB33B RAB33B, member RAS oncogene family 83452 4q28 9606 4 Official from a nomenclature committee GO_0000139 (EC: IEA); GO_0005525 (EC: IEA); GO_0005794 (EC: IDA); GO_0005796 (EC: IDA, PMID: 18448665); GO_0006914 (EC: IEA); GO_0007264 (EC: IEA); GO_0015031 (EC: IEA); GO_2000156 (EC: IMP); GO_2000785 (EC: ISS) PMID: 9512502; 11230166; 11256614; 11718716; 12477932; 15489334; 15761153; 15815621; 16923123; 18448665; 21139048; 22178446; 22652534; 23091056; 24250222 RAB33B, member RAS oncogene family Ensembl:ENSG00000172007 HGNC:16075 HPRD:05808 MIM:605950 Vega:OTTHUMG00000133384 Other designations: ras-related protein Rab-33B RAB33B OGG:3000083695 Bin Zhao, Yue Liu, Oliver He C12orf32 RHINO WEB: http://www.ncbi.nlm.nih.gov/gene RHNO1 RAD9-HUS1-RAD1 interacting nuclear orphan 1 83695 HKMT1188 12p13.33 20140408 9606 12 protein-coding Official from a nomenclature committee GO_0000077 (EC: IMP); GO_0000725 (EC: IMP); GO_0005515 (EC: IPI); GO_0005634 (EC: IDA); GO_0005694 (EC: IDA); GO_0034644 (EC: IDA); GO_0070318 (EC: IMP); GO_0071479 (EC: IDA) PMID: 11414747; 12477932; 14702039; 15221005; 15489334; 16341674; 16344560; 17525332; 19322201; 20811708; 21145461; 21659603 RAD9-HUS1-RAD1 interacting nuclear orphan 1 Ensembl:ENSG00000171792 HGNC:28206 HPRD:17487 MIM:614085 Vega:OTTHUMG00000158557 Other designations: RAD9, HUS1, RAD1-interacting nuclear orphan protein 1|Rad9, Rad1, Hus1 interacting nuclear orphan|rAD9, RAD1, HUS1-interacting nuclear orphan protein RHNO1 OGG:3000083729 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene INHBE inhibin, beta E 83729 12q13.3 9606 12 Official from a nomenclature committee GO_0005179 (EC: IEA); GO_0005576 (EC: IEA); GO_0008083 (EC: IEA); GO_0040007 (EC: IEA) PMID: 12242034; 12477932; 14702039; 15489334; 15717329; 16303743; 16426570; 18413775; 19322201; 20012305; 20033758; 20734064; 21092084; 23263486 inhibin, beta E Other designations: activin beta E|activin beta-E chain|inhibin beta E chain INHBE OGG:3000083854 Bin Zhao, Yue Liu, Oliver He AGF ARP5 WEB: http://www.ncbi.nlm.nih.gov/gene ANGPTL6 angiopoietin-like 6 83854 UNQ152/PRO178 19p13.2 9606 19 GO_0001525 (EC: IEA); GO_0005576 (EC: IEA); GO_0030141 (EC: IEA); GO_0030154 (EC: IEA) PMID:12477932; 12871997; 12975309; 14764539; 15231747; 16335952; 16806062; 18464913; 19447061; 20673930; 21460784; 22406517; 23070965; 23400010; 24250222 angiopoietin-like 6 Ensembl:ENSG00000130812 HGNC:23140 HPRD:12453 MIM:609336 Vega:OTTHUMG00000180395 Other designations: angiopoietin-like protein 6|angiopoietin-related growth factor|angiopoietin-related protein 5|angiopoietin-related protein 6 ANGPTL6 OGG:3000083939 Bin Zhao, Yue Liu, Oliver He EIF-2A MST089 MSTP004 MSTP089 WEB: http://www.ncbi.nlm.nih.gov/gene EIF2A eukaryotic translation initiation factor 2A, 65kDa 83939 CDA02 3q25.1 9606 3 GO_0000049 (EC: IMP, PMID:12133843); GO_0003743 (EC: IMP, PMID:12133843); GO_0005515 (EC: IPI, PMID:18816594); GO_0005615 (EC: IDA); GO_0005737 (EC: IDA, PMID:12133843); GO_0005850 (EC: IDA, PMID:12133843); GO_0006417 (EC: IMP, PMID:12133843); GO_0006468 (EC: IEA); GO_0009967 (EC: IEA); GO_0032933 (EC: IEA); GO_0042255 (EC: IMP, PMID:12133843); GO_0043022 (EC: IMP, PMID:12133843); GO_0072562 (EC: IDA) PMID:1620067; 12133843; 12370288; 12477932; 12687390; 14702039; 15341733; 15345721; 15475356; 15718232; 15781241; 15961545; 16373505; 16631606; 16717090; 16870703; 16928686; 17274640; 17407708; 17553788; 17715234; 17894550; 18063576; 18195013; 18274552; 18287093; 18337511; 18794359; 18816594; 19131336; 19190324; 19223463; 19229320; 19586904; 19605483; 19744687; 19913121; 20376341; 20434207; 20519500; 20628086; 20706999; 21085474; 21090173; 21139048; 21203563; 21622569; 21730287; 21832049; 21906983; 21963094; 22355666; 22505724; 22863883; 22915583; 22939629; 22948139; 23000965; 23046979; 23471998; 23690448 eukaryotic translation initiation factor 2A, 65kDa Ensembl:ENSG00000144895 HGNC:3254 HPRD:11739 MIM:609234 Vega:OTTHUMG00000159775 Other designations: 65 kDa eukaryotic translation initiation factor 2A|eukaryotic translation initiation factor 2A EIF2A OGG:3000084085 Bin Zhao, Yue Liu, Oliver He Fbx30 WEB: http://www.ncbi.nlm.nih.gov/gene FBXO30 F-box protein 30 84085 RP11-545I5.4 6q24 9606 6 Official from a nomenclature committee GO_0004842 (EC: IEA); GO_0008270 (EC: IEA) PMID: 12477932; 12536519; 12903040; 14574404; 14702039; 15489334; 15520277; 15761153; 18247557; 19322201; 20360068; 20936779; 21139048; 21145461 F-box protein 30 HGNC:15600 HPRD:10953 MIM:609101 Other designations: F-box domain protein|F-box only protein 30|F-box only protein, helicase, 18 FBXO30 OGG:3000084263 Bin Zhao, Yue Liu, Oliver He C9orf99 SDR13C1 WEB: http://www.ncbi.nlm.nih.gov/gene HSDL2 hydroxysteroid dehydrogenase like 2 84263 RP11-32M23.1 9q32 9606 9 Official from a nomenclature committee GO_0003674 (EC: ND); GO_0005739 (EC: IEA); GO_0005777 (EC: IDA, PMID: 19703561); GO_0008150 (EC: ND); GO_0016491 (EC: IEA); GO_0032934 (EC: IEA) PMID: 8125298; 12477932; 12834046; 14702039; 16344560; 16501878; 18369455; 19027726; 19703561; 20583170; 20877624; 21139048; 21890473; 22002062; 22082156; 22268729; 23455922; 23798571; 24244333; 24250222 hydroxysteroid dehydrogenase like 2 Ensembl:ENSG00000119471 HGNC:18572 HPRD:13679 Vega:OTTHUMG00000020504 Other designations: hydroxysteroid dehydrogenase-like protein 2|short chain dehydrogenase/reductase family 13C, member 1 HSDL2 OGG:3000084277 Bin Zhao, Yue Liu, Oliver He WBSCR18 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC30 DnaJ (Hsp40) homolog, subfamily C, member 30 84277 7q11.23 9606 7 GO_0005739 (EC: IEA) PMID:12073013; 12477932; 12853948; 14702039; 15231747; 15489334; 17207965; 20877624 DnaJ (Hsp40) homolog, subfamily C, member 30 Ensembl:ENSG00000176410 HGNC:16410 HPRD:10303 Vega:OTTHUMG00000023290 Other designations: Williams Beuren syndrome chromosome region 18|dnaJ homolog subfamily C member 30|williams-Beuren syndrome chromosomal region 18 protein DNAJC30 OGG:3000084285 Bin Zhao, Yue Liu, Oliver He haponin WEB: http://www.ncbi.nlm.nih.gov/gene EIF1AD eukaryotic translation initiation factor 1A domain containing 84285 11q13.1 9606 11 GO_0003743 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0043231 (EC: IDA); GO_0045111 (EC: IDA) PMID:12477932; 14702039; 15342556; 16189514; 16344560; 16751776; 17207965; 18173130; 19322201; 21139048; 21890473; 22095125; 23000965 eukaryotic translation initiation factor 1A domain containing Ensembl:ENSG00000175376 HGNC:28147 HPRD:14411 Vega:OTTHUMG00000166671 Other designations: eukaryotic translation initiation factor 1A domain-containing protein|probable RNA-binding protein EIF1AD EIF1AD OGG:3000084320 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene ACBD6 acyl-CoA binding domain containing 6 84320 1q25.1 9606 1 Official from a nomenclature committee GO_0000062 (EC: IEA); GO_0005737 (EC: IEA); GO_0008289 (EC: IEA) PMID: 8889549; 12477932; 15489334; 16710414; 18029348; 18268358; 19471022; 20098747; 20379614; 21139048; 21832049; 21890473; 21963094; 22053931 acyl-CoA binding domain containing 6 Other designations: acyl-CoA-binding domain-containing protein 6|acyl-Coenzyme A binding domain containing 6 ACBD6 OGG:3000084649 Bin Zhao, Yue Liu, Oliver He ARAT GS1999FULL WEB: http://www.ncbi.nlm.nih.gov/gene DGAT2 diacylglycerol O-acyltransferase 2 84649 HMFN1045 11q13.5 9606 11 Official from a nomenclature committee GO_0003846 (EC: IEA); GO_0004144 (EC: IDA, PMID: 11481335); GO_0005739 (EC: ISS, Qualifier: colocalizes_with); GO_0005783 (EC: IDA, PMID: 14521909); GO_0005789 (EC: TAS); GO_0005811 (EC: ISS, Qualifier: colocalizes_with); GO_0006071 (EC: IEA); GO_0006644 (EC: TAS); GO_0016021 (EC: IDA, PMID: 11481335); GO_0019432 (EC: IDA, PMID: 11481335); GO_0019432 (EC: IEA); GO_0019432 (EC: TAS); GO_0019915 (EC: ISS); GO_0030176 (EC: IC, PMID: 14521909); GO_0030176 (EC: ISS); GO_0034383 (EC: ISS); GO_0035336 (EC: IDA, PMID: 11481335); GO_0035356 (EC: ISS); GO_0036155 (EC: TAS); GO_0042632 (EC: ISS); GO_0042803 (EC: ISS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS); GO_0046339 (EC: IDA, PMID: 11481335); GO_0046474 (EC: TAS); GO_0048471 (EC: ISS); GO_0050252 (EC: IEA); GO_0055089 (EC: ISS); GO_0060613 (EC: ISS); GO_0071400 (EC: ISS); GO_0097006 (EC: ISS) PMID: 8944226; 11481335; 12477932; 12975309; 14521909; 14702039; 14970677; 15221005; 15258194; 15489334; 16870193; 17207965; 17477860; 17504763; 17940217; 18757836; 18980578; 19049983; 19913121; 20379614; 20628086; 20679960; 20739640; 21933415; 22315393; 22748069; 23489367 diacylglycerol O-acyltransferase 2 Ensembl:ENSG00000062282 HGNC:16940 HPRD:07376 MIM:606983 Vega:OTTHUMG00000165338 Other designations: acyl-CoA retinol O-fatty-acyltransferase|diacylglycerol O-acyltransferase homolog 2|diacylglycerol O-acyltransferase-like protein 2|diglyceride acyltransferase 2|retinol O-fatty-acyltransferase DGAT2 OGG:3000084675 Bin Zhao, Yue Liu, Oliver He MURF-2 RNF29 muRF2 WEB: http://www.ncbi.nlm.nih.gov/gene TRIM55 tripartite motif containing 55 84675 8q13.1 20140408 9606 8 protein-coding Official from a nomenclature committee GO_0004871 (EC: NAS, PMID: 11243782); GO_0005634 (EC: IEA); GO_0005737 (EC: IEA); GO_0005874 (EC: NAS, PMID: 11243782); GO_0007165 (EC: NAS, PMID: 11243782); GO_0008270 (EC: IEA); GO_0042802 (EC: IPI) PMID: 11243782; 11927605; 12414993; 12477932; 14702039; 15489334; 15782160; 15802564; 15967462; 18187620; 18854154; 19549727; 20379614; 22493164; 22626734; 22666496; 22939629 tripartite motif containing 55 Ensembl:ENSG00000147573 HGNC:14215 HPRD:05927 MIM:606469 Vega:OTTHUMG00000164473 Other designations: muscle specific ring finger 2|muscle-specific RING finger protein 2|ring finger protein 29|tripartite motif-containing 55|tripartite motif-containing protein 55 TRIM55 OGG:3000084696 Bin Zhao, Yue Liu, Oliver He LABH1 WEB: http://www.ncbi.nlm.nih.gov/gene ABHD1 abhydrolase domain containing 1 84696 2p23.3 9606 2 Official from a nomenclature committee GO_0003674 (EC: ND); GO_0008150 (EC: ND); GO_0016021 (EC: NAS, PMID: 12735795); GO_0016787 (EC: IEA) PMID: 11922611; 12477932; 12735795; 14702039; 15489334; 15815621 abhydrolase domain containing 1 Ensembl:ENSG00000143994 HGNC:17553 HPRD:07468 MIM:612195 Vega:OTTHUMG00000097072 Other designations: abhydrolase domain-containing protein 1|lung alpha/beta hydrolase 1 ABHD1 OGG:3000085406 Bin Zhao, Yue Liu, Oliver He DNAJ DRIP78 HDJ3 LIP6 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC14 DnaJ (Hsp40) homolog, subfamily C, member 14 85406 hCG_2016179 12q13.2 9606 12 GO_0005789 (EC: IEA); GO_0015031 (EC: IEA); GO_0016021 (EC: IEA) PMID:11181995; 11331877; 11984006; 12446598; 12477932; 12768437; 14702039; 14993367; 15489334; 16344560; 18029348; 19322201; 21249176; 22815758; 22915803 DnaJ (Hsp40) homolog, subfamily C, member 14 Ensembl:ENSG00000135392 HGNC:24581 HPRD:12082 MIM:606092 Vega:OTTHUMG00000170427 Other designations: LYST-interacting protein LIP6|dnaJ homolog subfamily C member 14|dnaJ protein homolog 3|dopamine receptor interacting protein|dopamine receptor-interacting protein of 78 kDa|hDj-3|human DnaJ protein 3 DNAJC14 OGG:3000085479 Bin Zhao, Yue Liu, Oliver He CSP-beta WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC5B DnaJ (Hsp40) homolog, subfamily C, member 5 beta 85479 8q13.1 9606 8 GO_0016020 (EC: IEA) PMID:12477932; 15489334; 17034881; 17207965; 22174851; 22666496 DnaJ (Hsp40) homolog, subfamily C, member 5 beta Ensembl:ENSG00000147570 HGNC:24138 HPRD:07474 MIM:613945 Vega:OTTHUMG00000164470 Other designations: beta cysteine string protein|beta-CSP|cysteine string protein beta|dnaJ homolog subfamily C member 5B|dnaJ homolog subfamily C member X DNAJC5B OGG:3000089978 Bin Zhao, Yue Liu, Oliver He ATPBD4 WEB: http://www.ncbi.nlm.nih.gov/gene DPH6 diphthamine biosynthesis 6 89978 15q14 9606 15 Official from a nomenclature committee GO_0005524 (EC: IEA); GO_0017178 (EC: TAS); GO_0017183 (EC: IEA); GO_0017183 (EC: TAS) PMID: 12477932; 14702039; 15489334; 16344560; 19913121; 20379614; 20628086; 20732626; 21890473; 21906983; 21963094; 22505724; 23169644; 23468660; 23776197; 24045676; 24250222 diphthamine biosynthesis 6 Ensembl:ENSG00000134146 HGNC:30543 HPRD:14443 Vega:OTTHUMG00000129759 Other designations: ATP binding domain 4|ATP-binding domain-containing protein 4|DPH6 homolog|diphthamide synthase|diphthamide synthetase|diphthine--ammonia ligase|protein DPH6 homolog DPH6 OGG:3000090637 Bin Zhao, Yue Liu, Oliver He AIRAP WEB: http://www.ncbi.nlm.nih.gov/gene ZFAND2A zinc finger, AN1-type domain 2A 90637 7p22.3 9606 7 Official from a nomenclature committee GO_0005634 (EC: IEA); GO_0005737 (EC: IEA); GO_0008270 (EC: IEA) PMID: 12477932; 15489334; 20185824; 21906983; 21988832; 22505724; 22990118; 24250222 zinc finger, AN1-type domain 2A Ensembl:ENSG00000178381 HGNC:28073 HPRD:14277 MIM:610699 Vega:OTTHUMG00000119019 Other designations: AN1-type zinc finger protein 2A|arsenite inducible RNA associated protein ZFAND2A OGG:3000090668 Bin Zhao, Yue Liu, Oliver He C14orf121 CARMIL3 crml-1 WEB: http://www.ncbi.nlm.nih.gov/gene LRRC16B leucine rich repeat containing 16B 90668 14q11.2 9606 14 Official from a nomenclature committee GO_0005737 (EC: IEA) PMID: 10737800; 12477932; 15028280; 16344560; 19846667; 21102520 leucine rich repeat containing 16B Ensembl:ENSG00000186648 HGNC:20272 HPRD:11278 MIM:614716 Vega:OTTHUMG00000172023 Other designations: leucine-rich repeat-containing protein 16B LRRC16B OGG:3000090693 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CCDC126 coiled-coil domain containing 126 90693 UNQ786/PRO1605 7p15.3 9606 7 Official from a nomenclature committee GO_0005576 (EC: IEA); GO_0006487 (EC: IEA); GO_0030144 (EC: IEA) PMID: 9847074; 12477932; 12690205; 12975309; 23275563 coiled-coil domain containing 126 Other designations: coiled-coil domain-containing protein 126 CCDC126 OGG:3000090865 Bin Zhao, Yue Liu, Oliver He C9orf26 DVS27 IL1F11 NF-HEV NFEHEV WEB: http://www.ncbi.nlm.nih.gov/gene IL33 interleukin 33 90865 RP11-575C20.2 9p24.1 20140408 9606 9 protein-coding Official from a nomenclature committee GO_0002686 (EC: IEA); GO_0002826 (EC: IEA); GO_0002830 (EC: IEA); GO_0005125 (EC: IDA, PMID: 19841166); GO_0005515 (EC: IPI, PMID: 16286016); GO_0005615 (EC: IEA); GO_0005634 (EC: IEA); GO_0005694 (EC: IEA); GO_0006351 (EC: IEA); GO_0030133 (EC: IEA); GO_0032689 (EC: IEA); GO_0032736 (EC: IEA); GO_0032753 (EC: IEA); GO_0032754 (EC: IEA); GO_0032755 (EC: IEA); GO_0043032 (EC: IDA, PMID: 19841166); GO_0045944 (EC: ISS, PMID: 19841166); GO_0050729 (EC: ISS, PMID: 19841166); GO_0051024 (EC: IEA); GO_0051025 (EC: IEA); GO_0090197 (EC: IDA, PMID: 19841166) PMID: 10566975; 12477932; 12819012; 15164053; 15489334; 16169070; 16286016; 17185418; 17623648; 17675461; 17700564; 17853410; 18250453; 18539196; 18688256; 18762778; 18787100; 18802081; 18827826; 18836528; 18941187; 18955562; 19037964; 19198610; 19204726; 19248109; 19266498; 19372185; 19393621; 19439663; 19465481; 19508382; 19559631; 19596270; 19756962; 19801525; 19841166; 19860791; 19888696; 19906013; 19913053; 19918048; 20029461; 20035719; 20072851; 20153038; 20305685; 20338108; 20379614; 20385815; 20405148; 20406635; 20532808; 20534741; 20682660; 20689058; 20708824; 20731692; 20816195; 20860503; 20926795; 20931364; 20958987; 20963466; 21037074; 21190867; 21246230; 21357533; 21431944; 21441054; 21454686; 21519352; 21674220; 21674479; 21682736; 21684348; 21734074; 21737781; 21765905; 21802127; 21804549; 21898270; 21935266; 21949719; 22079334; 22100205; 22189043; 22215666; 22233535; 22239947; 22246057; 22270365; 22304300; 22307629; 22315510; 22329990; 22349136; 22540331; 22587998; 22590860; 22627366; 22634619; 22673732; 22682001; 22699663; 22708120; 22785132; 22809957; 22819319; 22828942; 22836779; 22841163; 22858587; 22921786; 23000728; 23028054; 23039129; 23093619; 23159404; 23162017; 23178147; 23205532; 23206447; 23219168; 23261461; 23300625; 23319592; 23357301; 23362867; 23363980; 23433789; 23464866; 23472165; 23484079; 23485578; 23488689; 23521712; 23525523; 23585867; 23634226; 23641786; 23656573; 23725175; 23759184; 23764374; 23775566; 23805875; 23817569; 23855553; 23935505; 23936781; 23980170; 23999434; 24075188; 24106520; 24107076; 24116703; 24257755; 24323357; 24459820 interleukin 33 Ensembl:ENSG00000137033 HGNC:16028 HPRD:12275 MIM:608678 Vega:OTTHUMG00000019516 IL33 OGG:3000091543 Bin Zhao, Yue Liu, Oliver He 2510004L01Rik cig33 cig5 vig1 WEB: http://www.ncbi.nlm.nih.gov/gene RSAD2 radical S-adenosyl methionine domain containing 2 91543 2p25.2 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0001503 (EC: IEA); GO_0003824 (EC: IEA); GO_0005515 (EC: IPI); GO_0005739 (EC: IDA); GO_0005741 (EC: IDA); GO_0005743 (EC: IDA); GO_0005783 (EC: IDA, PMID: 11752458); GO_0005789 (EC: IDA, PMID: 19074433); GO_0005794 (EC: IEA); GO_0005811 (EC: ISS); GO_0009615 (EC: IDA); GO_0016032 (EC: IEA); GO_0030278 (EC: IEA); GO_0034157 (EC: ISS); GO_0034165 (EC: ISS); GO_0035710 (EC: ISS); GO_0043367 (EC: ISS); GO_0043621 (EC: IDA, PMID: 19074433); GO_0045071 (EC: IDA); GO_0045087 (EC: IEA); GO_0046872 (EC: IEA); GO_0050709 (EC: IDA, PMID: 19074433); GO_0051539 (EC: IDA); GO_0051607 (EC: IDA, PMID: 16108059); GO_2000553 (EC: ISS) PMID: 9391139; 11752458; 12477932; 15890971; 16108059; 16849320; 16982913; 17626075; 18005724; 18077728; 18768981; 19074433; 19920176; 20026307; 20176015; 20534863; 20628624; 21053045; 21527675; 21957124; 22045669; 22182524; 22363738; 22377585; 22647704; 22734835; 22896602; 23018837; 23160199; 23509962; 23638199; 23935494 radical S-adenosyl methionine domain containing 2 Ensembl:ENSG00000134321 HGNC:30908 HPRD:07423 MIM:607810 Vega:OTTHUMG00000090352 Other designations: cytomegalovirus-induced gene 5 protein|radical S-adenosyl methionine domain-containing protein 2|viperin|virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible RSAD2 OGG:3000093273 Bin Zhao, Yue Liu, Oliver He CT50 LEMP-1 WEB: http://www.ncbi.nlm.nih.gov/gene LEMD1 LEM domain containing 1 93273 1q32.1 9606 1 Official from a nomenclature committee GO_0016021 (EC: IEA) PMID: 12477932; 15254688; 17207965; 20682177 LEM domain containing 1 Ensembl:ENSG00000186007 HGNC:18725 HPRD:13983 MIM:610480 Vega:OTTHUMG00000037201 Other designations: LEM domain protein 1|LEM domain-containing protein 1|cancer/testis antigen 50 LEMD1 OGG:3000094241 Bin Zhao, Yue Liu, Oliver He SIP TP53DINP1 TP53INP1A TP53INP1B Teap p53DINP1 WEB: http://www.ncbi.nlm.nih.gov/gene TP53INP1 tumor protein p53 inducible nuclear protein 1 94241 8q22 9606 8 Official from a nomenclature committee GO_0005515 (EC: IPI); GO_0005634 (EC: IDA); GO_0005776 (EC: IDA); GO_0005829 (EC: IDA); GO_0006351 (EC: IEA); GO_0006914 (EC: IEA); GO_0006915 (EC: IEA); GO_0006950 (EC: TAS); GO_0007050 (EC: TAS); GO_0008285 (EC: ISS); GO_0009408 (EC: IEA); GO_0010508 (EC: IMP); GO_0016209 (EC: ISS); GO_0016605 (EC: IEA); GO_0030336 (EC: ISS); GO_0031410 (EC: IEA); GO_0034644 (EC: IEA); GO_0043065 (EC: IEA); GO_0045893 (EC: IDA); GO_0048102 (EC: IMP); GO_0071361 (EC: IEA); GO_0071447 (EC: IEA); GO_0072703 (EC: IEA); GO_2001235 (EC: IEA) PMID: 11511362; 12067065; 12438758; 12477932; 12851404; 14702039; 15489334; 15706352; 16044147; 16344560; 16521180; 17393983; 17537403; 18277906; 18277909; 18974142; 19322201; 20581827; 20889853; 21219856; 21339733; 21538421; 22213058; 22421968; 22470510; 22730212; 23333058; 23568502 tumor protein p53 inducible nuclear protein 1 Ensembl:ENSG00000164938 HGNC:18022 HPRD:09367 MIM:606185 Vega:OTTHUMG00000164697 Other designations: p53-dependent damage-inducible nuclear protein 1|p53-inducible p53DINP1|stress-induced protein|tumor protein p53-inducible nuclear protein 1 TP53INP1 OGG:3000112476 Bin Zhao, Yue Liu, Oliver He BFIC2 BFIS2 DSPB3 DYT10 EKD1 FICCA ICCA IFITMD1 PKC WEB: http://www.ncbi.nlm.nih.gov/gene PRRT2 proline-rich transmembrane protein 2 112476 16p11.2 9606 16 Official from a nomenclature committee GO_0005886 (EC: IEA); GO_0009607 (EC: IEA); GO_0016021 (EC: IEA); GO_0030054 (EC: IEA); GO_0045202 (EC: IEA); GO_0050884 (EC: IMP) PMID: 8125298; 12477932; 14702039; 16169070; 16303743; 16344560; 17207965; 20301633; 22101681; 22120146; 22131361; 22209761; 22243967; 22360420; 22363774; 22386217; 22399141; 22464846; 22543779; 22623405; 22744660; 22752065; 22782515; 22832103; 22845787; 22870186; 22875091; 22877996; 22902423; 22985072; 23063574; 23073245; 23077016; 23077017; 23077018; 23077019; 23077024; 23077026; 23126439; 23176561; 23180180; 23182655; 23190448; 23299620; 23343561; 23352743; 23360469; 23363396; 23398397; 23456995; 23529024; 23535490; 23566103; 23771590; 23963607; 24250222 proline-rich transmembrane protein 2 Ensembl:ENSG00000167371 HGNC:30500 HPRD:13995 MIM:614386 Vega:OTTHUMG00000177142 Other designations: dispanin subfamily B member 3|infantile convulsions and paroxysmal choreoathetosis|interferon induced transmembrane protein domain containing 1 PRRT2 OGG:3000112849 Bin Zhao, Yue Liu, Oliver He C14orf149 WEB: http://www.ncbi.nlm.nih.gov/gene L3HYPDH L-3-hydroxyproline dehydratase (trans-) 112849 14q23.1 9606 14 Official from a nomenclature committee GO_0008152 (EC: IDA); GO_0016836 (EC: IDA); GO_0018112 (EC: IDA, Qualifier: NOT); GO_0050346 (EC: IEA) PMID: 12477932; 20379614; 22528483; 22939629 L-3-hydroxyproline dehydratase (trans-) Ensembl:ENSG00000126790 HGNC:20488 HPRD:08065 MIM:614811 Vega:OTTHUMG00000028941 Other designations: probable proline racemase|trans-3-hydroxy-l-proline dehydratase|trans-3-hydroxyl-L-proline dehydratase|trans-L-3-hydroxyproline dehydratase L3HYPDH OGG:3000113130 Bin Zhao, Yue Liu, Oliver He SORORIN WEB: http://www.ncbi.nlm.nih.gov/gene CDCA5 cell division cycle associated 5 113130 11q12.1 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0000082 (EC: IDA, PMID: 15837422); GO_0000278 (EC: TAS); GO_0000775 (EC: TAS); GO_0000790 (EC: ISS); GO_0003682 (EC: TAS, PMID: 15837422); GO_0005515 (EC: IPI); GO_0005634 (EC: IDA); GO_0005634 (EC: ISS); GO_0005654 (EC: TAS); GO_0005694 (EC: TAS); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005737 (EC: ISS); GO_0005829 (EC: TAS); GO_0005886 (EC: IDA); GO_0006302 (EC: IMP, PMID: 17349791); GO_0007064 (EC: IMP, PMID: 17349791); GO_0007067 (EC: IDA, PMID: 15837422); GO_0007076 (EC: IMP, PMID: 15837422); GO_0007080 (EC: IMP, PMID: 15837422); GO_0008278 (EC: IDA, Qualifier: colocalizes_with, PMID: 15837422); GO_0051329 (EC: ISS); GO_0071922 (EC: IMP, PMID: 17349791) PMID: 11111111; 12188893; 12477932; 14702039; 15146197; 15489334; 15837422; 16169070; 16964243; 17081983; 17349791; 17361102; 18029348; 20360068; 20379614; 20551060; 21111234; 21115494; 21890473; 21987589; 21988832; 22833568; 22939629; 23455924 cell division cycle associated 5 Ensembl:ENSG00000146670 HGNC:14626 HPRD:13016 MIM:609374 Vega:OTTHUMG00000150420 Other designations: cell division cycle-associated protein 5|p35|sororin CDCA5 OGG:3000113612 Bin Zhao, Yue Liu, Oliver He P450TEC SPG49 SPG56 WEB: http://www.ncbi.nlm.nih.gov/gene CYP2U1 cytochrome P450, family 2, subfamily U, polypeptide 1 113612 4q25 9606 4 GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006805 (EC: TAS); GO_0008219 (EC: IEA); GO_0016021 (EC: IEA); GO_0019369 (EC: TAS); GO_0020037 (EC: IEA); GO_0044281 (EC: TAS); GO_0070330 (EC: IEA); GO_0097267 (EC: TAS) PMID:12107412; 12477932; 14660610; 14975754; 15128046; 15588491; 20332099; 20630735; 21707071 cytochrome P450, family 2, subfamily U, polypeptide 1 Ensembl:ENSG00000155016 HGNC:20582 HPRD:13109 MIM:610670 Vega:OTTHUMG00000161084 Other designations: cytochrome P450 2U1|spastic paraplegia 49 CYP2U1 OGG:3000114548 Bin Zhao, Yue Liu, Oliver He AGTAVPRL AII AVP C1orf7 CIAS1 CLR1.1 FCAS FCU MWS NALP3 PYPAF1 WEB: http://www.ncbi.nlm.nih.gov/gene NLRP3 NLR family, pyrin domain containing 3 114548 1q44 20140408 9606 1 protein-coding Official from a nomenclature committee GO_0002674 (EC: IMP, PMID: 11687797); GO_0005515 (EC: IPI, PMID: 11786556); GO_0005524 (EC: IEA); GO_0005737 (EC: IDA, PMID: 17164409); GO_0005737 (EC: TAS, PMID: 15967716); GO_0005829 (EC: TAS); GO_0006915 (EC: NAS, PMID: 12032915); GO_0006919 (EC: IEA); GO_0006952 (EC: TAS, PMID: 15967716); GO_0006954 (EC: IMP, PMID: 12093792); GO_0007165 (EC: NAS, PMID: 11786556); GO_0009595 (EC: TAS, PMID: 15967716); GO_0032088 (EC: IDA, PMID: 14662828); GO_0032611 (EC: IEA); GO_0032621 (EC: IEA); GO_0035872 (EC: TAS); GO_0042347 (EC: IDA, PMID: 14662828); GO_0042834 (EC: TAS, PMID: 15967716); GO_0043280 (EC: IDA, PMID: 15030775); GO_0044546 (EC: IEA); GO_0045087 (EC: TAS); GO_0050701 (EC: IEA); GO_0050713 (EC: IMP, PMID: 12483741); GO_0050718 (EC: IDA, PMID: 15030775); GO_0050728 (EC: IMP, PMID: 12483741); GO_0051092 (EC: IDA, PMID: 19158675); GO_0051259 (EC: TAS, PMID: 15967716); GO_0051607 (EC: IEA); GO_0071222 (EC: IMP, PMID: 12483741); GO_0072559 (EC: IDA, PMID: 15030775) PMID: 9653160; 10741953; 11042152; 11687797; 11786556; 11967258; 11992256; 12032915; 12093792; 12355493; 12477932; 12483741; 12522564; 12563287; 12615073; 12673085; 12766759; 14630794; 14662828; 15020601; 15030775; 15071491; 15107016; 15334500; 15593220; 15967716; 16037825; 16234278; 16344560; 16531551; 16642435; 16710414; 16868559; 17046979; 17164343; 17164409; 17178985; 17213252; 17284928; 17393462; 17435760; 17592301; 17599094; 17620097; 17697637; 17763411; 17907925; 18005730; 18063752; 18080732; 18084703; 18174231; 18175851; 18189199; 18263599; 18311798; 18576390; 18719602; 18772453; 19001869; 19058789; 19098911; 19120479; 19120481; 19158675; 19201894; 19223160; 19254587; 19319132; 19337385; 19364881; 19414800; 19454352; 19570822; 19579027; 19648107; 19767079; 19784369; 19805629; 19811501; 19824913; 19826485; 19890791; 19913121; 20002790; 20008285; 20011700; 20031576; 20038581; 20060594; 20131254; 20131270; 20135584; 20148899; 20179743; 20182451; 20237496; 20368800; 20370570; 20384614; 20401456; 20401526; 20403135; 20407038; 20421639; 20502346; 20506209; 20628086; 20668705; 20688930; 20800603; 20808838; 20884650; 20962258; 20980503; 21035374; 21051542; 21058222; 21109514; 21124315; 21124859; 21217695; 21241317; 21245836; 21300955; 21315400; 21342182; 21394384; 21421008; 21451572; 21508263; 21550598; 21560198; 21566220; 21621776; 21637346; 21646297; 21876553; 21880711; 21930705; 21940629; 21940680; 21971358; 21978001; 21994456; 22102247; 22112657; 22128899; 22146561; 22227418; 22227487; 22276187; 22295065; 22325453; 22403613; 22461501; 22490866; 22497426; 22503597; 22522430; 22524199; 22529966; 22541070; 22558425; 22608495; 22698681; 22723549; 22768094; 22796220; 22843550; 22904305; 22933232; 22933241; 22935299; 22948162; 22981536; 22984081; 22984082; 22997256; 23015306; 23066025; 23086037; 23110140; 23171454; 23206693; 23209696; 23211828; 23221073; 23254930; 23264657; 23271661; 23280543; 23315075; 23375846; 23382313; 23399110; 23427152; 23430110; 23434541; 23440695; 23505242; 23530046; 23549611; 23563199; 23567555; 23582325; 23588528; 23614732; 23633957; 23737748; 23738518; 23815151; 23825667; 23838163; 23840644; 23843215; 23871209; 23884315; 23911403; 23937860; 23954133; 23969696; 23973727; 23980097; 24008734; 24048902; 24144834; 24166187 NLR family, pyrin domain containing 3 Ensembl:ENSG00000162711 HGNC:16400 HPRD:05915 MIM:606416 Vega:OTTHUMG00000040647 Other designations: NACHT domain-, leucine-rich repeat-, and PYD-containing protein 3|NACHT, LRR and PYD containing protein 3|NACHT, LRR and PYD domains-containing protein 3|PYRIN-containing APAF1-like protein 1|caterpiller protein 1.1|cold autoinflammatory syndrome 1 protein|cryopyrin|nucleotide-binding oligomerization domain, leucine rich repeat and pyrin domain containing 3 NLRP3 OGG:3000114827 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene FHAD1 forkhead-associated (FHA) phosphopeptide binding domain 1 114827 RP3-467K16.1 1p36.21 9606 1 Official from a nomenclature committee PMID: 11572484; 12477932; 14702039; 15489334; 16344560; 16710414; 20379614 forkhead-associated (FHA) phosphopeptide binding domain 1 Other designations: FHA domain-containing protein 1|forkhead-associated domain-containing protein 1 FHAD1 OGG:3000115265 Bin Zhao, Yue Liu, Oliver He REDD2 Rtp801L WEB: http://www.ncbi.nlm.nih.gov/gene DDIT4L DNA-damage-inducible transcript 4-like 115265 4q24 9606 4 Official from a nomenclature committee GO_0005737 (EC: ISS); GO_0009968 (EC: IEA) PMID: 12453409; 12477932; 14702039; 15308555; 15632201; 16189514; 16344560; 17207965; 19268525; 19491193; 19616115 DNA-damage-inducible transcript 4-like Ensembl:ENSG00000145358 HGNC:30555 HPRD:09663 MIM:607730 Vega:OTTHUMG00000161019 Other designations: DNA damage-inducible transcript 4-like protein|HIF-1 responsive protein RTP801-like|REDD-2|homolog of mouse SMHS1|protein regulated in development and DNA damage response 2|regulated in development and DNA damage response 2 DDIT4L OGG:3000116150 Bin Zhao, Yue Liu, Oliver He C6orf68 MGC:7199 NgBR TANGO14 WEB: http://www.ncbi.nlm.nih.gov/gene NUS1 nuclear undecaprenyl pyrophosphate synthase 1 homolog (S. cerevisiae) 116150 6q22.1 9606 6 Official from a nomenclature committee GO_0001525 (EC: IEA); GO_0003674 (EC: ND); GO_0005515 (EC: IPI); GO_0005789 (EC: IDA, PMID: 19723497); GO_0006486 (EC: IEA); GO_0016021 (EC: IEA); GO_0016765 (EC: IEA); GO_0030154 (EC: IEA); GO_0032367 (EC: IGI, PMID: 19723497); GO_0055092 (EC: IEA) PMID: 9294218; 12477932; 14574404; 15489334; 16835300; 17764014; 19723497; 21572394 nuclear undecaprenyl pyrophosphate synthase 1 homolog (S. cerevisiae) Ensembl:ENSG00000153989 HGNC:21042 HPRD:12894 MIM:610463 Vega:OTTHUMG00000015458 Other designations: nogo-B receptor|transport and golgi organization 14 homolog NUS1 OGG:3000116842 Bin Zhao, Yue Liu, Oliver He LEAP-2 WEB: http://www.ncbi.nlm.nih.gov/gene LEAP2 liver expressed antimicrobial peptide 2 116842 5q31.1 9606 5 Official from a nomenclature committee GO_0005576 (EC: IEA); GO_0042742 (EC: IEA) PMID: 12477932; 12493837; 15489334; 19852990; 20038463; 20379614; 20845358 liver expressed antimicrobial peptide 2 HGNC:29571 HPRD:17269 MIM:611373 Other designations: liver-expressed antimicrobial peptide 2 LEAP2 OGG:3000120227 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CYP2R1 cytochrome P450, family 2, subfamily R, polypeptide 1 120227 11p15.2 9606 11 GO_0004497 (EC: IEA); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006766 (EC: TAS); GO_0006805 (EC: TAS); GO_0008202 (EC: TAS); GO_0010164 (EC: IEA); GO_0010212 (EC: IEA); GO_0016705 (EC: IEA); GO_0020037 (EC: IEA); GO_0030343 (EC: IEA); GO_0042359 (EC: TAS); GO_0044281 (EC: TAS) PMID:12464240; 12477932; 12867411; 14702039; 15128046; 15128933; 15465040; 15489334; 15583024; 15951480; 16600026; 17223345; 17607662; 18476984; 18511070; 19783860; 19852851; 20007432; 20418485; 20541252; 20619365; 20654748; 20809279; 21270327; 21441443; 22576297; 22801813; 22855339; 23047203; 23063903; 23190755; 23377224; 23734184; 23793229; 23826131; 24073854 cytochrome P450, family 2, subfamily R, polypeptide 1 Other designations: cytochrome P450 2R1|cytochrome P450, family 2, R1|vitamin D 25-hydroxylase CYP2R1 OGG:3000120526 Bin Zhao, Yue Liu, Oliver He DPH4 JJJ3 ZCSL3 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC24 DnaJ (Hsp40) homolog, subfamily C, member 24 120526 AC108456.1 11p13 9606 11 GO_0001671 (EC: IDA); GO_0005737 (EC: IEA); GO_0005856 (EC: IEA); GO_0008198 (EC: IDA); GO_0008270 (EC: IDA); GO_0017183 (EC: IEA); GO_0032781 (EC: IDA); GO_0055114 (EC: IEA); GO_0061077 (EC: TAS) PMID:12477932; 14702039; 15485916; 15489334; 22367199; 22509046 DnaJ (Hsp40) homolog, subfamily C, member 24 HGNC:26979 HPRD:15705 MIM:611072 Other designations: 1700030A21Rik|CSL-type zinc finger-containing protein 3|DPH4 homolog (JJJ3, S. cerevisiae)|DPH4, JJJ3 homolog|diphthamide biosynthesis protein 4|dnaJ homolog subfamily C member 24|zinc finger, CSL domain containing 3|zinc finger, CSL-type containing 3 DNAJC24 OGG:3000122618 Bin Zhao, Yue Liu, Oliver He C14orf175 WEB: http://www.ncbi.nlm.nih.gov/gene PLD4 phospholipase D family, member 4 122618 UNQ2488/PRO5775 14q32.33 9606 14 Official from a nomenclature committee GO_0004435 (EC: TAS); GO_0004630 (EC: IEA); GO_0005789 (EC: TAS); GO_0006644 (EC: TAS); GO_0006655 (EC: TAS); GO_0016021 (EC: IEA); GO_0016042 (EC: IEA); GO_0043647 (EC: TAS); GO_0044281 (EC: TAS); GO_0046474 (EC: TAS); GO_0070290 (EC: IEA) PMID: 12477932; 12975309; 15489334; 16094384; 21890473; 22446963; 23124809 phospholipase D family, member 4 Ensembl:ENSG00000166428 HGNC:23792 HPRD:11230 Vega:OTTHUMG00000144167 Other designations: PLD 4|choline phosphatase 4|phosphatidylcholine-hydrolyzing phospholipase D4|phospholipase D4 PLD4 OGG:3000122970 Bin Zhao, Yue Liu, Oliver He PTE-Ib PTE1B PTE2B WEB: http://www.ncbi.nlm.nih.gov/gene ACOT4 acyl-CoA thioesterase 4 122970 14q24.3 9606 14 GO_0000038 (EC: IDA, PMID:16940157); GO_0001676 (EC: IDA, PMID:16940157); GO_0004778 (EC: IDA, PMID:16141203); GO_0005102 (EC: IPI); GO_0005777 (EC: IDA, PMID:16141203); GO_0006104 (EC: IDA, PMID:16940157); GO_0006637 (EC: IDA, PMID:16940157); GO_0016290 (EC: IEA); GO_0019605 (EC: IDA, Qualifier: NOT, PMID:16940157); GO_0032788 (EC: IDA, PMID:16940157); GO_0032789 (EC: IDA, PMID:16940157); GO_0043648 (EC: IDA, PMID:16940157); GO_0043649 (EC: IDA, PMID:16141203); GO_0046459 (EC: IDA, PMID:16940157); GO_0047617 (EC: IDA, PMID:16141203) PMID:7596406; 10567408; 10944470; 12477932; 14702039; 15489334; 16103133; 16141203; 16940157; 18029348; 20178365 acyl-CoA thioesterase 4 HGNC:19748 HPRD:17928 MIM:614314 Other designations: PTE-2b|acyl-coenzyme A thioesterase 4|peroxisomal acyl coenzyme A thioester hydrolase Ib|peroxisomal acyl-CoA thioesterase 2B|peroxisomal long-chain acyl-CoA thioesterase Ib ACOT4 OGG:3000123688 Bin Zhao, Yue Liu, Oliver He AGPHD1 WEB: http://www.ncbi.nlm.nih.gov/gene HYKK hydroxylysine kinase 123688 15q25.1 9606 15 Official from a nomenclature committee GO_0005737 (EC: IEA); GO_0047992 (EC: IEA) PMID: 12477932; 16341674; 18385676; 18385738; 18780872; 19300482; 19654303; 19733931; 20548021; 20554942; 20587604; 21081471; 21685187; 21890473; 21963094; 22241472; 22701590; 22837378 hydroxylysine kinase Ensembl:ENSG00000188266 HGNC:34403 HPRD:12515 MIM:614681 Vega:OTTHUMG00000177204 Other designations: 5-hydroxy-L-lysine kinase|5-hydroxylysine kinase|aminoglycoside phosphotransferase domain containing 1|aminoglycoside phosphotransferase domain-containing protein 1 HYKK OGG:3000123876 Bin Zhao, Yue Liu, Oliver He A-923A4.1 ACSM2 WEB: http://www.ncbi.nlm.nih.gov/gene ACSM2A acyl-CoA synthetase medium-chain family member 2A 123876 16p12.3 20140408 9606 16 protein-coding Official from a nomenclature committee GO_0005524 (EC: IEA); GO_0005739 (EC: NAS, PMID: 19634011); GO_0005759 (EC: IEA); GO_0006631 (EC: IEA); GO_0036112 (EC: IDA, PMID: 19345228); GO_0042593 (EC: NAS, PMID: 16521160); GO_0046872 (EC: IEA); GO_0047760 (EC: IDA, PMID: 19345228); GO_0070328 (EC: NAS, PMID: 16521160) PMID: 10493829; 12477932; 14702039; 16344560; 16521160; 19345228; 19634011; 20877624 acyl-CoA synthetase medium-chain family member 2A Ensembl:ENSG00000183747 HGNC:32017 HPRD:17292 MIM:614358 Vega:OTTHUMG00000177401 Other designations: Homolog of rat kidney-specific (KS)|acyl-coenzyme A synthetase ACSM2A, mitochondrial|butyrate--CoA ligase 2A|butyryl-coenzyme A synthetase 2A|middle-chain acyl-CoA synthetase 2A ACSM2A OGG:3000126410 Bin Zhao, Yue Liu, Oliver He ARCI5 INLNE LI3 WEB: http://www.ncbi.nlm.nih.gov/gene CYP4F22 cytochrome P450, family 4, subfamily F, polypeptide 22 126410 19p13.12 9606 19 GO_0004497 (EC: IEA); GO_0005506 (EC: IEA); GO_0005789 (EC: IEA); GO_0016705 (EC: IEA); GO_0020037 (EC: IEA) PMID:10712205; 10712223; 12477932; 15128046; 16344560; 16436457; 18245815; 20301593; 21540472; 21906983; 22209317 cytochrome P450, family 4, subfamily F, polypeptide 22 Ensembl:ENSG00000171954 HGNC:26820 HPRD:08256 MIM:611495 Vega:OTTHUMG00000182451 Other designations: cytochrome P450 4F22|cytochrome P450, family 2, subfamily E, polypeptide 2 homolog CYP4F22 OGG:3000128346 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene C1orf162 chromosome 1 open reading frame 162 128346 1p13.2 9606 1 Official from a nomenclature committee GO_0016021 (EC: IEA) PMID: 12477932; 14702039 chromosome 1 open reading frame 162 Other designations: transmembrane protein C1orf162 C1orf162 OGG:3000128553 Bin Zhao, Yue Liu, Oliver He C20orf17 OVC10-2 TSH2 ZABC2 ZNF218 WEB: http://www.ncbi.nlm.nih.gov/gene TSHZ2 teashirt zinc finger homeobox 2 128553 RP5-823G15.3 20q13.2 9606 20 Official from a nomenclature committee GO_0003700 (EC: IEA); GO_0005634 (EC: IEA); GO_0006351 (EC: IEA); GO_0007275 (EC: IEA); GO_0043565 (EC: IEA); GO_0046872 (EC: IEA) PMID: 9671742; 11181995; 11780052; 12477932; 14702039; 15561718; 16344560; 19343227; 19745106; 19862010; 19913121; 20379614; 20628086; 21423795 teashirt zinc finger homeobox 2 Ensembl:ENSG00000182463 HGNC:13010 HPRD:10730 MIM:614118 Vega:OTTHUMG00000033058 Other designations: cell growth-inhibiting protein 7|ovarian cancer-related protein 10-2|serologically defined colon cancer antigen 33 like|teashirt family zinc finger 2|teashirt homolog 2|zinc finger protein 218 TSHZ2 OGG:3000129607 Bin Zhao, Yue Liu, Oliver He TMPK2 TYKi UMP-CMPK2 WEB: http://www.ncbi.nlm.nih.gov/gene CMPK2 cytidine monophosphate (UMP-CMP) kinase 2, mitochondrial 129607 2p25.2 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0004127 (EC: IDA, PMID: 17999954); GO_0004550 (EC: IDA); GO_0004798 (EC: IEA); GO_0005524 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0005739 (EC: IDA); GO_0006165 (EC: IDA); GO_0006227 (EC: IEA); GO_0006233 (EC: IEA); GO_0009142 (EC: IDA); GO_0033862 (EC: IDA, PMID: 17999954); GO_0071222 (EC: IEA) PMID: 12477932; 16344560; 17999954; 18029348; 18498354; 20379614; 22505724 cytidine monophosphate (UMP-CMP) kinase 2, mitochondrial Ensembl:ENSG00000134326 HGNC:27015 HPRD:11233 MIM:611787 Vega:OTTHUMG00000151629 Other designations: UMP-CMP kinase 2, mitochondrial|cytidylate kinase 2|mitochondrial UMP-CMP kinase|nucleoside-diphosphate kinase|thymidine monophosphate kinase 2|thymidylate kinase family LPS-inducible member CMPK2 OGG:3000131118 Bin Zhao, Yue Liu, Oliver He PAM18 TIM14 TIMM14 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC19 DnaJ (Hsp40) homolog, subfamily C, member 19 131118 3q26.33 9606 3 GO_0005739 (EC: IDA, PMID:12592411); GO_0005743 (EC: IEA); GO_0006457 (EC: NAS, PMID:16055927); GO_0006626 (EC: NAS, PMID:16055927); GO_0006626 (EC: TAS); GO_0007601 (EC: IMP, PMID:16055927); GO_0016021 (EC: NAS, PMID:16055927); GO_0044267 (EC: TAS); GO_0048806 (EC: IMP, PMID:16055927) PMID:8889548; 10737800; 12477932; 12592411; 14517234; 15489334; 16055927; 16344560; 16712791; 17244376; 19564938; 20053669; 21139048; 21832049; 21890473; 22544056; 22797137; 22939629 DnaJ (Hsp40) homolog, subfamily C, member 19 Ensembl:ENSG00000205981 HGNC:30528 HPRD:12349 MIM:608977 Vega:OTTHUMG00000158180 Other designations: homolog of yeast TIM14|mitochondrial import inner membrane translocase subunit TIM14 DNAJC19 OGG:3000133746 Bin Zhao, Yue Liu, Oliver He WHDC1L3 WEB: http://www.ncbi.nlm.nih.gov/gene JMY junction mediating and regulatory protein, p53 cofactor 133746 5q14.1 9606 5 Official from a nomenclature committee GO_0003713 (EC: ISS); GO_0003779 (EC: IEA); GO_0005515 (EC: IPI, PMID: 10518217); GO_0005634 (EC: ISS); GO_0005737 (EC: IEA); GO_0005856 (EC: IEA); GO_0006281 (EC: IEA); GO_0006357 (EC: ISS); GO_0007050 (EC: ISS); GO_0031252 (EC: IDA, PMID: 19287377); GO_0034314 (EC: ISS); GO_0043065 (EC: ISS); GO_0051091 (EC: ISS); GO_0070060 (EC: ISS); GO_0070358 (EC: ISS); GO_0072332 (EC: IEA) PMID: 8889548; 10518217; 12477932; 14702039; 15146197; 15706352; 16344560; 17170761; 18398821; 19287377; 19897726; 21625218; 21965285; 22262458; 23758122; 24250222 junction mediating and regulatory protein, p53 cofactor Ensembl:ENSG00000152409 HGNC:28916 HPRD:05045 MIM:604279 Vega:OTTHUMG00000131301 Other designations: WAS protein homology region 2 domain containing 1-like 3|junction-mediating and -regulatory protein|junction-mediating and regulatory protein JMY OGG:3000134218 Bin Zhao, Yue Liu, Oliver He DNAJA5 GS3 JJJ1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC21 DnaJ (Hsp40) homolog, subfamily C, member 21 134218 5p13.2 9606 5 GO_0003674 (EC: ND); GO_0005515 (EC: IPI, PMID:17500595); GO_0005840 (EC: NAS, PMID:16952052); GO_0006457 (EC: NAS, PMID:16952052); GO_0008270 (EC: IEA); GO_0044822 (EC: IDA) PMID:12477932; 14702039; 15067379; 15489334; 16952052; 17081983; 17500595; 18654987; 20195357; 21139048; 21145461; 21890473; 22566498; 23000965; 24457600 DnaJ (Hsp40) homolog, subfamily C, member 21 Ensembl:ENSG00000168724 HGNC:27030 HPRD:14056 Vega:OTTHUMG00000074103 Other designations: DnaJ homology subfamily A member 5|JJJ1 DnaJ domain protein homolog|dnaJ homolog subfamily A member 5|dnaJ homolog subfamily C member 21 DNAJC21 OGG:3000134526 Bin Zhao, Yue Liu, Oliver He CACH-1 Cach STARD15 THEAL WEB: http://www.ncbi.nlm.nih.gov/gene ACOT12 acyl-CoA thioesterase 12 134526 5q14.1 9606 5 GO_0003986 (EC: ISS); GO_0005524 (EC: IEA); GO_0005829 (EC: ISS); GO_0006084 (EC: IEA); GO_0006090 (EC: IEA); GO_0006631 (EC: IEA); GO_0006637 (EC: ISS); GO_0008289 (EC: IEA) PMID:11322891; 12477932; 12767336; 14702039; 15489334; 16103133; 16951743; 20379614; 22863734 acyl-CoA thioesterase 12 Ensembl:ENSG00000172497 HGNC:24436 HPRD:16680 MIM:614315 Vega:OTTHUMG00000131305 Other designations: START domain-containing protein 15|StAR-related lipid transfer (START) domain containing 15|acyl-CoA thioester hydrolase 12|acyl-coenzyme A thioesterase 12|cytoplasmic acetyl-CoA hydrolase 1|cytosolic acetyl-CoA hydrolase|hCACH-1 ACOT12 OGG:3000135932 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene TMEM139 transmembrane protein 139 135932 UNQ1932/PRO4407 7q34 20140408 9606 7 protein-coding Official from a nomenclature committee GO_0016021 (EC: IEA) PMID: 8889548; 12477932; 12690205; 12975309; 15231748; 16303743; 16344560; 16712791; 17213182; 19773279; 24250222 transmembrane protein 139 TMEM139 OGG:3000140809 Bin Zhao, Yue Liu, Oliver He C20orf139 Npn3 SRX SRX1 WEB: http://www.ncbi.nlm.nih.gov/gene SRXN1 sulfiredoxin 1 140809 20p13 9606 20 Official from a nomenclature committee GO_0005524 (EC: IEA); GO_0005829 (EC: IDA, PMID: 15448164); GO_0006979 (EC: IDA, PMID: 15448164); GO_0016667 (EC: IDA, PMID: 15448164); GO_0032542 (EC: IEA) PMID: 11076863; 11181995; 11230166; 11780052; 12477932; 15448164; 15489334; 15489336; 15590625; 15952770; 16381901; 16565085; 16818657; 17176052; 18172504; 18579529; 18593714; 19027064; 19057013; 19561357; 19812042; 20718723; 21487000; 21742584; 21800051; 21943684; 22086924; 22879602; 22934964; 22939629; 22964583 sulfiredoxin 1 Ensembl:ENSG00000271303 HGNC:16132 HPRD:12747 Vega:OTTHUMG00000031644 Other designations: sulfiredoxin-1 SRXN1 OGG:3000143244 Bin Zhao, Yue Liu, Oliver He EIF5AP1 bA342M3.3 WEB: http://www.ncbi.nlm.nih.gov/gene EIF5AL1 eukaryotic translation initiation factor 5A-like 1 143244 RP11-342M3.3 10q22.3 9606 10 GO_0003746 (EC: IEA); GO_0005643 (EC: IEA); GO_0005789 (EC: IEA); GO_0006452 (EC: IEA); GO_0008612 (EC: IEA); GO_0015031 (EC: IEA); GO_0043022 (EC: IEA); GO_0045901 (EC: IEA); GO_0045905 (EC: IEA); GO_0051028 (EC: IEA) PMID:1286667; 2492279; 3095320; 7545941; 7622067; 7759117; 8253832; 10944119; 11742107; 12477932; 15489334; 16519677; 16916647; 20639865; 21139048; 21890473; 21906983; 21963094; 22053931; 22505724; 23000965 eukaryotic translation initiation factor 5A-like 1 Ensembl:ENSG00000253626 HGNC:17419 Vega:OTTHUMG00000018563 Other designations: eukaryotic translation initiation factor 5A pseudogene 1|eukaryotic translation initiation factor 5A-1-like EIF5AL1 OGG:3000146225 Bin Zhao, Yue Liu, Oliver He CKLFSF2 WEB: http://www.ncbi.nlm.nih.gov/gene CMTM2 CKLF-like MARVEL transmembrane domain containing 2 146225 16q21 20140408 9606 16 protein-coding Official from a nomenclature committee GO_0005125 (EC: IEA); GO_0005615 (EC: IEA); GO_0005634 (EC: IDA); GO_0005730 (EC: IDA, Qualifier: NOT); GO_0006935 (EC: IEA); GO_0016021 (EC: IEA) PMID: 12477932; 12782130; 14702039; 15489334; 15778092; 15896670; 17334588; 18029348; 21034562; 21832049; 22901147 CKLF-like MARVEL transmembrane domain containing 2 Ensembl:ENSG00000140932 HGNC:19173 HPRD:07434 MIM:607885 Vega:OTTHUMG00000137501 CMTM2 OGG:3000150353 Bin Zhao, Yue Liu, Oliver He DJ5 HSC3 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB7 DnaJ (Hsp40) homolog, subfamily B, member 7 150353 22q13.2 9606 22 PMID:10591208; 11147971; 12477932; 15461802; 15489334; 18029348 DnaJ (Hsp40) homolog, subfamily B, member 7 Ensembl:ENSG00000172404 HGNC:24986 HPRD:07010 MIM:611336 Vega:OTTHUMG00000151202 Other designations: dnaJ homolog subfamily B member 7|novel DnaJ domain protein DNAJB7 OGG:3000150759 Bin Zhao, Yue Liu, Oliver He NCRNA00342 WEB: http://www.ncbi.nlm.nih.gov/gene LINC00342 long intergenic non-protein coding RNA 342 150759 2q11.2 9606 2 Official from a nomenclature committee PMID: 12477932; 14702039 long intergenic non-protein coding RNA 342 HGNC:42470 LINC00342 OGG:3000151056 Bin Zhao, Yue Liu, Oliver He PLB PLB/LIP hPLB WEB: http://www.ncbi.nlm.nih.gov/gene PLB1 phospholipase B1 151056 2p23.2 9606 2 Official from a nomenclature committee GO_0001523 (EC: TAS); GO_0004622 (EC: IEA); GO_0004623 (EC: IEA); GO_0005886 (EC: TAS); GO_0006644 (EC: TAS); GO_0007603 (EC: TAS); GO_0016021 (EC: IEA); GO_0016042 (EC: IEA); GO_0016324 (EC: IEA); GO_0036151 (EC: TAS); GO_0044281 (EC: TAS); GO_0046474 (EC: TAS) PMID: 8017323; 12150957; 12477932; 12804600; 14702039; 15583024 phospholipase B1 Ensembl:ENSG00000163803 HGNC:30041 HPRD:15141 MIM:610179 Vega:OTTHUMG00000152014 Other designations: lysophospholipase|phospholipase A2|phospholipase B|phospholipase B/lipase|phospholipase B1, membrane-associated PLB1 OGG:3000151126 Bin Zhao, Yue Liu, Oliver He ZNF533 WEB: http://www.ncbi.nlm.nih.gov/gene ZNF385B zinc finger protein 385B 151126 2q31.2-q31.3 9606 2 Official from a nomenclature committee GO_0002039 (EC: IPI); GO_0003676 (EC: IEA); GO_0005634 (EC: IDA); GO_0008270 (EC: IEA); GO_0072332 (EC: IDA) PMID: 12477932; 14702039; 15489334; 16344560; 19240061; 19401682; 20379614; 20849254; 21658281; 22945289; 23029477; 24457600 zinc finger protein 385B Ensembl:ENSG00000144331 HGNC:26332 HPRD:15823 MIM:612344 Vega:OTTHUMG00000154559 Other designations: zinc finger protein 533 ZNF385B OGG:3000153020 Bin Zhao, Yue Liu, Oliver He GPIG4 WEB: http://www.ncbi.nlm.nih.gov/gene RASGEF1B RasGEF domain family, member 1B 153020 4q21.21 9606 4 Official from a nomenclature committee GO_0005088 (EC: IDA, PMID: 19645719); GO_0005769 (EC: IEA); GO_0005770 (EC: IEA); GO_0007264 (EC: IEA); GO_0030496 (EC: IEA); GO_0032318 (EC: IDA, PMID: 19645719) PMID: 12477932; 12488504; 14702039; 18391951; 19645719; 22303795; 23377640 RasGEF domain family, member 1B Ensembl:ENSG00000138670 HGNC:24881 HPRD:17955 MIM:614532 Vega:OTTHUMG00000160890 Other designations: GPI gamma-4|GPI-gamma 4|ras-GEF domain-containing family member 1B RASGEF1B OGG:3000161253 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene REM2 RAS (RAD and GEM)-like GTP binding 2 161253 hCG_41987 14q11.2 9606 14 Official from a nomenclature committee GO_0003924 (EC: IEA); GO_0005525 (EC: IEA); GO_0005886 (EC: IEA); GO_0007264 (EC: IEA) PMID: 10727423; 11181995; 12477932; 14702039; 15489334; 15728182; 18056257; 20231315; 21044950; 21485012; 21980534; 22815963 RAS (RAD and GEM)-like GTP binding 2 Other designations: GTP-binding protein REM 2|Rad and Gem-related 2 (rat homolog)|rad and Gem-like GTP-binding protein 2 REM2 OGG:3000163590 Bin Zhao, Yue Liu, Oliver He IFRG15 LULL1 NET9 WEB: http://www.ncbi.nlm.nih.gov/gene TOR1AIP2 torsin A interacting protein 2 163590 RP11-12M5.5 1q25.2 9606 1 Official from a nomenclature committee GO_0001671 (EC: IDA); GO_0005789 (EC: IEA); GO_0016021 (EC: IEA); GO_0031965 (EC: IEA); GO_0032781 (EC: IDA); GO_0051117 (EC: IPI) PMID: 11181995; 12477932; 14702039; 15342556; 15489334; 15767459; 16710414; 16964240; 19295130; 19339278; 19615732; 19651773; 20861018; 21139048; 21145461; 21890473; 21906983; 21963094; 22190034; 22268729; 23569223 torsin A interacting protein 2 Ensembl:ENSG00000169905 HGNC:24055 HPRD:10048 MIM:614513 Vega:OTTHUMG00000035265 Other designations: 15 kDa interferon-responsive protein|interferon responsive gene 15|lumenal domain like LAP1|lumenal domain-like LAP1|torsin-1A-interacting protein 2 TOR1AIP2 OGG:3000165721 Bin Zhao, Yue Liu, Oliver He CT156 DJ6 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB8 DnaJ (Hsp40) homolog, subfamily B, member 8 165721 3q21.3 9606 3 GO_0044183 (EC: IDA); GO_0061077 (EC: IDA) PMID:11147971; 12477932; 15489334; 17207965; 20159555; 20556630; 22552285; 23612975 DnaJ (Hsp40) homolog, subfamily B, member 8 Ensembl:ENSG00000179407 HGNC:23699 HPRD:06684 HPRD:09921 MIM:611337 Vega:OTTHUMG00000159690 Other designations: dnaJ homolog subfamily B member 8 DNAJB8 OGG:3000166785 Bin Zhao, Yue Liu, Oliver He cblA WEB: http://www.ncbi.nlm.nih.gov/gene MMAA methylmalonic aciduria (cobalamin deficiency) cblA type 166785 4q31.21 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0005525 (EC: IEA); GO_0005759 (EC: TAS); GO_0006635 (EC: TAS); GO_0006766 (EC: TAS); GO_0006767 (EC: TAS); GO_0009235 (EC: TAS); GO_0009236 (EC: IEA); GO_0017111 (EC: IEA); GO_0019626 (EC: TAS); GO_0044255 (EC: TAS); GO_0044281 (EC: TAS) PMID: 12438653; 12477932; 14702039; 15308131; 15489334; 15523652; 16641088; 17597648; 17957493; 19371216; 20301409; 20876572; 21138732; 23026888; 24250222 methylmalonic aciduria (cobalamin deficiency) cblA type Ensembl:ENSG00000151611 HGNC:18871 HPRD:07394 MIM:607481 Vega:OTTHUMG00000161369 Other designations: methylmalonic aciduria type A protein, mitochondrial MMAA OGG:3000168620 Bin Zhao, Yue Liu, Oliver He BHLHB8 MIST1 WEB: http://www.ncbi.nlm.nih.gov/gene BHLHA15 basic helix-loop-helix family, member a15 168620 7q21.3 9606 7 Official from a nomenclature committee GO_0003677 (EC: IEA); GO_0005634 (EC: IEA); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0046983 (EC: IEA) PMID: 9073453; 9482738; 12477932; 12617822; 12690205; 12853948; 14516699; 15489334; 16645041; 18557763; 20038531; 20382342; 20709804; 21098683; 21907708; 22354994; 22374815; 22495370 basic helix-loop-helix family, member a15 Ensembl:ENSG00000180535 HGNC:22265 HPRD:16356 MIM:608606 Vega:OTTHUMG00000154289 Other designations: MIST-1|basic helix-loop-helix domain containing, class B, 8|class A basic helix-loop-helix protein 15|class B basic helix-loop-helix protein 8|class II bHLH protein MIST1|muscle, intestine and stomach expression 1 BHLHA15 OGG:3000196463 Bin Zhao, Yue Liu, Oliver He P76 WEB: http://www.ncbi.nlm.nih.gov/gene PLBD2 phospholipase B domain containing 2 196463 12q24.13 9606 12 Official from a nomenclature committee GO_0016042 (EC: IEA); GO_0016787 (EC: IEA); GO_0043202 (EC: IEA) PMID: 12477932; 15146197; 15193148; 17105447; 21906983; 21963094; 22268729; 22939629 phospholipase B domain containing 2 Ensembl:ENSG00000151176 HGNC:27283 HPRD:14116 Vega:OTTHUMG00000169567 Other designations: 76 kDa protein|LAMA-like protein 2|PLB homolog 2|lamina ancestor homolog 2|mannose-6-phosphate protein associated protein p76|phospholipase B domain-containing protein 2|phospholipase B-like 2 32 kDa form|phospholipase B-like 2 45 kDa form|putative phospholipase B-like 2 PLBD2 OGG:3000197350 Bin Zhao, Yue Liu, Oliver He CASP14L WEB: http://www.ncbi.nlm.nih.gov/gene CASP16 caspase 16, apoptosis-related cysteine peptidase (putative) 197350 16p13.3 9606 16 GO_0004197 (EC: IBA); GO_0005737 (EC: IBA); GO_0008630 (EC: IBA); GO_0097192 (EC: IBA) PMID:9847080; 12477932; 14702039; 15489334; 15616553; 18281271 caspase 16, apoptosis-related cysteine peptidase (putative) HGNC:27290 Other designations: putative caspase-14-like protein|putative caspase-16 CASP16 OGG:3000199974 Bin Zhao, Yue Liu, Oliver He CYP4A20 WEB: http://www.ncbi.nlm.nih.gov/gene CYP4Z1 cytochrome P450, family 4, subfamily Z, polypeptide 1 199974 UNQ3060/PRO9882 1p33 9606 1 GO_0005506 (EC: IEA); GO_0005789 (EC: IEA); GO_0016021 (EC: IEA); GO_0020037 (EC: IEA); GO_0070330 (EC: IEA) PMID:9068972; 12975309; 15059886; 15128046; 15797250; 19090726; 19473719; 22841774 cytochrome P450, family 4, subfamily Z, polypeptide 1 Ensembl:ENSG00000186160 HGNC:20583 HPRD:13111 Vega:OTTHUMG00000008019 Other designations: CYPIVZ1|cytochrome P450 4Z1 CYP4Z1 OGG:3000200576 Bin Zhao, Yue Liu, Oliver He CFD FAB1 HEL37 PIP5K PIP5K3 ZFYVE29 WEB: http://www.ncbi.nlm.nih.gov/gene PIKFYVE phosphoinositide kinase, FYVE finger containing 200576 2q34 20140408 9606 2 protein-coding Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0000285 (EC: IEA); GO_0005515 (EC: IPI, PMID: 15046600); GO_0005524 (EC: IEA); GO_0005829 (EC: IEA); GO_0006644 (EC: TAS); GO_0006661 (EC: TAS); GO_0006898 (EC: IMP, Qualifier: NOT, PMID: 14551253); GO_0010008 (EC: IDA, PMID: 17556371); GO_0016308 (EC: TAS, PMID: 15046600); GO_0031410 (EC: IEA); GO_0031901 (EC: IDA, PMID: 16448788); GO_0031901 (EC: TAS); GO_0031902 (EC: TAS); GO_0032288 (EC: IEA); GO_0034504 (EC: IMP, PMID: 17909029); GO_0035556 (EC: IEA); GO_0036092 (EC: TAS); GO_0042147 (EC: IMP, PMID: 14551253); GO_0043813 (EC: TAS); GO_0044267 (EC: IEA); GO_0044281 (EC: TAS); GO_0045121 (EC: IDA, PMID: 15046600); GO_0046854 (EC: TAS, PMID: 15046600); GO_0046872 (EC: IEA); GO_0048471 (EC: IEA) PMID: 10231032; 11706043; 11714711; 12270933; 12477932; 12607114; 14530284; 14551253; 14702039; 15046600; 15144186; 15542851; 15592455; 15902656; 16147992; 16448788; 16801682; 16954148; 17081983; 17146146; 17207965; 17556371; 17570343; 17909029; 18304842; 18429927; 18501703; 18774718; 18950639; 19037259; 19056739; 19232516; 19582903; 19840946; 19841139; 19852935; 19910676; 20041238; 20193073; 20379614; 20467438; 20945365; 21832049; 22065932; 22118674; 22621786; 23154468; 23188060; 23297396; 23757022; 24250222 phosphoinositide kinase, FYVE finger containing Ensembl:ENSG00000115020 HGNC:23785 HPRD:17852 MIM:609414 Vega:OTTHUMG00000132945 Other designations: 1-phosphatidylinositol 3-phosphate 5-kinase|1-phosphatidylinositol-3-phosphate 5-kinase|PIPkin-III|epididymis luminal protein 37|phosphatidylinositol 3-phosphate 5-kinase type III|phosphatidylinositol-3-phosphate/phosphatidylinositol 5-kinase, type III|type III PIP kinase|zinc finger, FYVE domain containing 29 PIKFYVE OGG:3000201163 Bin Zhao, Yue Liu, Oliver He BHD FLCL WEB: http://www.ncbi.nlm.nih.gov/gene FLCN folliculin 201163 17p11.2 9606 17 Official from a nomenclature committee GO_0000122 (EC: IDA); GO_0000122 (EC: IMP); GO_0001701 (EC: ISS); GO_0001932 (EC: IDA, PMID: 18663353); GO_0001934 (EC: ISS); GO_0005515 (EC: IPI, PMID: 17028174); GO_0005634 (EC: IDA, PMID: 17028174); GO_0005737 (EC: IDA); GO_0005886 (EC: IDA); GO_0007043 (EC: ISS); GO_0010628 (EC: ISS); GO_0010629 (EC: ISS); GO_0010823 (EC: ISS); GO_0030097 (EC: ISS); GO_0030308 (EC: IDA); GO_0030336 (EC: IMP); GO_0030496 (EC: IDA, Qualifier: colocalizes_with); GO_0030511 (EC: IDA); GO_0030511 (EC: ISS); GO_0031929 (EC: IMP, PMID: 17028174); GO_0032006 (EC: ISS); GO_0032007 (EC: ISS); GO_0032008 (EC: ISS); GO_0032403 (EC: IDA, PMID: 17028174); GO_0032465 (EC: IMP); GO_0035024 (EC: IMP); GO_0035065 (EC: ISS); GO_0043065 (EC: ISS); GO_0044291 (EC: IDA, Qualifier: colocalizes_with); GO_0045785 (EC: IMP); GO_0045944 (EC: IDA); GO_0045944 (EC: IMP); GO_0051898 (EC: ISS); GO_0070373 (EC: ISS); GO_1900181 (EC: IDA); GO_1901723 (EC: ISS); GO_2000506 (EC: ISS); GO_2000973 (EC: ISS); GO_2001170 (EC: ISS) PMID: 11526515; 11533913; 12204536; 12471204; 12477932; 12746401; 12843323; 12907635; 14627671; 14702039; 14961590; 15489334; 15579035; 15657874; 15852235; 15956655; 16344560; 16636660; 16870330; 17028174; 17149965; 17207965; 17496196; 18029348; 18206534; 18234728; 18403135; 18505456; 18573707; 18579543; 18663353; 18709329; 19116017; 19234517; 19327534; 19483054; 20227563; 20301695; 20413710; 20522427; 20562859; 20618353; 21079084; 21139048; 21209915; 21258407; 21412933; 21496834; 21538689; 21832049; 21890473; 22146830; 22190034; 22211584; 22446046; 22709692; 22965878; 22977732; 22990118; 23077212; 23139756; 23150719; 23155228; 23414156; 23784378; 23824909; 24095279 folliculin Ensembl:ENSG00000154803 HGNC:27310 HPRD:06278 MIM:607273 Vega:OTTHUMG00000059275 Other designations: BHD skin lesion fibrofolliculoma protein|birt-Hogg-Dube syndrome protein FLCN OGG:3000202052 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC18 DnaJ (Hsp40) homolog, subfamily C, member 18 202052 5q31.2 9606 5 GO_0016021 (EC: IEA) PMID:8889548; 12477932; 14702039; 15489334; 16344560; 17207965; 18676680; 19170196; 19240791; 19625176; 19692168 DnaJ (Hsp40) homolog, subfamily C, member 18 Other designations: dnaJ homolog subfamily C member 18 DNAJC18 OGG:3000203228 Bin Zhao, Yue Liu, Oliver He ALSFTD FTDALS WEB: http://www.ncbi.nlm.nih.gov/gene C9orf72 chromosome 9 open reading frame 72 203228 9p21.2 9606 9 Official from a nomenclature committee GO_0005515 (EC: IPI); GO_0005615 (EC: IDA); GO_0005634 (EC: IDA); GO_0005764 (EC: IDA); GO_0005768 (EC: IDA); GO_0005776 (EC: IDA); GO_0006897 (EC: IMP); GO_0006914 (EC: IMP); GO_0008219 (EC: IEA); GO_0017137 (EC: IDA) PMID: 11015796; 12477932; 12672552; 14702039; 15164053; 15489334; 16495328; 19322201; 19734901; 20301623; 20423481; 20562461; 20801717; 20801718; 21832049; 21890473; 21944778; 21944779; 22083254; 22181065; 22216764; 22228244; 22300873; 22300876; 22305801; 22343411; 22344582; 22366791; 22366792; 22366793; 22366794; 22366795; 22399792; 22399793; 22406228; 22410647; 22418734; 22426854; 22445326; 22459598; 22483864; 22487746; 22499346; 22502998; 22550220; 22564974; 22571983; 22650353; 22673113; 22678362; 22692064; 22702520; 22708871; 22721568; 22727276; 22732773; 22739338; 22742426; 22766072; 22766732; 22807188; 22815561; 22840558; 22843265; 22875086; 22875087; 22936364; 22959728; 22964910; 22964911; 22985429; 23012445; 23035801; 23036583; 23063644; 23084342; 23088937; 23100398; 23107433; 23111906; 23116878; 23117491; 23160421; 23254636; 23261768; 23264878; 23273600; 23284068; 23338682; 23352322; 23381195; 23393093; 23413259; 23421625; 23423380; 23434116; 23435409; 23437264; 23463871; 23473366; 23551834; 23555189; 23558488; 23587638; 23588422; 23588498; 23597494; 23602568; 23731538; 23771489; 23870417; 23894576; 24011653; 24027057; 24077574; 24081456; 24170860; 24185425; 24212388; 24248382; 24363131; 24549040; 24598541 chromosome 9 open reading frame 72 Ensembl:ENSG00000147894 HGNC:28337 HPRD:12975 MIM:614260 Vega:OTTHUMG00000019716 Other designations: protein C9orf72 C9orf72 OGG:3000219931 Bin Zhao, Yue Liu, Oliver He SHEP10 TPC2 WEB: http://www.ncbi.nlm.nih.gov/gene TPCN2 two pore segment channel 2 219931 11q13.3 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0005245 (EC: ISS); GO_0005515 (EC: IPI); GO_0005765 (EC: IDA, PMID: 19387438); GO_0005765 (EC: TAS); GO_0006874 (EC: IDA, PMID: 19387438); GO_0006939 (EC: ISS); GO_0010008 (EC: IDA, PMID: 19620632); GO_0016021 (EC: IEA); GO_0019901 (EC: IPI); GO_0034220 (EC: TAS); GO_0042802 (EC: IPI); GO_0051209 (EC: IEA); GO_0055085 (EC: TAS); GO_0072345 (EC: IDA, PMID: 19387438) PMID: 12477932; 14702039; 15203218; 15342556; 15489334; 16382101; 16554811; 18488028; 19387438; 19620632; 20495006; 20585627; 20720007; 23077736; 24250222 two pore segment channel 2 HGNC:20820 HPRD:18218 MIM:612163 Other designations: two pore calcium channel protein 2|two-pore calcium channel protein 2|voltage-dependent calcium channel protein TPC2 TPCN2 OGG:3000246175 Bin Zhao, Yue Liu, Oliver He CCR4b WEB: http://www.ncbi.nlm.nih.gov/gene CNOT6L CCR4-NOT transcription complex, subunit 6-like 246175 4q13.3 9606 4 Official from a nomenclature committee GO_0000288 (EC: TAS); GO_0000289 (EC: TAS); GO_0004535 (EC: TAS); GO_0005515 (EC: IPI, PMID: 17452450); GO_0005634 (EC: IDA); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0006351 (EC: IEA); GO_0006355 (EC: IEA); GO_0006417 (EC: IEA); GO_0008284 (EC: IMP); GO_0010467 (EC: TAS); GO_0010606 (EC: IMP); GO_0016070 (EC: TAS); GO_0016071 (EC: TAS); GO_0030014 (EC: IDA, PMID: 19558367); GO_0031047 (EC: IEA); GO_0046872 (EC: IEA); GO_0061157 (EC: IEA); GO_0090503 (EC: TAS) PMID: 14702039; 16344560; 17353931; 17452450; 18377426; 19558367; 20211142; 20360068; 20379614; 20628353; 20818722; 21233283; 23591815 CCR4-NOT transcription complex, subunit 6-like Ensembl:ENSG00000138767 HGNC:18042 HPRD:10841 Vega:OTTHUMG00000160832 Other designations: CCR4-NOT transcription complex subunit 6-like|carbon catabolite repressor protein 4 homolog B CNOT6L OGG:3000253314 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene EIF4E1B eukaryotic translation initiation factor 4E family member 1B 253314 5q35.2 9606 5 GO_0003743 (EC: IEA); GO_0005737 (EC: IEA); GO_0005845 (EC: ISS); GO_0006417 (EC: IEA) PMID:8889548; 14702039; 15372022; 16191198; 16344560 eukaryotic translation initiation factor 4E family member 1B Other designations: eukaryotic translation initiation factor 4E type 1B EIF4E1B OGG:3000253935 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene ANGPTL5 angiopoietin-like 5 253935 UNQ5795/PRO19600 11q22.1 9606 11 GO_0005576 (EC: IEA) PMID:12477932; 12624729; 12975309; 15489334; 21559522 angiopoietin-like 5 Other designations: angiopoietin-like protein 5|angiopoietin-related protein 5 ANGPTL5 OGG:3000257019 Bin Zhao, Yue Liu, Oliver He 4.1O EPB41L4O EPB41LO P410 WEB: http://www.ncbi.nlm.nih.gov/gene FRMD3 FERM domain containing 3 257019 RP11-439K3.2 9q21.32 9606 9 Official from a nomenclature committee GO_0005737 (EC: IEA); GO_0005856 (EC: IEA); GO_0008092 (EC: IEA); GO_0016021 (EC: IEA); GO_0019898 (EC: IEA) PMID: 8125298; 12477932; 12601556; 14702039; 17260017; 19252134; 20379614; 20460425; 21698141; 23434934 FERM domain containing 3 Ensembl:ENSG00000172159 HGNC:24125 HPRD:07402 MIM:607619 Vega:OTTHUMG00000020103 Other designations: FERM domain-containing protein 3|band 4.1-like protein 4|band 4.1-like protein 4O|ovary type protein 4.1|protein 4.1O FRMD3 OGG:3000260293 Bin Zhao, Yue Liu, Oliver He CYPIVX1 WEB: http://www.ncbi.nlm.nih.gov/gene CYP4X1 cytochrome P450, family 4, subfamily X, polypeptide 1 260293 RP11-184J23.1 1p33|1 9606 1 GO_0005506 (EC: IEA); GO_0005789 (EC: IEA); GO_0016021 (EC: IEA); GO_0020037 (EC: IEA); GO_0070330 (EC: IEA) PMID:12176035; 12477932; 12975309; 14702039; 15128046; 15489334; 15797250; 21890473 cytochrome P450, family 4, subfamily X, polypeptide 1 Ensembl:ENSG00000186377 HGNC:20244 HPRD:13110 MIM:614999 Vega:OTTHUMG00000008017 Other designations: cytochrome P450 4X1 CYP4X1 OGG:3000283131 Bin Zhao, Yue Liu, Oliver He LINC00084 NCRNA00084 TncRNA VINC WEB: http://www.ncbi.nlm.nih.gov/gene NEAT1 nuclear paraspeckle assembly transcript 1 (non-protein coding) 283131 11q13.1 20140408 9606 11 ncRNA Official from a nomenclature committee PMID: 9253601; 9858482; 11458881; 12565840; 17270048; 19217333; 19716791; 20881053; 21170033; 21532345; 22960638; 23362321; 23835137 nuclear paraspeckle assembly transcript 1 (non-protein coding) HGNC:30815 MIM:612769 NEAT1 OGG:3000283927 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene NUDT7 nudix (nucleoside diphosphate linked moiety X)-type motif 7 283927 16q23.1 9606 16 Official from a nomenclature committee GO_0000287 (EC: IEA); GO_0003674 (EC: ND); GO_0003986 (EC: ISS); GO_0005102 (EC: IPI); GO_0005777 (EC: ISS); GO_0008150 (EC: ND); GO_0009132 (EC: IEA); GO_0015938 (EC: ISS); GO_0030145 (EC: IEA); GO_0030515 (EC: ISS); GO_0046356 (EC: ISS); GO_0050072 (EC: ISS, Qualifier: NOT); GO_0050873 (EC: IEA) PMID: 11415433; 15146197; 15616553; 19844255; 20178365; 21145461; 23251661; 24250222 nudix (nucleoside diphosphate linked moiety X)-type motif 7 Other designations: peroxisomal coenzyme A diphosphatase NUDT7 NUDT7 OGG:3000284161 Bin Zhao, Yue Liu, Oliver He GDE4 WEB: http://www.ncbi.nlm.nih.gov/gene GDPD1 glycerophosphodiester phosphodiesterase domain containing 1 284161 17q22 9606 17 Official from a nomenclature committee GO_0005737 (EC: IEA); GO_0006071 (EC: IEA); GO_0006629 (EC: IEA); GO_0008889 (EC: IEA); GO_0016021 (EC: IEA); GO_0046872 (EC: IEA) PMID: 12477932; 14612981; 14702039; 15489334; 17690467; 18991142; 21139048; 21890473; 21906983; 24250222 glycerophosphodiester phosphodiesterase domain containing 1 Ensembl:ENSG00000153982 HGNC:20883 HPRD:08223 Vega:OTTHUMG00000179376 Other designations: glycerophosphodiester phosphodiesterase 4|glycerophosphodiester phosphodiesterase domain-containing protein 1 GDPD1 OGG:3000284541 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CYP4A22 cytochrome P450, family 4, subfamily A, polypeptide 22 284541 RP1-18D14.1 1p33 9606 1 GO_0005506 (EC: IEA); GO_0005789 (EC: IEA); GO_0018685 (EC: IEA); GO_0020037 (EC: IEA); GO_0052869 (EC: IEA) PMID:10860550; 12464262; 12477932; 15128046; 15611369; 20079672; 21820496 cytochrome P450, family 4, subfamily A, polypeptide 22 Other designations: CYPIVA22|cytochrome P450 4A22|cytochrome P450 4A22K|fatty acid omega-hydroxylase|lauric acid omega-hydroxylase CYP4A22 OGG:3000285126 Bin Zhao, Yue Liu, Oliver He CSP-gamma WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC5G DnaJ (Hsp40) homolog, subfamily C, member 5 gamma 285126 2p23.3 9606 2 GO_0016020 (EC: IEA) PMID:12477932; 14702039; 15489334 DnaJ (Hsp40) homolog, subfamily C, member 5 gamma Ensembl:ENSG00000163793 HGNC:24844 HPRD:07108 MIM:613946 Vega:OTTHUMG00000097079 Other designations: cysteine string protein-gamma|dnaJ homolog subfamily C member 5G|gamma cysteine string protein|gamma-CSP|gamma-cysteine string protein DNAJC5G OGG:3000285440 Bin Zhao, Yue Liu, Oliver He BCD CYP4AH1 WEB: http://www.ncbi.nlm.nih.gov/gene CYP4V2 cytochrome P450, family 4, subfamily V, polypeptide 2 285440 UNQ2560 4q35.2 9606 4 GO_0004497 (EC: IEA); GO_0005506 (EC: IEA); GO_0005789 (EC: IEA); GO_0007601 (EC: IEA); GO_0010430 (EC: IDA, PMID:19661213); GO_0016021 (EC: IEA); GO_0016705 (EC: IEA); GO_0020037 (EC: IEA); GO_0050896 (EC: IEA) PMID:11001583; 12477932; 12975309; 14702039; 15042513; 15128046; 15489334; 15860296; 16030350; 16088246; 16179904; 16186368; 17013694; 17249554; 17962476; 18349091; 19278955; 19508456; 19583818; 19661213; 20205591; 20379614; 21385027; 21540472; 21565171; 21850171; 21892605; 21988832; 22497028; 22605929; 22693542; 22916037; 23221965; 23242590; 23503679; 23538635 cytochrome P450, family 4, subfamily V, polypeptide 2 HGNC:23198 HPRD:16777 MIM:608614 Other designations: cytochrome P450 4V2 CYP4V2 OGG:3000317649 Bin Zhao, Yue Liu, Oliver He eIF-4E3 eIF4E-3 WEB: http://www.ncbi.nlm.nih.gov/gene EIF4E3 eukaryotic translation initiation factor 4E family member 3 317649 3p14 9606 3 GO_0003743 (EC: IEA); GO_0005829 (EC: TAS); GO_0005845 (EC: ISS); GO_0006417 (EC: IEA); GO_0019221 (EC: TAS) PMID:12477932; 15153109; 16344560; 19322201; 20434207; 23431134; 23587918 eukaryotic translation initiation factor 4E family member 3 Ensembl:ENSG00000163412 HGNC:31837 HPRD:10687 MIM:609896 Other designations: eukaryotic translation initiation factor 4E type 3 EIF4E3 OGG:3000319118 Bin Zhao, Yue Liu, Oliver He EIF4BP WEB: http://www.ncbi.nlm.nih.gov/gene EIF4BP1 eukaryotic translation initiation factor 4B pseudogene 1 319118 14q21.2 9606 14 Official from a nomenclature committee eukaryotic translation initiation factor 4B pseudogene 1 HGNC:19929 EIF4BP1 OGG:3000339761 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene CYP27C1 cytochrome P450, family 27, subfamily C, polypeptide 1 339761 2q14.3 9606 2 GO_0004497 (EC: IEA); GO_0005506 (EC: IEA); GO_0016020 (EC: IEA); GO_0016705 (EC: IEA); GO_0020037 (EC: IEA) PMID:12477932; 15128046; 20707712; 21890473 cytochrome P450, family 27, subfamily C, polypeptide 1 Other designations: cytochrome P450 27C1|cytochrome P450, family 27, subfamily C, polypeptide 13 CYP27C1 OGG:3000340485 Bin Zhao, Yue Liu, Oliver He ALKCDase2 ASAH3L WEB: http://www.ncbi.nlm.nih.gov/gene ACER2 alkaline ceramidase 2 340485 RP11-363E7.1 9p22.1 9606 9 Official from a nomenclature committee GO_0000139 (EC: TAS); GO_0001953 (EC: IDA, PMID: 18945876); GO_0005794 (EC: IDA, PMID: 16940153); GO_0006665 (EC: TAS); GO_0006672 (EC: IEA); GO_0006919 (EC: IMP); GO_0008284 (EC: IDA, PMID: 16940153); GO_0010942 (EC: IMP); GO_0017040 (EC: IDA, PMID: 16940153); GO_0030148 (EC: TAS); GO_0030173 (EC: IDA); GO_0032526 (EC: IDA, PMID: 18945876); GO_0033629 (EC: IDA, PMID: 18945876); GO_0035690 (EC: IEP); GO_0044281 (EC: TAS); GO_0046512 (EC: IDA, PMID: 16940153); GO_0071633 (EC: IDA); GO_0090285 (EC: IMP) PMID: 12477932; 15164053; 15489334; 15498874; 16940153; 18945876; 20089856; 20379614; 20628055 alkaline ceramidase 2 HGNC:23675 HPRD:16512 MIM:613492 Other designations: alkCDase 2|alkaline CDase 2|ceramide hydrolase|haCER2 ACER2 OGG:3000340665 Bin Zhao, Yue Liu, Oliver He FFDD4 WEB: http://www.ncbi.nlm.nih.gov/gene CYP26C1 cytochrome P450, family 26, subfamily C, polypeptide 1 340665 10q23.33 9606 10 GO_0001972 (EC: IDA, PMID:14532297); GO_0005506 (EC: IEA); GO_0005789 (EC: TAS); GO_0006766 (EC: TAS); GO_0006805 (EC: TAS); GO_0007417 (EC: ISS); GO_0008401 (EC: IDA, PMID:14532297); GO_0009952 (EC: ISS); GO_0014032 (EC: ISS); GO_0016021 (EC: IEA); GO_0020037 (EC: IEA); GO_0034653 (EC: IDA, PMID:14532297); GO_0044281 (EC: TAS); GO_0048284 (EC: ISS); GO_0048387 (EC: NAS, PMID:14532297); GO_0055114 (EC: IDA, PMID:14532297) PMID:14532297; 15128046; 15164054; 16385451; 16933217; 19703508; 21139048; 21850183; 23161670 cytochrome P450, family 26, subfamily C, polypeptide 1 Ensembl:ENSG00000187553 HGNC:20577 HPRD:12230 MIM:608428 Vega:OTTHUMG00000018766 Other designations: cytochrome P450 26C1 CYP26C1 OGG:3000347252 Bin Zhao, Yue Liu, Oliver He IGFBP-RP4 IGFBPRP4 bA113O24.1 WEB: http://www.ncbi.nlm.nih.gov/gene IGFBPL1 insulin-like growth factor binding protein-like 1 347252 9p13.1 9606 9 GO_0001558 (EC: IEA); GO_0005520 (EC: IEA); GO_0005576 (EC: IEA) PMID:14702039; 15845387; 17634530; 17884839; 24250222 insulin-like growth factor binding protein-like 1 HGNC:20081 HPRD:17138 MIM:610413 Other designations: IGFBP-related protein 10|insulin-like growth factor binding protein related protein 4|insulin-like growth factor-binding protein-like 1|insulin-like growth factor-binding-related protein 4 IGFBPL1 OGG:3000348158 Bin Zhao, Yue Liu, Oliver He ACSM2 HXMA WEB: http://www.ncbi.nlm.nih.gov/gene ACSM2B acyl-CoA synthetase medium-chain family member 2B 348158 HYST1046 16p12.3 20140408 9606 16 protein-coding Official from a nomenclature committee GO_0003674 (EC: ND); GO_0005524 (EC: IEA); GO_0005739 (EC: NAS, PMID: 19634011); GO_0005759 (EC: TAS); GO_0006631 (EC: IEA); GO_0006805 (EC: TAS); GO_0044281 (EC: TAS); GO_0046872 (EC: IEA); GO_0047760 (EC: IEA) PMID: 8884467; 8934636; 10434065; 11415461; 12616642; 15122652; 15221005; 16521160; 19634011; 20679960 acyl-CoA synthetase medium-chain family member 2B Ensembl:ENSG00000066813 HGNC:30931 HPRD:17124 MIM:614359 Vega:OTTHUMG00000131555 Other designations: acyl-CoA synthetase medium-chain family member 2|acyl-coenzyme A synthetase ACSM2B, mitochondrial|butyrate--CoA ligase 2B|butyryl-coenzyme A synthetase 2B|middle-chain acyl-CoA synthetase 2B|xenobiotic/medium-chain fatty acid-CoA ligase HXM-A|xenobiotic/medium-chain fatty acid:CoA ligase ACSM2B OGG:3000348235 Bin Zhao, Yue Liu, Oliver He FAM33A WEB: http://www.ncbi.nlm.nih.gov/gene SKA2 spindle and kinetochore associated complex subunit 2 348235 17q22 20140408 9606 17 protein-coding Official from a nomenclature committee GO_0000278 (EC: TAS); GO_0000940 (EC: IDA, PMID: 17093495); GO_0005515 (EC: IPI, PMID: 17093495); GO_0005737 (EC: IDA); GO_0005829 (EC: TAS); GO_0005876 (EC: IDA, PMID: 17093495); GO_0007059 (EC: IMP, PMID: 19289083); GO_0007067 (EC: IMP, PMID: 19289083); GO_0008017 (EC: IDA, PMID: 19289083); GO_0031110 (EC: IDA, PMID: 19289083); GO_0051301 (EC: IMP, PMID: 17093495) PMID: 12477932; 14702039; 15489334; 16344560; 17093495; 17207965; 18583474; 19156129; 19289083; 20470754; 21988832; 22371557; 22483620; 23666239 spindle and kinetochore associated complex subunit 2 Ensembl:ENSG00000182628 HGNC:28006 HPRD:13306 Vega:OTTHUMG00000179361 Other designations: family with sequence similarity 33, member A|spindle and KT (kinetochore) associated 2|spindle and kinetochore-associated protein 2 SKA2 OGG:3000353322 Bin Zhao, Yue Liu, Oliver He Lrp2bp WEB: http://www.ncbi.nlm.nih.gov/gene ANKRD37 ankyrin repeat domain 37 353322 4q35.1 9606 4 Official from a nomenclature committee GO_0005634 (EC: IEA); GO_0005737 (EC: IEA) PMID: 12477932; 15489334; 15809689; 19491311; 21890473; 24250222 ankyrin repeat domain 37 Ensembl:ENSG00000186352 HGNC:29593 HPRD:17461 Vega:OTTHUMG00000160459 Other designations: ankyrin repeat domain-containing protein 37|hLrp2bp|low density lipoprotein receptor-related protein binding protein|low-density lipoprotein receptor-related protein 2-binding protein ANKRD37 OGG:3000374383 Bin Zhao, Yue Liu, Oliver He B7-H6 B7H6 DKFZp686O24166 WEB: http://www.ncbi.nlm.nih.gov/gene NCR3LG1 natural killer cell cytotoxicity receptor 3 ligand 1 374383 11p15.1 20140408 9606 11 protein-coding Official from a nomenclature committee GO_0005198 (EC: IEA); GO_0005886 (EC: IEA); GO_0016021 (EC: IEA); GO_0019028 (EC: IEA) PMID: 12477932; 18187620; 19528259; 21422170; 21444796; 21875946; 21877119; 23066150; 23687088 natural killer cell cytotoxicity receptor 3 ligand 1 Ensembl:ENSG00000188211 HGNC:42400 HPRD:16820 MIM:613714 Vega:OTTHUMG00000165913 Other designations: B7 homolog 6|natural cytotoxicity triggering receptor 3 ligand 1|putative Ig-like domain-containing protein DKFZp686O24166/DKFZp686I21167 NCR3LG1 OGG:3000374407 Bin Zhao, Yue Liu, Oliver He RSPH16A TSARG5 TSARG6 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB13 DnaJ (Hsp40) homolog, subfamily B, member 13 374407 11q13.4 9606 11 GO_0003674 (EC: ND); GO_0005575 (EC: ND); GO_0006457 (EC: IEA); GO_0051082 (EC: IEA) PMID:12673577; 14702039; 14970903; 20677014 DnaJ (Hsp40) homolog, subfamily B, member 13 Ensembl:ENSG00000187726 HGNC:30718 HPRD:15573 MIM:610263 Vega:OTTHUMG00000168093 Other designations: 1700014P03Rik|DnaJ (Hsp40) related, subfamily B, member 13|DnaJ-like protein|dnaJ homolog subfamily B member 13|radial spoke 16 homolog A|testis and spermatogenesis cell-related protein 6|testis spermatocyte apoptosis-related gene 6 protein|testis spermatogenesis apoptosis-related gene 3 protein|testis spermatogenesis apoptosis-related gene 6 protein|testis spermatogenesis apoptosis-related protein 6 DNAJB13 OGG:3000387103 Bin Zhao, Yue Liu, Oliver He C6orf173 CENP-W CUG2 WEB: http://www.ncbi.nlm.nih.gov/gene CENPW centromere protein W 387103 6q22.32 9606 6 Official from a nomenclature committee GO_0000278 (EC: IMP); GO_0000775 (EC: IDA, PMID: 19533040); GO_0000776 (EC: IDA); GO_0000777 (EC: IEA); GO_0003677 (EC: IEA); GO_0005515 (EC: IPI, PMID: 19070575); GO_0005730 (EC: IEA); GO_0007059 (EC: IMP); GO_0007059 (EC: TAS, PMID: 19533040); GO_0007067 (EC: IEA); GO_0016363 (EC: IEA); GO_0034080 (EC: TAS, PMID: 19533040); GO_0046982 (EC: IEA); GO_0051276 (EC: IMP); GO_0051382 (EC: IMP) PMID: 12477932; 17610844; 18391951; 19070575; 19266077; 19430480; 19533040; 20075984; 20180024; 20546612; 20648695; 20846217; 20881960; 21102462; 21695110; 22002061; 22131368; 22504418; 23306614; 23563607; 23926101 centromere protein W Ensembl:ENSG00000203760 HGNC:21488 HPRD:16660 MIM:611264 Vega:OTTHUMG00000015518 Other designations: cancer-up-regulated gene 2 protein|cancer-upregulated gene 2 CENPW OGG:3000387755 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene INSC inscuteable homolog (Drosophila) 387755 11p15.2 9606 11 Official from a nomenclature committee GO_0000132 (EC: IEA); GO_0005737 (EC: IEA); GO_0007399 (EC: IEA); GO_0045177 (EC: IEA); GO_0060487 (EC: IEA) PMID: 12469229; 12477932; 16458856; 20065032; 20379614; 22074847; 22219177; 22889411; 22977735; 23251661; 23667675 inscuteable homolog (Drosophila) Other designations: inscuteable spindle orientation adaptor protein|protein inscuteable homolog INSC OGG:3000390756 olfactory receptor family 3 subfamily A member 4 pseudogene NCBI-Human-GeneID:390756 OR3A4 NCBI-Human-GeneID:390756 https://www.ncbi.nlm.nih.gov/gene/390756 OGG:3000406925 9606 NCBI-Human-GeneID:406925 MIR135A1 NCBI-Human-GeneID:406925 https://www.ncbi.nlm.nih.gov/gene/406925 OGG:3000406926 9606 NCBI-Human-GeneID:406926 MIR135A2 NCBI-Human-GeneID:406926 https://www.ncbi.nlm.nih.gov/gene/406926 OGG:3000406942 9606 NCBI-Human-GeneID:406942 MIR150 NCBI-Human-GeneID:406942 https://www.ncbi.nlm.nih.gov/gene/406942 OGG:3000414061 Bin Zhao, Yue Liu, Oliver He HCG3 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJB3 DnaJ (Hsp40) homolog, subfamily B, member 3 414061 2q37 9606 2 PMID:12477932; 15891074; 16189514; 17207965; 21890473; 21906983; 21963094; 23000965; 23824909 DnaJ (Hsp40) homolog, subfamily B, member 3 HGNC:32397 HPRD:13638 Other designations: dnaJ homolog subfamily B member 3 DNAJB3 OGG:3000415116 Bin Zhao, Yue Liu, Oliver He pim-3 WEB: http://www.ncbi.nlm.nih.gov/gene PIM3 pim-3 oncogene 415116 CITF22-49E9.1 22q13 20140408 9606 22 protein-coding Official from a nomenclature committee GO_0004674 (EC: IDA, PMID: 18593906); GO_0005515 (EC: IPI, PMID: 17270021); GO_0005524 (EC: IEA); GO_0005737 (EC: IEA); GO_0006468 (EC: IDA, PMID: 18593906); GO_0006915 (EC: IEA); GO_0007049 (EC: IEA); GO_0007346 (EC: IMP, PMID: 17270021); GO_0016572 (EC: IEA); GO_0043066 (EC: IMP, PMID: 17270021); GO_0046777 (EC: IEA); GO_0061179 (EC: ISS) PMID: 10713710; 12477932; 12798037; 15199164; 15489334; 15540201; 16403219; 17270021; 18593906; 19154409; 19266083; 19624871; 20101231; 20939820; 21187426; 21297633; 21646687; 21668797; 21870113; 21906983; 21963094; 22053931; 22939624; 23209281; 23760491; 23845873 pim-3 oncogene Ensembl:ENSG00000198355 HGNC:19310 HPRD:15137 MIM:610580 Vega:OTTHUMG00000150290 Other designations: serine/threonine kinase Pim-3|serine/threonine-protein kinase pim-3 PIM3 OGG:3000440275 Bin Zhao, Yue Liu, Oliver He GCN2 PVOD2 WEB: http://www.ncbi.nlm.nih.gov/gene EIF2AK4 eukaryotic translation initiation factor 2 alpha kinase 4 440275 15q15.1 9606 15 GO_0004674 (EC: ISS); GO_0004694 (EC: ISS); GO_0005524 (EC: IEA); GO_0006446 (EC: ISS); GO_0006468 (EC: ISS); GO_0009267 (EC: IEA); GO_0017148 (EC: IEA); GO_0022626 (EC: ISS); GO_0030968 (EC: IEA); GO_0042803 (EC: IEA); GO_0043558 (EC: IEA) PMID:10504407; 10718198; 12215525; 12477932; 14671302; 14702039; 15489334; 15761153; 15892049; 16121183; 16601681; 17081983; 17192257; 17202131; 17276353; 17620599; 18287093; 19029902; 19586904; 19615732; 20168091; 20473272; 20551969; 21076179; 21113813; 21139048; 21203563; 22301437; 22327514; 22435535; 22896630; 22969067; 23110064; 23129244; 23216249; 23354059; 23417324; 23908598; 24019515; 24113185; 24292273; 24310610 eukaryotic translation initiation factor 2 alpha kinase 4 Ensembl:ENSG00000128829 HGNC:19687 HPRD:18447 MIM:609280 Vega:OTTHUMG00000172403 Other designations: GCN2 eIF2alpha kinase|GCN2-like protein|eukaryotic translation initiation factor 2-alpha kinase 4|general control nonderepressible 2 EIF2AK4 OGG:3000441027 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene TMEM150C transmembrane protein 150C 441027 4q21.22 20140408 9606 4 protein-coding Official from a nomenclature committee GO_0016021 (EC: IEA) PMID: 12477932; 14702039; 21906983 transmembrane protein 150C TMEM150C OGG:3000548645 Bin Zhao, Yue Liu, Oliver He bA16L21.2.1 WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC25 DnaJ (Hsp40) homolog, subfamily C , member 25 548645 9q31.3 9606 9 GO_0016021 (EC: IEA) PMID:12477932; 14702039; 24250222 DnaJ (Hsp40) homolog, subfamily C , member 25 Ensembl:ENSG00000059769 HGNC:34187 HPRD:18685 Vega:OTTHUMG00000020491 Other designations: DnaJ-like protein|dnaJ homolog subfamily C member 25 DNAJC25 OGG:3000552891 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene DNAJC25-GNG10 DNAJC25-GNG10 readthrough 552891 9q31.3 9606 9 PMID:8889548; 12477932; 14702039; 15164053; 15489334; 20967262 DNAJC25-GNG10 readthrough Other designations: DNAJC25-GNG10 protein|DNAJC25-GNG10 readthrough transcript DNAJC25-GNG10 OGG:3000641371 Bin Zhao, Yue Liu, Oliver He ACH2 CTE-1 LACH2 WEB: http://www.ncbi.nlm.nih.gov/gene ACOT1 acyl-CoA thioesterase 1 641371 14q24.3 9606 14 GO_0000038 (EC: IDA, PMID:16940157); GO_0001676 (EC: IDA, PMID:16940157); GO_0005829 (EC: IDA, PMID:16940157); GO_0006637 (EC: IDA, PMID:16940157); GO_0016290 (EC: IEA); GO_0047617 (EC: IDA, PMID:16940157) PMID:12477932; 16103133; 16940157; 18029348; 20736409; 21890473; 21963094; 21987572; 22939629 acyl-CoA thioesterase 1 Ensembl:ENSG00000184227 HGNC:33128 MIM:614313 Vega:OTTHUMG00000171607 Other designations: CTE-I|CTE-Ib|acyl-coenzyme A thioesterase 1|inducible cytosolic acyl-coenzyme A thioester hydrolase|long chain acyl-CoA hydrolase|long chain acyl-CoA thioester hydrolase ACOT1 OGG:3000641372 Bin Zhao, Yue Liu, Oliver He C14orf42 c14_5530 WEB: http://www.ncbi.nlm.nih.gov/gene ACOT6 acyl-CoA thioesterase 6 641372 14q24.3 9606 14 GO_0005829 (EC: IDA, PMID:16940157); GO_0016787 (EC: IEA) PMID:12477932; 16103133; 16940157; 21822266 acyl-CoA thioesterase 6 Ensembl:ENSG00000205669 HGNC:33159 MIM:614267 Vega:OTTHUMG00000171609 Other designations: putative acyl-CoA thioesterase 6|putative acyl-coenzyme A thioesterase 6 ACOT6 OGG:3000728689 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene EIF3CL eukaryotic translation initiation factor 3, subunit C-like 728689 16p11.2 9606 16 GO_0001731 (EC: IEA); GO_0003743 (EC: IEA); GO_0005852 (EC: IEA); GO_0006446 (EC: IEA); GO_0016282 (EC: IEA); GO_0031369 (EC: IEA); GO_0033290 (EC: IEA) PMID:8995409; 10493829; 10504338; 12477932; 12588972; 14519125; 14702039; 15302935; 15489334; 15703437; 16083285; 16097034; 16286006; 16322461; 16766523; 16964243; 17081983; 17287340; 17322308; 17468741; 17581632; 18187866; 18599441; 18669648; 20360068; 20972266; 21145461; 21890473; 21906983; 21963094; 21987572; 22505724; 22863883; 23000965; 23463506; 23862649 eukaryotic translation initiation factor 3, subunit C-like Other designations: eIF3 p110|eIF3c|eukaryotic translation initiation factor 3 subunit 8|eukaryotic translation initiation factor 3 subunit C|eukaryotic translation initiation factor 3 subunit C-like protein|eukaryotic translation initiation factor 3, subunit 8, 110kDa-like EIF3CL OGG:3000729230 Bin Zhao, Yue Liu, Oliver He CC-CKR-2 CCR-2 CCR2A CCR2B CD192 CKR2 CKR2A CKR2B CMKBR2 MCP-1-R WEB: http://www.ncbi.nlm.nih.gov/gene CCR2 chemokine (C-C motif) receptor 2 729230 hCG_14621 3p21.31 9606 3 GO_0001974 (EC: ISS); GO_0002407 (EC: TAS, PMID:16621978); GO_0002827 (EC: ISS); GO_0002829 (EC: ISS); GO_0004950 (EC: TAS, PMID:10623817); GO_0005737 (EC: IDA, PMID:15995708); GO_0005829 (EC: ISS); GO_0005886 (EC: IDA, PMID:15995708); GO_0005886 (EC: TAS); GO_0005887 (EC: TAS, PMID:8146186); GO_0006874 (EC: ISS); GO_0006935 (EC: TAS, PMID:10623817); GO_0006954 (EC: IEA); GO_0006955 (EC: TAS, PMID:10751368); GO_0006968 (EC: TAS, PMID:10201901); GO_0007194 (EC: TAS, PMID:8995400); GO_0007204 (EC: TAS, PMID:9548499); GO_0007259 (EC: TAS, PMID:9670957); GO_0009611 (EC: TAS, PMID:8146186); GO_0010574 (EC: ISS); GO_0010820 (EC: ISS); GO_0016021 (EC: TAS, PMID:8530354); GO_0016032 (EC: IEA); GO_0016493 (EC: IEA); GO_0016525 (EC: ISS); GO_0019221 (EC: IDA, PMID:15995708); GO_0019725 (EC: ISS); GO_0030425 (EC: ISS); GO_0031727 (EC: IDA, PMID:15995708); GO_0032729 (EC: ISS); GO_0032743 (EC: ISS); GO_0035705 (EC: ISS); GO_0042535 (EC: ISS); GO_0042803 (EC: ISS); GO_0043025 (EC: ISS); GO_0043204 (EC: ISS); GO_0043310 (EC: ISS); GO_0045087 (EC: TAS); GO_0046641 (EC: ISS); GO_0048471 (EC: ISS); GO_0050729 (EC: ISS); GO_0050870 (EC: ISS); GO_0070098 (EC: ISS); GO_0090026 (EC: IDA, PMID:18587271); GO_0090026 (EC: ISS); GO_0090265 (EC: ISS); GO_2000439 (EC: ISS); GO_2000451 (EC: ISS); GO_2000464 (EC: IDA, PMID:12271471); GO_2000473 (EC: ISS) PMID:2834384; 8048929; 8146186; 8530354; 8884276; 8995400; 9058802; 9115216; 9143512; 9195948; 9225989; 9252328; 9287323; 9501202; 9548499; 9653051; 9662369; 9670957; 9710230; 9736741; 9789057; 9886417; 10201901; 10479649; 10486323; 10529171; 10623817; 10741397; 10751368; 10877489; 10888629; 10985245; 11023492; 11046064; 11115360; 11120855; 11175286; 11181995; 11264152; 11350939; 11377705; 11385319; 11468722; 11470772; 11477473; 11485615; 11500196; 11590385; 11596075; 11694103; 11696224; 11709782; 11729511; 11752157; 11756347; 11779135; 11782014; 11804551; 11856781; 11860793; 11860823; 11873083; 11898620; 11958683; 11964548; 11988632; 12001056; 12010355; 12032878; 12070001; 12078856; 12079277; 12082592; 12149192; 12192431; 12201365; 12215924; 12239249; 12271471; 12374865; 12399623; 12403355; 12426226; 12436194; 12445801; 12447757; 12469616; 12477932; 12556692; 12557141; 12571520; 12584049; 12651900; 12654703; 12680626; 12719858; 12837756; 12853162; 12853745; 12882757; 12884524; 12889997; 12913933; 13678532; 14533004; 14533983; 14624371; 14644039; 14647058; 14742283; 14981141; 15053339; 15076247; 15086346; 15086398; 15135805; 15140377; 15192276; 15230854; 15236615; 15257681; 15319853; 15362666; 15458467; 15465089; 15466648; 15472820; 15488313; 15489334; 15575507; 15579296; 15585333; 15602133; 15611878; 15639953; 15721423; 15750046; 15754978; 15769362; 15793370; 15863470; 15929697; 15976001; 15980693; 15992849; 15995708; 16033640; 16055130; 16095529; 16123688; 16140745; 16196460; 16206074; 16207551; 16261210; 16286054; 16286055; 16305685; 16314800; 16320328; 16323127; 16344560; 16356504; 16415174; 16426243; 16461193; 16478397; 16480760; 16485782; 16524739; 16529059; 16598837; 16621978; 16631114; 16641997; 16733654; 16781696; 16831471; 16858645; 16865553; 16903979; 16908772; 16950632; 17060059; 17091019; 17094383; 17135764; 17216598; 17240189; 17295203; 17298432; 17355643; 17361671; 17364026; 17395051; 17413295; 17417600; 17426779; 17428349; 17464174; 17465499; 17482150; 17499741; 17504503; 17558413; 17560067; 17596666; 17604544; 17615573; 17653321; 17664883; 17672867; 17688234; 17703277; 17703412; 17704101; 17715128; 17786209; 17845302; 17917677; 17934338; 17989610; 18055544; 18060801; 18093816; 18096169; 18164016; 18172114; 18186797; 18197127; 18240029; 18306985; 18332000; 18391751; 18513341; 18577758; 18587271; 18615095; 18633131; 18676680; 18763111; 18829011; 18845960; 18846510; 18855658; 18928397; 18936436; 18974840; 18977759; 18996288; 19002595; 19017998; 19028820; 19032065; 19037908; 19055601; 19064579; 19082218; 19098363; 19124913; 19131662; 19170196; 19196047; 19225544; 19258923; 19263529; 19411748; 19420105; 19433914; 19465829; 19479237; 19506371; 19520154; 19526283; 19527467; 19535619; 19559392; 19578796; 19625176; 19643177; 19669591; 19692168; 19693089; 19720836; 19841162; 19904283; 19917610; 19942750; 19950235; 19958843; 19965779; 20017911; 20038229; 20066125; 20153665; 20181074; 20182805; 20190752; 20220260; 20231199; 20339010; 20364004; 20380698; 20411675; 20442634; 20449800; 20452482; 20483750; 20485444; 20503287; 20531015; 20536507; 20537184; 20603037; 20605053; 20628649; 20637631; 20673868; 20681057; 20726788; 20740585; 20808917; 20842059; 20947712; 21054877; 21091093; 21097527; 21097672; 21146687; 21148810; 21220372; 21264360; 21322034; 21348591; 21396623; 21429204; 21440726; 21450101; 21461583; 21527853; 21570337; 21602126; 21667221; 21682549; 21868018; 21883707; 21890375; 22026334; 22041342; 22081934; 22086059; 22159219; 22183310; 22197827; 22218121; 22226505; 22276574; 22285384; 22479344; 22554651; 22607625; 22612293; 22615942; 22685564; 22752804; 22815949; 22842622; 22909007; 22927430; 23007133; 23041556; 23057571; 23090289; 23185481; 23185512; 23251661; 23298254; 23325742; 23374597; 23376609; 23408426; 23454776; 23612252; 23632061; 23657965; 23686489; 23880174; 24078580; 24128342 chemokine (C-C motif) receptor 2 Ensembl:ENSG00000121807 HGNC:1603 MIM:601267 Vega:OTTHUMG00000156466 Other designations: C-C chemokine receptor type 2|MCP-1 receptor|monocyte chemoattractant protein 1 receptor|monocyte chemotactic protein 1 receptor CCR2 OGG:3100133790 Bin Zhao, Yue Liu, Oliver He WEB: http://www.ncbi.nlm.nih.gov/gene 100133790 9606 NCBI-supplied PMID: 9334251; 22990020; 23316049 intestinal mucin-like MUC3 OGG:3100506742 Bin Zhao, Yue Liu, Oliver He CASP-12 CASP12P1 WEB: http://www.ncbi.nlm.nih.gov/gene CASP12 caspase 12 (gene/pseudogene) 100506742 UNQ9415 11q22.3 9606 11 GO_0004197 (EC: IBA); GO_0005737 (EC: IBA); GO_0030968 (EC: IEA); GO_0042981 (EC: IEA); GO_0050727 (EC: IBA, Qualifier: NOT); GO_0070059 (EC: IBA); GO_0072557 (EC: IBA, Qualifier: NOT); GO_0072559 (EC: IBA, Qualifier: NOT); GO_0097169 (EC: IBA, Qualifier: NOT); GO_0097194 (EC: IBA, Qualifier: NOT) PMID:9038361; 11278723; 11329013; 11943137; 12054529; 12975309; 14532116; 15033764; 15129283; 16532395; 16917906; 17574210; 18329614; 18332441; 18710920; 18791174; 19447924; 19721713; 20031604; 20041182; 20299359; 20299368; 20423816; 20577092; 20646990; 21706251; 21872999 caspase 12 (gene/pseudogene) Ensembl:ENSG00000204403 HGNC:19004 MIM:608633 Vega:OTTHUMG00000154965 Other designations: caspase 12 pseudogene 1|inactive caspase-12 CASP12 OGG:3100861540 Bin Zhao, Yue Liu, Oliver He CYP3A7-3AP1 CYP3A7.1L WEB: http://www.ncbi.nlm.nih.gov/gene 100861540 7q 9606 7 PMID:9847074; 11137287; 12853948; 15937338 CYP3A7-CYP3AP1 readthrough - CYP3A7-CYP3AP1 OGMS:0000014 A representation that is either the output of a clinical history taking or a physical examination or an image finding, or some combination thereof. clinical finding OGMS:0000073 The representation of a conclusion of a diagnostic process. diagnosis OMIT:0003800 A changing process in which cells become to have neoplastic quality. neoplastic cell Transformation PATO:0000011 A time quality inhering in a bearer by virtue of how long the bearer has existed. age (quality) A composite chromatic quality composed of hue, saturation and intensity parts. A composite chromatic quality composed of hue, saturation and intensity parts. PATO:0000020 colour relative color quality PATO:0000014 color (quality) PATO:0000014 A composite chromatic quality composed of hue, saturation and intensity parts. PATOC:GVG PATO:0000016 A scalar optical property that is the intensity, value or amount of perceived light. color intensity color brightness quality PATO:0000018 fluorescence A luminous flux quality inhering in a bearer by virtue of the bearer's emitting longer wavelength light following the absorption of shorter wavelength radiation; fluorescence is common with aromatic compounds with several rings joined together. fluorescence PATO:0000025 A single physical entity inhering in an bearer by virtue of the bearer's quantities or relative ratios of subparts composition PATO:0000039 A physical quality inhering in a bearer by virtue of the bearer's orientation in space. direction An organismal quality inhering in a bearer by virtue of the bearer's ability to undergo sexual reproduction in order to differentiate the individuals or types involved. An organismal quality inhering in a bearer by virtue of the bearer's ability to undergo sexual reproduction in order to differentiate the individuals or types involved. quality PATO:0000047 biological sex PATO:0000047 An organismal quality inhering in a bearer by virtue of the bearer's ability to undergo sexual reproduction in order to differentiate the individuals or types involved. MGED:MGED PATO:0000048 A physical quality inhering in a bearer by virtue of the bearer's resistance to pressure, being broken, or pierced hardness morphology A quality of a single physical entity inhering in the bearer by virtue of the bearer's size or shape or structure. A quality of a single physical entity inhering in the bearer by virtue of the bearer's size or shape or structure. quality PATO:0000051 morphology (quality) PATO:0000051 A quality of a single physical entity inhering in the bearer by virtue of the bearer's size or shape or structure. PATOC:GVG A morphological quality inhering in a bearer by virtue of the bearer's ratios of distances between its features (points, edges, surfaces and also holes etc). A morphological quality inhering in a bearer by virtue of the bearer's ratios of distances between its features (points, edges, surfaces and also holes etc). PATO:0001647 relational shape quality quality PATO:0000052 Shapes are invariant on size transformations. Shapes can be subdivided into 2D and 3D shapes, We can also make a distinction between shapes of complete self-connected objects, and shapes of parts of objects. shape (quality) PATO:0000052 A morphological quality inhering in a bearer by virtue of the bearer's ratios of distances between its features (points, edges, surfaces and also holes etc). PATOC:GVG A spatial quality inhering in a bearer by virtue of the bearer's exhibiting repetition of placement of its parts. A spatial quality inhering in a bearer by virtue of the bearer's exhibiting repetition of placement of its parts. PATO:0000132 PATO:0001565 distribution quality pattern PATO:0000060 spatial pattern PATO:0000060 A spatial quality inhering in a bearer by virtue of the bearer's exhibiting repetition of placement of its parts. PATOC:GVG PATO:0000068 qualitative property PATO:0000069 A quality inhering in a bearer by virtue of the whether the bearer differs from normal or average. normality (quality) PATO:0000070 The number of entities of this type that are part of the whole organism. quantity (property) PATO:0000078 A quality of a single process inhering in a bearer by virtue of the bearer's movement or variation characterized by the regular recurrence or alternation of different quantities or conditions. rhythm quality PATO:0000082 A rhythm quality inhering in a bearer by virtue of the repetitiveness of bearer's rhythm. persistence PATO:0000083 A quality that exists by virtue of being a particular point in the time of a cycle. phase PATO:0000117 A morphology quality inhering in a bearer by virtue of the bearer's physical magnitude. size PATO:0000119 A 1-D extent quality inhering in a bearer by virtue of the bearer's vertical dimension of extension. height PATO:0000122 A 1-D extent quality which is equal to the distance between two points. length PATO:0000125 A physical quality that inheres in a bearer by virtue of the proportion of the bearer's amount of matter. mass (quality) PATO:0000128 A physical attribute entity inhering in a bearer that has mass near a gravitational body. weight (quality) A morphological quality pertaining to the degree to which an object contains an opening, aperture, orifice or vent. A morphological quality pertaining to the degree to which an object contains an opening, aperture, orifice or vent. quality PATO:0000136 closure (quality) PATO:0000136 A morphological quality pertaining to the degree to which an object contains an opening, aperture, orifice or vent. PATOC:CJM PATOC:GVG PATO:0000140 A spatial quality inhering in a bearer by virtue of the bearer's being located toward the front of an organism relative to another entity. position PATO:0000141 A morphology quality inhering in a bearer by virtue of the bearer's relative position, shape, arrangements and connectivity of an organism's various parts; the pattern underlying its form. structure (quality) PATO:0000146 A physical attribure of the thermal energy of a system. temperature (quality) A morphologic quality inhering in a bearer by virtue of the bearer's relative size, organization and distribution of its surface elements or the representation or invention of the appearance of its surface; visual and tactile surface characteristics. A morphologic quality inhering in a bearer by virtue of the bearer's relative size, organization and distribution of its surface elements or the representation or invention of the appearance of its surface; visual and tactile surface characteristics. quality PATO:0000150 texture (quality) PATO:0000150 A morphologic quality inhering in a bearer by virtue of the bearer's relative size, organization and distribution of its surface elements or the representation or invention of the appearance of its surface; visual and tactile surface characteristics. PATOC:GVG PATO:0000165 A quality in which events occur in sequence. time quality PATO:0000169 An organismal quality inhering in a bearer or a population by virtue of the bearer's disposition to survive and develop normally or the number of surviving individuals in a given population. viability A reproductive quality inhering in a bearer by virtue of the bearer's initiating, sustaining, or supporting reproduction. A reproductive quality inhering in a bearer by virtue of the bearer's initiating, sustaining, or supporting reproduction. quality PATO:0000274 fertility (quality) PATO:0000274 A reproductive quality inhering in a bearer by virtue of the bearer's initiating, sustaining, or supporting reproduction. PATOC:GVG A reproductive quality inhering in the young of an animal by virtue of their number. A reproductive quality inhering in the young of an animal by virtue of their number. quality litter size PATO:0000276 brood size (quality) PATO:0000276 A reproductive quality inhering in the young of an animal by virtue of their number. PATOC:GVG A fertility quality of inhering in a male by virtue of the bearer's disposition to initiate, sustain, or support reproduction. A fertility quality of inhering in a male by virtue of the bearer's disposition to initiate, sustain, or support reproduction. quality PATO:0000279 male fertility (quality) PATO:0000279 A fertility quality of inhering in a male by virtue of the bearer's disposition to initiate, sustain, or support reproduction. PATOC:GVG PATO:0000308 An age which is relatively high. old (quality) PATO:0000309 An age which is relatively low. young (quality) PATO:0000322 A color hue with high wavelength of the long-wave end of the visible spectrum, evoked in the human observer by radiant energy with wavelengths of approximately 630 to 750 nanometers. red (quality) PATO:0000327 A color brightness which is relatively low. color brightness A spatial pattern inhering in a bearer by virtue of the bearer's magnitude of or the relationships between its repeated parts lack consistency. A spatial pattern inhering in a bearer by virtue of the bearer's magnitude of or the relationships between its repeated parts lack consistency. quality PATO:0000330 irregular spatial pattern (quality) PATO:0000330 A spatial pattern inhering in a bearer by virtue of the bearer's magnitude of or the relationships between its repeated parts lack consistency. PATOC:GVG A biological sex quality inhering in an individual or a population whose sex organs contain only male gametes. A biological sex quality inhering in an individual or a population whose sex organs contain only male gametes. quality PATO:0000384 male (quality) PATO:0000384 A biological sex quality inhering in an individual or a population whose sex organs contain only male gametes. MGED:MGED PATO:0000386 A hardness quality of being rigid and resistant to pressure. hard PATO:0000387 A hardness quality of giving little resistance to pressure. soft PATO:0000389 A quality of a process inhering in a bearer by virtue of the bearer's having a sudden onset, sharp rise, and short course. acute A branchiness quality inhering in a bearer by virtue of the bearer's having branches. A branchiness quality inhering in a bearer by virtue of the bearer's having branches. ramified ramiform quality PATO:0000402 branched (quality) PATO:0000402 A branchiness quality inhering in a bearer by virtue of the bearer's having branches. WordNet:WordNet A shape quality inhering in a bearer by virtue of the bearer's being curled or wound (especially in concentric rings or spirals). A shape quality inhering in a bearer by virtue of the bearer's being curled or wound (especially in concentric rings or spirals). PATO:0001363 spiral quality helical helicoid helicoidal helix-shaped PATO:0000404 coiled (quality) PATO:0000404 A shape quality inhering in a bearer by virtue of the bearer's being curled or wound (especially in concentric rings or spirals). WordNet:WordNet PATO:0000411 A shape quality inhering in a bearer by virtue of the bearer's being such that every part of the surface or the circumference is equidistant from the center. round rounded circular PATO:0000427 A quality of a single process inhering in a bearer by virtue of the bearer's occurring or appearing again or repeatedly. recurrent A pattern quality inhering in a bearer by virtue of the bearer's having a repeatable or predictable placement. A pattern quality inhering in a bearer by virtue of the bearer's having a repeatable or predictable placement. quality PATO:0000440 regular spatial pattern (quality) PATO:0000440 A pattern quality inhering in a bearer by virtue of the bearer's having a repeatable or predictable placement. PATOC:GVG PATO:0000441 A quality of a single process inhering in a bearer by virtue of the bearer's marked by tedious repetition. repetitive PATO:0000460 A quality inhering in a bearer by virtue of the bearer's deviation from normal or average. abnormal PATO:0000461 A quality inhering in a bearer by virtue of the bearer's exhibiting no deviation from normal or average. normal PATO:0000470 An amount which is relatively high. increased amount PATO:0000498 A duration quality of a process which is relatively high. increased duration PATO:0000499 A duration quality of a process which is relatively low. decreased duration PATO:0000502 A quality of a process which starts later than the natural start time or the reference process. delayed PATO:0000504 A rhythm quality inhering in a bearer by virtue of the bearer's lacking rhythm. arrhythmic PATO:0000505 A rhythm quality inhering in a bearer by virtue of the bearer's having rhythm. rhythmic PATO:0000573 A length quality which is relatively large. increased length PATO:0000574 A length quality which is relatively small. short shortened decreased length PATO:0000584 An increased size quality inhering in a bearer by virtue of the bearer's exhibiting enlargement of a cell or constituent group of cells (for example, organ). MeSH:D006984 http://purl.bioontology.org/ontology/SNOMEDCT/56246009 hypertrophy hypertrophic PATO:0000586 A size quality which is relatively high. big enlarged expanded great large increased size PATO:0000587 A size quality which is relatively low. hyposia reduced small tiny decreased size PATO:0000591 A thickness which is relatively high. high thickness increased thickness PATO:0000592 A thickness which is relatively low. low thickness thin decreased thickness PATO:0000595 A volume which is relatively high. high volume large volume increased volume PATO:0000596 A volume which is relatively low. low volume small volume decreased volume A morphological quality inhering in a bearer by virtue of the bearer's affording blocked passage or view. A morphological quality inhering in a bearer by virtue of the bearer's affording blocked passage or view. quality blocked PATO:0000608 closed (quality) PATO:0000608 A morphological quality inhering in a bearer by virtue of the bearer's affording blocked passage or view. answers.com:answers.com A pattern where all the repeated elements are oriented in the same direction. A pattern where all the repeated elements are oriented in the same direction. quality PATO:0000614 oriented PATO:0000614 A pattern where all the repeated elements are oriented in the same direction. PATOC:MAH A symmetry quality inhering in a bearer by virtue of the bearer's lacking symmetry. A symmetry quality inhering in a bearer by virtue of the bearer's lacking symmetry. asymmetric asymmetry quality PATO:0000616 asymmetrical (quality) PATO:0000616 A symmetry quality inhering in a bearer by virtue of the bearer's lacking symmetry. PATOC:GVG A shape quality inhering in a bearer by virtue of the bearer's having one or more angle(s) in its length. A shape quality inhering in a bearer by virtue of the bearer's having one or more angle(s) in its length. angled flexed quality PATO:0000617 bent (quality) PATO:0000617 A shape quality inhering in a bearer by virtue of the bearer's having one or more angle(s) in its length. PATOC:MAH An oriented quality inhering in a bearer by virtue of the bearer's being reversed in position, order, or condition. An oriented quality inhering in a bearer by virtue of the bearer's being reversed in position, order, or condition. quality backward reversed PATO:0000625 inverted (quality) PATO:0000625 An oriented quality inhering in a bearer by virtue of the bearer's being reversed in position, order, or condition. PATOC:GVG PATO:0000639 A structural quality inhering in a bearer whose structure deteriorates or is lost over time due to an active pathological process. degenerate (quality) A morphological quality inhering in a bearer by virtue of the bearer's being blocked or filled with obstacles or an obstacle. A morphological quality inhering in a bearer by virtue of the bearer's being blocked or filled with obstacles or an obstacle. quality PATO:0000648 obstructed (quality) PATO:0000648 A morphological quality inhering in a bearer by virtue of the bearer's being blocked or filled with obstacles or an obstacle. thefreedictionary.com:thefreedictionary.com PATO:0000690 A quality of a single process inhering in a bearer by virtue of the bearer's being marked by breaks or interruptions. discontinuous PATO:0000694 A quality of a process which starts earlier than the natural start time or the reference process. precocious premature early PATO:0000701 A texture quality inhering in a bearer by virtue of the bearer's processing a surface free of roughness or irregularities. smooth (quality) PATO:0000915 A 1-D extent quality which is equal to the dimension through an object as opposed to its length or width. thickness PATO:0000918 A 3-D extent quality inhering in a bearer by virtue of the bearer's amount of 3-dimensional space it occupies. volume A spheroid quality inhering in a bearer by virtue of the bearer's being oval with two axes of symmetry, as produced by a conical section. A spheroid quality inhering in a bearer by virtue of the bearer's being oval with two axes of symmetry, as produced by a conical section. ellipse-shaped ellipsoid elliptical quality oval ovoid PATO:0000947 elliptic (quality) PATO:0000947 A spheroid quality inhering in a bearer by virtue of the bearer's being oval with two axes of symmetry, as produced by a conical section. PATOC:GVG A fertility quality inhering in a bearer by virtue of the bearer's being capable of initiating, sustaining, or supporting reproduction. A fertility quality inhering in a bearer by virtue of the bearer's being capable of initiating, sustaining, or supporting reproduction. quality PATO:0000955 fertile (quality) PATO:0000955 A fertility quality inhering in a bearer by virtue of the bearer's being capable of initiating, sustaining, or supporting reproduction. PATOC:GVG A fertility quality inhering in a bearer by virtue of the bearer's being incapable of initiating, sustaining, or supporting reproduction. A fertility quality inhering in a bearer by virtue of the bearer's being incapable of initiating, sustaining, or supporting reproduction. WBPhenotype:0000311 quality PATO:0000956 sterile (quality) PATO:0000956 A fertility quality inhering in a bearer by virtue of the bearer's being incapable of initiating, sustaining, or supporting reproduction. PATOC:GVG A pattern quality of inhering in a bearer by virtue of the correspondence in size, shape, and relative position of the bearer's parts on opposite sides of a dividing line or median plane or about a center or axis. A pattern quality of inhering in a bearer by virtue of the correspondence in size, shape, and relative position of the bearer's parts on opposite sides of a dividing line or median plane or about a center or axis. quality PATO:0000965 symmetry (quality) PATO:0000965 A pattern quality of inhering in a bearer by virtue of the correspondence in size, shape, and relative position of the bearer's parts on opposite sides of a dividing line or median plane or about a center or axis. PATOC:GVG PATO:0000970 A structural quality inhering in a bearer by virtue of the bearer's disposition to being permeated or pervaded by a gas or liquid (as by osmosis or diffusion). permeability PATO:0001018 physical quality A quality of a physical entity that exists through action of continuants at the physical level of organisation in relation to other entities. physical quality PATO:0001024 A physical quality inhering in a bearer by virtue of the bearer's rate of doing work. A physical quality inhering in a bearer by virtue of the bearer's rate of doing work. power A physical quality inhering in a bearer by virtue of the bearer's rate of doing work. https://en.wikipedia.org/wiki/Power_(physics) PATO:0001025 A physical quality that inheres in a bearer by virtue of the bearer's amount of force per unit area it exerts. pressure PATO:0001031 A physical quality inhering in a bearer by virtue of the bearer's disposition to recover its size and shape after deformation in any way. elasticity PATO:0001035 A physical quaility inhering in a bearer by virtue of the bearer's rate of change of momentum. force (quality) PATO:0001159 A concentration quality inhering in a bearer by virtue of the bearer's exhibiting concentration. concentrated PATO:0001162 A concentration which is higher relative to the normal or average. high concentration increased concentration PATO:0001163 A concentration which is lower relative to the normal or average. decreased concentration PATO:0001230 A quality inhering in a bearer by virtue of the bearer's power or force. strength quality PATO:0001236 A quality which inheres in an process. process quality PATO:0001241 physical object quality A quality which inheres in a continuant. physical object quality PATO:0001291 electromagnetic (EM) radiation quality A physical quality that inheres in an bearer by virtue of how that bearer interacts with electromagnetic radiation. electromagnetic (EM) radiation quality PATO:0001296 luminous flux A scalar optical quality which obtains by the magnitude of the light emitted by the bearer. luminous flux PATO:0001300 optical quality An EM radiation quality in which the EM radiation is within the fiat range of the spectrum visible deemed to be light. optical quality PATO:0001309 A process quality inhering in a bearer by virtue of the bearer's magnitude of the temporal extent between the starting and ending point. period duration PATO:0001323 A 2-D extent quality inhering in a bearer by virtue of the bearer's two dimensional extent. area A biological sex quality inhering in an organism or a population with both male and female sexual organs in one individual. A biological sex quality inhering in an organism or a population with both male and female sexual organs in one individual. intersex quality PATO:0001340 hermaphrodite (phenotype) PATO:0001340 A biological sex quality inhering in an organism or a population with both male and female sexual organs in one individual. MGED:MGED PATO:0001416 A duration which has regular start and/or end times. reguar duration PATO:0001417 A duration quality of a process inhering in a bearer by virtue of the bearer's duration which has irregular start and/or end times. irregular duration PATO:0001421 alive PATO:0001422 A viability quality inhering in a bearer by virtue of the cessation of the bearer's life. dead PATO:0001429 An medium acidity quality inhering in a solution by virtue of the bearer's a high concentration of H+ ions. acidic PATO:0001430 An medium acidity quality inhering in a solution by virtue of the bearer's a low concentration of H+ ions. alkaline An organismal quality inhering in a bearer by virtue of the bearer's ability to produce new life or offspring. An organismal quality inhering in a bearer by virtue of the bearer's ability to produce new life or offspring. quality PATO:0001434 repeoductive quality PATO:0001434 An organismal quality inhering in a bearer by virtue of the bearer's ability to produce new life or offspring. WordNet:WordNet PATO:0001447 A composition quality inhering in an bearer by virtue of the bearer's being encrusted or impregnated with calcium carbonate (CHEBI:3311). calcified PATO:0001462 A quality inhering in a cell's plasma membrane by virtue of the electrical potential difference across it. A quality inhering in a cell's plasma membrane by virtue of the electrical potential difference across it. membrane potential A quality inhering in a cell's plasma membrane by virtue of the electrical potential difference across it. https://en.wikipedia.org/wiki/Membrane_potential PATO:0001464 A quality that is equal to the potential energy per unit charge associated with a static (time-invariant) electric field, also called the electrostatic potential. A quality that is equal to the potential energy per unit charge associated with a static (time-invariant) electric field, also called the electrostatic potential. electric potential A quality that is equal to the potential energy per unit charge associated with a static (time-invariant) electric field, also called the electrostatic potential. https://en.wikipedia.org/wiki/Electric_potential PATO:0001487 A time quality inhering in a bearer by virtue of the bearer's growing old; aging. senescent A concave quality inhering in a bearer by virtue of the bearer's shape being a V-shaped cut. A concave quality inhering in a bearer by virtue of the bearer's shape being a V-shaped cut. quality indented PATO:0001495 notched (quality) PATO:0001495 A concave quality inhering in a bearer by virtue of the bearer's shape being a V-shaped cut. thefreedictionary.com:thefreedictionary.com A reproductive quality inhering in the young of an animal by virtue of the bearer's being cared for at one time. A reproductive quality inhering in the young of an animal by virtue of the bearer's being cared for at one time. quality PATO:0001496 brood quality PATO:0001496 A reproductive quality inhering in the young of an animal by virtue of the bearer's being cared for at one time. WordNet:WordNet PATO:0001562 A mass which is lower than normal or average. decreased mass PATO:0001574 A physical quality inhering in a bearer by virtue of the bearer's motion characteristic. flow rate quality PATO:0001575 A pressure which is relatively low. low pressure decreased pressure PATO:0001576 A pressure which is relatively high. increased pressure PATO:0001577 A permeability which is relatively high. high permeability increased permeability PATO:0001578 A permeability which is relatively low. low permeability decreased permeability PATO:0001579 A physical quality that is the ability to contract or shrink. contractility (quality) PATO:0001580 A contractility which is relatively high. increased contractility PATO:0001581 A contractility which is relatively low. decreased contractility An oriented quality inhering in a bearer by virtue of the bearer's being turned outward in placement. An oriented quality inhering in a bearer by virtue of the bearer's being turned outward in placement. quality PATO:0001597 everted (quality) PATO:0001597 An oriented quality inhering in a bearer by virtue of the bearer's being turned outward in placement. thefreedictionary:thefreedictionary An oriented quality inhering in a bearer by virtue of the bearer's being relocated around an axis. An oriented quality inhering in a bearer by virtue of the bearer's being relocated around an axis. rotation quality PATO:0001599 rotated (quality) PATO:0001599 An oriented quality inhering in a bearer by virtue of the bearer's being relocated around an axis. answers.com:answers.com PATO:0001623 A size quality inhering in a bearer by virtue of a part or parts of the bearer's being decreased in size due to reduction in tissue mass through wasting. atrophic atrophied PATO:0001629 A spatial pattern inhering in a bearer by virtue of the bearer's being gathered or tending to gather into a mass or whole. aggregated PATO:0001632 A spatial quality inhering in a bearer by virtue of the bearer's being located toward the front of an organism relative to another entity. anterior to PATO:0001633 A spatial quality inhering in a bearer by virtue of the bearer's being located toward the rear of an organism relative to another entity. posterior to PATO:0001637 A quality of single process inhering in a bearer by virtue of whether the bearer is essential or indispensable. necessity of occurrent PATO:0001638 A necessity quality inhering in a process by virtue of the bearer's being essential or indispensable. necessary (occurrent) PATO:0001639 A necessity quality inhering in a process by virtue of the bearer's being non-essential or dispensable. unnecessary (occurrent) PATO:0001739 radiation quality A quality that inheres in an bearer by virtue of how that bearer interacts with radiation. radiation quality PATO:0001759 A composition quality inhering in a bearer by virtue of the bearer's containing granules. granular PATO:0001764 An age which is high relative to the normal or average high age increased age (quality) quality PATO:0001767 semi-fertile (quality) PATO:0001767 PATO:0001769 A positional quality inhering in a bearer by virtue of the bearer's location of features or characteristics along an axis. positional polarity A shape quality inhering in a bearer by virtue of the bearer's being wound in a continuous series of loops. A shape quality inhering in a bearer by virtue of the bearer's being wound in a continuous series of loops. quality PATO:0001794 coiling (quality) PATO:0001794 A shape quality inhering in a bearer by virtue of the bearer's being wound in a continuous series of loops. Online_Dictionary:Online_Dictionary A shape quality inhering in a bearer by virtue of the bearer's having multiple angles in its length. A shape quality inhering in a bearer by virtue of the bearer's having multiple angles in its length. quality tightly curled twisted PATO:0001798 kinked (quality) PATO:0001798 A shape quality inhering in a bearer by virtue of the bearer's having multiple angles in its length. thefreedictionary.com:thefreedictionary.com A grooved texture quality inhering in a bearer by virtue of the bearer's being marked by one or more creases in a normally smooth surface. A grooved texture quality inhering in a bearer by virtue of the bearer's being marked by one or more creases in a normally smooth surface. quality PATO:0001810 wrinkled (quality) PATO:0001810 A grooved texture quality inhering in a bearer by virtue of the bearer's being marked by one or more creases in a normally smooth surface. url:http://www.thefreedictionary.com/wrinkled PATO:0001818 A quality of a single process inhering in a bearer by virtue of the bearer's increasing over time. progressive A morphological quality inhering in a bearer by virtue of the bearer's absence or closure of a normal body orifice or tubular passage. A morphological quality inhering in a bearer by virtue of the bearer's absence or closure of a normal body orifice or tubular passage. atresia quality PATO:0001819 atretic (quality) PATO:0001819 A morphological quality inhering in a bearer by virtue of the bearer's absence or closure of a normal body orifice or tubular passage. answers.com:answers.com A fertility which is relatively low. A fertility which is relatively low. low fertility quality PATO:0001834 decreased fertility (quality) PATO:0001834 A fertility which is relatively low. PATOC:GVG A fertility which is relatively high. A fertility which is relatively high. high fertility quality PATO:0001835 increased fertility (quality) PATO:0001835 A fertility which is relatively high. PATOC:GVG PATO:0001838 A flow that is relatively low. decreased fluid flow (quality) PATO:0001839 A flow that is relatively high. increased fluid flow (quality) PATO:0001842 A concentration quality inhering in a bearer by virtue of the bearer's containing acid (hydrogen ions). pH acidity PATO:0001843 An acidity which is relatively low. decreased acidity PATO:0001844 An acidity which is relatively high. increased acidity PATO:0001850 A structural quality inhering in a bearer by virtue of the bearer's being fibrous tissue that replaces normal tissue destroyed by injury or disease. scarred (quality) PATO:0001851 A structure quality inhering in a bearer by virtue of the bearer's exhibiting transient abnormal enlargement, not due to cell proliferation. swelling swollen (phenotype) A shape quality in a bearer by virtue of the bearer's curving inward. A shape quality in a bearer by virtue of the bearer's curving inward. quality PATO:0001857 concave (quality) PATO:0001857 A shape quality in a bearer by virtue of the bearer's curving inward. WordNet:WordNet A convex 3-D shape quality inhering in a bearer by virtue of the bearer's exhibiting a consistently-sized round cross section. A convex 3-D shape quality inhering in a bearer by virtue of the bearer's exhibiting a consistently-sized round cross section. PATO:0001203 rod-like rod-shaped tubulate quality PATO:0001873 cylindrical (quality) PATO:0001873 A convex 3-D shape quality inhering in a bearer by virtue of the bearer's exhibiting a consistently-sized round cross section. PATOC:MAH PATO:0001884 A physical quality inhering in a bearer by virtue the bearer's disposition to being water-repellent; tending to repel and not absorb water. hydrophobicity PATO:0001886 A physical quality inhering in a bearer by virtue the bearer's disposition to having an affinity for water; it is readily absorbing or dissolving in water. hydrophilicity An organismal quality inhering in a bearer by virtue of the bearer's physical expression of sexual characteristics. quality PATO:0001894 phenotypic sex (quality) PATO:0001894 PATO:0001906 A physical quality inhering in a bearer by virtue of the bearer's participation in movement. movement quality A texture quality inhering in a bearer by virtue of a local accumulation of fluid underneath the surface of the bearer. A texture quality inhering in a bearer by virtue of a local accumulation of fluid underneath the surface of the bearer. blistering quality PATO:0001928 blistered (quality) PATO:0001928 A texture quality inhering in a bearer by virtue of a local accumulation of fluid underneath the surface of the bearer. PATOC:GVG A quality that inheres in an entire organism or part of an organism. A quality that inheres in an entire organism or part of an organism. quality PATO:0001995 organismal quality PATO:0001995 A quality that inheres in an entire organism or part of an organism. PATOC:CJM PATO:0001997 An amount which is relatively low. decreased amount HOIP_0002450 PATO:0002002 A number quality which is relatively many. increased number (quality) Surface shape that refers to the inward or outward curvature of the surface. Surface shape that refers to the inward or outward curvature of the surface. quality PATO:0002005 concavity (quality) PATO:0002005 Surface shape that refers to the inward or outward curvature of the surface. PATOC:MAH A shape that inheres in a 2 dimensional entity, such as a cross section or projection of a 3 dimensional entity. A shape that inheres in a 2 dimensional entity, such as a cross section or projection of a 3 dimensional entity. quality 2-D projection cross-sectional PATO:0002006 2-D shape (quality) PATO:0002006 A shape that inheres in a 2 dimensional entity, such as a cross section or projection of a 3 dimensional entity. PATOC:CJM A complete three dimensional shape in which for every line connecting pair of points on the object is within the object. Or: a shape lacking cavities. Contrast: concave. A complete three dimensional shape in which for every line connecting pair of points on the object is within the object. Or: a shape lacking cavities. Contrast: concave. Image:http://upload.wikimedia.org/wikipedia/commons/0/06/Convex_polygon_illustration1.png quality PATO:0002007 Use this term or an is_a child of this term when the entire shape of the object is known. convex 3-D shape (quality) PATO:0002007 A complete three dimensional shape in which for every line connecting pair of points on the object is within the object. Or: a shape lacking cavities. Contrast: concave. PATOC:CJM A shape quality inhering in a bearer by virtue of the degree to which there are subdivisions or offshoots in a bearer entity. A shape quality inhering in a bearer by virtue of the degree to which there are subdivisions or offshoots in a bearer entity. quality PATO:0002009 branchiness (quality) PATO:0002009 A shape quality inhering in a bearer by virtue of the degree to which there are subdivisions or offshoots in a bearer entity. PATOC:MAH PATO:0002011 A structural quality which is held by a bearer when the latter's disposition the presence of abnormally proliferating masses of cells. neoplastic (quality) PATO:0002024 A positional quality inhering in a bearer by virtue of the bearer's location of features or characteristics along the anterior-posterior axis. anterior-posterior polarity PATO:0002037 A structural quality inhering in a bearer by virtue of the bearer exhibiting deterioration of its structure. degeneration (quality) PATO:0002057 An area which is relatively high. increased area PATO:0002058 An area which is relatively low. decreased area PATO:0002070 A molecular quality that arises from the molecular attraction exerted between two atoms or compounds. affinity PATO:0002072 An affinity which is relatively low. decreased affinity PATO:0002091 A quality of a single process inhering in a bearer by virtue of the bearer's having an onset and time course between acute and chronic. subacute PATO:0002094 An affinity inhering in a tissue constituent by virtue of the bearer exhibiting a molecular interaction for basic dyes under specific ph conditions. basophilic PATO:0002096 A disposition inhering in a tumour by virtue of the bearer's disposition not to progress, invade surrounding tissues or metastasize. neoplastic, non-malignant PATO:0002097 A disposition inhering in a tumour by virtue of the bearer's disposition to progress, invade surrounding tissues or metastasize. neoplastic, malignant PATO:0002098 A disposition inhering in a tumour by virtue of the bearer's disposition to spread and invade distant tissues. neoplastic, metastatic PATO:0002104 A compositional quality inhering in an bearer by virtue of the bearer's infiltration by leukocytes, local edema and accumulation of plasma proteins. inflammatory PATO:0002114 A composition quality inhering in a bearer by virtue of the bearer's containing excess lipid. fatty PATO:0002129 A disposition inhering in a tumour by virtue of the bearer's disposition to invade surrounding tissues. neoplastic, invasive PATO:0002132 A disposition inhering in a tumour by virtue of the bearer's disposition not to invade surrounding tissues. neoplastic, non-invasive PATO:0002242 A physical quality inhering in a bearer by virtue of the bearer's rate of change of the position. velocity quality Texture quality inhering in a bearer by virtue of the bearer's being marked with one or more channels. Texture quality inhering in a bearer by virtue of the bearer's being marked with one or more channels. george 2010-09-01T10:27:48Z quality channeled creased PATO:0002255 grooved (quality) PATO:0002255 Texture quality inhering in a bearer by virtue of the bearer's being marked with one or more channels. PATOC:JE A shape that inheres in a 3 dimensional entity. A shape that inheres in a 3 dimensional entity. george 2010-10-05T12:31:16Z quality PATO:0002266 3-D shape (quality) PATO:0002266 A shape that inheres in a 3 dimensional entity. PATOC:OREGON PATO:0002269 A structural quality of the collection or massing of one physical object within another physical object. accumulation (quality) PATO:0002270 An increased number of physical objects that are accumulated within another physical object usually as a result of a failure to break down or remove objects in a timely manner. increased accumulation (quality) PATO:0002271 An accumulation which is relative low. decreased accumulation (quality) PATO:0002292 A structural quality inhering in a bearer by virtue of the bearer's underlying structure being capable of change. transient PATO:0002293 A structural quality inhering in a bearer by virtue of the bearer's underlying structure not changing over time. permanent A shape constituting a transition between a rectangle and a circle; a closed curve, of which the circle and ellipse are special cases, whose parametric equation is x = a.cos2/rt, y = b.cos2/rt A shape constituting a transition between a rectangle and a circle; a closed curve, of which the circle and ellipse are special cases, whose parametric equation is x = a.cos2/rt, y = b.cos2/rt George Gkoutos 2011-10-12T12:45:16Z Lamé curve quality PATO:0002318 superelliptic (quality) PATO:0002318 A shape constituting a transition between a rectangle and a circle; a closed curve, of which the circle and ellipse are special cases, whose parametric equation is x = a.cos2/rt, y = b.cos2/rt wiktionary:superellipse PATO:0002323 A temporal distribution pattern of process occurrences within a regulation/reference process. temporal distribution quality PATO:0002325 The temporal relation between the start of the process with respect to a reference process. onset quality PATO:0002353 A quality that inheres in a bearer in virtue of its realizing one of its functions. activation quality PATO:0002354 A quality of an physical object that is currently realizing one of its functions. active PATO:0002355 A quality of a physical object that is currently realizing none of its functions. inactive PATO:0002408 Having the consistency of water. watery PATO:0002420 Having both hydrophilic and hydrophobic (or lipophilic) groups. amphiphilic PATO:0002473 A disposition inhering in a tumour by virtue of the bearer's disposition to spontaneously arise. neoplastic, spontaneous PATO:0015002 The ability of a process to produce its output. process efficacy PATO:0015003 A decrease in the ability of a process to produce its output. decreased efficacy PATO:0015004 A increase in the ability of a process to produce its output. increased efficacy PR:000000001 PR:000000017 A type II interferon that is a translation product of the human IFNG gene or a 1:1 ortholog thereof. The core domain structure consists of an Interferon gamma domain (Pfam:PF00714) that is four-helical cytokine domain with an additional helix in one of the crossover connections. It is a cytokine produced by lymphocytes activated by specific antigens or mitogens that has important immunoregulatory functions. NCBI-Human-GeneID:3458 IFN-gamma interferon gamma Note: Some references consider 'gamma' and 'type II' to be synonyms. This is likely because gamma is the only type II interferon identified. However, the classification criteria for each nomenclature system differ. IFNG NCBI-Human-GeneID:3458 https://www.ncbi.nlm.nih.gov/gene/3458 PR:000000027 A protein with core domain composition consisting of one MH1 domain (Pfam:PF03165) at the N terminus and one MH2 domain (Pfam:PF03166) at the C-terminus, separated by a non-conserved linker region. Smad proteins are mediators of signal transduction in transforming growth factor beta (TGF-beta) superfamily pathways. Smads is a conserved family of signal transducers. Functionally, Smads fall into three subfamilies:R-Smads; Co-Smads; I-Smads. Eight Smad proteins are encoded in vertebrate, four in Drosophila, and three in C. elegans. Smads is a conserved family of signal transducers. Functionally, Smads fall into three subfamilies:R-Smads; Co-Smads; I-Smads. Eight Smad proteins are encoded in vertebrate, four in Drosophila, and three in C. elegans. PIRSF:PIRSF037286 SMAD smad protein Smads is a conserved family of signal transducers. Functionally, Smads fall into three subfamilies:R-Smads; Co-Smads; I-Smads. Eight Smad proteins are encoded in vertebrate, four in Drosophila, and three in C. elegans. PMID:11792802 PMID:16322555 PMID:9393997 PR:000000046 A TGF-beta-like cystine-knot cytokine whose propeptide region is a latent associated peptide (LAP) that remains associated to the mature TGF-beta after cleavage and secretion, keeping TGF-beta inactive. TGF-beta is the founding member of the cystine-knot cytokine family, and is related to the activin/inhibin, anti-Muellerian hormone, and bone morphogenic protein families, which are all involved in the regulation of cell growth and differentiation. transforming growth factor beta TGF-beta PR:000000093 p15-INK4b A protein that is a translation product of the human CDKN2B gene or a 1:1 ortholog thereof. HGNC:1787 PANTHER:PTHR24144:SF138 CDKN2B gene translation product INK4b MTS-2 cyclin-dependent kinase 4 inhibitor B multiple tumor suppressor 2 p15-INK4b p15INK4b CDKN2B PR:000000103 A mitogen-activated protein kinase that is a translation product of the human MAPK1 gene or a 1:1 ortholog thereof. ERK-2 ERT1 MAP kinase 1 MAP kinase 2 extracellular signal-regulated kinase 2 mitogen-activated protein kinase 1 ERK2 MAPK1 PRKM1 MAPK1 PR:000000104 A mitogen-activated protein kinase 3 that is encoded in the genome of human. Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:34497368). MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade also plays a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DEPTOR, FRS2 or GRB10) (PubMed:35216969). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade ERK-1 ERT2 MAP kinase 3 MAP kinase isoform p44 UniProtKB:P27361 extracellular signal-regulated kinase 1 mitogen-activated protein kinase 3 MAPK3 Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:34497368). MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade also plays a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DEPTOR, FRS2 or GRB10) (PubMed:35216969). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade UniProtKB:P27361 UniProtKB:P27361 Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:34497368). MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade also plays a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DEPTOR, FRS2 or GRB10) (PubMed:35216969). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade PR:000000134 A tumor necrosis factor, TNF-like that is a translation product of the human TNF gene or a 1:1 ortholog thereof. Tumour necrosis factor alpha (TNF) is a pleiotropic cytokine that mediates apoptosis, cell proliferation, immunomodulation, inflammation, viral replication, allergy, arthritis, septic shock, insulin resistance, autoimmune diseases, and other pathological conditions. TNF transduces these cellular responses through two distinct receptors: type I, which are expressed on all cell types, and type II, which are expressed only on cells of the immune system and endothelial cells. NCBI-Human-GeneID:7124 NCBI-Mouse-GeneID:21926 NCBI-Rat-GeneID:24835 TNF-a TNF-alpha cachectin tumor necrosis factor tumor necrosis factor alpha tumor necrosis factor ligand superfamily member 2 tumor necrosis factor NCBI-Human-GeneID:7124 http://www.ncbi.nlm.nih.gov/gene/7124 NCBI-Mouse-GeneID:21926 http://www.ncbi.nlm.nih.gov/gene/21926 NCBI-Rat-GeneID:24835 http://www.ncbi.nlm.nih.gov/gene/24835 PR:000000182 A TGF-beta that is a translation product of the human TGFB1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID: NCBI-Mouse-GeneID: NCBI-Rat-GeneID: TGFB1 TGF-beta 1 NCBI-Human-GeneID: http://www.ncbi.nlm.nih.gov/gene/7040 NCBI-Mouse-GeneID: http://www.ncbi.nlm.nih.gov/gene/21803 NCBI-Rat-GeneID: http://www.ncbi.nlm.nih.gov/gene/59086 PR:000000183 A TGF-beta that is a translation product of the human TGFB2 gene or a 1:1 ortholog thereof. transforming growth factor-beta 2 TGF-beta 2 PR:000000184 A TGF-beta that is a translation product of the human TGFB3 gene or a 1:1 ortholog thereof. transforming growth factor-beta 3 TGF-beta 3 PR:000001091 A protein with a core domain composition consisting of a propeptide region and an Interleukin-1 / 18 domain. IL-1 interleukin-1 PR:000001092 A protein that is a T cell-derived cytokine that may play an important role in the initiation or maintenance of the proinflammatory response. Except for IL-17B, all other IL-17 family members are homodimers containing five highly conserved cysteine residues forming characteristic cystein-knot structure, similar to that found in the TGF-beta-like cystine-knot (PR:000000008). This class consists of six cytokines. Among them, interleukin 17A (IL-17) and IL-17F are expressed by a novel subset of CD4+ helper T (Th) cells and play a critical role in inflammation and autoimmunity. On the other hand, IL-17E, also called IL-25, has been associated with allergic responses. NCBI-Human-GeneID:3605 CTLA-8 IL-17 cytotoxic T lymphocyte-associated antigen 8 interleukin-17 NCBI-Human-GeneID:3605 https://www.ncbi.nlm.nih.gov/gene/3605 PR:000001096 A protein with a core domain composition consisting of a signal peptide, an extracellular domain with multiple Leucine rich repeat (Pfam:PF13855) domain (LRR), a cysteine-rich region, a single-pass transmembrane domain and a C-terminal cytoplasmic tail containing a TIR domain (Pfam:PF01582). TLR Toll-like receptor PR:000001135 An interleukin-1 that is a translation product of the human IL1A gene or a 1:1 ortholog thereof. Critical mediator of the immune and inflammatory responses. IL-1 alpha hematopoietin-1 interleukin-1 alpha IL1A PR:000001136 An interleukin-1 that is a translation product of the human IL1B gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3553 NCBI-Mouse-GeneID:16176 NCBI-Rat-GeneID:24494 IL-1 beta IL1B interleukin-1 beta NCBI-Human-GeneID:3553 http://www.ncbi.nlm.nih.gov/gene/3553 NCBI-Mouse-GeneID:16176 http://www.ncbi.nlm.nih.gov/gene/16176 NCBI-Rat-GeneID:24494 http://www.ncbi.nlm.nih.gov/gene/24494 PR:000001138 An interleukin-17 that is a translation product of the human IL17A gene or a 1:1 ortholog thereof. The active product is a proinflammatory cytokine produced by activated T cells. This cytokine regulates the activities of NF-kappaB and mitogen-activated protein kinases. CTLA-8 IL-17A IL17A cytotoxic T-lymphocyte-associated antigen 8 interleukin-17A PR:000001151 A Toll-like receptor that is a translation product of the human TLR1 gene or a 1:1 ortholog thereof. TLR1 Toll-like receptor 1 PR:000001153 TLR2 Toll-like receptor 2 PR:000001154 A Toll-like receptor that is a translation product of the human TLR3 gene or a 1:1 ortholog thereof. CD283 TLR3 Toll-like receptor 3 PR:000001155 A Toll-like receptor that is a translation product of the human TLR4 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7099 NCBI-Mouse-GeneID:21898 NCBI-Rat-GeneID:29260 CD284 TLR4 Toll-like receptor 4 NCBI-Human-GeneID:7099 https://www.ncbi.nlm.nih.gov/gene/7099 NCBI-Mouse-GeneID:21898 https://www.ncbi.nlm.nih.gov/gene/21898 NCBI-Rat-GeneID:29260 https://www.ncbi.nlm.nih.gov/gene/29260 PR:000001156 A Toll-like receptor that is a translation product of the human TLR5 gene or a 1:1 ortholog thereof. TLR5 Toll-like receptor 5 PR:000001157 A Toll-like receptor that is a translation product of the human TLR6 gene or a 1:1 ortholog thereof. TLR6 Toll-like receptor 6 PR:000001158 A Toll-like receptor that is a translation product of the human TLR7 gene or a 1:1 ortholog thereof. TLR7 Toll-like receptor 7 PR:000001159 A Toll-like receptor that is a translation product of the human TLR8 gene or a 1:1 ortholog thereof. TLR8 Toll-like receptor 8 PR:000001160 A Toll-like receptor that is a translation product of the human TLR9 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:54106 NCBI-Mouse-GeneID:81897 NCBI-Rat-GeneID:338457 TLR9 Toll-like receptor 9 NCBI-Human-GeneID:54106 https://www.ncbi.nlm.nih.gov/gene/54106 NCBI-Mouse-GeneID:81897 https://www.ncbi.nlm.nih.gov/gene/81897 NCBI-Rat-GeneID:338457 https://www.ncbi.nlm.nih.gov/gene/338457 PR:000001251 An angiotensin II receptor that is a translation product of the human AGTR1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:185 angiotensin II receptor 1 AGTR1 (mol) NCBI-Human-GeneID:185 http://www.ncbi.nlm.nih.gov/gene/185 PR:000001279 ADAM17 A protein that is a translation product of the human ADAM17 gene or a 1:1 ortholog thereof. ADAM 17 TNF-alpha convertase TNF-alpha converting enzyme ADAM 17 endopeptidase PR:000001313 A protein with core domain structure consisting of one lectin C-type domain (Pfam:PF00059), followed by one EGF domain (Pfam:PF00008), followed by 4-9 sushi domains (Pfam:PF00084), with the P-selectins generally being longer. E/P-selectin famiy PR:000001317 A protein that is a translation product of the human IL7 gene or a 1:1 ortholog thereof. IL-7 IL7 interleukin-7 PR:000001341 A protein that is a translation product of the human DPP4 gene or a 1:1 ortholog thereof. ADABP DPP IV DPP4 T-cell activation antigen CD26 adenosine deaminase complexing protein 2 dipeptidyl peptidase IV PR:000001361 A protein that is a translation product of the human IFNGR1 gene or a 1:1 ortholog thereof. CDw119 IFN-gamma receptor 1 IFN-gamma-R-alpha interferon gamma receptor alpha chain IFNGR1 PR:000001370 A protein that is a translation product of the human IL13 gene or a 1:1 ortholog thereof. Interleukin-13 is a pleiotropic cytokine which may be important in the regulation of the inflammatory and immune responses. It inhibits inflammatory cytokine production and synergises with IL-2 in regulating interferon-gamma synthesis. The sequences of IL-4 and IL-13 are distantly related. IL-13 IL13 interleukin-13 PR:000001373 A protein that is a translation product of the human IL15 gene or a 1:1 ortholog thereof. IL-15 interleukin-15 PR:000001376 A protein that is a translation product of the human IL18 gene or a 1:1 ortholog thereof. IFN-gamma-inducing factor IL-1 gamma IL-18 IL18 iboctadekin interleukin-18 PR:000001379 A protein that is a translation product of the human IL2 gene or a 1:1 ortholog thereof. Interleukin-2 has a dual role in maintaining tolerance and contributing to immunity. A protein that is a translation product of the human IL2 gene or a 1:1 ortholog thereof. Interleukin-2 has a dual role in maintaining tolerance and contributing to immunity. NCBI-Human-GeneID:3558 NCBI-Mouse-GeneID:16183 NCBI-Rat-GeneID:116562 IL-2 IL2 T-cell growth factor interleukin-2 A protein that is a translation product of the human IL2 gene or a 1:1 ortholog thereof. Interleukin-2 has a dual role in maintaining tolerance and contributing to immunity. PMID:18062768 NCBI-Human-GeneID:3558 http://www.ncbi.nlm.nih.gov/gene/3558 NCBI-Mouse-GeneID:16183 http://www.ncbi.nlm.nih.gov/gene/16183 NCBI-Rat-GeneID:116562 http://www.ncbi.nlm.nih.gov/gene/116562 PR:000001387 A protein that is a translation product of the human IL3 gene or a 1:1 ortholog thereof. IL-3 multipotential colony-stimulating factor interleukin-3 PR:000001388 A protein that is a translation product of the human IL32 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:9235 natural killer cells protein 4 interleukin-32 NCBI-Human-GeneID:9235 http://www.ncbi.nlm.nih.gov/gene/9235 PR:000001391 A protein that is a translation product of the human IL4 gene or a 1:1 ortholog thereof. B-cell IgG differentiation factor B-cell growth factor 1 B-cell stimulatory factor 1 IL-4 interleukin-4 PR:000001392 A protein that is a translation product of the human IL5 gene or a 1:1 ortholog thereof. B-cell differentiation factor I B-cell growth factor II IL-5 cytotoxic T-lymphocyte inducer interleukin-5 PR:000001393 A protein that is a translation product of the human IL6 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3569 B-cell hybridoma growth factor B-cell stimulatory factor 2 IL-6 IL6 interleukin-6 NCBI-Human-GeneID:3569 http://www.ncbi.nlm.nih.gov/gene/3569 PR:000001394 A protein that is a translation product of the human IL6R gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3665 CD126 IL-6RA IL6R interleukin-6 receptor subunit alpha NCBI-Human-GeneID:3665 http://www.ncbi.nlm.nih.gov/gene/3665 PR:000001395 A protein that is a translation product of the human CXCL8 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3576 C-X-C motif chemokine 8 CXCL8 interleukin-8 monocyte-derived neutrophil-activating peptide interleukin-8 NCBI-Human-GeneID:3576 http://www.ncbi.nlm.nih.gov/gene/3576 PR:000001415 An E/P-selectin that is a translation product of the human SELE gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:6401 NCBI-Mouse-GeneID:20339 CD62 antigen-like family member E CD62E ELAM-1 LECAM2 endothelial leukocyte adhesion molecule 1 leukocyte-endothelial cell adhesion molecule 2 E-selectin NCBI-Human-GeneID:6401 http://www.ncbi.nlm.nih.gov/gene/6401 NCBI-Mouse-GeneID:20339 http://www.ncbi.nlm.nih.gov/gene/20339 PR:000001432 An E/P-selectin that is a translation product of the human SELP gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:6403 NCBI-Mouse-GeneID:20344 NCBI-Rat-GeneID:25651 CD62 antigen-like family member P CD62P GMP-140 GMRP LECAM3 PADGEM SELP granule membrane protein 140 leukocyte-endothelial cell adhesion molecule 3 platelet activation dependent granule-external membrane protein P-selectin NCBI-Human-GeneID:6403 http://www.ncbi.nlm.nih.gov/gene/6403 NCBI-Mouse-GeneID:20344 http://www.ncbi.nlm.nih.gov/gene/20344 NCBI-Rat-GeneID:25651 http://www.ncbi.nlm.nih.gov/gene/25651 PR:000001447 A cadherin that is a translation product of the human CDH1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:999 NCBI-Mouse-GeneID:12550 NCBI-Rat-GeneID:83502 ARC-1 CAM 120/80 CD324 E-cadherin cadherin-1 epithelial cadherin uvomorulin CDH1 HOIP_0005074 NCBI-Human-GeneID:999 http://www.ncbi.nlm.nih.gov/gene/999 NCBI-Mouse-GeneID:12550 http://www.ncbi.nlm.nih.gov/gene/12550 NCBI-Rat-GeneID:83502 http://www.ncbi.nlm.nih.gov/gene/83502 PR:000001471 A class 2 cytokine, IL-10 type that is a translation product of the human IL10 gene or a 1:1 ortholog thereof. Active interleukin-10 inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T cells. Structurally, IL-10 is a protein of about 160 amino acids that contains four conserved cysteines involved in disulfide bonds. IL-10 interleukin-10 PR:000001752 A protein that is a translation product of the human IKBKG gene or a 1:1 ortholog thereof. In response to a large variety of stimuli, among them pro-inflammatory cytokines, growth factors and microbial pathogens, signals emanating from cell surface receptors converge at the IkappaB kinase (IKK) complex. This complex is composed of four subunits, IKKalpha, IKKbeta, ELK, and NEMO. IKKbeta and NEMO subunits are known to be essential for activating NF-kappaB. Activation of NF-kappaB dimers is the result of IKK-mediated, phosphorylation-induced degradation of the IkappaB inhibitor, which enables the NF-kappaB dimers to enter the nucleus and activate specific target gene expression. HGNC:5961 I-kappa-B kinase subunit gamma (human) IKK-gamma (human) NF-kappa-B essential modulator (human) NEMO inhibitor of nuclear factor kappa-B kinase subunit gamma (human) IKBKG PR:000001753 A protein with a core domain composition consisting of a Rel homology domain (RHD) (Pfam:PF00554), an IPT/TIG domain (Pfam:PF01833), six copies of the Ankyrin repeat (Pfam:PF00023), a Death domain (Pfam:PF00531) and a C-terminal PEST region. IPR:000451 NF-kappa-B NFkB Rel/NF-kappaB family nuclear factor-kappa B transcription factor NF-kappa-B subunit PR:000001754 A transcription factor NF-kappa-B subunit that is a translation product of the human NFKB1 gene or a 1:1 ortholog thereof. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NCBI-Human-GeneID:4790 NCBI-Mouse-GeneID:18033 NCBI-Rat-GeneID:81736 DNA-binding factor KBF1 nuclear factor NF-kappa-B p105 subunit NFKB1 NCBI-Human-GeneID:4790 http://www.ncbi.nlm.nih.gov/gene/4790 NCBI-Mouse-GeneID:18033 http://www.ncbi.nlm.nih.gov/gene/18033 NCBI-Rat-GeneID:81736 http://www.ncbi.nlm.nih.gov/gene/81736 PR:000001757 A nuclear factor NF-kappa-B p105 subunit isoform 1 that has been processed by proteolytic cleavage to remove the C-terminal domain of p105 downstream from the 23 residue, glycine rich region (GRR). GRR functions as a processing signal for the generation of p50. p50 NF-KAPPA-B P50 NFKB1 p50 nuclear factor NF-kappa-B p105 subunit isoform 1 cleaved 1 nuclear factor NF-kappa-B p50 subunit NFKBp50 PR:000001900 NRP1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:8829 A5 protein BDCA-4 CD304 NRP1 blood dendritic cell antigen 4 neuropilin-1 NCBI-Human-GeneID:8829 http://www.ncbi.nlm.nih.gov/gene/8829 PR:000001919 A protein that is a translation product of the human PDCD1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:5133 NCBI-Mouse-GeneID:18566 CD279 PD-1 PD1 PDCD1 programmed cell death protein 1 NCBI-Human-GeneID:5133 http://www.ncbi.nlm.nih.gov/gene/5133 NCBI-Mouse-GeneID:18566 http://www.ncbi.nlm.nih.gov/gene/18566 PR:000001933 A protein with core architecture consisting of a STAT protein, protein interaction domain (Pfam:PF02865), an SH2 domain (Pfam:PF01017), a STAT protein, DNA binding domain (Pfam:PF02864), and a second SH2 domain. signal transducer and transcription activator STAT STAT PR:000001940 A protein that is a translation product of the human F3 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:2152 NCBI-Mouse-GeneID:14066 NCBI-Rat-GeneID:25584 CD142 Cf-3 F3 thromboplastin tissue factor HOIP_0041710 NCBI-Human-GeneID:2152 http://www.ncbi.nlm.nih.gov/gene/2152 NCBI-Mouse-GeneID:14066 http://www.ncbi.nlm.nih.gov/gene/14066 NCBI-Rat-GeneID:25584 http://www.ncbi.nlm.nih.gov/gene/25584 PR:000001966 A two-pore channel protein that is a translation product of the human TPCN2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:219931 NCBI-Mouse-GeneID:233979 NCBI-Rat-GeneID:309139 TPC2 TPCN2 voltage-dependent calcium channel protein TPC2 two pore calcium channel protein 2 NCBI-Human-GeneID:219931 https://www.ncbi.nlm.nih.gov/gene/219931 NCBI-Mouse-GeneID:233979 https://www.ncbi.nlm.nih.gov/gene/233979 NCBI-Rat-GeneID:309139 https://www.ncbi.nlm.nih.gov/gene/309139 PR:000001992 A C/C-C motif small inducible chemokine that is a translation product of the human CCL20 gene or a 1:1 ortholog thereof. C-C motif chemokine 20 CCL20 PR:000002023 NCBI-Human-GeneID:3821 NCBI-Mouse-GeneID:77286 CD159 antigen-like family member A CD159a KLRC1 NK cell receptor A NKG2-A/B-activating NK receptor NKG2A NKG2-A/NKG2-B type II integral membrane protein NCBI-Human-GeneID:3821 Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. The protein encoded by this gene belongs to the killer cell lectin-like receptor family, also called NKG2 family, which is a group of transmembrane proteins preferentially expressed in NK cells. This family of proteins is characterized by the type II membrane orientation and the presence of a C-type lectin domain. This protein forms a complex with another family member, KLRD1/CD94, and has been implicated in the recognition of the MHC class I HLA-E molecules in NK cells. The genes of NKG2 family members form a killer cell lectin-like receptor gene cluster on chromosome 12. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jan 2015] http://www.ncbi.nlm.nih.gov/gene/55922 NCBI-Mouse-GeneID:77286 http://www.ncbi.nlm.nih.gov/gene/77286 PR:000002043 An interferon regulatory factor 1/2 that is a translation product of the human IRF1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3659 NCBI-Mouse-GeneID:16362 NCBI-Rat-GeneID:24508 IRF-1 IRF1 interferon regulatory factor 1 NCBI-Human-GeneID:3659 http://www.ncbi.nlm.nih.gov/gene/3659 NCBI-Mouse-GeneID:16362 http://www.ncbi.nlm.nih.gov/gene/16362 NCBI-Rat-GeneID:24508 http://www.ncbi.nlm.nih.gov/gene/24508 PR:000002045 An interferon regulatory factor 3-9 that is a translation product of the human IRF3 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3661 NCBI-Mouse-GeneID:54131 NCBI-Rat-GeneID:292892 IRF-3 IRF3 interferon regulatory factor 3 NCBI-Human-GeneID:3661 http://www.ncbi.nlm.nih.gov/gene/3661 NCBI-Mouse-GeneID:54131 http://www.ncbi.nlm.nih.gov/gene/54131 NCBI-Rat-GeneID:292892 http://www.ncbi.nlm.nih.gov/gene/292892 PR:000002049 An interferon regulatory factor 3-9 that is a translation product of the human IRF7 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3665 NCBI-Mouse-GeneID:54123 NCBI-Rat-GeneID:293624 IRF-7 IRF7 interferon regulatory factor 7 NCBI-Human-GeneID:3665 http://www.ncbi.nlm.nih.gov/gene/3665 NCBI-Mouse-GeneID:54123 http://www.ncbi.nlm.nih.gov/gene/54123 NCBI-Rat-GeneID:293624 http://www.ncbi.nlm.nih.gov/gene/293624 PR:000002087 A signal transducer and transcription activator STAT that is a translation product of the human STAT1 gene or a 1:1 ortholog thereof. STAT1 signal transducer and activator of transcription 1-alpha/beta signal transducer and activator of transcription 1 PR:000002089 A signal transducer and transcription activator STAT that is a translation product of the human STAT3 gene or a 1:1 ortholog thereof. STAT3 acute-phase response factor signal transducer and activator of transcription 3 PR:000002122 An eotaxin-like cytokine that is a translation product of the human CCL2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:6347 NCBI-Mouse-GeneID:20296 NCBI-Rat-GeneID:24770 CCL2 HC11 MCAF monocyte chemoattractant protein 1 monocyte chemotactic and activating factor MCP1 C-C motif chemokine 2 NCBI-Human-GeneID:6347 http://www.ncbi.nlm.nih.gov/gene/6347 NCBI-Mouse-GeneID:20296 http://www.ncbi.nlm.nih.gov/gene/20296 NCBI-Rat-GeneID:24770 http://www.ncbi.nlm.nih.gov/gene/24770 PR:000002123 NCBI-Human-GeneID:6348 CCL3 MIP-1-alpha macrophage inflammatory protein 1-alpha C-C motif chemokine 3 HOIP_0041807 NCBI-Human-GeneID:6348 http://www.ncbi.nlm.nih.gov/gene/6348 PR:000002186 A protein that is a translation product of the human BCL2, BCL2L1, or BCL2L2 genes, 1:1 orthologs thereof, or a semi-ortholog thereof. The core domain architecture consists of an amino-terminal BH4 domain (Pfam:PF02180), which confers apoptosis inhibitory activity, and a Bcl-2 domain (Pfam:PF02180) common to many apoptosis regulator proteins. Bcl-2-like apoptosis inhibitor PR:000002190 An AKT kinase that is a translation product of the human AKT1 gene or a 1:1 ortholog thereof. PKB AKT1 kinase PKB alpha RAC-PK-alpha protein kinase B protein kinase B alpha proto-oncogene c-Akt thymoma viral proto-oncogene Akt RAC AKT1 PR:000002193 A protein that is a translation product of the human BAX gene or a 1:1 ortholog thereof. In this class the Bcl-2 domain is characterized by the presence of the BH3, BH1, and BH2 motifs. Bcl-2-like protein 4 Bcl2-L-4 apoptosis regulator BAX BCL2L4 BAX PR:000002307 An apoptosis regulator Bcl-2 that is encoded in the genome of human. NCBI-Human-GeneID:596 NCBI-Mouse-GeneID:12043 NCBI-Rat-GeneID:24224 apoptosis regulator Bcl-2 BCL2 NCBI-Human-GeneID:596 http://www.ncbi.nlm.nih.gov/gene/596 NCBI-Mouse-GeneID:12043 http://www.ncbi.nlm.nih.gov/gene/12043 NCBI-Rat-GeneID:24224 http://www.ncbi.nlm.nih.gov/gene/24224 PR:000002308 A Bcl-2-like apoptosis inhibitor that is a translation product of the human BCL2L1 gene or a 1:1 ortholog thereof. Bcl-2-like protein 1 Bcl2-L-1 apoptosis regulator Bcl-X BCL2L BCLX BCL2L1 PR:000002309 A caspase-1-like protease that is a translation product of the human CASP1 gene or a 1:1 ortholog thereof. The active form of this protein proteolytically cleaves pro-IL-1beta to its mature, active form. The holoenzyme is a homodimer of catalytic domains, each of which contains the cleaved products caspase-1 p20 and p10 subunits. NCBI-Human-GeneID:834 NCBI-Rat-GeneID:25166 caspase-1 NCBI-Human-GeneID:834 https://www.ncbi.nlm.nih.gov/gene/834 NCBI-Rat-GeneID:25166 https://www.ncbi.nlm.nih.gov/gene/25166 PR:000003035 A protein that is a translation product of the human TP53 gene or a 1:1 ortholog thereof. Antigen NY-CO-13 Cellular tumor antigen p53 P53 Phosphoprotein p53 Tumor suppressor p53 p53 protein TP53 PR:000003041 A protein that is a translation product of the human MTOR gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:2475 NCBI-Mouse-GeneID:56717 NCBI-Rat-GeneID:56718 https://omim.org/entry/601231 FK506-binding protein 12-rapamycin complex-associated protein 1 FKBP12-rapamycin complex-associated protein mTOR mammalian target of rapamycin mechanistic target of rapamycin rapamycin target protein 1 serine/threonine-protein kinase mTOR MTOR NCBI-Human-GeneID:2475 https://www.ncbi.nlm.nih.gov/gene/2475 NCBI-Mouse-GeneID:56717 https://www.ncbi.nlm.nih.gov/gene/56717 NCBI-Rat-GeneID:56718 https://www.ncbi.nlm.nih.gov/gene/56718 PR:000003090 A protein that is a translation product of the human CDKN1B gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:1026 cyclin-dependent kinase inhibitor 1B cyclin-dependent kinase inhibitor p27 p27Kip1 KIP1 p27 CDKN1B NCBI-Human-GeneID:1026 http://www.ncbi.nlm.nih.gov/gene/1026 PR:000003106 A protein that is a serine/threonine-specific protein kinase that responds to extracellular stimuli (environmental stress, pro-inflammatory cytokines and lipopolysaccharide) and regulates cellular activities such as gene expression, mitosis, differentiation, and cell survival/apoptosis. The activated form phosphorylates target substrates on Ser or Thr residues followed by a proline. A distinguishing feature is the conserved sequence TxY. https://en.wikipedia.org/wiki/P38_mitogen-activated_protein_kinases map kinase p38 MAPKp38 PR:000003107 A map kinase p38 that is a translation product of the human MAPK14 gene or a 1:1 ortholog thereof. CRK1 CSAID-binding protein MAP kinase 14 MAP kinase MXI2 MAP kinase p38 alpha MAPK 14 MAX-interacting protein 2 cytokine suppressive anti-inflammatory drug-binding protein mitogen-activated protein kinase 14 mitogen-activated protein kinase p38 alpha CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A MAPK14 PR:000003137 A subtilisin/kexin-type proprotein convertase that is a translation product of the FURIN gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:5045 NCBI-Mouse-GeneID:18550 NCBI-Rat-GeneID:54281 PACE furin NCBI-Human-GeneID:5045 https://www.ncbi.nlm.nih.gov/gene/5045 NCBI-Mouse-GeneID:18550 https://www.ncbi.nlm.nih.gov/gene/18550 NCBI-Rat-GeneID:54281 https://www.ncbi.nlm.nih.gov/gene/54281 PR:000003237 A protein that is a stand alone version of the 14-3-3 protein (Pfam:PF00244) domain. PMID:11911880 14-3-3 PR:000003271 A CDK2-related kinase that is a translation product of the human CDK1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:983 NCBI-Mouse-GeneID:12534 NCBI-Rat-GeneID:54237 http://www.reactome.org/content/detail/R-HSA-68889 cell division control protein 2 homolog cell division protein kinase 1 cyclin-dependent kinase 1 CDC2 CDC28A CDKN1 P34CDC2 p33 protein kinase p34 protein kinase CDK1 NCBI-Human-GeneID:983 http://www.ncbi.nlm.nih.gov/gene/983 NCBI-Mouse-GeneID:12534 http://www.ncbi.nlm.nih.gov/gene/12534 NCBI-Rat-GeneID:54237 http://www.ncbi.nlm.nih.gov/gene/54237 PR:000003292 A protein that is a translation product of the human NFKBIA, NFKBIB, or NFKBIE genes, 1:1 orthologs thereof, or a semi-ortholog thereof. It contains multiple copies of the Ankyrin repeats (Pfam:PF00023 or Pfam:PF12796). IkB inhibitor of NF-kappaB NF-kappa-B inhibitor PR:000003293 An NF-kappa-B inhibitor that is a translation product of the human NFKBIA gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:4792 NCBI-Mouse-GeneID:18035 NCBI-Rat-GeneID:25493 I-kappaB alpha IkB-alpha inhibitor of NF-kappaB alpha NF-kappa-B inhibitor alpha NCBI-Human-GeneID:4792 https://www.ncbi.nlm.nih.gov/gene/4792 NCBI-Mouse-GeneID:18035 https://www.ncbi.nlm.nih.gov/gene/18035 NCBI-Rat-GeneID:25493 https://www.ncbi.nlm.nih.gov/gene/25493/ PR:000003502 A leukocyte granule-associated proteinase that is a translation product of the human GZMA gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3001 UniProtKB:P12544 granzyme A (human) NCBI-Human-GeneID:3001 http://www.ncbi.nlm.nih.gov/gene/3001 PR:000003622 A protein that is a translation product of the human ACE2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:59272 NCBI-Mouse-GeneID:70008 NCBI-Rat-GeneID:302668 ACE2 angiotensin-converting enzyme 2 NCBI-Human-GeneID:59272 http://www.ncbi.nlm.nih.gov/gene/59272 NCBI-Mouse-GeneID:70008 http://www.ncbi.nlm.nih.gov/gene/70008 NCBI-Rat-GeneID:302668 http://www.ncbi.nlm.nih.gov/gene/302668 PR:000003912 An AKT kinase that is a translation product of the human AKT2 gene or a 1:1 ortholog thereof. PKB beta RAC-PK-beta RAC-beta serine/threonine protein kinase protein kinase B beta AKT2 PR:000003913 PKB gamma RAC-PK-gamma RAC-gamma serine/threonine protein kinase STK-2 protein kinase B gamma AKT3 PR:000004024 NCBI-Human-GeneID:285 NCBI-Mouse-GeneID:11601 NCBI-Rat-GeneID:89805 ANG-2 ANGPT2 angiopoietin-2 NCBI-Human-GeneID:285 http://www.ncbi.nlm.nih.gov/gene/285 NCBI-Mouse-GeneID:11601 http://www.ncbi.nlm.nih.gov/gene/11601 NCBI-Rat-GeneID:89805 http://www.ncbi.nlm.nih.gov/gene/89805 PR:000004158 NCBI-Human-GeneID:8542 APOL1 ApoL ApoL-I apo-L apolipoprotein L apolipoprotein L-I apolipoprotein L1 NCBI-Human-GeneID:8542 http://www.ncbi.nlm.nih.gov/gene/8542 PR:000004367 A protein that is a translation product of the human ASF1A gene or a 1:1 ortholog thereof. ASF1 CCG1-interacting factor A anti-silencing function protein 1 homolog A histone chaperone ASF1A CGI-98 CIA HSPC146 hAsf1 ASF1A PR:000004427 A protein that is a translation product of the human ATM gene or a 1:1 ortholog thereof. https://www.ncbi.nlm.nih.gov/gene/641371 NCBI-Human-GeneID:472 NCBI-Mouse-GeneID:11920 NCBI-Rat-GeneID:300711 A-T mutated A-T mutated homolog ataxia telangiectasia mutated ataxia telangiectasia mutated homolog serine-protein kinase ATM ATM HOIP_0003252 NCBI-Human-GeneID:472 http://www.ncbi.nlm.nih.gov/gene/472 NCBI-Mouse-GeneID:11920 http://www.ncbi.nlm.nih.gov/gene/11920 NCBI-Rat-GeneID:300711 http://www.ncbi.nlm.nih.gov/gene/300711 PR:000004499 A protein that is a translation product of the human ATR gene, the yeast MEC1 gene, or 1:1 orthologs thereof. IUPHARobj:1935 NCBI-Human-GeneID:545 NCBI-Mouse-GeneID:245000 NCBI-Rat-GeneID:685055 DNA-damage checkpoint kinase MEC1 FRAP-related protein 1 ataxia telangiectasia and Rad3-related protein mitosis entry checkpoint protein 1 serine/threonine-protein kinase ATR FRP1 Kiaa4069 ATR NCBI-Human-GeneID:545 http://www.ncbi.nlm.nih.gov/gene/545 NCBI-Mouse-GeneID:245000 http://www.ncbi.nlm.nih.gov/gene/245000 NCBI-Rat-GeneID:685055 http://www.ncbi.nlm.nih.gov/gene/685055 PR:000004515 An aurora kinase that is a translation product of the human AURKA gene or a 1:1 ortholog thereof. ARK-1 AURKA aurora kinase A PR:000004698 A Bcl-2-like apoptosis inhibitor that is a translation product of the human BCL2L2 gene or a 1:1 ortholog thereof. BCL2L2-PABPN1 protein | Bcl-2-like protein 2 Bcl2-L-2 apoptosis regulator Bcl-W BCLW BCL2L2 PR:000004770 A protein that is a translation product of the human BMI1 gene or a 1:1 ortholog thereof. Polycomb group RING finger protein 4 RING finger protein 51 Polycomb complex protein BMI-1 BMI1 PR:000004801 A protein that is a translation product of the human BRAF gene or a 1:1 ortholog thereof. V-Raf murine sarcoma viral oncogene homolog B1 p94 (human) proto-oncogene B-Raf serine/threonine-protein kinase B-raf BRAF BRAF1 RAFB1 BRAF PR:000005114 A cyclin-A that is a translation product of the human CCNA1 gene or a 1:1 ortholog thereof. cyclin-A1 CCNA1 PR:000005116 A G2/mitotic-specific cyclin-B that is a translation product of the human CCNB1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:891 NCBI-Mouse-GeneID:268697 NCBI-Rat-GeneID:25203 G2/mitotic-specific cyclin-B1 CCNB Ccn-2 Ccnb1-rs13 Cycb Cycb1 CCNB1 HOIP_0004227 NCBI-Human-GeneID:891 http://www.ncbi.nlm.nih.gov/gene/891 NCBI-Mouse-GeneID:268697 http://www.ncbi.nlm.nih.gov/gene/268697 NCBI-Rat-GeneID:25203 http://www.ncbi.nlm.nih.gov/gene/25203 PR:000005118 A G2/mitotic-specific cyclin-B that is a translation product of the human CCNB2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:9133 NCBI-Mouse-GeneID:12442 NCBI-Rat-GeneID:363088 Cycb2 CCNB2 NCBI-Human-GeneID:9133 http://www.ncbi.nlm.nih.gov/gene/9133 NCBI-Mouse-GeneID:12442 http://www.ncbi.nlm.nih.gov/gene/12442 NCBI-Rat-GeneID:363088 http://www.ncbi.nlm.nih.gov/gene/363088 PR:000005121 A cyclin-D that is a translation product of the human CCND1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:595 NCBI-Mouse-GeneID:12443 NCBI-Rat-GeneID:58919 B-cell lymphoma 1 protein BCL-1 BCL-1 oncogene G1/S-specific cyclin-D1 PRAD1 oncogene Cyclin D1 NCBI-Human-GeneID:595 http://www.ncbi.nlm.nih.gov/gene/595 NCBI-Mouse-GeneID:12443 http://www.ncbi.nlm.nih.gov/gene/12443 NCBI-Rat-GeneID:58919 http://www.ncbi.nlm.nih.gov/gene/58919 PR:000005125 A cyclin-E that is a translation product of the human CCNE1 gene or a 1:1 ortholog thereof. G1/S-specific cyclin-E1 CCNE1 PR:000005201 A protein that is a translation product of the human CDC37 gene or a 1:1 ortholog thereof. UniProtKB:O02108 CDC37 Hsp90 chaperone protein kinase-targeting subunit p50Cdc37 CDC37A W08F4.8 Hsp90 co-chaperone cdc37 PR:000005204 A protein that is a translation product of the human CDC42 gene or a 1:1 ortholog thereof. CDC42 G25K GTP-binding protein cell division control protein 42 PR:000005253 A CDK2-related kinase that is a translation product of the human CDK2 gene or a 1:1 ortholog thereof. Cell division protein kinase 2 Cell division protein kinase 2 (EC 2.7.1.-)(p33 protein kinase)(CDK2) cyclin-dependent kinase 2 p33 protein kinase CDKN2 CDK2 PR:000005257 A CDK2-related kinase that is a translation product of the human CDK4 gene or a 1:1 ortholog thereof. cyclin dependent kinase 4 NCBI-Human-GeneID:1019 NCBI-Mouse-GeneID:12567 NCBI-Rat-GeneID:94201 OMIM:123829 CRK3 Cell division protein kinase 4 Cell division protein kinase 4 (EC 2.7.1.- ) (Cyclin-dependent kinase 4) (PSK-J3) (CDK4) PSK-J3 CDK4 NCBI-Human-GeneID:1019 http://www.ncbi.nlm.nih.gov/gene/1019 NCBI-Mouse-GeneID:12567 http://www.ncbi.nlm.nih.gov/gene/12567 NCBI-Rat-GeneID:94201 http://www.ncbi.nlm.nih.gov/gene/94201 PR:000005264 A CDK2-related kinase that is a translation product of the human CDK6 gene or a 1:1 ortholog thereof. CRK2 Cdk6 Cell division protein kinase 6 Cell division protein kinase 6 (EC 2.7.1.-)(Serine/threonine-protein kinase) (PLSTIRE)(CDK6) Serine/threonine protein kinase PLSTIRE CDK6 PR:000005274 A protein that is a translation product of the human CDKN1A gene or a 1:1 ortholog thereof. p21 NCBI-Human-GeneID:1026 NCBI-Mouse-GeneID:12575 NCBI-Rat-GeneID:114851 CDK-interacting protein 1 MDA-6 cyclin-dependent kinase inhibitor 1 melanoma differentiation-associated protein melanoma differentiation-associated protein 6 CDKN1A NCBI-Human-GeneID:1026 http://www.ncbi.nlm.nih.gov/gene/1026 NCBI-Mouse-GeneID:12575 http://www.ncbi.nlm.nih.gov/gene/12575 NCBI-Rat-GeneID:114851 http://www.ncbi.nlm.nih.gov/gene/114851 PR:000005308 A protein that is a translation product of the human CEBPB gene or a 1:1 ortholog thereof. AGP/EBP C/EBP beta CCAAT/enhancer-binding protein beta IL-6DBP TCF-5 interleukin-6-dependent-binding protein liver activator protein liver-enriched transcriptional activator nuclear factor NF-IL6 transcription factor 5 PP9092 TCF5 CEBPB PR:000005417 A protein that is a translation product of the human CHEK1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:1111 CHK1 checkpoint homolog cell cycle checkpoint kinase checkpoint kinase-1 serine/threonine-protein kinase Chk1 CHK1 CHEK1 NCBI-Human-GeneID:1111 http://www.ncbi.nlm.nih.gov/gene/1111 PR:000005418 A protein that is a translation product of the human CHEK2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:11200 CHK2 checkpoint homolog cds1 checkpoint kinase 2 serine/threonine-protein kinase Chk2 CDS1 CHK2 RAD53 CHEK2 NCBI-Human-GeneID:11200 http://www.ncbi.nlm.nih.gov/gene/11200 PR:000005442 A protein that is a translation product of the human CHN1 gene or a 1:1 ortholog thereof. N-chimaerin CHN CHN1 PR:000005513 A creatine kinase that is a translation product of the human CKB gene or a 1:1 ortholog thereof. CKB creatine kinase, brain creatine kinase B type PR:000005515 A creatine kinase that is a translation product of the human CKM gene or a 1:1 ortholog thereof. CKM creatine kinase, muscle creatine kinase M type PR:000005931 NCBI-Human-GeneID:1437 NCBI-Mouse-GeneID:12981 NCBI-Rat-GeneID:116630 GM-CSF granulocyte-macrophage colony-stimulating factor NCBI-Human-GeneID:1437 http://www.ncbi.nlm.nih.gov/gene/1437 NCBI-Mouse-GeneID:12981 http://www.ncbi.nlm.nih.gov/gene/50798 NCBI-Rat-GeneID:116630 http://www.ncbi.nlm.nih.gov/gene/116630 PR:000005932 A protein that is a translation product of the human CSF3 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:1440 NCBI-Mouse-GeneID:12985 NCBI-Rat-GeneID:25610 CSF3 GCSF granulocyte colony-stimulating factor NCBI-Human-GeneID:1440 http://www.ncbi.nlm.nih.gov/gene/1440 NCBI-Mouse-GeneID:12985 http://www.ncbi.nlm.nih.gov/gene/12985 NCBI-Rat-GeneID:25610 http://www.ncbi.nlm.nih.gov/gene/25610 PR:000006023 A cathepsin-like protease that is a translation product of the human CTSB gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:1508 NCBI-Mouse-GeneID:13030 NCBI-Rat-GeneID:64529 APP secretase APPS CTSB cathepsin B1 cathepsin B HOIP_0003843 NCBI-Human-GeneID:1508 https://www.ncbi.nlm.nih.gov/gene/1508 NCBI-Mouse-GeneID:13030 https://www.ncbi.nlm.nih.gov/gene/13030 NCBI-Rat-GeneID:64529 https://www.ncbi.nlm.nih.gov/gene/64529 PR:000006030 NCBI-Human-GeneID:1514 CTSL cathepsin L1 major excreted protein procathepsin L NCBI-Human-GeneID:1514 https://www.ncbi.nlm.nih.gov/gene/1514 PR:000006063 A protein that is a translation product of the human CXCL1 gene or a 1:1 ortholog thereof. C-X-C motif chemokine 1 GRO-alpha(1-73) NAP-3 growth-regulated alpha protein melanoma growth stimulatory activity neutrophil-activating protein 3 platelet-derived growth factor-inducible protein KC secretory protein N51 GRO GRO1 GROA MGSA SCYB1 CXCL1 PR:000006064 NCBI-Human-GeneID:3627 NCBI-Mouse-GeneID:15945 NCBI-Rat-GeneID:3627 10 kDa interferon gamma-induced protein C-X-C motif chemokine 10 IP-10 gamma-IP10 CXCL10 HOIP_0003281 NCBI-Human-GeneID:3627 http://www.ncbi.nlm.nih.gov/gene/3627 NCBI-Mouse-GeneID:15945 http://www.ncbi.nlm.nih.gov/gene/15945 NCBI-Rat-GeneID:3627 http://www.ncbi.nlm.nih.gov/gene/245920 PR:000006601 A protein that is a translation product of the human DNM1 gene or a 1:1 ortholog thereof. DNM1 (mol) PR:000006852 An E2F protein that is a translation product of the human E2F1 gene or a 1:1 ortholog thereof. E2F-1 PBR3 RBAP-1 RBBP-3 pRB-binding protein E2F-1 transcription factor E2F1 E2F1 PR:000006885 A protein that is a translation product of the human ECT2 gene or a 1:1 ortholog thereof. epithelial cell-transforming sequence 2 oncogene ECT2 PR:000006959 A protein that is a translation product of the human EIF2AK2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:5610 NCBI-Mouse-GeneID:19106 NCBI-Rat-GeneID:54287 EIF2AK2 PKR eIF-2A protein kinase 2 protein kinase R interferon-induced, double-stranded RNA-activated protein kinase NCBI-Human-GeneID:5610 http://www.ncbi.nlm.nih.gov/gene/5610 NCBI-Mouse-GeneID:19106 http://www.ncbi.nlm.nih.gov/gene/19106 NCBI-Rat-GeneID:54287 http://www.ncbi.nlm.nih.gov/gene/54287 PR:000007102 A transcription adapter with TAZ, KIX and bromo-domains that is a translation product of the human EP300 gene or a 1:1 ortholog thereof. E1A-associated protein p300 histone acetyltransferase p300 histone butyryltransferase p300 histone crotonyltransferase p300 p300 HAT EP300 PR:000007221 A protein that is a translation product of the human ETS1 gene or a 1:1 ortholog thereof. p54 E26 transformation-specific1 protein C-ets-1 ETS1 PR:000007222 A protein that is a translation product of the human ETS2 gene or a 1:1 ortholog thereof. E26 transformation-specific2 protein C-ets-2 ETS2 PR:000007640 A protein that is a translation product of the human FOXO1 gene or a 1:1 ortholog thereof. FKHR FOXO1A forkhead box protein O1 forkhead box protein O1A forkhead in rhabdomyosarcoma FOXO1 PR:000007641 A protein that is a translation product of the human FOXO3 gene or a 1:1 ortholog thereof. AF6q21 protein forkhead box protein O3 forkhead in rhabdomyosarcoma-like 1 FKHRL1 FOXO3A FOXO3 PR:000007859 A protein that is a translation product of the human GATA4 gene or a 1:1 ortholog thereof. GATA-binding factor 4 transcription factor GATA-4 Gata-4 GATA4 PR:000008016 A protein that is a translation product of the human GLB1 gene or a 1:1 ortholog thereof in eukaryotes. The eukaryotic-type beta-galactosidase contains a Glycosyl hydrolases family 35 (Pfam:PF01301) domain instead of the Glycosyl hydrolases family 2 (Pfam:PF00703) domain typical of the bacterial-type acid beta-galactosidase beta-galactosidase 1 elastin receptor 1 eukaryotic-type beta-galactosidase GLB1 PR:000008153 A protein that is a translation product of the GOT1 gene or a 1:1 ortholog thereof. AST transaminase A NCBI-Human-GeneID:2805 NCBI-Mouse-GeneID:14718 NCBI-Rat-GeneID:24401 GOT1 glutamic-oxaloacetic transaminase 1 Note: This form is predominantly found in red blood cells and heart in humans. aspartate aminotransferase, cytoplasmic NCBI-Human-GeneID:2805 http://www.ncbi.nlm.nih.gov/gene/2805 NCBI-Mouse-GeneID:14718 http://www.ncbi.nlm.nih.gov/gene/14718 NCBI-Rat-GeneID:24401 http://www.ncbi.nlm.nih.gov/gene/24401 PR:000008208 A protein that is a translation product of the human GPT gene or a 1:1 ortholog thereof. ALT NCBI-Human-GeneID:2875 NCBI-Mouse-GeneID:76282 NCBI-Rat-GeneID:81670 ALT1 GPT GPT1 glutamate pyruvate transaminase 1 glutamic--pyruvic transaminase alanine aminotransferase 1 NCBI-Human-GeneID:2875 http://www.ncbi.nlm.nih.gov/gene/2875 NCBI-Mouse-GeneID:76282 http://www.ncbi.nlm.nih.gov/gene/76282 NCBI-Rat-GeneID:81670 http://www.ncbi.nlm.nih.gov/gene/81670 PR:000008418 A histone H2A that is a translation product of the human H2AFX gene or a 1:1 ortholog thereof. HGNC:4739 Hist5-2ax NCBI-Human-GeneID:3014 H2a/x histone H2A.X histone H2A.x histone H2AX H2a.x H2AFX NCBI-Human-GeneID:3014 http://www.ncbi.nlm.nih.gov/gene/3014 PR:000008419 A histone H2A that is a translation product of the human MACROH2A1 gene or a 1:1 ortholog thereof. H2A.y H2A/y core histone macro-H2A.1 histone H2A.y histone macroH2A1 mH2A1 medulloblastoma antigen MU-MB-50.205 H2AFY MACROH2A1 PR:000008555 A protein that is a translation product of the human HIF1A gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3091 NCBI-Mouse-GeneID:15251 NCBI-Rat-GeneID:29560 HIF-1-alpha HIF1A hypoxia-inducible factor 1-alpha NCBI-Human-GeneID:3091 http://www.ncbi.nlm.nih.gov/gene/3091 NCBI-Mouse-GeneID:15251 http://www.ncbi.nlm.nih.gov/gene/15251 NCBI-Rat-GeneID:29560 http://www.ncbi.nlm.nih.gov/gene/29560 PR:000008570 A protein that is a translation product of the human HIRA gene or a 1:1 ortholog thereof. TUP1-like enhancer of split protein 1 protein HIRA DGCR1 HIR TUPLE1 HIRA PR:000008628 A protein that is a translation product of the human HMGA1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3159 NCBI-Mouse-GeneID:15361 NCBI-Rat-GeneID:117062 HMG-I(Y) high mobility group AT-hook protein 1 high mobility group protein A1 high mobility group protein HMG-I/HMG-Y high mobility group protein R HMGIY Hmgi HMGA1 NCBI-Human-GeneID:3159 http://www.ncbi.nlm.nih.gov/gene/3159 NCBI-Mouse-GeneID:15361 http://www.ncbi.nlm.nih.gov/gene/15361 NCBI-Rat-GeneID:117062 http://www.ncbi.nlm.nih.gov/gene/117062 PR:000008629 A protein that is a translation product of the human HMGA2 gene or a 1:1 ortholog thereof. high mobility group AT-hook protein 2 high mobility group protein HMGI-C HMGIC HMGA2 PR:000008630 A protein that is a translation product of the human HMGB1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3146 NCBI-Mouse-GeneID:15289 HMG-1 high mobility group protein 1 high mobility group protein B1 HMGB1 NCBI-Human-GeneID:3146 http://www.ncbi.nlm.nih.gov/gene/3146 NCBI-Mouse-GeneID:15289 http://www.ncbi.nlm.nih.gov/gene/15289 PR:000008905 A protein that is a translation product of the human IFI30 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:10437 NCBI-Mouse-GeneID:65972 NCBI-Rat-GeneID:290644 IFI30 gamma-interferon-inducible protein IP-30 gamma-interferon-inducible lysosomal thiol reductase HOIP_0040273 NCBI-Human-GeneID:10437 http://www.ncbi.nlm.nih.gov/gene/10437 NCBI-Mouse-GeneID:65972 http://www.ncbi.nlm.nih.gov/gene/65972 NCBI-Rat-GeneID:290644 http://www.ncbi.nlm.nih.gov/gene/290644 PR:000008915 NCBI-Human-GeneID:3440 IFN-alpha-2 IFNA2 interferon alpha-2 NCBI-Human-GeneID:3440 https://www.ncbi.nlm.nih.gov/gene/3440 PR:000008922 A protein that is a translation product of the IFNAR1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3454 CRF2-1 IFN-R-1 IFN-alpha/beta receptor 1 IFNAR1 Interferon alpha/beta receptor-1 interferon-alpha/beta receptor alpha chain NCBI-Human-GeneID:3454 http://www.ncbi.nlm.nih.gov/gene/3454 PR:000008923 A protein that is a translation product of the IFNAR2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3455 IFNAR2 Interferon alpha/beta receptor-2 interferon alpha/beta receptor 2 NCBI-Human-GeneID:3455 http://www.ncbi.nlm.nih.gov/gene/3455 PR:000008924 An interferon beta that is a translation product of the human IFNB1 gene or a 1:1 ortholog thereof. IFN-beta IFNB1 Interferon beta interferon beta 1 PR:000008926 A protein that is a translation product of the IFNGR2 gene or a 1:1 ortholog thereof. IFNG receptor beta chain accessory factor-1 interferon-gamma receptor beta chain IFNGR2 PR:000008942 A protein that is a translation product of the human IGF2 gene or a 1:1 ortholog thereof. IGF-II insulin-like growth factor II PR:000008953 A protein that is a translation product of the human IGFBP7 gene or a 1:1 ortholog thereof. insulin-like growth factor-binding protein 7 IBP-7 TAF IGFBP7 PR:000009054 An insulin family protein that is a translation product of the human INS gene or a 1:1 ortholog thereof. A protein hormone secreted by beta cells of the pancreas. Insulin plays a major role in the regulation of glucose metabolism, generally promoting the cellular utilization of glucose. It is also an important regulator of protein and lipid metabolism. Insulin is used as a drug to control insulin-dependent diabetes mellitus. A protein hormone secreted by beta cells of the pancreas. Insulin plays a major role in the regulation of glucose metabolism, generally promoting the cellular utilization of glucose. It is also an important regulator of protein and lipid metabolism. Insulin is used as a drug to control insulin-dependent diabetes mellitus. MeSH:D007328 INS insulin A protein hormone secreted by beta cells of the pancreas. Insulin plays a major role in the regulation of glucose metabolism, generally promoting the cellular utilization of glucose. It is also an important regulator of protein and lipid metabolism. Insulin is used as a drug to control insulin-dependent diabetes mellitus. MeSH:D007328 PR:000009064 A protein that is a translation product of the human INSR gene or a 1:1 ortholog thereof. CD220 antigen INSR IR insulin receptor alpha subunit insulin receptor beta subunit insulin receptor precursor insulin receptor PR:000009182 A protein that is a translation product of the human IGF1 gene or a 1:1 ortholog thereof. IGF-I insulin-like growth factor I PR:000009196 A Janus kinase that is a translation product of the human JAK1 gene or a 1:1 ortholog thereof. JAK-1 JAK1 tyrosine-protein kinase JAK1 PR:000009217 A protein that is a translation product of the human KDM6B gene or a 1:1 ortholog thereof. JmjC domain-containing protein 3 [histone H3]-trimethyl-L-lysine(27) demethylase 6B histone demethylase JMJD3 lysine-specific demethylase 6B JMJD3 KIAA0346 KDM6B PR:000009347 A protein that is a translation product of the human KL gene or a 1:1 ortholog thereof. klotho KL PR:000009420 A protein that is a translation product of the human KLKB1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3818 NCBI-Mouse-GeneID:16621 NCBI-Rat-GeneID:25048 KLKB1 fletcher factor kininogenin plasma kallikrein NCBI-Human-GeneID:3818 http://www.ncbi.nlm.nih.gov/gene/3818 NCBI-Mouse-GeneID:16621 http://www.ncbi.nlm.nih.gov/gene/16621 NCBI-Rat-GeneID:25048 http://www.ncbi.nlm.nih.gov/gene/25048 PR:000009442 A protein that is a translation product of the human KRAS gene or a 1:1 ortholog thereof NCBI-Human-GeneID:3845 NCBI-Mouse-GeneID:16653 NCBI-Rat-GeneID:24525 GTPase KRas K-Ras KRAS2 Ki-ras KRAS NCBI-Human-GeneID:3845 https://www.ncbi.nlm.nih.gov/gene/3845 NCBI-Mouse-GeneID:16653 https://www.ncbi.nlm.nih.gov/gene/16653 NCBI-Rat-GeneID:24525 https://www.ncbi.nlm.nih.gov/gene/24525 PR:000009739 An L-lactate dehydrogenase, cytoplasmic that is a translation product of the human LDHA gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3939 NCBI-Mouse-GeneID:16828 NCBI-Rat-GeneID:24533 LDH-A LDH-M lactate dehydrogenase A L-lactate dehydrogenase A chain HOIP_0040102 NCBI-Human-GeneID:3939 http://www.ncbi.nlm.nih.gov/gene/3939 NCBI-Mouse-GeneID:16828 http://www.ncbi.nlm.nih.gov/gene/16828 NCBI-Rat-GeneID:24533 http://www.ncbi.nlm.nih.gov/gene/24533 PR:000009766 A protein that is a translation product of the human LGALS1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3956 NCBI-Mouse-GeneID:16852 NCBI-Rat-GeneID:56646 14 kDa laminin-binding protein HBL LGALS1 gal-1 lectin galactoside-binding soluble 1 galectin-1 NCBI-Human-GeneID:3956 http://www.ncbi.nlm.nih.gov/gene/3956 NCBI-Mouse-GeneID:16852 http://www.ncbi.nlm.nih.gov/gene/16852 NCBI-Rat-GeneID:56646 http://www.ncbi.nlm.nih.gov/gene/56646 PR:000009860 A protein that is a translation product of the human LMNB1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:4001 NCBI-Mouse-GeneID:16906 NCBI-Rat-GeneID:116685 LMN2 LMNB lamin-B1 LMNB1 NCBI-Human-GeneID:4001 http://www.ncbi.nlm.nih.gov/gene/4001 NCBI-Mouse-GeneID:16906 http://www.ncbi.nlm.nih.gov/gene/16906 NCBI-Rat-GeneID:116685 http://www.ncbi.nlm.nih.gov/gene/116685 PR:000009897 A protein that is a translation product of the human LPL gene or a 1:1 ortholog thereof. Category=gene. LPL lipoprotein lipase PR:000009989 An Ly-6-like protein that is a translation product of the human LY6E gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:4061 NCBI-Mouse-GeneID:17069 NCBI-Rat-GeneID:362934 Ly6E RIG-E SCA-2 TSA-1 retinoic acid-induced gene E protein stem cell antigen 2 thymic shared antigen 1 lymphocyte antigen 6E NCBI-Human-GeneID:4061 http://www.ncbi.nlm.nih.gov/gene/4061 NCBI-Mouse-GeneID:17069 http://www.ncbi.nlm.nih.gov/gene/17069 NCBI-Rat-GeneID:362934 http://www.ncbi.nlm.nih.gov/gene/362934 PR:000010120 A protein that is a translation product of the human MAP1LC3B gene or a 1:1 ortholog thereof. MAP1 light chain 3-like protein 2 MAP1A/MAP1B LC3 B MAP1A/MAP1B light chain 3 B autophagy-related protein LC3 B autophagy-related ubiquitin-like modifier LC3 B microtubule-associated protein 1 light chain 3 beta microtubule-associated proteins 1A/1B light chain 3B MAP1ALC3 MAP1LC3B PR:000010152 A map kinase p38 that is a translation product of the human MAPK11 gene or a 1:1 ortholog thereof. MAP kinase 11 MAP kinase p38 beta mitogen-activated protein kinase 11 mitogen-activated protein kinase p38 beta p38-2 p38b stress-activated protein kinase 2 PRKM11 SAPK2 SAPK2B MAPK11 PR:000010153 A map kinase p38 that is a translation product of the human MAPK12 gene or a 1:1 ortholog thereof. ERK-6 MAP kinase 12 MAP kinase p38 gamma MAPK 12 SAPK3 extracellular signal-regulated kinase 6 mitogen-activated protein kinase 12 mitogen-activated protein kinase p38 gamma stress-activated protein kinase 3 ERK6 MAPK12 PR:000010154 A map kinase p38 that is a translation product of the human MAPK13 gene or a 1:1 ortholog thereof. MAP kinase 13 MAP kinase p38 delta MAPK 13 PRKM3 SAPK4 mitogen-activated protein kinase 13 mitogen-activated protein kinase p38 delta stress-activated protein kinase 4 MAPK13 Serk4 PR:000010165 A protein that is a translation product of the human MAPKAPK2 gene or a 1:1 ortholog thereof. MAP kinase-activated protein kinase 2 MAPK- activated protein kinase 2 MK-2 MK2 MAPKAPK2 PR:000010194 A protein that is a translation product of the human MASP2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:10747 NCBI-Mouse-GeneID:17175 NCBI-Rat-GeneID:64459 MASP-2 MASP2 mannose-binding protein-associated serine protease 2 mannan-binding lectin serine protease 2 NCBI-Human-GeneID:10747 http://www.ncbi.nlm.nih.gov/gene/10747 NCBI-Mouse-GeneID:17175 http://www.ncbi.nlm.nih.gov/gene/17175 NCBI-Rat-GeneID:64459 http://www.ncbi.nlm.nih.gov/gene/64459 PR:000010210 A protein that is a translation product of the human MAVS gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:57506 CARD adapter inducing interferon beta IPS-1 MAVS cardif interferon beta promoter stimulator protein 1 mitochondrial antiviral-signaling protein putative NF-kappa-B-activating protein 031N virus-induced-signaling adapter mitochondrial antiviral-signaling protein NCBI-Human-GeneID:57506 http://www.ncbi.nlm.nih.gov/gene/57506 PR:000010220 A mannose-binding protein C that is encoded in the genome of human. NCBI-Human-GeneID:4153 NCBI-Mouse-GeneID:17195 MBP-C MBP1 collectin-1 mannose-binding protein C MBL2 HOIP_0041757 NCBI-Human-GeneID:4153 http://www.ncbi.nlm.nih.gov/gene/4153 NCBI-Mouse-GeneID:17195 http://www.ncbi.nlm.nih.gov/gene/17195 PR:000010258 A protein that is a translation product of the human MDC1 gene or a 1:1 ortholog thereof. mediator of DNA damage checkpoint protein 1 nuclear factor with BRCT domains 1 KIAA0170 NFBD1 MDC1 PR:000010267 A protein that is a translation product of the human MDM2 gene or a 1:1 ortholog thereof. IMR:0010776 E3 ubiquitin-protein ligase Mdm2 RING-type E3 ubiquitin transferase Mdm2 double minute 2 protein hdm2 oncoprotein Mdm2 p53-binding protein Mdm2 MDM2 PR:000010491 A protein that is a translation product of the human MMP9 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:4318 NCBI-Mouse-GeneID:17395 NCBI-Rat-GeneID:81687 92 kDa gelatinase 92 kDa type IV collagenase GELB gelatinase B matrix metalloproteinase-9 MMP9 NCBI-Human-GeneID:4318 http://www.ncbi.nlm.nih.gov/gene/4318 NCBI-Mouse-GeneID:17395 http://www.ncbi.nlm.nih.gov/gene/17395 NCBI-Rat-GeneID:81687 http://www.ncbi.nlm.nih.gov/gene/81687 PR:000010567 A protein that is a translation product of the human MYL12A gene or a 1:1 ortholog thereof. MLC-2B MYL12A myosin regulatory light chain 2, nonsarcomeric MLCB MRLC3 RLC myosin RLC myosin regulatory light chain MRLC3 PR:000010788 A protein that is a translation product of the human MX1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:4599 NCBI-Mouse-GeneID:17857 IFI-78K MX1 influenza resistance protein interferon-induced protein p78 interferon-regulated resistance GTP-binding protein MxA myxovirus resistance protein 1 interferon-induced GTP-binding protein Mx1 HOIP_0040223 NCBI-Human-GeneID:4599 http://www.ncbi.nlm.nih.gov/gene/4599 NCBI-Mouse-GeneID:17857 http://www.ncbi.nlm.nih.gov/gene/17857 PR:000011271 A protein that is a translation product of the human NLRP3 gene or a 1:1 ortholog thereof. NLRP3 is a inflammasome component NCBI-Human-GeneID:114548 NCBI-Mouse-GeneID:216799 NCBI-Rat-GeneID:287362 CLR1.1 NLRP3 PYRIN-containing APAF1-like protein 1 angiotensin/vasopressin receptor AII/AVP-like cold autoinflammatory syndrome 1 protein NACHT, LRR and PYD domains-containing protein 3 NCBI-Human-GeneID:114548 http://www.ncbi.nlm.nih.gov/gene/114548 NCBI-Mouse-GeneID:216799 http://www.ncbi.nlm.nih.gov/gene/216799 NCBI-Rat-GeneID:287362 http://www.ncbi.nlm.nih.gov/gene/287362 PR:000011574 A protein that is a translation product of the human OAS1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:4938 (2-5')oligo(A) synthetase 1 OAS1 2'-5'-oligoadenylate synthase 1 NCBI-Human-GeneID:4938 http://www.ncbi.nlm.nih.gov/gene/4938 PR:000012279 A protein that is a translation product of the human PARD3 gene or a 1:1 ortholog thereof. CTCL tumor antigen se2-5 PAR3-alpha atypical PKC isotype-specific-interacting protein partitioning defective 3 PAR-3 PAR3 PAR3A PARD3 (mol) PR:000012289 A protein that is a translation product of the human PARP1 gene or a 1:1 ortholog thereof. ADP-ribosyltransferase diphtheria toxin-like 1 ADPRT 1 ARTD1 DNA ADP-ribosyltransferase PARP1 NAD(+) ADP-ribosyltransferase 1 poly [ADP-ribose] polymerase 1 PARP1 PR:000012504 A protein that is a translation product of the human PDK1 gene or a 1:1 ortholog thereof. [pyruvate dehydrogenase [lipoamide]] kinase isozyme 1] PDH kinase 1 PDHK1 [pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial pyruvate dehydrogenase kinase isoform 1 PDK1 PR:000012513 A protein that is a translation product of the human PDP1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:57546 NCBI-Mouse-GeneID:382051 NCBI-Rat-GeneID:246311 PDP PDPC 1 PDPMC protein phosphatase 2C PDH pyruvate dehydrogenase phosphatase catalytic subunit 1 PDP1 NCBI-Human-GeneID:57546 http://www.ncbi.nlm.nih.gov/gene/57546 NCBI-Mouse-GeneID:382051 http://www.ncbi.nlm.nih.gov/gene/382051 NCBI-Rat-GeneID:246311 http://www.ncbi.nlm.nih.gov/gene/246311 PR:000012514 A protein that is a translation product of the human PDP2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:57546 NCBI-Mouse-GeneID:382051 NCBI-Rat-GeneID:246311 KIAA1348 PDPC 2 pyruvate dehydrogenase phosphatase catalytic subunit 2 PDP2 [pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial NCBI-Human-GeneID:57546 http://www.ncbi.nlm.nih.gov/gene/57546 NCBI-Mouse-GeneID:382051 http://www.ncbi.nlm.nih.gov/gene/382051 NCBI-Rat-GeneID:246311 http://www.ncbi.nlm.nih.gov/gene/246311 PR:000012580 A 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase that is a translation product of the human PFKFB3 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:5209 NCBI-Mouse-GeneID:170768 NCBI-Rat-GeneID:117276 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 PFK/FBPase 3 PFKFB3 iPFK-2 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 HOIP_0040060 NCBI-Human-GeneID:5209 http://www.ncbi.nlm.nih.gov/gene/5209 NCBI-Mouse-GeneID:170768 http://www.ncbi.nlm.nih.gov/gene/170768 NCBI-Rat-GeneID:117276 http://www.ncbi.nlm.nih.gov/gene/117276 PR:000012747 A protein that is a translation product of the human PIKFYVE gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:200576 NCBI-Mouse-GeneID:18711 NCBI-Rat-GeneID:316457 FYVE finger-containing phosphoinositide kinase KIAA0981 PIKFYVE phosphatidylinositol 3-phosphate 5-kinase type III 1-phosphatidylinositol 3-phosphate 5-kinase NCBI-Human-GeneID:200576 https://www.ncbi.nlm.nih.gov/gene/200576 NCBI-Mouse-GeneID:18711 https://www.ncbi.nlm.nih.gov/gene/18711 NCBI-Rat-GeneID:316457 https://www.ncbi.nlm.nih.gov/gene/316457 PR:000012783 A protein that is a translation product of the human PKM gene or a 1:1 ortholog thereof. CTHBP OIP-3 cytosolic thyroid hormone-binding protein NCBI-Human-GeneID:5315 NCBI-Mouse-GeneID:18746 NCBI-Rat-GeneID:25630 PKM2 pyruvate kinase M1/2 pyruvate kinase PKM NCBI-Human-GeneID:5315 http://www.ncbi.nlm.nih.gov/gene/5315 NCBI-Mouse-GeneID:18746 http://www.ncbi.nlm.nih.gov/gene/18746 NCBI-Rat-GeneID:25630 http://www.ncbi.nlm.nih.gov/gene/25630 PR:000012870 A protein that is a translation product of the human PLK1 gene or a 1:1 ortholog thereof. PLK-1 Polo-like kinase 1 serine/threonine-protein kinase PLK1 PLK1 PR:000013514 A protein that is a translation product of the human PYCARD gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:29108 ASC CARD5 Caspase Recruitment Domain-Containing Protein 5 PYCARD PYD and CARD domain-containing protein apoptosis-associated speck-like protein containing a CARD NCBI-Human-GeneID:29108 https://www.ncbi.nlm.nih.gov/gene/29108 PR:000013773 A protein that is a translation product of the human RB1 gene or a 1:1 ortholog thereof. Rb p105-Rb p110-RB1 pRb pp105 pp110 retinoblastoma-associated protein RB1 PR:000013875 A protein that is a translation product of the human RELA gene or a 1:1 ortholog thereof. nuclear factor NF-kappa-B p65 subunit p65 transcription factor p65 RELA PR:000014243 A protein that is a translation product of the human RPP21 gene or a 1:1 ortholog thereof. ribonuclease P protein subunit p21 RPP21 PR:000014282 A ribosomal protein S6 kinase alpha that is a translation product of the human RPS6KA1 gene or a 1:1 ortholog thereof. 90 kDa ribosomal protein S6 kinase 1 MAP kinase-activated protein kinase 1a MAPK-activated protein kinase 1a MAPKAP kinase 1a p90-RSK 1 ribosomal protein S6 kinase alpha-1 RPS6KA1 PR:000014286 A ribosomal protein S6 kinase alpha that is a translation product of the human RPS6KA5 gene or a 1:1 ortholog thereof. nuclear mitogen- and stress-activated protein kinase 1 ribosomal protein S6 kinase alpha-5 MSK1 RPS6KA5 PR:000014702 A serpin that is a translation product of the human SERPINE1 gene or a 1:1 ortholog thereof. UniProtKB:P05121 PAI PAI-1 endothelial plasminogen activator inhibitor plasminogen activator inhibitor 1 serpin E1 SERPINE1 PR:000014888 A protein that is a translation product of the human SIRT1 gene or a 1:1 ortholog thereof. NAD-dependent protein deacetylase sirtuin-1 SIR2-like protein 1 hSIR2 regulatory protein SIR2 homolog 1 SIRT1 PR:000015058 A protein that is a translation product of the human SLC2A1 gene or a 1:1 ortholog thereof. SLC2A1 NCBI-Human-GeneID:6513 NCBI-Mouse-GeneID:20525 NCBI-Rat-GeneID:24778 GLUT1 solute carrier family 2 member 1 solute carrier family 2, facilitated glucose transporter member 1 HOIP_0040115 NCBI-Human-GeneID:6513 http://www.ncbi.nlm.nih.gov/gene/6513 NCBI-Mouse-GeneID:20525 http://www.ncbi.nlm.nih.gov/gene/20525 NCBI-Rat-GeneID:24778 http://www.ncbi.nlm.nih.gov/gene/24778 PR:000015066 A protein that is a translation product of the human SLC2A4 gene or a 1:1 ortholog thereof. GLUT-4 GLUT4 glucose transporter type 4, insulin-responsive solute carrier family 2, facilitated glucose transporter member 4 SLC2A4 PR:000015322 A protein that is a translation product of the human SNCA gene or a 1:1 ortholog thereof. NACP alpha-synuclein non-A beta component of AD amyloid non-A4 component of amyloid precursor SNCA PR:000016014 A protein that is a translation product of the human TAF1 gene or a 1:1 ortholog thereof. TAF1 BA2R CCG1 CCGS transcription initiation factor TFIID subunit 1 PR:000016131 An IKK-related kinase that is a translation product of the human TBK1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:29110 NF-kappa-B-activating kinase TANK-binding kinase 1 TANK-binding kinase 1-binding protein 1 TBK1 serine/threonine-protein kinase TBK1 NCBI-Human-GeneID:29110 http://www.ncbi.nlm.nih.gov/gene/29110 PR:000016238 A protein that is a translation product of the human TERT gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7015 NCBI-Mouse-GeneID:21752 NCBI-Rat-GeneID:301965 EST2 TCS1 TRT telomerase catalytic subunit telomerase reverse transcriptase telomerase-associated protein 2 TERT NCBI-Human-GeneID:7015 http://www.ncbi.nlm.nih.gov/gene/7015 NCBI-Mouse-GeneID:21752 http://www.ncbi.nlm.nih.gov/gene/21752 NCBI-Rat-GeneID:301965 http://www.ncbi.nlm.nih.gov/gene/301965 PR:000016456 A protein that is a translation product of the human TMPRSS2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7113 NCBI-Mouse-GeneID:50528 NCBI-Rat-GeneID:156435 TMPRSS2 epitheliasin plasmic transmembrane protein X serine protease 10 transmembrane protease serine 2 NCBI-Human-GeneID:7113 https://www.ncbi.nlm.nih.gov/gene/7113 NCBI-Mouse-GeneID:50528 https://www.ncbi.nlm.nih.gov/gene/50528 NCBI-Rat-GeneID:156435 https://www.ncbi.nlm.nih.gov/gene/156435 PR:000016458 A protein that is a translation product of the human TMPRSS4 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:56649 NCBI-Mouse-GeneID:214523 NCBI-Rat-GeneID:367074 TMPRSS4 membrane-bound channel-activating protease 2 membrane-type serine protease 2 transmembrane protease serine 4 NCBI-Human-GeneID:56649 https://www.ncbi.nlm.nih.gov/gene/56649 NCBI-Mouse-GeneID:214523 https://www.ncbi.nlm.nih.gov/gene/214523 NCBI-Rat-GeneID:367074 https://www.ncbi.nlm.nih.gov/gene/367074 PR:000016558 A protein that is a translation product of the human TP53BP1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7158 53BP1 TP53-binding protein 1 p53-binding protein 1 p53BP1 tumor suppressor p53-binding protein 1 Trp53bp1 TP53BP1 NCBI-Human-GeneID:7158 http://www.ncbi.nlm.nih.gov/gene/7158 PR:000017137 A protein that is a translation product of the human USF1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7391 NCBI-Mouse-GeneID:22278 NCBI-Rat-GeneID:83586 upstream transcription factor 1 USF1 (mol) NCBI-Human-GeneID:7391 http://www.ncbi.nlm.nih.gov/gene/7391 NCBI-Mouse-GeneID:22278 http://www.ncbi.nlm.nih.gov/gene/22278 NCBI-Rat-GeneID:83586 http://www.ncbi.nlm.nih.gov/gene/83586 PR:000017138 A protein that is a translation product of the human USF2 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7392 NCBI-Mouse-GeneID:22282 NCBI-Rat-GeneID:81817 USF2 (mol) NCBI-Human-GeneID:7392 http://www.ncbi.nlm.nih.gov/gene/7392 NCBI-Mouse-GeneID:22282 http://www.ncbi.nlm.nih.gov/gene/22282 NCBI-Rat-GeneID:81817 http://www.ncbi.nlm.nih.gov/gene/81817 PR:000017272 Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane. Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane. vinculin Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane. UniProt:P18206 PR:000017284 A protein that is a translation product of the human VEGFA gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7422 NCBI-Mouse-GeneID:22339 NCBI-Rat-GeneID:83785 Uniprot:P15692 vascular endothelial growth factor vascular endothelial growth factor A VEGFA NCBI-Human-GeneID:7422 https://www.ncbi.nlm.nih.gov/gene/7422 NCBI-Mouse-GeneID:22339 https://www.ncbi.nlm.nih.gov/gene/22339 NCBI-Rat-GeneID:83785 https://www.ncbi.nlm.nih.gov/gene/83785 PR:000023089 DNA ligase A protein that is a translation product of the Escherichia coli K-12 ligA gene or a 1:1 ortholog thereof. Definition defined by OBI developers: an enzyme that covalently joins two compatible pieces of DNA through the cleavage of an ATP molecule ligase DNA ligase PR:000024938 A protein that consists solely of an Interferon alpha domain and which binds to a specific cell surface receptor complex known as the IFN-alpha receptor (IFNAR), a heterodimer of IFNAR1 and IFNAR2 chains Interferon alpha interferon alpha PR:000024939 IFNB Category=family. interferon beta PR:000024990 A protein that binds to a specific cell surface receptor complex known as the IFN-gamma receptor (IFNGR), a complex of two IFNGR1 and two IFNGR2 chains. IFN type II Note: Some references consider 'gamma' and 'type II' to be synonyms. This is likely because gamma is the only type II interferon identified. However, the classification criteria for each nomenclature system differ. type II Interferon PR:000025304 A protein with core architecture containing a single Interferon regulatory factor transcription factor domain (Pfam:PF00605) in the amino-terminal region. interferon regulatory factor IRF family PR:000025748 A protein with core domain composition consisting of an N-termianl FERM domain, followed by a copy of the SH2 domain (Pfam:PF00017), and two copies of the Protein tyrosine kinase (Pfam:PF07714) domain. Janus kinase is a non-receptor tyrosine kinase. A protein with core domain composition consisting of an N-termianl FERM domain, followed by a copy of the SH2 domain (Pfam:PF00017), and two copies of the Protein tyrosine kinase (Pfam:PF07714) domain. Janus kinase is a non-receptor tyrosine kinase. Janus kinase JAK A protein with core domain composition consisting of an N-termianl FERM domain, followed by a copy of the SH2 domain (Pfam:PF00017), and two copies of the Protein tyrosine kinase (Pfam:PF07714) domain. Janus kinase is a non-receptor tyrosine kinase. PMID:15575979 PR:000025848 A protein that consists solely of an Interferon alpha/beta domain (Pfam:PF00143) and which binds to a specific cell surface receptor complex known as the IFN-alpha receptor (IFNAR), a heterodimer of IFNAR1 and IFNAR2 chains type I Interferon type I interferon PR:000025875 A protein that is primarily known as an irreversible serine protease inhibitor active against S1, S8 and C14 peptidases. There are both extra- and intra-cellular serpins, which are found in all groups of organisms with the notable exception of fungi. Serpin contains a copy of the Serpin (Pfam:PF00079) domain. InterPro:IPR000215 PANTHER:PTHR11461 serpin PR:000026439 A phosphoinositide 3-kinase complex whose components are encoded in the genome of human. PI3K class III (human) phosphoinositide 3-kinase complex (human) PR:000026741 A cyclin D1:Cdk4 whose components are encoded in the genome of human. cyclin D1:Cdk4 (human) PR:000026745 A cyclin-dependent protein kinase holoenzyme complex that has a cyclin E1 regulatory subunit and a Cdk2 kinase subunit. A protein complex consisting of cyclin E1 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. A protein complex consisting of cyclin E1 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. http://purl.obolibrary.org/obo/GO_0097134 cyclin E1:Cdk2 complex A protein complex consisting of cyclin E1 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner. PMID:15935619 PR:000026768 A cyclin E1:Cdk2 complex whose components are encoded in the genome of human. cyclin E1:Cdk2 complex (human) PR:000027547 A core histone that is a translation product of one of the H2A gene variants. It is a core histone and contains a copy of the Histone (Pfam:PF00125) domain. histone H2A PR:000027594 A core histone that is a translation product of one of the H3 gene variants. It is a core histone and contains a copy of the Histone (Pfam:PF00125) domain at its C-terminus. A core histone that is a translation product of one of the H3 gene variants. It is a core histone and contains a copy of the Histone (Pfam:PF00125) domain at its C-terminus. histone H3 H3(any) A core histone that is a translation product of one of the H3 gene variants. It is a core histone and contains a copy of the Histone (Pfam:PF00125) domain at its C-terminus. PMID:18443735 PMID:19234519 PR:000028746 A protein that is a translation product of the human PTEN gene or a 1:1 ortholog thereof. HGNC:9588 NCBI Gene:5728 PMID:21241890 UniProtKB:P60484 mutated in multiple advanced cancers 1 phosphatase and tensin homolog phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN MMAC1 PTEN TEP PTEN PMID:21241890 We show that nuclear PTEN interacts with APC/C, promotes APC/C association with CDH1, and thereby enhances the tumor-suppressive activity of the APC-CDH1 complex. This nuclear function of PTEN provides a straightforward mechanistic explanation for the fail-safe cellular senescence response elicited by acute PTEN loss and the tumor-suppressive activity of catalytically inactive PTEN. Remarkably, nuclear but not cytoplasmic PTEN immunoprecipitates were capable of ubiquitinating Cyclin B PR:000029097 p16-INK4 A protein that is a translation product of the human CDKN2A gene or a 1:1 ortholog thereof. HGNC:1787 NCBI-Human-GeneID:1029 CDK4I CDKN2A gene translation product INK4a MTS-1 cyclin-dependent kinase inhibitor 2A multiple tumor suppressor 1 p16 p16-INK4 p16INK4a ARF Tumor Suppressor ARF cyclin-dependent kinase inhibitor 2A (melanoma, p16, inhibits CDK4) p14ARF CDKN2A NCBI-Human-GeneID:1029 PR:000029189 A protein that has a core domain composition consisting of a PH domain (Pfam:PF00169), Protein kinase domain (Pfam:PF00069) and a Protein kinase C terminal domain (Pfam:PF00433). Mammals have three genes encoding AKT1, AKT2 and AKT3. The second messenger phosphatidylinositol-3,4,5-trisphosphate [PIP(3)], product of phosphatidylinositol 3-kinase, acts largely through its role as a kinase activator. Binding of the pleckstrin domain to PIP(3) results in its targeting to the plasma membrane. Full activity is gained only after phosphorylation at two sites. A protein that has a core domain composition consisting of a PH domain (Pfam:PF00169), Protein kinase domain (Pfam:PF00069) and a Protein kinase C terminal domain (Pfam:PF00433). Mammals have three genes encoding AKT1, AKT2 and AKT3. The second messenger phosphatidylinositol-3,4,5-trisphosphate [PIP(3)], product of phosphatidylinositol 3-kinase, acts largely through its role as a kinase activator. Binding of the pleckstrin domain to PIP(3) results in its targeting to the plasma membrane. Full activity is gained only after phosphorylation at two sites. PKB AKT serine-threonine kinase Akt AKT kinase A protein that has a core domain composition consisting of a PH domain (Pfam:PF00169), Protein kinase domain (Pfam:PF00069) and a Protein kinase C terminal domain (Pfam:PF00433). Mammals have three genes encoding AKT1, AKT2 and AKT3. The second messenger phosphatidylinositol-3,4,5-trisphosphate [PIP(3)], product of phosphatidylinositol 3-kinase, acts largely through its role as a kinase activator. Binding of the pleckstrin domain to PIP(3) results in its targeting to the plasma membrane. Full activity is gained only after phosphorylation at two sites. PMID:9736715 PR:000029191 A protein that consists of a copy of the Cyclin, N-terminal domain (Pfam:PF00134). This class includes the G1/S cyclins, essential for the control of the cell cycle at the G1/S transition, and the G2/M cyclins, essential for the control of the cell cycle at the G2/M transition. cyclin-related protein cyclin PR:000029192 A cyclin-related protein that is a translation product of the human CCNB1, CCNB2, or CCNB3 genes, or 1:1 orthologs thereof. G2/mitotic-specific cyclin-B cyclin B CCNB PR:000029394 A protein that is a translation product of the human DDX58 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:23586 DDX58 DEAD box protein 58 RIG-I RIG1 RLR-1 antiviral innate immune response receptor RIG-I antiviral innate immune response receptor RIG-I NCBI-Human-GeneID:23586 http://www.ncbi.nlm.nih.gov/gene/23586 PR:000029971 A protein that contains a single ATP:guanido phosphotransferase N-terminal domain (Pfam:PF02807) followed by a single ATP:guanido phosphotransferase C-terminal catalytic domain (Pfam:PF00217). creatine kinase PR:000030011 p16-INK4 (human) A CDKN2A gene translation product that is encoded in the genome of human. HGNC:1787 NCBI-Human-GeneID:1029 UniiProt:P42771. K7PML8 CDKN2A gene translation product (human) INK4a cyclin-dependent kinase inhibitor 2A (human) p16 p16INK4a ARF (human) P14ARF (human) Tumor Suppressor ARF (human) cyclin-dependent kinase inhibitor 2A (melanoma, p16, inhibits CDK4) hCDKN2A NCBI-Human-GeneID:1029 PR:000030833 A protein that is a translation product of the human CGAS gene or a 1:1 ortholog thereof. 2'3'-cGAMP synthase Mab-21 domain-containing protein 1 cGAMP synthase cyclic GMP-AMP synthase C6orf150 CGAS PR:000035365 A protein that is a serine-threonine protein kinase that controls several aspects of cell division. It contains a copy of the Protein kinase domain aurora kinase PR:000036008 An angiotensinogen proteolytic cleavage product that is formed via the action of renin on angiotensinogen, signal peptide removed form. Hypertensin angiotensin angiotensin I PR:000036009 An angiotensinogen proteolytic cleavage product that is formed via the action of angiotensin converting enzyme on angiotensin I. ang II angiotensin 1-8 angiotensin 2 angiotensin II PR:000036010 An angiotensinogen proteolytic cleavage product that is formed via the action of aminopeptidase A on angiotensin II. angiotensin III PR:000036013 An angiotensinogen proteolytic cleavage product that is formed via the action of angiotensin converting enzyme 2 on angiotensin II. ang 1-7 angiotensin 1-7 PR:000036197 A protein that is encoded in the genome of some virus. virus protein viral protein PR:000043452 A protein that contains a single copy of the Histone (Pfam:PF00125) domain, optionally followed by a C-terminus of histone H2A (Pfam:PF16211) domain (for histone H2A) with or without a Macro domain (Pfam:PF01661). coreHistone PR:000044430 A cyclin-related protein that is a translation product of the human CCNE1 or CCNE2 genes, 1:1 orthologs thereof, or a semi-ortholog thereof. cyclin-E CCNE PR:000044507 A 14-3-3 protein that is encoded in the genome of human. 14-3-3 protein (human) PR:000044524 An interleukin-12 complex that is a heterodimer of human IL-12p35 (alpha) and IL-12p40 (beta) subunits. interleukin-12 complex (human) PR:000044694 An interferon alpha that is encoded in the genome of human. IFN alpha (human) hIFNA interferon alpha (human) PR:000045218 A histone H3.1 (human) that has had the initiator methionine removed and that has been trimethylated at the position equivalent to Lys-10 of the amino acid sequence represented by UniProtKB:P68431. UniProtKB:P68431, 2-136, Lys-10, MOD:00083. H3.1:H3K9me3 histone H3.1, initiator methionine removed trimethylated 5 (human) hH3.1/InitMet-/Me3:5 PR:000045309 A histone H3.3 (human) that has had the initiator methionine removed and that has been trimethylated at the position equivalent to Lys-10 of the amino acid sequence represented by UniProtKB:P84243. UniProtKB:P84243, 2-136, Lys-10, MOD:00083. H3.3:H3K9me3 histone H3.3, initiator methionine removed trimethylated 5 (human) hH3.3/InitMet-/Me3:5 PR:000045358 Insulin superfamily genes are ubiquitous in vertebrates, and have been identified in invertebrates, including insects, molluscs, and the nematode Caenorhabditis elegans. Seven members of the insulin superfamily have been identified in humans, including insulin, insulin-like growth factors (IGFs) I and II, relaxins HI and HII, early placenta insulin-like peptide (EPIL), and relaxin-like factor. Insulin superfamily genes are ubiquitous in vertebrates, and have been identified in invertebrates, including insects, molluscs, and the nematode Caenorhabditis elegans. Seven members of the insulin superfamily have been identified in humans, including insulin, insulin-like growth factors (IGFs) I and II, relaxins HI and HII, early placenta insulin-like peptide (EPIL), and relaxin-like factor. insulin family protein Insulin superfamily genes are ubiquitous in vertebrates, and have been identified in invertebrates, including insects, molluscs, and the nematode Caenorhabditis elegans. Seven members of the insulin superfamily have been identified in humans, including insulin, insulin-like growth factors (IGFs) I and II, relaxins HI and HII, early placenta insulin-like peptide (EPIL), and relaxin-like factor. PMID:11274053 PR:000050097 A creatine kinase that is encoded in the genome of human. creatine kinase (human) PR:000050262 A protein that is encoded in the genome of severe acute respiratory syndrome coronavirus 2. 2019-nCoV protein SARS-CoV-2 protein SARS2 protein severe acute respiratory syndrome coronavirus 2 protein PR:000050263 A protein that is a translation product of the rep gene in SARS-CoV-2. rep (SARS2) GU280_gp01 ORF1a-1b ORF1ab rep Category=organism-gene. Note: The rep gene produces two translation products, one with (ORF1ab) and one without (ORF1a) -1 ribosomal frameshifting. Both products are further processed by proteolytic cleavage to yield 10 identical chains, while 1 additional chain is unique to ORF1a and 5 additional chains are unique to ORF1ab. rep gene translation product (SARS-CoV-2) PR:000050266 PRO_0000449646 S/SigPep- (SARS2) UniProtKB:P0DTC2, 13-1273 spike glycoprotein, signal peptide removed form (SARS-CoV-2) PR:000050267 A spike glycoprotein, signal peptide removed form (SARS-CoV-2) that has been processed by proteolytic cleavage to yield the N-terminal portion. UniProtKB:P0DTC2, 13-685. PMID:32142651 S1 (SARS-CoV-2) spike protein S1 (SARS-CoV-2) PR:000050268 A spike glycoprotein, signal peptide removed form (SARS-CoV-2) that has been processed by proteolytic cleavage to yield the C-terminal portion. UniProtKB:P0DTC2, 686-1273. PRO_0000449648 UniProtKB:P0DTC2, 686-1273 S2 (SARS-CoV-2) S2 (SARS-CoV-2) [COVID-19] S2 (SARS2) spike protein S2 (SARS-CoV-2) PR:000050269 A spike protein S2 (SARS-CoV-2) that has been further processed by proteolytic cleavage to yield the C-terminal portion. UniProtKB:P0DTC2, 816-1273. PMID:32142651 PRO_0000449649 UniProtKB:P0DTC2, 816-1273 S2' (SARS2) spike protein S2\' (SARS-CoV-2) PR:000050270 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of PL-PRO proteinase (nsp3) when it cleaves the precursor between residues 180-181. GenPept:YP_009725297 PRO_0000449619 PRO_0000449635 UniProtKB:P0DTC1, 1-180 UniProtKB:P0DTD1, 1-180 leader protein (SARS2) non-structural protein 1 (SARS2) nsp1 (SARS2) rep/Clv:nsp1 (SARS2) Category=organism-modification. Note: 180 aa protein. Proteinase inferred from PMID:15564471. host translation inhibitor nsp1 (SARS-CoV-2) PR:000050271 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of PL-PRO proteinase (nsp3) when it cleaves the precursor between residues 180-181 and 818-819. GenPept:YP_009725298 PRO_0000449620 PRO_0000449636 UniProtKB:P0DTC1, 181-818 UniProtKB:P0DTD1, 181-818 nsp2 (SARS2) p65 homolog (SARS2) rep/Clv:nsp2 (SARS2) Category=organism-modification. Note: 638 aa protein. non-structural protein 2 (SARS-CoV-2) PR:000050272 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the autocatalytic action of PL-PRO proteinase (nsp3) when it cleaves the precursor between residues 818-819 and 2763-2764. GenPept:YP_009725299 PL-PRO (SARS-CoV2) PLpro (SARS2) PRO_0000449621 PRO_0000449637 UniProtKB:P0DTC1, 819-2763 main proteinase (SARS2) non-structural protein 3 (SARS-CoV2) nsp3 (SARS2) papain-like proteinase (SARS2) rep/Clv:nsp3 (SARS2) PL2-PRO (SARS2) Category=organism-modification. Note: 1945 aa protein. Unlike some other coronaviruses, SARS coronaviruses only encode a single papain-like proteinase, PLpro. [PMID:15564471] non-structural protein 3 (SARS-CoV-2) PR:000050273 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the combined actions of PL-PRO proteinase (nsp3) when it cleaves the precursor between residues 2763-2764, and 3CL-PRO (nsp5) when it cleaves the precursor between residues 3263-3264. GenPept:YP_009725300 PRO_0000449622 PRO_0000449638 UniProtKB:P0DTC1, 2764-3263 UniProtKB:P0DTD1, 2764-3263 nsp4 (SARS2) rep/Clv:nsp4 (SARS2) Category=organism-modification. Note: 500 aa protein. non-structural protein 4 (SARS-CoV-2) PR:000050274 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the autocatalytic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 3263-3264 and 3569-3570. GenPept:YP_009725301 3CL-PRO (SARS2) 3CLp (SARS2) 3CLpro (SARS2) PRO_0000449623 PRO_0000449639 UniProtKB:P0DTC1, 3264-3569 UniProtKB:P0DTD1, 3264-3569 nsp5 (SARS2) picornavirus 3C-like protease (SARS2) rep/Clv:nsp5 (SARS2) Category=organism-modification. Note: 306 aa protein. 3C-like proteinase (SARS-CoV-2) PR:000050275 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 3569-3570 and 3859-3860. GenPept:YP_009725302 PRO_0000449624 PRO_0000449640 UniProtKB:P0DTC1, 3570-3859 UniProtKB:P0DTD1, 3570-3859 nsp6 (SARS2) rep/Clv:nsp6 (SARS2) Category=organism-modification. Note: 290 aa protein. non-structural protein 6 (SARS-CoV-2) PR:000050276 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 3859-3860 and 3942-3943. GenPept:YP_009725303 PRO_0000449625 PRO_0000449641 UniProtKB:P0DTC1, 3860-3942 UniProtKB:P0DTD1, 3860-3942 nsp7 (SARS2) rep/Clv:nsp7 (SARS2) Category=organism-modification. Note: 83 aa protein. non-structural protein 7 (SARS-CoV-2) PR:000050277 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 3942-3943 and 4140-4141. GenPept:YP_009725304 PRO_0000449626 PRO_0000449642 UniProtKB:P0DTC1, 3943-4140 UniProtKB:P0DTD1, 3943-4140 nsp8 (SARS2) rep/Clv:nsp8 (SARS2) Category=organism-modification. Note: 198 aa protein. non-structural protein 8 (SARS-CoV-2) PR:000050278 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 4140-4141 and 4253-4254. GenPept:YP_009725305 PRO_0000449627 PRO_0000449643 UniProtKB:P0DTC1, 4141-4253 UniProtKB:P0DTD1, 4141-4253 nsp9 (SARS2) rep/Clv:nsp9 (SARS2) Category=organism-modification. Note: 113 aa protein. non-structural protein 9 (SARS-CoV-2) PR:000050279 A rep gene proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 4253-4254 and 4392-4393. GenPept:YP_009725306 GFL (SARS2) PRO_0000449628 PRO_0000449644 UniProtKB:P0DTC1, 4254-4392 UniProtKB:P0DTD1, 4254-4392 growth factor-like peptide (SARS2) nsp10 (SARS2) rep/Clv:nsp10 (SARS2) Category=organism-modification. Note: 139 aa protein. non-structural protein 10 (SARS-CoV-2) PR:000050280 An ORF1a proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 4392-4393 and 4405-4406. UniProtKB:P0DTC1, 4393-4405. GenPept:YP_009725312 PRO_0000449645 UniProtKB:P0DTC1, 4393-4405 nsp11 (SARS2) rep/Clv:nsp11 (SARS2) Category=organism-modification. Note: 13 aa protein. non-structural protein 11 (SARS-CoV-2) PR:000050281 A rep gene translation product (SARS-CoV-2) that has been processed by proteolytic cleavage. rep/ClvPrd (SARS2) Category=organism-modification. rep gene proteolytic cleavage product (SARS-CoV-2) PR:000050282 A replicase polyprotein 1a (SARS-CoV-2) that has been processed by proteolytic cleavage. ORF1a/ClvPrd (SARS2) Category=organism-modification. ORF1a proteolytic cleavage product (SARS-CoV-2) PR:000050283 A replicase polyprotein 1ab (SARS-CoV-2) that has been processed by proteolytic cleavage. ORF1ab/ClvPrd (SARS2) Category=organism-modification. ORF1ab proteolytic cleavage product (SARS-CoV-2) PR:000050284 An ORF1ab proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 4392-4393 and 5324-5325. GenPept:YP_009725307 ORF1ab/Clv:nsp12 (SARS2) PRO_0000449629 Pol (SARS2) RdRp (SARS2) UniProtKB:P0DTD1, 4393-5324 nsp12 (SARS2) Category=organism-modification. Note: 932 aa protein. RNA-directed RNA polymerase (SARS-CoV-2) PR:000050285 An ORF1ab proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 5324-5325 and 5925-5926. GenPept:YP_009725308 Hel (SARS2) ORF1ab/Clv:nsp13 (SARS2) PRO_0000449630 UniProtKB:P0DTD1, 5325-5925 nsp13 (SARS2) Category=organism-modification. Note: 601 aa protein. helicase (SARS-CoV-2) PR:000050286 An ORF1ab proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 5925-5926 and 6452-6453. GenPept:YP_009725309 ExoN (SARS2) ORF1ab/Clv:nsp14 (SARS2) PRO_0000449631 UniProtKB:P0DTD1, 5926-6452 nsp14 (SARS2) 3'-to-5' exonuclease (SARS2) guanine-N7 methyltransferase (SARS2) Category=organism-modification. Note: 527 aa protein. bifunctional exonuclease/methyltransferase (SARS-CoV-2) PR:000050287 An ORF1ab proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 6452-6453 and 6798-6799. GenPept:YP_009725310 NendoU (SARS2) ORF1ab/Clv:nsp15 (SARS2) PRO_0000449632 UniProtKB:P0DTD1, 6453-6798 endoRNAse (SARS2) nsp15 (SARS2) Category=organism-modification. Note: 346 aa protein. uridylate-specific endoribonuclease (SARS-CoV-2) PR:000050288 An ORF1ab proteolytic cleavage product (SARS-CoV-2) that is the portion produced by the enzymatic action of 3CL-PRO proteinase (nsp5) when it cleaves the precursor between residues 6798-6799. GenPept:YP_009725311 2'-O-ribose methyltransferase (SARS2) ORF1ab/Clv:nsp16 (SARS2) PRO_0000449633 UniProtKB:P0DTD1, 6799-7096 nsp16 (SARS2) Category=organism-modification. Note: 298 aa protein. 2'-O-methyltransferase (SARS-CoV-2) PR:000050342 A ferritin complex that is composed of varying ratios of ferritin heavy chain (human) and ferritin light chain (human) for a total of twenty-four subunits. PMID:32412710 ferritin complex (human) PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. These organ failures may be associated with clinical and laboratory signs of inflammation, including high fevers, thrombocytopenia, hyperferritinemia, and elevations in C-reactive protein and interleukin-6. PR:000050385 A histone H3 that is encoded in the genome of human. histone H3 (human) There are seven histone H3 variants in human. hH3(any) PR:000060080 A protein that is a translation product of the human STEEP1 gene or a 1:1 ortholog thereof. STEEP STING ER exit protein CXorf56 STEEP1 PR:A0A663DJA2 A protein that is a translation product of the ORF10 gene in SARS-CoV-2. GenPept:YP_009725255 UniProtKB:A0A663DJA2 ORF10 (SARS2) GU280_gp11 ORF10 Category=organism-gene. Note: 38 aa protein. ORF10 protein (SARS-CoV-2) PR:O00187 A mannan-binding lectin serine protease 2 that is encoded in the genome of human. NCBI-Human-GeneID:10747 UniProtKB:O00187 MASP-2 (human) hMASP2 mannose-binding protein-associated serine protease 2 (human) mannan-binding lectin serine protease 2 (human) NCBI-Human-GeneID:10747 http://www.ncbi.nlm.nih.gov/gene/10747 PR:O00206 A Toll-like receptor 4 that is encoded in the genome of human. UniProtKB:O00206 CD283 (human) hTLR4 Toll-like receptor 4 (human) PR:O02108 An Hsp90 co-chaperone Cdc37 that is encoded in the genome of worm. Is predicted to enable chaperone binding activity; heat shock protein binding activity; and unfolded protein binding activity. Located in condensed chromosome; cytoplasm; and mitotic spindle. Is expressed in anchor cell. Is an ortholog of human CDC37 (cell division cycle 37, HSP90 cochaperone). Is predicted to enable chaperone binding activity; heat shock protein binding activity; and unfolded protein binding activity. Located in condensed chromosome; cytoplasm; and mitotic spindle. Is expressed in anchor cell. Is an ortholog of human CDC37 (cell division cycle 37, HSP90 cochaperone). UniProtKB:O02108 http://www.wormbase.org/species/c_elegans/gene/WBGene00021097 Hsp90 chaperone protein kinase-targeting subunit (worm) cell division cycle-related protein 37 (worm) probable Hsp90 co-chaperone cdc37 (worm) W08F4.8 cdc-37 CDC37 (worm) Is predicted to enable chaperone binding activity; heat shock protein binding activity; and unfolded protein binding activity. Located in condensed chromosome; cytoplasm; and mitotic spindle. Is expressed in anchor cell. Is an ortholog of human CDC37 (cell division cycle 37, HSP90 cochaperone). http://www.wormbase.org/species/c_elegans/gene/WBGene00021097 PR:O14746 A telomerase reverse transcriptase that is encoded in the genome of human. NCBI-Human-GeneID:7015 EST2 (human) TCS1 (human) TRT (human) telomerase catalytic subunit (human) telomerase reverse transcriptase (human) telomerase-associated protein 2 (human) hTERT NCBI-Human-GeneID:7015 http://www.ncbi.nlm.nih.gov/gene/7015 PR:O14757 A serine/threonine-protein kinase Chk1 that is encoded in the genome of human. DTO:03100082 HGNC:1925 NCBI-Human-GeneID:1111 UniProtKB:O14757 CHK1 checkpoint homolog (human) cell cycle checkpoint kinase (human) checkpoint kinase-1 (human) serine/threonine-protein kinase Chk1 (human) CHK1 hCHEK1 NCBI-Human-GeneID:1111 http://www.ncbi.nlm.nih.gov/gene/1111 PR:O14786 A neuropilin-1 that is encoded in the genome of human. NCBI-Human-GeneID:8829 PMID:33082294 PMID:33395426 UniProtKB:O14786 CD304 (human) hNRP1 vascular endothelial cell growth factor 165 receptor (human) neuropilin-1 (human) NCBI-Human-GeneID:8829 This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contains a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. This protein has also been determined to act as a co-receptor for SARS-CoV-2 (which causes COVID-19) to infect host cells. [provided by RefSeq, Nov 2020] http://www.ncbi.nlm.nih.gov/gene/8829 PMID:33082294 The host protease furin cleaves the full-length precursor S glycoprotein into two associated polypeptides: S1 and S2. Cleavage of S generates a polybasic Arg-Arg-Ala-Arg carboxyl-terminal sequence on S1, which conforms to a C-end rule (CendR) motif that binds to cell surface neuropilin-1 (NRP1) and NRP2 receptors. PMID:33395426 Neuropilin-1 (NRP-1), a member of a family of signaling proteins, was shown to serve as an entry factor and potentiate SARS Coronavirus 2 (SARS-CoV-2) infectivity in vitro. NRP-1 has 2 isoforms: a truncated, secreted form, and a transmembrane form which interacts with SARS-CoV-2. PR:O14791 An apolipoprotein L1 that is encoded in the genome of human. NCBI-Human-GeneID:8542 UniProtKB:O14791 ApoL-I (human) apo-L (human) apolipoprotein L (human) apolipoprotein L-I (human) hAPOL1 apolipoprotein L1 (human) NCBI-Human-GeneID:8542 http://www.ncbi.nlm.nih.gov/gene/8542 PR:O15054 A lysine-specific demethylase 6B that is encoded in the genome of human. UniProtKB:O15054 JmjC domain-containing protein 3 (human) [histone H3]-trimethyl-L-lysine(27) demethylase 6B (human) histone demethylase JMJD3 (human) lysine-specific demethylase 6B (human) JMJD3 KIAA0346 hKDM6B PR:O15123 An angiopoietin-2 that is encoded in the genome of human. NCBI-Human-GeneID:285 PMID:32629875 UniProtKB:O15123 ANG-2 (human) hANGPT2 angiopoietin-2 (human) NCBI-Human-GeneID:285 http://www.ncbi.nlm.nih.gov/gene/285 PMID:32629875 The rationale for this approach is that circulating levels of angiopoietin-2 (ANG2) are abnormally elevated in severe COVID-19 patients. PR:O15226 An NF-kappa-B-repressing factor that is encoded in the genome of human. NF-kappa-B-repressing factor (human) PR:O15393 A transmembrane protease serine 2 that is encoded in the genome of human. NCBI-Human-GeneID:7113 PMID:21068237 PMID:32142651 PMID:32327758 PMID:32404436 PMID:32413319 PMID:33077917 UniProtKB:O15393 hTMPRSS2 serine protease 10 (human) transmembrane protease serine 2 (human) NCBI-Human-GeneID:7113 https://www.ncbi.nlm.nih.gov/gene/7113 PMID:32327758 TMPRSS2 was highly expressed with a broader distribu- tion (Fig. 1a; second column), suggesting that ACE2, rather than TMPRSS2, may be a limiting factor for viral entry at the initial infection stage. Cells from the respiratory tree, cornea, esophagus, ileum, colon, gallbladder and common bile duct expressed both genes in the same cell (Fig. 1a; third column). PMID:32404436 Here, we present evidence that SARS-CoV-2 infects human mature enterocytes from the apical surface and triggers epithelial cell fusion. TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion. Both ACE2 and TMPRSS2 are expressed highly in the gastrointestinal (GI) tract, in particular by intestinal epithelial cells (IECs), the predominant target cells for many human enteric viruses. PMID:32413319 We identify ACE2 and TMPRSS2 co-expressing cells within lung type II pneumocytes, ileal absorptive enterocytes, and nasal goblet secretory cells. Here, we found that ACE2 and TMPRSS2 were primarily expressed within type II pneumocytes and ciliated cells, in line with our analysis of the NHP-derived cells (Figures 1 and 2A, 2B). These findings are aligned with concurrent work by the HCA Lung Biological Network on human nasal scRNA-seq data, which identified nasal secretory cells to be enriched for ACE2 and TMPRSS2 expression (Sungnak et al., 2020). PMID:33077917 Tubule epithelial cells and podocytes exhibit high levels of ACE2 and TMPRSS2, suggesting that they are potential SARS-CoV-2 targets. PR:O15455 A Toll-like receptor 3 that is encoded in the genome of human. NCBI-Human-GeneID:7098 UniProtKB:O15455 CD283 (human) Toll-like receptor 3 (human) hTLR3 Toll-like receptor 3 (human) NCBI-Human-GeneID:7098 http://www.ncbi.nlm.nih.gov/gene/7098 PR:O43524 A forkhead box protein O3 that is encoded in the genome of human. HGNC:3821 UniProtKB:O43524 AF6q21 protein (human) forkhead box protein O3 (human) forkhead in rhabdomyosarcoma-like 1 (human) FKHRL1 FOXO3A hFOXO3 PR:O55042 An alpha-synuclein that is encoded in the genome of mouse. MGI:1277151 OMA:O55042 NACP (mouse) alpha-synuclein (mouse) non-A beta component of AD amyloid (mouse) non-A4 component of amyloid precursor (mouse) mSNCA PR:O75367 A core histone macro-H2A.1 that is encoded in the genome of human. HGNC:4740 NCBI Gene:9555 UniProtKB:O75367 H2A.y (human) H2A/y (human) core histone macro-H2A.1 (human) histone H2A.y (human) histone macroH2A1 (human) mH2A1 (human) medulloblastoma antigen MU-MB-50.205 (human) H2AFY hMACROH2A1 PR:O75582 A ribosomal protein S6 kinase alpha-5 that is encoded in the genome of human. UniProtKB:O75582 nuclear mitogen- and stress-activated protein kinase 1 ribosomal protein S6 kinase alpha-5 MSK1 hRPS6KA5 PR:O95067 A G2/mitotic-specific cyclin-B2 that is encoded in the genome of human. HGNC:1580 NCBI-Human-GeneID:9133 UniProtKB:O95067 Cycb2 hCCNB2 NCBI-Human-GeneID:9133 http://www.ncbi.nlm.nih.gov/gene/9133 PR:O95786 An antiviral innate immune response receptor RIG-I that is encoded in the genome of human. NCBI-Human-GeneID:23586 UniProtKB:O95786 DEAD box protein 58 (human) RIG-1 (human) RIG-I (human) hDDX58 retinoic acid-inducible gene 1 protein (human) retinoic acid-inducible gene I protein (human) antiviral innate immune response receptor RIG-I (human) NCBI-Human-GeneID:23586 http://www.ncbi.nlm.nih.gov/gene/23586 PR:O96017 A serine/threonine-protein kinase Chk2 that is encoded in the genome of human. DTO:03100083 HGNC:16627 NCBI-Human-GeneID:11200 OMA:O96017 UniProtKB:O96017 CHK2 checkpoint homolog (human) Cds1 homolog (human) Hucds1 (human) checkpoint kinase 2 (human) hCds1 serine/threonine-protein kinase Chk2 (human) CDS1 CHEK2 CHK2 RAD53 hCHEK2 NCBI-Human-GeneID:11200 http://www.ncbi.nlm.nih.gov/gene/11200 PR:P00338 An L-lactate dehydrogenase A chain that is encoded in the genome of human. NCBI-Human-GeneID:3939 PMID:32697943 UniProtKB:P00338 LDH-A (human) hLDHA L-lactate dehydrogenase A chain (human) NCBI-Human-GeneID:3939 http://www.ncbi.nlm.nih.gov/gene/3939 PMID:32697943 Finally, to evaluate the importance of aerobic glycolysis for CoV-2 infection, we blocked lactate dehydrogenase A (LDH-A) activity with oxamate. This also completely abrogated viral replication and reduced ACE2 and IL-1b expression in CoV-2-infected cells (Figures 2K and S3F). PR:P00973 A 2'-5'-oligoadenylate synthase 1 that is encoded in the genome of human. Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L. Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L. NCBI-Human-GeneID:4938 PMID:32726803 UniProtKB:P00973 hOAS1 2'-5'-oligoadenylate synthase 1 (human) Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L. https://www.uniprot.org/uniprot/P00973#function NCBI-Human-GeneID:4938 http://www.ncbi.nlm.nih.gov/gene/4938 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). PR:P01116 A GTPase KRas that is encoded in the genome of human. HGNC:6407 UniProtKB:P01116 KRAS hKRAS PR:P01137 A TGF-beta 1 that is encoded in the genome of human. NCBI-Human-GeneID: UniProtKB:P01137 transforming growth factor beta-1 (human) hTGFB1 NCBI-Human-GeneID: http://www.ncbi.nlm.nih.gov/gene/7040 PR:P01308 An insulin gene translation product that is encoded in the genome of human. HGNC:6081 UniProtKB:P01308 hINS PR:P01375 A tumor necrosis factor that is encoded in the genome of human. NCBI-Human-GeneID:7124 UniProtKB:P01375 TNF-a (human) TNF-alpha (human) cachectin (human) hTNF tumor necrosis factor (human) tumor necrosis factor ligand superfamily member 2 (human) tumor necrosis factor (human) NCBI-Human-GeneID:7124 http://www.ncbi.nlm.nih.gov/gene/7124 PR:P01563 An interferon alpha-2 that is encoded in the genome of human. NCBI-Human-GeneID:3440 PMID:32413319 UniProtKB:P01563 IFN-alpha-2 (human) hIFNA2 interferon alpha-A (human) interferon alpha-2 (human) NCBI-Human-GeneID:3440 https://www.ncbi.nlm.nih.gov/gene/3440 PMID:32413319 Only IFN-a2 and IFN-g led to upregulation of ACE2 over the time period tested, and compared with all other cytokines, IFN-a2 lead to greater and more significant upregulation over all doses tested (Fig- ure S3D,Wilcoxon test: IFN-a2 FDR-adjusted p = 4.1E-07; IFN-g p = 9.3E-03,Figures S3E and S3F, all statistical tests compared with 0 ng/mL dose). PR:P01574 An interferon beta 1 that is encoded in the genome of human. NCBI-Human-GeneID:3456 IFNB1 (human) hIFNB1 interferon beta (human) NCBI-Human-GeneID:3456 https://www.ncbi.nlm.nih.gov/gene/3456 PR:P01579 An interferon gamma that is encoded in the genome of human. NCBI-Human-GeneID:3458 PMID:32413319 IFNG (human) immune interferon (human) interferon gamma (human) hIFNG HOIP_0040056 NCBI-Human-GeneID:3458 https://www.ncbi.nlm.nih.gov/gene/3458 PMID:32413319 Only IFN-a2 and IFN-g led to upregulation of ACE2 over the time period tested, and compared with all other cytokines, IFN-a2 lead to greater and more significant upregulation over all doses tested (Fig- ure S3D,Wilcoxon test: IFN-a2 FDR-adjusted p = 4.1E-07; IFN-g p = 9.3E-03,Figures S3E and S3F, all statistical tests compared with 0 ng/mL dose). PR:P01583 An interleukin-1 alpha that is encoded in the genome of human. HGNC:5991 NCBI-Human-GeneID:3552 UniProtKB:P01583 IL-1 alpha (human) IL1F1 hematopoietin-1 (human) hIL1A NCBI-Human-GeneID:3552 http://www.ncbi.nlm.nih.gov/gene/3553 PR:P01584 An interleukin-1 beta that is encoded in the genome of human. NCBI-Human-GeneID:3553 PMID:32404672 UniProtKB:P01584 IL-1 beta (human) hIL1B interleukin-1 beta (human) NCBI-Human-GeneID:3553 http://www.ncbi.nlm.nih.gov/gene/3553 PR:P01589 An interleukin-2 receptor subunit alpha that is encoded in the genome of human. UniProtKB:P01589 interleukin-2 receptor subunit alpha (human) PR:P02741 A C-reactive protein that is encoded in the genome of human. NCBI-Human-GeneID:1401 PMID:32412710 UniProtKB:P02741 https://omim.org/entry/123260 https://www.ncbi.nlm.nih.gov/gene/1401 hCRP PTX1 C-reactive protein (human) NCBI-Human-GeneID:1401 http://www.ncbi.nlm.nih.gov/gene/1401 PMID:32412710 Severe Covid-19 may also lead to acute cardiac, kidney, and liver injury, in addition to cardiac arrhythmias, rhabdomyolysis, coagulopathy, and shock. These organ failures may be associated with clinical and laboratory signs of inflammation, including high fevers, thrombocytopenia, hyperferritinemia, and elevations in C-reactive protein and interleukin-6. PR:P02778 A C-X-C motif chemokine 10 that is encoded in the genome of human. This antimicrobial gene encodes a chemokine of the CXC subfamily and ligand for the receptor CXCR3. Binding of this protein to CXCR3 results in pleiotropic effects, including stimulation of monocytes, natural killer and T-cell migration, and modulation of adhesion molecule expression. This gene may also be a key regulator of the 'cytokine storm' immune response to SARS-CoV-2 infection. This antimicrobial gene encodes a chemokine of the CXC subfamily and ligand for the receptor CXCR3. Binding of this protein to CXCR3 results in pleiotropic effects, including stimulation of monocytes, natural killer and T-cell migration, and modulation of adhesion molecule expression. This gene may also be a key regulator of the 'cytokine storm' immune response to SARS-CoV-2 infection. NCBI-Human-GeneID:3627 UniProtKB:P02778 10 kDa interferon gamma-induced protein (human) C-X-C motif chemokine 10 (human) gamma-IP10 (human) hCXCL10 This antimicrobial gene encodes a chemokine of the CXC subfamily and ligand for the receptor CXCR3. Binding of this protein to CXCR3 results in pleiotropic effects, including stimulation of monocytes, natural killer and T-cell migration, and modulation of adhesion molecule expression. This gene may also be a key regulator of the 'cytokine storm' immune response to SARS-CoV-2 infection. https://www.ncbi.nlm.nih.gov/gene/3627 NCBI-Human-GeneID:3627 http://www.ncbi.nlm.nih.gov/gene/3627 PR:P03952 A plasma kallikrein that is encoded in the genome of human. NCBI-Human-GeneID:3818 UniProtKB:P03952 fletcher factor (human) hKLKB1 kininogenin (human) plasma kallikrein (human) NCBI-Human-GeneID:3818 http://www.ncbi.nlm.nih.gov/gene/3818 PR:P04141 A granulocyte-macrophage colony-stimulating factor that is encoded in the genome of human. NCBI-Human-GeneID:1437 CSF (human) GM-CSF (human) granulocyte-macrophage colony-stimulating factor (human) HOIP_0041822 NCBI-Human-GeneID:1437 http://www.ncbi.nlm.nih.gov/gene/1437 PR:P04637 A cellular tumor antigen p53 that is encoded in the genome of human. Reactome:R-HSA-69488 UniProtKB:P04637 http://purl.obolibrary.org/obo/HGNC_11998 TP53 (human) cellular tumor antigen p53 (human) hTP53 PR:P05112 An interleukin-4 that is encoded in the genome of human. NCBI-Human-GeneID:3565 UniProtKB:P05112 B-cell stimulatory factor 1 (human) BSF-1 (human); IL-4 (human) IL-4 (human) hIL4 interleukin-4(human) NCBI-Human-GeneID:3565 http://www.ncbi.nlm.nih.gov/gene/3565 PR:P05113 An interleukin-5 that is encoded in the genome of human. NCBI-Human-GeneID:3567 UniProtKB:P05113 B-cell differentiation factor I B-cell growth factor II IL-5 (human) cytotoxic T-lymphocyte inducer eosinophil differentiation factor hIL5 interleukin-5(human) interleukin-5 (human) NCBI-Human-GeneID:3567 http://www.ncbi.nlm.nih.gov/gene/3567 PR:P05121 A plasminogen activator inhibitor 1 that is encoded in the genome of human. HGNC:8583 UniProtKB:P05121 PAI (human) PAI-1 (human) endothelial plasminogen activator inhibitor (human) plasminogen activator inhibitor 1 (human) serpin E1 (human) hSERPINE1 PR:P05161 A ubiquitin-like protein ISG15 that is encoded in the genome of human. NCBI-Human-GeneID:9636 PMID:32726803 UniProtKB:P05161 hISG15 ubiquitin-like protein ISG15 (human) NCBI-Human-GeneID:9636 http://www.ncbi.nlm.nih.gov/gene/9636 PR:P05231 An interleukin-6 that is encoded in the genome of human. NCBI-Human-GeneID:3569 PMID:32505227 UniProtKB:P05231 B-cell stimulatory factor 2 (human) BSF-2 (human) IFN-beta-2 (human) IL-6 (human) interleukin-6 (human) hIL6 NCBI-Human-GeneID:3569 http://www.ncbi.nlm.nih.gov/gene/3569 PR:P06213 An insulin receptor that is encoded in the genome of human. HGNC:6091 UniProtKB:P06213 CD220 (human) IR (human) insulin receptor (human) hINSR PR:P06400 A retinoblastoma-associated protein that is encoded in the genome of human. Ensembl:ENSG00000139687 HGNC:9884 NCBI-Human-GeneID:5925 UniProtKB:P06400 Rb (human) p105-Rb (human) p110-RB1 (human) pRb (human) pp110 (human) retinoblastoma-associated protein (human) hRB1 NCBI-Human-GeneID:5925 http://www.ncbi.nlm.nih.gov/gene/5925 PR:P06493 A cyclin-dependent kinase 1 that is encoded in the genome of human HGNC:1722 NCBI-Human-GeneID:983 UniProtKB:P06493 http://www.reactome.org/content/detail/R-HSA-68889 cell division control protein 2 homolog (human) cell division protein kinase 1 (human) cyclin-dependent kinase 1 (human) hCDK1 NCBI-Human-GeneID:983 http://www.ncbi.nlm.nih.gov/gene/983 PR:P07711 A procathepsin L that is encoded in the genome of human. NCBI-Human-GeneID:1514 PMID:32142651 PMID:32361028 UniProtKB:P07711 hCTSL procathepsin L (human) cathepsin L1 (human) NCBI-Human-GeneID:1514 https://www.ncbi.nlm.nih.gov/gene/1514 PMID:32142651 Ammonium chloride treatment strongly inhibited SARS-2-S- and SARS-S-driven entry into TMPRSS2 293T cells (Figure S3 A), suggesting CatB/L dependence. Full inhibition was attained when camostat mesylate and E-64d, an inhibitor of CatB/L, were added (Figure 4A; Figure S3B), indicating that SARS-2-S can use both CatB/L as well as TMPRSS2 for priming in these cell lines. PMID:32361028 SARS-Cov-2 entry into a cell is dependent upon binding of the viral spike (S) protein to cellular receptor and on cleavage of the spike protein by the host cell proteases such as Cathepsin L and Cathepsin B. PR:P07858 A cathepsin B that is encoded in the genome of human. NCBI-Human-GeneID:1508 PMID:32361028 UniProtKB:P07858 APP secretase (human) APPS (human) cathepsin B1 (human) hCTSB cathepsin B (human) NCBI-Human-GeneID:1508 https://www.ncbi.nlm.nih.gov/gene/1508 PMID:32361028 SARS-Cov-2 entry into a cell is dependent upon binding of the viral spike (S) protein to cellular receptor and on cleavage of the spike protein by the host cell proteases such as Cathepsin L and Cathepsin B. PR:P08700 A protein that is a translation product of the human IL4 gene or a 1:1 ortholog thereof. An interleukin-3 that is encoded in the genome of human. NCBI-Human-GeneID:3562 UniProtKB:P05112 IL-3 (human) MCGF (human) hIL3 multipotential colony-stimulating factor (human) interleukin-3 (human) NCBI-Human-GeneID:3562 http://www.ncbi.nlm.nih.gov/gene/3562 PR:P08887 A protein that is a translation product of the human IL6R gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3570 UniProtKB:P08887 CD126 (human) IL-6RA (human) IL6R (human) interleukin-6 receptor subunit alpha (human) NCBI-Human-GeneID:3570 http://www.ncbi.nlm.nih.gov/gene/3570 PR:P09341 A growth-regulated alpha protein that is encoded in the genome of human. HGNC:4602 NCBI Gene:2919 UniProtKB:P09341 C-X-C motif chemokine 1 (human) GRO-alpha(1-73) (human) NAP-3 (human) growth-regulated alpha protein (human) melanoma growth stimulatory activity (human) neutrophil-activating protein 3 (human) platelet-derived growth factor-inducible protein KC (human) secretory protein N51 (human) GRO GRO1 GROA MGSA SCYB1 hCXCL1 PR:P09382 A galectin-1 that is encoded in the genome of human. NCBI-Human-GeneID:3956 PMID:32726803 UniProtKB:P09382 galectin-1 (human) NCBI-Human-GeneID:3956 http://www.ncbi.nlm.nih.gov/gene/3956 PMID:32726803 For SCoV2-PLpro, these interactions include PRKDC (associated with induction by type I interferons24), heterogenous nuclear ribonucleo-protein K (HNRNPK; involved in host RNA splicing, a process essential for SARS-CoV-2 replication in cells25) and galectin1, which can induce viral fusion with target cells during HIV infection26 (Fig. 4a). PR:P09429 A high mobility group protein B1 that is encoded in the genome of human. HGNC:4983 NCBI Gene:3146 UniProtKB:P09429 HMG-1 (human) high mobility group protein 1 (human) high mobility group protein B1 (human) hHMGB1 PR:P09874 A poly [ADP-ribose] polymerase 1 that is encoded in the genome of human. HGNC:270 NCBI Gene:142 UniProtKB:P09874 ADP-ribosyltransferase diphtheria toxin-like 1 (human) ADPRT 1 (human) ARTD1 (human) DNA ADP-ribosyltransferase PARP1 (human) NAD(+) ADP-ribosyltransferase 1 (human) poly [ADP-ribose] polymerase 1 (human) hPARP1 PR:P09919 A granulocyte colony-stimulating factor that is encoded in the genome of human. NCBI-Human-GeneID:1440 G-CSF (human) UniProtKB:P09919 hCSF3 granulocyte colony-stimulating factor (human) NCBI-Human-GeneID:1440 http://www.ncbi.nlm.nih.gov/gene/1440 PR:P09958 A furin that is encoded in the genome of human. NCBI-Human-GeneID:5045 PMID:32362314 UniProtKB:P09958 FURIN (human) NCBI-Human-GeneID:5045 https://www.ncbi.nlm.nih.gov/gene/5045 PMID:32362314 Furin Cleaves the SARS-CoV-2 Spike Protein at the S1/ S2 Site, and Cleavage Is Required for Efficient Cell-Cell Fusion PR:P0DTC1-1 A rep gene translation product (SARS-CoV-2) that is a translation product of some mRNA giving rise to a protein with the amino acid sequence represented by UniProtKB:P0DTC1-1. GenPept:YP_009725295 UniProtKB:P0DTC1 ORF1a polyprotein (SARS2) PRO_0000449634 pp1a (SARS2) rep/iso:ORF1a (SARS2) Category=organism-sequence. Note: 4405 aa protein. Undergoes additional processing by proteolytic cleavage. replicase polyprotein 1a (SARS-CoV-2) PR:P0DTC2 A protein that is a translation product of the S gene in SARS-CoV-2. GenPept:YP_009724390 NCBI-SARS-CoV2-GeneID:43740568 PMID:32142651 PMID:33123165 UniProtKB:P0DTC2 E2 (SARS2) S (SARS2) S glycoprotein (SARS2) peplomer protein (SARS2) spike glycoprotein surface glycoprotein surface glycoprotein (SARS2) surface glycoprotein [Severe acute respiratory syndrome coronavirus 2] GU280_gp02 S spike glycoprotein (SARS-CoV-2) NCBI-SARS-CoV2-GeneID:43740568 http://www.ncbi.nlm.nih.gov/gene/43740568 PMID:33123165 The S glycoprotein (spike) exists in trimeric form and is the structure by which binding to the host cells occurs. The virus receptor, angiotensin-converting enzyme 2 (ACE2), expressed on the surface of multiple human cells is engaged via the receptor binding domain (RBD), which is part of the S1 subunit of the S glycoprotein (Figure 1). The S2 subunit consists of two heptad repeat fusion regions, HR1 and HR2, responsible for membrane fusion and cell entry. The RBD domain can either be down and buried or rotated up and primed for ACE2 binding. The hidden down state is the predominant state of the S protein trimer in SARS-CoV-2, and likely a mechanism the virus uses to hide the entry epitopes and evade the host immune response. Two S trimers can concurrently bind to an ACE2 dimer. Following S protein binding in its prefusion state, the S1 subunit is cleaved and shed permitting the S2 dramatic conformational changes which constitute the post-fusion state required for viral entry. PR:P0DTC3 A protein that is a translation product of the ORF3a gene in SARS-CoV-2. GenPept:YP_009724391 UniProtKB:P0DTC3 ORF3a (SARS2) PRO_0000449650 accessory protein 3a (SARS2) protein U274 (SARS2) protein X1 (SARS2) GU280_gp03 ORF3a Category=organism-gene. Note: 275 aa protein. protein 3a (SARS-CoV-2) PR:P0DTC4 A protein that is a translation product of the E gene in SARS-CoV-2. GenPept:YP_009724392 NCBI-SARS-CoV2-GeneID:43740570 UniProtKB:P0DTC4 E (SARS2) E (SARS2)[COVID-19] E protein (SARS2) PRO_0000449651 envelope protein (SARS2) sM protein (SARS2) E GU280_gp04 ORF4 Category=organism-gene. Note: 75 aa protein. envelope small membrane protein (SARS-CoV-2) envelope small membrane protein(SARS-CoV2) NCBI-SARS-CoV2-GeneID:43740570 http://www.ncbi.nlm.nih.gov/gene/43740570 PR:P0DTC5 A protein that is a translation product of the M gene in SARS-CoV-2. GenPept:YP_009724393 NCBI-SARS-CoV2-GeneID:43740571 UniProtKB:P0DTC5 E1 glycoprotein (SARS2) M (SARS-CoV2)[COVID-19] M (SARS2) M protein (SARS2) PRO_0000449652 matrix glycoprotein (SARS2) membrane glycoprotein (SARS2) GU280_gp05 M ORF5 Category=organism-gene. Note: 222 aa protein. membrane protein (SARS-CoV-2) NCBI-SARS-CoV2-GeneID:43740571 http://www.ncbi.nlm.nih.gov/gene/43740571 PR:P0DTC6 A protein that is a translation product of the ORF6 gene in SARS-CoV-2. GenPept:YP_009724394 UniProtKB:P0DTC6 ORF6 (SARS2) PRO_0000449653 accessory protein 6 (SARS2) ns6 (SARS2) protein X3 (SARS2) GU280_gp06 ORF6 non-structural protein 6 (SARS2) Category=organism-gene. Note: 61 aa protein. ORF6 protein (SARS-CoV-2) PR:P0DTC7 A protein that is a translation product of the ORF7a gene in SARS-CoV-2. GenPept:YP_009724395 UniProtKB:P0DTC7 ORF7a (SARS2) accessory protein 7a (SARS2) protein U122 (SARS2) protein X4 (SARS2) GU280_gp07 ORF7a Category=organism-gene. Note: 121 aa protein. protein 7a (SARS-CoV-2) PR:P0DTC8 A protein that is a translation product of the ORF8 gene in SARS-CoV-2. GenPept:YP_009724396 UniProtKB:P0DTC8 ORF8 (SARS2) ns8 (SARS2) GU280_gp09 ORF8 non-structural protein 8 (SARS2) Category=organism-gene. Note: 121 aa protein. ORF8 protein (SARS-CoV-2) PR:P0DTC9 A protein that is a translation product of the N gene in SARS-CoV-2. GenPept:YP_009724397 NCBI-SARS-CoV2-GeneID:43740575 UniProtKB:P0DTC9 N (SARS-CoV2)[COVID-19] N (SARS2) NC (SARS2) PRO_0000449656 nucleocapsid phosphoprotein(SARS-CoV2)[COVID-19] nucleocapsid protein (SARS2) protein N (SARS2) GU280_gp10 N ORF9 Category=organism-gene. Note: 419 aa protein. nucleoprotein (SARS-CoV-2) NCBI-SARS-CoV2-GeneID:43740575 http://www.ncbi.nlm.nih.gov/gene/43740575 PR:P0DTD1-1 A rep gene translation product (SARS-CoV-2) that is a translation product of some mRNA giving rise to a protein with the amino acid sequence represented by UniProtKB:P0DTD1-1. Requires ribosomal frameshifting. GenPept:YP_009724389 PMID:32726803 PR:P0DTD1 UniProtKB:P0DTD1 ORF1ab polyprotein (SARS2) PRO_0000449618 pp1ab (SARS2) rep/iso:ORF1ab (SARS2) Category=organism-sequence. Note: 7096 aa protein. Undergoes additional processing by proteolytic cleavage. replicase polyprotein 1ab (SARS-CoV-2) PMID:32726803 Here we perform biochemical, structural and functional characterization of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) PLpro (SCoV2-PLpro) and outline differences with SARS-CoV PLpro (SCoV-PLpro) in regulation of host interferon and NF-κB pathways. Furthermore, upon infection, SCoV2-PLpro contributes to the cleavage of ISG15 from interferon responsive factor 3 (IRF3) and attenuates type I interferon responses. PR:P0DTD2 A protein that is a translation product of the ORF9b gene in SARS-CoV-2. UniProtKB:P0DTD2 ORF-9b (SARS2) ORF9b (SARS2) PRO_0000449657 accessory protein 9b (SARS2) ORF9b Category=organism-gene. Note: 97 aa protein. protein 9b (SARS-CoV-2) PR:P0DTD3 A protein that is a translation product of the ORF14 gene in SARS-CoV-2. UniProtKB:P0DTD3 ORF14 (SARS2) PRO_0000449658 ORF14 Category=organism-gene. Note: 73 aa protein. uncharacterized protein 14 (SARS-CoV-2) PR:P0DTD8 A protein that is a translation product of the ORF7b gene in SARS-CoV-2. GenPept:YP_009725318 UniProtKB:P0DTD8 ORF7b (SARS2) PRO_0000449799 accessory protein 7b (SARS2) non-structural protein 7b (SARS2) ns7b (SARS2) GU280_gp08 ORF7b Category=organism-gene. Note: 43 aa protein. protein 7b (SARS-CoV-2) PR:P10144 A leukocyte granule-associated proteinase that is a translation product of the human GZMB gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3022 UniProtKB:P10144 granzyme B (human) NCBI-Human-GeneID:3022 http://www.ncbi.nlm.nih.gov/gene/3002 PR:P10145 An interleukin-8 that is encoded in the genome of human. NCBI-Human-GeneID:3576 PMID:32505227 UniProtKB:P10145 C-X-C motif chemokine 8 (human) IL-8 (human) interleukin-8 (human) monocyte-derived neutrophil chemotactic factor (human) neutrophil-activating protein 1 (human) hCXCL8 NCBI-Human-GeneID:3576 http://www.ncbi.nlm.nih.gov/gene/3576 PR:P10147 A C-C motif chemokine 3 that is encoded in the genome of human. NCBI-Human-GeneID:6348 UniProtKB:P10147 MIP-1-alpha (human) hCCL3 macrophage inflammatory protein 1-alpha (human) C-C motif chemokine 3 (human) NCBI-Human-GeneID:6348 http://www.ncbi.nlm.nih.gov/gene/6348 PR:P10415 An apoptosis regulator Bcl-2 that is encoded in the genome of human. HGNC:990 BCL2 NCBI-Human-GeneID:596 UniProtKB:P10415 apoptosis regulator Bcl-2 (human) hBCL2 NCBI-Human-GeneID:596 http://www.ncbi.nlm.nih.gov/gene/596 PR:P11166 A solute carrier family 2, facilitated glucose transporter member 1 that is encoded in the genome of human. NCBI-Human-GeneID:6513 UniProtKB:P11166 GLUT-1 (human) HepG2 glucose transporter (human) glucose transporter type 1, erythrocyte/brain (human) hSLC2A1 solute carrier family 2, facilitated glucose transporter member 1 (human) NCBI-Human-GeneID:6513 http://www.ncbi.nlm.nih.gov/gene/6513 PR:P11226 A mannose-binding protein C that is encoded in the genome of human. NCBI-Human-GeneID:4153 UniProtKB:P11226 MBP-C (human) MBP1 (human) collectin-1 (human) mannose-binding protein C (human) hMBL2 NCBI-Human-GeneID:4153 http://www.ncbi.nlm.nih.gov/gene/4153 PR:P11802 A cell division protein kinase 4 that is encoded in the genome of human. cyclin dependent kinase 4 NCBI-Human-GeneID:1019 http://www.drugtargetontology.org/dto/DTO_03100070 CRK3 (human) PSK-J3 (human) cyclin-dependent kinase 4 (human) hCDK4 NCBI-Human-GeneID:1019 http://www.ncbi.nlm.nih.gov/gene/1019 PR:P12830 A cadherin-1 that is encoded in the genome of human. HGNC:1748 NCBI-Human-GeneID:999 UniProtKB:P12830 ARC-1 (human) CAM 120/80 (human) CD324 (human) E-cadherin (human) cadherin-1 (human) epithelial cadherin (human) uvomorulin (human) hCDH1 NCBI-Human-GeneID:999 http://www.ncbi.nlm.nih.gov/gene/999 PR:P13232 An interleukin-7 that is encoded in the genome of human. NCBI-Human-GeneID:3574 IL-7 (human) hIL7 interleukin-7 (human) NCBI-Human-GeneID:3574 http://www.ncbi.nlm.nih.gov/gene/3574 PR:P13284 A gamma-interferon-inducible lysosomal thiol reductase that is encoded in the genome of human. NCBI-Human-GeneID:10437 PMID:32641482 UniProtKB:P13284 GILT hIFI30 gamma-interferon-inducible lysosomal thiol reductase (human) NCBI-Human-GeneID:10437 http://www.ncbi.nlm.nih.gov/gene/10437 PMID:32641482 As shown in Fig. 4A, we found that ADAP2, GILT, and LY6E mRNAs were expressed at significantly higher levels in HepG2 cells. PR:P13500 A C-C motif chemokine 2 that is encoded in the genome of human. NCBI-Human-GeneID:6347 UniProtKB:P13500 C-C motif chemokine 2 (human) HC11 (human) MCAF (human) MCP-1 (human) monocyte chemoattractant protein 1 (human) monocyte chemotactic and activating factor (human) hCCL2 NCBI-Human-GeneID:6347 http://www.ncbi.nlm.nih.gov/gene/6347 PR:P13726 A tissue factor that is encoded in the genome of human. NCBI-Human-GeneID:2152 UniProt:P13726 CD142 (human) coagulation factor III (human) hF3 thromboplastin (human) tissue factor (human) NCBI-Human-GeneID:2152 http://www.ncbi.nlm.nih.gov/gene/2152 PR:P14618 A pyruvate kinase PKM that is encoded in the genome of human. NCBI-Human-GeneID:5315 UniProtKB:P14618 OIP-3 (human) THBP1 (human) hPKM2 pyruvate kinase 2/3 (human) thyroid hormone-binding protein 1 (human) pyruvate kinase PKM (human) NCBI-Human-GeneID:5315 http://www.ncbi.nlm.nih.gov/gene/5315 PR:P14635 A G2/mitotic-specific cyclin-B1 that is encoded in the genome of human. HGNC:1579 NCBI-Human-GeneID:891 UniProtKB:P14635 G2/mitotic-specific cyclin-B1 (human) CCNB CCNB1 hCCNB1 NCBI-Human-GeneID:891 http://www.ncbi.nlm.nih.gov/gene/891 PR:P14672 A solute carrier family 2, facilitated glucose transporter member 4 that is encoded in the genome of human. HGNC:11009 UniProtKB:P14672 GLUT-4 (human) glucose transporter type 4, insulin-responsive (human) solute carrier family 2, facilitated glucose transporter member 4 (human) hSLC2A4 PR:P14780 A protein that is a translation product of the human MMP9 gene or a 1:1 ortholog thereof. HGNC:7176 NCBI-Human-GeneID:4318 NCBI-Mouse-GeneID:17395 NCBI-Rat-GeneID:81687 UniProtKB:P14780 92 kDa gelatinase (human) 92 kDa type IV collagenase (human) GELB (human) gelatinase B (human) matrix metalloproteinase-9 (human) hMMP9 NCBI-Human-GeneID:4318 http://www.ncbi.nlm.nih.gov/gene/4318 NCBI-Mouse-GeneID:17395 http://www.ncbi.nlm.nih.gov/gene/17395 NCBI-Rat-GeneID:81687 http://www.ncbi.nlm.nih.gov/gene/81687 PR:P14784 An interleukin-2 receptor subunit beta that is encoded in the genome of human. UniProtKB:P14784 interleukin-2 receptor subunit beta (human) PR:P14921 A protein C-ets-1 that is encoded in the genome of human. NCBI Gene:2113 HGNC:3488 UniProtKB:P14921 protein C-ets-1 (human) hETS1 PR:P15036 A protein C-ets-2 that is encoded in the genome of human. NCBI Gene:2114 HGNC:3489 Reactome:R-HSA-1629811 UniProtKB:P15036 protein C-ets-2 (human) hETS2 PR:P15056 A B-Raf proto-oncogene serine/threonine-protein kinase that is encoded in the genome of human. HGNC:1097 UniProtKB:P15056 V-Raf murine sarcoma viral oncogene homolog B1 (human) p94 (human) proto-oncogene B-Raf (human) serine/threonine-protein kinase B-raf (human) BRAF BRAF1 RAFB1 hBRAF PR:P15260 An interferon gamma receptor alpha chain that is encoded in the genome of human. CDw119 (human) IFN-gamma-R-alpha (human) hIFNGR1 interferon gamma receptor 1 (human) IFNGR1 (human) PR:P15692 A vascular endothelial growth factor A that is encoded in the genome of human. HGNC:12680 NCBI-Human-GeneID:7422 UniProtKB:P15692 VEGF-A (human) vascular endothelial growth factor A (human) hVEGFA NCBI-Human-GeneID:7422 https://www.ncbi.nlm.nih.gov/gene/7422 PR:P16104 A histone H2AX that is encoded in the genome of human. Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). HGNC:4739 NCBI-Human-GeneID:3014 UniProtKB:P16104 H2a/x (human) histone H2A.X (human) histone H2A.x (human) histone H2AX (human) H2AX hH2AFX Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). PMID:33328614 NCBI-Human-GeneID:3014 http://www.ncbi.nlm.nih.gov/gene/3014 PR:P16109 A P-selectin that is encoded in the genome of human. NCBI-Human-GeneID:6403 UniProtKB:P16109 CD62 antigen-like family member P (human) CD62P (human) GMP-140 (human) GMRP (human) LECAM3 (human) PADGEM (human) SELP (human) granule membrane protein 140 (human) leukocyte-endothelial cell adhesion molecule 3 (human) platelet activation dependent granule-external membrane protein (human) P-selectin (human) NCBI-Human-GeneID:6403 http://www.ncbi.nlm.nih.gov/gene/6403 PR:P16278 A eukaryotic-type beta-galactosidase that is encoded in the genome of human. HGNC: 4298 NCBI Gene: 2720 UniProtKB: P16278 acid beta-galactosidase (human) beta-galactosidase 1 (human) elastin receptor 1 (human) eukaryotic-type beta-galactosidase (human) hGLB1 PR:P16581 An E-selectin that is encoded in the genome of human. NCBI-Human-GeneID:6401 CD62 antigen-like family member E (human) CD62E (human) ELAM-1 (human) LECAM2 (human) endothelial leukocyte adhesion molecule 1 (human) leukocyte-endothelial cell adhesion molecule 2 (human) E-selectin (human) NCBI-Human-GeneID:6401 http://www.ncbi.nlm.nih.gov/gene/6401 PR:P17096 A high mobility group protein HMG-I/HMG-Y that is encoded in the genome of human. HGNC:5010 NCBIGene:3159 UniProtKB:P17096 HMG-I(Y) (human) high mobility group AT-hook protein 1 (human) high mobility group protein A1 (human) high mobility group protein HMG-I/HMG-Y (human) high mobility group protein R (human) hHMGA1 PR:P17174 A protein that is a translation product of the human GOT1 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:2805 cysteine aminotransferase, cytoplasmic (human) glutamic-oxaloacetic transaminase 1 hAST1 hGOT1 aspartate aminotransferase, cytoplasmic (human) NCBI-Human-GeneID:2805 http://www.ncbi.nlm.nih.gov/gene/2805 PR:P17181 An interferon-alpha/beta receptor alpha chain that is encoded in the genome of human. NCBI-Human-GeneID:3454 IFN-alpha/beta receptor 1 (human) hIFNAR1 type I interferon receptor 1 (human) interferon alpha/beta receptor 1 (human) NCBI-Human-GeneID:3454 http://www.ncbi.nlm.nih.gov/gene/3454 PR:P17676 A CCAAT/enhancer-binding protein beta that is encoded in the genome of human. LAP (human) HGNC:1834 NCBI-Human-GeneID:1051 UniProtKB:P17676 C/EBP beta (human) CCAAT/enhancer-binding protein beta (human) LIP (human) TCF-5 (human) interleukin-6-dependent-binding protein liver activator protein (human) liver-enriched inhibitory protein (human) nuclear factor NF-IL6 (human) transcription factor 5 (human) PP9092 TCF5 hCEBPB NCBI-Human-GeneID:1051 http://www.ncbi.nlm.nih.gov/gene/1051 PR:P18510 An interleukin-1 receptor antagonist protein that is encoded in the genome of human. C759H1186N208O232S10 DrugBank: DB00026 KEGG DRUG: D02934 PMID:31924766 PMID:32629875 PMID:33995419 anakinra (human) hIL1RN interleukin-1 receptor antagonist protein (human) KEGG DRUG: D02934 https://www.genome.jp/dbget-bin/www_bget?dr_ja:D02934 PMID:31924766 The clinical response to treatment with the IL-1 receptor antagonist anakinra mirrors the increased presence of IL-1beta in FACAS tissue similar to other urticarial autoinflammatory diseases such as CAPS. Incomplete clinical improvement by anakinra may be explained by continuous bradykinin generation via complex feedback loops and possibly further cytokines such as TNFalpha, which are induced by bradykinin and not inhibited by IL-1 blockade. Surprisingly, the IL-1beta priming effect is not linked to FXIIa activity as shown by the missing impact of alphaFXIIa on IL-1beta secretion. Thus, we believe that conformational changes of FXII p.W268R result in the recognition as a danger signal that serves as toll-like receptor agonist and inducer of IL-1beta release. PMID:32629875 Table 2. Investigational treatments with potential impact on vascular manifestations of COVID-19. These include anti-coagulant drugs to prevent thrombotic and thromboembolic disease; anti-inflammatory agents, such as steroids, interferon α2b, inhibitors of the JAK1/JAK2 kinases and of the Bruton tyrosine kinase; IL-6 or IL-6R inhibitors to neutralize IL-6 activity; anti-angiogenic agents targeting VEGF and angiopoietin 2; and renin-angiotensin-aldosterone system (RAAS) inhibitors. PMID:33995419 Anakinra is a recombinant replica of the IL-1 receptor antagonist that binds to soluble IL-1α and IL-1β preventing their pro-inflammatory activity. Anakinra, sarilumab, and tocilizumab were each associated with a statistically significant survival advantage compared to matched comparators (p < 0.05 for all comparisons) . We found that IL-1 and IL-6 inhibition improved long-term survival when initiated in the early phases of COVID-19 pneumonia before the establishment of severe ARDS (namely, PaO2/FiO2 ratio < 100 mmHg). The survival advantage offered by sarilumab and tocilizumab, in fact, was lost in patients with severe respiratory failure, and the efficacy of anakinra was markedly reduced although still proving superior to standard management. PR:P19320 A vascular cell adhesion protein 1 that is encoded in the genome of human. NCBI-Human-GeneID:7412 UniProtKB:P19320 INCAM-100 (human) V-CAM 1 (human) VCAM-1 (human) hVCAM1 vascular cell adhesion protein 1 (human) NCBI-Human-GeneID:7412 http://www.ncbi.nlm.nih.gov/gene/7412 PR:P19525 An interferon-induced, double-stranded RNA-activated protein kinase that is encoded in the genome of human. NCBI-Human-GeneID:5610 PMID:32726803 UniProtKB:P19525 eIF-2A protein kinase 2 (human) hEIF2AK2 protein kinase R (human) PKR interferon-induced, double-stranded RNA-activated protein kinase (human) NCBI-Human-GeneID:5610 http://www.ncbi.nlm.nih.gov/gene/5610 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). PR:P19838 A nuclear factor NF-kappa-B p105 subunit that is encoded in the genome of human. A nuclear factor NF-kappa-B p50 subunit in human. NCBI-Human-GeneID:4790 UniProtKB:P19838 DNA-binding factor KBF1 (human) EBP-1 (human) NFKB1 (human) nuclear factor NF-kappa-B p105 subunit (human) nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 (human) hNFKB1 NCBI-Human-GeneID:4790 http://www.ncbi.nlm.nih.gov/gene/4790 PR:P20591 An interferon-induced GTP-binding protein Mx1 that is encoded in the genome of human. NCBI-Human-GeneID:4599 PMID:32726803 PMID:33748697 UniProtKB:P20591 hMX1 interferon-induced GTP-binding protein Mx1 (human) NCBI-Human-GeneID:4599 http://www.ncbi.nlm.nih.gov/gene/4599 PMID:32726803 Notably, GRL-0617 treatment significantly rescued the expression of IFN-responsive genes (ISG15, OAS1, PKR (also known as EIF2AK2)) and MX1) in SARS-CoV-2-infected cells (Fig. 5g, Extended Data Fig. 7b). PMID:33748697 MX1 is part of the antiviral response induced by type I and III interferons . Inactivating mutations in genes belonging to type I interferon pathway and the consequently decreased levels of proteins have been shown to occur in patients with severe COVID-19. PR:P20700 A lamin-B1 that is encoded in the genome of human. HGNC:6637 NCBI-Human-GeneID:4001 NCBI-Mouse-GeneID:16906 NCBI-Rat-GeneID:116685 UniProtKB:P20700 lamin-B1 (human) LMN2 LMNB hLMNB1 NCBI-Human-GeneID:4001 http://www.ncbi.nlm.nih.gov/gene/4001 NCBI-Mouse-GeneID:16906 http://www.ncbi.nlm.nih.gov/gene/16906 NCBI-Rat-GeneID:116685 http://www.ncbi.nlm.nih.gov/gene/116685 PR:P21675 A transcription initiation factor TFIID subunit 1 that is encoded in the genome of human. HGNC:11535 Reactome:R-HSA-65539 UniProtKB:P21675 transcription initiation factor TFIID subunit 1 (human) hTAF1 PR:P22301 An interleukin-10 that is encoded in the genome of human. NCBI-Human-GeneID:3586 UniProtKB:P22301 IL-10 (human) hIL10 Active interleukin-10 inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T cells. Structurally, IL-10 is a protein of about 160 amino acids that contains four conserved cysteines involved in disulfide bonds. interleukin-10 (human) NCBI-Human-GeneID:3586 http://www.ncbi.nlm.nih.gov/gene/3586 PR:P23458 A tyrosine-protein kinase JAK1 that is encoded in the genome of human. NCBI-Human-GeneID:3716 UniProtKB:P23458 JAK-1 (human) Janus kinase 1 (human) hJAK1 tyrosine-protein kinase JAK1 (human) tyrosine-protein kinase JAK1 (human) NCBI-Human-GeneID:3716 http://www.ncbi.nlm.nih.gov/gene/3716 PR:P24298 An alanine aminotransferase 1 that is encoded in the genome of human. NCBI-Human-GeneID:2875 NCBI-Mouse-GeneID:76282 NCBI-Rat-GeneID:81670 ALT1 (human) GPT 1 (human) glutamate pyruvate transaminase 1 (human) glutamic--pyruvic transaminase glutamic--pyruvic transaminase (human) hGPT alanine aminotransferase 1 (human) HOIP_0040632 NCBI-Human-GeneID:2875 http://www.ncbi.nlm.nih.gov/gene/2875 NCBI-Mouse-GeneID:76282 http://www.ncbi.nlm.nih.gov/gene/76282 NCBI-Rat-GeneID:81670 http://www.ncbi.nlm.nih.gov/gene/81670 PR:P24385 A G1/S-specific cyclin-D1 that is encoded in the genome of human. NCBI-Human-GeneID:595 B-cell lymphoma 1 protein (human) BCL-1 (human) BCL-1 oncogene (human) G1/S-specific cyclin-D1 (human) PRAD1 oncogene (human) hCCND1 NCBI-Human-GeneID:595 http://www.ncbi.nlm.nih.gov/gene/595 PR:P24864 A G1/S-specific cyclin-E1 that is encoded in the genome of human. Ensembl:ENSG00000105173 HGNC:1589 NCBI-Human-GeneID:898 G1/S-specific cyclin-E1 (human) hCCNE1 NCBI-Human-GeneID:898 http://www.ncbi.nlm.nih.gov/gene/898 PR:P25963 An NF-kappa-B inhibitor alpha that is encoded in the genome of human. NCBI-Human-GeneID:4792 PMID:32726803 UniProtKB:P25963 I-kappaB alpha IkB-alpha inhibitor of NF-kappaB alpha NF-kappa-B inhibitor alpha (human) NCBI-Human-GeneID:4792 https://www.ncbi.nlm.nih.gov/gene/4792 PR:P26715 NCBI-Human-GeneID:3821 CD159 antigen-like family member A (human) CD159a (human) KLRC1 (human) NK cell receptor A (human) NKG2-A/B-activating NK receptor (human) NKG2A (human) NKG2-A/NKG2-B type II integral membrane protein (human) NCBI-Human-GeneID:3821 Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. The protein encoded by this gene belongs to the killer cell lectin-like receptor family, also called NKG2 family, which is a group of transmembrane proteins preferentially expressed in NK cells. This family of proteins is characterized by the type II membrane orientation and the presence of a C-type lectin domain. This protein forms a complex with another family member, KLRD1/CD94, and has been implicated in the recognition of the MHC class I HLA-E molecules in NK cells. The genes of NKG2 family members form a killer cell lectin-like receptor gene cluster on chromosome 12. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jan 2015] http://www.ncbi.nlm.nih.gov/gene/55922 PR:P27361 A mitogen-activated protein kinase 3 that is encoded in the genome of human. HGNC:6877 UniProtKB:P27361 ERK-1 (human) ERT2 (human) MAP kinase 3 (human) MAP kinase isoform p44 (human) UniProtKB:P27361 extracellular signal-regulated kinase 1 (human) mitogen-activated protein kinase 3 (human) hMAPK3 UniProtKB:P27361 Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:34497368). MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade also plays a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DEPTOR, FRS2 or GRB10) (PubMed:35216969). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade PR:P27487 A dipeptidyl peptidase IV that is encoded in the genome of human. NCBI-Human-GeneID:1803 UniProtKB:P27487 hDPP4 dipeptidyl peptidase 4 (human) NCBI-Human-GeneID:1803 http://www.ncbi.nlm.nih.gov/gene/59272 PR:P28482 A mitogen-activated protein kinase 1 that is encoded in the genome of human. HGNC:6871 UniProtKB:P28482 ERK-2 (human) ERT1 (human) MAP kinase 1 (human) MAP kinase 2 (human) extracellular signal-regulated kinase 2 (human) mitogen-activated protein kinase 1 (human) ERK2 MAPK1 PRKM1 hMAPK1 PR:P29459 An interleukin-12 subunit alpha that is encoded in the genome of human. NCBI-Human-GeneID:3592 UniProtKB:P29459 IL-12 subunit p35 (human) IL-12A (human) hIL12A interleukin-12 subunit alpha (human) NCBI-Human-GeneID:3592 http://www.ncbi.nlm.nih.gov/gene/3592 PR:P29460 An interleukin-12 subunit beta that is encoded in the genome of human. NCBI-Human-GeneID:3593 UniProtKB:P29460 IL-12 subunit p40 (human) IL-12B (human) NK cell stimulatory factor chain 2 (human) hIL12B IL12B (human)in COVID-19 interleukin-12 subunit beta (human) NCBI-Human-GeneID:3593 http://www.ncbi.nlm.nih.gov/gene/3593 PR:P29466 A caspase-1 that is encoded in the genome of human. NCBI-Human-GeneID:834 PMID:20303873 CASP-1 (human) ICE (human) IL-1 beta-converting enzyme (human) IL-1BC (human) interleukin-1 beta convertase (human) caspase-1 (human) NCBI-Human-GeneID:834 https://www.ncbi.nlm.nih.gov/gene/834 NCBI-Human-GeneID:834 http://www.ncbi.nlm.nih.gov/gene/834 PR:P30556 An angiotensin II receptor 1 that is encoded in the genome of human. NCBI-Human-GeneID:185 PMID:32142651 UniProtKB:P30556 AT1 (human) AT1AR (human) AT1BR (human) angiotensin II type-1 receptor (human) hAGTR1 AGTR1 type-1 angiotensin II receptor (human) NCBI-Human-GeneID:185 http://www.ncbi.nlm.nih.gov/gene/185 PR:P31749 A RAC-alpha serine/threonine-protein kinase that is encoded in the genome of human HGNC:391 UniProtKB:P31749 PKB alpha (human) RAC-PK-alpha (human) RAC-alpha serine/threonine-protein kinase (human) protein kinase B (human) protein kinase B alpha (human) proto-oncogene c-Akt (human) AKT1 PKB RAC hAKT1 PR:P31785 A cytokine receptor common subunit gamma that is encoded in the genome of human. UniProtKB:P31785 cytokine receptor common subunit gamma (human) PR:P34331 A protein that is a translation product of the plk-1 gene in worm. Enables protein kinase activity. Involved in several processes, including organelle organization; positive regulation of nematode male tail tip morphogenesis; and protein phosphorylation. Located in several cellular components, including condensed chromosome; microtubule cytoskeleton; and nucleus. Expressed in AB and embryonic cell. Human ortholog(s) of this gene implicated in several diseases, including breast carcinoma; reproductive organ cancer (multiple); and urinary bladder cancer. Is an ortholog of human PLK1 (polo like kinase 1). Enables protein kinase activity. Involved in several processes, including organelle organization; positive regulation of nematode male tail tip morphogenesis; and protein phosphorylation. Located in several cellular components, including condensed chromosome; microtubule cytoskeleton; and nucleus. Expressed in AB and embryonic cell. Human ortholog(s) of this gene implicated in several diseases, including breast carcinoma; reproductive organ cancer (multiple); and urinary bladder cancer. Is an ortholog of human PLK1 (polo like kinase 1). plk-1 encodes a serine/threonine polo-like kinase homologous to Drosophila polo and Saccharomyces cerevisiae CDC5; during development, plk-1 functions to regulate meiotic cell cycle progression as well as embryonic cytoplasmic polarity in newly fertilized embryos and possibly germline development; specifically, plk-1 is required for meiotic nuclear envelope breakdown, polar body formation and extrusion, and proper chromosome segregation during meiosis possibly via phosphorylation and subsequent degradation of REC-8, a meiotic-specific cohesin; in regulating embryonic polarity, PLK-1 functions to regulate activity of the MEX-5/6 zinc-finger proteins, with which it interacts, via its polo box domain, in yeast two-hybrid assays; PLK-1 is localized diffusely in the cytoplasm of mature oocytes, but during meiosis I becomes associated with pre-metaphase chromatin and then at anaphase with chromatin and the area between dividing chromatin; in embryos, PLK-1 localizes to the cytoplasm of somatic blastomeres and during mitosis, to centrosomes, metaphase chromatin and, at telophase, to the area between dividing chromatin; the asymmetric localization of PLK-1 to somatic cytoplasm of early embryos is dependent upon the PAR proteins and MEX-5/6. plk-1 encodes a serine/threonine polo-like kinase homologous to Drosophila polo and Saccharomyces cerevisiae CDC5; during development, plk-1 functions to regulate meiotic cell cycle progression as well as embryonic cytoplasmic polarity in newly fertilized embryos and possibly germline development; specifically, plk-1 is required for meiotic nuclear envelope breakdown, polar body formation and extrusion, and proper chromosome segregation during meiosis possibly via phosphorylation and subsequent degradation of REC-8, a meiotic-specific cohesin; in regulating embryonic polarity, PLK-1 functions to regulate activity of the MEX-5/6 zinc-finger proteins, with which it interacts, via its polo box domain, in yeast two-hybrid assays; PLK-1 is localized diffusely in the cytoplasm of mature oocytes, but during meiosis I becomes associated with pre-metaphase chromatin and then at anaphase with chromatin and the area between dividing chromatin; in embryos, PLK-1 localizes to the cytoplasm of somatic blastomeres and during mitosis, to centrosomes, metaphase chromatin and, at telophase, to the area between dividing chromatin; the asymmetric localization of PLK-1 to somatic cytoplasm of early embryos is dependent upon the PAR proteins and MEX-5/6. PMID:29276126 UniProtKB:P34331 https://wormbase.org/species/c_elegans/gene/WBGene00004042 plk-1 (worm) PLK1 (worm) Enables protein kinase activity. Involved in several processes, including organelle organization; positive regulation of nematode male tail tip morphogenesis; and protein phosphorylation. Located in several cellular components, including condensed chromosome; microtubule cytoskeleton; and nucleus. Expressed in AB and embryonic cell. Human ortholog(s) of this gene implicated in several diseases, including breast carcinoma; reproductive organ cancer (multiple); and urinary bladder cancer. Is an ortholog of human PLK1 (polo like kinase 1). https://wormbase.org/species/c_elegans/gene/WBGene00004042 plk-1 encodes a serine/threonine polo-like kinase homologous to Drosophila polo and Saccharomyces cerevisiae CDC5; during development, plk-1 functions to regulate meiotic cell cycle progression as well as embryonic cytoplasmic polarity in newly fertilized embryos and possibly germline development; specifically, plk-1 is required for meiotic nuclear envelope breakdown, polar body formation and extrusion, and proper chromosome segregation during meiosis possibly via phosphorylation and subsequent degradation of REC-8, a meiotic-specific cohesin; in regulating embryonic polarity, PLK-1 functions to regulate activity of the MEX-5/6 zinc-finger proteins, with which it interacts, via its polo box domain, in yeast two-hybrid assays; PLK-1 is localized diffusely in the cytoplasm of mature oocytes, but during meiosis I becomes associated with pre-metaphase chromatin and then at anaphase with chromatin and the area between dividing chromatin; in embryos, PLK-1 localizes to the cytoplasm of somatic blastomeres and during mitosis, to centrosomes, metaphase chromatin and, at telophase, to the area between dividing chromatin; the asymmetric localization of PLK-1 to somatic cytoplasm of early embryos is dependent upon the PAR proteins and MEX-5/6. https://wormbase.org/species/c_elegans/gene/WBGene00004042 PMID:29276126 During the asymmetric division of the C. elegans zygote, the RNA-binding protein MEX-5 forms an anterior-rich cytoplasmic gradient that causes the RNA-binding protein POS-1 to form an opposing, posterior-rich gradient. We demonstrate that the polo-like kinase PLK-1 mediates the repulsive coupling between MEX-5 and POS-1 by increasing the mobility of POS-1 in the anterior. PLK-1 is enriched in the anterior cytoplasm and phosphorylates POS-1, which is both necessary and sufficient to increase POS-1 mobility. Regulation of POS-1 mobility depends on both the interaction between PLK-1 and MEX-5 and between MEX-5 and RNA, suggesting that MEX-5 may recruit PLK-1 to RNA in the anterior. The low concentration of MEX-5/PLK-1 in the posterior cytoplasm provides a permissive environment for the retention of POS-1, which depends on POS-1 RNA binding. PR:P34482 A protein that is a translation product of the zif-1 gene in worm. Involved in embryo development and ubiquitin-dependent protein catabolic process. Involved in embryo development and ubiquitin-dependent protein catabolic process. zif-1 encodes a SOCS-box protein that promotes establishment of the germ line by targetting germline proteins for cullin-dependent degradation in non-germline (somatic) cells; ZIF-1 binds germline CCCH-(zinc)-finger proteins and the E3 ubiquitin ligase subunit elongin C (ELC-1); while ZIF-1 has no obvious homologs, it may be analogous to the Drosophila SOCS-box protein GUSTAVUS, which is required for VASA localization to the germline and which does have mammalian homologs. zif-1 encodes a SOCS-box protein that promotes establishment of the germ line by targetting germline proteins for cullin-dependent degradation in non-germline (somatic) cells; ZIF-1 binds germline CCCH-(zinc)-finger proteins and the E3 ubiquitin ligase subunit elongin C (ELC-1); while ZIF-1 has no obvious homologs, it may be analogous to the Drosophila SOCS-box protein GUSTAVUS, which is required for VASA localization to the germline and which does have mammalian homologs. UniProtKB:P34482 WormBase:WBGene00006977 zif-1 (worm) zinc finger-interacting factor 1 (worm) ZIF1 (worm) Involved in embryo development and ubiquitin-dependent protein catabolic process. https://wormbase.org/species/c_elegans/gene/WBGene00006977 zif-1 encodes a SOCS-box protein that promotes establishment of the germ line by targetting germline proteins for cullin-dependent degradation in non-germline (somatic) cells; ZIF-1 binds germline CCCH-(zinc)-finger proteins and the E3 ubiquitin ligase subunit elongin C (ELC-1); while ZIF-1 has no obvious homologs, it may be analogous to the Drosophila SOCS-box protein GUSTAVUS, which is required for VASA localization to the germline and which does have mammalian homologs. https://wormbase.org/species/c_elegans/gene/WBGene00006977 PR:P34707 A protein that is a translation product of the skn-1 gene in worm. Enables Hsp70 protein binding activity and RNA polymerase II transcription regulatory region sequence-specific DNA binding activity. Involved in several processes, including endoderm development; endoplasmic reticulum unfolded protein response; and positive regulation of macromolecule metabolic process. Located in endoplasmic reticulum; mitochondrion; and nucleus. Expressed in several structures, including germ line; head ganglion; intestine; neurons; and pharynx. Human ortholog(s) of this gene implicated in several diseases, including Alzheimer's disease; liver disease (multiple); obesity; and pulmonary emphysema. Is an ortholog of human NFE2L1 (nuclear factor, erythroid 2 like 1); NFE2L2 (nuclear factor, erythroid 2 like 2); and NFE2L3 (nuclear factor, erythroid 2 like 3). Enables Hsp70 protein binding activity and RNA polymerase II transcription regulatory region sequence-specific DNA binding activity. Involved in several processes, including endoderm development; endoplasmic reticulum unfolded protein response; and positive regulation of macromolecule metabolic process. Located in endoplasmic reticulum; mitochondrion; and nucleus. Expressed in several structures, including germ line; head ganglion; intestine; neurons; and pharynx. Human ortholog(s) of this gene implicated in several diseases, including Alzheimer's disease; liver disease (multiple); obesity; and pulmonary emphysema. Is an ortholog of human NFE2L1 (nuclear factor, erythroid 2 like 1); NFE2L2 (nuclear factor, erythroid 2 like 2); and NFE2L3 (nuclear factor, erythroid 2 like 3). skn-1 encodes a bZip transcription factor orthologous to the mammalian Nrf (Nuclear factor-erythroid-related factor) transcription factors; during early embryogenesis, maternally provided SKN-1 is required for specification of the EMS blastomere, a mesendodermal precursor that gives rise to pharyngeal, muscle, and intestinal cells; later, during postembryonic development, SKN-1 functions in the p38 MAPK pathway to regulate the oxidative stress response and in parallel to DAF-16/FOXO in the DAF-2-mediated insulin/IGF-1-like signaling pathway to regulate adult lifespan; in vitro assays indicate that SKN-1 can be directly phosphorylated by the AKT-1, AKT-2, and SGK-1 kinases that lie downstream of DAF-2 in the insulin signaling pathway and in vivo experiments suggest that this phosphorylation is essential for regulation of SKN-1 nuclear accumulation and hence, transcriptional regulator activity; in the early embryo, SKN-1 is detected at highest levels in nuclei of the P1 blastomere and its descendants through the 8-cell stage of embryogenesis; later in embryogenesis, SKN-1 is observed in all hypodermal and intestinal nuclei, with reporter constructs indicating that intestinal expression begins as early as the 50-100-cell stage; in larvae and young adults, SKN-1::GFP reporters are expressed in the intestine and ASI neurons, with expression in intestinal nuclei enhanced under conditions of stress or reduced DAF-2 signaling. skn-1 encodes a bZip transcription factor orthologous to the mammalian Nrf (Nuclear factor-erythroid-related factor) transcription factors; during early embryogenesis, maternally provided SKN-1 is required for specification of the EMS blastomere, a mesendodermal precursor that gives rise to pharyngeal, muscle, and intestinal cells; later, during postembryonic development, SKN-1 functions in the p38 MAPK pathway to regulate the oxidative stress response and in parallel to DAF-16/FOXO in the DAF-2-mediated insulin/IGF-1-like signaling pathway to regulate adult lifespan; in vitro assays indicate that SKN-1 can be directly phosphorylated by the AKT-1, AKT-2, and SGK-1 kinases that lie downstream of DAF-2 in the insulin signaling pathway and in vivo experiments suggest that this phosphorylation is essential for regulation of SKN-1 nuclear accumulation and hence, transcriptional regulator activity; in the early embryo, SKN-1 is detected at highest levels in nuclei of the P1 blastomere and its descendants through the 8-cell stage of embryogenesis; later in embryogenesis, SKN-1 is observed in all hypodermal and intestinal nuclei, with reporter constructs indicating that intestinal expression begins as early as the 50-100-cell stage; in larvae and young adults, SKN-1::GFP reporters are expressed in the intestine and ASI neurons, with expression in intestinal nuclei enhanced under conditions of stress or reduced DAF-2 signaling. UniProtKB:P34707 WormBase:WBGene00004804 protein skinhead-1 (worm) skn-1 (worm) SKN1 (worm) Enables Hsp70 protein binding activity and RNA polymerase II transcription regulatory region sequence-specific DNA binding activity. Involved in several processes, including endoderm development; endoplasmic reticulum unfolded protein response; and positive regulation of macromolecule metabolic process. Located in endoplasmic reticulum; mitochondrion; and nucleus. Expressed in several structures, including germ line; head ganglion; intestine; neurons; and pharynx. Human ortholog(s) of this gene implicated in several diseases, including Alzheimer's disease; liver disease (multiple); obesity; and pulmonary emphysema. Is an ortholog of human NFE2L1 (nuclear factor, erythroid 2 like 1); NFE2L2 (nuclear factor, erythroid 2 like 2); and NFE2L3 (nuclear factor, erythroid 2 like 3). https://wormbase.org/species/c_elegans/gene/WBGene00004804 skn-1 encodes a bZip transcription factor orthologous to the mammalian Nrf (Nuclear factor-erythroid-related factor) transcription factors; during early embryogenesis, maternally provided SKN-1 is required for specification of the EMS blastomere, a mesendodermal precursor that gives rise to pharyngeal, muscle, and intestinal cells; later, during postembryonic development, SKN-1 functions in the p38 MAPK pathway to regulate the oxidative stress response and in parallel to DAF-16/FOXO in the DAF-2-mediated insulin/IGF-1-like signaling pathway to regulate adult lifespan; in vitro assays indicate that SKN-1 can be directly phosphorylated by the AKT-1, AKT-2, and SGK-1 kinases that lie downstream of DAF-2 in the insulin signaling pathway and in vivo experiments suggest that this phosphorylation is essential for regulation of SKN-1 nuclear accumulation and hence, transcriptional regulator activity; in the early embryo, SKN-1 is detected at highest levels in nuclei of the P1 blastomere and its descendants through the 8-cell stage of embryogenesis; later in embryogenesis, SKN-1 is observed in all hypodermal and intestinal nuclei, with reporter constructs indicating that intestinal expression begins as early as the 50-100-cell stage; in larvae and young adults, SKN-1::GFP reporters are expressed in the intestine and ASI neurons, with expression in intestinal nuclei enhanced under conditions of stress or reduced DAF-2 signaling. https://wormbase.org/species/c_elegans/gene/WBGene00004804 PR:P35225 An interleukin-13 that is encoded in the genome of human. NCBI-Human-GeneID:3596 UniProtKB:P35225 IL-13 (human) hIL13 interleukin-13(human) interleukin-13 (human) NCBI-Human-GeneID:3596 http://www.ncbi.nlm.nih.gov/gene/3596 PR:P35613 A basigin that is encoded in the genome of human. UniProtKB:P35613 CD147 hBSG basigin (human) PR:P37840 An alpha-synuclein that is encoded in the genome of human. HGNC:11138 UniProtKB:P37840 NACP (human) alpha-synuclein (human) non-A beta component of AD amyloid (human) non-A4 component of amyloid precursor (human) hSNCA PR:P38484 An interferon-gamma receptor beta chain that is encoded in the genome of human. AF-1 (human) IFN-gamma receptor 2 (human) hIFNGR2 interferon gamma receptor 2 (human) IFNGR2 (human) PR:P38936 A protein that is a translation product of the human CDKN1B gene or a 1:1 ortholog thereof. p21 (human) NCBI-Human-GeneID:1026 UniProtKB:P38936 CDK-interacting protein 1 (human) MDA-6 (human) cyclin-dependent kinase inhibitor 1 (human) melanoma differentiation-associated protein (human) melanoma differentiation-associated protein 6 (human) hCDKN1A NCBI-Human-GeneID:1026 http://www.ncbi.nlm.nih.gov/gene/1026 PR:P39055 A dynamin-1 that is encoded in the genome of worm. UniProtKB: P39055 Wormbase:WBGene00001130 DNM1 (worm) Wormbase:WBGene00001130 Enables GTPase activity. Involved in several processes, including embryo development; positive regulation of necrotic cell death; and vesicle-mediated transport. Located in several cellular components, including plasma membrane; plasma membrane bounded cell projection; and spindle microtubule. Expressed in several structures, including neurons; non-striated muscle; pharyngeal-intestinal valve; rectal valve cell; and somatic nervous system. Used to study early infantile epileptic encephalopathy. Human ortholog(s) of this gene implicated in several diseases, including Alzheimer's disease; Charcot-Marie-Tooth disease dominant intermediate B; centronuclear myopathy 1; and developmental and epileptic encephalopathy 31. Is an ortholog of human DNM1 (dynamin 1); DNM2 (dynamin 2); and DNM3 (dynamin 3). dyn-1 encodes the C. elegans ortholog of the dynamin GTPase; dyn-1 activity is required for endocytosis, synaptic vesicle recycling, cytokinesis, and the CED-1 pathway that regulates engulfment and degradation of apoptotic cells; mutations in dyn-1 affect locomotion, egg-laying, defecation, and embryonic development, indicating that dyn-1's endocytic function is required for a number of diverse processes; dyn-1 reporter fusion constructs are expressed in motor neurons, intestinal cells, and pharyngeal muscle. http://www.wormbase.org/species/c_elegans/gene/WBGene00001130 PR:P39689 A cyclin-dependent kinase inhibitor 1 that is encoded in the genome of mouse. MGI:104556 NCBI Gene ID:12575 NCBI-Human-GeneID:1026 CDK-interacting protein 1 (mouse) cyclin-dependent kinase inhibitor 1 (mouse) melanoma differentiation-associated protein (mouse) mCDKN1A NCBI-Human-GeneID:1026 http://www.ncbi.nlm.nih.gov/gene/1026 PR:P40763 A signal transducer and activator of transcription 3 that is encoded in the genome of human. NCBI-Human-GeneID: PMID:25181692 UniProtKB:P40763 acute-phase response factor (human) hSTAT3 signal transducer and activator of transcription 3 (human) NCBI-Human-GeneID: http://www.ncbi.nlm.nih.gov/gene/6774 PMID:25181692 Tumor-Associated Macrophages Produce Interleukin 6 and Signal via STAT3 to Promote Expansion of Human Hepatocellular Carcinoma Stem Cells TAMs produce IL6, which promotes expansion of these CSCs and tumorigenesis. Levels of IL6 in human HCC samples correlate with tumor stage and markers of CSCs. We have identified that STAT3 signaling in HCC cells following TAM interaction is critical to increased CSC expansion and increased tumor growth. PR:P40933 A protein that is a translation product of the human IL15 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:3600 UniProtKB:P40933 IL-15 (human) hIL15 interleukin-15 (human) NCBI-Human-GeneID:3600 http://www.ncbi.nlm.nih.gov/gene/3600 PR:P41932 A protein that is a translation product of the par-5 gene in worm. Is involved in several processes, including cell differentiation; establishment of localization in cell; and multicellular organism development. Located in cell cortex and nucleus. Is expressed in head neurons. Human ortholog(s) of this gene are implicated in several diseases, including carcinoma (multiple); developmental and epileptic encephalopathy 56; and urinary bladder cancer. Is an ortholog of human YWHAB (tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein beta) and YWHAZ (tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta). PAR-5 encodes one of two C. elegans 14-3-3 proteins; par-5 is essential for early embryonic development, particularly for early embryonic asymmetry; PAR-5 also functions in a Wnt/MAPK signaling pathway to regulate the nuclear level of the POP-1/TCF transcription factor; PAR-5 has been shown to physically interact with a number of proteins, including those involved in G protein signaling pathways and regulation of adult lifespan. UniProtKB:P41932 http://www.wormbase.org/species/c_elegans/gene/WBGene00003920 14-3-3-like protein 1 (worm) par-5 (worm) partitioning defective protein 5 (worm) M117.2 par-5 PAR5 (worm) PR:P42224 A signal transducer and activator of transcription 1 that is encoded in the genome of human. UniProtKB:P42224 hSTAT1 signal transducer and activator of transcription 1-alpha/beta (human) transcription factor ISGF-3 components p91/p84 (human) signal transducer and activator of transcription 1-alpha/beta (human) PR:P42345 A serine/threonine-protein kinase mTOR that is encoded in the genome of human. NCBI-Human-GeneID:2475 NCBI-Mouse-GeneID:56717 NCBI-Rat-GeneID:56718 https://omim.org/entry/601231 FK506-binding protein 12-rapamycin complex-associated protein 1 (human) FKBP12-rapamycin complex-associated protein (human) mTOR (human) mammalian target of rapamycin (human) mechanistic target of rapamycin (human) rapamycin target protein 1 (human) serine/threonine-protein kinase mTOR (human) hMTOR NCBI-Human-GeneID:2475 https://www.ncbi.nlm.nih.gov/gene/2475 NCBI-Mouse-GeneID:56717 https://www.ncbi.nlm.nih.gov/gene/56717 NCBI-Rat-GeneID:56718 https://www.ncbi.nlm.nih.gov/gene/56718 PR:P42771 p16-INK4 (human) A cyclin-dependent kinase inhibitor 2A (human), isoforms h1, h2, h3, and h5." HGNC:1787 NCBI-Human-GeneID:1029 UniiProt:P42771 cyclin-dependent kinase inhibitor 2A, isoforms h1/h2/h3/h5 (human) hCDKN2A/iso:[1/2/3/5] NCBI-Human-GeneID:1029 PR:P42772 p15-INK4b (human) A cyclin-dependent kinase 4 inhibitor B that is encoded in the genome of human. HGNC:1788 NCBI-Human-GeneID:1030 PANTHER:PTHR24144:SF138 CDK4I CDKN2B gene translation product (human) INK4b (human) MTS-2 (human) cyclin-dependent kinase 4 inhibitor B (human) multiple tumor suppressor 2 (human) p15-INK4b (human) p15INK4b (human) hCDKN2B NCBI-Human-GeneID:1030 PR:P43694 A transcription factor GATA-4 that is encoded in the genome of human. HGNC:4173 NCBI-Human-GeneID:2626 UniProtKB:P43694 GATA-binding factor 4 (human) transcription factor GATA-4 (human) Gata-4 hGATA4 NCBI-Human-GeneID:2626 https://www.ncbi.nlm.nih.gov/gene/2626 PR:P46527 A protein that is a translation product of the human CDKN1B gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:1027 UniProtKB:P46527 cyclin-dependent kinase inhibitor 1B (human) cyclin-dependent kinase inhibitor p27 (human) p27Kip1 (human) KIP1 p27 hCDKN1B NCBI-Human-GeneID:1027 http://www.ncbi.nlm.nih.gov/gene/1027 PR:P48551 An interferon alpha/beta receptor 2 that is encoded in the genome of human. NCBI-Human-GeneID:3455 UniProtKB:P48551 IFN-alpha binding protein (human) Interferon alpha/beta receptor-2 (human) hIFNAR2 interferon alpha/beta receptor 2 (human) NCBI-Human-GeneID:3455 http://www.ncbi.nlm.nih.gov/gene/3455 PR:P49137 A MAP kinase-activated protein kinase 2 that is encoded in the genome of human. MAP kinase-activated protein kinase 2 (human) MAPK- activated protein kinase 2 (human) MK-2 (human) MK2 (human) hMAPKAPK2 PR:P52926 A high mobility group protein HMGI-C that is encoded in the genome of human. HGNC:5009 NCBI Gene:8091 UniProtKB:P52926 high mobility group AT-hook protein 2 (human) high mobility group protein HMGI-C (human) HMGIC hHMGA2 PR:P54198 A protein HIRA that is encoded in the genome of human. HGNC:4916 NCBI-Human-GeneID:7290 UniProtKB:P54198 TUP1-like enhancer of split protein 1 (human) protein HIRA DGCR1 HIR TUPLE1 hHIRA NCBI-Human-GeneID:7290 http://www.ncbi.nlm.nih.gov/gene/7290 PR:P57764 A gasdermin-D that is encoded in the genome of human. NCBI-Human-GeneID:79792 NCBI-Mouse-GeneID:69146 NCBI-Rat-GeneID:315084 UniProtKB:P57764 hGSDMD gasdermin-D (human) NCBI-Human-GeneID:79792 https://www.ncbi.nlm.nih.gov/gene/79792 NCBI-Mouse-GeneID:69146 https://www.ncbi.nlm.nih.gov/gene/69146 NCBI-Rat-GeneID:315084 https://www.ncbi.nlm.nih.gov/gene/315084 PR:P60484 A phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN that is encoded in the genome of human. HGNC:9588 NCBI Gene:5728 UniProtKB:P60484 mutated in multiple advanced cancers 1 (human) phosphatase and tensin homolog (human) phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (human) MMAC1 PTEN TEP hPTEN PR:P60568 An interleukin-2 that is encoded in the genome of human. NCBI-Human-GeneID:3558 UniProtKB:P60568 IL-2 (human) T-cell growth factor (human) hIL2 interleukin-2 (human) interleukin-2 (human) NCBI-Human-GeneID:3558 http://www.ncbi.nlm.nih.gov/gene/3558 PR:P61978 A heterogeneous nuclear ribonucleoprotein K that is encoded in the genome of human. NCBI-Human-GeneID:3190 PMID:32726803 UniProtKB:P61978 TUNP (human) hHNRNPK transformation up-regulated nuclear protein (human) heterogeneous nuclear ribonucleoprotein K (human) NCBI-Human-GeneID:3190 http://www.ncbi.nlm.nih.gov/gene/3190 PR:P78396 A cyclin-A1 that is encoded in the genome of human. HGNC:1577 NCBI Gene:8900 UniProtKB:P78396] cyclin-A1 (human) hCCNA1 PR:P78527 A DNA-dependent protein kinase catalytic subunit that is encoded in the genome of human. NCBI-Human-GeneID:5591 PMID:32726803 UniProtKB:P78527 DNA-PK catalytic subunit (human) DNPK1 (human) hPRKDC DNA-dependent protein kinase catalytic subunit (human) NCBI-Human-GeneID:5591 http://www.ncbi.nlm.nih.gov/gene/5591 PR:P78536 An ADAM 17 endopeptidase that is encoded in the genome of human. NCBI-Human-GeneID:6868 ADAM 17 (human) TNF-alpha convertase (human) hADAM17 disintegrin and metalloproteinase domain-containing protein 17 (human) NCBI-Human-GeneID:6868 http://www.ncbi.nlm.nih.gov/gene/6868 PR:P78556 A C-C motif chemokine 20 that is encoded in the genome of human. UniProtKB:P78556 C-C motif chemokine 20 (human) hCCL20 PR:Q00534 A CDK2-related kinase that is a translation product of the human CDK6 gene or a 1:1 ortholog thereof. UniProtKB:Q00534 http://www.drugtargetontology.org/dto/DTO_03100072 CRK2 (human) Cell division protein kinase 6 (human) Serine/threonine protein kinase PLSTIRE (human) hCDK6 PR:Q00987 An E3 ubiquitin-protein ligase Mdm2 that is encoded in the genome of human. HGNC:6973 NCBI Gene:4193 UniProtKB:Q00987 E3 ubiquitin-protein ligase Mdm2 (human) RING-type E3 ubiquitin transferase Mdm2 (human) double minute 2 protein (human) hdm2 (human) oncoprotein Mdm2 (human) p53-binding protein Mdm2 (human) hMDM2 PR:Q01094 A transcription factor E2F1 that is encoded in the genome of human. Ensembl:ENSG00000101412 HGNC:3113 NCBI-Human-GeneID:1869 UniProtKB:Q01094 E2F-1 (human) PBR3 (human) RBAP-1 (human) RBBP-3 (human) pRB-binding protein E2F-1 (human) transcription factor E2F1 (human) hE2F1 NCBI-Human-GeneID:1869 http://www.ncbi.nlm.nih.gov/gene/1869 PR:Q04206 A transcription factor p65 that is encoded in the genome of human. NCBI-Human-GeneID:5970 PMID:32726803 nuclear factor NF-kappa-B p65 subunit (human) nuclear factor of kappa light polypeptide gene enhancer in B-cells 3 (human) transcription factor p65 (human) hRelA NCBI-Human-GeneID:5970 http://www.ncbi.nlm.nih.gov/gene/5970 PMID:32726803 Moreover, phosphorylation of IRF3 and TBK1, markers for IFN pathway activation, and p65 phosphorylation, used to monitor NF-κB pathway activation, were increased in SARS-CoV-2-infected cells upon GRL-0617 treatment (Fig. 5f). PR:Q07812 An apoptosis regulator BAX that is encoded in the genome of human. HGNC:959 NCBI Gene:581 UniProtKB:Q07812 Bcl-2-like protein 4 (human) Bcl2-L-4 (human) apoptosis regulator BAX (human) BAX BCL2L4 hBAX PR:Q07817 A Bcl-2-like protein 1 that is encoded in the genome of human. HGNC:992 NCBI Gene: 598 UniProtKB:Q07817 Bcl-2-like protein 1 (human) Bcl2-L-1 (human) apoptosis regulator Bcl-X (human) BCL2L (human) BCLX hBCL2L1 PR:Q09436 A protein that is a translation product of the mex-6 gene in worm. Enables mRNA 3'-UTR binding activity; protein domain specific binding activity; and protein kinase binding activity. Involved in regulation of protein localization. Located in P granule. Expressed in AB; ABa; ABp; and germ line. Enables mRNA 3'-UTR binding activity; protein domain specific binding activity; and protein kinase binding activity. Involved in regulation of protein localization. Located in P granule. Expressed in AB; ABa; ABp; and germ line. mex-6 encodes a CCCH zinc-finger protein highly similar to MEX-5 that functions with MEX-5 to affect embryonic viability, establish soma germline asymmetry in embryos and establish PIE-1, MEX-1, and POS-1 asymmetry in embryos, and also affects formation of intestinal cells; MEX-6 and MEX-5 may act downstream of the PAR proteins mex-6 encodes a CCCH zinc-finger protein highly similar to MEX-5 that functions with MEX-5 to affect embryonic viability, establish soma germline asymmetry in embryos and establish PIE-1, MEX-1, and POS-1 asymmetry in embryos, and also affects formation of intestinal cells; MEX-6 and MEX-5 may act downstream of the PAR proteins PMID:10882103 UniProtKB:Q9XUB2 https://wormbase.org/species/c_elegans/gene/WBGene00003231 mex-6 (worm) zinc finger protein mex-6 (worm) MEX6 (worm) Enables mRNA 3'-UTR binding activity; protein domain specific binding activity; and protein kinase binding activity. Involved in regulation of protein localization. Located in P granule. Expressed in AB; ABa; ABp; and germ line. http://www.wormbase.org/species/c_elegans/gene/WBGene00003231 mex-6 encodes a CCCH zinc-finger protein highly similar to MEX-5 that functions with MEX-5 to affect embryonic viability, establish soma germline asymmetry in embryos and establish PIE-1, MEX-1, and POS-1 asymmetry in embryos, and also affects formation of intestinal cells; MEX-6 and MEX-5 may act downstream of the PAR proteins http://www.wormbase.org/species/c_elegans/gene/WBGene00003231 PMID:10882103 Many of the examples of protein mislocalization we observe in mex-5;mex-6 mutant embryos involve the anterior misexpression of proteins that normally are expressed in posterior and germline blastomeres. For example, the proteins SKN-1, PAL-1, MEX-1, PIE-1, POS-1, and SKN-1 are each misexpressed in the anterior of mex-5;mex-6 mutant embryos. This result suggests that in wild-type embryos, MEX-5/MEX-6 function to inhibit the anterior expression of these proteins. PR:Q09472 A histone acetyltransferase p300 that is encoded in the genome of human. HGNC:3373 UniProtKB:Q09472 E1A-associated protein p300 (human) histone acetyltransferase p300 (human) histone butyryltransferase p300 (human) histone crotonyltransferase p300 (human) p300 HAT (human) hEP300 PR:Q09510 mlc-4 A myosin regulatory light chain MRLC3 that is encoded in the genome of worm. [OMA:Q09510, PRO:DNx] WormBase:WBGene00003372 myosin regulatory light chain (worm) nmRLC (worm) non-muscle myosin regulatory light chain (worm) C56G7.1 mlc-4 MYL12A (worm) WormBase:WBGene00003372 http://www.wormbase.org/species/c_elegans/gene/WBGene00003372 PR:Q12778 A forkhead box protein O1 that is encoded in the genome of human. HGNC:3819 forkhead box protein O1A (human) forkhead in rhabdomyosarcoma (human) FKHR FOXO1 FOXO1A hFOXO1 PR:Q12888 A TP53-binding protein 1 that is encoded in the genome of human. Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). HGNC:11999 NCBI-Human-GeneID:7158 UniProtKB:Q12888 53BP1 (human) TP53-binding protein 1 (human) p53-binding protein 1 (human) p53BP1 (human) hTP53BP1 Some DDR factors accumulate at sites of DNA damage and form cytologically detectable nuclear foci composed of extended chromatin modification events, such as the phosphorylation of histone H2AX, and the proteins associated with them, including MDC1, 53BP1 and the activated form of the kinase ataxia telangiectasia mutated (ATM). PMID:33328614 NCBI-Human-GeneID:7158 http://www.ncbi.nlm.nih.gov/gene/7158 PR:Q13315 A serine-protein kinase ATM that is encoded in the genome of human. https://www.ncbi.nlm.nih.gov/gene/641371 NCBI-Human-GeneID:472 NCBI-Mouse-GeneID:11920 NCBI-Rat-GeneID:300711 A-T mutated (human) A-T mutated homolog (human) ataxia telangiectasia mutated (human) ataxia telangiectasia mutated homolog (human) serine-protein kinase ATM (human) hATM HOIP_0003252 NCBI-Human-GeneID:472 http://www.ncbi.nlm.nih.gov/gene/472 NCBI-Mouse-GeneID:11920 http://www.ncbi.nlm.nih.gov/gene/11920 NCBI-Rat-GeneID:300711 http://www.ncbi.nlm.nih.gov/gene/300711 PR:Q13535 A serine/threonine-protein kinase ATR that is encoded in the genome of human. HGNC:882 NCBI-Human-GeneID:545 FRAP-related protein 1 (human) ataxia telangiectasia and Rad3-related protein (human) serine/threonine-protein kinase ATR FRP1 hATR NCBI-Human-GeneID:545 http://www.ncbi.nlm.nih.gov/gene/545 PR:Q14116 An interleukin-18 that is encoded in the genome of human. UniProtKB:Q14116 IFN-gamma-inducing factor (human) IL-1 gamma (human) IL-18 (human) hIL18 iboctadekin (human) interleukin-18 (human) PR:Q14653 An interferon regulatory factor 3 that is encoded in the genome of human. NCBI-Human-GeneID:3661 UniProtKB:Q14653 IRF-3 (human) hILF3 interferon regulatory factor 3 (human) interferon regulatory factor 3 (human) NCBI-Human-GeneID:3661 http://www.ncbi.nlm.nih.gov/gene/3661 PR:Q14676 A mediator of DNA damage checkpoint protein 1 that is encoded in the genome of human. HGNC:21163 NCBI-Human-GeneID:9656 Reactome:R-HSA-75231 UniProtKB:Q14676 mediator of DNA damage checkpoint protein 1 (human) nuclear factor with BRCT domains 1 (human) KIAA0170 MDC1 NFBD1 hMDC1 NCBI-Human-GeneID:9656 http://www.ncbi.nlm.nih.gov/gene/9656 PR:Q15109 An advanced glycosylation end product-specific receptor that is encoded in the genome of human. advanced glycosylation end product-specific receptor (human) PR:Q15116 A programmed cell death protein 1 that is encoded in the genome of human. NCBI-Human-GeneID:5133 UniProtKB:Q15116 CD279 (human) hPD-1 hPDCD1 programmed cell death protein 1 (human) NCBI-Human-GeneID:5133 http://www.ncbi.nlm.nih.gov/gene/5133 PR:Q15118 A [pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial that is encoded in the genome of human. HGNC:8809 PDK1 UniProtKB:Q15118 PDH kinase 1 (human) PDHK1 [pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial (human) pyruvate dehydrogenase kinase isoform 1 (human) hPDK1 PR:Q15418 A ribosomal protein S6 kinase alpha-1 that is encoded in the genome of human. HGNC:10430 UniProtKB:Q15428 90 kDa ribosomal protein S6 kinase 1 (human) MAP kinase-activated protein kinase 1a (human) MAPK-activated protein kinase 1a (human) MAPKAP kinase 1a (human) p90-RSK 1 (human) ribosomal protein S6 kinase alpha-1 (human) hRPS6KA1 PR:Q15759 A mitogen-activated protein kinase 11 that is encoded in the genome of human. HGNC:6873 NCBI-Human-GeneID:5600 UniProtKB:Q15759 MAP kinase 11 (human) MAP kinase p38 beta (human) mitogen-activated protein kinase 11 (human) mitogen-activated protein kinase p38 beta p38-2 (human) p38b (human) stress-activated protein kinase 2b (human) PRKM11 SAPK2 SAPK2B hMAPK11 NCBI-Human-GeneID:5600 http://www.ncbi.nlm.nih.gov/gene/26419 PR:Q16270 An insulin-like growth factor-binding protein 7 that is encoded in the genome of human. HGNC:5476 IGFBP7 UniProtKB:Q16270 insulin-like growth factor-binding protein 7 (human) IBP-7 (human) TAF (human) hIGFBP7 PR:Q16552 An interleukin-17A that is encoded in the genome of human. NCBI-Human-GeneID:3605 UniProtKB:Q16552 CTLA-8 (human) IL-17A (human) hIL17A interleukin-17A (human) NCBI-Human-GeneID:3605 https://www.ncbi.nlm.nih.gov/gene/3605 PR:Q16553 A lymphocyte antigen 6E that is encoded in the genome of human. NCBI-Human-GeneID:4061 PMID:32505227 PMID:32641482 PMID:32704094 UniProtKB:Q16553 Ly-6E (human) RIG-E (human) SCA-2 (human) hLy6E lymphocyte antigen 6E (human) lymphocyte antigen 6E (human) NCBI-Human-GeneID:4061 http://www.ncbi.nlm.nih.gov/gene/4061 PMID:32505227 Lymphocyte antigen 6 complex locus E (LY6E) has been shown to interfere with SARS-CoV-2 spike (S) protein-mediated membrane fusion. PMID:32641482 As shown in Fig. 4A, we found that ADAP2, GILT, and LY6E mRNAs were expressed at significantly higher levels in HepG2 cells. PMID:32704094 Here, we show that lymphocyte antigen 6 complex, locus E (LY6E) potently restricts infection by multiple CoVs, including SARS-CoV, SARS-CoV-2 and MERS-CoV. Mechanistic studies revealed that LY6E inhibits CoV entry into cells by interfering with spike protein-mediated membrane fusion. PR:Q16611 A Bcl-2 homologous antagonist/killer that is encoded in the genome of human. HGNC:949 NCBI-Human-GeneID:578 NCBI-Mouse-GeneID:12018 NCBI-Rat-GeneID:116502 UniProtKB:Q16611 Bcl-2 homologous antagonist/killer (human) Bcl-2-like protein 7 (human) Bcl2 homologous antagonist/killer (human) Bcl2-L-7 (human) apoptosis regulator BAK BAK BCL2L7 CDN1 hBAK1 NCBI-Human-GeneID:578 http://www.ncbi.nlm.nih.gov/gene/578 NCBI-Mouse-GeneID:12018 http://www.ncbi.nlm.nih.gov/gene/12018 NCBI-Rat-GeneID:116502 http://www.ncbi.nlm.nih.gov/gene/116502 PR:Q16665 A hypoxia-inducible factor 1-alpha that is encoded in the genome of human. NCBI-Human-GeneID:3091 UniProtKB:Q16665 HIF-1-alpha (human) hHIF1A hypoxia-inducible factor 1-alpha (human) NCBI-Human-GeneID:3091 http://www.ncbi.nlm.nih.gov/gene/3091 PR:Q16875 A 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 that is encoded in the genome of human. NCBI-Human-GeneID:5209 PMID:32697943 UniProtKB:Q16875 PFK/FBPase 3 (human) hPFKFB3 iPFK-2 (human) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (human) NCBI-Human-GeneID:5209 http://www.ncbi.nlm.nih.gov/gene/5209 PMID:32697943 To reduce the glycolytic rate of monocytes, we inhibited the enzyme 6-phospho- fructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), an allosteric activator of phosphofructokinase-1 (Breda et al., 2019), with 3-PO. This also resulted in decreased viral replication and ACE2 and IL-1b expression (Figures 2J and S3E). PR:Q17353 par-3 (worm) A protein that is a translation product of the par-3 gene in worm. Is predicted to enable phosphatidylinositol binding activity. Is involved in several processes, including cell adhesion; establishment of mitotic spindle orientation; and multicellular organism development. Located in P granule; basal part of cell; and cell cortex region. Is integral component of membrane. Is expressed in several structures, including AB; Psub1; excretory cell; hermaphrodite gonad; and vulval cell. Is an ortholog of human PARD3 (par-3 family cell polarity regulator). Is predicted to enable phosphatidylinositol binding activity. Is involved in several processes, including cell adhesion; establishment of mitotic spindle orientation; and multicellular organism development. Located in P granule; basal part of cell; and cell cortex region. Is integral component of membrane. Is expressed in several structures, including AB; Psub1; excretory cell; hermaphrodite gonad; and vulval cell. Is an ortholog of human PARD3 (par-3 family cell polarity regulator). par-3 encodes a PDZ domain-containing protein orthologous to mammalian atypical PKC isotype-specific interacting protein (ASIP) and Drosophila Bazooka; PAR-3 is required maternally for polarization of the zygote along the anterior-posterior (A-P) axis; PAR-3, PAR-6, and PKC-3 form a complex that localizes to the anterior cytoplasmic cortex of the one- and two-cell embryo; this localization is regulated spatially by PAR-2, which segregates to the posterior cortex. par-3 encodes a PDZ domain-containing protein orthologous to mammalian atypical PKC isotype-specific interacting protein (ASIP) and Drosophila Bazooka; PAR-3 is required maternally for polarization of the zygote along the anterior-posterior (A-P) axis; PAR-3, PAR-6, and PKC-3 form a complex that localizes to the anterior cytoplasmic cortex of the one- and two-cell embryo; this localization is regulated spatially by PAR-2, which segregates to the posterior cortex. UniProtKB:Q17353 http://www.wormbase.org/species/c_elegans/gene/WBGene00003918 SCRIB (worm) partitioning defective protein 3 (worm) F54E7.3 par-3 PAR3 (worm) Is predicted to enable phosphatidylinositol binding activity. Is involved in several processes, including cell adhesion; establishment of mitotic spindle orientation; and multicellular organism development. Located in P granule; basal part of cell; and cell cortex region. Is integral component of membrane. Is expressed in several structures, including AB; Psub1; excretory cell; hermaphrodite gonad; and vulval cell. Is an ortholog of human PARD3 (par-3 family cell polarity regulator). http://www.wormbase.org/species/c_elegans/gene/WBGene00003918 par-3 encodes a PDZ domain-containing protein orthologous to mammalian atypical PKC isotype-specific interacting protein (ASIP) and Drosophila Bazooka; PAR-3 is required maternally for polarization of the zygote along the anterior-posterior (A-P) axis; PAR-3, PAR-6, and PKC-3 form a complex that localizes to the anterior cytoplasmic cortex of the one- and two-cell embryo; this localization is regulated spatially by PAR-2, which segregates to the posterior cortex. http://www.wormbase.org/species/c_elegans/gene/WBGene00003918 PR:Q19266 A protein that is a translation product of the pkc-3 gene in worm. Enables protein domain specific binding activity and protein serine/threonine kinase activity. Is involved in several processes, including defense response to fungus; gonad development; and peptidyl-serine phosphorylation. Located in apical plasma membrane; cortical actin cytoskeleton; and cytosol. Is expressed in several structures, including Psub4; enteric muscle; hypodermis; pharyngeal-intestinal valve; and vulva. Human ortholog(s) of this gene are implicated in invasive ductal carcinoma and ovarian carcinoma. Is an ortholog of human PRKCI (protein kinase C iota) and PRKCZ (protein kinase C zeta). evidence Enables protein domain specific binding activity and protein serine/threonine kinase activity. Is involved in several processes, including defense response to fungus; gonad development; and peptidyl-serine phosphorylation. Located in apical plasma membrane; cortical actin cytoskeleton; and cytosol. Is expressed in several structures, including Psub4; enteric muscle; hypodermis; pharyngeal-intestinal valve; and vulva. Human ortholog(s) of this gene are implicated in invasive ductal carcinoma and ovarian carcinoma. Is an ortholog of human PRKCI (protein kinase C iota) and PRKCZ (protein kinase C zeta). evidence pkc-3 encodes an atypical protein kinase that lacks a DAG binding domain; during early embryonic development, pkc-3 plays an essential role in establishing anterior-posterior polarity; PKC-3 localizes to the anterior periphery of the one-cell embryo in a manner dependent upon the PAR-3 PDZ domain-containing protein with which PKC-3 physically interacts; PKC-3 also localizes to the outer, apical surfaces of cells. pkc-3 encodes an atypical protein kinase that lacks a DAG binding domain; during early embryonic development, pkc-3 plays an essential role in establishing anterior-posterior polarity; PKC-3 localizes to the anterior periphery of the one-cell embryo in a manner dependent upon the PAR-3 PDZ domain-containing protein with which PKC-3 physically interacts; PKC-3 also localizes to the outer, apical surfaces of cells. UniProtKB:Q19266 http://www.wormbase.org/species/c_elegans/gene/WBGene00004034 https://wormbase.org/species/c_elegans/protein/CE02604 aPKC3 (worm) atypical protein kinase C-3 (worm) pkc-3 (worm) protein kinase C-like 3 (worm) F09E5.1 aPKC pkc-3 aPKC 3 (worm) Enables protein domain specific binding activity and protein serine/threonine kinase activity. Is involved in several processes, including defense response to fungus; gonad development; and peptidyl-serine phosphorylation. Located in apical plasma membrane; cortical actin cytoskeleton; and cytosol. Is expressed in several structures, including Psub4; enteric muscle; hypodermis; pharyngeal-intestinal valve; and vulva. Human ortholog(s) of this gene are implicated in invasive ductal carcinoma and ovarian carcinoma. Is an ortholog of human PRKCI (protein kinase C iota) and PRKCZ (protein kinase C zeta). evidence http://www.wormbase.org/species/c_elegans/gene/WBGene00004034 pkc-3 encodes an atypical protein kinase that lacks a DAG binding domain; during early embryonic development, pkc-3 plays an essential role in establishing anterior-posterior polarity; PKC-3 localizes to the anterior periphery of the one-cell embryo in a manner dependent upon the PAR-3 PDZ domain-containing protein with which PKC-3 physically interacts; PKC-3 also localizes to the outer, apical surfaces of cells. http://www.wormbase.org/species/c_elegans/gene/WBGene00004034 PR:Q22038 A protein that is a translation product of the rho-1 gene in worm. UniProtKB:Q22038 WormBase:WBGene00004357 rho-1 Ras-like GTP-binding protein rhoA (worm) rho-1 (worm) Y51H4A.3 rhoa RHO1 (worm) WormBase:WBGene00004357 rho-1 http://www.wormbase.org/species/c_elegans/gene/WBGene00004357 PR:Q6MZP7 HGNC:25397 UniProtKB:Q6MZP7 CXC domain-containing protein 1 (human) protein lin-54 homolog (human) CXCDC1 KIAA2037 DREAM complex:A multisubunit complex formed by the assembly of p130 and p107 with their dimerization partner, E2F4/5, and a multi-vulva class-B core complex. hLIN54 DREAM complex:A multisubunit complex formed by the assembly of p130 and p107 with their dimerization partner, E2F4/5, and a multi-vulva class-B core complex. PMID:35922662 PR:Q7Z434 NCBI-Human-GeneID:57506 UniProtKB:Q7Z434 A mitochondrial antiviral-signaling protein that is encoded in the genome of human. MAVS (human) hMAVS mitochondrial antiviral-signaling protein (human) mitochondrial antiviral-signaling protein (human) NCBI-Human-GeneID:57506 http://www.ncbi.nlm.nih.gov/gene/57506 PR:Q80UV9 A transcription initiation factor TFIID subunit 1 that is encoded in the genome of mouse. MGI:1336878 OMA:Q80UV9 PMID:29212961 transcription initiation factor TFIID subunit 1 (mouse) mTAF1 OMA:Q80UV9 http://omabrowser.org/cgi-bin/gateway.pl?f=DisplayEntry&p2=orthologs&p1=Q80UV9 PMID:29212961 Maternal RNA/protein degradation and zygotic genome activation (ZGA), occurring during maternal-to-zygotic transition (MZT), are the first essential events for the development of pre-implantation embryos. Previously, we have shown the importance of the ubiquitin-proteasome system (UPS) for initiation of minor ZGA at the 1-cell stage of mouse embryos. As shown in Fig. 2, the delay in recruitment and phosphorylation of Pol II in transient MG132-treated 1-cell embryos are resultants of improper chromatin remodeling for Pol II recruitment. In general, UPS regulates gene expression and interacts with chromatin at multiple steps. Transcriptional activators cannot translocate into nucleus or bind to DNA due to the failure of degrading their repressive regulators; a large number of transcription factors and cofactors have been reported to be regulated by UPS, indicating that UPS-mediated proteolysis of those factors is inherently linked to the way they stimulate transcription. For example, in Caenorhabditis elegans, zinc-finger proteins OMA-1/2 bind to TBP-associated factor-4 (TAF-4), which is a component of the transcription factor-II D (TFIID) and pre-initiation complex of Pol II, sequestering TAF-4 into the cytoplasm during 1- and 2-cell stages. After the cell division, OMA-1/2 is degraded by UPS, TAF-4 is translocated into the nucleus, and is involved in TFIID-mediated transcriptional activation of the zygotic genome. Furthermore, many histone modification enzymes, which are related to transcriptional silencing and activation, such as histone deacetylases (HDACs), methyltransferases (HMTs), and demethyltransferases (HDMs) are regulated by ubiquitin-mediated proteasomal degradation. At present, the molecular mechanisms of UPS governing minor ZGA in 1-cell embryos remain to be determined. PR:Q8N726 A CDKN2A gene translation product (human), isoforms ARF and smARF. UniProtKB:Q8N726 doi:10.14952/SEIKAGAKU.2016.880207 tumor suppressor ARF/smARF (human) cyclin-dependent kinase inhibitor 2A isoforms 4/6 (human) hCDKN2A/iso:[ARF/smARF] UniProtKB:Q8N726 Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Plays a role in inhibiting ribosome biogenesis, perhaps by binding to the nucleolar localization sequence of transcription termination factor TTF1, and thereby preventing nucleolar localization of TTF1 (By similarity). Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland developmen PR:Q8N726-1 A tumor suppressor ARF that is encoded in the genome of human. UniProtKB:Q8N726-1 doi:10.14952/SEIKAGAKU.2016.880207 CDKN2A isoform 4 (human) cyclin-dependent kinase inhibitor 2A isoform 4 (human) cyclin-dependent kinase inhibitor 2A isoform p19ARF (human) tumor suppressor ARF (human) hCDKN2A/iso:ARF UniProtKB:Q8N726-1 Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Plays a role in inhibiting ribosome biogenesis, perhaps by binding to the nucleolar localization sequence of transcription termination factor TTF1, and thereby preventing nucleolar localization of TTF1 (By similarity). Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development PR:Q8N884 A protein MB21D1 that is encoded in the genome of human. HGNC:21367 NCBI Gene:115004 UniProtKB:Q8N884 2'3'-cGAMP synthase (human) Mab-21 domain-containing protein 1 (human) cGAMP synthase (human) cGAS (human) cyclic GMP-AMP synthase (human) h-cGAS C6orf150 CGAS MB21D1 hCGAS PR:Q8NHX9 A two pore calcium channel protein 2 that is encoded in the genome of human. NCBI-Human-GeneID:219931 PMID:32221306 UniProtKB:Q8NHX9 hTPCN2 voltage-dependent calcium channel protein TPC2 (human) two pore calcium channel protein 2 (human) NCBI-Human-GeneID:219931 https://www.ncbi.nlm.nih.gov/gene/219931 PMID:32221306 Here, using SARS-CoV-2 S protein pseudovirus system, we confirm that human angiotensin converting enzyme 2 (hACE2) is the receptor for SARS-CoV-2, find that SARS-CoV-2 enters 293/hACE2 cells mainly through endocytosis, that PIKfyve, TPC2, and cathepsin L are critical for entry, and that SARS-CoV-2 S protein is less stable than SARS-CoV S. While blocking TPC2 activity by tetrandrine, an inhibitor for TPC2, decreased entry of SARS-CoV-2 S pseudovirions (Fig. 3f), treatment of cells with 130, a TRPML1 inhibitor, had no effect (Supplementary Fig. 1), indicating that TPC2, not TRPML1, is important for SARS-CoV-2 entry. PR:Q92985 An interferon regulatory factor 7 that is encoded in the genome of human. NCBI-Human-GeneID:3665 UniProtKB:Q92985 IRF-7 (human) hILF7 interferon regulatory factor 7 (human) NCBI-Human-GeneID:3665 http://www.ncbi.nlm.nih.gov/gene/3665 PR:Q93009 A protein that is a translation product of the human USP7 gene or a 1:1 ortholog thereof. NCBI-Human-GeneID:7874 NCBI-Mouse-GeneID:252870 NCBI-Rat-GeneID:360471 USP7 ubiquitin specific peptidase 7 ubiquitin carboxyl-terminal hydrolase 7 (human) NCBI-Human-GeneID:7874 http://www.ncbi.nlm.nih.gov/gene/7874 NCBI-Mouse-GeneID:252870 https://www.ncbi.nlm.nih.gov/gene/252870 NCBI-Rat-GeneID:360471 https://www.ncbi.nlm.nih.gov/gene/360471 PR:Q94131 A protein that is a translation product of the pie-1 gene in worm. Predicted to enable mRNA 3'-UTR binding activity. Involved in several processes, including embryonic pattern specification; formation of primary germ layer; and negative regulation of nitrogen compound metabolic process. Located in several cellular components, including P granule; centrosome; and cytosol. Expressed in germ line; head muscle; and nerve ring. Predicted to enable mRNA 3'-UTR binding activity. Involved in several processes, including embryonic pattern specification; formation of primary germ layer; and negative regulation of nitrogen compound metabolic process. Located in several cellular components, including P granule; centrosome; and cytosol. Expressed in germ line; head muscle; and nerve ring. pie-1 encodes a C-x8-C-x5-C-x3-H-type zinc-finger protein; maternally provided PIE-1 is essential for germline cell fate determination, as it functions as a repressor of RNA polymerase II-dependent gene expression in the developing germ line; PIE-1 localization, initially uniform and then concentrated in the posterior germ cell lineages, is regulated by other maternally supplied gene products including PAR-1, MEX-5, and MEX-6. pie-1 encodes a C-x8-C-x5-C-x3-H-type zinc-finger protein; maternally provided PIE-1 is essential for germline cell fate determination, as it functions as a repressor of RNA polymerase II-dependent gene expression in the developing germ line; PIE-1 localization, initially uniform and then concentrated in the posterior germ cell lineages, is regulated by other maternally supplied gene products including PAR-1, MEX-5, and MEX-6. PMID:30042214 UniProtKB:Q94131 WormBase:WBGene00004027 pharynx and intestine in excess protein 1 (worm) pie-1 (worm) PIE1 (worm) Predicted to enable mRNA 3'-UTR binding activity. Involved in several processes, including embryonic pattern specification; formation of primary germ layer; and negative regulation of nitrogen compound metabolic process. Located in several cellular components, including P granule; centrosome; and cytosol. Expressed in germ line; head muscle; and nerve ring. https://wormbase.org//species/c_elegans/gene/WBGene00004027 pie-1 encodes a C-x8-C-x5-C-x3-H-type zinc-finger protein; maternally provided PIE-1 is essential for germline cell fate determination, as it functions as a repressor of RNA polymerase II-dependent gene expression in the developing germ line; PIE-1 localization, initially uniform and then concentrated in the posterior germ cell lineages, is regulated by other maternally supplied gene products including PAR-1, MEX-5, and MEX-6. https://wormbase.org//species/c_elegans/gene/WBGene00004027 PMID:30042214 Our findings suggest that both proteins interconvert between fast-diffusing and slow-diffusing states on timescales that are much shorter (seconds) than the timescale of gradient formation (minutes). The kinetics of diffusion-state switching are strongly polarized along the anterior/posterior (A/P) axis by the PAR polarity system such that fast-diffusing MEX-5 and PIE-1 particles are approximately symmetrically distributed, whereas slow-diffusing particles are highly enriched in the anterior and posterior cytoplasm, respectively. PR:Q96EB6 An NAD-dependent protein deacetylase sirtuin-1 that is encoded in the genome of human. HGNC:14929 UniProtKB:Q96EB6 NAD-dependent protein deacetylase sirtuin-1 (human) SIR2-like protein 1 (human) hSIR2 regulatory protein SIR2 homolog 1 (human) hSIRT1 PR:Q96P20 A NACHT, LRR and PYD domains-containing protein 3 that is encoded in the genome of human. NLRP3 is a inflammasome component NCBI-Human-GeneID:114548 UniProtKB:Q96P20 CLR1.1 (human) PYRIN-containing APAF1-like protein 1 (human) angiotensin/vasopressin receptor AII/AVP-like (human) hNLRP3 NACHT, LRR and PYD domains-containing protein 3 (human) NCBI-Human-GeneID:114548 http://www.ncbi.nlm.nih.gov/gene/114548 PR:Q9BYF1 An angiotensin-converting enzyme 2 that is encoded in the genome of human. NCBI-Human-GeneID:59272 PMID:32142651 PMID:32327758 PMID:32404436 PMID:32413319 PMID:32629875 PMID:32651579 UniProtKB:Q9BYF1 ACE-related carboxypeptidase (human) ACE2 (human) hACE2 angiotensin-converting enzyme 2 (human) NCBI-Human-GeneID:59272 http://www.ncbi.nlm.nih.gov/gene/59272 PMID:32327758 Consistently with independent studies, ACE2 was expressed in cells from multiple tissues, including airways, cornea, esophagus, ileum, colon, liver, gallbladder, heart, kidney and testis (Fig. 1a; first column). Cells from the respiratory tree, cornea, esophagus, ileum, colon, gallbladder and common bile duct expressed both genes in the same cell (Fig. 1a; third column). We found that, despite a low level of expression overall, ACE2 was expressed in multiple epithelial cell types across the airway, as well as in alveolar epithelial type II cells in the parenchyma, consistently with previous studies. Notably, nasal epithelial cells, including two previously described clusters of goblet cells and one cluster of ciliated cells, show the highest expression among all investigated cells in the respiratory tree (Fig. 1b). PMID:32404436 Both ACE2 and TMPRSS2 are expressed highly in the gastrointestinal (GI) tract, in particular by intestinal epithelial cells (IECs), the predominant target cells for many human enteric viruses. ACE2 expression is substantially higher in the small intestine than all the other organs including the lung in both humans and mice (Fig. S1A-B). PMID:32413319 We identify ACE2 and TMPRSS2 co-expressing cells within lung type II pneumocytes, ileal absorptive enterocytes, and nasal goblet secretory cells. Here, we found that ACE2 and TMPRSS2 were primarily expressed within type II pneumocytes and ciliated cells, in line with our analysis of the NHP-derived cells (Figures 1 and 2A, 2B). In an additional dataset consisting of endoscopic biopsies from the terminal ileum of a human pediatric cohort (n = 13 donors, ranging in age from 10 to 18 years old), collected with 10X 30 v2, we confirmed a large abundance of ACE2+ cells with selective expression within absorptive enterocytes (29.7% ACE2+, FDR-adjusted p = 2.46E-100) (Figures 3D and 3E; Table S5; STAR Methods). We observed significant enrichment of ACE2 expression in apical epithelial cells and, to a lesser extent, ciliated cells compared with all cell types recovered from surgically resected mucosa (1% of apical epithelial cells, FDR-adjusted p = 4.55E-6, n.s. in ciliated cells) (Figure 4B; Table S6). These findings are aligned with concurrent work by the HCA Lung Biological Network on human nasal scRNA-seq data, which identified nasal secretory cells to be enriched for ACE2 and TMPRSS2 expression (Sungnak et al., 2020). PMID:32629875 Angiotensin converting enzyme 2 (ACE2), the receptor for SARS-CoV-2 and other coronaviruses, is a transmembrane protein expressed by lung alveolar epithelial cells, enterocytes, and vascular endothelial cells, whose physiologic role is to induce the maturation of angiotensin I to generate angiotensin, a peptide hormone that controls vasoconstriction and blood pressure. This is consistent with immunohistochemical detection of the viral nucleocapsid antigen in the epithelium of the stomach, duodenum, and rectum of a COVID-19 patient where ACE2 protein was also detected. However, cardiomyocytes are potential targets of SARS-CoV-2 infection as they express ACE2. PMID:32651579 ACE2 has high expression in cardiovascular tissue, including cardiac myocytes, fibroblasts, endothelial cells, and smooth-muscle cells in support of a possible mechanism of direct viral injury. In addition, ACE2 expression has been reported in the endocrine pancreas, albeit inconsistently. This raises the possibility that direct binding of SARS-CoV-2 to ACE2 on beta-cells might contribute to insulin deficiency and hyperglycemia, as has been shown previously for infection with SARS-CoV179. Nasal epithelial cells display the highest expression of ACE2 (the receptor for SARS-CoV-2) in the respiratory tree; this may account for the symptoms of altered sense of taste or smell frequently reported retrospectively in the majority of outpatients with COVID-19. PR:Q9GZQ8 A microtubule-associated proteins 1A/1B light chain 3B that is encoded in the genome of human. HGNC:13352 NCBI Gene:81631 UniProtKB:Q9GZQ8 MAP1 light chain 3-like protein 2 (human) MAP1A/MAP1B LC3 B (human) MAP1A/MAP1B light chain 3 B (human) autophagy-related protein LC3 B (human) autophagy-related ubiquitin-like modifier LC3 B (human) microtubule-associated protein 1 light chain 3 beta (human) microtubule-associated proteins 1A/1B light chain 3B (human) MAP1ALC3 hMAP1LC3B PR:Q9H5V9 A STING ER exit protein that is encoded in the genome of human. HGNC:26239 NCBI Gene:63932 UniProtKB:Q9H5V9 STEEP (human) STING ER exit protein (human) CXorf56 hSTEEP1 PR:Q9H633 A ribonuclease P protein subunit p21 that is encoded in the genome of human. HGNC:21300 RNaseP protein p21 (human) ribonuclease P protein subunit p21 (human) ribonuclease P/MRP 21 kDa subunit (human) ribonucleoprotein V (human) hRPP21 PR:Q9NAN2 par-6 (worm) A protein that is a translation product of the par-6 gene in worm. UniProtKB:Q17353 par-6 (worm) partitioning defective protein 6 (worm) T26E3.3 par-6 PAR6 (worm) PR:Q9NPF8 An Arf-GAP with dual PH domain-containing protein 2 that is encoded in the genome of human. UniProtKB:Q9NPF8 Arf-GAP with dual PH domain-containing protein 2 (human) PR:Q9NR96 A Toll-like receptor 9 that is encoded in the genome of human. NCBI-Human-GeneID:54106 PMID:31623280 UniProtKB:Q9NR96 CD289 (human) Toll-like receptor 9 (human) UNQ5798/PRO19605 hTLR9 Toll-like receptor 9 (human) NCBI-Human-GeneID:54106 http://www.ncbi.nlm.nih.gov/gene/54106 PMID:31623280 Mitochondrial DAMPs (MTDs) activate pattern recognition receptors (PRRs), such as Toll-like receptor (TLR)9. After binding to TLR9, mitochondrial DAMPs trigger numerous downstream pathways, including nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), the nucleotide binding oligomerization domain (NOD)-like receptor family, pyrin domain containing 3 (NLRP3), and interferon regulatory factor-dependent type 1 to promote inflammation. PR:Q9NR97-2 A Toll-like receptor 8 that is encoded in the genome of human. NCBI-Human-GeneID:51311 UniProtKB:Q9NR97 CD288 (human) UNQ249/PRO286 hTLR8 Toll-like receptor 8 (human) NCBI-Human-GeneID:51311 https://www.ncbi.nlm.nih.gov/gene/51311/ PR:Q9NRS4 A transmembrane protease serine 4 that is encoded in the genome of human. NCBI-Human-GeneID:56649 PMID:32404436 UniProtKB:Q9NRS4 MT-SP2 (human) channel-activating protease 2 (human) hTMPRSS4 transmembrane protease serine 4 (human) NCBI-Human-GeneID:56649 https://www.ncbi.nlm.nih.gov/gene/56649 PMID:32404436 Here, we present evidence that SARS-CoV-2 infects human mature enterocytes from the apical surface and triggers epithelial cell fusion. TMPRSS2 and TMPRSS4 serine proteases mediate this process by inducing cleavage of the S protein and enhancing membrane fusion. PR:Q9NYK1 A Toll-like receptor 7 that is encoded in the genome of human. NCBI-Human-GeneID:54106 UniProtKB:Q9NYK1 UNQ248/PRO285 (human) hTLR7 Toll-like receptor 7 (human) NCBI-Human-GeneID:54106 http://www.ncbi.nlm.nih.gov/gene/54106 PR:Q9P0J1 A [pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial that is encoded in the genome of human. HGNC:9279 NCBI-Human-GeneID:54704 UniProtKB:Q9P0J1 PDP1 (human) [pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (human) PDP PDPC 1 (human) PPM2C hPDP1 NCBI-Human-GeneID:54704 http://www.ncbi.nlm.nih.gov/gene/54704 PR:Q9P2J9 A [pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial that is encoded in the genome of human. HGNC:30263 NCBI-Human-GeneID:57546 KIAA1348 PDPC 2 (human) pyruvate dehydrogenase phosphatase catalytic subunit 2 (human) hPDP2 NCBI-Human-GeneID:57546 http://www.ncbi.nlm.nih.gov/gene/57546 PR:Q9UEF7 A klotho that is encoded in the genome of human. Ensembl:ENSG00000133116 HGNC:6344 NCBI Gene:9365 UniProtKB:Q9UEF7 KL klotho (human) hKL NCBI Gene:9365 This gene encodes a type-I membrane protein that is related to beta-glucosidases. Reduced production of this protein has been observed in patients with chronic renal failure (CRF), and this may be one of the factors underlying the degenerative processes (e.g., arteriosclerosis, osteoporosis, and skin atrophy) seen in CRF. Also, mutations within this protein have been associated with ageing and bone loss. [provided by RefSeq, Jul 2008] PR:Q9UHD2 A serine/threonine-protein kinase TBK1 that is encoded in the genome of human. NCBI-Human-GeneID:29110 UniProtKB:Q9UHD2 NF-kappa-B-activating kinase (human) TANK-binding kinase 1 (human) hTBK1 serine/threonine-protein kinase TBK1 (human) serine/threonine-protein kinase TBK1 (human) NCBI-Human-GeneID:29110 http://www.ncbi.nlm.nih.gov/gene/29110 PR:Q9ULZ3 An apoptosis-associated speck-like protein containing a CARD that is encoded in the genome of human. NCBI-Human-GeneID:29108 UniProtKB:Q9ULZ3 Caspase Recruitment Domain-Containing Protein 5 PYD and CARD domain-containing protein (human) apoptosis-associated speck-like protein containing a CARD (human) caspase recruitment domain-containing protein 5 (human) hASC hPYCARD apoptosis-associated speck-like protein containing a CARD (human) NCBI-Human-GeneID:29108 https://www.ncbi.nlm.nih.gov/gene/29108 PR:Q9XUB2 A protein that is a translation product of the mex-5 gene in worm. Enables RNA binding activity; protein domain specific binding activity; and protein kinase binding activity. Involved in regulation of protein localization. Located in P granule and centrosome. Expressed in germ line; head muscle; head neurons; intestine; and somatic nervous system. Is an ortholog of human ZFP36L1 (ZFP36 ring finger protein like 1). Enables RNA binding activity; protein domain specific binding activity; and protein kinase binding activity. Involved in regulation of protein localization. Located in P granule and centrosome. Expressed in germ line; head muscle; head neurons; intestine; and somatic nervous system. Is an ortholog of human ZFP36L1 (ZFP36 ring finger protein like 1). mex-5 encodes a novel protein that contains two CCCH zinc finger motifs; maternally provided MEX-5, which functions partly redundantly with the highly similar CCCH finger protein MEX-6, is essential for transducing polarity cues and establishing soma/germline asymmetry in the early embryo; in regulating soma/germline asymmetry, MEX-5 interacts with, and activates, the SOCS-box protein ZIF-1, which functions as part of an E3 ubiquitin ligase complex that degrades germ plasm proteins in somatic blastomeres; accordingly, ectopic expression of MEX-5 throughout the early embryo results in reduced expression of germline proteins in germline blastomeres; MEX-5 activity is regulated in vivo by PLK-1 and PLK-2, which presumably bind and phosphorylate MBK-2-primed MEX-5; MEX-5 is a cytoplasmic protein expressed at uniform levels in oocytes and newly fertilized eggs; from the 1-cell to 4-cell stages of embryogenesis, MEX-5 expression is dynamic, with highest levels seen in the anterior AB blastomere and, for a time, its daughters, the anterior portion of the P1 blastomere, P1 centrosomes (both, then posterior only), and the EMS and C blastomeres; the asymmetric distribution of MEX-5 in early embryos depends upon a phosphorylation/dephosphorylation cycle by the PAR-1 kinase and PP2A phosphatases including LET-92, that regulate MEX-5's association with slow- or fast-diffusing RNA-containing complexes. mex-5 encodes a novel protein that contains two CCCH zinc finger motifs; maternally provided MEX-5, which functions partly redundantly with the highly similar CCCH finger protein MEX-6, is essential for transducing polarity cues and establishing soma/germline asymmetry in the early embryo; in regulating soma/germline asymmetry, MEX-5 interacts with, and activates, the SOCS-box protein ZIF-1, which functions as part of an E3 ubiquitin ligase complex that degrades germ plasm proteins in somatic blastomeres; accordingly, ectopic expression of MEX-5 throughout the early embryo results in reduced expression of germline proteins in germline blastomeres; MEX-5 activity is regulated in vivo by PLK-1 and PLK-2, which presumably bind and phosphorylate MBK-2-primed MEX-5; MEX-5 is a cytoplasmic protein expressed at uniform levels in oocytes and newly fertilized eggs; from the 1-cell to 4-cell stages of embryogenesis, MEX-5 expression is dynamic, with highest levels seen in the anterior AB blastomere and, for a time, its daughters, the anterior portion of the P1 blastomere, P1 centrosomes (both, then posterior only), and the EMS and C blastomeres; the asymmetric distribution of MEX-5 in early embryos depends upon a phosphorylation/dephosphorylation cycle by the PAR-1 kinase and PP2A phosphatases including LET-92, that regulate MEX-5's association with slow- or fast-diffusing RNA-containing complexes. PMID:10882103 PMID:21925318 PMID:30042214 UniProtKB:Q9XUB2 https://wormbase.org/species/c_elegans/gene/WBGene00003230 mex-5 (worm) zinc finger protein mex-5 (worm) MEX5 (worm) Enables RNA binding activity; protein domain specific binding activity; and protein kinase binding activity. Involved in regulation of protein localization. Located in P granule and centrosome. Expressed in germ line; head muscle; head neurons; intestine; and somatic nervous system. Is an ortholog of human ZFP36L1 (ZFP36 ring finger protein like 1). http://www.wormbase.org/species/c_elegans/gene/WBGene00003230 mex-5 encodes a novel protein that contains two CCCH zinc finger motifs; maternally provided MEX-5, which functions partly redundantly with the highly similar CCCH finger protein MEX-6, is essential for transducing polarity cues and establishing soma/germline asymmetry in the early embryo; in regulating soma/germline asymmetry, MEX-5 interacts with, and activates, the SOCS-box protein ZIF-1, which functions as part of an E3 ubiquitin ligase complex that degrades germ plasm proteins in somatic blastomeres; accordingly, ectopic expression of MEX-5 throughout the early embryo results in reduced expression of germline proteins in germline blastomeres; MEX-5 activity is regulated in vivo by PLK-1 and PLK-2, which presumably bind and phosphorylate MBK-2-primed MEX-5; MEX-5 is a cytoplasmic protein expressed at uniform levels in oocytes and newly fertilized eggs; from the 1-cell to 4-cell stages of embryogenesis, MEX-5 expression is dynamic, with highest levels seen in the anterior AB blastomere and, for a time, its daughters, the anterior portion of the P1 blastomere, P1 centrosomes (both, then posterior only), and the EMS and C blastomeres; the asymmetric distribution of MEX-5 in early embryos depends upon a phosphorylation/dephosphorylation cycle by the PAR-1 kinase and PP2A phosphatases including LET-92, that regulate MEX-5's association with slow- or fast-diffusing RNA-containing complexes. http://www.wormbase.org/species/c_elegans/gene/WBGene00003230 PMID:21925318 Protein concentration gradients encode spatial information across cells and tissues and often depend on spatially localized protein synthesis. Here, we report that a different mechanism underlies the MEX-5 gradient. MEX-5 is an RNA-binding protein that becomes distributed in a cytoplasmic gradient along the anterior-to-posterior axis of the one-cell C. elegans embryo. We demonstrate that the MEX-5 gradient is a direct consequence of an underlying gradient in MEX-5 diffusivity. The MEX-5 diffusion gradient arises when the PAR-1 kinase stimulates the release of MEX-5 from slow-diffusive, RNA-containing complexes in the posterior cytoplasm. PAR-1 directly phosphorylates MEX-5 and is antagonized by the spatially uniform phosphatase PP2 PMID:30042214 Our findings suggest that both proteins interconvert between fast-diffusing and slow-diffusing states on timescales that are much shorter (seconds) than the timescale of gradient formation (minutes). The kinetics of diffusion-state switching are strongly polarized along the anterior/posterior (A/P) axis by the PAR polarity system such that fast-diffusing MEX-5 and PIE-1 particles are approximately symmetrically distributed, whereas slow-diffusing particles are highly enriched in the anterior and posterior cytoplasm, respectively. PR:Q9Y294 A histone chaperone ASF1A that is encoded in the genome of human. ASF1 CIA (human) HGNC:20995 NCBI-Human-GeneID:25842 UniProtKB:Q9Y294 CCG1-interacting factor A (human) anti-silencing function protein 1 homolog A (human) hAsf1a hCIA histone chaperone ASF1A CGI-98 HSPC146 hAsf1 hASF1A NCBI-Human-GeneID:25842 http://www.ncbi.nlm.nih.gov/gene/25842 PR:Q9Y2I7 A 1-phosphatidylinositol 3-phosphate 5-kinase that is encoded in the genome of human. NCBI-Human-GeneID:200576 PMID:32221306 UniProtKB:Q9Y2I7 KIAA0981 PIKfyve (human) PIP5K3 hPIKFYVE serine-protein kinase PIKFYVE (human) 1-phosphatidylinositol 3-phosphate 5-kinase (human) NCBI-Human-GeneID:200576 https://www.ncbi.nlm.nih.gov/gene/200576 PMID:32221306 Here, using SARS-CoV-2 S protein pseudovirus system, we confirm that human angiotensin converting enzyme 2 (hACE2) is the receptor for SARS-CoV-2, find that SARS-CoV-2 enters 293/hACE2 cells mainly through endocytosis, that PIKfyve, TPC2, and cathepsin L are critical for entry, and that SARS-CoV-2 S protein is less stable than SARS-CoV S. PR:Q9Y6K9 An NF-kappa-B essential modulator that is encoded in the genome of human. HGNC:5961 I-kappa-B kinase subunit gamma (human) IKK-gamma (human) NF-kappa-B essential modulator (human) NEMO inhibitor of nuclear factor kappa-B kinase subunit gamma (human) hIKBKG REX:0000173 The spreading or scattering of a gaseous or liquid material. diffusion RO:0002577 SO:0000001 region A sequence_feature with an extent greater than zero. A nucleotide region is composed of bases and a polypeptide region is composed of amino acids. primary structure of sequence macromolecule sequence region SO:0000127 A gene that is silenced. silenced_gene SO:0000149 contig A contiguous sequence derived from sequence assembly. Has no gaps, but may contain N's from unavailable bases. contig SO:0000235 TF_binding_site A DNA site where a transcription factor binds. TF_binding_site SO:0000276 miRNA Small, ~22-nt, RNA molecule that is the endogenous transcript of a miRNA gene (or the product of other non coding RNA genes. Micro RNAs are produced from precursor molecules (SO:0001244) that can form local hairpin structures, which ordinarily are processed (usually via the Dicer pathway) such that a single miRNA molecule accumulates from one arm of a hairpin precursor molecule. Micro RNAs may trigger the cleavage of their target molecules or act as translational repressors. miRNA SO:0000353 sequence_assembly A sequence of nucleotides that has been algorithmically derived from an alignment of two or more different sequences. sequence_assembly SO:0000646 A small RNA molecule that is the product of a longer exogenous or endogenous dsRNA, which is either a bimolecular duplex or very long hairpin, processed (via the Dicer pathway) such that numerous siRNAs accumulate from both strands of the dsRNA. siRNAs trigger the cleavage of their target molecules. small interfering rna siRNA SO:0000673 An RNA synthesized on a DNA or RNA template by an RNA polymerase. transcript transcript SO:0000988 SO:0001248 assembly A region of the genome of known length that is composed by ordering and aligning two or more different regions. assembly SO:0001410 experimental_feature A region which is the result of some arbitrary experimental procedure. The procedure may be carried out with biological material or inside a computer. experimental_feature SO:0002031 A short hairpin RNA (shRNA) is an RNA transcript that makes a tight hairpin turn that can be used to silence target gene expression via RNA interference. Wikipedia:Small_hairpin_RNA short hairpin RNA small hairpin RNA shRNA SO:0005836 regulatory_region A region of sequence that is involved in the control of a biological process. regulatory_region SYMP:0000016 Confusion is a neurological and physiological symptom characterized by a disturbance of consciousness characterized by inability to engage in orderly thought or by lack of power to distinguish, choose, or act decisively. confusion SYMP:0000020 Dehydration is a nutrition, metabolism, and development symptom characterized by an abnormal depletion of body fluids. dehydration SYMP:0000021 A neurological and physiological symptom that is characterized by a mental disturbance characterized by confusion, disordered speech, and hallucinations. delirium SYMP:0000022 A neurological and physiological symptom that is characterized by a chronic feeling of emptiness, sadness, or inability to feel pleasure that may appear to happen for no clear reason. Additionally one may experience feelings of hopelessness, pessimism, irritability, frustration, or restlessness, guilt, worthlessness and thoughts of death or suicide. symptoms depression SYMP:0000039 Enteritis is a digestive system symptom involving the inflammation of the small intestines and especially of the human ileum. enteritis SYMP:0000040 A urinary system symptom characterized by the presence of blood or blood cells in the urine. haematuria hematuria SYMP:0000089 Meningoencephalitis is a nervous system symptom characterized as an inflammation of the brain and meninges. meningoencephalitis SYMP:0000156 Thirst is a general symptom characterized by a sensation of dryness in the mouth and throat associated with a desire for liquids. 口渇 thirst SYMP:0000226 A cardiac fibrillation consisting of a very rapid uncoordinated contractions of the atria of the heart resulting in a lack of synchronism between heartbeat and pulse beat. atrial fibrillation SYMP:0000260 dry mouth SYMP:0000287 Arrhythmia is a cardiovascular system symptom consisting of an alteration in rhythm of the heartbeat either in time or force. arrhythmia SYMP:0000313 SYMP:0000337 night sweats SYMP:0000399 A dizziness that is characterized by a specific type of dizziness, a major symptom of a balance disorder. It is the sensation of spinning or swaying while the body is stationary with respect to the surroundings. vertigo SYMP:0000402 A nutrition, metabolism, and development symptom that is characterized by a general physical wasting and malnutrition usually associated with chronic disease. general physical wasting and malnutrition cachexia SYMP:0000410 A neurological and physiological symptom that is characterized by a chronic feeling of emptiness, sadness, or inability to feel pleasure that may appear to happen for no clear reason. Additionally one may experience feelings of hopelessness, pessimism, irritability, frustration, or restlessness, guilt, worthlessness and thoughts of death or suicide. neurological and physiological symptom SYMP:0000449 Cardiogenic shock (CS) is a medical emergency resulting from inadequate blood flow due to the dysfunction of the ventricles of the heart. Cardiogenic shock (CS) is a medical emergency resulting from inadequate blood flow due to the dysfunction of the ventricles of the heart. cardiogenic shock Cardiogenic shock (CS) is a medical emergency resulting from inadequate blood flow due to the dysfunction of the ventricles of the heart. https://en.wikipedia.org/wiki/Cardiogenic_shock SYMP:0000450 A cardiovascular system symptom that is characterized as a state of profound depression of the vital processes of the body that is characterized by pallor, rapid but weak pulse, rapid and shallow respiration, reduced total blood volume, and low blood pressure and that is caused usually by severe especially crushing injuries, hemorrhage, burns, or major surgery. shock SYMP:0000451 septic shock SYMP:0000458 Nausea is a digestive system symptom characterized by an uneasy or unsettled feeling in the stomach together with an urge to vomit. nausea SYMP:0000459 ICD9CM_2005:787 UMLS_CUI:C0159058 UMLS_ICD9CM_2005_AUI:A0284224 digestive system symptom SYMP:0000462 A symptom is a perceived change in function, sensation, loss, disturbance or appearance reported by a patient indicative of a disease. https://link.springer.com/chapter/10.1007/978-1-4615-4789-1_5 https://www.merriam-webster.com/dictionary/symptom https://www.nature.com/subjects/signs-and-symptoms symptom SYMP:0000482 alteration of consciousness SYMP:0000486 urinary system symptom SYMP:0000487 A skin and integumentary tissue symptom characterized as an eruption on the body typically with little or no elevation above the surface. erythema rubor skin rash rash SYMP:0000504 Headache is a pain characterized by a pain in the head. headache SYMP:0000523 Anorexia is a nutrition, metabolism, and development symptom characterized by a loss of appetite especially when prolonged. anorexia SYMP:0000538 A skin and integumentary tissue symptom characterized as an abnormal excess accumulation of serous fluid in connective tissue or in a serous cavity edema SYMP:0000551 taste alteration disturbances of sensation of smell and taste SYMP:0000563 frequent urination urinary frequency SYMP:0000565 A urinary system symptom that is characterized by the excessive secretion of urine. polyuria SYMP:0000570 Diarrhea is a feces and droppng symptom involving the abnormally frequent intestinal evacuations with more or less fluid stools. diarrhea SYMP:0000610 Dizziness is a neurological and physiological symptom characterized by a sensation of unsteadiness accompanied by a feeling of movement within the head. dizziness SYMP:0000613 Fever is a neurological and physiological symptom characterized by a rise of body temperature above the normal whether a natural response (as to infection) or artificially induced for therapeutic reasons. fever SYMP:0000614 Cough is a respiratory system and chest symptom characterized by an explosive expulsion of air from the lungs acting as a protective mechanism to clear the air passages or as a symptom of pulmonary disturbance. [database_cross_reference: URL:http://www2.merriam-webster.com/cgi-bin/mwmednlm?book=Medical&va=cough] cough SYMP:0000686 SYMP:0000692 low blood pressure SYMP:0000716 swelling symptom SYMP:0000718 loss of consciousness SYMP:0000734 Stroke is a nervous system symptom characterized by a sudden diminution or loss of consciousness, sensation, and voluntary motion caused by rupture or obstruction (as by a clot) of a blood vessel of the brain. stroke SYMP:0000827 A tachycardia that is associated with the generation of improper electrical impulses within the ventricles, characterized by an electrocardiogram showing a rate of greater than 120 BPM and three or more wide QRS complexes in a row. ventricular tachycardia SYMP:0000881 Mild fever is a fever that occurs in a mild form. mild fever SYMP:0000882 High fever is a fever that involved an elevated temperature. high fever SYMP:0000899 A cardiac fibrillation associated with quivering of the lower chambers of the heart, preventing blood from being pumped and causing cardiac arrest. ventricular fibrillation SYMP:0019145 Vomiting is a digestive system symptom characterized by throwing up the stomach contents. vomiting SYMP:0019153 Dyspnea is a respiratory abnormality characterized by difficult or labored respiration. Dyspnea shortness of breath SYMP:0019161 Muscle pain is a pain characterized by pain in one or more muscles. myalgia muscle pain SYMP:0019168 Pneumonia is a pneumonitis characterized as an inflammatory illness of the lung resulting from a variety of causes including infection with bacteria, viruses, fungi, or parasites, and chemical or physical injury to the lungs. Its cause may also be officially described as idiopathic, that is, unknown, when infectious causes have been excluded. pneumonia SYMP:0019169 SYMP:0019177 Fatigue is a neurological and physiological symptom characterized by a weariness or exhaustion from labor, exertion, or stress. fatigue TXPO:0005185 A recombinant chimeric, mouse-human monoclonal antibody directed against tumor necrosis factor alpha (TNF-alpha), a protein involved in inflammation, cell survival, and apoptosis. Infliximab may be pro- apoptotic or anti-apoptotic, depending on cell type. (https://www.ebi.ac.uk/ols/ontologies/ncit/terms?iri=http%3A%2F%2Fpurl.obolibrary.org%2Fobo%2FNCIT_C1789) DrugBank:DB00065 PMID:33753421 http://purl.obolibrary.org/obo/DRON_00012887 infliximab HOIP_0005185 PMID:33753421 For the individual anti-TNF-treated patient, lower rates of seroconversion and reduced anti-SARS-CoV-2 antibody reactivity levels may increase their susceptibility to recurrent COVID-19. Seroprevalence, seroconversion and the magnitude of anti-SARS-CoV-2 antibody reactivity was significantly attenuated in infliximab-treated patients compared with vedolizumab-treated patients. Concomitant immunomodulator use with a thiopurine or methotrexate further blunted serological responses to SARS-CoV-2 infection in infliximab-treated patients, with only a third of patients having detectable anti-SARS-CoV-2 antibodies. TXPO:1000172 C24H20F3N5O CAS:1337531-36-8 PubChem:53469448 Wikipedia:GSK2606414 GSK2606414 HOIP_1000172 UBERON:0000004 The olfactory organ of vertebrates, consisting of nares, olfactory epithelia and the structures and skeletal framework of the nasal cavity. Organ that is the specialized structure of the face that contains olfactory neurons. The peripheral olfactory organ is paired[ZFA:0000047]. a protuberance in vertebrates that houses the nostrils, or nares, which admit and expel air for respiration in conjunction with the mouth. Behind the nose are the olfactory mucosa and the sinuses. Behind the nasal cavity, air next passes through the pharynx, shared with the digestive system, and then into the rest of the respiratory system. In humans, the nose is located centrally on the face; on most other mammals, it is on the upper tip of the snout[WP]. GO: The nose is the specialized structure of the face that serves as the organ of the sense of smell and as part of the respiratory system. Includes the nasi externus (external nose) and cavitas nasi (nasal cavity)[Wikipedia:Nose]. the organ that is specialized for smell and is part of the respiratory system BTO:0000840 CALOHA:TS-2037 EHDAA2:0001274 EHDAA:1502 EMAPA:16542 EV:0100037 EV:0100370 FMA:46472 GAID:77 MA:0000281 MAT:0000139 MESH:D009666 MIAA:0000139 OpenCyc:Mx4rvViCbJwpEbGdrcN5Y29ycA TAO:0000047 UMLS:C0028429 ZFA:0000047 galen:Nose nasal sac nose peripheral olfactory organ nasus olfactory apparatus proboscis the structure of the nose varies across vertebrates. In tetrapods the nose is part of the respiratory system.[PMID:25312359] nose UBERON:0000016 The part of the pancreas that is part of the endocrine system and is made up of islet cells, which produce insulin, glucagon and somatostatin. endocrine pancreas UBERON:0000020 An organ that is capable of transducing sensory stimulus to the nervous system. AEO:0000094 BSA:0000121 BTO:0000202 CALOHA:TS-2043 EHDAA2:0001824 EHDAA:500 EMAPA:16192 EMAPA:35955 FBbt:00005155 GAID:63 HAO:0000930 MA:0000017 MESH:D012679 UMLS:C0935626 VHOG:0001407 WBbt:0006929 organ of sense organ system organ of sensory organ system organ of sensory system sense organ system organ sensory organ sensory organ system organ sensory system organ sensillum Sinnesorgan sensor sense organ UBERON:0000025 Any hollow cylindrical anatomical structure containing a lumen through which substances are transported. anatomical tube not every anatomical conduit is a tube - for example, a bone foramen is an opening in the bone, and there is no distinct separate tube structure. Tubes may transport large mixed objects (for example, a bolus of food in the digestive tube) or they may transport the secretions of a single gland (for example, gland ducts) tube (anatomical) UBERON:0000029 Any of the rounded masses of lymphoid tissue that are surrounded by a capsule of connective tissue, are distributed along the lymphatic vessels, and contain numerous lymphocytes which filter the flow of lymph. lymph node UBERON:0000056 Muscular duct that propels urine from the kidneys to the urinary bladder, or related organs. Anatomical structure consisting of long narrow duct which carries urine from the kidney to the urinary bladder.[AAO] The duct of amniotes that carries urine from a metanephric kidney to the urinary bladder. [Bemis_WE, Functional_Anatomy_of_the_Vertebrates:_An_Evolutionary_Perspective, Glossary_G-29, Grande_L, Liem_KF, Third_Edition_(2001)_Orlando_Fla.:_Harcourt_College_Publishers, Walker_WF][VHOG] The first embryonic hint of a metanephros is the formation of the metanephric duct that appears as a ureteric diverticulum arising at the base of preexisting mesonephric duct. The ureteric diverticulum grows dorsally into the posterior region of the nephric ridge. Here it enlarges and stimulates the growth of metanephric tubules that come to make up the metanephric kidney. The metanephros becomes the adult kidney of amniotes, and the metanephric duct is usually called the ureter.[well established][VHOG] AAO:0010254 BTO:0001409 CALOHA:TS-1084 EFO:0000930 EHDAA2:0002139 EHDAA:9341 EMAPA:17950 EV:0100097 FMA:9704 GAID:438 MA:0000378 MAT:0000120 MESH:D014513 MIAA:0000120 OpenCyc:Mx4rvhmm6JwpEbGdrcN5Y29ycA UMLS:C0041951 VHOG:0000605 XAO:0000144 galen:Ureter metanephric duct in humans, consists of adventitial, muscular and mucoa layers ureter UBERON:0000058 A tubular structure that transports secreted or excreted substances. anatomical duct duct UBERON:0000059 A subdivision of the digestive tract that connects the small intestine to the cloaca or anus. Lacks or has few villi[Kardong]. A subdivision of the digestive tract that connects the small intestine to the cloaca or anus. Lacks or has few villi[Kardong]. FMA:7201 NCIT:C12379 UMLS:C0021851 large intestine A subdivision of the digestive tract that connects the small intestine to the cloaca or anus. Lacks or has few villi[Kardong]. ISBN10:0073040584 UBERON:0000061 Material anatomical entity that is a single connected structure with inherent 3D shape generated by coordinated expression of the organism's own genome. AAO:0010825 AEO:0000003 BILA:0000003 CARO:0000003 EHDAA2:0003003 EMAPA:0 FBbt:00007001 FMA:67135 GAID:781 HAO:0000003 MA:0003000 MESH:D000825 TAO:0000037 TGMA:0001823 VHOG:0001759 WBbt:0000100 XAO:0003000 ZFA:0000037 biological structure connected biological structure anatomical structure UBERON:0000062 Anatomical structure that performs a specific function or group of functions [WP]. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions. CARO:0020004 EFO:0000634 EMAPA:35949 ENVO:01000162 FMA:67498 MA:0003001 OpenCyc:Mx4rv5XMb5wpEbGdrcN5Y29ycA OpenCyc:Mx4rwP3iWpwpEbGdrcN5Y29ycA UMLS:C0178784 WBbt:0003760 anatomical unit body organ element organ UBERON:0000064 A multicellular structure that is a part of an organ. currently defined in a very broad sense, may be replaced by more specific classes in the future AAO:0011124 EFO:0000635 FMA:82472 cardinal organ part regional part of organ organ part UBERON:0000068 A life cycle stage that starts with fertilization and ends with the fully formed embryo. embryo stage UBERON:0000074 A capillary tuft which forms a close network with the visceral epithelium (podocytes) and the mesangium to form the filtration barrier and is surrounded by Bowman's capsule in nephrons of the vertebrate kidney. renal glomerulus UBERON:0000080 The second stage of the kidney. It serves as the main excretory organ of aquatic vertebrates and as a temporary embryonic kidney in higher vertebrates. It is composed of the mesonephric duct (also called the Wolffian duct), mesonephric tubules, and associated capillary tufts. A single tubule and its associated capillary tuft is called a mesonephric excretory unit; these units are similar in structure and function to nephrons of the adult kidney. The mesonephros is derived from intermediate mesoderm in the vertebrate embryo. Wolffian body mesonephric kidney mesonephroi mesonephros UBERON:0000105 A spatiotemporal region encompassing some part of the life cycle of an organism. life cycle stage UBERON:0000112 BTO:0002168 EFO:0001300 EV:0300051 MmusDv:0000043 XAO:1000010 ZFS:0000051 immature stage juvenile stage sexually immature stage UBERON:0000113 The stage of being a sexually mature adult animal. adult stage post-juvenile adult stage UBERON:0000115 The epithelial layer of the lung. lung epithelium UBERON:0000120 Cell layer consisting of lining cells that separates the central nervous system and the bloodstream. The BBB may consist of endothelial cells or glial cells. An endothelial barrier may have arisen independently several times during evolution. In bichir and lungfish the barrier is formed by brain endothelial cells, while in sturgeon it is formed by a complex perivascular glial sheath, but with no detectable tight junctions. blood brain barrier UBERON:0000160 Segment of the alimentary canal extending from the stomach to the anus and, in humans and other mammals, consists of two segments, the small intestine and the large intestine intestine UBERON:0000170 The pair of anatomical structures comprised of a left lung and right lung. FMA:68877 OpenCyc:Mx4rvVjKy5wpEbGdrcN5Y29ycA lungs lungs pair pulmones set of lungs pair of lungs UBERON:0000171 Organ that functions in gaseous exchange between an organism and its environment. In plants, microorganisms, and many small animals, air or water makes direct contact with the organism's cells or tissue fluids, and the processes of diffusion supply the organism with dioxygen (O2) and remove carbon dioxide (CO2). In larger animals the efficiency of gaseous exchange is improved by specialized respiratory organs, such as lungs and gills, which are ventilated by breathing mechanisms. EMAPA:17607 SPD:0000428 TGMA:0001247 apparatus respiratorius organ breathing organ organ of apparatus respiratorius organ of respiratory system respiratory organ respiratory system organ gas exchange organ respiration organ UBERON:0000177 Pus is a bodily fluid consisting of a whitish-yellow or yellow substance produced during inflammatory responses of the body that can be found in regions of pyogenic bacterial infections. Pus is produced from the dead and living cells which travel into the intercellular spaces around the affected cells. pus UBERON:0000178 A fluid that is composed of blood plasma and erythrocytes. This class excludes blood analogues, such as the insect analog of blood. See UBERON:0000179 haemolymphatic fluid. A complex mixture of cells suspended in a liquid matrix that delivers nutrients to cells and removes wastes. (Source: BioGlossary, www.Biology-Text.com)[TAO] Highly specialized circulating tissue consisting of several types of cells suspended in a fluid medium known as plasma.[AAO] Recent findings strongly suggest that the molecular pathways involved in the development and function of blood cells are highly conserved among vertebrates and various invertebrates phyla. (...) There is now good reason to believe that, in vertebrates and invertebrates alike, blood cell lineages diverge from a common type of progenitor cell, the hemocytoblast.[well established][VHOG] AAO:0000046 BTO:0000089 CALOHA:TS-0079 EFO:0000296 EHDAA2:0000176 EHDAA:418 EMAPA:16332 ENVO:02000027 EV:0100047 FMA:9670 GAID:965 MA:0000059 MESH:D001769 MIAA:0000315 OpenCyc:Mx4rvVjI8JwpEbGdrcN5Y29ycA TAO:0000007 UMLS:C0005767 VHOG:0000224 XAO:0000124 ZFA:0000007 galen:Blood portion of blood vertebrate blood whole blood blood UBERON:0000179 Circulating fluid that is part of the hemolymphoid system. Blood, lymph, interstitial fluid or its analogs. CARO:0000081 blood or blood analog circulating fluid haemolymphatic fluid UBERON:0000347 The insulating envelope that surrounds nerve fibers or axons. entire myelin sheath UBERON:0000415 An anatomical wall that is part of an artery. arterial wall artery wall UBERON:0000454 The layer located below the cerebral cortex that includes the forebrain, midbrain and hindbrain. subcortex cerebral subcortex UBERON:0000463 Material anatomical entity in a gaseous, liquid, semisolid or solid state; produced by anatomical structures or derived from inhaled and ingested substances that have been modified by anatomical structures as they pass through the body. body substance organism substance UBERON:0000464 Non-material anatomical entity of three dimensions, that is generated by morphogenetic or other physiologic processes; is surrounded by one or more anatomical structures; contains one or more organism substances or anatomical structures. lumen space anatomical space UBERON:0000467 Multicellular, connected anatomical structure that has multiple organs as parts and whose parts work together to achieve some shared function. system AAO:0000007 AEO:0000011 BILA:0000011 BSA:0000049 CALOHA:TS-2088 CARO:0000011 EHDAA2:0003011 EHDAA:392 EMAPA:16103 EV:0100000 FBbt:00004856 FMA:7149 HAO:0000011 MA:0000003 OpenCyc:Mx4rCWM0QCtDEdyAAADggVbxzQ TAO:0001439 TGMA:0001831 UMLS:C0460002 VHOG:0001725 WBbt:0005746 WBbt:0005763 XAO:0003002 ZFA:0001439 galen:AnatomicalSystem body system connected anatomical system organ system anatomical systems anatomical system UBERON:0000468 Anatomical structure that is an individual member of a species and consists of more than one cell. Anatomical structure that is an individual member of a species and consists of more than one cell. whole body multi-cellular organism multicellular organism Anatomical structure that is an individual member of a species and consists of more than one cell. Wikipedia:Multi-cellular_organism UBERON:0000473 A gonad of a male animal. A gonad produces and releases sperm. testis UBERON:0000477 UBERON:0000479 Multicellular anatomical structure that consists of many cells of one or a few types, arranged in an extracellular matrix such that their long-range organisation is at least partly a repetition of their short-range organisation. AAO:0000607 AAO:0010054 AEO:0000043 BILA:0000043 CALOHA:TS-2090 CARO:0000043 EHDAA2:0003043 EMAPA:35868 FBbt:00007003 FMA:9637 HAO:0000043 MA:0003002 MESH:D014024 TAO:0001477 TGMA:0001844 UMLS:C0040300 VHOG:0001757 WBbt:0005729 XAO:0003040 ZFA:0001477 galen:Tissue portion of tissue tissue portion simple tissue tissue UBERON:0000483 epithelium Portion of tissue, that consists of one or more layers of epithelial cells connected to each other by cell junctions and which is underlain by a basal lamina. Examples: simple squamous epithelium, glandular cuboidal epithelium, transitional epithelium, myoepithelium[CARO]. The two basic types of metazoan tissue are epithelial and connective. The simplest metazoans, and developmental stages of many primitive invertebrates, consist solely of these two layers. Thus, epithelial and connective tissues may be the primary (original) tissues of metazoans, and both are important in the functional organization of animals.[well established][VHOG] AAO:0000144 AAO:0010055 AEO:0000066 BILA:0000066 BTO:0000416 CALOHA:TS-0288 CARO:0000066 EHDAA2:0003066 EMAPA:32738 FBbt:00007005 FMA:9639 GAID:402 HAO:0000066 MA:0003060 MESH:D004848 TAO:0001486 UMLS:C0014609 VHOG:0000387 XAO:0003045 ZFA:0001486 epithelial tissue portion of epithelium epithelium UBERON:0000922 Anatomical entity that comprises the organism in the early stages of growth and differentiation that are characterized by cleavage, the laying down of fundamental tissues, and the formation of primitive organs and organ systems. For example, for mammals, the process would begin with zygote formation and end with birth. For insects, the process would begin at zygote formation and end with larval hatching. For plant zygotic embryos, this would be from zygote formation to the end of seed dormancy. For plant vegetative embryos, this would be from the initial determination of the cell or group of cells to form an embryo until the point when the embryo becomes independent of the parent plant. embryonic organism embryo UBERON:0000941 Cranial nerve fiber tract which is comprised of retinal ganglion cell axons running posterior medially towards the optic chiasm, at which some of the axons cross the midline and after which the structure is termed the optic tract. Transmits visual information from the retina to the brain optic nerve FMA:50863 cranial nerve II UBERON:0000945 An expanded region of the vertebrate alimentary tract that serves as a food storage compartment and digestive organ. A stomach is lined, in whole or in part by a glandular epithelium. Portion of alimentary canal with increased circular and longitudinal smooth muscle. Bounded posteriorly by the pyloric sphincter. Mucosal lining has increased folding.[AAO] It appears that the stomach has an ancient origin. The stomach first appears in the fish lineage. The prevertebrate chordates do not have a true stomach, whereas the cartilaginous and bony fish do. Although most fish do have a true stomach, some fish species appear to have lost the stomach secondarily. The remaining vertebrate lineages do have a true stomach (at least in the adult animal), although there is great variation in the size and shape of the stomach.[well established][VHOG] AAO:0000579 ANISEED:1235297 BTO:0001307 CALOHA:TS-0980 EFO:0000837 EHDAA2:0001915 EHDAA:2993 EMAPA:17021 EV:0100070 FMA:7148 GAID:293 MA:0000353 MAT:0000051 MESH:A03.492.766 MIAA:0000051 OpenCyc:Mx4rvVjlqpwpEbGdrcN5Y29ycA TAO:0002121 UMLS:C0038351 VHOG:0000408 XAO:0000128 galen:Stomach stomach chamber Ventricular anterior intestine gaster mesenteron ventriculus UBERON ontology restricts this to the vertebrate specific structure - see the grouping class 'food storage organ' for analogous structures in other species. Teleosts: Zebrafish is functionally stomach-less, but may retain ontogenic footprint. Although the precise shape and size of the stomach varies widely among different vertebrates, the relative positions of the oesophageal and duodenal openings remain relatively constant. As a result, the organ always curves somewhat to the left before curving back to meet the pyloric sphincter. However, lampreys, hagfishes, chimaeras, lungfishes, and some teleost fish have no stomach at all, with the oesophagus opening directly into the intestine. The gastric lining is usually divided into two regions, an anterior portion lined by fundic glands, and a posterior with pyloric glands. Cardiac glands are unique to mammals, and even then are absent in a number of species. The distributions of these glands vary between species, and do not always correspond with the same regions as in man. Furthermore, in many non-human mammals, a portion of the stomach anterior to the cardiac glands is lined with epithelium essentially identical to that of the oesophagus. Ruminants, in particular, have a complex stomach, the first three chambers of which are all lined with oesophageal mucosa stomach UBERON:0000948 A myogenic muscular circulatory organ found in the vertebrate cardiovascular system composed of chambers of cardiac muscle. It is the primary circulatory organ. [database_cross_reference: http://orcid.org/0000-0002-6601-2165][database_cross_reference: http://en.wikipedia.org/wiki/Heart] BTO:0000562 C0018787 EFO:0000815 EHDAA:420 FMA:7088 MESH:D006321 NCIT:C12727 UMLS:C0018787 Taxon notes:" the ascidian tube-like heart lacks chambers....The ascidian heart is formed after metamorphosis as a simple tube-like structure with a single-layered myoepithelium that is continuous with a single-layered pericar- dial wall. It lacks chambers and endocardium.... The innovation of the chambered heart was a key event in vertebrate evolution, because the chambered heart generates one-way blood flow with high pressure, a critical requirement for the efficient blood supply of large-body vertebrates... all extant vertebrates have hearts with two or more chambers (Moorman and Christoffels 2003)" http://dx.doi.org/10.1101/gad.1485706 heart UBERON:0000949 Anatomical system that consists of the glands and parts of glands that produce endocrine secretions and help to integrate and control bodily metabolic activity. Anatomical system containing glands which regulates bodily functions though the secretion of hormones.[AAO] Multicellular organisms have complex endocrine systems, allowing responses to environmental stimuli, regulation of development, reproduction, and homeostasis. Nuclear receptors (NRs), a metazoan-specific family of ligand-activated transcription factors, play central roles in endocrine responses, as intermediates between signaling molecules and target genes. The NR family includes ligand-bound and orphan receptors, that is, receptors with no known ligand or for which there is no ligand Pocket. Understanding NR evolution has been further improved by comparison of several completed genomes, particularly those of deuterostomes and ecdysozoans. In contrast, evolution of NR ligands is still much debated. One hypothesis proposes that several independent gains and losses of ligand-binding ability in NRs occurred in protostomes and deuterostomes. A second hypothesis, pertaining to the NR3 subfamily (vertebrate steroid hormone receptors and estrogen related receptor), proposes that before the divergence of protostomes and deuterostomes, there was an ancestral steroid receptor (AncSR) that was ligand-activated and that orphan receptors secondarily lost the ability to bind a ligand. (...) Our analysis reveals that steroidogenesis has been independently elaborated in the 3 main bilaterian lineages (...).[well established][VHOG] AAO:0010279 CALOHA:TS-1301 EFO:0002969 EHDAA2:0002224 EMAPA:35306 EV:0100128 FBbt:00005068 FMA:9668 GAID:439 MA:0000012 MESH:D004703 TAO:0001158 UMLS:C0014136 VHOG:0000098 XAO:0000158 ZFA:0001158 endocrine glandular system endocrine system systema endocrinum endocrine system UBERON:0000955 brain The brain is the center of the nervous system in all vertebrate, and most invertebrate, animals. Some primitive animals such as jellyfish and starfish have a decentralized nervous system without a brain, while sponges lack any nervous system at all. In vertebrates, the brain is located in the head, protected by the skull and close to the primary sensory apparatus of vision, hearing, balance, taste, and smell[WP]. requires review for applicability to invertebrate structures, e.g. synganglion Cavitated compound organ which is comprised of gray and white matter and surrounds the cerebral ventricular system.[TAO] Part of the central nervous system situated within the cranium and composed of both nerve cell bodies and nerve fibers.[AAO] The part of the central nervous system contained within the cranium, comprising the forebrain, midbrain, hindbrain, and metencephalon. It is derived from the anterior part of the embryonic neural tube (or the encephalon). Does not include retina. (CUMBO) (...) at some stage of its development, every chordate exhibits five uniquely derived characters or synapomorphies of the group: (...) (4) a single, tubular nerve cord that is located dorsal to the notochord (...) (reference 1); The neural tube is destined to differentiate into the brain and spinal cord (the central nervous system) (reference 2).[well established][VHOG] AAO:0010478 ABA:Brain BAMS:Br BAMS:Brain BILA:0000135 BTO:0000142 CALOHA:TS-0095 DHBA:10155 EFO:0000302 EHDAA2:0000183 EHDAA:2641 EHDAA:6485 EMAPA:16894 EV:0100164 FBbt:00005095 FMA:50801 GAID:571 HBA:4005 MA:0000168 MAT:0000098 MESH:D001921 MIAA:0000098 OpenCyc:Mx4rvVjT65wpEbGdrcN5Y29ycA PBA:3999 TAO:0000008 UMLS:C0006104 UMLS:C1269537 VHOG:0000157 XAO:0000010 ZFA:0000008 galen:Brain http://braininfo.rprc.washington.edu/centraldirectory.aspx?ID=21 encephalon suprasegmental levels of nervous system suprasegmental structures synganglion the brain brain UBERON:0000956 The thin layer of gray matter on the surface of the cerebral hemisphere that develops from the telencephalon. It consists of the neocortex (6 layered cortex or isocortex), the hippocampal formation and the olfactory cortex. cerebral cortex UBERON:0000964 the transparent anterior portion of the fibrous coat of the eye that serves as the chief refractory structure cornea UBERON:0000966 The retina is the innermost layer or coating at the back of the eyeball, which is sensitive to light and in which the optic nerve terminates. FMA:58301 http://en.wikipedia.org/wiki/Retina inner layer of eyeball retina http://upload.wikimedia.org/wikipedia/commons/e/ed/Human_eye_cross-sectional_view_grayscale.png UBERON:0000970 An organ that detects light. This class encompasses a variety of light-detecting structures from different phyla with no implication of homology, from the compound insect eye to the vertebrate camera-type eye (distinct classes are provided for each) BILA:0000017 BTO:0000439 CALOHA:TS-0309 EFO:0000827 EV:0100336 FBbt:00005162 GAID:69 MAT:0000140 MESH:D005123 MIAA:0000140 OpenCyc:Mx4rvViTvpwpEbGdrcN5Y29ycA light-detecting organ visual apparatus Note that whilst this is classified as an organ, it is in fact more of a unit composed of different structures: in Drosophila, it includes the interommatidial bristle as a part; we consider here the vertebrate eye to include the eyeball/eye proper as a part, with the eye having as parts (when present): eyelids, conjuctiva, eye UBERON:0000990 Anatomical system that has as its parts the organs concerned with reproduction. consider splitting genitalia from reproductive system Anatomical system which consists of organs and tissues associated with sexual reproduction of the organism.[AAO] Arguably, one of the most important aspects of urbilaterian organogenesis would have been gonadogenesis, since Urbilateria must have successfully generated gametes and developed a strategy for extrusion and fertilization, in order to be the ancestor of all living Bilateria.[well established][VHOG] AAO:0010258 BILA:0000103 BTO:0000081 CALOHA:TS-1318 EFO:0000809 EHDAA2:0001603 EHDAA:5923 EMAPA:17381 EV:0100100 FBbt:00004857 FMA:7160 GAID:363 HAO:0000374 HAO:0000895 MA:0000326 MIAA:0000305 OpenCyc:Mx4rvVja4ZwpEbGdrcN5Y29ycA TAO:0000632 UMLS:C1261210 VHOG:0000182 WBbt:0005747 XAO:0000142 ZFA:0000632 Geschlechtsorgan animal reproductive system genital system genital tract genitalia organa genitalia reproductive tissue reproductive tract systemata genitalia reproductive system UBERON:0000992 The gonad of a female organism which contains germ cells. FBbt:00004865 FMA:7209 MESH:D010053 Wikipedia:Ovary ovary UBERON:0000993 A tube or collection of tubes in an animal from the ovaries to the outside of the body. sometimes oviduct is used interchangeably with follaopian tube. Here they are different - the oviduct connects the gonad to the outside in a variety of animals. The mammal-class fallopian tube is derived from the mullerian duct and connects the gonads/infubdibulum to the uterus In all remaining vertebrates (i.e., coelacanths, lungfishes, amphibians, reptiles, birds, and mammals), the oviduct arises in ontogeny as a longitudinal, groovelike invagination of the coelomic epithelium on the lateral surface of the mesonephros oviduct UBERON:0000994 An organ of the female reproductive tract that functions to receive and store sperm from the male, and can sometimes be the site of fertilization when the oocytes are ready. Some species have multiple spermathecae, as seen in earthworms, where four pairs of spermathecae are present. One pair in 6,7,8 and 9 segments. They receive and store the spermatozoa of another earthworm during copulation spermathecum UBERON:0001004 Functional system which consists of structures involved in respiration. The anatomical system in which the exchange of oxygen and carbon dioxide between the organism and its environment.[AAO] There is no doubt that the primitive pattern of vertebrate air-breathing is the buccal pulse pump found in actinopterygian fishes.[well established][VHOG] AAO:0000541 BTO:0000203 CALOHA:TS-1319 EFO:0000804 EHDAA2:0001604 EHDAA:2203 EMAPA:16727 EV:0100036 FMA:7158 GAID:78 MA:0000327 MAT:0000030 MESH:D012137 MIAA:0000030 OpenCyc:Mx4rvVjzFJwpEbGdrcN5Y29ycA TAO:0000272 UMLS:C0035237 VHOG:0000202 XAO:0000117 ZFA:0000272 apparatus respiratorius respiratory system Atmungssystem apparatus respiratorius systema respiratorium respiratory system UBERON:0001005 An airway through which respiratory air passes in organisms. airways respiratory airway UBERON:0001007 Anatomical system that has as its parts the organs devoted to the ingestion, digestion, and assimilation of food and the discharge of residual wastes. An anatomical system consisting of the alimentary canal and digestive glands responsible for intake, absorption, digestion and excretion of food.[AAO] AAO:0000129 BILA:0000082 BTO:0000058 CALOHA:TS-1293 EFO:0000793 EV:0100056 FBbt:00005055 FMA:7152 GAID:278 MA:0002431 MAT:0000018 MESH:D004064 MIAA:0000018 TADS:0000170 TAO:0000339 WBbt:0005748 XAO:0000125 ZFA:0000339 galen:DigestiveSystem ncithesaurus:Digestive_System alimentary system alimentary tract gastrointestinal system gut digestive system UBERON:0001008 The renal system in an anatomical system that maintains fluid balance and contributes to electrolyte balance, acid/base balance, and disposal of nitrogenous waste products.. In various sources such as Encyclopedia Britannica, the excretory and urinary systems are indeed the same system (see wikipedia talk page); we merge two BTO classes here Evolution of vertebrate renal anatomy appears quite conservative when compared, for example, to evolution of respiratory and cardiovascular systems in vertebrates. Major anatomical changes in vertebrates kidneys separate those of birds and mammals from kidneys of lower vertebrates. General increase in animal size from fish to mammals is reflected by an increase in total number of nephrons per kidney, rather than by constant change in tubular dimensions.[well established][VHOG] FMA:7159 MESH:D014551 galen:UrinaryTract excretory system renal system systema urinaria systema urinarium urinary system urinary tract renal or urinary system renal/urinary system In humans, the renal system comprises a pair of kidneys, a pair of ureters, urinary bladder, urethra, sphincter muscle and associated blood vessels renal system UBERON:0001009 organ system that passes nutrients (such as amino acids and electrolytes), gases, hormones, blood cells, etc. to and from cells in the body to help fight diseases and help stabilize body temperature and pH to maintain homeostasis[WP]. the cardiovascular system and the lymphatic system are parts of the circulatory system Anatomical system of ion binding, a pumping mechanism, and an efficient vascular system; consisting of the blood, heart, and blood and lymph vessels, respectively.[AAO] We should divest ourselves of the view that earlier vertebrate groups were 'on their way' to becoming mammals, as clearly they were not such visionaries. Neither were their systems 'imperfect' as earlier anatomists thought. Instead, their circulatory systems served them well to address the ecological demands arising from their lifestyles.[well established][VHOG] AAO:0000959 CALOHA:TS-2103 FBbt:00005057 OpenCyc:Mx4rvVjzG5wpEbGdrcN5Y29ycA VHOG:0001248 systema cardiovasculare circulatory system UBERON:0001013 adipose tissue Portion of connective tissue composed of adipocytes enmeshed in areolar tissue adipose tissue UBERON:0001016 The nervous system is an organ system containing predominantly neuron and glial cells. In bilaterally symmetrical organism, it is arranged in a network of tree-like structures connected to a central body. The main functions of the nervous system are to regulate and control body functions, and to receive sensory input, process this information, and generate behavior [CUMBO]. A regulatory system of the body that consists of neurons and neuroglial cells. The nervous system is divided into two parts, the central nervous system (CNS) and the peripheral nervous system (PNS). (Source: BioGlossary, www.Biology-Text.com)[TAO] Anatomical system consisting of nerve bodies and nerve fibers which regulate the response of the body to external and internal stimuli.[AAO] Nervous systems evolved in the ancestor of Eumetazoa.[well established][VHOG] AAO:0000324 BILA:0000079 BTO:0001484 CALOHA:TS-1313 EFO:0000802 EHDAA2:0001246 EHDAA:826 EMAPA:16469 EV:0100162 FBbt:00005093 FMA:7157 GAID:466 MA:0000016 MAT:0000026 MESH:D009420 MIAA:0000026 OpenCyc:Mx4rvViT_pwpEbGdrcN5Y29ycA TAO:0000396 UMLS:C0027763 VHOG:0000402 WBbt:0005735 XAO:0000177 ZFA:0000396 neurological system nerve net systema nervosum nervous system UBERON:0001017 The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the neural tube derivatives: the brain and spinal cord. In invertebrates it includes central ganglia plus nerve cord. Part of the nervous system which includes the brain and spinal cord.[AAO] The brain and spinal cord. Kimmel et al, 1995.[TAO] The central nervous system (CNS) is the part of the nervous system which includes the brain, spinal cord, and nerve cell layer of the retina (CUMBO). (...) at some stage of its development, every chordate exhibits five uniquely derived characters or synapomorphies of the group: (...) (4) a single, tubular nerve cord that is located dorsal to the notochord (...) (reference 1); The neural tube is destined to differentiate into the brain and spinal cord (the central nervous system) (reference 2); Taken together, our data make a very strong case that the complex molecular mediolateral architecture of the developing trunk CNS (central nervous system), as shared between Platynereis and vertebrates, was already present in their last common ancestor, Urbilateria. The concept of bilaterian nervous system centralization implies that neuron types concentrate on one side of the trunk, as is the case in vertebrates and many invertebrates including Platynereis, where they segregate and become spatially organized (as opposed to a diffuse nerve net). Our data reveal that a large part of the spatial organization of the annelid and vertebrate CNS was already present in their last common ancestor, which implies that Urbilateria had already possessed a CNS (reference 3).[well established][VHOG] AAO:0000090 BAMS:CNS BILA:0000080 BTO:0000227 CALOHA:TS-0150 EFO:0000908 EHDAA2:0000225 EHDAA:828 EMAPA:16470 EMAPA:16754 EV:0100163 FBbt:00005094 FMA:55675 GAID:570 MA:0000167 MAT:0000457 MESH:D002490 OpenCyc:Mx4rvzYt3pwpEbGdrcN5Y29ycA TAO:0000012 UMLS:C0927232 VHOG:0000293 XAO:0000215 ZFA:0000012 CNS systema nervosum centrale cerebrospinal axis neuraxis central nervous system UBERON:0001032 Anatomical system that overlaps the nervous system and is responsible for receiving and processing sensory information. An early step in the evolution of neural crest, therefore, may have been the origin of a specific dorsal neural cell population contributing to sensory processing; this would predate the divergence of the amphioxus and vertebrate lineages.[well established][VHOG] AAO:0000555 BAMS:SEN BILA:0000099 EFO:0000805 EHDAA2:0003094 EMAPA:16192 FBbt:00005827 FMA:75259 MA:0002442 MAT:0000031 MIAA:0000031 TAO:0000282 VHOG:0001674 XAO:0003194 ZFA:0000282 organa sensuum sense organ subsystem sense organs sense organs set sensory subsystem sensory systems organa sensuum sensory organ system set of sense organs sensory system UBERON:0001043 Tube that connects the pharynx to the stomach. In mammals, the oesophagus connects the buccal cavity with the stomach. The stratified squamous non-keratinised epithelium lining the buccal cavity is continued through the pharynx down into the oesophagus. The lowest part of the oesophagus (ca. 2 cm) is lined with gastric mucosa and covered by peritoneum. The main body of the oesophagus is lined with small, simple mucous glands. Each gland opens into the lumen by a long duct which pierces the muscularis mucosae (Wilson and Washington, 1989). A sphincter is situated at the point where the oesophagus enters the stomach to prevent gastro-oesophageal reflux, i.e. to prevent acidic gastric contents from reaching stratified epithelia of the oesophagus, where they can cause inflammation and irritation (Wilson and Washington, 1989; Brown et al., 1993). Anterior end of the alimentary canal lined with smooth muscle. Bounded anteriorly by a constriction in the pharynx. Bounded posteriorly by and increase in circular and/or longitudinal smooth muscle associated with the stomach.[AAO] The few structural specializations in (adult lampreys) pharynx include complex valves on the external gill openings that direct the tidal flow, and the division of the ancestral pharynx into an oesophagus and a respiratory pharynx.[well established][VHOG] AAO:0000145 ANISEED:1235301 BTO:0000959 CALOHA:TS-0700 EFO:0000835 EHDAA2:0001285 EHDAA:2937 EMAPA:16833 EV:0100069 FMA:7131 GAID:291 MA:0000352 MAT:0000048 MESH:A03.365 MIAA:0000048 OpenCyc:Mx4rvVj9Q5wpEbGdrcN5Y29ycA TAO:0000204 UMLS:C0014876 VHOG:0000450 XAO:0000127 ZFA:0000204 galen:Esophagus gullet oesophagus esophagus UBERON:0001052 the terminal portion of the intestinal tube, terminating with the anus FMA:14544 NCIT:C12390 UMLS:C0034896 http://en.wikipedia.org/wiki/Rectum http://www.snomedbrowser.com/Codes/Details/181261002 rectum UBERON:0001062 Biological entity that is either an individual member of a biological species or constitutes the structural organization of an individual member of a biological species. Biological entity that is either an individual member of a biological species or constitutes the structural organization of an individual member of a biological species. anatomical entity Biological entity that is either an individual member of a biological species or constitutes the structural organization of an individual member of a biological species. FMA:62955 UBERON:0001088 urine Excretion that is the output of a kidney BTO:0001419 CALOHA:TS-1092 EFO:0001939 EMAPA:36554 ENVO:00002047 FMA:12274 GAID:1189 MA:0002545 MAT:0000058 MESH:D014556 MIAA:0000058 OpenCyc:Mx4rvVjGppwpEbGdrcN5Y29ycA UMLS:C0042036 galen:Urine kidney excreta from some taxa (e.g. in aves) may not be liquid urine UBERON:0001113 Traditional gross anatomy divided the liver into four lobes based on surface features. The falciform ligament is visible on the front (anterior side) of the liver. This divides the liver into a left anatomical lobe, and a right anatomical lobe. FMA:13361 UMLS:C0447541 hepatic lobe liver lobe lobus hepatis lobe of liver UBERON:0001115 The left lobe is smaller and more flattened than the right. It is situated in the epigastric and left hypochondriac regions. Its upper surface is slightly convex and is moulded on to the diaphragm; its under surface presents the gastric impression and omental tuberosity. FMA:13363 http://en.wikipedia.org/wiki/Left_lobe_of_liver http://www.snomedbrowser.com/Codes/Details/362183003 left liver lobe liver left lobe lobus hepaticus sinister left lobe of liver UBERON:0001134 skeletal muscle tissue Muscle tissue that consists primarily of skeletal muscle fibers. skeletal muscle tissue UBERON:0001135 Muscle tissue which is unstriated, composed primarily of smooth muscle fibers surrounded by a reticulum of collagen and elastic fibers. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. smooth muscle tissue UBERON:0001143 Vein that carries blood away from the liver. http://en.wikipedia.org/wiki/Hepatic_vein hepatic vein UBERON:0001155 Last portion of the large intestine before it becomes the rectum. EFO:0000361 NCIT:C12382 UMLS:C0009368 Although all vertebrates have a digestive tract and accessory glands, various parts of this system are not necessarily homologous, analogous, or even present in all species. Therefore, broad comparisons can be best made under the listings of headgut, foregut, midgut, pancreas and biliary system, hindgut.[uncertain][VHOG] colon UBERON:0001173 A complex network of conduits that begins with the canals of Hering (intralobar bile duct) and progressively merges into a system of interlobular, septal, and major ducts which then coalesce to form the extrahepatic bile ducts, which finally deliver bile to the intestine, and in some species to the gallbladder. Hollow tree organ, the organ parts of which consist of the bile ducts.[AAO] AAO:0011020 EMAPA:35172 FMA:14665 UMLS:C0005423 XAO:0000455 biliary tract The path in many species is as follows: Bile canaliculi -> Canals of Hering (intralobar bile duct) -> interlobular bile ducts -> intrahepatic bile ducts -> left and right hepatic ducts merge to form -> common hepatic duct *exits liver* and joins -> cystic duct (from gall bladder) forming -> common bile duct -> joins with pancreatic duct -> forming ampulla of Vater -> enters duodenum [WP] biliary tree UBERON:0001193 An artery that supplies the liver. currently defined in a generic fashion. Artery that supplies blood to the liver.[TAO] BTO:0004307 EMAPA:17859 FMA:14769 GAID:496 MA:0001963 MESH:D006499 OpenCyc:Mx4rvzKtFpwpEbGdrcN5Y29ycA TAO:0005161 UMLS:C0019145 ZFA:0005161 galen:HepaticArtery http://en.wikipedia.org/wiki/Hepatic_artery_proper arteria hepatica propria arteria hepatica hepatic artery UBERON:0001264 An endoderm derived structure that produces precursors of digestive enzymes and blood glucose regulating enzymes[GO]. Organ which secretes a fluid containing enzymes that aid in the digestion of food.[AAO] In the hagfish and lampreys (our most primitive vertebrate species of today), the first sign of 'a new organ' is found as collections of endocrine cells around the area of the bile duct connection with the duodenum. These endocrine organs are composed of 99% beta cells and 1% somatostatin-producing delta cells. Compared to the more primitive protochordates (e.g. amphioxus), this represents a stage where all previously scattered insulin-producing cells of the intestinal tissue have now quantitatively migrated to found a new organ involved in sensing blood glucose rather than gut glucose. Only later in evolution, the beta cells are joined by exocrine tissue and alpha cells (exemplified by the rat-, rabbit- and elephant-fishes). Finally, from sharks and onwards in evolution, we have the islet PP-cell entering to complete the pancreas.[well established][VHOG] As a secretory organ serving exocrine and endocrine functions, the pancreas is specific to the vertebrates[PMID:16417468] Hagfishes and lampreys are unique in the complete separation of their endocrine pancreas (islet or- gan) and their exocrine pancreas (50). The endocrine and exocrine pancreas are coassociated in crown gnathostomes (50). In Branchiostoma and Ciona, there is no diverticulum as there is in hagfishes, lampreys, and gnathostomes, only dispersed insulin-secreting cells in the walls of the gastrointestinal tract (51, 52) The mature pancreas of higher vertebrates and mammals comprises two major functional units: the exocrine pancreas, which is responsible for the production of digestive enzymes to be secreted into the gut lumen, and the endocrine pancreas, which has its role in the synthesis of several hormones with key regulatory functions in food uptake and metabolism. The exocrine portion constitutes the majority of the mass of the pancreas, and contains only two different cell types, the secretory acinar cells and the ductular cells. The endocrine portion, which comprises only 1-2% of the total mass, contains five different cell types, which are organized into mixed functional assemblies referred to as the islets of Langerhans AAO:0010112 BTO:0000988 CALOHA:TS-0736 EFO:0000855 EHDAA2:0001367 EHDAA:6893 EMAPA:17503 EV:0100092 FMA:7198 GAID:334 MA:0000120 MAT:0000075 MESH:D010179 MIAA:0000075 OpenCyc:Mx4rvVimZZwpEbGdrcN5Y29ycA TAO:0000140 UMLS:C0030274 VHOG:0000050 XAO:0000136 ZFA:0000140 galen:Pancreas pancreas UBERON:0001276 The epithelial layer of the stomach. epithelium of stomach UBERON:0001281 Wide thin-walled blood vessels in the liver. In mammals they have neither veinous or arterial markers. liver hepatic sinusoids liver sinusoid liver sinusoidal blood vessel sinusoid of liver vas capillare sinusoideum hepatic sinusoid UBERON:0001283 An intercellular channel that takes up bile from hepatocytes, transporting it to the bile ducts. bile canaliculus bile canaliculus http://en.wikipedia.org/wiki/Bile_canaliculus UBERON:0001434 Anatomical system that is a multi-element, multi-tissue anatomical cluster that consists of the skeleton and the articular system. Anatomical system consisting of multiple elements and tissues that provides physical support.[TAO] Anatomical system that is a multi-element, multi-tissue anatomical cluster that consists of the skeleton and the articular system.[VSAO] System that provides physical support to the organism.[AAO] By taking a holistic approach, integration of the evidence from molecular and developmental features of model organisms, the phylogenetic distribution in the 'new animal phylogeny' and the earliest fossilized remains of mineralized animal skeletons suggests independent origins of the skeleton at the phylum level.[debated][VHOG] AAO:0000566 BTO:0001486 CALOHA:TS-1320 EFO:0000806 EHDAA2:0003168 EMAPA:35773 FMA:23881 MA:0000018 OpenCyc:Mx4rvVi1rpwpEbGdrcN5Y29ycA TAO:0000434 UMLS:C0037253 VHOG:0001254 VSAO:0000027 XAO:0003060 ZFA:0000434 https://github.com/obophenotype/uberon/wiki/The-skeletal-system skeleton system set of all bones and joints Skelettsystem skeletal system UBERON:0001557 The segment of the respiratory tract that starts proximally with the nose and ends distally with the cricoid cartilage, before continuing to the trachea. upper respiratory tract UBERON:0001558 The segment of the respiratory tract that starts proximally with the trachea and includes all distal structures including the lungs. lower respiratory tract UBERON:0001621 An artery that supplies the myocardium. BTO:0000290 CALOHA:TS-0176 EFO:0002551 EMAPA:19160 EMAPA:25968 EV:0100383 FMA:49893 MA:0002453 OpenCyc:Mx4rvoL56ZwpEbGdrcN5Y29ycA UMLS:C0205042 VHOG:0001557 ZFA:0005812 galen:CoronaryArtery coronary arterial tree coronary vessel coronary artery UBERON:0001630 Organ consisting of a tissue made up of various elongated cells that are specialized to contract and thus to produce movement and mechanical work[GO]. Portion of tissue composed of contractile fibers.[TAO] It seems clear that the metazoan ancestor inherited from its unicellular descendants an actin cytoskeleton and motor-proteins of the myosin superfamily. Within metazoans, these two molecules were arranged into effective contractile units, the muscles. The basic trends for muscle evolution are already expressed in the diploblastic taxa.[well established][VHOG] muscle AAO:0011066 EMAPA:32715 EV:0100146 FMA:5022 GAID:131 MA:0000015 OpenCyc:Mx4rv2kf-5wpEbGdrcN5Y29ycA TAO:0005145 VHOG:0001245 XAO:0000172 ZFA:0005145 galen:Muscle muscle organ UBERON:0001637 An epithelial tube or tree of tibes that transports blood away from the heart[modified from AEO definition]. Note that in FMA an artery is a tree, whereas AEO/JB defines it as a tube; FMA includes a separate class for what it calls the trunk. Classification in this ontology may currently (Jan 2012) represent a mix of both schemes, although we are gradually revising in the direction of the AEO scheme. Part of the circulatory system composed of blood vessels which carry oxygenated blood away from the heart to the rest of the body.[AAO] The appearance of Chordata and subsequently the vertebrates is accompanied by a rapid structural diversification of this primitive linear heart: looping, unidirectional circulation, an enclosed vasculature, and the conduction system.[well established][VHOG] AAO:0010211 AEO:0000208 BTO:0000573 CALOHA:TS-0054 EFO:0000814 EHDAA2:0000143 EHDAA2:0003253 EMAPA:35147 EV:0100026 FMA:50720 GAID:468 MA:0000064 MAT:0000034 MESH:D001158 MIAA:0000034 OpenCyc:Mx4rvVjknZwpEbGdrcN5Y29ycA TAO:0000005 UMLS:C0003842 VHOG:0001251 XAO:0000114 ZFA:0000005 galen:Artery arterial subtree arterial tree organ part arteries arterial system arterial vessel artery UBERON:0001638 Any of the tubular branching vessels that carry blood from the capillaries toward the heart. TODO - check with MA - vein vs venous blood vessel Part of the circulatory system composed of blood vessels which carry blood from other organs, tissues, and cells to the heart.[AAO] The appearance of Chordata and subsequently the vertebrates is accompanied by a rapid structural diversification of this primitive linear heart: looping, unidirectional circulation, an enclosed vasculature, and the conduction system.[well established][VHOG] venous subtree venous vessel AAO:0010212 AEO:0000209 BTO:0000234 CALOHA:TS-1108 EFO:0000816 EHDAA2:0003254 EMAPA:35906 EV:0100031 FMA:50723 GAID:492 MA:0000067 MAT:0000037 MESH:D014680 MIAA:0000037 OpenCyc:Mx4rvVjkWpwpEbGdrcN5Y29ycA TAO:0000082 UMLS:C0042449 VHOG:0001743 XAO:0000115 ZFA:0000082 galen:Vein venous tree organ part vascular element vena venae vein UBERON:0001690 Sense organ in vertebrates that is specialized for the detection of sound, and the maintenance of balance. Includes the outer ear and middle ear, which collect and transmit sound waves; and the inner ear, which contains the organs of balance and (except in fish) hearing. Also includes the pinna, the visible part of the outer ear, present in some mammals. The organ of hearing and of equilibrium. [TFD][VHOG] Both vertebrate and invertebrate auditory organs are thought to have evolved from primitive mechanosensors, but the nature of the ancestral structure and the evolutionary trajectories followed in distinct animal lineages remain unknown. In particular, we do not know how many types of mechanosensor existed in the protostome-deuterostome ancestor from which insects and vertebrates evolved or whether the PDA had an auditory organ.[well established][VHOG] AAO:0011014 BTO:0000368 CALOHA:TS-1165 EFO:0000826 EHDAA2:0000423 EHDAA:502 EMAPA:16193 EV:0100353 FMA:52780 GAID:62 MA:0000236 MAT:0000138 MESH:D004423 MIAA:0000138 OpenCyc:Mx4rvViXS5wpEbGdrcN5Y29ycA OpenCyc:Mx4rvVjL05wpEbGdrcN5Y29ycA UMLS:C0013443 UMLS:C0521421 VHOG:0000330 XAO:0000189 galen:Ear auditory apparatus auris ear UBERON:0001723 A muscular organ in the floor of the mouth. in MA the tongue is part of the oral region, which in uberon is treated as the oral opening. consider revising oral opening - oral region equivalence. A mobile mass of muscular tissue that is covered with mucous membrane, occupies much of the cavity of the mouth, forms part of its floor, bears the organ of taste, and assists in chewing and swallowing. [TFD][VHOG] Muscular organ in the floor of the mouth.[FEED] The tongue is the movable, muscular organ on the floor of the mouth of most vertebrates, in many other mammals is the principal organ of taste, aids in the prehension of food, in swallowing, and in modifying the voice as in speech[GO][GO:0043586]. Most adult amphibians have a tongue, as do all known reptiles, birds and mammals. Thus it is likely that the tongue appeared with the establishment of tetrapods and this structure seems to be related, to some extant, to the terrestrial lifestyle.[well established][VHOG] Many species of fish have small folds at the base of their mouths that might informally be called tongues, but they lack a muscular structure like the true tongues found in most tetrapods The tongue has contributions from all pharyngeal arches which changes with time. The tongue initially begins as swelling rostral to foramen cecum, the median tongue bud.. tongue muscles derive from the somites - http://php.med.unsw.edu.au/embryology/index.php?title=Tongue_Development#Pharyngeal_Arch_Contributions AAO:0010360 BTO:0001385 CALOHA:TS-1050 EFO:0000833 EHDAA2:0002062 EHDAA:9144 EMAPA:17185 EV:0100058 FMA:54640 GAID:816 MA:0000347 MAT:0000040 MESH:D014059 MIAA:0000040 OpenCyc:Mx4rvVjmJ5wpEbGdrcN5Y29ycA_53KXLq9EdqAAAACs6hnmQ TAO:0005333 UMLS:C0040408 VHOG:0000419 XAO:0000446 ZFA:0005333 glossus tongue UBERON:0001811 The mucous membrane that lines the inner surface of the eyelids and the front of the eyeball. conjunctiva UBERON:0001826 The mucous membrane that lines the nasal cavity. nasal cavity mucosa UBERON:0001915 An endothelium that is part of a capillary. endothelium of capillary UBERON:0001969 The liquid component of blood, in which erythrocytes are suspended. plasma portion of plasma BTO:0000131 CALOHA:TS-0800 EFO:0001905 EMAPA:35690 FMA:62970 GAID:1178 MA:0002501 MAT:0000052 MESH:D010949 MIAA:0000052 OpenCyc:Mx4rEg4ZYrIbEduAAAAOpmP6tw UMLS:C0032105 blood plasm portion of blood plasma blood plasma UBERON:0001970 bile vital aqueous secretion of the liver that is formed by hepatocytes and modified down stream by absorptive and secretory properties of the bile duct epithelium. aids the process of digestion of lipids in the small intestine bile salts function to emulsify dietary fats and facilitate their intestinal absorption elimination of cholesterol major excretory route for potentially harmful exogenous lipophilic substances many hormones and pheromones are excreted in bile, and contribute to growth and development of the intestine in some species and provide attractants for the weaning of non-human vertebrates protects the organism from enteric infections by excreting immune globulin A (IgA), inflammatory cytokines, and stimulating the innate immune system in the intestine BTO:0000121 CALOHA:TS-1172 ENVO:02000023 FMA:62971 GAID:1157 MA:0002513 MESH:D001646 UMLS:C0005388 galen:Bile fel gall In many species, bile is stored in the gallbladder and upon eating is discharged into the duodenum. bile UBERON:0001977 The portion of blood plasma that excludes clotting factors. blood serum UBERON:0001979 One of the minute vessels that collect deoxygenated blood from the capillary plexuses returns it to the veins. venule UBERON:0001980 The smallest division of the artery located between the muscular arteries and the capillaries. arteriole UBERON:0001981 A vessel through which blood circulates in the body. consider adopting the EMAPA superclass 'vascular element', which includes microvasculature (e.g. capillaries), vascular plexus should not be confused with the anatomic lobes of the liver (caudate lobe, quadrate lobe, left lobe, and right lobe), or any of the functional lobe classification systems.[WP] Any of the vessels through which blood circulates in the body. [XAO:0001011_][VHOG] Any of the vessels through which blood circulates in the body.[AAO] The appearance of Chordata and subsequently the vertebrates is accompanied by a rapid structural diversification of this primitive linear heart: looping, unidirectional circulation, an enclosed vasculature, and the conduction system.[well established][VHOG] annelids have blood vessels, but this class is not applicable to annelids. vascular element AAO:0011004 AEO:0000207 BTO:0001102 CALOHA:TS-0080 EFO:0000817 EHDAA2:0003252 EHDAA:240 EMAPA:32743 EMAPA:35993 FMA:50722 FMA:63183 GAID:169 MA:0000060 MAT:0000393 MESH:D001808 NCIT:C12679 OpenCyc:Mx4rvVjxlpwpEbGdrcN5Y29ycA TAO:0002137 UMLS:C0005847 VHOG:0001250 XAO:0001011 ZFA:0005314 MESH:D001808 region of vascular tree organ vascular tree organ region vas sanguineum FMA:63183 Blood vessel is categorized as 'general anatomical term'. Suggestion to map to region of vascular tree from Terry H at JAX blood vessel UBERON:0001982 Any of the smallest blood vessels connecting arterioles with venules. capillary UBERON:0001986 A layer of epithelium that lines the heart, blood vessels (endothelium, vascular), lymph vessels (endothelium, lymphatic), and the serous cavities of the body[MESH]. Simple squamous epithelium which lines blood and lymphatic vessels and the heart. endothelium UBERON:0002012 An artery that carries deoxygenated blood from heart to the lungs. They are the only arteries (other than umbilical arteries in the fetus) that carry deoxygenated blood. pulmonary artery UBERON:0002017 A vein that conducts blood from the digestive organs, spleen, pancreas, and gallbladder to the liver. portal vein UBERON:0002048 Respiration organ that develops as an oupocketing of the esophagus. Either of two organs which allow gas exchange absorbing oxygen from inhaled air and releasing carbon dioxide with exhaled air.[AAO] Lungs had already developed as paired ventral pockets from the intestine in the ancestor of Osteognathostomata. (...) In actinopterygian fishes, apart from Cladistia, the ventral intestinal pocket migrates dorsally and becomes the swim-bladder, a mainly hydrostatical organ (reference 1); Comparative transcriptome analyses indicate molecular homology of zebrafish swimbladder and Mammalian lung (reference 2).[well established][VHOG] respiration organ in all air-breathing animals, including most tetrapods, a few fish and a few snails. In mammals and the more complex life forms, the two lungs are located in the chest on either side of the heart. Their principal function is to transport oxygen from the atmosphere into the bloodstream, and to release carbon dioxide from the bloodstream into the atmosphere. This exchange of gases is accomplished in the mosaic of specialized cells that form millions of tiny, exceptionally thin-walled air sacs called alveoli. // Avian lungs do not have alveoli as mammalian lungs do, they have Faveolar lungs. They contain millions of tiny passages known as para-bronchi, connected at both ends by the dorsobronchi AAO:0000275 AAO:0010567 BTO:0000763 CALOHA:TS-0568 EFO:0000934 EHDAA2:0001042 EHDAA:1554 EHDAA:2205 EMAPA:16728 EV:0100042 FMA:7195 GAID:345 MA:0000415 MAT:0000135 MESH:D008168 MIAA:0000135 OpenCyc:Mx4rvVjKy5wpEbGdrcN5Y29ycA UMLS:C0024109 VHOG:0000310 XAO:0000119 galen:Lung pulmo Snakes and limbless lizards typically possess only the right lung as a major respiratory organ; the left lung is greatly reduced, or even absent. Amphisbaenians, however, have the opposite arrangement, with a major left lung, and a reduced or absent right lung [WP] lung UBERON:0002080 A cardiac ventricle that is in the right side of the heart. heart right ventricle UBERON:0002082 Cardiac chamber through which blood leaves the heart. cardiac ventricle UBERON:0002084 A cardiac ventricle that is in the left side of the heart. heart left ventricle UBERON:0002097 The organ covering the body that consists of the dermis and epidermis. consider 'integumentary system' for invertebrates BTO:0001253 CALOHA:TS-0934 EFO:0000962 EHDAA2:0001844 EMAPA:17525 FMA:7163 MESH:D012867 MFMO:0000099 OpenCyc:Mx4rvVjX3ZwpEbGdrcN5Y29ycA UMLS:C1123023 XAO:0000023 galen:Skin entire skin skin organ entire integument integument integumental organ pelt skin skin of body UBERON:0002103 A (free) limb that is connected to a pelvic girdle region. The extent of this structure includes autopod, stylopod and zeugopod regions when present, but excludes the pelvic girdle and its parts. hindlimb UBERON:0002106 the organ that functions to filter blood and to store red corpuscles and platelets UMLS:C0037993 http://en.wikipedia.org/wiki/Spleen http://upload.wikimedia.org/wikipedia/commons/d/d6/Illu_spleen.jpg spleen http://www.snomedbrowser.com/Codes/Details/181279003 UBERON:0002107 An exocrine gland which secretes bile and functions in metabolism of protein and carbohydrate and fat, synthesizes substances involved in the clotting of the blood, synthesizes vitamin A, detoxifies poisonous substances, stores glycogen, and breaks down worn-out erythrocytes. An exocrine gland which secretes bile and functions in metabolism of protein and carbohydrate and fat, synthesizes substances involved in the clotting of the blood, synthesizes vitamin A, detoxifies poisonous substances, stores glycogen, and breaks down worn-out erythrocytes. Organ which secretes bile and participates in formation of certain blood proteins.[AAO] All vertebrates possess a liver (reference 1); Later in craniate evolution, an anterior gill arch was transformed into jaws, and many new types of feeding subsequently evolved.(...) A liver evolved that, among its many functions, stores considerable energy as glycogen or lipid (reference 2).[well established][VHOG] An organ sometimes referred to as a liver is found associated with the digestive tract of the primitive chordate Amphioxus. However, this is an enzyme secreting gland, not a metabolic organ, and it is unclear how truly homologous it is to the vertebrate liver. The zebrafish liver differs from the mammalian liver in that the hepatocytes are not clearly organized in cords or lobules and the typical portal triads are not apparent. In addition, the zebrafish liver does not have Kuppfer cells. Furthermore, a clear distinction can be made between the male and female liver in the adult zebrafish. The female hepatocytes are very basophilic (Figure 15c) as a result of the production of vitellogenin (Van der Ven et al. 2003). The liver is found in all vertebrates, and is typically the largest visceral organ. Its form varies considerably in different species, and is largely determined by the shape and arrangement of the surrounding organs. Nonetheless, in most species it is divided into right and left lobes; exceptions to this general rule include snakes, where the shape of the body necessitates a simple cigar-like form. The internal structure of the liver is broadly similar in all vertebrates. secretes bile and functions in metabolism of protein and carbohydrate and fat, synthesizes substances involved in the clotting of the blood, synthesizes vitamin A, detoxifies poisonous substances, stores glycogen, and breaks down worn-out erythrocytes[GO]. AAO:0010111 BTO:0000759 CALOHA:TS-0564 EFO:0000887 EHDAA2:0000997 EHDAA:2197 EMAPA:16846 EV:0100089 FMA:7197 GAID:288 MA:0000358 MAT:0000097 MESH:D008099 MIAA:0000097 OpenCyc:Mx4rvVimppwpEbGdrcN5Y29ycA TAO:0000123 UMLS:C0023884 VHOG:0000257 XAO:0000133 ZFA:0000123 galen:Liver iecur jecur liver An exocrine gland which secretes bile and functions in metabolism of protein and carbohydrate and fat, synthesizes substances involved in the clotting of the blood, synthesizes vitamin A, detoxifies poisonous substances, stores glycogen, and breaks down worn-out erythrocytes. BTO:0000759 http://en.wikipedia.org/wiki/Liver UBERON:0002108 Subdivision of digestive tract that connects the stomach to the large intestine and is where much of the digestion and absorption of food takes place (with the exception of ruminants). The mammalian small intestine is long and coiled and can be differentiated histologically into: duodenum, jejunem, ileum[WP,cjm,Kardong]. The terminal region of the mid intestine is comprised of specialized enterocytes that appear to play a role in mucosal immunity. Wallace et al, 2005.[TAO] Intestinal surface area also is increased in amphibians and reptiles by internal folds and occasionally by a few villi. The intestine can be divided into a small intestine and a slightly wider large intestine.[well established][VHOG] AAO:0010397 BTO:0000651 CALOHA:TS-0942 EFO:0000841 EMAPA:32834 EV:0100072 FMA:7200 GAID:313 MA:0000337 MAT:0000047 MESH:A03.492.411.620 MIAA:0000047 OpenCyc:Mx4rvVjlIJwpEbGdrcN5Y29ycA TAO:0001323 UMLS:C0021852 VHOG:0000055 XAO:0000130 ZFA:0001323 galen:SmallIntestine small bowel small intestine anterior intestine intestinum tenue mid intestine small intestine UBERON:0002110 An organ that aids digestion and stores bile produced by the liver[WP]. Membranous muscular sac in which the bile from the liver remains stored until it is required. [Dorian_AF, Elsevier's_encyclopaedic_dictionary_of_medicine, Part_B:_Anatomy_(1988)_Amsterdam_etc.:_Elsevier][VHOG] Organ attached to the liver which stores bile and empties into the duodenum via the bile duct as needed for digestion.[AAO] The presence of a gallbladder appears to be a primitive trait. It is found in most fish and all adult reptiles and amphibians and has been well conserved in mammals, for the most part.[well established][VHOG] AAO:0010114 BTO:0000493 CALOHA:TS-0394 EFO:0000853 EHDAA2:0000699 EHDAA:8062 EMAPA:17202 EV:0100090 FMA:7202 MA:0000356 MAT:0000072 MESH:D005704 MIAA:0000072 OpenCyc:Mx4rvVkGr5wpEbGdrcN5Y29ycA TAO:0000208 UMLS:C0016976 VHOG:0000221 XAO:0000135 ZFA:0000208 galen:Gallbladder gall bladder gallbladder vesica biliaris vesica fellea Rats do not have a gallbladder, but produce bile. The bile flows directly from the liver through the (hepatic) bile duct into the small intestine (Hebel and Stromberg, 1988) gall bladder UBERON:0002113 A paired organ of the urinary tract which has the production of urine as its primary function. One of either of a pair of structures lying on either side of the dorsal aorta in which fluid balance is regulated and waste is excreted out in the form of urine.[AAO] AAO:0000250 BTO:0000671 CALOHA:TS-0510 EFO:0000929 EMAPA:17373 EV:0100096 FMA:7203 GAID:423 MA:0000368 MAT:0000119 MESH:D007668 MIAA:0000119 OpenCyc:Mx4rvVjlYpwpEbGdrcN5Y29ycA UMLS:C0022646 XAO:0003267 galen:Kidney reniculate kidney kidney UBERON:0002114 The first part of the small intestine. At the junction of the stomach and the duodenum the alimentary canal is inflected. The duodenum first goes anteriorly for a short distance, turns dorsally, and eventually caudally, thus it is a U-shaped structure with two horizontal sections (a ventral and a dorsal one). duodenum UBERON:0002116 the portion of the small intestine that extends from the jejunum to the colon ileum UBERON:0002167 Lung which consists of the right upper lobe, middle lobe and right lower lobe.[FMA] Lungs had already developed as paired ventral pockets from the intestine in the ancestor of Osteognathostomata.[well established][VHOG] EHDAA2:0001730 EHDAA:4969 EMAPA:17661 FMA:7309 MA:0000426 OpenCyc:Mx8Ngh4rvgHsHZwpEbGdrcN5Y29ycB4rvVjKy5wpEbGdrcN5Y29ycA UMLS:C0225706 VHOG:0000301 https://github.com/obophenotype/uberon/wiki/Modeling-paired-structures-Design-Pattern right lung UBERON:0002168 Lung which consists of the left upper lobe and left lower lobe.[FMA] Lungs had already developed as paired ventral pockets from the intestine in the ancestor of Osteognathostomata.[well established][VHOG] EHDAA2:0000943 EHDAA:4947 EMAPA:17653 FMA:7310 MA:0000425 OpenCyc:Mx8Ngh4rvgIFoJwpEbGdrcN5Y29ycB4rvVjKy5wpEbGdrcN5Y29ycA UMLS:C0225730 VHOG:0000618 https://github.com/obophenotype/uberon/wiki/Modeling-paired-structures-Design-Pattern left lung UBERON:0002193 Anatomical cluster consisting of the hematopoietic system and the lymphoid system, or its analogs. CALOHA:TS-2018 EHDAA2:0004615 EMAPA:18765 FMA:74562 MA:0000013 hematolymphoid system lymphomyeloid complex haemolymphoid system hemolymphoid system UBERON:0002204 Anatomical system that consists of the muscular and skeletal systems. Anatomical system that provides locomotion and physical support to the organism.[AAO] There are more than 50,000 extant vertebrate species, representing over 500 million years of evolution. During that time, the vertebrate musculoskeletal systems have adapted to aquatic, terrestrial, fossorial, and arboreal lifestyles, while simultaneously retaining functionally integrated axial and appendicular skeletal systems.[well established][VHOG] AAO:0010546 CALOHA:TS-1311 EMAPA:32714 EV:0100139 FMA:7482 GAID:98 MA:0002418 MESH:D009141 OpenCyc:Mx4rQRpVNgAKEdyHxgDggVfs8g UMLS:C0026860 VHOG:0001275 VSAO:0000031 XAO:0000168 musculo-skeletal system musculoskeletal system UBERON:0002223 From the posterior wall of the saccule a canal, the ductus endolymphaticus, is given off; this duct is joined by the ductus utriculosaccularis, and then passes along the aquaeductus vestibuli and ends in a blind pouch, the endolymphatic sac, on the posterior surface of the petrous portion of the temporal bone, where it is in contact with the dura mater. Studies suggest that the endolymphatic duct and endolymphatic sac perform both absorptive and secretory, as well as phagocytic and immunodefensive,functions . FMA:75639 MA:0001188 http://en.wikipedia.org/wiki/Endolymphatic_sac endolymphatic sac UBERON:0002240 Part of the central nervous system located in the vertebral canal continuous with and caudal to the brain; demarcated from brain by plane of foramen magnum. It is composed of an inner core of gray matter in which nerve cells predominate, and an outer layer of white matter in which myelinated nerve fibers predominate, and surrounds the central canal. (CUMBO) TODO - add superclass to unify with VNC? Part of the central nervous system which descends from the hindbrain within the vertebral column.[AAO] (...) at some stage of its development, every chordate exhibits five uniquely derived characters or synapomorphies of the group: (...) (4) a single, tubular nerve cord that is located dorsal to the notochord (...) (reference 1); The neural tube is destined to differentiate into the brain and spinal cord (the central nervous system) (reference 2).[well established][VHOG] AAO:0010151 BAMS:SP BAMS:Spinal BM:SpC BTO:0001279 CALOHA:TS-0953 DHBA:12890 DMBA:17651 EFO:0000110 EHDAA2:0001255 EHDAA:2863 EMAPA:17577 EV:0100316 FMA:7647 GAID:695 MA:0000216 MAT:0000183 MESH:D013116 MIAA:0000183 OpenCyc:Mx4rvVjjk5wpEbGdrcN5Y29ycA TAO:0000075 UMLS:C0037925 VHOG:0000601 XAO:0000020 ZFA:0000075 http://braininfo.rprc.washington.edu/centraldirectory.aspx?ID=22 SpC cerebro-cerebellar fissure cerebrocerebellar fissure fissura cerebro-cerebellaris fissura cerebrocerebellaris medulla spinalis spinal cord structure spinal medulla spinal cord UBERON:0002264 A bulbous anterior projection of the olfactory lobe that is the place of termination of the olfactory nerves and is especially well developed in lower vertebrates (as fishes). olfactory bulb UBERON:0002268 An organ that houses olfactory neurons and is responsible for the sense of smell. Examples include the vertebrate nose and the Drosophila dorsal organ. An olfactory organ overlaps with the olfactory system, because some parts of the nose (e.g. nasal skeleton) are parts of the skeletal system, which is spatially disjoint AAO:0010180 BTO:0001772 FBbt:00005158 FMA:77659 VHOG:0000287 XAO:0000273 olfactory organ olfactory sense organ olfactory sensory organ main olfactory organ primary olfactory organ olfactory neuroepithelium organ olfactus organum olfactorium olfactory organ UBERON:0002294 Organ system subdivision that consists of the organs and ducts that are involved in the production and transportation of bile. In most species this is the gallbladder and the bile ducts (biliary tree). FMA:79646 GAID:279 MA:0001273 MESH:D001659 biliary apparatus biliary tract biliary system UBERON:0002298 Stalk-like part of the brain that includes amongst its parts the medulla oblongata of the hindbrain and the tegmentum of the midbrain. brainstem UBERON:0002299 Spherical outcropping of the respiratory bronchioles and primary site of gas exchange with the blood. Alveoli are particular to mammalian lungs. Different structures are involved in gas exchange in other vertebrates. alveolus of lung UBERON:0002330 Anatomical system that consists of the glands and parts of glands that produce exocrine secretions and help to integrate and control bodily metabolic activity. Exocrine glands are glands that secrete their products (hormones) into ducts (duct glands). They are the counterparts to endocrine glands, which secrete their products (hormones) directly into the bloodstream (ductless glands) or release hormones (paracrines) that affect only target cells nearby the release site. [Wikipedia]. CALOHA:TS-2057 EHDAA2:0002225 EMAPA:35329 FMA:85539 MA:0002411 UMLS:C1516995 WikipediaCategory:Exocrine_system exocrine glandular system exocrine system UBERON:0002349 the middle layer of the heart, comprised mainly of striated cardiac muscle fibers myocardium UBERON:0002350 The cardiac conduction system consists of specialized cardiomyocytes that regulate the frequency of heart beat. cardiac conduction system conducting system of heart UBERON:0002360 Membrane organ that surrounds the brain and the spinal cord. layer of meninges meninx UBERON:0002365 A gland that secretes products (excluding hormones and other chemical messengers) into ducts (duct glands) which lead directly into the external environment. Typical exocrine glands include sweat glands, salivary glands, mammary glands, stomach, liver, pancreas FMA:9596 MESH:D005088 NCIT:C12712 UMLS:C0015282 exocrine gland UBERON:0002368 Endocrine glands are glands of the endocrine system that secrete their products directly into the circulatory system rather than through a duct. FMA:9602 MESH:D004702 NCIT:C1270 UMLS:C0014133 endocrine gland http://upload.wikimedia.org/wikipedia/commons/d/da/Illu_endocrine_system.png UBERON:0002371 bone marrow the soft tissue that fills the cavities of bones bone marrow UBERON:0002384 Tissue with cells that deposit non-polarized extracellular matrix including connective tissue fibers and ground substance. One of the four types of tissue in traditional classifications. It is largely a category of exclusion rather than one with a precise definition, but there are certain characteristics shared by all or most tissues in this category, such as involvement in structure and support, derived from mesoderm, and characterized largely by the traits of non-living tissue.[AAO] Portion of tissue that consists of mesodermally derived cells and intercellular matrix comprised of protein fibers and carbohydrates, which supports, ensheathes and binds together other tissues.[TAO] Tissue with cells that deposit non-polarized extracellular matrix including connective tissue fibers and ground substance.[VSAO] AAO:0000098 BTO:0000421 CALOHA:TS-2009 EFO:0000952 EMAPA:35251 FMA:9640 GAID:100 MA:0000011 MAT:0000301 MESH:D003238 MIAA:0000301 OpenCyc:Mx4rv-aBgZwpEbGdrcN5Y29ycA TAO:0001641 UMLS:C0009780 VSAO:0000017 XAO:0001017 ZFA:0001632 galen:ConnectiveTissue portion of connective tissue textus connectivus Bindegewebe connective tissue UBERON:0002385 Muscle tissue is a contractile tissue made up of actin and myosin fibers[GO]. One of the four types of tissue in traditional classifications. Tissue that contains cells with contractile filaments that move past each other and change the size of the cell. Muscle tissue also is separated into three distinct categories.[AAO] AAO:0000306 AEO:0000122 CALOHA:TS-0642 EHDAA2:0003122 EMAPA:32715 FMA:9641 MA:0002437 MESH:D009132 UMLS:C2328219 galen:MuscleTissue muscular tissue portion of muscle tissue textus muscularis Vertebrate muscle is categorized into three major muscle types defined by their structural and functional properties: skeletal, cardiac and smooth. In Dmel the counterparts are somatic, heart/cardiac and visceral. Here we take a cell type based approach. muscle tissue UBERON:0002390 Anatomical system that is involved in the production of hematopoietic cells. Anatomical system that consists of the blood and blood forming tissues.[AAO] Zebrafish developmental hematopoiesis shows close correspondence to the development of the mammalian hematopoietic system and is regulated by conserved molecular pathways.[well established][VHOG] AAO:0011002 BTO:0000570 CALOHA:TS-0449 EFO:0000798 EMAPA:35402 EV:0100045 FMA:9667 GAID:1008 MA:0002434 MAT:0000022 MESH:D006413 MIAA:0000022 TAO:0005023 UMLS:C0018957 VHOG:0001624 XAO:0000122 ZFA:0005023 haematological system haemopoietic system organa haemopoietica Blutbildungssystem haematopoietic system hematological system hematolymphoid system hemopoietic system In humans this is primarily the bone marrow, spleen, tonsils, and lymph nodes hematopoietic system UBERON:0002394 Any of the ducts that form the biliary tree, carrying bile from the liver to the small intestine. bile tube biliary duct gall duct hepatic duct bile duct UBERON:0002405 Anatomical system that protects the body from foreign substances, cells, and tissues by producing the immune response and that includes especially the thymus, spleen, lymphoid tissue, lymphocytes including the B cells and T cells, and antibodies. The antibody-based immune system defined by the presence of the major histocompatibility complex (MHC), T cell receptor (TCR), B cell receptor (BCR) or recombination activating genes (RAGs) is known beginning from jawed fishes.[well established][VHOG] AAO:0011003 BILA:0000104 FMA:9825 GAID:328 MA:0002711 MESH:D007107 NCIT:C12735 OpenCyc:Mx4rvWNkm5wpEbGdrcN5Y29ycA TAO:0001159 UMLS:C0020962 VHOG:0001247 XAO:0003152 ZFA:0001159 http://www.snomedbrowser.com/Codes/Details/362590003 immune system UBERON:0002416 Connected anatomical system that forms a barrier between an animal and its environment. In vertebrates, the integumental system consists of the epidermis, dermis plus associated glands and adnexa such as hair and scales. In invertebrates, the integumental system may include cuticle. (...) the integument of many tetrapods is reinforced by a morphologically and structurally diverse assemblage of skeletal elements. These elements are widely understood to be derivatives of the once all-encompassing dermal skeleton of stem-gnathostomes (...).[well established][VHOG] UBERON:0007029 AEO:0000154 BILA:0000118 CALOHA:TS-1299 CARO:0002001 EFO:0000807 EHDAA2:0000836 EHDAA2_RETIRED:0003154 EHDAA:6520 EMAPA:17524 EV:0100151 FBbt:00004969 FMA:72979 HAO:0000421 MA:0000014 MAT:0000033 MESH:D034582 MIAA:0000033 TADS:0000108 UMLS:C0037267 VHOG:0000403 XAO:0000176 galen:Surface integumentary system body surface dermal system external covering of organism integumentum commune organism surface surface integumental system UBERON:0002420 An individual member of a collection of basal ganglia. Basal ganglia are subcortical masses of gray matter in the forebrain and midbrain that are richly interconnected and so viewed as a functional system. The nuclei usually included are the caudate nucleus (caudoputamen in rodents), putamen, globus pallidus, substantia nigra (pars compacta and pars reticulata) and the subthalamic nucleus. Some also include the nucleus accumbens and ventral pallidum. basal ganglion UBERON:0002423 The part of the digestive system that contains the liver and the biliary system System responsible for the production and movement of bile[ZFIN:curator]. The hepaticobiliary system is responsible for metabolic and catabolic processing of small molecules absorbed from the blood or gut, hormones and serum proteins, detoxification, storage of glycogen, triglycerides, metals and lipid soluble vitamins and excretion of bile. Included are the synthesis of albumin, blood coagulation factors, complement, and specific binding proteins. The parts are: liver, bile duct, gall bladder and hepatic duct [GO:0061008] AAO:0011056 CALOHA:TS-1308 EFO:0000800 EHDAA2:0000998 EHDAA:2189 EMAPA:16840 EV:0100088 MA:0000324 MAT:0000024 MIAA:0000024 TAO:0000036 UMLS:C1711359 VHOG:0000294 XAO:0000132 ZFA:0000036 hepaticobiliary system liver and biliary system liver/biliary system hepatobiliary system UBERON:0002481 Skeletal tissue with a collagen-rich extracellular matrix vascularized, mineralized with hydroxyapatite and typically including osteocytes located in lacunae that communicate with one another by cell processes (in canaliculi). Bone is deposited by osteoblasts. see https://github.com/obophenotype/uberon/issues/27 Skeletal tissue with a collagen-rich extracellular matrix vascularized, mineralized with hydroxyapatite and typically including osteocytes located in lacunae that communicate with one another by cell processes (in canaliculi). Bone is deposited by osteoblasts.[VSAO] CALOHA:TS-2011 EMAPA:35179 FMA:224804 MA:0002780 MESH:D001842 UMLS:C0391978 VSAO:0000047 XAO:0004040 ZFA:0005621 galen:BoneTissue calcium tissue osseous tissue osteogenic tissue mineralized bone tissue bone portion of bone tissue bone tissue UBERON:0002530 An organ that functions as a secretory or excretory organ FMA:7146 NCIT:C13319 UMLS:C1285092 glandular organ gland http://upload.wikimedia.org/wikipedia/commons/a/a1/Gray1026.png UBERON:0002548 A distinct juvenile form many animals undergo before metamorphosis into adults. Animals with indirect development such as insects, amphibians, or cnidarians typically have a larval phase of their life cycle. larva UBERON:0003054 A single row of glia at the dorsal midline of the developing neural tube along the entire anterior-posterior axis. This region provides inductive signals for the specification of neuronal cell types and of the specification of neural crest cells. The cells comprising the roof plate are the precursors to radial glial cells. EMAPA:35361 roof plate neural tube roof plate neural tube region roofplate roof plate UBERON:0003133 An organ involved in reproduction EMAPA:17381 MA:0001752 MESH:D005835 OpenCyc:Mx4rwO39aJwpEbGdrcN5Y29ycA TGMA:0000591 UMLS:C0017420 WBbt:0008422 genital organ reproductive system organ sex organ genitalia reproductive organ UBERON:0003134 A female organ involved in reproduction EMAPA:28540 MA:0000544 female organism reproductive organ female organism reproductive structure female organism reproductive system organ female organism sex organ female reproductive gland/organ female reproductive system organ female sex organ reproductive organ of female organism reproductive structure of female organism reproductive system organ of female organism sex organ of female organism female reproductive organ UBERON:0003135 A male organ involved in reproduction male reproductive organ UBERON:0003354 An epithelium that is part of a rectum. epithelium of rectum UBERON:0003495 An arteriole that is part of a respiratory system. respiratory system arteriole UBERON:0003499 A blood vessel that is part of a brain. An arterial blood vessel that is part of a brain brain blood vessel UBERON:0003501 A blood vessel that is part of a retina. MESH:D012171 http://www.snomedbrowser.com/Codes/Details/280692003 retina blood vessel UBERON:0003509 A blood vessel that is part of the arterial system. Includes artery, arteriole and aorta. EMAPA:35144 MA:0000061 only in MA - supertype of artery, arteriole, aorta. arterial blood vessel UBERON:0003517 A blood vessel that is part of a kidney. kidney blood vessel UBERON:0003714 Portion of tissue in the nervous system which consists of neurons and glial cells, and may also contain parts of the vasculature. neural tissue UBERON:0003909 small blood vessel similar to a capillary but with a fenestrated endothelium. Sinusoids are found in the liver, lymphoid tissue, endocrine organs, and hematopoietic organs such as the bone marrow and the spleen. Sinusoids found within terminal villi of the placenta are not comparable to these; they possess a continuous endothelium and complete basal lamina[WP]. http://purl.obolibrary.org/obo/UBERON sinusoid UBERON:0003920 A blood vessel that carries blood from the capillaries toward the heart EMAPA:35932 FMA:86188 MA:0000066 segment of venous tree organ venous tree organ segment Compare to: vein venous blood vessel UBERON:0003928 A duct that is part of a digestive system [Automatically generated definition]. duct of digestive system duct of gastrointestinal system gastrointestinal system duct digestive system duct UBERON:0004111 Any tube, opening or passage that connects two distinct anatomical spaces. ostia ostium anatomical conduit UBERON:0004122 Anatomical system that has as its parts the organs concerned with the production and excretion of urine and those concerned with reproduction. Anatomical system that has as its parts the organs concerned with the production and excretion of urine and those concerned with reproduction.[AAO] Kidneys and gonads (of vertebrates) develop from adjacent tissues, and after the excretory or urinary ducts have developed, the reproductive system usually taps into them or their derivatives.[well established][VHOG] AAO:0000624 BILA:0000122 BTO:0003091 EFO:0003864 EHDAA:1013 EMAPA:16367 EV:0100094 FMA:280610 GAID:362 MESH:D014566 OpenCyc:Mx4rQRpVMgAKEdyHxgDggVfs8g UMLS:C0042066 VHOG:0000286 XAO:0000140 galen:GenitoUrinarySystem urogenital system GU tract UG tract Urogenitalsystem genito-urinary system genitourinary tract urogenital tract genitourinary system UBERON:0004134 In mammals, the proximal tubule is a nephron tubule that connects Bowman's capsule to the loop of Henle. It has a brush border epithelial morphology. proximal tubule UBERON:0004212 the small branching blood vessels in the kidney glomerulus that receives blood from the kidney afferent arterioles; these capillaries are under high pressure for filtering within the glomerulus. glomerular capillary UBERON:0004288 Anatomical cluster that consists of all the skeletal elements (eg., bone, cartilage, and teeth) of the body. Anatomical cluster that consists of all the skeletal elements (eg., bone, cartilage, and teeth) of the body.[VSAO] AEO:0000168 EHDAA2:0001843 EHDAA:5047 EMAPA:17213 FMA:23875 GAID:177 MA:0003006 MAT:0000032 MESH:D012863 MIAA:0000032 OpenCyc:Mx4rvVi1rpwpEbGdrcN5Y29ycA VSAO:0000026 XAO:0004053 galen:Skeleton https://github.com/obophenotype/uberon/wiki/The-skeletal-system set of all bones set of bones of body skeleton UBERON:0004297 A blood vessel smooth muscle that is part of a respiratory system. respiratory system blood vessel smooth muscle UBERON:0004535 Anatomical system that has as its parts the heart and blood vessels. we treat cardiovascular as part of circulatory system, with the latter including other kinds of circulation, including lymph. The vessels of the cardiovascular system are as varied as the diverse organs they supply. However, these variations are based on modifications of a fundamental plan of organization common to vertebrates.[well established][VHOG] AAO:0011001 BILA:0000016 BTO:0000088 CALOHA:TS-1297 EFO:0000791 EHDAA2:0000216 EHDAA:394 EMAPA:16104 EMAPA:16370 EV:0100017 FMA:7161 GAID:467 MA:0000010 MAT:0000016 MESH:D002319 MIAA:0000016 OpenCyc:Mx4rvVjzG5wpEbGdrcN5Y29ycA TAO:0000010 UMLS:C0007226 VHOG:0000302 WikipediaCategory:Cardiovascular_system XAO:0000100 XAO:0001010 ZFA:0000010 CV system Herz und Gefaesssystem cardiovascular system UBERON:0004571 The part of the arterial system which carries oxygenated blood away from the heart to the body, and returns deoxygenated blood back to the heart. FMA:45623 systemic arterial circulatory system systemic arterial system UBERON:0004572 The part of the cardiovascular system consisting of all arteries. The appearance of Chordata and subsequently the vertebrates is accompanied by a rapid structural diversification of this primitive linear heart: looping, unidirectional circulation, an enclosed vasculature, and the conduction system.[well established][VHOG] BTO:0004690 EHDAA2:0000143 EHDAA:396 EMAPA:16201 EMAPA:16371 MA:0002719 VHOG:0000273 arterial system UBERON:0004582 The part of the cardiovascular system consisting of all venous vessels. In vertebrates with a double circulation, this can be divided into systemic and pulmonary portions. The appearance of Chordata and subsequently the vertebrates is accompanied by a rapid structural diversification of this primitive linear heart: looping, unidirectional circulation, an enclosed vasculature, and the conduction system.[well established][VHOG] BTO:0004692 EHDAA2:0002171 EHDAA:486 EMAPA:16240 MA:0002720 UMLS:C1267406 VHOG:0000277 vein system venous system UBERON:0004755 A specialized form of connective tissue in which the extracellular matrix is firm, providing the tissue with resilience, and/or mineralized and that functions in mechanical and structural support.[VSAO] A specialized form of connective tissue in which the extracellular matrix is firm, providing the tissue with resilience, and/or mineralized and that functions in mechanical and structural support.[VSAO] MA:0003047 VSAO:0000015 XAO:0004038 ZFA:0005619 Four classes of mineralized tissues are found in vertebrates: bone, cartilage, dentine, and enamel. We think of cartilage and bone as skeletal tissues and of enamel and dentine as dental tissues, but enamel and dentine arose evolutionarily together with bone as skeletal tissues in the dermal skeleton (exoskeleton) of early vertebrates. Scales and teeth of sharks are examples of dermal skeletal elements that are still composed of the three ancient components-enamel, dentine, and bone. Cartilage, on the other hand, provided the basis for the second vertebrate skeletal system, the endoskeleton (Smith and Hall, 1990; Hall, 1998a,b). some invertebrate skeletal tissues have surprisingly bone-like features. Examples include chondrocytes interconnected by cell processes in cephalopod cartilages (Cole and Hall, 2004a,b), and the calcium phosphate layer in the shells of brachiopods (Rodland et al., 2003). However, neither bone nor mineralized cartilage have been found in invertebrates. Editors notes: TODO - develops_from skeletal tissue UBERON:0004770 Anatomical system that consists of all the joints of the body. EMAPA:35150 FMA:23878 MA:0003007 VSAO:0000181 joint system set of all joints of body set of all joints set of joints of body articular system UBERON:0004807 An epithelium that is part of a respiratory system. respiratory system epithelium UBERON:0005057 An organ that is part of a immune system. immune organ UBERON:0005169 Connective tissue between the cellular elements of a structure. interstitial tissue UBERON:0005215 The interstitial compartment of the kidney, comprising the extravascular intertubular spaces of the renal parenchyma, with their attendant cellular elements and extracellular substances, bounded on all sides by epithelial and vascular basement membranes. kidney interstitium UBERON:0005291 A portion of tissue that is part of an embryo. embryonic tissue UBERON:0005384 An epithelium that lines the nasal cavity. nasal cavity epithelium UBERON:0005616 Arteries which arise from the abdominal aorta and distribute to most of the intestines. mesenteric artery UBERON:0005769 An acellular membrane that is part of the epithelium, lies adjacent to the epithelial cells, and is the fusion of the the basal lamina and the reticular lamina. basement membrane of epithelium UBERON:0006314 Liquid components of living organisms. includes fluids that are excreted or secreted from the body as well as body water that normally is not. fluid FMA:280556 GAID:266 MESH:D001826 galen:BodyFluid body fluid bodily fluid UBERON:0006524 System pertaining to a bronchus and alveoli. alveolar system UBERON:0006841 Vein that is central to a lobule in the liver. central vein terminal branch of hepatic vein terminal hepatic venule vena centralis (hepar) central vein of liver UBERON:0007023 A multicellular organism that existence_ends_with a post-juvenile adult stage and existence_starts_with a post-juvenile adult stage. adult organism UBERON:0007221 Of or pertaining to the period of time immediately following birth, or to the newborn. neonate stage UBERON:0007222 HsapDv:0000093 NCIT:C16268 NIF_Organism:birnlex_691 elderly elderly stage geriatric stage late adult stage UBERON:0007798 Anatomical system that consists of all blood and lymph vessels. consider merging with vasculature The cardiovascular and lymphatic systems, collectively[ncithesaurus:Vascular_System]. BTO:0001085 CALOHA:TS-2053 EHDAA2:0004520 EMAPA:35905 MA:0002718 UMLS:C0489903 Gefaesssystem@ge vascular system UBERON:0008346 An epithelium that is part of a duodenum. duodenal epithelium UBERON:0008946 A parenchyma that is part of a lung pulmonary parenchyma lung parenchyma UBERON:0008998 System pertaining to blood vessels in the brain. vasculature of brain UBERON:0009566 A submucosa that is part of a intestine. intestinal submucosa UBERON:0009773 A renal tubule is a tube that filters, re-absorbs and secretes substances to rid an organism of waste and to play a role in fluid homeostasis. renal tubule UBERON:0010000 An anatomical structure that has more than one cell as a part. CARO:0010000 FBbt:00100313 multicellular structure multicellular anatomical structure UBERON:0010210 A semisolid gelatinous mass of coagulated blood that consists of red blood cells, white blood cells, and platelets entrapped in a fibrin network. coagulated blood fibrin clot thrombus blood clot UBERON:0011216 A subdivision of an anatomical system. FBbt:00007330 FMA:67509 http://www.snomedbrowser.com/Codes/Details/91690000 organ system subdivision UBERON:0013686 An anatomical space which is the lumen of some anatomical conduit and connects two or more spaces together [FMA,modified]. anatomical conduit space UBERON:0013756 A blood that is part of a vein. FMA:83067 blood in vein portion of venous blood venous blood venous blood UBERON:0013765 Any of the organs or elements that are part of the digestive system. Examples: tongue, esophagus, spleen, crop, lunge feeding organ, tooth elements. digestive organ digestive system organ gastrointestinal system digestive system element UBERON:0014892 A muscle organ that consists of skeletal muscle tissue ensheathed in epimysium, that develops from myotome and that is innervated by some somatic motor neuron. Skeletal muscles are typically attached (via a tendon) to a bone but there are exceptions (e.g. intrinsic tongue muscles). skeletal muscle AAO:0011099 BTO:0001103 CALOHA:TS-0933 EFO:0000888 EHDAA:5035 EHDAA:5043 EHDAA:5978 EHDAA:5984 EMAPA:35988 EV:0100377 GAID:141 MA:0003148 MAT:0000302 MESH:D018482 MIAA:0000302 OpenCyc:Mx4rv2kf-5wpEbGdrcN5Y29ycA TAO:0005277 VHOG:0000319 XAO:0000174 ZFA:0005277 skeletal muscle organ UBERON:0015129 Visceral intrapericardial fat contiguous with the myocardial surface. epicardial fat UBERON:0015480 The hepatic artery proper (also proper hepatic artery), arises from the common hepatic artery and runs alongside the portal vein and the common bile duct to form the portal triad. The hepatic artery proper gives off a small supraduodenal artery to the duodenal bulb. Then the right gastric artery comes off and runs to the left along the lesser curvature of the stomach to meet the left gastric artery, which is a branch of the celiac trunk. It subsequently gives off the cystic artery, which feeds the gallbladder, before bifurcating into the right and left hepatic arteries. Of note, the right and left hepatic arteries may demonstrate variant anatomy. A replaced right hepatic artery may arise from the superior mesenteric artery (SMA) and a replaced left hepatic artery may arise from the left gastric artery. http://en.wikipedia.org/wiki/Hepatic_artery_proper hepatic artery proper UBERON:0015481 A hepatic artery that is part of a left lobe of liver. FMA:14779 left branch of hepatic artery left part of hepatic artery proper ramus sinister (arteria hepatica propria) left hepatic artery http://upload.wikimedia.org/wikipedia/commons/a/a3/Gray1087-liver.png UBERON:0015482 A hepatic artery that is part of a right lobe of liver. right hepatic artery UBERON:0015796 A liver blood vessel that is part of a liver. liver blood vessel UBERON:0016535 A white matter of cerebral lobe that is part of a occipital lobe. white matter of occipital lobe UBERON:0018241 A life cycle stage that starts at completion of development and growth of the sexually mature adult animal, and ends before senescence. adulthood stage prime adult stage UBERON:0018674 An interconnected tubular multi-tissue structure that contains fluid that is actively transported around the heart. heart vasculature UBERON:0034919 The stage of being no more dependent of the nest and/or from caregivers for subsistence while having not reach sexual maturity. juvenile stage UBERON:0034920 Nursing stage that follows the neonate stage in mammals and ends at weaning. infant stage UBERON:0034925 A collection of anatomical structures that are alike in terms of their morphology or developmental origin. resolve if this should be a subclass of disconnected anatomical group. Some collections (e.g. the skeleton or skull) are arguably connected anatomical collection UBERON:0035552 A blood vessel carrying deoxygenated blood far beneath the skin usually accompanying an artery. deep vein UBERON:0035965 blood vessel wall wall of blood vessel UBERON:0035966 The perforated part of the sclera through which pass the axons of the retinal ganglion cells. scleral lamina cribrosa UO:0000001 length unit UO:0000002 mass unit UO:0000003 time unit UO:0000008 m metre meter UO:0000010 second UO:0000016 millimetre mm millimeter UO:0000031 min minute UO:0000236 image resolution unit UO:0000239 spatial resolution unit UO:0000243 ipm pixels per millimetre pixels per millimeter UO:0010066 kilometre km kilometer VO:0000001 A vaccine is a processed material with the function that when administered, it prevents or ameliorates a disorder in a target organism by inducing or modifying adaptive immune responses specific to the antigens in the vaccine. Vaccine VO:0000002 a process of administering substance in vivo that involves in adding a vaccine into a host (e.g., human) in vivo with the intent to invoke a protective or therapeutic adaptive immune response. vaccination VO:0000609 A vaccine that targets against a viral disease. viral vaccine VO:0001274 a role of host that contains vaccine. It is a role that inheres in an organism that is the target of a vaccine administration (vaccination process). vaccine host role VO:0004897 A vaccine against coronavirus infection coronavirus vaccine VO:0004908 SARS-CoV-2 vaccine COVID-19 vaccine VO:0004994 A SARS-CoV-2 trimeric S protein subunit vaccine. PMID:32887954 PMID:33340022 https://clinicaltrials.gov/ct2/show/NCT04405908 SCB-2019 vaccine PMID:32887954 Table 2 Preclinical data: Information released suggesting induction of neutralizing antibodies in multiple animal species PMID:33340022 Protein subunit Ectodomain of wild-type S in-frame fusion to trimer-tag Clover Biopharmaceuticals, with GSK and Dynavax, China Induction of S-trimer-binding antibodies and nAbs in mice and NHPs; induction of high TH1 cell responses but low TH2 cell responses in mice VO:0005141 A SARS-CoV-2 whole virus vaccine made from a purified inactivated SARS-CoV-2 virus. PMID:32376603 PMID:32887954 PMID:32967006 PMID:33123165 CoronaVac vaccine PiCoVacc vaccine PMID:32887954 It protects rhesus macaques against SARS-CoV-2, with reduced viral titres and immunopathology associated with antibodies to S protein and nucleocapsid. PMID:32967006 Very recently, Sinovac reported results from a randomized, double-blind, placebo-controlled phase II trial (NCT04352608) of the inactivated vaccine CoronaVac (Fig. 3c; the name PiCoVacc was used in the paper describing the NHP results, Table 1) in 600 healthy adults (18–59 years of age). It was found that individuals between 18 and 39 years old had notably higher antibody responses than older individuals, suggesting that perhaps higher doses or different adjuvants might be needed for the latter group. PMID:33123165 An alum adjuvanted purified formaldehyde inactivated whole virus vaccine developed by Sinovac Biotech., called PiCoVacc, has been shown to be immunogenic in mice, rats and non-human primates. It induced nAbs to both vaccine and non-vaccine strains and provided partial or complete protection of macaques in challenge studies and has now entered human clinical trials in China (Table 2). VO:0005143 A SARS-CoV-2 RNA vaccine made of self-coding RNA encoding SARS-CoV-2 spike protein encapsulated within a lipid nanoparticle. PMID:32647131 PMID:32887954 PMID:33340022 LNP-nCoVsaRNA PMID:32887954 Table 2 Preclinical data: table 2 Published report showing induction of neutralizing antibodies and TH1 cell responses in mouse models PMID:33340022 RBD Protein subunit (Baculovirus/Sf9) RBD (residues 319–545) West China Hospital, Sichuan University, China Induction of RBD-specific IgG and nAbs in mice, rabbits and NHPs; induction of both TH1 and TH2 cell responses in mice VO:0005144 A SARS-CoV-2 vaccine made of self-coding RNA encoding SARS-CoV-2 spike protein encapsulated within a lipid nanoparticle. PMID:32450106 PMID:32702299 PMID:32887954 PMID:33123165 PMID:33340022 Ad5-nCoV vaccine PMID:32702299 RBD-specific ELISA antibody responses induced by the Ad5-vectored COVID-19 vaccine were detected from day 14 onwards, with GMTs of 94·5 (95% CI 80·5–110·8) and 85·1 (66·0–109·7) in the 1×1011 and 5×1010 viral particles dose groups, respectively (figure 2). Both vaccine doses induced significant neutralising antibody responses to live SARS-CoV-2, with GMTs of 19·5 (95% CI 16·8–22·7) and 18·3 (14·4–23·3) in participants in the 1 × 1011 and 5 × 1010 viral particles dose groups, respectively, at day 28 post vaccination (figure 2). Ad5-vectored COVID-19 vaccine induced significant SARS-CoV-2 spike glycoprotein-specific IFNgamma-ELISpot responses in 227 (90%, 95% CI 85–93) of 253 participants receiving the 1×1011 viral particles dose, and 113 (88%, 81–92) of 129 participants receiving the 5 × 1010 viral particles dose at day 28 (figure 3). Significant increases of post-vaccination T-cell responses in terms of spot-forming cells were observed both in participants with high and low pre-existing neutralising antibody at day 28. PMID:32887954 Whereas the highest dose generated unacceptable toxicity and was dropped from the phase II study, the smaller doses induced S protein-specific neutralizing antibodies in only 50% of the vaccine recipients. The phase II study largely reaffirms the phase I observations that, although the vaccine induces both antibody and T cell responses, its potency is reduced by pre-existing immunity to Ad5, particularly in elderly participants. PMID:33123165 The three in clinical trials include CanSino’s Ad5-nCoV, Janssen’s Ad26COVS1 and Gamelaya’s Ad26-based Gam-COVID-Vac Lyo vaccine (Table 2). All three encode the S protein. The Ad5-nCoV randomized, double-blind, placebo-controlled phase 2 trial results involving 603 volunteers ≥18 years of age showed >95% seroconversion by RBD-ELISA, but only 59% seroconversion of nAb responses in the higher dose group and 47% in the lower dose group after a single immunization. Both vaccine constructs elicited T cell responses which peaked at 14 days post-immunization, as determined by interferon- gamma (IFN-γ) enzyme linked immunospot (ELISpot) assay. Intracellular staining confirmed production of IFN-γ, tumor necrosis factor (TNF) and interleukin-2 (IL-2) by both CD4+ and CD8+ T cells following Ad5-nCoV immunization, with more cytokine detected in CD4+ T cells as compared to CD8+ T cells. PMID:33340022 Virus vector (Ad5):Full-length S Induction of RBD-specific IgG and nAbs in humans; induction of TH1 cell responses VO:0005155 A SARS-CoV 2 (rSARS-CoV-2) subunit vaccine made of nanoparticle composed of a trimeric full-length SARS-CoV-2 spike glycoproteins and Matrix-M1 adjuvant. PMID:32376603 PMID:32877576 PMID:32887954 PMID:33123165 PMID:33340022 NVX-CoV2373 vaccine PMID:32887954 Table 2 Preclinical data: Unpublished information indicates high levels of S-specific neutralizing antibodies PMID:33123165 Other groups have focused on using powerful adjuvants to ensure immunogenicity, for example Novavax’s recombinant S protein SARS-CoV-2 nanoparticle vaccine, NVX-CoV2373, combined with an adjuvant called Matrix-M1TM. This is a saponin-based adjuvant that enhances APC recruitment and action and stimulates high levels of nAbs and cell-mediated immune responses. Primary phase 1 clinical trial results have just been reported from a randomized, observer-blind, placebo-controlled trial of NVX-CoV2373 conducted in 131 healthy adults (Table 2). A strong correlation was observed between nAb titers and anti-spike IgG to S protein with the adjuvanted, but not the unadjuvanted, vaccine. Levels were comparable to those in convalescent sera (r = 0.958). T cell responses measured in 16 participants showed that NVX-CoV2373/Matrix-M1 induces antigen-specific polyfunctional CD4+ T cell responses (IFN-γ, IL-2, and TNF- α) in response to spike protein stimulation; there was a strong bias toward this Th1 phenotype. PMID:33340022 Protein subunit (CHO) Full-length S with two proline substitutions (K986P and V987P) and three mutations at furin cleavage site (R682Q, R683Q and R685Q) Novavax, USA Induction of S-specific IgG and nAbs in mice, NHPs and humans, with nAb titres in humans higher than convalescent plasma; induction of high TH1 cell responses but low TH2 cell responses in mice, NHPs and humans PMID:33340022 S-2P (comprising proline substitutions at residues K986 and V987) is used as the target antigen in three gene-based vaccine candidates (mRNA vaccines by Moderna/National Institute of Allergy and Infectious Diseases (NIAID) and BioNTech/Pfizer and a recombinant Ad26 vaccine by Janssen Pharmaceutical Companies) and a protein-based candidate (by Novavax)4,86–96 (Table 1). Moreover, mutation at the cleavage sites in the S protein is also believed to stabilize the pre-fusion conformation of the S protein. S-2P in the Janssen Ad26-vectored vaccine (Ad26.COV2.S) and in the Novavax protein-based vaccine (NVX-CoV2373) contains additional mutations at the S1–S2 polybasic cleavage site from RRAR to SRAG or QQAQ to render it protease resistant, which helps to further stabilize the S protein in its pre-fusion conformation96,97. All these candidates elicited protective immunity in animal models86,87,90 and have advanced into phase III clinical trials (Table 1). In particular, a preclinical study showed that Ad26 expressing S-2P elicited higher nAb titres and better protection in NHPs than other candidates based on the wild-type S protein4. The clinical studies for the two mRNA vaccines (BNT162b2 by BioNTech/Pfizer and mRNA1273 by Moderna/NIAID) and the protein subunit vaccine, NVX-CoV2373, encouragingly showed that all these vaccines elicited both high titres of nAbs beyond the levels observed in convalescent patients and substantial T cell responses. VO:0005157 A SARS-CoV2 RNA vaccine made of lipid nanoparticle with mRNA which encodes the S-2P antigen, made of the SARS-CoV-2 glycoprotein with a transmembrane anchor and intact S1-S2 cleavage site. PMID:32663912 PMID:32756549 PMID:32887954 PMID:32967006 PMID:33123165 PMID:33340022 PMID:33378609 https://clinicaltrials.gov/ct2/show/NCT04470427 mRNA-1273 vaccine PMID:32663912 The candidate vaccine mRNA-1273 encodes the stabilized prefusion SARS-CoV-2 spike protein. Binding antibody IgG geometric mean titers (GMTs) to S-2P increased rapidly after the first vaccination, with seroconversion in all participants by day 15 (Table 2 and Fig. 2A). The 25-micro g and 100-microg doses elicited CD4 T-cell responses (Figs. S9 and S10) that on stimulation by S-specific peptide pools were strongly biased toward expression of Th1 cytokines (tumor necrosis factor alpha > interleukin 2 > interferon gamma), with minimal type 2 helper T-cell (Th2) cytokine expression (interleukin 4 and interleukin 13). The mRNA-1273 vaccine was immunogenic, inducing robust binding antibody responses to both full-length S-2P and receptor-binding domain in all participants after the first vaccination in a time- and dose-dependent fashion. Commensurately high neutralizing antibody responses were also elicited in a dose-dependent fashion. PMID:32756549 Structural studies have led to the development of mutations that stabilize Betacoronavirus spike proteins in the prefusion state, improving their expression and increasing immunogenicity. This principle has been applied to design mRNA-1273, an mRNA vaccine that encodes a SARS-CoV-2 spike protein that is stabilized in the prefusion conformation. Here we have shown that 1 μg of mRNA-1273 is sufficient to induce robust pseudovirus-neutralizing activity and CD8 T cell responses, balanced TH1–TH2 antibody isotype responses, and protection from viral replication for more than three months following a prime–boost regimen similar to the one being tested in humans. PMID:32887954 Recently published phase I clinical trial data indicate that low and medium doses of two repeated parenteral injections are generally safe and induce strong S protein-specific antibody responses and a primarily CD4+ T cell response in most trial participants. PMID:32967006 More informative, PRNT80 values with authentic SARS-CoV-2 reached 1:339.7 and 1:654.3 in the 25 micro g and 100 micro g groups (data for the 250 micro g group was not provided), which is within the range seen in convalescent samples from patients who have recovered from COVID-19. CD8+ T cell responses were detected but were low, as expected for the SARS-CoV-2 spike protein. PMID:33123165 Moderna/NIAID have published preliminary results from their phase 1 dose-ranging, safety and immunogenicity trial of 2 doses of mRNA-1273 encoding the S protein conducted in 45 healthy adults aged 18–55 years. The S protein in mRNA-1273 is stabilized in its prefusion state by 2 proline substitutions in the S2 subunit; and the lipid nanoparticle coat consists of 4 lipids. All participants developed RBD Abs by ELISA and SARS-CoV-2-specific nAbs by neutralization assay after 2 doses in the upper range of those who have recovered from COVID-19 (convalescent serum). T cell responses measured by intracellular staining for Th1 (TNF, IL-2, IFN-γ) and Th2 (IL-4, IL-13) cytokines following stimulation with an S protein peptide pool showed a Th1 cytokine bias and low-level CD8 T cell responses. PMID:33340022 LNP-mRNA Full-length S with two proline substitutions (K986P and V987P) Moderna, with National Institute of Allergy and Infectious Diseases, USA Induction of S-specific IgG and nAbs in mice, NHPs and humans, with nAb titres higher than convalescent plasma; induction of high TH1 cell responses but low TH2 cell responses in mice, NHPs and humans VO:0005158 A SARS-CoV2 recombinat vector vaccine made of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein PMID:32702298 PMID:32887954 PMID:32967006 PMID:33123165 PMID:33340022 AZD-1222 ChAdOx1 nCoV19 vaccine PMID:32702298 We did a phase 1/2, single-blind, randomised controlled trial in five trial sites in the UK of a chimpanzee adenovirus-vectored vaccine (ChAdOx1 nCoV-19) expressing the SARS-CoV-2 spike protein compared with a meningococcal conjugate vaccine (MenACWY) as control. In the ChAdOx1 nCoV-19 group, spike-specific T-cell responses peaked on day 14 (median 856 spot-forming cells per million peripheral blood mononuclear cells, IQR 493–1802; n=43). Anti-spike IgG responses rose by day 28 (median 157 ELISA units [EU], 96–317; n=127), and were boosted following a second dose (639 EU, 360–792; n=10). Immunisation with ChAdOx1 nCoV-19 results in rapid induction of both humoral and cellular immune responses against SARS-CoV-2, with increased responses after a second dose. In the ChAdOx1 nCoV-19 group, antibodies against SARS-CoV-2 spike protein peaked by day 28 (median 157 ELISA units [EU], IQR 96–317; n=127) and remained elevated to day 56 (119 EU, 70–203; n=43) in participants who received only one dose, and increased to a median of 639 EU (360–792) at day 56 in the ten participants who received a booster dose (figure 3). Similar increases in serum antibody levels to both the spike protein and the receptor binding domain by day 28 and after a booster dose were observed when measured by MIA (appendix p 16). Interferon-gamma ELISpot responses against SARS-CoV-2 spike peptides peaked at 856 spot-forming cells per million peripheral blood mononuclear cells (IQR 493–1802; n=43) at day 14, declining to 424 (221–799; n=43) by day 56 after vaccination (figure 6). Adenovirus-vectored vaccines are known to induce strong cellular immunity and ChAdOx1 nCoV-19 vaccination resulted in marked increases in SARS-CoV-2 spike-specific effector T-cell responses as early as day 7, peaking at day 14 and maintained up to day 56 as expected with adenoviral vectors. PMID:32887954 A recently reported phase I/II study shows its safety and the induction of potent neutralizing antibody and T cell responses following a single parenteral injection, which are boosted further by a second homologous vaccination. PMID:32967006 Cellular immunity peaked at day 14, with 856 SFU per 106 cells, and decreased to 424 SFU by day 56. PMID:33123165 Neutralization titers were comparable to those observed in convalescent plasma from people who had recovered from COVID-19. Both vaccine constructs elicited T cell responses which peaked at 14 days post-immunization, as determined by interferon- gamma (IFN-γ) enzyme linked immunospot (ELISpot) assay. PMID:33340022 Virus vector (ChAdOx1) Full-length S University of Oxford, with AstraZeneca, UK Induction of S-specific IgG and nAbs in mice and NHPs; induction of high TH1 cell responses but low TH2 cell responses in mice; induction of S-specific IgG and nAbs in humans, with nAb titres similar to convalescent plasma VO:0005159 A SARS-CoV-2 recombinant viral vector vaccine composed of Ad26 vector expressing S protein. PMID:32731257 PMID:33123165 PMID:33340022 Ad26COVS1(JNJ-78436735) PMID:33123165 The three in clinical trials include CanSino’s Ad5-nCoV, Janssen’s Ad26COVS1 and Gamelaya’s Ad26-based Gam-COVID-Vac Lyo vaccine (Table 2). All three encode the S protein. PMID:33340022 Virus-vectored (Ad26) Full-length S with two proline substitutions (K986P and V987P) and two mutations at furin cleavage site (R682S and R685G) J anssen Pharmaceutical Companies, USA Induction of RBD-specific IgG and nAbs in hamsters and NHPs; higher nAb titres induced by S-2P-based vaccine rather than by wild-type S in NHPs; induction of high TH1 cell responses but low TH2 cell responses in NHPs VO:0005160 A SARS-CoV-2 inactivated whole virus vaccine that is developed by the Wuhan Institute of Biological Products. PMID:32789505 PMID:33123165 COVID-19 inactivated virus vaccine by Wuhan Institute of Biological Products PMID:33123165 The China National Pharmaceutical Group (Sinopharm) have also developed inactivated whole virus vaccines with the Wuhan Institute of Biological Products and Beijing Institute of Biological Products which are currently in phase 3 clinical trials. The Wuhan vaccine has been shown to be safe and immunogenic in a randomized, double-blind, placebo-controlled phase 1/2 trial, which recently reported interim results. Reasonable geometric mean anti-SARS-CoV-2 nAb titers (206–316) in 50% plaque reduction neutralization assays were induced at 14 days post- immunization. The vaccine did not appear to cause changes in serum innate (IL-1β, IL-6, IL-8, TNF-β), Th1 [IL-2, IL-12(p70), IFN-γ, TNF-α], Th2 (IL-4, IL-5, IL-10), or Th17 (IL-17, IL- 21) cytokines, although formal statistical analysis of these data has not been reported. VO:0005161 A SARS-CoV-2 mRNA vaccine made of lipid nanoparticle-encapsulated mRNA (mRNA-LNP) encoding the receptor binding domain (RBD) of SARS-CoV-2 PMID:32795413 PMID:32887954 ARCoV vaccine PMID:32887954 Table 2 Preclinical data: Information released suggesting induction of neutralizing antibodies in mice and NHPs VO:0005162 A SARS-CoV-2 plasmid DNA vaccine that encodes the envelope protein. PMID:32800805 PMID:32887954 ZyCoV-D vaccine PMID:32887954 Table 2 Preclinical data: Information released to indicate immune responses in several animal species VO:0005163 A SARS-CoV-2 recombinant viral vector vaccine composed of Ad26 and Ad5 vectors expressing S protein that lyophilised. PMID:32887954 PMID:32896291 PMID:33123165 Sputnik V Gam-Covid-Vac Lyo PMID:32887954 Table 2 PMID:33123165 The three in clinical trials include CanSino’s Ad5-nCoV, Janssen’s Ad26COVS1 and Gamelaya’s Ad26-based Gam-COVID-Vac Lyo vaccine (Table 2). All three encode the S protein. VO:0005164 A SARS-CoV-2 investigational vaccine comprising a self-replicating (replicon) mRNA that encodes for the prefusion spike protein of 2019-nCoV formulated in a lipid nanoparticle PMID:32973505 ARCT-021 vaccine VO:0005166 A SARS-CoV-2 inactivated whole virus vaccine that produced in Vero cells that is developed by the Beijin Institute of Biological Products. ChiCTR2000032459, ChiCTR2000034780 COVID-19 inactivated virus vaccine by Beijing Institute of Biological Products VO:0005167 A SARS-CoV-2 inactivated whole virus vaccine that is developed by the Chinese Academy of Medical Sciences. PMID:32376603 COVID-19 inactivated virus vaccine by Chinese Academy of Medical Science VO:0005170 A SARS-CoV-2 DNA vaccine experessing SARS-CoV-2 protein NCT04445389 PMID:32887954 GX19 COVID19 Vaccine PMID:32887954 Table 2 VO:0005172 A DNA vaccine that expresses S protein from the pGX9501 vector PMID:32433465 PMID:32887954 PMID:33123165 INO-4800 vaccine PMID:32887954 Two repeated injections of an S protein-expressing plasmid DNA vaccine resulted in robust protective immunity in rhesus macaques. PMID:33123165 Inovio Pharmaceuticals is testing their CELLECTRA electroporation i.d. delivery device to administer their S protein-based DNA plasmid vaccine INO-4800 which induces nAbs and T cells in mice and guinea pigs (Table 2). VO:0005198 COVID-19 mRNA vaccine VO:0005199 COVID-19 recombinant viral vector vaccine VO:0005200 COVID-19 recombinant adenoviral vector vaccine VO:0005201 COVID-19 inactivated vaccine VO:0005203 COVID-19 DNA vaccine VO:0005204 COVID-19 live attenuated vaccine Any variation in the form, structure or composition of the mature male gamete, which merges with an oocyte to create a fertilized embryo copared to control (Wormatlas). Any variation in the form, structure or composition of the mature male gamete, which merges with an oocyte to create a fertilized embryo copared to control (Wormatlas). sperm morphology abnormal C_elegans_phenotype_ontology WBPhenotype:0000388 sperm morphology variant WBPhenotype:0000388 Any variation in the form, structure or composition of the mature male gamete, which merges with an oocyte to create a fertilized embryo copared to control (Wormatlas). WB:WBPerson2021 WB:WBPerson557 WBPhenotype:0000533 Any variation in the form or composition of the basic structural and functional unit of all organisms compared to control. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope. nematode cell morphology variant WBPhenotype:0000886 Animals exhibit variations compared to a given control. nematode phenotype WBPhenotype:0000900 Animals exhibit variations in any physical or chemical process required for the muscle cell to carry out its normal functions or activities or be able to perceive and respond to stimuli, compared to control animals. muscle cell physiology variant Haploid female germ cells (oocytes) exhibit variations in their overall structure, appearance or contents compared to control. Haploid female germ cells (oocytes) exhibit variations in their overall structure, appearance or contents compared to control. oocyte morphology abnormal C_elegans_phenotype_ontology WBPhenotype:0001260 oocyte morphology variant WBPhenotype:0001260 Haploid female germ cells (oocytes) exhibit variations in their overall structure, appearance or contents compared to control. WB:WBPaper00001883 WB:WBPerson2021 Any variation in the form or composition of specialized cell types, compared to control. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope. Any variation in the form or composition of specialized cell types, compared to control. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope. C_elegans_phenotype_ontology WBPhenotype:0002108 nematode cell type morphology variant WBPhenotype:0002108 Any variation in the form or composition of specialized cell types, compared to control. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope. WB:WBPaper00041129 WB:WBPerson2987 An anatomical entity of the nematode Caenorhabditis elegans. An anatomical entity of the nematode Caenorhabditis elegans. worm_anatomy WBbt:0000100 C. elegans anatomical entity WBbt:0000100 An anatomical entity of the nematode Caenorhabditis elegans. WB:WBPerson2987 WBbt:0003681 LINKOUT::WORMATLAS::<http://wormatlas.org/ver1/handbook/alimentary/alimentary1.htm#generalinfopharynx> esophagus C. elegans pharynx WBbt:0003732 cell of epithelium, the layer of cells that cover the external surface of an organism as well as forming an inner lining between the tissues and organs of that organism and the external environment. In C. elegans epithelial cells include epithelium of the alimentary tract, intestinal cells, hypodermis, interfacial cells and somatic gonad cells. epithelium C. elegans epithelial cell a collection of cells or cell groups that collectively perform a function a collection of cells or cell groups that collectively perform a function worm_anatomy WBbt:0003760 C. elegans organ WBbt:0003760 a collection of cells or cell groups that collectively perform a function WB:rynl WBbt:0003810 Embryonic founder cell lineage name: P0.ppa C WBbt:0004015 Embryonic founder cell AB blastomere lineage name: P0.a AB a cellular object that consists of subcellular components, expresses genes or functions. a cellular object that consists of subcellular components, expresses genes or functions. WBbt:0003730 CL:0000000 worm_anatomy Cell type WBbt:0004017 C. elegans Cell WBbt:0004017 a cellular object that consists of subcellular components, expresses genes or functions. WB:rynl WBbt:0004421 Embryonic founder cell of germ line P4 P4' lineage name: P0.pppp Psub4 WBbt:0004422 Single cell zygote P0 WBbt:0004458 Embryonic founder cell lineage name: P0.paa MS WBbt:0004534 Excretory socket cell, links duct to hypodermis exc socket excretory pore cell lineage name: G2.p excretory socket cell WBbt:0004540 cell that forms the duct of the excretory system. excretory duct cell WBbt:0004575 Germ line precursor cell C.elegans Z3 WBbt:0004804 Embryonic founder cell lineage name: P0.pap E WBbt:0004873 Embryonic founder cell lineage name: P0.pppa D organ producing either sperm or ova. organ producing either sperm or ova. worm_anatomy WBbt:0005175 C. elegans gonad WBbt:0005175 organ producing either sperm or ova. ISBN:0140512888 organ in hermaphrodite animal that produces both ova and sperm. organ in hermaphrodite animal that produces both ova and sperm. worm_anatomy ovotestis WBbt:0005178 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/reproductivesystem/reproductivesystem1.htm> C. elegans hermaphrodite gonad WBbt:0005178 organ in hermaphrodite animal that produces both ova and sperm. WB:rynl cuticle-lined lumenal region surrounded by pharyngeal epithelium, situated at the anterior end of pharynx. cuticle-lined lumenal region surrounded by pharyngeal epithelium, situated at the anterior end of pharynx. worm_anatomy WBbt:0005255 C. elegans buccal cavity WBbt:0005255 cuticle-lined lumenal region surrounded by pharyngeal epithelium, situated at the anterior end of pharynx. WB:rynl WBPaper:00038216 an accordion-like tube that contains sperm and is the site of oocyte fertilization. an accordion-like tube that contains sperm and is the site of oocyte fertilization. WBbt:0005319 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/reproductivesystem/reproductivesystem1.htm#Thespermatheca> C. elegans spermatheca WBbt:0005319 an accordion-like tube that contains sperm and is the site of oocyte fertilization. WBPaper:00038216 That portion of the male reproductive tract, through which sperm are delivered to the proctodeum and then the cloaca in the tail. Thus that portion which is distal to the testis, made of a total of 30 cells. That portion of the male reproductive tract, through which sperm are delivered to the proctodeum and then the cloaca in the tail. Thus that portion which is distal to the testis, made of a total of 30 cells. WBPaper:00038216 worm_anatomy gon_male_vdef sperm duct WBbt:0005337 C. elegans vas deferens WBbt:0005337 That portion of the male reproductive tract, through which sperm are delivered to the proctodeum and then the cloaca in the tail. Thus that portion which is distal to the testis, made of a total of 30 cells. WB:rynl WBPaper:00038216 openning of the rectum openning of the rectum WBbt:0005335 WB:rynl worm_anatomy anus interface WBbt:0005364 C. elegans anus WBbt:0005364 openning of the rectum WB:rynl spermatheca in anterior gonad arm. spermatheca in anterior gonad arm. worm_anatomy gon_herm_spth_A WBbt:0005368 C. elegans anterior spermatheca WBbt:0005368 spermatheca in anterior gonad arm. WB:rynl WBbt:0005374 Anterior lobe of the bi-lobbed hermaphrodite gonad. C. elegans anterior gonad arm worm_anatomy WBbt:0005437 C. elegans pharyngeal nerve process WBbt:0005437 WBbt:0005440 The pharyngeal nervous system is composed of 20 pharyngeal neurons which lie completely within the pharynx. C. elegans pharyngeal nervous system A set of three longitudinal nerves (I1L, NSML and M2L) running along the anterior/posterior axis within the pharynx, each lying within a narrow groove created between syncytial pairs of muscles. One nerve lies dorsally, in close apposition to the dorsal gland duct, while the other two nerves lie subventrally. A set of three longitudinal nerves (I1L, NSML and M2L) running along the anterior/posterior axis within the pharynx, each lying within a narrow groove created between syncytial pairs of muscles. One nerve lies dorsally, in close apposition to the dorsal gland duct, while the other two nerves lie subventrally. worm_anatomy WBbt:0005441 C. elegans pharyngeal nerve WBbt:0005441 A set of three longitudinal nerves (I1L, NSML and M2L) running along the anterior/posterior axis within the pharynx, each lying within a narrow groove created between syncytial pairs of muscles. One nerve lies dorsally, in close apposition to the dorsal gland duct, while the other two nerves lie subventrally. WBPaper:00038216 spermatheca in posterior gonad arm. spermatheca in posterior gonad arm. worm_anatomy gon_herm_spth_P WBbt:0005462 C. elegans posterior spermatheca WBbt:0005462 spermatheca in posterior gonad arm. WB:rynl Association of cells with a common embryological origin or pathway and similar structure and function. Usually, cells of a tissue are contiguous at cell membranes and may be of one or more types. Tissues aggregate to form organs. Association of cells with a common embryological origin or pathway and similar structure and function. Usually, cells of a tissue are contiguous at cell membranes and may be of one or more types. Tissues aggregate to form organs. CARO:0000043 ISBN:0-14-051288-8 WB:rynl worm_anatomy WBbt:0005729 C. elegans Tissue WBbt:0005729 Association of cells with a common embryological origin or pathway and similar structure and function. Usually, cells of a tissue are contiguous at cell membranes and may be of one or more types. Tissues aggregate to form organs. ISBN:0-14-051288-8 WB:rynl WBbt:0005730 lies within the body wall, in close relation to nervous system and excretory system. lies within the body wall, in close relation to nervous system and excretory system. C. elegans epithelial system lies within the body wall, in close relation to nervous system and excretory system. WBPaper:00038216 worm_anatomy WBbt:0005731 C. elegans rectal lumen WBbt:0005731 Anatomical structures that exist outside of cells; non-cellular. Anatomical structures that exist outside of cells; non-cellular. CARO:0000040 WB:pws worm_anatomy WBbt:0005732 C. elegans extracellular component WBbt:0005732 Anatomical structures that exist outside of cells; non-cellular. WB:rynl WBbt:0005735 Complement of nervous tissue (neurones, nerves, receptors and support cells) serving to detect, relay and coordinate information about an animal's internal and external environments and to initiate and integrate its effector responses and activities. LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/MoW_built0.92/nervous_system.html> C. elegans nervous system WBbt:0005736 C. elegans excretory system region of the body by which tissues, cells or cell parts are classified region of the body by which tissues, cells or cell parts are classified worm_anatomy WBbt:0005738 C. elegans body region WBbt:0005738 region of the body by which tissues, cells or cell parts are classified WBPaper:00038216 anterior-most body region containing the pharynx. anterior-most body region containing the pharynx. worm_anatomy WBbt:0005739 C. elegans head WBbt:0005739 anterior-most body region containing the pharynx. WB:rynl body region posterior to the head and anterior to the tail body region posterior to the head and anterior to the tail worm_anatomy WBbt:0005740 C. elegans midbody WBbt:0005740 body region posterior to the head and anterior to the tail WB:rynl posterior region, from rectum to the end posterior region, from rectum to the end worm_anatomy WBbt:0005741 C. elegans tail WBbt:0005741 posterior region, from rectum to the end WB:rynl exterior tube of two concentric tubes that make up the body, includes the epidermal cells and the attached neurons and muscles. exterior tube of two concentric tubes that make up the body, includes the epidermal cells and the attached neurons and muscles. worm_anatomy WBbt:0005742 C. elegans body wall WBbt:0005742 exterior tube of two concentric tubes that make up the body, includes the epidermal cells and the attached neurons and muscles. WB:Paper00000978 WB:rynl inner tube of two concentric tubes that make up the body inner tube of two concentric tubes that make up the body worm_anatomy WBbt:0005743 C. elegans digestive tract WBbt:0005743 inner tube of two concentric tubes that make up the body WB:rynl worm_anatomy WBbt:0005744 C. elegansreproductive tract WBbt:0005744 A fluid-filled space enclosed on the outside by the basal laminae of the bodywall tissues, principally those of the bodywall muscles and the hypodermis. Within this space the digestive tract and reproductive tract lie separately, each enclosed by its own basal lamina. Intercellular signals, nutrients and waste products can travel between all tissues bordering this space. A fluid-filled space enclosed on the outside by the basal laminae of the bodywall tissues, principally those of the bodywall muscles and the hypodermis. Within this space the digestive tract and reproductive tract lie separately, each enclosed by its own basal lamina. Intercellular signals, nutrients and waste products can travel between all tissues bordering this space. WBPaper:00038216 worm_anatomy body cavity WBbt:0005745 C. elegans pseudocoelom WBbt:0005745 A fluid-filled space enclosed on the outside by the basal laminae of the bodywall tissues, principally those of the bodywall muscles and the hypodermis. Within this space the digestive tract and reproductive tract lie separately, each enclosed by its own basal lamina. Intercellular signals, nutrients and waste products can travel between all tissues bordering this space. WBPaper:00038216 WBbt:0005746 intergrated group of organs, performing one or more unified functions. intergrated group of organs, performing one or more unified functions. C. elegans organ system intergrated group of organs, performing one or more unified functions. ISBN:0-14-051288-8 WBbt:0005747 C. elegans reproductive system WBbt:0005748 C. elegans alimentary system WBbt:0005749 C. elegans coelomic system anatomical or cell objects that exist in only one, male or hermaphrodite, sex. anatomical or cell objects that exist in only one, male or hermaphrodite, sex. worm_anatomy WBbt:0005752 C. elegans sex specific entity WBbt:0005752 anatomical or cell objects that exist in only one, male or hermaphrodite, sex. WB:rynl a rigid external coating which is secreted by the hypodermis, seam and some transitional epithelial cells which covers the outer body, the major openings into the body cavity from the exterior, and two large sensory bristles, the male spicules. The cuticle of the spicules, the hook, and of some portions of the spicule channels is especially rigid and is probably sclerotized. Similar sclerotic features are occasionally noted in the ventral surface of the male tail fan. a rigid external coating which is secreted by the hypodermis, seam and some transitional epithelial cells which covers the outer body, the major openings into the body cavity from the exterior, and two large sensory bristles, the male spicules. The cuticle of the spicules, the hook, and of some portions of the spicule channels is especially rigid and is probably sclerotized. Similar sclerotic features are occasionally noted in the ventral surface of the male tail fan. WBPaper:00038216 worm_anatomy exoskeleton WBbt:0005755 C. elegans cuticle WBbt:0005755 a rigid external coating which is secreted by the hypodermis, seam and some transitional epithelial cells which covers the outer body, the major openings into the body cavity from the exterior, and two large sensory bristles, the male spicules. The cuticle of the spicules, the hook, and of some portions of the spicule channels is especially rigid and is probably sclerotized. Similar sclerotic features are occasionally noted in the ventral surface of the male tail fan. WBPaper:00038216 WBPaper:00038216 worm_anatomy ECM basement membrane extracellular matrix lamina WBbt:0005756 C. elegans basal lamina WBbt:0005756 cells or anatomical parts specific to the hermaphrodite sex cells or anatomical parts specific to the hermaphrodite sex worm_anatomy WBbt:0005758 C. elegans hermaphrodite-specific anatomical entity WBbt:0005758 cells or anatomical parts specific to the hermaphrodite sex WB:rynl WBbt:0005760 Part of the nervous system that lies completely outside the pharynx. C. elegans somatic nervous system A group of six equivalent cells forms a tightly constructed 'valve' that links the posterior bulb of the pharynx to the anterior four cells of the intestine. These six cells comprise a small epithelial channel with a cuticular lining in continuity with the pharyngeal cuticle and link the lumen of the pharynx to the large lumen of the anterior intestine. A group of six equivalent cells forms a tightly constructed 'valve' that links the posterior bulb of the pharynx to the anterior four cells of the intestine. These six cells comprise a small epithelial channel with a cuticular lining in continuity with the pharyngeal cuticle and link the lumen of the pharynx to the large lumen of the anterior intestine. WBbt:0005435 WBPaper:00038216 worm_anatomy cardia esophago-intestinal valve pharyngeal valve pharyngo-intestinal valve WBbt:0005767 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/alimentary/alimentary1.htm#vip> pharyngeal-intestinal valve WBbt:0005767 A group of six equivalent cells forms a tightly constructed 'valve' that links the posterior bulb of the pharynx to the anterior four cells of the intestine. These six cells comprise a small epithelial channel with a cuticular lining in continuity with the pharyngeal cuticle and link the lumen of the pharynx to the large lumen of the anterior intestine. WBPaper:00038216 spatial axis spatial axis worm_anatomy WBbt:0005768 C. elegans axis WBbt:0005768 spatial axis WB:rynl anteria-posterior axis anteria-posterior axis worm_anatomy WBbt:0005769 C. elegans anterior-posterior WBbt:0005769 anteria-posterior axis WB:rynl dorsal-ventral axis dorsal-ventral axis worm_anatomy WBbt:0005770 C. elegans dorsal-ventral WBbt:0005770 dorsal-ventral axis WB:rynl left-right axis left-right axis worm_anatomy WBbt:0005771 C. elegans left-right WBbt:0005771 left-right axis WB:rynl WBbt:0005772 A chain of very large cuboidal cells forming a wide central lumen in which food arrives from the posterior pharynx, is digested, and from which waste products proceed to the rectum. Intestinal rings form in groups of two and four cells surrounding the common lumen; thus the epithelium is only one cell deep at any point, with neighboring cells firmly secured to their neighbors by apical adherens junctions. These cells have very large nuclei and many large vacuoles, yolk granules, and other inclusions; the latter increase in number and electron density as the animal ages. LINKOUT::WORMATLAS::<http://wormatlas.org/ver1/handbook/alimentary/alimentary2.htm> WBPaper:00038216 gut mesenteron C. elegans intestine The passageway in the hindgut between the posterior intestine, the rectal valve and the opening to the exterior. The passageway in the hindgut between the posterior intestine, the rectal valve and the opening to the exterior. worm_anatomy WBbt:0005773 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/alimentary/alimentary3.htm> C. elegans rectum WBbt:0005773 The passageway in the hindgut between the posterior intestine, the rectal valve and the opening to the exterior. WB:rynl WBPaper:00038216 Four processes (canals) of the excretory canal cell each contain a central collecting lumen which feeds to a central lumenal canal in the cell body; the central canal forms a specialized membrane to release fluids into the excretory duct. These five canals form a continuous H-shaped channel which extends almost the full length of the body, generally in contact with the lateral hypodermis and the pseudocoelom. Four processes (canals) of the excretory canal cell each contain a central collecting lumen which feeds to a central lumenal canal in the cell body; the central canal forms a specialized membrane to release fluids into the excretory duct. These five canals form a continuous H-shaped channel which extends almost the full length of the body, generally in contact with the lateral hypodermis and the pseudocoelom. WBPaper:00038216 worm_anatomy canal WBbt:0005775 C. elegans excretory canal WBbt:0005775 Four processes (canals) of the excretory canal cell each contain a central collecting lumen which feeds to a central lumenal canal in the cell body; the central canal forms a specialized membrane to release fluids into the excretory duct. These five canals form a continuous H-shaped channel which extends almost the full length of the body, generally in contact with the lateral hypodermis and the pseudocoelom. WBPaper:00038216 The extracellular sinus formed by the excretory duct and pore cells. The extracellular sinus formed by the excretory duct and pore cells. worm_anatomy WBbt:0005777 C. elegans excretory duct WBbt:0005777 The extracellular sinus formed by the excretory duct and pore cells. WBPaper:00038216 The outlet of the excretory sinus to the exterior environment through the cuticle, on the ventral side of the head, just behind the nerve ring. The outlet of the excretory sinus to the exterior environment through the cuticle, on the ventral side of the head, just behind the nerve ring. WBPaper:00038216 worm_anatomy pore WBbt:0005778 C. elegans excretory pore WBbt:0005778 The outlet of the excretory sinus to the exterior environment through the cuticle, on the ventral side of the head, just behind the nerve ring. WBPaper:00038216 cell line which early in development becomes differentiated from the remaining somatic cell line, and alone has the potential to undergo meiosis and form gametes. cell line which early in development becomes differentiated from the remaining somatic cell line, and alone has the potential to undergo meiosis and form gametes. worm_anatomy germline WBbt:0005784 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/reproductivesystem/reproductivesystem2.htm> C. elegans germ line WBbt:0005784 cell line which early in development becomes differentiated from the remaining somatic cell line, and alone has the potential to undergo meiosis and form gametes. ISBN:0140512888 The components of the gonad that are separate from the germline proper. In hermaphrodite, these include five tissues which are all derived from the somatic primordium : the distal tip cells, the gonadal sheath, the spermatheca, the spermatheca-uterine valve (sp-ut) and the uterus. The components of the gonad that are separate from the germline proper. In hermaphrodite, these include five tissues which are all derived from the somatic primordium : the distal tip cells, the gonadal sheath, the spermatheca, the spermatheca-uterine valve (sp-ut) and the uterus. worm_anatomy somatic germline WBbt:0005785 C. elegans somatic gonad WBbt:0005785 The components of the gonad that are separate from the germline proper. In hermaphrodite, these include five tissues which are all derived from the somatic primordium : the distal tip cells, the gonadal sheath, the spermatheca, the spermatheca-uterine valve (sp-ut) and the uterus. WB:rynl WBPaper:00038216 worm_anatomy WBbt:0005789 C. elegans pharyngeal segment WBbt:0005789 the space in the center of pharynx which allows the passage of food. the space in the center of pharynx which allows the passage of food. worm_anatomy WBbt:0005790 C. elegans pharyngeal lumen WBbt:0005790 the space in the center of pharynx which allows the passage of food. WB:rynl worm_anatomy WBbt:0005791 C. elegans intestinal lumen WBbt:0005791 WBbt:0005812 H-shaped cell associated with the excretory system, largest cell in C. elegans. exc_cell excretory canal cell lineage name: ABplpappaap LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/excretory.htm#exccanalcell> C. elegans excretory cell a large process bundle that runs along the vental mid-line extending from the ventral region of the nerve ring. a large process bundle that runs along the vental mid-line extending from the ventral region of the nerve ring. worm_anatomy ventral cord ventral cord WBbt:0005829 C. elegans ventral nerve cord WBbt:0005829 a large process bundle that runs along the vental mid-line extending from the ventral region of the nerve ring. WB:Paper00000938 ventral cord WB:Paper00000938 The shell or external calcareous covering of an egg The shell or external calcareous covering of an egg worm_anatomy WBbt:0005843 C. elegans eggshell WBbt:0005843 The shell or external calcareous covering of an egg ISBN:0198611862 WBbt:0005906 embryonic cell ABa WBbt:0005994 embryonic cell ABp WBbt:0006110 embryonic cell doi/10.1895/wormbook.1.30.2 ABal doi/10.1895/wormbook.1.30.2 During these early cleavage divisions, the three principal axes of the body plan are established. First, the anterior-posterior (AP) axis is set up in the one-cell stage, with the sperm-derived centrosome breaking the symmetry of the oocyte and initiating a sequence of events relying on maternally-contributed proteins. Second, the dorso-ventral (DV) axis becomes apparent at the transition between the two- and four-cell stage, with EMS defining the ventral side of the embryo. Third, the left-right (LR) axis is detectable at the transition between the four- and six-cell stage, with the location of two granddaughters of AB (ABal and ABpl) defining the left side of the embryo. Because the position of the mitotic spindle in animal cells determines the relative size and spatial relationship of daughter cells (reviewed in Rappaport, 1971), proper spindle positioning during these early cleavage divisions is crucial for correct segregation of cell fate determinants and cell division patterns. WBbt:0006411 embryonic cell doi/10.1895/wormbook.1.30.2 ABar doi/10.1895/wormbook.1.30.2 During these early cleavage divisions, the three principal axes of the body plan are established. First, the anterior-posterior (AP) axis is set up in the one-cell stage, with the sperm-derived centrosome breaking the symmetry of the oocyte and initiating a sequence of events relying on maternally-contributed proteins. Second, the dorso-ventral (DV) axis becomes apparent at the transition between the two- and four-cell stage, with EMS defining the ventral side of the embryo. Third, the left-right (LR) axis is detectable at the transition between the four- and six-cell stage, with the location of two granddaughters of AB (ABal and ABpl) defining the left side of the embryo. Because the position of the mitotic spindle in animal cells determines the relative size and spatial relationship of daughter cells (reviewed in Rappaport, 1971), proper spindle positioning during these early cleavage divisions is crucial for correct segregation of cell fate determinants and cell division patterns. WBbt:0006422 embryonic cell doi/10.1895/wormbook.1.30.2 ABpr http://purl.obolibrary.org/obo/WBbt_0006422 doi/10.1895/wormbook.1.30.2 During these early cleavage divisions, the three principal axes of the body plan are established. First, the anterior-posterior (AP) axis is set up in the one-cell stage, with the sperm-derived centrosome breaking the symmetry of the oocyte and initiating a sequence of events relying on maternally-contributed proteins. Second, the dorso-ventral (DV) axis becomes apparent at the transition between the two- and four-cell stage, with EMS defining the ventral side of the embryo. Third, the left-right (LR) axis is detectable at the transition between the four- and six-cell stage, with the location of two granddaughters of AB (ABal and ABpl) defining the left side of the embryo. Because the position of the mitotic spindle in animal cells determines the relative size and spatial relationship of daughter cells (reviewed in Rappaport, 1971), proper spindle positioning during these early cleavage divisions is crucial for correct segregation of cell fate determinants and cell division patterns. WBbt:0006571 embryonic cell doi/10.1895/wormbook.1.30.2 ABpl doi/10.1895/wormbook.1.30.2 During these early cleavage divisions, the three principal axes of the body plan are established. First, the anterior-posterior (AP) axis is set up in the one-cell stage, with the sperm-derived centrosome breaking the symmetry of the oocyte and initiating a sequence of events relying on maternally-contributed proteins. Second, the dorso-ventral (DV) axis becomes apparent at the transition between the two- and four-cell stage, with EMS defining the ventral side of the embryo. Third, the left-right (LR) axis is detectable at the transition between the four- and six-cell stage, with the location of two granddaughters of AB (ABal and ABpl) defining the left side of the embryo. Because the position of the mitotic spindle in animal cells determines the relative size and spatial relationship of daughter cells (reviewed in Rappaport, 1971), proper spindle positioning during these early cleavage divisions is crucial for correct segregation of cell fate determinants and cell division patterns. female genital. female genital. worm_anatomy WBbt:0006748 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/reproductivesystem/reproductivesystem3a.htm#Thevulva> C. elegans vulva WBbt:0006748 female genital. WB:rynl the most extensive region of neuropil in the animal, consists of a large toroidal bundle of processes. the most extensive region of neuropil in the animal, consists of a large toroidal bundle of processes. worm_anatomy circumpharyngeal nerve ring circumpharyngeal nerve ring WBbt:0006749 C. elegans nerve ring WBbt:0006749 the most extensive region of neuropil in the animal, consists of a large toroidal bundle of processes. WB:Paper00000938 circumpharyngeal nerve ring WB:Paper00000938 A valve tissue that connects the spermatheca and the uterus of a hermaphrodite gonad. A valve tissue that connects the spermatheca and the uterus of a hermaphrodite gonad. WBbt:0005317 spermatheca-uterus valve worm_anatomy sp-ut valve spermathecal valve WBbt:0006756 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/reproductivesystem/reproductivesystem1.htm#Thespermatheca-uterinevalve> C. elegans spermathecal-uterine junction WBbt:0006756 A valve tissue that connects the spermatheca and the uterus of a hermaphrodite gonad. WB:rynl spermathecal-uterine junction of the anterior gonad arm. spermathecal-uterine junction of the anterior gonad arm. worm_anatomy gon_herm_sujn_A WBbt:0006757 C. elegans anterior spermathecal-uterine junction WBbt:0006757 spermathecal-uterine junction of the anterior gonad arm. WB:wjc spermathecal-uterine junction of the posterior gonad arm. spermathecal-uterine junction of the posterior gonad arm. worm_anatomy gon_herm_sujn_P WBbt:0006758 C. elegans posterior spermathecal-uterine junction WBbt:0006758 spermathecal-uterine junction of the posterior gonad arm. WB:wjc The organ in which the eggs are developed and protected until laid. The organ in which the eggs are developed and protected until laid. worm_anatomy WBbt:0006760 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/reproductivesystem/reproductivesystem3a.htm#Theuterus> C. elegans uterus WBbt:0006760 The organ in which the eggs are developed and protected until laid. ISBN:0198611862 WB:rynl gonad of a male animal, produces sperm. gonad of a male animal, produces sperm. worm_anatomy WBbt:0006794 C. elegans male gonad WBbt:0006794 gonad of a male animal, produces sperm. WB:wjc WBbt:0006796 A cell, of either sex, directly concerned in the production of a new organism. C.elegans germ cell a female haploid germ cell. a female haploid germ cell. worm_anatomy ovum WBbt:0006797 C. elegans oocyte WBbt:0006797 a female haploid germ cell. WB:wjc WBbt:0006798 Male haploid germ cell. C.elegans sperm WBbt:0006799 A cell which gives rise to spermatids by meiosis. C.elegans spermatocyte WBbt:0006800 An immature sperm cell which undergoes morphogenesis to form mature, amoeboid sperm. C.elegans spermatid cell nucleus with a defined lineage. cell nucleus with a defined lineage. worm_anatomy WBbt:0006803 C. elegans Nucleus WBbt:0006803 cell nucleus with a defined lineage. WB:rynl WBbt:0006849 Germ line precursor cell C.elegans Z2 WBbt:0006850 An organ system consists of the excretory system and associated glands. An organ system consists of the excretory system and associated glands. C. elegans excretory secretory system An organ system consists of the excretory system and associated glands. WB:Paper00000536 part of male gonad that holds mature sperm, made of a total of 12 nuclei. part of male gonad that holds mature sperm, made of a total of 12 nuclei. worm_anatomy gon_male_sves WBbt:0006870 C. elegans seminal vesicle WBbt:0006870 part of male gonad that holds mature sperm, made of a total of 12 nuclei. WB:Paper00000193 WB:rynl WBbt:0006873 embryonic founder cell P2 P2' lineage name: P0.pp Psub2 WBbt:0006874 P1 embryonic founder cell P1 P1' lineage name: P0.p Psub1 WBbt:0006875 embryonic founder cell P3 P3' lineage name: P0.ppp Psub3 WBbt:0006876 embryonic cell EMS immature gonadal structure of hermaphrodite. immature gonadal structure of hermaphrodite. worm_anatomy WBbt:0006903 C. elegans developing hermaphrodite gonad WBbt:0006903 immature gonadal structure of hermaphrodite. WB:rynl body region surrounding the anus. body region surrounding the anus. worm_anatomy WBbt:0006919 C. elegans anal region WBbt:0006919 body region surrounding the anus. WB:rynl An acellular thin cuticle whip formed at the very end of the tail during embryogenesis. An acellular thin cuticle whip formed at the very end of the tail during embryogenesis. worm_anatomy WBbt:0006979 LINKOUT::WORMATLAS::<http://www.wormatlas.org/ver1/handbook/hypodermis/hypsupportother.htm#tailspikecells> C. elegans tail spike WBbt:0006979 An acellular thin cuticle whip formed at the very end of the tail during embryogenesis. WB:rynl WBPaper:00038216 WBbt:0007028 cell that exists in and is part of an embryo of C. elegans. C. elegans embryonic cell Small linear ridges running along the lateral lines of the cuticle, lengthwise along the body; these thickenings lie in register with the seam cells which likely produce them and are present in the cuticle of the L1, dauer and adult stages, but not in other larval stages. The alae are suspected to provide better traction when the animal generates a bodywave. Since the animal usually lies on its side, the alae are in perfect position to catch against the substrate. Small linear ridges running along the lateral lines of the cuticle, lengthwise along the body; these thickenings lie in register with the seam cells which likely produce them and are present in the cuticle of the L1, dauer and adult stages, but not in other larval stages. The alae are suspected to provide better traction when the animal generates a bodywave. Since the animal usually lies on its side, the alae are in perfect position to catch against the substrate. worm_anatomy alae WBbt:0007832 C. elegans cuticular ala WBbt:0007832 Small linear ridges running along the lateral lines of the cuticle, lengthwise along the body; these thickenings lie in register with the seam cells which likely produce them and are present in the cuticle of the L1, dauer and adult stages, but not in other larval stages. The alae are suspected to provide better traction when the animal generates a bodywave. Since the animal usually lies on its side, the alae are in perfect position to catch against the substrate. WB:rynl WBPaper:00038216 Anatomical structure that is an individual member of a species and consists of more than one cell. Anatomical structure that is an individual member of a species and consists of more than one cell. worm_anatomy WBbt:0007833 XREF::CARO:0000012 C. elegans organism WBbt:0007833 Anatomical structure that is an individual member of a species and consists of more than one cell. WB:rynl Multi-cellular organism that can produce both male and female gametes. Multi-cellular organism that can produce both male and female gametes. CARO:0000029 worm_anatomy hermaphroditic organism WBbt:0007849 C. elegans hermaphrodite WBbt:0007849 Multi-cellular organism that can produce both male and female gametes. CARO:0000029 Gonochoristic organism that can produce male gametes. Gonochoristic organism that can produce male gametes. CARO:0000027 worm_anatomy male organism WBbt:0007850 C. elegans male organism WBbt:0007850 Gonochoristic organism that can produce male gametes. CARO:0000027 a region around premature germline, consists of cells of pedigree Z1 and Z4, which develops to become the somatic gonad. a region around premature germline, consists of cells of pedigree Z1 and Z4, which develops to become the somatic gonad. worm_anatomy WBbt:0008366 C. elegans gonadal primordium WBbt:0008366 a region around premature germline, consists of cells of pedigree Z1 and Z4, which develops to become the somatic gonad. WB:rynl gonadal primordium in male. gonadal primordium in male. worm_anatomy WBbt:0008367 C. elegans gonadal primordium male WBbt:0008367 gonadal primordium in male. WB:rynl gonadal primordium in hermaphrodite. gonadal primordium in hermaphrodite. worm_anatomy WBbt:0008368 C. elegans gonadal primordium hermaphrodite WBbt:0008368 gonadal primordium in hermaphrodite. WB:rynl Portion of the digestive tract between the oral opening and the definitely tri-radiate beginning of the esophagus (pharynx). Portion of the digestive tract between the oral opening and the definitely tri-radiate beginning of the esophagus (pharynx). worm_anatomy WBbt:0008374 C. elegans stoma WBbt:0008374 Portion of the digestive tract between the oral opening and the definitely tri-radiate beginning of the esophagus (pharynx). ISBN:0-8391-0697-1 a structure surrounds the lumen of pharyngeal terminal bulb that is formed by folded cuticles and serves the function of grinding up food, bacteria. a structure surrounds the lumen of pharyngeal terminal bulb that is formed by folded cuticles and serves the function of grinding up food, bacteria. worm_anatomy WBbt:0008408 C. elegans grinder WBbt:0008408 a structure surrounds the lumen of pharyngeal terminal bulb that is formed by folded cuticles and serves the function of grinding up food, bacteria. WB:rynl anatomical part of the body which is involved in sexual reproduction and constitutes the reproductive system. anatomical part of the body which is involved in sexual reproduction and constitutes the reproductive system. worm_anatomy genitalia WBbt:0008422 Term definition modified from wikipedia entry. C. elegans sex organ WBbt:0008422 anatomical part of the body which is involved in sexual reproduction and constitutes the reproductive system. WB:rynl antomical structure of the male involved in sexual reproduction. antomical structure of the male involved in sexual reproduction. worm_anatomy WBbt:0008423 C. elegans male genital WBbt:0008423 antomical structure of the male involved in sexual reproduction. WB:rynl The extreme anterior portion of the body. The extreme anterior portion of the body. worm_anatomy WBbt:0008426 C. elegans nose WBbt:0008426 The extreme anterior portion of the body. WB:Paper00038216 The fluid-filled compartment inside the developing embryo at the onset of gastrulation, surrounded by the early blastomeres, into which some cells begin to migrate at gastrulation to create a multi-layered embryo. This internal space later is converted into the pseudocoelom as the embryo develops. The fluid-filled compartment inside the developing embryo at the onset of gastrulation, surrounded by the early blastomeres, into which some cells begin to migrate at gastrulation to create a multi-layered embryo. This internal space later is converted into the pseudocoelom as the embryo develops. worm_anatomy WBbt:0008427 C. elegans blastocoel WBbt:0008427 The fluid-filled compartment inside the developing embryo at the onset of gastrulation, surrounded by the early blastomeres, into which some cells begin to migrate at gastrulation to create a multi-layered embryo. This internal space later is converted into the pseudocoelom as the embryo develops. WB:Paper00038216 A hole in the ventral/posterior side of the embryo caused by the inward flow of cells during gastrulation. A hole in the ventral/posterior side of the embryo caused by the inward flow of cells during gastrulation. worm_anatomy gastrulation pore WBbt:0008428 C. elegans blastopore WBbt:0008428 A hole in the ventral/posterior side of the embryo caused by the inward flow of cells during gastrulation. WB:Paper00038216 An anatomical region of the male vas deferens that is adjacent to the seminal vesicle. An anatomical region of the male vas deferens that is adjacent to the seminal vesicle. raymond 2012-01-31T02:30:37Z worm_anatomy WBbt:0008440 C. elegans vas deferens valve region WBbt:0008440 An anatomical region of the male vas deferens that is adjacent to the seminal vesicle. WB:rynl WBPaper:00038216 WBbt:0008447 Embryonic cell which descends from the same parent cell as a germline blastomere. somatic blastomere WBbt:0008448 Embryonic cell that has the developmental potential to generate a germ cell. germline blastomere An apparatus for laying eggs of the hermaphrodite reproductive system, consists of the uterus, the uterine muscles, the vulva, the vulval muscles, and a local neuropil formed by the egg-laying neurons. An apparatus for laying eggs of the hermaphrodite reproductive system, consists of the uterus, the uterine muscles, the vulva, the vulval muscles, and a local neuropil formed by the egg-laying neurons. raymond 2012-10-30T12:29:21Z worm_anatomy WBbt:0008587 C. elegans egg-laying apparatus WBbt:0008587 An apparatus for laying eggs of the hermaphrodite reproductive system, consists of the uterus, the uterine muscles, the vulva, the vulval muscles, and a local neuropil formed by the egg-laying neurons. WB:Paper00038216 WB:rynl WBbt:0008591 A diploid immature germ cell which forms in the gonad when a spermatogonial stem cell buds off from the rachis to form a single cell that quickly enters metaphase I and divides to form secondary spermatocytes attached to a residual body. C.elegans primary spermatocyte WBbt:0008592 A haploid immature germ cell which forms in the gonad by the division of a diploid primary spermatocyte. It undergoes a second meiotic division to complete meiosis, at which time the daughter cells detach from the residual body to become spermatids. C.elegans secondary spermatocyte Gonochoristic organism that can produce female gametes. Gonochoristic organism that can produce female gametes. raymond 2013-11-11T10:03:43Z CARO:0000028 worm_anatomy WBbt:0008595 C. elegans female organism WBbt:0008595 Gonochoristic organism that can produce female gametes. CARO:0000028 The remnant the midbody from the first embryonic cell division, eventually becomes absorbed by the EMS blastomere. The remnant the midbody from the first embryonic cell division, eventually becomes absorbed by the EMS blastomere. raymond 2015-03-20T03:02:28Z GO:0030496 worm_anatomy WBbt:0008609 C. elegans midbody remnant WBbt:0008609 The remnant the midbody from the first embryonic cell division, eventually becomes absorbed by the EMS blastomere. WBPaper:00044848 WBbt:0008629 A lobe of the gonad. In a monodelphic gonad, there is one arm, whereas in a didelphic gonad, there are two arms. A lobe of the gonad. In a monodelphic gonad, there is one arm, whereas in a didelphic gonad, there are two arms. C. elegans gonad arm A lobe of the gonad. In a monodelphic gonad, there is one arm, whereas in a didelphic gonad, there are two arms. WB:rynl The nematode life-cycle stage that occurs entirely outside of a host organism. The nematode life-cycle stage that occurs entirely outside of a host organism. jl16 2015-03-19T10:42:18Z worm_development WBls:0000001 free-living nematode stage WBls:0000001 The nematode life-cycle stage that occurs entirely outside of a host organism. WB:jl The whole period of embryogenesis in the nematode Caenorhabditis elegans, from the formation of an egg until hatching. The whole period of embryogenesis in the nematode Caenorhabditis elegans, from the formation of an egg until hatching. embryo worm_development WBls:0000003 embryo Ce WBls:0000003 The whole period of embryogenesis in the nematode Caenorhabditis elegans, from the formation of an egg until hatching. WB:WBPerson2987 WB:wjc The C. elegans life stage spanning 0-350min after first cleavage at 20 Centigrade. Proliferate from 1 cell to 560 cells. From start of first cleavage until cleavage is over. The C. elegans life stage spanning 0-350min after first cleavage at 20 Centigrade. Proliferate from 1 cell to 560 cells. From start of first cleavage until cleavage is over. proliferating embryo early embryo worm_development WBls:0000004 proliferating embryo Ce WBls:0000004 The C. elegans life stage spanning 0-350min after first cleavage at 20 Centigrade. Proliferate from 1 cell to 560 cells. From start of first cleavage until cleavage is over. WB:wjc WBls:0000005 The C. elegans life stage spanning 0-100min after first cleavage at 20 Centigrade. Proliferate from 1 cell to 28 cells. From first cleavage until the start of gastrulation. blastula embryo Ce WBls:0000006 Also called zygote. -50min till 0min of first cleavage at 20 Centigrade. Contains 1 cell. 1-cell embryo fertilized egg 1-cell embryo Ce WBls:0000007 The C. elegans life stage spanning 0-20min after first cleavage at 20 Centigrade. Contains 2 cells. 2-cell embryo 2-cell embryo Ce WBls:0000008 The C. elegans life stage spanning 20-40min after first cleavage at 20 Centigrade. Contains 4 cells. 4-cell embryo 4-cell embryo Ce WBls:0000010 he C. elegans life stage spanning 100-290min after first cleavage at 20 Centigrade. Proliferate from 28 cells to 421 cells. Referring to the whole period of gastrulation gastrulating embryo Ce WBls:0000013 The C. elegans life stage spanning 290-350min after first cleavage at 20 Centigrade. Proliferate from 421 cells to 560 cells. The stage when embryo just finished gastrulation and is enclosing. enclosing embryo Ce WBls:0000014 The C. elegans life stage spanning 210-350min after first cleavage at 20 Centigrade. Proliferate from 421 cells to 560 cells. The stage before the fast cleavage of cells finishes. late cleavage stage embryo Ce The C. elegans life stage spanning 350-620min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The stage that embryo starts elongation until elongation is over. The C. elegans life stage spanning 350-620min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The stage that embryo starts elongation until elongation is over. elongating embryo mid embryo worm_development WBls:0000015 elongating embryo Ce WBls:0000015 The C. elegans life stage spanning 350-620min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The stage that embryo starts elongation until elongation is over. WB:wjc The C. elegans life stage spanning 350-390min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. Emrbyo elongation started but have not formed comma shape yet. The shape of embryo looks like a lima bean. A stage right before comma embryo. Also called lima embryo or lima bean stage. The C. elegans life stage spanning 350-390min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. Emrbyo elongation started but have not formed comma shape yet. The shape of embryo looks like a lima bean. A stage right before comma embryo. Also called lima embryo or lima bean stage. bean embryo worm_development WBls:0000016 bean embryo Ce WBls:0000016 The C. elegans life stage spanning 350-390min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. Emrbyo elongation started but have not formed comma shape yet. The shape of embryo looks like a lima bean. A stage right before comma embryo. Also called lima embryo or lima bean stage. WB:wjc The C. elegans life stage spanning 390-420min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo looks like a comma. A stage between bean embryo and 1.5-fold embryo. The C. elegans life stage spanning 390-420min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo looks like a comma. A stage between bean embryo and 1.5-fold embryo. comma embryo worm_development WBls:0000017 comma embryo Ce WBls:0000017 The C. elegans life stage spanning 390-420min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo looks like a comma. A stage between bean embryo and 1.5-fold embryo. WB:wjc The C. elegans life stage spanning 420-460min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and fold back 50%. A stage between comma embryo and 2-fold embryo. The C. elegans life stage spanning 420-460min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and fold back 50%. A stage between comma embryo and 2-fold embryo. 1.5-fold embryo worm_development WBls:0000018 1.5-fold embryo Ce WBls:0000018 The C. elegans life stage spanning 420-460min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and fold back 50%. A stage between comma embryo and 2-fold embryo. WB:wjc The C. elegans life stage spanning 460-520min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and double fold. A stage between 1.5-fold embryo and 3-fold embryo. The C. elegans life stage spanning 460-520min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and double fold. A stage between 1.5-fold embryo and 3-fold embryo. 2-fold embryo worm_development WBls:0000019 2-fold embryo Ce WBls:0000019 The C. elegans life stage spanning 460-520min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and double fold. A stage between 1.5-fold embryo and 3-fold embryo. WB:wjc The C. elegans life stage spanning 520-620min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and tripple fold. A stage between 2-fold embryo and fully-elongated embryo. Also called pretzel embryo or pretzel stage. The C. elegans life stage spanning 520-620min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and tripple fold. A stage between 2-fold embryo and fully-elongated embryo. Also called pretzel embryo or pretzel stage. 3-fold embryo worm_development WBls:0000020 3-fold embryo Ce WBls:0000020 The C. elegans life stage spanning 520-620min after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. The shape of embryo is elongated and tripple fold. A stage between 2-fold embryo and fully-elongated embryo. Also called pretzel embryo or pretzel stage. WB:wjc The C. elegans life stage spanning 620-800min(hatch) after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. A stage after elongation is over. The last stage of embryogenesis. Also called pre-hatched embryo, late embryo or morphogenetic embryo. The C. elegans life stage spanning 620-800min(hatch) after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. A stage after elongation is over. The last stage of embryogenesis. Also called pre-hatched embryo, late embryo or morphogenetic embryo. fully-elongated embryo late embryo morphogenetic stage pre-hatched embryo worm_development WBls:0000021 fully-elongated embryo Ce WBls:0000021 The C. elegans life stage spanning 620-800min(hatch) after first cleavage at 20 Centigrade. Cell number remains at ~560 cells, with some new cells generated and some cells go through programmed cell death. A stage after elongation is over. The last stage of embryogenesis. Also called pre-hatched embryo, late embryo or morphogenetic embryo. WB:wjc WBls:0000022 A developemental life stage of the nematode Caenorhabditis elegans that occurs from egg hatching until death. postembryonic Ce WBls:0000023 A developmental life stage of the nematode Caenorhabditis elegans that occurs from egg hatching until adulthood. larva Ce WBls:0000024 The first stage larva. At 25 Centigrade, it ranges 14-25.5 hours after fertilization, 0-11.5 hours after hatch. L1 larva Ce WBls:0000027 The second stage larva. At 25 Centigrade, it ranges 25.5-32.5 hours after fertilization, 11.5-18.5 hours after hatch. L2 larva L2 larva Ce WBls:0000035 The third stage larva. At 25 Centigrade, it ranges 32.5-40 hours after fertilization, 18.5-26 hours after hatch. L3 larva Ce WBls:0000038 he fourth stage larva. At 25 Centigrade, it ranges 40-49.5 hours after fertilization, 26-35.5 hours after hatch. L4 larva Ce WBls:0000040 The stage when an animal shifts from L4 larva to adult. It includes the synthesis of new cuticle, cease of phrayngeal pumping during a lethargus stage, and the shed off of old cuticle. L4-adult molt C The stage that begins when a C.elegans individual is fully-developed and has reached maturity. The stage that begins when a C.elegans individual is fully-developed and has reached maturity. adult worm_development WBls:0000041 adult Ce WBls:0000041 The stage that begins when a C.elegans individual is fully-developed and has reached maturity. WB:wjc The stage after an male animal is fully-developed and reaches maturity. The stage after an male animal is fully-developed and reaches maturity. adult male worm_development WBls:0000056 adult male Ce WBls:0000056 The stage after an male animal is fully-developed and reaches maturity. WB:wjc The stage after an hermaphrodite animal is fully-developed and reaches maturity. The stage after an hermaphrodite animal is fully-developed and reaches maturity. adult hermaphrodite worm_development WBls:0000057 adult hermaphrodite Ce WBls:0000057 The stage after an hermaphrodite animal is fully-developed and reaches maturity. WB:wjc Very young adult hermaphrodites that do not have eggs in the uterus yet. At 20 Centigrade: 0 - 13 hours after L4-adult molt. 3 days after first cleaveage. Very young adult hermaphrodites that do not have eggs in the uterus yet. At 20 Centigrade: 0 - 13 hours after L4-adult molt. 3 days after first cleaveage. pre-reproductive stage adult hermaphrodite worm_development WBls:0000058 pre-reproductive stage adult hermaphrodite Ce WBls:0000058 Very young adult hermaphrodites that do not have eggs in the uterus yet. At 20 Centigrade: 0 - 13 hours after L4-adult molt. 3 days after first cleaveage. WB:wjc Adult hermaphrodites continuously laying fertilized eggs. Hermaphrodite in egg laying stages--usually up to 4/5 days after L4-adult molt at Centigrade. From the first fertilized egg is laid, till all sperms are used. At 20 Centigrade: 13 hours after L4-adult molt until about 5.4 days after the L4-adult molt. 3-8.4 days after first cleavage. Adult hermaphrodites continuously laying fertilized eggs. Hermaphrodite in egg laying stages--usually up to 4/5 days after L4-adult molt at Centigrade. From the first fertilized egg is laid, till all sperms are used. At 20 Centigrade: 13 hours after L4-adult molt until about 5.4 days after the L4-adult molt. 3-8.4 days after first cleavage. reproductive stage adult hermaphrodite worm_development WBls:0000060 reproductive stage adult hermaphrodite Ce WBls:0000060 Adult hermaphrodites continuously laying fertilized eggs. Hermaphrodite in egg laying stages--usually up to 4/5 days after L4-adult molt at Centigrade. From the first fertilized egg is laid, till all sperms are used. At 20 Centigrade: 13 hours after L4-adult molt until about 5.4 days after the L4-adult molt. 3-8.4 days after first cleavage. WB:wjc When egg-laying is still going on but intermittent and during which a significant number of oocytes are laid. Included in reproductive stage adult hermaphrodite. When egg-laying is still going on but intermittent and during which a significant number of oocytes are laid. Included in reproductive stage adult hermaphrodite. oocyte-laying stage adult hermaphrodite worm_development WBls:0000061 oocyte-laying stage adult hermaphrodite Ce WBls:0000061 When egg-laying is still going on but intermittent and during which a significant number of oocytes are laid. Included in reproductive stage adult hermaphrodite. WB:wjc Adult hermaphrodites that contain no more sperm, thus stop egg-laying, but still alive. At 20 Centigrade: 5.4 days after L4-adult molt until the death. 8.4 - 13.2 (average wild type life span) days after first cleavage. Adult hermaphrodites that contain no more sperm, thus stop egg-laying, but still alive. At 20 Centigrade: 5.4 days after L4-adult molt until the death. 8.4 - 13.2 (average wild type life span) days after first cleavage. post-reproductive stage adult hermaphrodite worm_development WBls:0000062 post-reproductive stage adult hermaphrodite Ce WBls:0000062 Adult hermaphrodites that contain no more sperm, thus stop egg-laying, but still alive. At 20 Centigrade: 5.4 days after L4-adult molt until the death. 8.4 - 13.2 (average wild type life span) days after first cleavage. WB:wjc At 20 Centigrade: 0-24 hours after L4-adult molt. At 20 Centigrade: 0-24 hours after L4-adult molt. newly molted young adult hermaphrodite worm_development WBls:0000063 newly molted young adult hermaphrodite Ce WBls:0000063 At 20 Centigrade: 0-24 hours after L4-adult molt. WB:wjc At 20 Centigrade: 24-48 hours after L4-adult molt. 4-5 days after first cleavage. At 20 Centigrade: 24-48 hours after L4-adult molt. 4-5 days after first cleavage. 1-day post-L4 adult hermaphrodite worm_development WBls:0000064 1-day post-L4 adult hermaphrodite Ce WBls:0000064 At 20 Centigrade: 24-48 hours after L4-adult molt. 4-5 days after first cleavage. WB:wjc WBls:0000071 The C. elegans life stage spanning ; 50 min after first cleavage at 20 Centigrade. Contains 8 cells. 8-cell embryo 8-cell embryo Ce WBls:0000072 The C. elegans life stage spanning ; 55 min after first cleavage at 20 Centigrade. Contains 12 cells. 12-cell embryo 12-cell embryo Ce A developemental life stage of a worm A developemental life stage of a worm danielaraciti worm_development WBls:0000075 worm life stage WBls:0000075 A developemental life stage of a worm WB:WBPerson2987 WBls:0000084 E-cell has divided into Ea and Ep. Contains 14 cells. 14-cell embryo 14-cell embryo Ce WBls:0000085 Fourth cleavage of the AB lineage. Contains 24 cells. 24-cell embryo 24-cell embryo Ce Any developmental stage in a nematode, including embryo, larva and adult stage. Any developmental stage in a nematode, including embryo, larva and adult stage. danielaraciti 2013-11-25T06:13:37Z all stages nematode nematode developmental stage worm_development WBls:0000101 Nematode life stage WBls:0000101 Any developmental stage in a nematode, including embryo, larva and adult stage. WB:dr WB:jl WBls:0000102 The whole period of embryogenesis in a nematode, from the formation of an egg until hatching. nematode embryo A developemental life stage in a nematode that occurs from egg hatching until death. A developemental life stage in a nematode that occurs from egg hatching until death. danielaraciti 2013-11-25T06:14:39Z worm_development WBls:0000103 postembryonic nematode WBls:0000103 A developemental life stage in a nematode that occurs from egg hatching until death. WB:WBPerson2987 WB:dr The nematode life-stage that begins when the organism is fully-developed and has reached maturity. The nematode life-stage that begins when the organism is fully-developed and has reached maturity. danielaraciti 2013-11-25T06:18:53Z L5 adult nematode worm_development WBls:0000104 nematode adult WBls:0000104 The nematode life-stage that begins when the organism is fully-developed and has reached maturity. WB:dr WBls:0000105 The stage that begins after hatching and ends when the nematode becomes adult. nematode larval stage WBls:0000106 The first stage larva of nematodes. L1 larval stage WBls:0000107 The second stage larva of nematodes. L2 larval stage WBls:0000108 The third stage larva of nematodes. L3 larval stage WBls:0000111 At 20 Centigrade: 16-18 days after L4-adult molt. 18-21 days after first cleavage. 16-18 days post-L4 adult hermaphrodite Ce A developmental life stage of the nematode Caenorhabditis elegans that occurs in an egg (oocyte), before fertilization by sperm. A developmental life stage of the nematode Caenorhabditis elegans that occurs in an egg (oocyte), before fertilization by sperm. danielaraciti 2014-11-26T11:49:22Z unfertilized egg worm_development WBls:0000669 unfertilized egg Ce WBls:0000669 A developmental life stage of the nematode Caenorhabditis elegans that occurs in an egg (oocyte), before fertilization by sperm. WB:WBPerson2987 At 20 Centigrade: 15-16 days after L4-adult molt. 18-19 days after first cleavage. At 20 Centigrade: 15-16 days after L4-adult molt. 18-19 days after first cleavage. 15-days post-L4 adult hermaphrodite worm_development WBls:0000675 15-days post-L4 adult hermaphrodite Ce WBls:0000675 At 20 Centigrade: 15-16 days after L4-adult molt. 18-19 days after first cleavage. WB:dr At 20 Centigrade: 20-21 days after L4-adult molt. 23-24 days after first cleavage. At 20 Centigrade: 20-21 days after L4-adult molt. 23-24 days after first cleavage. 20-days post-L4 adult hermaphrodite worm_development WBls:0000676 20-days post-L4 adult hermaphrodite Ce WBls:0000676 At 20 Centigrade: 20-21 days after L4-adult molt. 23-24 days after first cleavage. WB:dr WBls:0000800 At 20 Centigrade: 14-15 days after L4-adult molt. 17-18 days after first cleavage. 14-days post-L4 adult hermaphrodite Ce A C. elegans life stage that occurs during embryogenesis A C. elegans life stage that occurs during embryogenesis worm_development WBls:0000803 C. elegans life stage occurring during embryogenesis WBls:0000803 A C. elegans life stage that occurs during embryogenesis WB:WBPerson2987 A C. elegans life stage that occurs after embryogenesis A C. elegans life stage that occurs after embryogenesis worm_development WBls:0000804 C. elegans life stage occurring post embryogenesis WBls:0000804 A C. elegans life stage that occurs after embryogenesis WB:WBPerson2987 WBls:0000805 A C. elegans life stage that occurs during the elongating embryo life stage C. elegans life stage occurring during elongating embryo A C. elegans life stage that occurs during the 1.5-fold embryo life stage A C. elegans life stage that occurs during the 1.5-fold embryo life stage worm_development WBls:0000806 C. elegans life stage occurring during 1.5-fold embryo WBls:0000806 A C. elegans life stage that occurs during the 1.5-fold embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the 2-fold embryo life stage A C. elegans life stage that occurs during the 2-fold embryo life stage worm_development WBls:0000807 C. elegans life stage occurring during 2-fold embryo WBls:0000807 A C. elegans life stage that occurs during the 2-fold embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the 3-fold embryo life stage A C. elegans life stage that occurs during the 3-fold embryo life stage worm_development WBls:0000808 C. elegans life stage occurring during 3-fold embryo WBls:0000808 A C. elegans life stage that occurs during the 3-fold embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the bean embryo life stage A C. elegans life stage that occurs during the bean embryo life stage worm_development WBls:0000809 C. elegans life stage occurring during bean embryo WBls:0000809 A C. elegans life stage that occurs during the bean embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the comma embryo life stage A C. elegans life stage that occurs during the comma embryo life stage worm_development WBls:0000810 C. elegans life stage occurring during comma embryo WBls:0000810 A C. elegans life stage that occurs during the comma embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the fully-elongating embryo life stage A C. elegans life stage that occurs during the fully-elongating embryo life stage worm_development WBls:0000811 C. elegans life stage occurring during fully-elongated embryo WBls:0000811 A C. elegans life stage that occurs during the fully-elongating embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the proliferating embryo life stage A C. elegans life stage that occurs during the proliferating embryo life stage worm_development WBls:0000812 C. elegans life stage occurring during proliferating embryo WBls:0000812 A C. elegans life stage that occurs during the proliferating embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the blastula embryo life stage A C. elegans life stage that occurs during the blastula embryo life stage worm_development WBls:0000813 C. elegans life stage occurring during blastula embryo WBls:0000813 A C. elegans life stage that occurs during the blastula embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the gastrulating embryo life stage A C. elegans life stage that occurs during the gastrulating embryo life stage worm_development WBls:0000814 C. elegans life stage occurring during gastrulation WBls:0000814 A C. elegans life stage that occurs during the gastrulating embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the enclosing embryo life stage A C. elegans life stage that occurs during the enclosing embryo life stage worm_development WBls:0000815 C. elegans life stage occurring during enclosing embryo WBls:0000815 A C. elegans life stage that occurs during the enclosing embryo life stage WB:WBPerson2987 A C. elegans life stage that occurs during the adult life stage A C. elegans life stage that occurs during the adult life stage worm_development WBls:0000816 C. elegans life stage occurring during adulthood WBls:0000816 A C. elegans life stage that occurs during the adult life stage WB:WBPerson2987 A C. elegans life stage that occurs during the larval life stage A C. elegans life stage that occurs during the larval life stage worm_development WBls:0000817 C. elegans life stage occurring during larval stage WBls:0000817 A C. elegans life stage that occurs during the larval life stage WB:WBPerson2987 A C. elegans life stage that occurs during the L1 larval life stage A C. elegans life stage that occurs during the L1 larval life stage worm_development WBls:0000818 C. elegans life stage occurring during L1 larval stage WBls:0000818 A C. elegans life stage that occurs during the L1 larval life stage WB:WBPerson2987 A C. elegans life stage that occurs during the L2 larval life stage A C. elegans life stage that occurs during the L2 larval life stage worm_development WBls:0000819 C. elegans life stage occurring during L2 larval stage WBls:0000819 A C. elegans life stage that occurs during the L2 larval life stage WB:WBPerson2987 A C. elegans life stage that occurs during the L3 larval life stage A C. elegans life stage that occurs during the L3 larval life stage worm_development WBls:0000820 C. elegans life stage occurring during L3 larval stage WBls:0000820 A C. elegans life stage that occurs during the L3 larval life stage WB:WBPerson2987 A C. elegans life stage that occurs during the L4 larval life stage A C. elegans life stage that occurs during the L4 larval life stage worm_development WBls:0000821 C. elegans life stage occurring during L4 larval stage WBls:0000821 A C. elegans life stage that occurs during the L4 larval life stage WB:WBPerson2987 C. elegans life stage classified by the number of cells in the organism. C. elegans life stage classified by the number of cells in the organism. worm_development WBls:0000823 C. elegans life stage by number of cells WBls:0000823 C. elegans life stage classified by the number of cells in the organism. WB:WBPerson2987 C. elegans life stage that occurs during a larval molt C. elegans life stage that occurs during a larval molt worm_development WBls:0000824 C. elegans life stage occurring during larval molt WBls:0000824 C. elegans life stage that occurs during a larval molt WB:WBPerson2987 WBls:0000825 life stage of the nematode Caenorhabditis elegans C. elegans life stage A C. elegans life stage that occurs after the animal has recovered from the dauer diapause. This includes the post dauer L3 (PDL3) stage, the post dauer L4 (PDL4) stage, and post dauer adult stage. A C. elegans life stage that occurs after the animal has recovered from the dauer diapause. This includes the post dauer L3 (PDL3) stage, the post dauer L4 (PDL4) stage, and post dauer adult stage. worm_development WBls:0000827 post dauer stage Ce WBls:0000827 A C. elegans life stage that occurs after the animal has recovered from the dauer diapause. This includes the post dauer L3 (PDL3) stage, the post dauer L4 (PDL4) stage, and post dauer adult stage. PMID:27417559 WB:WBPerson2987 A C. elegans adult life stage that occurs after the animal has recovered from the dauer diapause. A C. elegans adult life stage that occurs after the animal has recovered from the dauer diapause. worm_development WBls:0000829 post dauer adult stage Ce WBls:0000829 A C. elegans adult life stage that occurs after the animal has recovered from the dauer diapause. PMID:27417559 WB:WBPerson2987 System of partial differential equations which is linear. linear partial differential equation Dynamical simulation, in computational physics, is the simulation of systems of objects that are free to move, usually in three dimensions according to Newton's laws of dynamics, or approximations thereto. Dynamical simulation is used in computer animation to assist animators to produce realistic motion, in industrial design (for example to simulate crashes as an early step in crash testing), and in video games. Body movement is calculated using time integration methods. Dynamical simulation, in computational physics, is the simulation of systems of objects that are free to move, usually in three dimensions according to Newton's laws of dynamics, or approximations thereto. Dynamical simulation is used in computer animation to assist animators to produce realistic motion, in industrial design (for example to simulate crashes as an early step in crash testing), and in video games. Body movement is calculated using time integration methods. dynamics simulation Dynamical simulation, in computational physics, is the simulation of systems of objects that are free to move, usually in three dimensions according to Newton's laws of dynamics, or approximations thereto. Dynamical simulation is used in computer animation to assist animators to produce realistic motion, in industrial design (for example to simulate crashes as an early step in crash testing), and in video games. Body movement is calculated using time integration methods. http://en.wikipedia.org/wiki/Dynamical_simulation Model that mathematically describes features of diffusion. "Diffusion describes the spread of particles through random motion from regions of higher concentration to regions of lower concentration. The time dependence of the statistical distribution in space is given by the diffusion equation. The concept of diffusion is tied to that of mass transfer driven by a concentration gradient, but diffusion can still occur when there is no concentration gradient (but there will be no net flux). ... In molecular diffusion, the moving entities are small molecules which are self propelled by thermal energy and do not require a concentration gradient to spread out through random motion. They move at random because they frequently collide. Diffusion is this thermal motion of all (liquid and gas) molecules at temperatures above absolute zero. Diffusion rate is a function of only temperature, and is not affected by concentration. Brownian motion is observed in molecules that are so large that they are not driven by their own thermal energy but by collisions with solvent particles." "Diffusion describes the spread of particles through random motion from regions of higher concentration to regions of lower concentration. The time dependence of the statistical distribution in space is given by the diffusion equation. The concept of diffusion is tied to that of mass transfer driven by a concentration gradient, but diffusion can still occur when there is no concentration gradient (but there will be no net flux). ... In molecular diffusion, the moving entities are small molecules which are self propelled by thermal energy and do not require a concentration gradient to spread out through random motion. They move at random because they frequently collide. Diffusion is this thermal motion of all (liquid and gas) molecules at temperatures above absolute zero. Diffusion rate is a function of only temperature, and is not affected by concentration. Brownian motion is observed in molecules that are so large that they are not driven by their own thermal energy but by collisions with solvent particles." diffusion model "Diffusion describes the spread of particles through random motion from regions of higher concentration to regions of lower concentration. The time dependence of the statistical distribution in space is given by the diffusion equation. The concept of diffusion is tied to that of mass transfer driven by a concentration gradient, but diffusion can still occur when there is no concentration gradient (but there will be no net flux). ... In molecular diffusion, the moving entities are small molecules which are self propelled by thermal energy and do not require a concentration gradient to spread out through random motion. They move at random because they frequently collide. Diffusion is this thermal motion of all (liquid and gas) molecules at temperatures above absolute zero. Diffusion rate is a function of only temperature, and is not affected by concentration. Brownian motion is observed in molecules that are so large that they are not driven by their own thermal energy but by collisions with solvent particles." http://en.wikipedia.org/wiki/Diffusion Model that mathematically describes features of "systems of objects that are free to move, usually in three dimensions according to Newton's laws of dynamics, or approximations thereto. " Model that mathematically describes features of "systems of objects that are free to move, usually in three dimensions according to Newton's laws of dynamics, or approximations thereto. " dynamics model Model that mathematically describes features of "systems of objects that are free to move, usually in three dimensions according to Newton's laws of dynamics, or approximations thereto. " http://en.wikipedia.org/wiki/Dynamical_simulation Changeable; active; in motion usually as the result of an external force. dynamic quality A mathematical entity is an information content entity that are components of a mathematical system or can be defined in mathematical terms. mathematical entity An equation is a mathematical statement that asserts the equality of two expressions. equation A differential equation is a mathematical equation for an unknown function of one or several variables that relates the values of the function itself and its derivatives of various orders. differential equation cancer cell line RNAi profiling is an assay in which double stranded RNA is synthesized with a sequence complementary to a gene(s) of interest and introduced into a cell or organism, where it is recognized as exogenous genetic material and activates the RNAi pathway resulting in knockdown of the transcripts and providing a means to study downstream changes in gene expression. RNAi profiling by array An assay with input RNA RNA assay Typically small, circular, intronless, and maternally inherited, mitochondrial DNA (mtDNA) is the multicopy deoxyribonucleic acid genome of mitochondria, intracellular organelles responsible for vital respiratory chain and oxidative phosphorylation reactions in higher eukaryotes. Replicated and transcribed by a separate enzymatic machinery from that of nuclear DNA, mtDNA encodes only a subset of mitochondrial functions. (by EFO) http://www.ebi.ac.uk/efo/EFO_0008480 mtDNA mitochondrial DNA owl:Thing A Polycomb complex protein BMI-1 that is encoded in the genome of human. HGNC:1066 BMI1 Polycomb group RING finger protein 4 (human) RING finger protein 51 (human) UniProtKB:P35226 Polycomb complex protein BMI-1 (human) hBMI1 Aging https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig1.jpg Robbins Basic Pathology 9th edition Aging MeSHID:D000375 Aging MESHID:D000375 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5748990/bin/JCB_201708092_Fig1.jpg 老年医学　系統講義テキスト　日本老年医学会編 2章老化メカニズムと老化制御 2024/04/03 Person:Alan Ruttenberg Yuki Yamagata yuki.yamagata[at]riken.jp Homeostasis imbalance process ontology (HOIP) systematizes a wide variety of processes triggered by homeostatic imbalance. The version of HoiP focuses on COVID-19 infectious processes and cellular senescence. The HoIP contains an is-a hierarchy that is organized into three layers: the top layer contains general terms, mostly derived from the Basic Formal Ontology. The top layer also defines functioning-related processes. The intermediate layer contains biomedical terms in OBO foundry from VO, UBERON, Cell Ontology, NCBI Taxon, ChEBI, Gene Ontology, PATO, OGG, INOH, HINO, DOID, HP, Protein Ontology, Symptom Ontology, CIDO, BSPO, WBbt, WBIs, HuPSON, NCIT, and Relational ontology (RO). The lower layer contains homeostasis imbalance-dependent terms. Related article: Ontology for Cellular Senescence Mechanisms Yuki Yamagata, Tsubasa Fukuyama, Shuichi Onami, Hiroshi Masuya bioRxiv 2023.03.09.531883; doi: https://doi.org/10.1101/2023.03.09.531883 Homeostasis imbalance process ontology (HOIP) severe COVID-19 course: http://purl.bioontology.org/ontology/HOIP/HOIP_0039222 COVID-19 course associated with acute respiratory distress syndrome http://purl.bioontology.org/ontology/HOIP/HOIP_0036006 COVID-19 specific process. http://purl.bioontology.org/ontology/HOIP/HOIP_0037002 Cellular senescence course: http://purl.bioontology.org/ontology/HOIP/HOIP_0060024 Chronic cellular senescence course http://purl.bioontology.org/ontology/HOIP/HOIP_0060195 2024/04/03 my body has part my brain (continuant parthood, two material entities) my stomach has part my stomach cavity (continuant parthood, material entity has part immaterial entity) a core relation that holds between a whole and its part Parthood requires the part and the whole to have compatible classes: only an occurrent have an occurrent as part; only a process can have a process as part; only a continuant can have a continuant as part; only an independent continuant can have an independent continuant as part; only a specifically dependent continuant can have a specifically dependent continuant as part; only a generically dependent continuant can have a generically dependent continuant as part. (This list is not exhaustive.) A continuant cannot have an occurrent as part: use 'participates in'. An occurrent cannot have a continuant as part: use 'has participant'. An immaterial entity cannot have a material entity as part: use 'location of'. An independent continuant cannot have a specifically dependent continuant as part: use 'bearer of'. A specifically dependent continuant cannot have an independent continuant as part: use 'inheres in'. has part realizes this disease course realizes this disease this investigation realizes this investigator role this shattering realizes this fragility to say that b realizes c at t is to assert that there is some material entity d & b is a process which has participant d at t & c is a disposition or role of which d is bearer_of at t& the type instantiated by b is correlated with the type instantiated by c. (axiom label in BFO2 Reference: [059-003]) Paraphrase of elucidation: a relation between a process and a realizable entity, where there is some material entity that is bearer of the realizable entity and participates in the process, and the realizable entity comes to be realized in the course of the process realizes X is preceded by y if and only if the time point at which y ends is before or equivalent to the time point at which x starts. Formally: x preceded by y iff ω(y) <= α(x), where α is a function that maps a process to a start point, and ω is a function that maps a process to an end point. An example is: translation preceded_by transcription; aging preceded_by development (not however death preceded_by aging). Where derives_from links classes of continuants, preceded_by links classes of processes. Clearly, however, these two relations are not independent of each other. Thus if cells of type C1 derive_from cells of type C, then any cell division involving an instance of C1 in a given lineage is preceded_by cellular processes involving an instance of C. The assertion P preceded_by P1 tells us something about Ps in general: that is, it tells us something about what happened earlier, given what we know about what happened later. Thus it does not provide information pointing in the opposite direction, concerning instances of P1 in general; that is, that each is such as to be succeeded by some instance of P. Note that an assertion to the effect that P preceded_by P1 is rather weak; it tells us little about the relations between the underlying instances in virtue of which the preceded_by relation obtains. Typically we will be interested in stronger relations, for example in the relation immediately_preceded_by, or in relations which combine preceded_by with a condition to the effect that the corresponding instances of P and P1 share participants, or that their participants are connected by relations of derivation, or (as a first step along the road to a treatment of causality) that the one process in some way affects (for example, initiates or regulates) the other. preceded by occurs in b occurs_in c =def b is a process and c is a material entity or immaterial entity& there exists a spatiotemporal region r and b occupies_spatiotemporal_region r.& forall(t) if b exists_at t then c exists_at t & there exist spatial regions s and s’ where & b spatially_projects_onto s at t& c is occupies_spatial_region s’ at t& s is a proper_continuant_part_of s’ at t occurs_in unfolds in unfolds_in Paraphrase of definition: a relation between a process and an independent continuant, in which the process takes place entirely within the independent continuant occurs in a relation between a continuant and a process, in which the process takes place entirely within the independent continuant [copied from inverse property 'occurs in'] b occurs_in c =def b is a process and c is a material entity or immaterial entity& there exists a spatiotemporal region r and b occupies_spatiotemporal_region r.& forall(t) if b exists_at t then c exists_at t & there exist spatial regions s and s’ where & b spatially_projects_onto s at t& c is occupies_spatial_region s’ at t& s is a proper_continuant_part_of s’ at t contains process To say that each spatiotemporal region s temporally_projects_onto some temporal region t is to say that t is the temporal extension of s. (axiom label in BFO2 Reference: [080-003]) To say that each spatiotemporal region s temporally_projects_onto some temporal region t is to say that t is the temporal extension of s. (axiom label in BFO2 Reference: [080-003]) To say that spatiotemporal region s spatially_projects_onto spatial region r at t is to say that r is the spatial extent of s at t. (axiom label in BFO2 Reference: [081-003]) To say that spatiotemporal region s spatially_projects_onto spatial region r at t is to say that r is the spatial extent of s at t. (axiom label in BFO2 Reference: [081-003]) To say that each spatiotemporal region s temporally_projects_onto some temporal region t is to say that t is the temporal extension of s. (axiom label in BFO2 Reference: [080-003]) To say that spatiotemporal region s spatially_projects_onto spatial region r at t is to say that r is the spatial extent of s at t. (axiom label in BFO2 Reference: [081-003]) x anterior to y iff x is further along the antero-posterior axis than y, towards the head. An antero-posterior axis is an axis that extends through an organism from head end to opposite end of body or tail. x anterior to y iff x is further along the antero-posterior axis than y, towards the head. An antero-posterior axis is an axis that extends through an organism from head end to opposite end of body or tail. BSPO:0000096 rostral_to spatial anterior_to anterior_to anterior to x anterior to y iff x is further along the antero-posterior axis than y, towards the head. An antero-posterior axis is an axis that extends through an organism from head end to opposite end of body or tail. BSPO:cjm x distal to y iff x is further along the proximo-distal axis than y, towards the appendage tip. A proximo-distal axis extends from tip of an appendage (distal) to where it joins the body (proximal). x distal to y iff x is further along the proximo-distal axis than y, towards the appendage tip. A proximo-distal axis extends from tip of an appendage (distal) to where it joins the body (proximal). BSPO:0000097 spatial distal_to distal_to distal to x distal to y iff x is further along the proximo-distal axis than y, towards the appendage tip. A proximo-distal axis extends from tip of an appendage (distal) to where it joins the body (proximal). BSPO:cjm x dorsal to y iff x is further along the dorso-ventral axis than y, towards the back. A dorso-ventral axis is an axis that extends through an organism from back (e.g. spinal column) to front (e.g. belly). x dorsal to y iff x is further along the dorso-ventral axis than y, towards the back. A dorso-ventral axis is an axis that extends through an organism from back (e.g. spinal column) to front (e.g. belly). BSPO:0000098 spatial dorsal_to dorsal_to dorsal to x dorsal to y iff x is further along the dorso-ventral axis than y, towards the back. A dorso-ventral axis is an axis that extends through an organism from back (e.g. spinal column) to front (e.g. belly). BSPO:cjm x posterior to y iff x is further along the antero-posterior axis than y, towards the body/tail. An antero-posterior axis is an axis that extends through an organism from head end to opposite end of body or tail. x posterior to y iff x is further along the antero-posterior axis than y, towards the body/tail. An antero-posterior axis is an axis that extends through an organism from head end to opposite end of body or tail. BSPO:0000099 caudal to caudal to spatial posterior_to posterior_to posterior to x posterior to y iff x is further along the antero-posterior axis than y, towards the body/tail. An antero-posterior axis is an axis that extends through an organism from head end to opposite end of body or tail. BSPO:cjm caudal to x proximal to y iff x is closer to the point of attachment with the body than y. x proximal to y iff x is closer to the point of attachment with the body than y. BSPO:0000100 spatial proximal_to proximal_to The elbow is proximal to the hand, but distal to the shoulder. proximal to x proximal to y iff x is closer to the point of attachment with the body than y. BSPO:cjm Crosses at an angle that is 90 degrees, or close to 90 degrees. In any non-linear organism, the main axes are rarely perpendicular when taken through the organism as a whole. Crosses at an angle that is 90 degrees, or close to 90 degrees. In any non-linear organism, the main axes are rarely perpendicular when taken through the organism as a whole. BSPO:0000104 spatial approximately_perpendicular_to approximately_perpendicular_to approximately perpendicular to Crosses at an angle that is 90 degrees, or close to 90 degrees. In any non-linear organism, the main axes are rarely perpendicular when taken through the organism as a whole. BSPO:cjm Closer to the left side of the organism. Example: The dorsal fin is right of the left pectoral fin, but is left of the right eye. On the type level: X left of Y <=> every instance x of X is left of some instance y of Y, and there exists some organism o such that x part of o and y part of o. Closer to the left side of the organism. Example: The dorsal fin is right of the left pectoral fin, but is left of the right eye. On the type level: X left of Y <=> every instance x of X is left of some instance y of Y, and there exists some organism o such that x part of o and y part of o. BSPO:0000110 spatial left_of left_of left of Closer to the left side of the organism. Example: The dorsal fin is right of the left pectoral fin, but is left of the right eye. On the type level: X left of Y <=> every instance x of X is left of some instance y of Y, and there exists some organism o such that x part of o and y part of o. BSPO:cjm Direcly opposite to. i.e. on the opposite side through the axis. Direcly opposite to. i.e. on the opposite side through the axis. BSPO:0000113 spatial opposite_to opposite_to opposite to Direcly opposite to. i.e. on the opposite side through the axis. BSPO:cjm X in left side of Y <=> if Y is subdivided into two left and right portions, X is part of the left portion. X in left side of Y <=> if Y is subdivided into two left and right portions, X is part of the left portion. BSPO:0000120 spatial in_left_side_of in_left_side_of in left side of https://github.com/obophenotype/uberon/wiki/Modeling-paired-structures-Design-Pattern X in left side of Y <=> if Y is subdivided into two left and right portions, X is part of the left portion. BSPO:PATO_mtg_2009 X in right side of Y <=> if Y is subdivided into two left and right portions, X is part of the right portion. X in right side of Y <=> if Y is subdivided into two left and right portions, X is part of the right portion. BSPO:0000121 spatial in_right_side_of in_right_side_of in right side of https://github.com/obophenotype/uberon/wiki/Modeling-paired-structures-Design-Pattern X in right side of Y <=> if Y is subdivided into two left and right portions, X is part of the right portion. BSPO:PATO_mtg_2009 X posterior side of Y <=> if Y is subdivided into two anterior and posterior portions, X is part of the posterior portion. X posterior side of Y <=> if Y is subdivided into two anterior and posterior portions, X is part of the posterior portion. BSPO:0000122 spatial in_posterior_side_of in_posterior_side_of in posterior side of X posterior side of Y <=> if Y is subdivided into two anterior and posterior portions, X is part of the posterior portion. BSPO:PATO_mtg_2009 X anterior side of Y <=> if Y is subdivided into two anterior and posterior portions, X is part of the anterior portion. X anterior side of Y <=> if Y is subdivided into two anterior and posterior portions, X is part of the anterior portion. BSPO:0000123 spatial in_anterior_side_of in_anterior_side_of in anterior side of X anterior side of Y <=> if Y is subdivided into two anterior and posterior portions, X is part of the anterior portion. BSPO:PATO_mtg_2009 BSPO:0015001 spatial finishes_axis finishes_axis A directional axis can be divided by a plane. Following Allen Interval Algebra terminology we say that the side on which the axis initiates starts the axis, with the other side finishing the axis. If s finishes axis x, and x has end point p, then x overlaps p finishes axis BSPO:0015002 spatial follows_axis follows_axis follows axis BSPO:0015003 spatial has_axis has_axis has axis crossing at right angles crossing at right angles BSPO:0015005 spatial orthogonal_to orthogonal_to orthogonal to crossing at right angles BSPO:cjm BSPO:0015007 spatial starts_axis starts_axis A directional axis can be divided by a plane. Following Allen Interval Algebra terminology we say that the side on which the axis initiates starts the axis, with the other side finishing the axis. . If s starts axis x, and x has start point p, then x overlaps p starts axis BSPO:0015008 spatial surface_of surface_of placeholder. used for relation between anatomical surface and an anatomical side. surface of Any process mediated by a virus that results in the death of a cell in the host organism. killing by virus of host cell This document is about information artifacts and their representations A (currently) primitive relation that relates an information artifact to an entity. 7/6/2009 Alan Ruttenberg. Following discussion with Jonathan Rees, and introduction of "mentions" relation. Weaken the is_about relationship to be primitive. We will try to build it back up by elaborating the various subproperties that are more precisely defined. Some currently missing phenomena that should be considered "about" are predications - "The only person who knows the answer is sitting beside me" , Allegory, Satire, and other literary forms that can be topical without explicitly mentioning the topic. person:Alan Ruttenberg Smith, Ceusters, Ruttenberg, 2000 years of philosophy is about m is a quality measurement of q at t. When q is a quality, there is a measurement process p that has specified output m, a measurement datum, that is about q 8/6/2009 Alan Ruttenberg: The strategy is to be rather specific with this relationship. There are other kinds of measurements that are not of qualities, such as those that measure time. We will add these as separate properties for the moment and see about generalizing later From the second IAO workshop [Alan Ruttenberg 8/6/2009: not completely current, though bringing in comparison is probably important] This one is the one we are struggling with at the moment. The issue is what a measurement measures. On the one hand saying that it measures the quality would include it "measuring" the bearer = referring to the bearer in the measurement. However this makes comparisons of two different things not possible. On the other hand not having it inhere in the bearer, on the face of it, breaks the audit trail. Werner suggests a solution based on "Magnitudes" a proposal for which we are awaiting details. -- From the second IAO workshop, various comments, [commented on by Alan Ruttenberg 8/6/2009] unit of measure is a quality, e.g. the length of a ruler. [We decided to hedge on what units of measure are, instead talking about measurement unit labels, which are the information content entities that are about whatever measurement units are. For IAO we need that information entity in any case. See the term measurement unit label] [Some struggling with the various subflavors of is_about. We subsequently removed the relation represents, and describes until and only when we have a better theory] a represents b means either a denotes b or a describes describe: a describes b means a is about b and a allows an inference of at least one quality of b We have had a long discussion about denotes versus describes. From the second IAO workshop: An attempt at tieing the quality to the measurement datum more carefully. a is a magnitude means a is a determinate quality particular inhering in some bearer b existing at a time t that can be represented/denoted by an information content entity e that has parts denoting a unit of measure, a number, and b. The unit of measure is an instance of the determinable quality. From the second meeting on IAO: An attempt at defining assay using Barry's "reliability" wording assay: process and has_input some material entity and has_output some information content entity and which is such that instances of this process type reliably generate outputs that describes the input. This one is the one we are struggling with at the moment. The issue is what a measurement measures. On the one hand saying that it measures the quality would include it "measuring" the bearer = referring to the bearer in the measurement. However this makes comparisons of two different things not possible. On the other hand not having it inhere in the bearer, on the face of it, breaks the audit trail. Werner suggests a solution based on "Magnitudes" a proposal for which we are awaiting details. Alan Ruttenberg is quality measurement of The inverse property of is_specified_input_of has_specified_input A relation between a planned process and a continuant participating in that process. The presence of the continuant at the end of the process is explicitly specified in the objective specification which the process realizes the concretization of. has_specified_output is_specified_output_of is_specified_output_of A relation between a planned process and a continuant participating in that process. The presence of the continuant at the end of the process is explicitly specified in the objective specification which the process realizes the concretization of. Alan Ruttenberg PERSON:Bjoern Peters is_specified_output_of achieves_planned_objective A cell sorting process achieves the objective specification 'material separation objective' This relation obtains between a planned process and a objective specification when the criteria specified in the objective specification are met at the end of the planned process. BP, AR, PPPB branch PPPB branch derived modified according to email thread from 1/23/09 in accordince with DT and PPPB branch achieves_planned_objective the relation of the cells in the finger of the skin to the finger, in which an indeterminate number of grains are parts of the whole by virtue of being grains in a collective that is part of the whole, and in which removing one granular part does not necessarily damage or diminish the whole. Ontological Whether there is a fixed, or nearly fixed number of parts - e.g. fingers of the hand, chambers of the heart, or wheels of a car - such that there can be a notion of a single one being missing, or whether, by contrast, the number of parts is indeterminate - e.g., cells in the skin of the hand, red cells in blood, or rubber molecules in the tread of the tire of the wheel of the car. has grain a relation between a gene and the organism where this gene belongs to the organism in nature. It does not include a foreign gene that is transferred to an organism by a genetic engineering method. is gene of organism inheres in this fragility inheres in this vase this red color inheres in this apple a relation between a specifically dependent continuant (the dependent) and an independent continuant (the bearer), in which the dependent specifically depends on the bearer for its existence A dependent inheres in its bearer at all times for which the dependent exists. inheres_in inheres in participates in this blood clot participates in this blood coagulation this input material (or this output material) participates in this process this investigator participates in this investigation a relation between a continuant and a process, in which the continuant is somehow involved in the process participates_in participates in a relation between a process and a continuant, in which the continuant is somehow involved in the process Example: Protein refolding process hasParticipant "GRP78/Bip" that has a chaperon role . http://www.obofoundry.org/ro/#OBO_REL:has_participant has participant this catalysis function is a function of this enzyme A relation between a function and an independent continuant (the bearer), in which the function specifically depends on the bearer for its existence function_of is_function_of function of a relation between an independent continuant (the bearer) and a function, in which the function specifically depends on the bearer for its existence A bearer can have many functions, and its functions can exist for different periods of time, but none of its functions can exist when the bearer does not exist. A function need not be realized at all the times that the function exists. has function a relation between an independent continuant (the bearer) and a quality, in which the quality specifically depends on the bearer for its existence hasQuality is a relation between an entity and the quality that it bears. has_quality has quality a relation between an independent continuant (the bearer) and a role, in which the role specifically depends on the bearer for its existence has_role A bearer can have many roles, and its roles can exist for different periods of time, but none of its roles can exist when the bearer does not exist. A role need not be realized at all the times that the role exists. has role a relation between two distinct material entities, the new entity and the old entity, in which the new entity begins to exist when the old entity ceases to exist, and the new entity inherits the significant portion of the matter of the old entity derives from located in my brain is located in my head this rat is located in this cage a relation between two independent continuants, the target and the location, in which the target is entirely within the location Location as a relation between instances: The primitive instance-level relation c located_in r at t reflects the fact that each continuant is at any given time associated with exactly one spatial region, namely its exact location. Following we can use this relation to define a further instance-level location relation - not between a continuant and the region which it exactly occupies, but rather between one continuant and another. c is located in c1, in this sense, whenever the spatial region occupied by c is part_of the spatial region occupied by c1. Note that this relation comprehends both the relation of exact location between one continuant and another which obtains when r and r1 are identical (for example, when a portion of fluid exactly fills a cavity), as well as those sorts of inexact location relations which obtain, for example, between brain and head or between ovum and uterus Most location relations will only hold at certain times, but this is difficult to specify in OWL. See http://purl.obolibrary.org/obo/ro/docs/temporal-semantics/ located_in http://www.obofoundry.org/ro/#OBO_REL:located_in located in t1 simultaneous_with t2 iff:= t1 before_or_simultaneous_with t2 and not (t1 before t2) simultaneous with X immediately_preceded_by Y iff: end(X) simultaneous_with start(Y) X immediately_preceded_by Y iff: end(X) simultaneous_with start(Y) immediately preceded by happens during U only_in_taxon T: U is a feature found in only in organisms of species of taxon T. The feature cannot be found in an organism of any species outside of (not subsumed by) that taxon. Down-propagates in U hierarchy, up-propagates in T hierarchy (species taxonomy). Implies applicable_to_taxon. only_in_taxon relation between an artery and the structure is supplies with blood supplies W 'has component' p if w 'has part' p and w is such that it can be directly disassembled into into n parts p, p2, p3, ..., pn, where these parts are of similar type. has component x expressed in y if and only if there is a gene expression process (GO:0010467) that occurs in y, and one of the following holds: (i) x is a gene, and x is transcribed into a transcript as part of the gene expression process (ii) x is a transcript, and the transcription of x is part of the gene expression process (iii) x is a mature gene product such as a protein, and x was translated or otherwise processes from a transcript that was transcribed as part of this gene expression process expressed in process(P1) regulates process(P2) iff: P1 results in the initiation or termination of P2 OR affects the frequency of its initiation or termination OR affects the magnitude or rate of output of P2. regulates Process(P1) negatively regulates process(P2) iff: P1 terminates P2, or P1 descreases the the frequency of initiation of P2 or the magnitude or rate of output of P2. negatively regulates Process(P1) postively regulates process(P2) iff: P1 initiates P2, or P1 increases the the frequency of initiation of P2 or the magnitude or rate of output of P2. positively regulates A relation between a material entity (such as a cell) and a process, in which the material entity has the ability to carry out the process. capable_of A caterpillar walking on the surface of a leaf is adjacent_to the leaf, if one of the caterpillar appendages is touching the leaf. In contrast, a butterfly flying close to a flower is not considered adjacent, unless there are any touching parts. The epidermis layer of a vertebrate is adjacent to the dermis. The plasma membrane of a cell is adjacent to the cytoplasm, and also to the cell lumen which the cytoplasm occupies. The skin of the forelimb is adjacent to the skin of the torso if these are considered anatomical subdivisions with a defined border. Otherwise a relation such as continuous_with would be used. x adjacent to y if and only if x and y share a boundary. This relation acts as a join point with BSPO Chris Mungall RO:0002220 spatial adjacent_to adjacent to A caterpillar walking on the surface of a leaf is adjacent_to the leaf, if one of the caterpillar appendages is touching the leaf. In contrast, a butterfly flying close to a flower is not considered adjacent, unless there are any touching parts. Every insulin receptor signaling pathway starts with the binding of a ligand to the insulin receptor x starts with y if and only if x has part y and the time point at which x starts is equivalent to the time point at which y starts. Formally: α(y) = α(x) ∧ ω(y) < ω(x), where α is a function that maps a process to a start point, and ω is a function that maps a process to an end point. starts with x ends with y if and only if x has part y and the time point at which x ends is equivalent to the time point at which y ends. Formally: α(y) > α(x) ∧ ω(y) = ω(x), where α is a function that maps a process to a start point, and ω is a function that maps a process to an end point. finished by ends with P has output c iff c is a participant in p, c is present at the beginning of p. has input P has output c iff c is a participant in p, c is present at the end of p has output results in formation of Holds between p and c when p is a localization process (localization covers maintenance of localization as well as its establishment) and the outcome of this process is to regulate the localization of c. transports or maintains localization of This relationship holds between p and l when p is a transport or localization process in which the outcome is to move some cargo c from some initial location l to some destination. has target start location RO:0002339 This relationship holds between p and l when p is a transport or localization process in which the outcome is to move some cargo c from a an initial location to some destination. has target end location has member is a mereological relation between a collection and an item. has member is a mereological relation between a collection and an item. SIO has member p 'causally upstream or within' q iff (1) the end of p is before the end of q and (2) the execution of p exerts some causal influence over the outputs of q; i.e. if p was abolished or the outputs of p were to be modified, this would necessarily affect q. influences (processual) affects causally upstream of or within inverse of causally upstream of or within: p 'causally upstream or within' q iff (1) the end of p is before the end of q and (2) the execution of p exerts some causal influence over the outputs of q; i.e. if p was abolished or the outputs of p were to be modified, this would necessarily affect q. causally downstream of or within x composed_primarily_of_y if:more than half of the mass of x is made from parts of y composed_primarily_of X starts ends with y if and only if the time point at which x starts is equivalent to the time point at which y starts. Formally: x existence starts with y iff α(x) = α(y). existence starts with X existence ends with y if and only if the time point at which x ends is equivalent to the time point at which y ends. Formally: x existence ends with y iff ω(x) = ω(y). existence ends with results in assembly of Holds between c and p if and only if c is capable of some activity a, and a regulates p. capable of regulating Holds between c and p if and only if c is capable of some activity a, and a positively regulates p. capable of positively regulating Holds between c and p if and only if c is capable of some activity a, and a negatively regulates p. capable of negatively regulating Inverse of is-model-of has model A relation between a biological, experimental, or computational artifact and an entity it is used to study, in virtue of its replicating or approximating features of the studied entity. has role in modeling x is parallel t y iff x and y are lines or planes which when extended indefinitely do not cross. x is parallel t y iff x and y are lines or planes which when extended indefinitely do not cross. spatial parallel_to parallel to x is parallel t y iff x and y are lines or planes which when extended indefinitely do not cross. BSPO:curators 'channel for' is a relation between a channel that is a passage and an entity such a solvent (e.g., ion) to pass. channel for