Proteins > Receptor-interacting serine/threonine-protein kinase 1
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Receptor-interacting serine/threonine-protein kinase 1
A receptor-interacting serine/threonine-protein kinase 1 that is encoded in the genome of human. [PRO:DNx]
Synonyms
EC 2.7.11.1;
Cell death protein RIP;
Receptor-interacting protein 1;
RIP-1
Research
Bioassay Publications (12)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (25.00) | 29.6817 |
| 2010's | 5 (41.67) | 24.3611 |
| 2020's | 4 (33.33) | 2.80 |
Compounds (82)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Small-Molecule Inhibitors of Necroptosis: Current Status and Perspectives.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Discovery of novel 2,8-diazaspiro[4.5]decan-1-one derivatives as potent RIPK1 kinase inhibitors.Bioorganic & medicinal chemistry, , 04-01, Volume: 59, 2022
Non-kinase targets of protein kinase inhibitors.Nature reviews. Drug discovery, , Volume: 16, Issue:6, 2017
Discovery of a Highly Potent, Selective, and Metabolically Stable Inhibitor of Receptor-Interacting Protein 1 (RIP1) for the Treatment of Systemic Inflammatory Response Syndrome.Journal of medicinal chemistry, , 02-09, Volume: 60, Issue:3, 2017
Identification of RIP1 kinase as a specific cellular target of necrostatins.Nature chemical biology, , Volume: 4, Issue:5, 2008
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Tozasertib Analogues as Inhibitors of Necroptotic Cell Death.Journal of medicinal chemistry, , 03-08, Volume: 61, Issue:5, 2018
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Small-Molecule Inhibitors of Necroptosis: Current Status and Perspectives.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Small-Molecule Inhibitors of Necroptosis: Current Status and Perspectives.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Small-Molecule Inhibitors of Necroptosis: Current Status and Perspectives.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Small-Molecule Inhibitors of Necroptosis: Current Status and Perspectives.Journal of medicinal chemistry, , 02-27, Volume: 63, Issue:4, 2020
Small-Molecule Receptor-Interacting Protein 1 (RIP1) Inhibitors as Therapeutic Agents for Multifaceted Diseases: Current Medicinal Chemistry Insights and Emerging Opportunities.Journal of medicinal chemistry, , 11-24, Volume: 65, Issue:22, 2022
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Enables
This protein enables 13 target(s):
| Target | Category | Definition |
|---|
| protein kinase activity | molecular function | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. [PMID:25399640] |
| protein serine/threonine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. [GOC:bf, MetaCyc:PROTEIN-KINASE-RXN, PMID:2956925] |
| death receptor binding | molecular function | Binding to a member of the death receptor (DR) family. The DR family falls within the tumor necrosis factor receptor superfamily and is characterized by a cytoplasmic region of ~80 residues termed the death domain (DD). [GOC:ceb, GOC:rl, PMID:15654015] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
| ubiquitin protein ligase binding | molecular function | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. [GOC:vp] |
| signaling adaptor activity | molecular function | The binding activity of a molecule that brings together two or more molecules in a signaling pathway, permitting those molecules to function in a coordinated way. Adaptor molecules themselves do not have catalytic activity. [GOC:bf, PMID:19104498] |
| identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
| protein homodimerization activity | molecular function | Binding to an identical protein to form a homodimer. [GOC:jl] |
| protein-containing complex binding | molecular function | Binding to a macromolecular complex. [GOC:jl] |
| death domain binding | molecular function | Binding to a death domain of a protein. The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DD bind each other forming oligomers. Some DD-containing proteins are involved in the regulation of apoptosis and inflammation through their activation of caspases and NF-kappaB. [GOC:BHF, GOC:rl, InterPro:IPR000488, Pfam:PF00531] |
| protein serine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989] |
| JUN kinase kinase kinase activity | molecular function | Catalysis of the reaction: JNKK + ATP = JNKK phosphate + ADP. This reaction is the phosphorylation and activation of JUN kinase kinases (JNKKs). [GOC:bf] |
Located In
This protein is located in 4 target(s):
| Target | Category | Definition |
|---|
| mitochondrion | cellular component | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| endosome membrane | cellular component | The lipid bilayer surrounding an endosome. [GOC:mah] |
Part Of
This protein is part of 4 target(s):
| Target | Category | Definition |
|---|
| death-inducing signaling complex | cellular component | A protein complex formed by the association of signaling proteins with a death receptor upon ligand binding. The complex includes procaspases and death domain-containing proteins in addition to the ligand-bound receptor, and may control the activation of caspases 8 and 10. [GOC:mtg_apoptosis, PMID:12628743, PMID:12655293, PMID:8521815] |
| protein-containing complex | cellular component | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah] |
| receptor complex | cellular component | Any protein complex that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. [GOC:go_curators] |
| ripoptosome | cellular component | A protein complex whose core components are the receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (also called RIP1 and RIP3). Formation of the ripoptosome can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more. [GOC:bhm, GOC:mtg_apoptosis, PMID:22265414, PMID:22274400] |
Involved In
This protein is involved in 48 target(s):
| Target | Category | Definition |
|---|
| MAPK cascade | biological process | An intracellular protein kinase cascade containing at least a MAP kinase (MAPK). It starts with the activation of a MAP3K, and the consecutive activation of a MPK2K and a MAPK. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinase in the downstream tier to transmit a signal within a cell. [PMID:20811974, PMID:9561267] |
| positive regulation of protein phosphorylation | biological process | Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein. [GOC:hjd] |
| apoptotic process | biological process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. [GOC:cjm, GOC:dhl, GOC:ecd, GOC:go_curators, GOC:mtg_apoptosis, GOC:tb, ISBN:0198506732, PMID:18846107, PMID:21494263] |
| inflammatory response | biological process | The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. [GO_REF:0000022, ISBN:0198506732] |
| response to oxidative stress | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:jl, PMID:12115731] |
| positive regulation of gene expression | biological process | Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). [GOC:txnOH-2018] |
| protein catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. [GOC:mah] |
| positive regulation of interleukin-8 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-8 production. [GOC:mah] |
| positive regulation of tumor necrosis factor production | biological process | Any process that activates or increases the frequency, rate or extent of tumor necrosis factor production. [GO_REF:0000058, GOC:TermGenie, PMID:10891884, PMID:15560120] |
| tumor necrosis factor-mediated signaling pathway | biological process | The series of molecular signals initiated by tumor necrosis factor binding to its receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling] |
| response to tumor necrosis factor | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus. [GOC:mah] |
| intracellular signal transduction | biological process | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. [GOC:bf, GOC:jl, GOC:signaling, ISBN:3527303782] |
| peptidyl-serine autophosphorylation | biological process | The phosphorylation by a protein of one or more of its own serine amino acid residues, or a serine residue on an identical protein. [GOC:pm] |
| positive regulation of apoptotic process | biological process | Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
| negative regulation of apoptotic process | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
| positive regulation of programmed cell death | biological process | Any process that activates or increases the frequency, rate or extent of programmed cell death, cell death resulting from activation of endogenous cellular processes. [GOC:jl] |
| positive regulation of canonical NF-kappaB signal transduction | biological process | Any process that activates or increases the frequency, rate or extent of a canonical NF-kappaB signaling cascade. [GOC:jl] |
| negative regulation of canonical NF-kappaB signal transduction | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of a canonical NF-kappaB signaling cascade. [GOC:jl] |
| positive regulation of neuron apoptotic process | biological process | Any process that activates or increases the frequency, rate or extent of cell death of neurons by apoptotic process. [GOC:go_curators, GOC:mtg_apoptosis] |
| positive regulation of macrophage differentiation | biological process | Any process that activates or increases the frequency, rate or extent of macrophage differentiation. [GOC:go_curators] |
| positive regulation of transcription by RNA polymerase II | biological process | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH] |
| positive regulation of JNK cascade | biological process | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the JNK cascade. [GOC:bf] |
| protein autophosphorylation | biological process | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). [ISBN:0198506732] |
| positive regulation of inflammatory response | biological process | Any process that activates or increases the frequency, rate or extent of the inflammatory response. [GOC:ai] |
| positive regulation of NF-kappaB transcription factor activity | biological process | Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB. [GOC:dph, GOC:tb, PMID:15087454, PMID:15170030] |
| positive regulation of necroptotic process | biological process | Any process that increases the rate, frequency or extent of a necroptotic process, a necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors. [GOC:BHF, GOC:dph, GOC:mtg_apoptosis, GOC:tb] |
| negative regulation of necroptotic process | biological process | Any process that decreases the rate, frequency or extent of a necroptotic process, a necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors. [GOC:BHF, GOC:dph, GOC:mtg_apoptosis, GOC:tb] |
| positive regulation of programmed necrotic cell death | biological process | Any process that increases the frequency, rate or extent of programmed necrotic cell death. [GOC:aruk, GOC:rph, PMID:27258785] |
| positive regulation of interleukin-6-mediated signaling pathway | biological process | Any process that increases the rate, frequency or extent of an interleukin-6-mediated signaling pathway. [GOC:BHF, GOC:mah] |
| T cell apoptotic process | biological process | Any apoptotic process in a T cell, a type of lymphocyte whose defining characteristic is the expression of a T cell receptor complex. [CL:0000084, GOC:add, GOC:mtg_apoptosis, ISBN:0781765196] |
| necroptotic process | biological process | A programmed necrotic cell death process which begins when a cell receives a signal (e.g. a ligand binding to a death receptor or to a Toll-like receptor), and proceeds through a series of biochemical events (signaling pathways), characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3) and by critical dependence on mixed lineage kinase domain-like (MLKL), and which typically lead to common morphological features of necrotic cell death. The process ends when the cell has died. The process is divided into a signaling phase, and an execution phase, which is triggered by the former. [GOC:BHF, GOC:dph, GOC:mah, GOC:mtg_apoptosis, GOC:tb, PMID:18846107, PMID:20823910, PMID:21737330, PMID:21760595, PMID:21876153] |
| cellular response to hydrogen peroxide | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus. [CHEBI:16240, GOC:mah] |
| regulation of ATP:ADP antiporter activity | biological process | Any process that modulates the activity of an ATP:ADP antiporter. [GOC:BHF, GOC:mah] |
| cellular response to tumor necrosis factor | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus. [GOC:mah] |
| cellular response to growth factor stimulus | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus. [GOC:mah] |
| extrinsic apoptotic signaling pathway | biological process | The series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered. [GOC:mtg_apoptosis, GOC:yaf, PMID:17340152] |
| programmed necrotic cell death | biological process | A necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors. [GOC:mtg_apoptosis, PMID:21760595] |
| ripoptosome assembly | biological process | The aggregation, arrangement and bonding together of a set of components to form a ripoptosome, a protein complex whose formation can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more. [GOC:mtg_apoptosis, PMID:22274400] |
| necroptotic signaling pathway | biological process | The series of molecular signals which triggers the necroptotic death of a cell. The pathway starts with reception of a signal, is characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3), and ends when the execution phase of necroptosis is triggered. [GOC:mtg_apoptosis, PMID:20823910] |
| positive regulation of execution phase of apoptosis | biological process | Any process that activates or increases the frequency, rate or extent of execution phase of apoptosis. [GOC:mtg_apoptosis, GOC:TermGenie] |
| ripoptosome assembly involved in necroptotic process | biological process | The aggregation, arrangement and bonding together of ripoptosome components leading to a necroptotic process. [GOC:mtg_apoptosis, GOC:TermGenie, PMID:22274400] |
| positive regulation of non-canonical NF-kappaB signal transduction | biological process | Any process that activates or increases the frequency, rate or extent of the non-canonical NF-kappaB cascade. [GOC:TermGenie] |
| positive regulation of tumor necrosis factor-mediated signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of tumor necrosis factor-mediated signaling pathway. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:23453807] |
| amyloid fibril formation | biological process | The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins. [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159] |
| positive regulation of reactive oxygen species metabolic process | biological process | Any process that activates or increases the frequency, rate or extent of reactive oxygen species metabolic process. [GOC:mah] |
| negative regulation of extrinsic apoptotic signaling pathway | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of extrinsic apoptotic signaling pathway. [GOC:mtg_apoptosis] |
| positive regulation of extrinsic apoptotic signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of extrinsic apoptotic signaling pathway. [GOC:mtg_apoptosis] |
| negative regulation of extrinsic apoptotic signaling pathway in absence of ligand | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of extrinsic apoptotic signaling pathway in absence of ligand. [GOC:mtg_apoptosis] |