about
Fas (TNFRSF6)-associated via death domainCaspase 8Receptor interacting serine/threonine kinase 1Toll like receptor adaptor molecule 1CASP8 and FADD like apoptosis regulatorToll-like receptor adaptor molecule 1CASP8 and FADD-like apoptosis regulatorReceptor (TNFRSF)-interacting serine-threonine kinase 1Caspase 10Caspase 8Fas associated via death domainReceptor interacting serine/threonine kinase 1Caspase 8Fas associated via death domain
P681
The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosisThe mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathwaysPick your poison: the Ripoptosome, a cell death platform regulating apoptosis and necroptosiscIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoformsAn outline of necrosome triggersFunctional Amyloid Signaling via the Inflammasome, Necrosome, and Signalosome: New Therapeutic Targets in Heart FailureTNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II membersThe Gβγ-Src signaling pathway regulates TNF-induced necroptosis via control of necrosome translocationReceptor interacting protein kinase 1 mediates murine acetaminophen toxicity independent of the necrosome and not through necroptosis.CYLD deubiquitinates RIP1 in the TNFα-induced necrosome to facilitate kinase activation and programmed necrosis.Synergistic anticancer effect of cisplatin and Chal-24 combination through IAP and c-FLIPL degradation, Ripoptosome formation and autophagy-mediated apoptosis.ZFP36 stabilizes RIP1 via degradation of XIAP and cIAP2 thereby promoting ripoptosome assembly.Cellular IAP proteins and LUBAC differentially regulate necrosome-associated RIP1 ubiquitinationThe necrosome promotes pancreatic oncogenesis via CXCL1 and Mincle-induced immune suppression.RIP1 autophosphorylation is promoted by mitochondrial ROS and is essential for RIP3 recruitment into necrosome.Characterization of the ripoptosome and its components: implications for anti-inflammatory and cancer therapy.Ripoptosome Analysis by Caspase-8 Coimmunoprecipitation.Necrosome core machinery: MLKL.The Necrosome in Acute Kidney Injury.Targeting Thioredoxin-1 by dimethyl fumarate induces ripoptosome-mediated cell death.Molecular Pathways: The Necrosome-A Target for Cancer Therapy.Obatoclax (GX15-070) triggers necroptosis by promoting the assembly of the necrosome on autophagosomal membranes.The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs.Sorafenib tosylate inhibits directly necrosome complex formation and protects in mouse models of inflammation and tissue injury.Structural study of the RIPoptosome core reveals a helical assembly for kinase recruitmentCLL cells are resistant to smac mimetics because of an inability to form a ripoptosome complex.Shikonin induces glioma cell necroptosis in vitro by ROS overproduction and promoting RIP1/RIP3 necrosome formation.Smac mimetic and glucocorticoids synergize to induce apoptosis in childhood ALL by promoting ripoptosome assembly.The Ripoptosome: death decision in the cytosol.The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex.Novel smac mimetic APG-1387 elicits ovarian cancer cell killing through TNF-alpha, Ripoptosome and autophagy mediated cell death pathway.RIP3 is an upregulator of aerobic metabolism and the enhanced respiration by necrosomal RIP3 feeds back on necrosome to promote necroptosis.Ripoptosome: a novel IAP-regulated cell death-signalling platform.Triad3a induces the degradation of early necrosome to limit RipK1-dependent cytokine production and necroptosis.Correction to: Novel smac mimetic APG-1387 elicits ovarian cancer cell killing through TNF-alpha, Ripoptosome and autophagy mediated cell death pathway.Nuclear RIPK3 and MLKL contribute to cytosolic necrosome formation and necroptosisErratum: Obatoclax (GX15-070) triggers necroptosis by promoting the assembly of the necrosome on autophagosomal membranesCoupling Between Interleukin-1R1 and Necrosome Complex Involves in Hemin-Induced Neuronal Necroptosis After Intracranial HemorrhageAnalysis of Cytokine- and Influenza A Virus-Driven RIPK3 Necrosome FormationRIPK1 and Caspase-8 Ensure Chromosome Stability Independently of Their Role in Cell Death and Inflammation
P921
Q14907140-B820122E-73BD-41B9-8154-2EC077E0EAC5Q14911968-350C02E5-7B0F-4496-9EE5-3CCDD0632038Q21101871-2CAF0859-0598-44B1-AB3E-797F00135628Q21127355-85F699EA-3F58-47FF-BD9A-729E0901AA04Q21151736-CE364EB6-C7CD-4DFA-84B0-1DFFE28D54ADQ21494909-2C546FF2-4116-4BE3-A860-F4E50BCA44FAQ21495069-A356858C-E58A-4040-AACA-83905317029CQ21981433-05B9F692-805C-4615-B524-DAA8EA257C83Q22679036-BC266E46-6447-4926-B1D1-B63E23F92331Q28560308-43B6E31C-A469-4CBA-8DD9-227FAF3A96D6Q29524318-DF7B57B7-7605-4F22-B7C8-61942A6393ACQ29527229-BBB032A5-00DC-45A1-9E77-98E4434415C4Q5049059-2B7E2F5B-7BAE-4764-91A2-8F9BC3BCF16CQ994646-8BB31D58-6D00-419D-BD3B-CAB41C3A2642
P681
Q24293754-9F84F307-350C-4BC2-9EF2-845CFF170851Q24302411-C45E03C3-D762-47AA-ACCE-E5E401899CFCQ24303473-594B2288-1316-4E2B-BE7F-8D28A031AA0BQ24311676-12550EA8-A773-4923-83D5-2F41826E53FFQ26751108-4B209D6A-06B1-4781-AB17-8EAC9987B035Q26776120-C59F3043-F131-40EE-A8E1-4A957701174FQ28505598-A18D3487-6E5C-470B-A676-0E8AF7BE578CQ28505598-A767E914-D6D2-45B9-8978-76A2C2E04B89Q28660413-D3D6BFDC-9B86-4B28-8835-479F9B22C0C0Q30009153-4220834D-34C4-47C4-8F86-260A1B951FE8Q35009699-13A43F50-FF65-4AE6-8509-5CCCA18D4E9CQ35176405-B85B5A17-DB86-4E54-95C2-2AE2BD037CF8Q35621928-EC087758-5288-4772-A5D8-106B614922D7Q36347355-F1663B0C-7B51-4583-90FC-889E5B606362Q36803448-ACB9472A-D72F-49DF-8F64-F956F5A45AC6Q37642622-7CB3E40A-1223-4A13-A5A4-4AEDFA2CB8F0Q38234369-861D0F38-F4D5-4136-A6EE-C086A6E4041CQ38789738-DA8BC535-2B99-4E80-983D-D6879369355AQ38799137-121D2AE8-F687-4C70-80EE-70DE69044AE9Q38875293-74971C27-FAD2-4BD9-AB5B-605353FEC319Q38944398-5E9BD7A8-87B5-404A-82B7-F7C4714D4BF8Q39118065-0B66FE70-CA44-4535-871E-9D826CAF8D25Q39142897-F6B77284-8F3F-4D37-A2AE-B37F68BB4632Q39511129-284A5FC7-0E66-4DA9-B7A7-39FE7C49105FQ40153668-DAEFC0F7-B459-4F2A-A3B5-A6C5966C0686Q42173418-482F3F62-6DB7-41EA-B9C5-B3F5DA119B70Q42585598-792B190B-F18D-498E-A565-0740DE1119FFQ46319827-CFE2BD93-783F-4F13-BBBF-8EEA01A37A26Q46890911-38734DE7-0E9F-4CBD-8E66-DA6A62A769A5Q49051642-B042CAD3-19C0-4B7B-B454-27E702F3A403Q52313311-68A40CD4-EC0D-4B00-AEDE-691564683B9CQ52358778-82269681-9D80-4503-A75C-302F10F4AB84Q52663545-81D6365B-21D6-48C4-BC9E-32C463050916Q54547717-ABFA80D4-C64C-4F59-A6D8-52AC66EDB736Q55031782-C00CCEEB-7813-482C-8C85-C293322638E9Q55177698-57861B47-F950-4853-8BB3-0091757B2DE6Q57148426-7BC11F9A-A624-4128-9095-7607EAC0AC0AQ57243277-C858378C-7ECD-46F6-9DA6-F89938AAE9B6Q57820720-4080CC1C-F943-42A8-87B0-5C2200AB0F58Q59354056-A229B418-13B5-49F1-B244-C290B7B9781E
P921
description
A protein complex whose core c ...... pathway or a necroptotic signa
@en
cellulaire component
@nl
name
ripoptosome
@en
type
label
ripoptosome
@en
altLabel
GO:0097342
@en
prefLabel
ripoptosome
@en
P2888
P361
P686
GO:0097342