The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
about
Interchangeable binding of Bcl10 to TRAF2 and cIAPs regulates apoptosis signalingCharacterization of fortilin, a novel antiapoptotic proteinIAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1 signaling cascade and caspase inhibition.Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspasesThe p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosisVIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that modulates caspase activationResearch progress on Livin protein: an inhibitor of apoptosisARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspasesIdentification of ARIA regulating endothelial apoptosis and angiogenesis by modulating proteasomal degradation of cIAP-1 and cIAP-2Livin promotes Smac/DIABLO degradation by ubiquitin-proteasome pathwayIAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspasesApoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs.Molecular cloning of ILP-2, a novel member of the inhibitor of apoptosis protein familyFunctional characterization of the X-linked inhibitor of apoptosis (XIAP) internal ribosome entry site element: role of La autoantigen in XIAP translationNF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosisAutocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosisLithocholic bile acid selectively kills neuroblastoma cells, while sparing normal neuronal cellsUbiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell deathNAIP interacts with hippocalcin and protects neurons against calcium-induced cell death through caspase-3-dependent and -independent pathwaysStructures of BIR domains from human NAIP and cIAP2Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the familyThe intriguing biology of the tumour necrosis factor/tumour necrosis factor receptor superfamily: players, rules and the gamesCloning and characterization of the rat homologues of the Inhibitor of Apoptosis protein 1, 2, and 3 genesSurvivin: a unique target for tumor therapycIAP-1 controls innate immunity to C. pneumoniae pulmonary infectionTargeting Non-proteolytic Protein Ubiquitination for the Treatment of Diffuse Large B Cell LymphomaEquine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinaseTRAF1 is a substrate of caspases activated during tumor necrosis factor receptor-alpha-induced apoptosisRegulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated proteinStructure of the MLT gene and molecular characterization of the genomic breakpoint junctions in the t(11;18)(q21;q21) of marginal zone B-cell lymphomas of MALT typeTwo splicing variants of a new inhibitor of apoptosis gene with different biological properties and tissue distribution patternTL1A-induced NF-kappaB activation and c-IAP2 production prevent DR3-mediated apoptosis in TF-1 cellsILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosisYeast two-hybrid screening using constitutive-active caspase-7 as bait in the identification of PA28gamma as an effector caspase substrateIsolation and characterization of a novel gene, hRFI, preferentially expressed in esophageal cancerNeurotrophin receptor-interacting mage homologue is an inducible inhibitor of apoptosis protein-interacting protein that augments cell deathA single BIR domain of XIAP sufficient for inhibiting caspasesSmall molecules destabilize cIAP1 by activating auto-ubiquitylationNeuronal apoptosis-inhibitory protein does not interact with Smac and requires ATP to bind caspase-9
P2860
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P2860
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@ast
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@en
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@en-gb
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@nl
type
label
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@ast
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@en
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@en-gb
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@nl
prefLabel
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@ast
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@en
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@en-gb
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@nl
P2093
P2860
P3181
P356
P1433
P1476
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/16.23.6914
P407
P577
1997-12-01T00:00:00Z