FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
about
The CED-4-homologous protein FLASH is involved in Fas-mediated activation of caspase-8 during apoptosisRegulation of acidification and apoptosis by SHP-1 and Bcl-2F1Aalpha, a death receptor-binding protein homologous to the Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase substrate that mediates apoptosisThe C Terminus of HIV-1 Tat Modulates the Extent of CD178-mediated Apoptosis of T CellsThe prodomain of caspase-1 enhances Fas-mediated apoptosis through facilitation of caspase-8 activationIdentification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosisMST, a physiological caspase substrate, highly sensitizes apoptosis both upstream and downstream of caspase activationKeratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADDFas-associated factor 1, FAF1, is a member of Fas death-inducing signaling complexPossible role of death receptor-mediated apoptosis by the E3 ubiquitin ligases Siah2 and POSHCaspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.DJ-1 inhibits TRAIL-induced apoptosis by blocking pro-caspase-8 recruitment to FADDPalmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signalingCaspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspasesDEDD, a novel death effector domain-containing protein, targeted to the nucleolusHsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis.The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulumFLICE-inhibitory proteins: regulators of death receptor-mediated apoptosisCaspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondriaUpstream regulatory role for XIAP in receptor-mediated apoptosisRipped to deathIFN regulatory factor 8 sensitizes soft tissue sarcoma cells to death receptor-initiated apoptosis via repression of FLICE-like protein expressionCaspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosisDEDD regulates degradation of intermediate filaments during apoptosisMolecular cloning and characterization of human caspase-activated DNaseGlutamate-induced apoptosis in primary cortical neurons is inhibited by equine estrogens via down-regulation of caspase-3 and prevention of mitochondrial cytochrome c releaseDED or alive: assembly and regulation of the death effector domain complexesRegulation of CD95/Fas signaling at the DISCThe role of CD95 and CD95 ligand in cancerFlavivirus Activates Phosphatidylinositol 3-Kinase Signaling To Block Caspase-Dependent Apoptotic Cell Death at the Early Stage of Virus InfectionThe solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADDInsights on Molecular Mechanisms of Chondrocytes Death in OsteoarthritisFrequent nuclear localization of ICAD and cytoplasmic co-expression of caspase-8 and caspase-3 in human lymphomasRole of apoptosis and CD95-receptor/ligand system in aspirin- and Helicobacter pylori-induced cell deathCaspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomainInactivation of caspase-8 on mitochondria of Bcl-xL-expressing MCF7-Fas cells: role for the bifunctional apoptosis regulator proteinCellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complexHIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentationDeath effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC
P2860
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P2860
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
description
1997 nî lūn-bûn
@nan
1997 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մայիսին 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
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)
@nl
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
@ast
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
@en
type
label
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)
@nl
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
@ast
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
@en
prefLabel
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)
@nl
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
@ast
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
@en
P2093
P2860
P3181
P356
P1433
P1476
FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).
@en
P2093
Kischkel FC
Krammer PH
Scaffidi C
Shevchenko A
P2860
P304
P3181
P356
10.1093/EMBOJ/16.10.2794
P407
P577
1997-05-01T00:00:00Z