Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function.
about
Modulation of tumor necrosis factor by microbial pathogens.DED or alive: assembly and regulation of the death effector domain complexesRecognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domainMolecular architecture of the DED chains at the DISC: regulation of procaspase-8 activation by short DED proteins c-FLIP and procaspase-8 prodomainPaclitaxel promotes a caspase 8-mediated apoptosis through death effector domain association with microtubules.The death domain superfamily in intracellular signaling of apoptosis and inflammation.Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibitionThe molecular regulation of programmed necrotic cell injury.Role of the serine-threonine kinase PAK-1 in myxoma virus replicationThe human papillomavirus 16 E6 protein can either protect or further sensitize cells to TNF: effect of dosePoxvirus immunomodulatory strategies: current perspectivesMolecular genetic analysis of orf virus: a poxvirus that has adapted to skinEngagement of Fas on Macrophages Modulates Poly I:C induced cytokine production with specific enhancement of IP-10.Poxvirus infection and apoptosis.The MC159 protein from the molluscum contagiosum poxvirus inhibits NF-κB activation by interacting with the IκB kinase complex.The molluscum contagiosum virus death effector domain containing protein MC160 RxDL motifs are not required for its known viral immune evasion functions.Childhood molluscum contagiosum.Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF).CXCR4 chemokine receptor signaling induces apoptosis in acute myeloid leukemia cells via regulation of the Bcl-2 family members Bcl-XL, Noxa, and BakFLIP as an anti-cancer therapeutic target.Inhibition of interferon gene activation by death-effector domain-containing proteins from the molluscum contagiosum virus.Going up in flames: necrotic cell injury and inflammatory diseases.When autophagy meets viruses: a double-edged sword with functions in defense and offense.Viral cell death inhibitor MC159 enhances innate immunity against vaccinia virus infection.Functional Comparison of Molluscum Contagiosum Virus vFLIP MC159 with Murine Cytomegalovirus M36/vICA and M45/vIRA Proteins.Poxviruses Utilize Multiple Strategies to Inhibit Apoptosis.The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis.Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis.Identification of an expanded binding surface on the FADD death domain responsible for interaction with CD95/Fas.Differential affinity of FLIP and procaspase 8 for FADD's DED binding surfaces regulates DISC assemblyMutational analyses of c-FLIPR, the only murine short FLIP isoform, reveal requirements for DISC recruitment.
P2860
Q21089629-A856DF97-2870-40A1-80EC-AEDCE5503D18Q26796544-AB2320F5-D0D7-4C71-BA68-CD2AD83B5F1AQ27640045-2C328505-F81A-480D-8F09-A354A0755F08Q28268989-1FCC939F-76F6-4636-961B-BC3624F31123Q33775805-68CBADAB-5B9A-4188-B4A5-A2540F648AD3Q33996534-5A61EE8A-E893-41EF-A7B5-B3EECDC8C646Q34012966-5274B946-F7AD-451F-9082-9F33C8AC8005Q34021860-A4164BA0-2F29-45D3-9894-8135EF0636D3Q34976922-437CC684-4FB1-47ED-BB6C-80624099D9F4Q35098707-DD933318-4E9F-4A3B-AE0D-953008E6C42BQ35125981-0E864110-A07C-44BC-A5D1-0A5E3D2751CEQ35232853-E1D617C6-2DC0-4609-B1DD-A56696B95D2FQ35596730-D82B063E-C91A-4AFF-BCC8-3851548AC1DFQ35613796-0C43046D-C722-4655-BAD3-3A58AF0721C0Q35785785-14DC7C53-B4C5-4F1E-B136-D9CC3087EDE7Q36351550-EB0A121F-259D-492E-BAFC-50FAA1CDFA2EQ36381373-6BC0DC84-1162-4D5B-8A8D-05273DD8BCDCQ37024785-6ABD767A-CD30-424E-9F93-368D176E34C8Q37095358-0A4FB244-BA9E-40F3-8247-182C39D4CA47Q37096732-0C9FEB21-AAC8-4E9C-A33D-575CE127A7CEQ37495190-7276271E-6C37-4219-83C0-24387F74A2A4Q37763609-8B49B72A-C938-417A-846C-FF1D66E53C07Q37791919-E4573F8C-F6BC-4366-911D-E9C4C09F8E63Q38341747-20D91903-6CED-4954-A328-58D781993D96Q38807626-4DCCB938-EDBF-4422-B2BC-86801A5AFF9CQ40090965-17CDA52E-7E58-45D4-A174-5F05D7A5423AQ40330298-F9B9AC3F-AC77-4E29-8443-75C46FFA812AQ40330319-73F79B95-BF22-4A49-A752-7E3884531B11Q40624013-EC1E091D-AB58-46CE-B20C-8140FB200679Q41999028-D3F20962-2454-47A5-83E5-82319A23C744Q42817747-75E82B02-A14D-490E-8C15-A68F0E1169A3
P2860
Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@ast
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@en
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@nl
type
label
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@ast
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@en
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@nl
prefLabel
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@ast
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@en
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@nl
P2093
P2860
P1433
P1476
Binding of FADD and caspase-8 ...... or its antiapoptotic function.
@en
P2093
Jeffrey I Cohen
John Bertin
Michael J Lenardo
Richard M Siegel
Tara L Garvey
P2860
P304
P356
10.1128/JVI.76.2.697-706.2002
P407
P577
2002-01-01T00:00:00Z