Structure/Function Analysis of p55 Tumor Necrosis Factor Receptor and Fas-associated Death Domain
Open Access
- 1 December 2000
- journal article
- Published by Elsevier
- Vol. 275 (48), 37596-37603
- https://doi.org/10.1074/jbc.m007166200
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Activation of a pro‐apoptotic amplification loop through inhibition of NF‐κB‐dependent survival signals by caspase‐mediated inactivation of RIPFEBS Letters, 2000
- Resistance to the Cytotoxic Effects of Tumor Necrosis Factor α Can Be Overcome by Inhibition of a FADD/Caspase-dependent Signaling PathwayPublished by Elsevier ,1999
- The 55-kDa Tumor Necrosis Factor Receptor Induces Clustering of Mitochondria through Its Membrane-proximal RegionJournal of Biological Chemistry, 1998
- An Induced Proximity Model for Caspase-8 ActivationJournal of Biological Chemistry, 1998
- The apoptosis-necrosis paradox. Apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell deathOncogene, 1997
- FLICE, A Novel FADD-Homologous ICE/CED-3–like Protease, Is Recruited to the CD95 (Fas/APO-1) Death-Inducing Signaling ComplexCell, 1996
- Involvement of MACH, a Novel MORT1/FADD-Interacting Protease, in Fas/APO-1- and TNF Receptor–Induced Cell DeathCell, 1996
- A Novel Cytoplasmic Domain of the p55 Tumor Necrosis Factor Receptor Initiates the Neutral Sphingomyelinase PathwayJournal of Biological Chemistry, 1996
- A novel domain within the 55 kd TNF receptor signals cell deathCell, 1993
- Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosisNature, 1992